{
  "AMGAB0001": {
    "Interaction ID": "AMGAB0001",
    "Antibody ID": "ABID0002",
    "Antibody name": "Gantenerumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1001/archneurol.2011.1538",
    "PMID": 21987394.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo,",
    "Experimental method(s)": "Immunohistochemistry, Positron emission tomography (PET), Semiquantitative assessment of gantenerumab-induced phagocytosis,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The mean (95% CI) percent change from baseline difference relative to placebo (n = 4) in cortical brain amyloid level was −15.6% (95% CI, −42.7 to 11.6) for the 60-mg group (n = 6) and −35.7% (95% CI, −63.5 to −7.9) for the 200-mg group (n = 6).\", \"Gantenerumab treatment resulted in a dose-dependent reduction in brain amyloid level, possibly through an effector cell–mediated mechanism of action.·, \"Table 2\", \"Adjusting for baseline SUVR, we found that a nonparametric analysis of covariance on this percent change suggested that the 200-mg group differed from the placebo group (P = .06). The dose dependency of the amyloid-reducing effect was indicated by the nonparametric linear regression analysis on the baseline-adjusted percent change values over the specific PiB signal: slope of −0.13 (r2 = 0.29; P = .03) (Figure 3).\", \"Figure 2\", \"Figure 3\", \"Scatterplot shows percent change from baseline (specific [11C]PiB signal) in cortical composite SUVR over gantenerumab doses for all patients with an end-of-treatment scan who received gantenerumab (60 or 200 mg) or placebo every 4 weeks. The dose-response relationship is indicated by the linear regression line (% change in amyloid = 12.81 − 0.13 × dose) of the baseline-adjusted percent change residual value (vertical axis) vs actual dose of gantenerumab (horizontal axis).(opens in new tab)\", \"Figure 4\", \"Figure 7\", \"Percent reduction (specific carbon 11–labeled Pittsburgh Compound B signal) from baseline in cortical composite region vs fluid-attenuated inversion recovery (FLAIR) area. This figure summarizes in quantitative terms the results shown in Figure 6. In both patients A and B, reduction in the standard uptake value ratio is larger in the volume representing the magnetic resonance imaging finding (FLAIR) than in the cortical composite volume of interest (VOI). This is true for both time points: the end of treatment and posttreatment.\", \"A decrease in Aβ amyloid plaque in sections of brain that were incubated with microglia cells was dependent on the concentration of gantenerumab, with a slight effect at 50 ng/mL of gantenerumab and substantial plaque clearance at 500 and 5000 ng/mL (Figure 8).\", \"Figure 8\", \"Aβ amyloid plaques were decreased in the presence of human microglia after preincubation with gantenerumab in a concentration-dependent manner, with slight clearance of small plaques seen at 50 ng/mL (B) and substantial decrease of plaques at 500 ng/mL (C) and 5000 ng/mL (D).\", \"Our study demonstrates that 2 to 7 months of treatment with gantenerumab led to dose-dependent amyloid reduction in the brains of patients with AD.\",",
    "Curator Statement": false
  },
  "AMGAB0002": {
    "Interaction ID": "AMGAB0002",
    "Antibody ID": "ABID0003",
    "Antibody name": "Donanemab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1001/jama.2023.13239",
    "PMID": 37459141.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"At 76 weeks, brain amyloid plaque level decreased by 88.0 Centiloids (95% CI, −90.20 to −85.87) with donanemab treatment and increased by 0.2 Centiloids (95% CI, −1.91 to 2.26) in the placebo group in the low/medium tau population; in the combined population, amyloid plaque level decreased by 87.0 Centiloids (95% CI, −88.90 to −85.17) with donanemab treatment and decreased by 0.67 Centiloids (95% CI, −2.45 to 1.11) in the placebo group (Figure 3A). The percentages of donanemab-treated participants in the low/medium tau population who reached amyloid clearance29,38 were 34.2% (95% CI, 30.22%-38.34%) at 24 weeks and 80.1% (95% CI, 76.12%-83.62%) at 76 weeks compared with 0.2% (95% CI, 0.03%-1.02%) at 24 weeks and 0% (95% CI, 0.00%-0.81%) at 76 weeks of placebo-treated participants. In the combined population, amyloid clearance was reached in 29.7% (95% CI, 26.56%-33.04%) of participants at 24 weeks and 76.4% (95% CI, 72.87%-79.57%) at 76 weeks of donanemab-treated participants compared with 0.2% (95% CI, 0.07%-0.90%) at 24 weeks and 0.3% (95% CI, 0.08%-1.05%) at 76 weeks of placebo-treated participants (Figure 3B).\", \"Figure 3\", \"Donanemab treatment resulted in significantly reduced brain amyloid plaque in participants at all time points assessed, with 80% (low/medium tau population) and 76% (combined population) of participants achieving amyloid clearance at 76 weeks.\"",
    "Curator Statement": false
  },
  "AMGAB0003": {
    "Interaction ID": "AMGAB0003",
    "Antibody ID": "ABID0030.5",
    "Antibody name": "Ta1505",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1002/acn3.171",
    "PMID": 25815351.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" The anti-pSer413 antibody significantly improved memory, whereas the anti-pSer396 antibodies showed less effect. The cognitive improvement paralleled a reduction in the levels of tau hyperphosphorylation, tau oligomer accumulation, synapse loss, tangle formation, and neuronal loss.\", \"Figure 4\", \"Compared with control antibody-treated mice, Ta1505-treated mice showed a significant reduction in Ta1505-, PHF-1-, and AT8-positive staining in the hippocampal mossy fibers (Fig.4A and C).\", \"Ta1505-treated mice showed an apparent reduction in Ta1505- and PHF-1-positive staining (Fig. S4A and C), whereas Ta9-treated mice exhibited no effect (Fig. S4B and C).\", \"Supplementary Figure S4 \", \"Ta1505-treated mice showed an apparent reduction of hyperphosphorylated tau in hippocampal mossy fibers (A).\", \"Ta1505-treated mice showed significantly lower levels of total (i.e., pool-2-positive) and Ta1505-, PHF-1-, and AT8-positive tau than did control antibody-treated mice in the TBS-soluble and GuHCl-soluble fractions (Fig.5A and B).\", \"Figure 5\", \"Ta1505-treated mice showed significantly lower levels of total and Ta1505-, PHF-1-, and AT8-positive tau than did control antibody-treated mice in TBS-soluble and GuHCl-soluble fractions (B).\", \"Ta1505 significantly reduced the levels of tau oligomers, but Ta4 and Ta9 did not (Fig. S6B and C).\", \"Supplementary Figure S6\", \"The levels of tau oligomers in both TBS-soluble brain fractions and total tau extracts were significantly decreased by Ta1505 injection (Fig. S6D and E).\", \"Ta1505-treated mice displayed significantly decreased levels of NFTs in the EC-II/III region (Fig.7A and B), whereas Ta4- and Ta9-treated mice showed little changes (Fig.7C and D and Fig. S8A and B).\", \"Figure 7\", \"Ta1505-treated mice showed apparently reduced levels of NFTs (A), whereas Ta4-treated mice exhibited no changes (C).\", \" Ta1505-treated mice showed an apparent reduction of hyperphosphorylated tau in hippocampal mossy fibers (A).\", \" Ta1505- and, to a lesser extent, Ta9-treated mice showed reduced levels of tau oligomers, but Ta4-treated mice did not. \", \" Ta1505 significantly decreased the levels of tau oligomers in both TBS-soluble fractions and total tau extracts, but Ta4 and Ta9 did not. \",",
    "Curator Statement": false
  },
  "AMGAB0004": {
    "Interaction ID": "AMGAB0004",
    "Antibody ID": "ABID0553",
    "Antibody name": "Ta4",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1002/acn3.171",
    "PMID": 25815351.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" The anti-pSer413 antibody significantly improved memory, whereas the anti-pSer396 antibodies showed less effect. The cognitive improvement paralleled a reduction in the levels of tau hyperphosphorylation, tau oligomer accumulation, synapse loss, tangle formation, and neuronal loss.\", \"Figure 4\", \"In contrast, Ta4- and Ta9-treated mice exhibited a significant reduction in PHF-1-positive staining but little in Ta1505- and AT8-staining (Fig.4B and C and Fig. S3A and B).\", \"In contrast, Ta4-treated mice exhibited reduced PHF-1-staining but not Ta1505- or AT8-staining (B). \", \"Figure 4\", \" In contrast, Ta4-treated mice exhibited a significant reduction only of PHF-1-positive tau in the GuHCl-soluble fraction (Fig.5C and D).\", \"In contrast, Ta4-treated mice exhibited a significant reduction only of PHF-1-positive tau in GuHCl-soluble fraction (D).\",",
    "Curator Statement": false
  },
  "AMGAB0005": {
    "Interaction ID": "AMGAB0005",
    "Antibody ID": "ABID0553",
    "Antibody name": "Ta4",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1002/acn3.171",
    "PMID": 25815351.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"In contrast, Ta4-treated mice exhibited reduced PHF-1-staining but not Ta1505- or AT8-staining (B). \", \"Ta1505 significantly reduced the levels of tau oligomers, but Ta4 and Ta9 did not (Fig. S6B and C).\", \"Supplementary Figure S6\", \"Ta1505-treated mice displayed significantly decreased levels of NFTs in the EC-II/III region (Fig.7A and B), whereas Ta4- and Ta9-treated mice showed little changes (Fig.7C and D and Fig. S8A and B).\", \"Figure 7\", \"Ta1505-treated mice showed apparently reduced levels of NFTs (A), whereas Ta4-treated mice exhibited no changes (C).\", \" Ta1505- and, to a lesser extent, Ta9-treated mice showed reduced levels of tau oligomers, but Ta4-treated mice did not. \", \" Ta1505 significantly decreased the levels of tau oligomers in both TBS-soluble fractions and total tau extracts, but Ta4 and Ta9 did not. \",",
    "Curator Statement": false
  },
  "AMGAB0006": {
    "Interaction ID": "AMGAB0006",
    "Antibody ID": "ABID0554",
    "Antibody name": "Ta9",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1002/acn3.171",
    "PMID": 25815351.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" The anti-pSer413 antibody significantly improved memory, whereas the anti-pSer396 antibodies showed less effect. The cognitive improvement paralleled a reduction in the levels of tau hyperphosphorylation, tau oligomer accumulation, synapse loss, tangle formation, and neuronal loss.\",\"Supplementary Figure S3\", \"In contrast, Ta4- and Ta9-treated mice exhibited a significant reduction in PHF-1-positive staining but little in Ta1505- and AT8-staining (Fig.4B and C and Fig. S3A and B).\", \"Finally, Ta9-treated mice showed significantly reduced levels of PHF-1-positive tau in the TBS-soluble and GuHCl-soluble fractions, and Ta1505- and AT8-positive tau in either fraction, but the effects were weaker than those in Ta1505-treated mice (Fig. S5A and B).\", \"Supplementary Figure S5\", \" Ta9-treated mice showed reduced PHF-1-staining but not Ta1505- or AT8-staining in hippocampal mossy fibers. \", \" Ta9-treated mice showed significantly reduced levels of PHF-1-positive tau in TBS-soluble and GuHCl-soluble fractions. \", \" Ta1505- and, to a lesser extent, Ta9-treated mice showed reduced levels of tau oligomers, but Ta4-treated mice did not. \",",
    "Curator Statement": false
  },
  "AMGAB0007": {
    "Interaction ID": "AMGAB0007",
    "Antibody ID": "ABID0554",
    "Antibody name": "Ta9",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1002/acn3.171",
    "PMID": 25815351.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S4 \", \"Ta1505-treated mice showed an apparent reduction in Ta1505- and PHF-1-positive staining (Fig. S4A and C), whereas Ta9-treated mice exhibited no effect (Fig. S4B and C).\",\"Ta1505 significantly reduced the levels of tau oligomers, but Ta4 and Ta9 did not (Fig. S6B and C).\", \"Supplementary Figure S6\", \"Ta1505-treated mice displayed significantly decreased levels of NFTs in the EC-II/III region (Fig.7A and B), whereas Ta4- and Ta9-treated mice showed little changes (Fig.7C and D and Fig. S8A and B).\", \"Supplementary Figure S8\", \" Ta1505-treated mice showed an apparent reduction of hyperphosphorylated tau in hippocampal mossy fibers (A). In contrast, Ta9-treated mice exhibited no effects (B).\", \" Ta1505 significantly decreased the levels of tau oligomers in both TBS-soluble fractions and total tau extracts, but Ta4 and Ta9 did not. \",",
    "Curator Statement": false
  },
  "AMGAB0008": {
    "Interaction ID": "AMGAB0008",
    "Antibody ID": "ABID0555",
    "Antibody name": "4C10F4",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1002/acn3.171",
    "PMID": 25815351.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"In contrast, Ta4- and Ta9-treated mice exhibited a significant reduction in PHF-1-positive staining but little in Ta1505- and AT8-staining (Fig.4B and C and Fig. S3A and B).\", \"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0009": {
    "Interaction ID": "AMGAB0009",
    "Antibody ID": "ABID0556",
    "Antibody name": "11F11",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1002/acn3.171",
    "PMID": 25815351.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Compared with control antibody-treated mice, Ta1505-treated mice showed a significant reduction in Ta1505-, PHF-1-, and AT8-positive staining in the hippocampal mossy fibers (Fig.4A and C).\", \"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0010": {
    "Interaction ID": "AMGAB0010",
    "Antibody ID": "ABID0557",
    "Antibody name": "6F11B6",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1002/acn3.171",
    "PMID": 25815351.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S3 \", \"In contrast, Ta4- and Ta9-treated mice exhibited a significant reduction in PHF-1-positive staining but little in Ta1505- and AT8-staining (Fig.4B and C and Fig. S3A and B).\",",
    "Curator Statement": false
  },
  "AMGAB0011": {
    "Interaction ID": "AMGAB0011",
    "Antibody ID": "ABID0019.6",
    "Antibody name": "HJ8.5",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1002/acn3.176",
    "PMID": 25815354.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo, In cellulo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA,",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-tau antibody reduces insoluble tau and decreases brain atrophy\", \"Treatment with HJ8.5 at 50 mg/kg showed a very strong decrease in detergent-insoluble tau.\", \"HJ8.5 treatment reduced hippocampal CA1 cellular layer staining with the p-tau antibody AT8 and thio-S-positive tau aggregates in piriform cortex and amygdala.\", \"Our results indicate that systemically administered anti-tau antibody HJ8.5 significantly decreases insoluble tau, decreases brain atrophy, and improves motor/sensorimotor function in a mouse model of tauopathy. \", \"Our results suggest that this treatment reduces tau pathology, improves certain motor functions, and reduces brain atrophy.\", \"Anti-tau antibody treatment reduces detergent/insoluble tau\", \"We further analyzed the detergent-insoluble human tau load that was solubilized by 70% FA. We found that at a dose of 50 mg/kg, HJ8.5 treatment markedly reduced detergent insoluble tau by ∽75% compared to vehicle-treated mice (Fig.1C).\", \"Figure 1\", \"Anti-tau antibody markedly reduces insoluble tau. \", \"HJ8.5 treatment at 50 mg/kg significantly decreased insoluble human tau (P < 0.0001) compared to vehicle-treated mice.\", \"Anti-tau antibody treatment reduced thio-S staining\", \"We found that HJ8.5-treated animals showed less thio-S-positive staining compared to vehicle-treated mice (Fig.3A). By semiquantitative analysis of all treated mice, we observed there was a significant decrease in thio-S-positive staining in mice treated with HJ8.5 at both 10 and 50 mg/kg compared to vehicle-treated mice (Fig.3B).\", \"Figure 3\", \"Thio-S staining is decreased in anti-tau antibody-treated P301S mice.\", \"Both doses of HJ8.5 antibody treatment showed significantly lower thio-S staining compared to vehicle-treated mice.\", \"HJ8.5 was found to strongly reduce detergent insoluble tau and phospho-tau staining in the CA1 region of the hippocampus.\", \" To the best of our knowledge, the effect of HJ8.5 on reducing detergent insoluble tau by 75% is the largest effect on this parameter reported to date.\",",
    "Curator Statement": "While higher dose of 50 mg/kg, lower doses of 10 mg/kg resulted in no differences in insoluble tau."
  },
  "AMGAB0012": {
    "Interaction ID": "AMGAB0012",
    "Antibody ID": "ABID0019.6",
    "Antibody name": "HJ8.5",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1002/acn3.176",
    "PMID": 25815354.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo, In cellulo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\",",
    "Curator Statement": "While the higher dose of 50 mg/kg showed lower insoluble tau by ELISA, lower doses of 10 mg/kg resulted in no differences in this assay."
  },
  "AMGAB0013": {
    "Interaction ID": "AMGAB0013",
    "Antibody ID": "ABID0294",
    "Antibody name": "07G10",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,  Immunogold electron microscopy",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"Supplementary Figure S2\", \"Treatment of diabetic mice with the mAbs delays disease progression and dramatically increases overall survival.\", \"Two monoclonal antibodies (mAbs) are reported that bind human islet amyloid polypeptide (hIAPP) protofibrils and inhibit their aggregation and toxicity to pancreatic islets in a mouse model of rapidly progressing type 2 diabetes mellitus (T2D)\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\", \"The mAb 07G10 decreased the end‐stage total fluorescence by more than half of the value of the control condition.\", \"Together, these data suggest that the candidate mAbs prevent protofibril aggregation, while also preventing β‐cell damage from both the cytotoxic‐ and macrophage‐mediated inflammatory effects of hIAPP aggregation.\", \"Two novel mAbs are reported that bind hIAPP protofibrils and inhibit their aggregation and toxicity to pancreatic islets in a mouse model of rapidly progressing type 2 diabetes mellitus (T2D). \"",
    "Curator Statement": false
  },
  "AMGAB0014": {
    "Interaction ID": "AMGAB0014",
    "Antibody ID": "ABID0295",
    "Antibody name": "10H04",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Immunogold electron microscopy",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"Supplementary Figure S2\", \"Treatment of diabetic mice with the mAbs delays disease progression and dramatically increases overall survival.\", \"Two monoclonal antibodies (mAbs) are reported that bind human islet amyloid polypeptide (hIAPP) protofibrils and inhibit their aggregation and toxicity to pancreatic islets in a mouse model of rapidly progressing type 2 diabetes mellitus (T2D)\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\", \"The mAb 10H04 delayed the increase in fluorescence, and only partially decreased end‐stage fluorescence compared with the control.\", \"Together, these data suggest that the candidate mAbs prevent protofibril aggregation, while also preventing β‐cell damage from both the cytotoxic‐ and macrophage‐mediated inflammatory effects of hIAPP aggregation.\", \"Two novel mAbs are reported that bind hIAPP protofibrils and inhibit their aggregation and toxicity to pancreatic islets in a mouse model of rapidly progressing type 2 diabetes mellitus (T2D). \"",
    "Curator Statement": false
  },
  "AMGAB0015": {
    "Interaction ID": "AMGAB0015",
    "Antibody ID": "ABID0296",
    "Antibody name": "01H12",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\",",
    "Curator Statement": false
  },
  "AMGAB0016": {
    "Interaction ID": "AMGAB0016",
    "Antibody ID": "ABID0297",
    "Antibody name": "02A09",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\",",
    "Curator Statement": false
  },
  "AMGAB0017": {
    "Interaction ID": "AMGAB0017",
    "Antibody ID": "ABID0298",
    "Antibody name": "02D09",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\",",
    "Curator Statement": false
  },
  "AMGAB0018": {
    "Interaction ID": "AMGAB0018",
    "Antibody ID": "ABID0299",
    "Antibody name": "02G11",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\",",
    "Curator Statement": false
  },
  "AMGAB0019": {
    "Interaction ID": "AMGAB0019",
    "Antibody ID": "ABID0300",
    "Antibody name": "08A11",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\",",
    "Curator Statement": false
  },
  "AMGAB0020": {
    "Interaction ID": "AMGAB0020",
    "Antibody ID": "ABID0301",
    "Antibody name": "02C05",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\",",
    "Curator Statement": false
  },
  "AMGAB0021": {
    "Interaction ID": "AMGAB0021",
    "Antibody ID": "ABID0302",
    "Antibody name": "03B05",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\",",
    "Curator Statement": false
  },
  "AMGAB0022": {
    "Interaction ID": "AMGAB0022",
    "Antibody ID": "ABID0303",
    "Antibody name": "09F08",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\",",
    "Curator Statement": false
  },
  "AMGAB0023": {
    "Interaction ID": "AMGAB0023",
    "Antibody ID": "ABID0304",
    "Antibody name": "09G05",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\",",
    "Curator Statement": false
  },
  "AMGAB0024": {
    "Interaction ID": "AMGAB0024",
    "Antibody ID": "ABID0305",
    "Antibody name": "11H08",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\",",
    "Curator Statement": false
  },
  "AMGAB0025": {
    "Interaction ID": "AMGAB0025",
    "Antibody ID": "ABID0306",
    "Antibody name": "12B06",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\",",
    "Curator Statement": false
  },
  "AMGAB0026": {
    "Interaction ID": "AMGAB0026",
    "Antibody ID": "ABID0307",
    "Antibody name": "15G06",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\",",
    "Curator Statement": false
  },
  "AMGAB0027": {
    "Interaction ID": "AMGAB0027",
    "Antibody ID": "ABID0308",
    "Antibody name": "13H02",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1002/advs.202202342",
    "PMID": 36257905.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Abstract figure\", \"Protofibril‐Specific mAbs Inhibit hIAPP Protofibril Aggregation\",",
    "Curator Statement": false
  },
  "AMGAB0028": {
    "Interaction ID": "AMGAB0028",
    "Antibody ID": "ABID0004",
    "Antibody name": "Crenezumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1002/ana.25513",
    "PMID": 31168802.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Crenezumab lowers amyloid β oligomers in cerebrospinal fluid\", \"Crenezumab lowered CSF oAβ levels in the large majority of treated patients tested. \"",
    "Curator Statement": false
  },
  "AMGAB0029": {
    "Interaction ID": "AMGAB0029",
    "Antibody ID": "ABID0008.5",
    "Antibody name": "NI006",
    "Amyloid ID": "AGAMYID0010",
    "Amyloid name": "Transthyretin",
    "DOI": "10.1002/cpt.3455",
    "PMID": 39410666.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"NI006 concentration‐dependent amyloid depletion rate\",  \"NI006 binding to ATTR results in antibody‐target complex that is eliminated by phagocytic immune cells.\", @The NI006‐ATTR complex elimination rate was estimated to 0.066 per day in this assay, corresponding to an elimination half‐life of 10.5 days (Figure 2 a ).\", \"Figure 2\", \"An in vivo model was also developed, consisting of a subcutaneous graft of patient derived ATTR fibrils in mice. 6 Fibril elimination in this xenograft model was faster, with an elimination rate estimated to 0.37 per day, corresponding to an elimination half‐life of 1.9 days (Figure 2 b ).\", \"The NI006‐ATTR elimination rate by phagocytic immune cells was estimated using data from the tissue amyloid depletion assay (in vitro) and the patient‐derived fibril xenograft model (in mice).\",",
    "Curator Statement": false
  },
  "AMGAB0030": {
    "Interaction ID": "AMGAB0030",
    "Antibody ID": "ABID0419",
    "Antibody name": "BAM-10",
    "Amyloid ID": "AGAMYID0015",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1002/jum.14256",
    "PMID": 28543446.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Amyloid β Plaque Reduction With Antibodies Crossing the Blood-Brain Barrier, Which Was Opened in 3 Sessions of Focused Ultrasound in a Rabbit Model\", \"It was shown that with this animal model, the plaques were 30 μm in diameter. By increasing the number of sessions, the number of plaques decreased (both for focused US only and focused US and antibodies). Without the application of focused US, the average number of plaques dropped from 200/cm2 (before treatment) to 170/cm2 (after treatment). The effect of treatment with focused US with antibodies was more drastic. With 3 BBB opening sessions, the average number of plaques was reduced from 200 to 78/cm2 .\", \"Figure 3D shows a coronal section of a rabbit brain, with BBB opening using antibodies only (group D), showing some visible reduction of plaques in the right hemisphere. The plaque load decreased from 200/cm2 (control group B) to 190/cm2. Figure 3E shows a coronal section of a rabbit brain with BBB opening using focused US and antibodies (group E), showing some small reduction of plaques in the right hemisphere. The plaque load decreased from 200/cm2 (control group B) to 133/cm2.\", \"Figure 3\", \"This result showed that the full effect of antibodies on plaque reduction was reached after 3 days.\", \"Figure 4\", \"Having established the time for maximizing the effect of antibodies, a series of experiments were conducted by varying the number of sessions of BBB opening. Figure 5A shows a coronal section of a rabbit brain, cut in the hippocampus treated with exogenous antibodies and 1 session of BBB opening using focused US. The left part of the brain included severe accumulation of Aβ-42 plaques. The right part of the brain showed a substantial reduction of Aβ plaques. Figure 5B shows the corresponding result with 2 sessions of BBB opening using focused US. Each session was 3 days apart. The right part of the brain showed reduction of Aβ plaques compared with the case of 1 session of focused US (P < .001). Figure 5C shows the corresponding result with 3 sessions of BBB opening. The right part of the brain showed a reduction of Aβ plaques compared with the case of 1 session of focused US (P < .001). In all animal groups injected with exogenous antibodies, a significant reduction in plaques was observed (P < .05; P < .001; and P < .001 for 1, 2, and 3 sessions, respectively).\", \"Figure 5\", \"Figure 6\", \"Table 2\", \"The reduction in the number of plaques due to the two methods (focused US only and focused US with antibodies) is summarized in Table 2, which shows the average number of plaques per square centimeter with standard deviations versus the treatment method (focused US only or focused US and exogenous antibodies) at different instances (control and after opening the BBB once, twice, and 3 times).\", \"The major conclusion was that by increasing the number of sessions, the number of plaques decreased (both for the focused US-only approach and for the focused US and antibody approach).\", \"The effect of exogenous antibodies was more drastic. With 3 sessions, the average number of plaques was reduced from 200 to 78/cm2. As we know, part of this reduction (nearly 30/cm2) was possibly due to the endogenous antibodies,15, 16 which entered the brain by BBB opening. The rest of the reduction was attributed to the exogenous antibodies. Jordão et al14 showed that in some mice, a reduction in the number of plaques of almost 20% was achieved because of exogenous antibodies. The larger drop observed in our results is attributed to the multiple sessions delivered (3 sessions).\", \"In conclusion, the main objective of this study was to remove Aβ plaques by using multiple sessions of focused US-induced BBB opening using microbubbles with and without antibodies in a rabbit model.\",",
    "Curator Statement": "The authors refer to focused ultrasound as (US). Despite the authors report the results from antibody BC-10, different reviews have corrected its name to BAM-10. We have followed this path due to several line of evidence: i) authors cite a paper by Jordão anc ollaborators which use BAM-10, but rename it as BC-10 \"Moreover, in the study by Jordão et al,14 exogenous antibodies (BC-10) were used as a therapeutic agent against Aβ plaque destruction.\", ii) being consistent with the later literature, iii) as it follows Sigma-Aldrich's naming scheme (BAM corresponding to Beta Amyloid Mouse)."
  },
  "AMGAB0031": {
    "Interaction ID": "AMGAB0031",
    "Antibody ID": "ABID0007.1",
    "Antibody name": "scFv-h3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1002/nbm.4263",
    "PMID": 32067292.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, immunofluorescence,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Treatment with scFv-h3D6 tended to reduce the number of plaques, mainly in the entorhinal and piriform cortex zones, as they were the regions within the 3xTg-AD mice brains where more plaques were detected. \", \"Figure 8. shows the quantification of the number (A, B) and intensity (C, D) of 6E10 immunoreactive (6E10+) neurons in both the hippocampus (A,C) and cortex (B, D). As can be observed, the 3xTg-AD/− values are higher than NTg values in all the plots, and the treatment is able to reduce the 3xTg-AD/− levels to values similar to those shown by the NTg groups.\", \"Figure 7\", Figure 8\", \"Moreover, it also agrees with differences observed at 12-mo by histological analyses, where the treatment was capable of diminishing Aβ pathology in both regions but had a higher effect in the cortex\", \"In addition, we have observed that scFv h3D6 reduces the amyloid plaque number and Aβ levels in protein extracts assessed at 12-mo.\",",
    "Curator Statement": false
  },
  "AMGAB0032": {
    "Interaction ID": "AMGAB0032",
    "Antibody ID": "ABID0153",
    "Antibody name": "Nb24",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Mutant P52G (P32G on the paper numeration)",
    "DOI": "10.1002/pro.2321",
    "PMID": 23904325.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"PDB 4KDT\", \"One nanobody (Nb24) that efficiently blocks fibril elongation was used as a chaperone to co-crystallize the Pro32Gly β2m monomer under physiological conditions.\", \"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0033": {
    "Interaction ID": "AMGAB0033",
    "Antibody ID": "ABID0153",
    "Antibody name": "Nb24",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Mutant ΔN6",
    "DOI": "10.1002/pro.2321",
    "PMID": 23904325.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0034": {
    "Interaction ID": "AMGAB0034",
    "Antibody ID": "ABID0153",
    "Antibody name": "Nb24",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Beta-2-microglobulin",
    "DOI": "10.1002/pro.2321",
    "PMID": 23904325.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0035": {
    "Interaction ID": "AMGAB0035",
    "Antibody ID": "ABID0154",
    "Antibody name": "Nb108",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Mutant P52G (P32G on the paper numeration)",
    "DOI": "10.1002/pro.2321",
    "PMID": 23904325.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"A nanobody raised against an irrelevant antigen (Nb108) was included in these seeding experiments as a negative control.\", \"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0036": {
    "Interaction ID": "AMGAB0036",
    "Antibody ID": "ABID0154",
    "Antibody name": "Nb108",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Mutant ΔN6",
    "DOI": "10.1002/pro.2321",
    "PMID": 23904325.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0037": {
    "Interaction ID": "AMGAB0037",
    "Antibody ID": "ABID0154",
    "Antibody name": "Nb108",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Beta-2-microglobulin",
    "DOI": "10.1002/pro.2321",
    "PMID": 23904325.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0038": {
    "Interaction ID": "AMGAB0038",
    "Antibody ID": "ABID0181",
    "Antibody name": "hWO-2 Fab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1002/pro.312",
    "PMID": 20014445.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Furthermore, in vitro the humanized antibody fragments were able to inhibit amyloid fibril formation, oligomer-mediated neurotoxicity, and disaggregating preformed amyloid fibrils.\", \"The activity of the hWO-2 Fab on Aβ1−42 fibril formation was examined by a thioflavine T (ThT) fluorescence assay over a period of 5 days. When Aβ1−42 was incubated with a control Fab (32G12, an irrelevant antibody), the fluorescence intensity increased over time indicating the formation of cross β-sheets structures in the solution, characteristic of insoluble amyloid protofibril and fibril formation. However, incubation of Aβ1−42 with hWO-2 Fab and cWO-2 Fab produced a significantly lower level of fluorescence [Fig. 4(A)].\", \"Figure 4\", \"In the presence of 32G12 Fab, the fluorescence decreased to 82% compared with the maximum fluorescence signal. In contrast, when treated with hWO-2 or cWO-2 Fab, the fluorescence signal decreases to ∼14% over the same time period. Together, these data imply that the humanized Fab fragment can inhibit the formation of Aβ1−42 amyloid fibrils and promote the disaggregation of preformed amyloid fibrils.\", \" Moreover, the abilities of hWO-2 Fab to inhibit aggregation and oligomer-mediated toxicity as well as promoting amyloid fibrils disaggregation show the value of such fragment for AD therapy.\"",
    "Curator Statement": false
  },
  "AMGAB0039": {
    "Interaction ID": "AMGAB0039",
    "Antibody ID": "ABID0182",
    "Antibody name": "cWO-2 Fab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1002/pro.312",
    "PMID": 20014445.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Furthermore, in vitro the humanized antibody fragments were able to inhibit amyloid fibril formation, oligomer-mediated neurotoxicity, and disaggregating preformed amyloid fibrils.\", \"The activity of the hWO-2 Fab on Aβ1−42 fibril formation was examined by a thioflavine T (ThT) fluorescence assay over a period of 5 days. When Aβ1−42 was incubated with a control Fab (32G12, an irrelevant antibody), the fluorescence intensity increased over time indicating the formation of cross β-sheets structures in the solution, characteristic of insoluble amyloid protofibril and fibril formation. However, incubation of Aβ1−42 with hWO-2 Fab and cWO-2 Fab produced a significantly lower level of fluorescence [Fig. 4(A)].\", \"Figure 4\", \"In the presence of 32G12 Fab, the fluorescence decreased to 82% compared with the maximum fluorescence signal. In contrast, when treated with hWO-2 or cWO-2 Fab, the fluorescence signal decreases to ∼14% over the same time period. Together, these data imply that the humanized Fab fragment can inhibit the formation of Aβ1−42 amyloid fibrils and promote the disaggregation of preformed amyloid fibrils.\", \" Moreover, the abilities of hWO-2 Fab to inhibit aggregation and oligomer-mediated toxicity as well as promoting amyloid fibrils disaggregation show the value of such fragment for AD therapy.\"",
    "Curator Statement": false
  },
  "AMGAB0040": {
    "Interaction ID": "AMGAB0040",
    "Antibody ID": "ABID0183",
    "Antibody name": "32G12",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1002/pro.312",
    "PMID": 20014445.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"The activity of the hWO-2 Fab on Aβ1−42 fibril formation was examined by a thioflavine T (ThT) fluorescence assay over a period of 5 days. When Aβ1−42 was incubated with a control Fab (32G12, an irrelevant antibody), the fluorescence intensity increased over time indicating the formation of cross β-sheets structures in the solution, characteristic of insoluble amyloid protofibril and fibril formation. However, incubation of Aβ1−42 with hWO-2 Fab and cWO-2 Fab produced a significantly lower level of fluorescence [Fig. 4(A)].\", \"Figure 4\", \"In the presence of 32G12 Fab, the fluorescence decreased to 82% compared with the maximum fluorescence signal. In contrast, when treated with hWO-2 or cWO-2 Fab, the fluorescence signal decreases to ∼14% over the same time period.\",",
    "Curator Statement": false
  },
  "AMGAB0041": {
    "Interaction ID": "AMGAB0041",
    "Antibody ID": "ABID0126",
    "Antibody name": "Nbα-syn01",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1002/pro.4875",
    "PMID": 38105512.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "Higher affinity for α‐syn fibrils than monomeric form",
    "Antibody paratope, CDR, or Negative control": "CDR3: S97-G110",
    "Quote of the interaction": "\"Nbα‐syn01 and ∆NterNbα‐syn01 were both found to inhibit the in‐vitro α‐syn seeded aggregation (Figure 6).\", \"Figure 6\"",
    "Curator Statement": "Different time points"
  },
  "AMGAB0042": {
    "Interaction ID": "AMGAB0042",
    "Antibody ID": "ABID0126",
    "Antibody name": "Nbα-syn01",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1002/pro.4875",
    "PMID": 38105512.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Nbα‐syn01 and ∆NterNbα‐syn01 were both found to inhibit the in‐vitro α‐syn seeded aggregation (Figure 6).\", \"Figure 6\"",
    "Curator Statement": false
  },
  "AMGAB0043": {
    "Interaction ID": "AMGAB0043",
    "Antibody ID": "ABID0127",
    "Antibody name": "ΔNterNbα-syn01",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1002/pro.4875",
    "PMID": 38105512.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "α-Synuclein peptide, residues 43–56",
    "Quote of the interaction": "\"Nbα‐syn01 and ∆NterNbα‐syn01 were both found to inhibit the in‐vitro α‐syn seeded aggregation (Figure 6).\", \"The designed truncated nanobody not only binds α‐syn peptide tightly but also efficiently inhibits aggregation in vitro. \", \"Figure 6\"",
    "Curator Statement": false
  },
  "AMGAB0044": {
    "Interaction ID": "AMGAB0044",
    "Antibody ID": "ABID0127",
    "Antibody name": "ΔNterNbα-syn01",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1002/pro.4875",
    "PMID": 38105512.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Nbα‐syn01 and ∆NterNbα‐syn01 were both found to inhibit the in‐vitro α‐syn seeded aggregation (Figure 6).\", \"The designed truncated nanobody not only binds α‐syn peptide tightly but also efficiently inhibits aggregation in vitro. \", \"Figure 6\"",
    "Curator Statement": false
  },
  "AMGAB0045": {
    "Interaction ID": "AMGAB0045",
    "Antibody ID": "ABID0128",
    "Antibody name": "NbS21A",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1002/pro.4875",
    "PMID": 38105512.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "α-Synuclein peptide, residues 43–56",
    "Quote of the interaction": "\"The NbS21A form did not inhibit the seeded aggregation as observed by initial Th‐S signal; however, the aggregation was delayed compared to the control (Figure 6).\", \"Figure 6\"",
    "Curator Statement": false
  },
  "AMGAB0046": {
    "Interaction ID": "AMGAB0046",
    "Antibody ID": "ABID0003",
    "Antibody name": "Donanemab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1002/trc2.12112",
    "PMID": 33614890.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Amyloid reduction of 40% to 50% was achieved. \", \"Donanemab 10 mg/kg intravenous can reduce amyloid deposits in Alzheimer's disease despite having a shorter than expected half‐life.\", \"Compared to placebo at 28 weeks, there was a statistically significant reduction in cerebral amyloid observed by PET at the highest dose of 10 mg/kg (P < 0.0002). The analysis showed a consistent reduction in cortical amyloid among patients receiving three to five doses of 10 mg/kg donanemab. The 10‐mg/kg IV arm had a mean SUVR change from baseline of −0.26 (standard deviation [SD] = 0.12), and a mean centiloid change from baseline of −44.4 (SD = 14.2), which corresponds to an average reduction of brain amyloid of 40% to 50%, compared to minimal change from baseline in the pooled placebo arms (Figure 4A).\", \"Figure 4\", \"The results suggest that as few as three to five doses of donanemab 10 mg/kg IV can substantially reduce amyloid deposits in AD. The significant reduction in brain amyloid after treatment with 10 mg/kg donanemab is consistent with the amyloid‐lowering observed with other amyloid therapies like bapineuzumab and gantenerumab. 7 , 8 , 9 The lack of change in plasma Aβ1‐40 and Aβ1‐42 supports the mechanism of action of donanemab being centered on deposited amyloid plaque rather than soluble forms of Aβ.\", \"Donanemab 10 mg/kg intravenous can reduce amyloid deposits in AD despite having a shorter than expected half‐life.\",",
    "Curator Statement": false
  },
  "AMGAB0047": {
    "Interaction ID": "AMGAB0047",
    "Antibody ID": "ABID0002.6",
    "Antibody name": "chGantenerumab",
    "Amyloid ID": "AGAMYID0001",
    "Amyloid name": "Aβ-38",
    "DOI": "10.1007/s00401-015-1484-2",
    "PMID": 26433971.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry, multiplex ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"3D6 significantly reduced the amount of aggregated (formic acid soluble) Aβ38 compared to Gantenerumab or irrelevant IgG2a injection (Fig. 3d, p = 0.0168 and p = 0.0073, respectively).\", \"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0048": {
    "Interaction ID": "AMGAB0048",
    "Antibody ID": "ABID0002.6",
    "Antibody name": "chGantenerumab",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1007/s00401-015-1484-2",
    "PMID": 26433971.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry, multiplex ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0049": {
    "Interaction ID": "AMGAB0049",
    "Antibody ID": "ABID0002.6",
    "Antibody name": "chGantenerumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s00401-015-1484-2",
    "PMID": 26433971.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry, multiplex ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"This translated into 3D6 effectively clearing plaques and reducing the levels of insoluble Aβ, whilst chGantenerumab and mC2 did not.\", \"Injection of 3D6 significantly reduced Aβ plaque load in comparison to chGantenerumab and mC2 (Fig. 2a, p = 0.0013 and p = 0.026, respectively). Due to the potential of antigenic masking by injected antibodies, Congo red staining was used to detect the clearance of congophilic deposits after antibody injection. 3D6 significantly reduced the number of Congo red-positive plaques in the hippocampus compared to irrelevant IgG2a and chGantenerumab injected animals (Fig. 2b, p = 0.0265 and p = 0.0178, respectively).\", \"Figure 2\", \"Figure 3\", \"3D6 significantly reduced the number of congophilic plaques compared to irrelevant IgG2a and chGantenerumab (p = 0.0265 and p = 0.0178, respectively).\", \"Gantenerumab did not significantly reduce the levels of Aβ, but detection of mouse IgG bound to plaques provides clear evidence for target engagement. \",",
    "Curator Statement": false
  },
  "AMGAB0050": {
    "Interaction ID": "AMGAB0050",
    "Antibody ID": "ABID0004.5",
    "Antibody name": "mC2",
    "Amyloid ID": "AGAMYID0001",
    "Amyloid name": "Aβ-38",
    "DOI": "10.1007/s00401-015-1484-2",
    "PMID": 26433971.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry, multiplex ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0051": {
    "Interaction ID": "AMGAB0051",
    "Antibody ID": "ABID0004.5",
    "Antibody name": "mC2",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1007/s00401-015-1484-2",
    "PMID": 26433971.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry, multiplex ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0052": {
    "Interaction ID": "AMGAB0052",
    "Antibody ID": "ABID0004.5",
    "Antibody name": "mC2",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s00401-015-1484-2",
    "PMID": 26433971.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"This translated into 3D6 effectively clearing plaques and reducing the levels of insoluble Aβ, whilst chGantenerumab and mC2 did not.\", \"Injection of 3D6 significantly reduced Aβ plaque load in comparison to chGantenerumab and mC2 (Fig. 2a, p = 0.0013 and p = 0.026, respectively). Due to the potential of antigenic masking by injected antibodies, Congo red staining was used to detect the clearance of congophilic deposits after antibody injection. 3D6 significantly reduced the number of Congo red-positive plaques in the hippocampus compared to irrelevant IgG2a and chGantenerumab injected animals (Fig. 2b, p = 0.0265 and p = 0.0178, respectively).\", \"Figure 2\", \"Figure 3\", \"3D6 significantly reduced the number of congophilic plaques compared to irrelevant IgG2a and chGantenerumab (p = 0.0265 and p = 0.0178, respectively).\", \"The antibody mC2 was unable to clear Aβ plaques 7 days post-injection, but unlike chGantenerumab, this antibody did not induce any detectable changes in microglial phenotype or cytokine levels, despite having similar effector function.\", \"Treatment with 3D6 is effective at clearing plaques, however, part of this response causes increased neuroinflammation.\",",
    "Curator Statement": false
  },
  "AMGAB0053": {
    "Interaction ID": "AMGAB0053",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0001",
    "Amyloid name": "Aβ-38",
    "DOI": "10.1007/s00401-015-1484-2",
    "PMID": 26433971.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry, multiplex ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"3D6 significantly reduced the amount of aggregated (formic acid soluble) Aβ38 compared to Gantenerumab or irrelevant IgG2a injection (Fig. 3d, p = 0.0168 and p = 0.0073, respectively).\",",
    "Curator Statement": false
  },
  "AMGAB0054": {
    "Interaction ID": "AMGAB0054",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1007/s00401-015-1484-2",
    "PMID": 26433971.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry, multiplex ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"3D6 also significantly lowered the amount of aggregated Aβ42 compared to irrelevant IgG2a (Fig. 3f, p = 0.041), and cleared aggregated Aβ40 in 50 % of mice treated with this antibody (Fig. 3e). chGantenerumab and mC2 did not induce significant changes to aggregated Aβ levels.\", \"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0055": {
    "Interaction ID": "AMGAB0055",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s00401-015-1484-2",
    "PMID": 26433971.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry, multiplex ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"This translated into 3D6 effectively clearing plaques and reducing the levels of insoluble Aβ, whilst chGantenerumab and mC2 did not.\", \"Injection of 3D6 significantly reduced Aβ plaque load in comparison to chGantenerumab and mC2 (Fig. 2a, p = 0.0013 and p = 0.026, respectively). Due to the potential of antigenic masking by injected antibodies, Congo red staining was used to detect the clearance of congophilic deposits after antibody injection. 3D6 significantly reduced the number of Congo red-positive plaques in the hippocampus compared to irrelevant IgG2a and chGantenerumab injected animals (Fig. 2b, p = 0.0265 and p = 0.0178, respectively).\", \"Figure 2\", \"3D6 also significantly lowered the amount of aggregated Aβ42 compared to irrelevant IgG2a (Fig. 3f, p = 0.041), and cleared aggregated Aβ40 in 50 % of mice treated with this antibody (Fig. 3e). chGantenerumab and mC2 did not induce significant changes to aggregated Aβ levels.\", \"Figure 3\",  \"3D6 significantly reduced the number of congophilic plaques compared to irrelevant IgG2a and chGantenerumab (p = 0.0265 and p = 0.0178, respectively).\", \"These observations are relevant for biological function, as 3D6, which had the strongest affinity for Aβ plaques in our model, was the only antibody to significantly reduce Aβ levels in vivo.\",",
    "Curator Statement": false
  },
  "AMGAB0056": {
    "Interaction ID": "AMGAB0056",
    "Antibody ID": "ABID0020.9",
    "Antibody name": "Antibody D",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1007/s00401-018-1911-2",
    "PMID": 30238240.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay,  Western Blot",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The selected antibody (D), directed to the mid-region of Tau (amino acids 235–250), potently blocked the seeding of human AD Tau and was also fully efficacious against seeds from progressive supranuclear palsy.\", \"Figure 7\", \"The most effective antibody tested against AD-PHF Tau was antibody D which fully neutralized seeding activity with an IC50 of 2.9 nM (Fig. 7).\", \"Generally, Tau antibodies binding the N- (antibodies A and B) or C-termini (antibody E) do not efficiently neutralize Tau seeds from Alzheimer’s disease. While antibody A was essentially inactive in this assay, antibody B did show activity against AD Tau, but only at high concentrations. Phospho-specific antibody C partially neutralized Tau seeds, while antibody D fully and efficiently neutralized Tau seeds. Antibody F showed only partial activity on AD Tau.\", \"Figure 8\", \"Table 2\", \"Antibody D was both fully efficacious and highly potent against PSP Tau seeds in our assay, yielding an IC50 of 5.6 nM (Fig. 8b and Table 2).\", \"Antibody D fully and efficiently neutralizes Tau seeds from PSP in addition to AD. Data were analyzed by one-way ANOVA followed by Dunnett’s post hoc test. ***P < 0.001, ****P < 0.0001\", \"Antibody D efficiently neutralizes Tau seeds from PSP as well as AD.\",",
    "Curator Statement": false
  },
  "AMGAB0057": {
    "Interaction ID": "AMGAB0057",
    "Antibody ID": "ABID0521",
    "Antibody name": "Antibody A",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1007/s00401-018-1911-2",
    "PMID": 30238240.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay, Microfluidic-based Tau aggregate spreading assay",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"When tested against AD-PHF Tau, antibodies A and E failed to substantially neutralize seeding activity in a dose-dependent manner (Fig. 7).\", \"Figure 7\", \"Generally, Tau antibodies binding the N- (antibodies A and B) or C-termini (antibody E) do not efficiently neutralize Tau seeds from Alzheimer’s disease. While antibody A was essentially inactive in this assay, antibody B did show activity against AD Tau, but only at high concentrations. Phospho-specific antibody C partially neutralized Tau seeds, while antibody D fully and efficiently neutralized Tau seeds. Antibody F showed only partial activity on AD Tau.\", \"This observation, however, did not fully explain the low-level activity exhibited by antibodies A and B as large proportions of full length Tau were also present.\",",
    "Curator Statement": false
  },
  "AMGAB0058": {
    "Interaction ID": "AMGAB0058",
    "Antibody ID": "ABID0559",
    "Antibody name": "Antibody C",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1007/s00401-018-1911-2",
    "PMID": 30238240.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay, Microfluidic-based Tau aggregate spreading assay",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" Neutralization of AD-PHF by antibody C also reached a plateau and failed to fully prevent seeding (Fig. 7).\", \"Figure 7\", \"Generally, Tau antibodies binding the N- (antibodies A and B) or C-termini (antibody E) do not efficiently neutralize Tau seeds from Alzheimer’s disease. While antibody A was essentially inactive in this assay, antibody B did show activity against AD Tau, but only at high concentrations. Phospho-specific antibody C partially neutralized Tau seeds, while antibody D fully and efficiently neutralized Tau seeds. Antibody F showed only partial activity on AD Tau.\", \"Antibody C, however, is a high-affinity antibody which exhibits good potency in our assay, but interestingly, the titration curve reaches a plateau at less than 60% inhibition.\",",
    "Curator Statement": false
  },
  "AMGAB0059": {
    "Interaction ID": "AMGAB0059",
    "Antibody ID": "ABID0560",
    "Antibody name": "Antibody B",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1007/s00401-018-1911-2",
    "PMID": 30238240.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay, Microfluidic-based Tau aggregate spreading assay",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" In contrast, antibody B demonstrated partial activity against AD-PHF Tau, neutralizing seeding activity by 74% (Fig. 7).\", \"Figure 7\", \"Generally, Tau antibodies binding the N- (antibodies A and B) or C-termini (antibody E) do not efficiently neutralize Tau seeds from Alzheimer’s disease. While antibody A was essentially inactive in this assay, antibody B did show activity against AD Tau, but only at high concentrations. Phospho-specific antibody C partially neutralized Tau seeds, while antibody D fully and efficiently neutralized Tau seeds. Antibody F showed only partial activity on AD Tau.\", \"This observation, however, did not fully explain the low-level activity exhibited by antibodies A and B as large proportions of full length Tau were also present.\",",
    "Curator Statement": false
  },
  "AMGAB0060": {
    "Interaction ID": "AMGAB0060",
    "Antibody ID": "ABID0561",
    "Antibody name": "Antibody E",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1007/s00401-018-1911-2",
    "PMID": 30238240.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay, Microfluidic-based Tau aggregate spreading assay",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"When tested against AD-PHF Tau, antibodies A and E failed to substantially neutralize seeding activity in a dose-dependent manner (Fig. 7).\", \"Figure 7\", \"Generally, Tau antibodies binding the N- (antibodies A and B) or C-termini (antibody E) do not efficiently neutralize Tau seeds from Alzheimer’s disease. While antibody A was essentially inactive in this assay, antibody B did show activity against AD Tau, but only at high concentrations. Phospho-specific antibody C partially neutralized Tau seeds, while antibody D fully and efficiently neutralized Tau seeds. Antibody F showed only partial activity on AD Tau.\",\"Indeed, antibody E was entirely inactive; however, this may be attributed to the fact that this antibody has a lower binding affinity than the other antibodies tested in this study.\",",
    "Curator Statement": false
  },
  "AMGAB0061": {
    "Interaction ID": "AMGAB0061",
    "Antibody ID": "ABID0562",
    "Antibody name": "Antibody F",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1007/s00401-018-1911-2",
    "PMID": 30238240.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay, Microfluidic-based Tau aggregate spreading assay",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 7\", \"Antibody F only exhibited activity against AD-PHF Tau at the highest concentrations tested (Fig. 7).\",\"Generally, Tau antibodies binding the N- (antibodies A and B) or C-termini (antibody E) do not efficiently neutralize Tau seeds from Alzheimer’s disease. While antibody A was essentially inactive in this assay, antibody B did show activity against AD Tau, but only at high concentrations. Phospho-specific antibody C partially neutralized Tau seeds, while antibody D fully and efficiently neutralized Tau seeds. Antibody F showed only partial activity on AD Tau.\",",
    "Curator Statement": false
  },
  "AMGAB0062": {
    "Interaction ID": "AMGAB0062",
    "Antibody ID": "ABID0029",
    "Antibody name": "ABBV-916",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s00401-025-02892-5",
    "PMID": 40455292.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"ABBV-916 significantly reduced dense plaques from brain tissue that were co-cultured with hiPSC-derived phagocytes.\", \"ABBV-916 stimulated amyloid plaque removal from unfixed APPPS1-21 brain tissue by hiPSC derived phagocytes\", \"Unfixed brain sections from 21 month-old APPPS1-21 mice were treated with 0, 1, 5 and 10 µg/mL ABBV-916 followed by co-culture with hiPSC-derived phagocytes for 72 hr (Fig. 3a). ABBV-916 led to significant reductions of amyloid plaques at 1, 5, or 10 µg/mL (Fig. 3b, c, n= 6, p < 0.0001 for the comparison of 1, 5, or 10 µg/mL to 0 µg/mL,).\", \"Figure 3\", \"ABBV-916 stimulated amyloid plaque removal from unfixed APPPS1-21 brain tissue by hiPSC derived phagocytes.\", \"When incubated with brain tissue containing amyloid plaques, ABBV-916 promoted plaque clearance by hiPSC-derived phagocytes in vitro.\",",
    "Curator Statement": false
  },
  "AMGAB0063": {
    "Interaction ID": "AMGAB0063",
    "Antibody ID": "ABID0029.5",
    "Antibody name": "ABBV-916 chi",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1007/s00401-025-02892-5",
    "PMID": 40455292.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "In vivo two-photon microscopy",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S3\", \" In the control antibody treated animals, the sizes of plaques and CAA continued to increase over an 8 weeks period. In ABBV-916 chi treated animals, the size of the plaques increased slower as compared to the control group (Fig. 6f, 2-way ANOVA, repeated measures, n = 12/group). After 4 weeks of treatment, the size of plaques in the ABBV-916 chi treated animals was significantly smaller than those in the control mIgG2a treated animals (Fig. 6g). However, ABBV-916 chi treatment did not have significant effects on the CAA volume around arteries over time (Supplementary Fig. 3c, d).\",",
    "Curator Statement": "Even if the effect is not statistically significant, it is visible in the total and in the weekly CAA volume."
  },
  "AMGAB0064": {
    "Interaction ID": "AMGAB0064",
    "Antibody ID": "ABID0029.5",
    "Antibody name": "ABBV-916 chi",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1007/s00401-025-02892-5",
    "PMID": 40455292.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "In vivo two-photon microscopy",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"ABBV-916 chi did not affect the CAA volume change over time in APPPS1-21 mice\", \"Supplementary Figure S3\", \" In the control antibody treated animals, the sizes of plaques and CAA continued to increase over an 8 weeks period. In ABBV-916 chi treated animals, the size of the plaques increased slower as compared to the control group (Fig. 6f, 2-way ANOVA, repeated measures, n = 12/group). After 4 weeks of treatment, the size of plaques in the ABBV-916 chi treated animals was significantly smaller than those in the control mIgG2a treated animals (Fig. 6g). However, ABBV-916 chi treatment did not have significant effects on the CAA volume around arteries over time (Supplementary Fig. 3c, d).\",",
    "Curator Statement": "Even if the effect is not statistically significant, it is visible in the total and in the weekly CAA volume."
  },
  "AMGAB0065": {
    "Interaction ID": "AMGAB0065",
    "Antibody ID": "ABID0029.5",
    "Antibody name": "ABBV-916 chi",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s00401-025-02892-5",
    "PMID": 40455292.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), In vivo two-photon microscopy",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-pyroglutamate-3 Aβ immunotherapy engages microglia and inhibits amyloid accumulation in transgenic mouse models of Aβ amyloidosis\", \"In addition, three months of weekly administration of ABBV-916 murine surrogate antibody significantly decreased amyloid plaques in APPPS1-21 mice. In vivo two-photon imaging revealed that the murine version of ABBV-916 inhibited the growth of the plaques in APPPS1-21 mice.\", \"Chronic dosing of ABBV-916 reduced amyloid plaques in APPPS1-21 mice\", \"The ratio of ABBV-916 plaques/Total plaques was 0.07% (n=20). After 3 months of treatment, APPPS1-21 mice treated with ABBV-916 chi had significantly lower total plaques and fibrillary plaques as compared to mice treated with control antibody (p<0.05, t-test, n=51–52, Fig. 5).\", \" In the control antibody treated animals, the sizes of plaques and CAA continued to increase over an 8 weeks period. In ABBV-916 chi treated animals, the size of the plaques increased slower as compared to the control group (Fig. 6f, 2-way ANOVA, repeated measures, n = 12/group). After 4 weeks of treatment, the size of plaques in the ABBV-916 chi treated animals was significantly smaller than those in the control mIgG2a treated animals (Fig. 6g). However, ABBV-916 chi treatment did not have significant effects on the CAA volume around arteries over time (Supplementary Fig. 3c, d).\", \"Figure 5\", \"Figure 6\", \"Three months of weekly treatment with ABBV-916 chimeric mIgG2a antibody significantly decreased amyloid plaques in the cortex of the APPPS1-21 mice despite only a small proportion of plaques containing ABBV-916 target.\", \"In APPPS1-21 mice, a single IV dose of ABBV-916 at 25 mg/kg and 50 mg/kg reached 66% and 90% target occupancy, respectively (Fig. 4). However, after 3 months of weekly IP injections at a similar dose (40 mg/kg), ABBV-916 only had a small effect on the total plaque load as compared to the control antibody.\", \"Additionally, in vivo two-photon longitudinal imaging suggested that ABBV-916 inhibited the growth of individual plaques instead of removing plaques in APPPS1-21 mice (Fig. 6f).\",",
    "Curator Statement": false
  },
  "AMGAB0066": {
    "Interaction ID": "AMGAB0066",
    "Antibody ID": "ABID0029.5",
    "Antibody name": "ABBV-916 chi",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1007/s00401-025-02892-5",
    "PMID": 40455292.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), In vivo two-photon microscopy",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Next, we examined the treatment effects on the AβpE3 amyloid. ABBV-916 chi antibody was used as primary antibody for the IHC. Although this method underestimated the efficacy because the ABBV-916 chi injected into the animal bound to the plaques and could also be detected by the anti-mIgG secondary antibody while the negative control antibody did not (Supplementary Fig. 4a), the treatment effects on the ABBV-916 IR plaques were stronger as compared to that on the total or fibrillary plaques (p<0.01, t-test, n=51–52, Supplementary Fig. 2).\", \"Figure 5\", \"Supplementary Figure S2\"",
    "Curator Statement": false
  },
  "AMGAB0067": {
    "Interaction ID": "AMGAB0067",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s12031-018-1139-6",
    "PMID": 30062438.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western Blot",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We also investigated its cellular and molecular mechanisms and found that scFv17 and 6E10 (a positive control) exhibited similar Aβ-clearing ability and that scFv17 produced a stronger effect in clearing Aβ oligomers than 6E10.\", \"Figure 1\", \"scFv17 and 6E10 effectively reduced Aβ immunopositive particle aggregation in the hippocampus and frontal cortex (Fig. 1a). The percentage of Aβ-positive stained area in the hippocampus of the APP/PS1 saline group (Fig. 1b) was 8.91 ± 0.80%. scFv17 and 6E10 treatments significantly decreased the positive area to 1.51 ± 0.25% (P < 0.001) and 1.61 ± 0.17% (P < 0.001), respectively. scFv17 and 6E10 also significantly reduced Aβ plaques in the frontal cortex (Fig. 1c) from 9.50 ± 0.55% in the saline group to 1.74 ± 0.32% (P < 0.001) and 1.46 ± 0.39% (P < 0.001), respectively.\", \"6E10 and scFv17 significantly reduced Aβ immunopositive aggregates to a nearly equivalent extent. ***P < 0.001, n = 6 for each group\", \"Notably, 6E10 injection decreased Aβ 12-mer (Fig. 2b) and Aβ 6-mer (Fig. 2c) levels from 100% in controls to 39.80 ± 9.61% (relative optical densities 6.79 ± 0.36 to 2.70 ± 0.65, P < 0.001) and 49.34 ± 19.89% (relative optical densities 0.48 ± 0.05 to 0.24 ± 0.10, P < 0.05), respectively. However, the levels of Aβ 3-mer (Fig. 2d) increased significantly from 100% in controls to 254.78 ± 4.39% (relative optical densities 0.20 ± 0.09 to 0.50 ± 0.01, P < 0.001).\", \"Figure 2\", \"scFv17 and 6E10 differentially altered the levels of Aβ oligomers in the hippocampus of APP/PS1 AD mice.\", \"6E10 injection decreased the levels of the Aβ 12-mer and Aβ 6-mer compared to the APP/PS1 saline group (b and c) but increased the level of the Aβ 3-mer (d).\", \"Our immunohistochemistry demonstrated that scFv17 and 6E10 produced a similar clearance effect on Aβ plaques in the frontal cortex and hippocampus of APP/PS1 mice (Fig. 1). However, scFv17 and 6E10 exhibited different effects on Aβ components in Western blot experiments (Fig. 2). scFv17 significantly reduced the levels of all Aβ oligomers, including the 12-mer, 6-mer, and 3-mer, which suggests that scFv17 decreased Aβ aggregation and inhibited Aβ production. 6E10 decreased only the 12-mer and 6-mer and significantly increased the Aβ 3-mer, which suggests that 6E10 inhibited Aβ aggregation but stimulated new Aβ production. scFv17 also exhibited stronger effects than 6E10 in clearing the 3-mer and 12-mer.\", \" scFv17 and 6E10 effectively cleared Aβ in the brain, and the production of neprilysin is proportionate to Aβ concentrations (Marr et al. 2003).\",",
    "Curator Statement": false
  },
  "AMGAB0068": {
    "Interaction ID": "AMGAB0068",
    "Antibody ID": "ABID0332",
    "Antibody name": "scFv17",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s12031-018-1139-6",
    "PMID": 30062438.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western Blot",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We also investigated its cellular and molecular mechanisms and found that scFv17 and 6E10 (a positive control) exhibited similar Aβ-clearing ability and that scFv17 produced a stronger effect in clearing Aβ oligomers than 6E10.\", \"scFv17 Reduced Aβ Load in APP/PS1 Mouse Brains\", \"Figure 1\", \"scFv17 and 6E10 effectively reduced Aβ immunopositive particle aggregation in the hippocampus and frontal cortex (Fig. 1a). The percentage of Aβ-positive stained area in the hippocampus of the APP/PS1 saline group (Fig. 1b) was 8.91 ± 0.80%. scFv17 and 6E10 treatments significantly decreased the positive area to 1.51 ± 0.25% (P < 0.001) and 1.61 ± 0.17% (P < 0.001), respectively. scFv17 and 6E10 also significantly reduced Aβ plaques in the frontal cortex (Fig. 1c) from 9.50 ± 0.55% in the saline group to 1.74 ± 0.32% (P < 0.001) and 1.46 ± 0.39% (P < 0.001), respectively.\", \"scFv17 reduced Aβ immunopositive aggregates in the hippocampus and frontal cortex of APP/PS1 AD mice.\", \"6E10 and scFv17 significantly reduced Aβ immunopositive aggregates to a nearly equivalent extent. ***P < 0.001, n = 6 for each group\", \"scFv17 injection significantly reduced the levels of all Aβ oligomers, including 12-mer, 6-mer, and 3-mer, from 100% in controls to 5.60 ± 1.53% (relative optical densities 6.79 ± 0.36 to 0.38 ± 0.10, P < 0.001), 49.25 ± 24.73% (relative optical densities 0.48 ± 0.05 to 0.24 ± 0.12, P < 0.05), and 65.48 ± 9.60% (relative optical densities 0.20 ± 0.09 to 0.13 ± 0.02, P > 0.05), respectively. A more prominent decrease was observed for the Aβ 12-mer.\", \"Figure 2\", \"scFv17 and 6E10 differentially altered the levels of Aβ oligomers in the hippocampus of APP/PS1 AD mice.\",\" However, scFv17 treatment significantly reduced all Aβ oligomers, including the Aβ 3-mer, with a prominent decline in the Aβ 12-mer. ***P < 0.001, n = 6 for each group\", \"Our immunohistochemistry demonstrated that scFv17 and 6E10 produced a similar clearance effect on Aβ plaques in the frontal cortex and hippocampus of APP/PS1 mice (Fig. 1). However, scFv17 and 6E10 exhibited different effects on Aβ components in Western blot experiments (Fig. 2). scFv17 significantly reduced the levels of all Aβ oligomers, including the 12-mer, 6-mer, and 3-mer, which suggests that scFv17 decreased Aβ aggregation and inhibited Aβ production. 6E10 decreased only the 12-mer and 6-mer and significantly increased the Aβ 3-mer, which suggests that 6E10 inhibited Aβ aggregation but stimulated new Aβ production. scFv17 also exhibited stronger effects than 6E10 in clearing the 3-mer and 12-mer.\", \" scFv17 and 6E10 effectively cleared Aβ in the brain, and the production of neprilysin is proportionate to Aβ concentrations (Marr et al. 2003).\", \"In summary, the present study demonstrated, for the first time, that the novel monoclonal anti-Aβ31-35 antibody scFv17 effectively cleared Aβ plaques and Aβ oligomers in the brains of APP/PS1 transgenic mice primarily via enhancement of the anti-inflammatory reaction and sAPPα activity.\",",
    "Curator Statement": false
  },
  "AMGAB0069": {
    "Interaction ID": "AMGAB0069",
    "Antibody ID": "ABID0198",
    "Antibody name": "IgVL5D3",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s12035-014-8691-z",
    "PMID": 24733587.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Prophylactic and therapeutic injection of rAAV9-IgVL5D3 reduced Aβ load in the ipsilateral hippocampus of AD model mice. No evidence of hemorrhages, increased vascular amyloid deposits, increased pro-inflammatory cytokines or infiltrating T cells in the brains was found in the experimental animals.\", \"IgVL5D3 Brain Expression via Prophylactic rAAV9 Injection Reduces Aβ Load in the Right Hippocampus\", \"Figure 5\", \"Diffuse and fibrillar Aβ deposits in the right brain hemispheres were visualized by 6E10 antibody (Fig. 5a) and fibrillar Aβ deposits were identified by thioflavin S fluorescence (Fig. 5c). The visualized areas were quantified by morphometric analysis and expressed as the percentage of area positive for Aβ immunohistochemistry or thioflavin fluorescence. The average Aβ loads in right hippocampus by 6E10 immunoreactivity were 0.315±0.030 and 0.470±0.058 % for mice treated with rAAV9-IgVL5D3 and PBS, respectively (Fig. 5b). The average Aβ loads in right neocortex by 6E10 immunoreactivity were 0.541±0.065 and 0.868±0.096 % for mice treated with rAAV9-IgVL5D3 and PBS, respectively (Fig. 5b). Thus, prophylactic injection of rAAV9-IgVL5D3 reduced the Aβ-immunoreactive deposits in the right hemisphere compared with PBS injection (p = 0.03 for the hippocampus and p = 0.01 for the neocortex). In the right hippocampus, the average amyloid load by thioflavin S fluorescence in rAAV9-IgVL5D3-treated mice (0.22±0.04 %) was significantly less than that in PBS-treated mice (0.36±0.05 %, p = 0.04) (Fig. 5d). Although, in the right neocortex, the average amyloid load by thioflavin fluorescence in rAAV9-IgVL5D3-treated mice (0.36±0.07 %) was less than that in PBS-treated (0.45±0.06 %, p = 0.24) mice, the difference was not significant. Thus, prophylactic rAAV9-IgVL5D3 injection reduced the Aβ load in the right hippocampus by approximately 20 to 40 % as compared with PBS injection.\", \"Prophylactic rAAV9-IgVL5D3 injection decreases Aβ load in the right hippocampus.\", \"IgVL5D3 Brain Expression via Therapeutic rAAV9 Injection Reduces Aβ-immunoreactive Deposits in the Right Hippocampus and Fibrillar Aβ Deposits in the Right Neocortex\", \"Figure 7\", \"Diffuse and fibrillar Aβ deposits in the right brain hemispheres were visualized by anti-Aβ 6E10 antibody (Fig. 7a) and fibrillar Aβ deposits were detected by thioflavin S fluorescence (Fig. 7c). The visualized areas were quantified by morphometric analysis. Aβ immunoreactive areas in the right hippocampus reduced in the rAAV9-IgVL5D3-treated transgenic group (1.38±0.09 %) compared to the PBS-treated transgenic group (1.86±0.13 %, p = 0.02) but the reduction in the neocortex in the rAAV9-IgVL5D3-treated group was not significant (1.97±0.11 for IgVL5D3 and 2.32±0.19 for PBS, p = 0.19) (Fig. 7b). Thioflavin S-positive areas in the right neocortex in the rAAV9-IgVL5D3-treated transgenic group (0.69±0.04 %) significantly decreased compared to those in the PBS-treated transgenic group (0.88±0.05 %, p = 0.03) but the reduction in the right hippocampus in the rAAV9-IgVL5D3-treated transgenic group barely missed its significance (0.47±0.05 for IgVL5D3 and 0.62±0.06 for PBS, P = 0.09) (Fig. 7d). The reasons for the discrepancies in Aβ load between Aβ-immunoreactivity and thioflavin S fluorescence are not clear but probably due to varying levels of IgVL5D3 expression and the small numbers of experimental animals. Thus, brain-targeted IgVL5D3 expression via therapeutic rAAV9 injection reduced Aβ-immunoreactive deposits in the right hippocampus and fibrillar Aβ deposits in the right neocortex.\", \"Therapeutic rAAV9-IgVL5D3 injection decreases Aβ-immunoreactive deposits in the right hippocampus and fibrillar Aβ-deposits in the right neocortex.\", \"In line with our hypothesis, prophylactic and therapeutic injection of rAAV9-IgVL5D3 into the right lateral ventricles of TgAPPswe/PS1dE9 mice reduced Aβ load without causing CAA, hemorrhages and inflammation.\",  \"Intracranial expression of IgVL5D3 via rAAV9 reduced the cerebral Aβ load without inducing brain inflammation, cerebral hemorrhages, and exacerbation of CAA.\",",
    "Curator Statement": false
  },
  "AMGAB0070": {
    "Interaction ID": "AMGAB0070",
    "Antibody ID": "ABID0138",
    "Antibody name": "AS",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s12035-014-8910-7",
    "PMID": 25330935.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Oligomers, Protofibrils,",
    "Antibody paratope, CDR, or Negative control": "{\"VH\": {\"CDR1\": \"GFTFSSQG\", \"CDR2\": \"IRRDGSNI\", \"CDR3\": \"AKGGSFDL\"},\"VL\": {\"CDR1\": \"QAIINS\", \"CDR2\": \"AAS\", \"CDR3\": \"QQSYSTLWT\"},}",
    "Quote of the interaction": "\"In this study, we studied a novel single-chain variable fragment (scFv), AS, generated from an antibody library of AD patients, which recognized and bound specifically to medium-size amyloid β peptide (Aβ42) oligomers and immature protofibrils (25–55 kDa) and, more importantly, reduced their level by blocking their formation or inducing their disassembly.\", \"scFv AS Inhibited Aβ42 Aggregation/Fibrillogenesis or Induced Disassembly of Aβ42 Aggregates In Vitro\", \"As shown in Fig. 3a–d, in the absence of scFv AS, Aβ42 peptide started to gradually form the larger aggregates after 3 h of incubation as monitored by ThT binding fluorescence. After 48 h of incubation, Aβ42 monomers, oligomers, or protofibrils gave relatively stronger fluorescence than the corresponding co-incubated Aβ42 samples with scFv AS (molar ratio 1:1, scFv:Aβ42), especially in the cases of Aβ42 oligomers or protofibrils (Fig. 3a–d). The remarkable decrease in the fluorescence intensity of these Aβ42 species in the presence of scFv AS (Fig. 3a–c) indicated that scFv AS bound to these Aβ42 species, especially Aβ42 oligomers or protofibrils, and effectively suppressed their further aggregation/fibrillogenesis.\", \"Figure 3\", \"In the series of experiments described above, scFv AS was also exhibited a certain ability to disaggregate already pre-formed Aβ42 aggregates, especially Aβ42 oligomers or protofibrils (Fig. 3b, c). The addition of scFv AS to the Aβ42 oligomers or protofibrils significantly reduced their fluorescence intensity (Fig. 3b, c) even to lower than their own baseline fluorescence intensity. Therefore, scFv AS not only effectively prevented the formation or further aggregation/fibrogenesis of Aβ42 oligomers or immature protofibrils but also facilitated their disassembly. However, no obvious decrease in fluorescence intensity was observed in Aβ42 fibrils even after 48 h of its co-incubation with scFv AS (Fig. 3d). These results were also indicated in a certain sense that scFv AS inhibited Aβ42 aggregation/fibrillogenesis more efficiently than induced disassembly of Aβ42 aggregates.\", \"The effects of scFv AS on Aβ42 aggregation/fibrillogenesis were further confirmed by electron microscopy after 24 h of co-incubation of the four Aβ42 species with scFv AS at 37 °C, respectively (Fig. 4). ScFv AS effectively blocked the assembly of Aβ42 monomer into larger aggregates in a large extent (Fig. 4a, b), suppressed the fibrillogenesis of Aβ42 oligomers or protofibrils (Fig. 4c–f), and induce the disassembly of Aβ42 oligomers into much smaller globular units (Fig. 4d) or induce Aβ42 protofibrils and fibrils into the amorphous and diffuse forms which were different from Aβ42 oligomers and which might be the huge Aβ42-AS complexes (Fig. 4f, h).\", \"Figure 4\", \"After 24 h of co-incubation with scFv AS at 37 °C, the state of Aβ42-M (b), Aβ42-O (d), Aβ42-P (f), or Aβ42-F (h) was easily distinguishable from that of the corresponding Aβ42-M (a), Aβ42-O (c), Aβ42-P (e), or Aβ42-F (g) in the absence of scFv AS. In the cases of Aβ42 protofibrils and Aβ42 fibrils, they were disassembled into amorphous or diffuse states (f and h, respectively) by 24 h of co-incubation with scFv AS. \", \"We found that scFv AS not only effectively suppressed the further aggregation/fibrogenesis of the medium-size Aβ42 oligomers and immature protofibrils (Figs. 3 and 4) but also ameliorated or prevented their cytotoxicity mainly because of its cytotoxicity-inhibiting activity either in SH-SY5Y cells or rat primary cultured neurons in vitro (Figs. 5 and 6 and Supplementary Figure 4); thus, it was believed that scFv AS would play a significant role in preventing the occurrence and development of AD after its entering the central nervous system because SH-SY5Y cells and rat primary cultured neurons provide a particularly amenable model system for both morphological and biochemical assessments of AD.\",",
    "Curator Statement": false
  },
  "AMGAB0071": {
    "Interaction ID": "AMGAB0071",
    "Antibody ID": "ABID0253",
    "Antibody name": "scFv-Bsec",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s12035-019-1597-z",
    "PMID": 31041656.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other: Congo Red staining,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"While both the iBsec1 and Diab constructs reduced plaque loads to similar extents, the Diab also increased sAPPα levels, improved neuronal health, and dramatically increased survival compared with iBsec1 by itself suggesting that tailoring APP processing by simultaneously inhibiting β-secretase processing of APP and promoting α-secretase processing is a promising therapeutic approach for treating both AD and other diseases such as Down’s syndrome which overexpress APP.\",\"Both scFv-Diab and scFv-Bsec Decrease Aβ Deposits in APP/PS1 Mice\", \"The number of 6E10-positive plaques was decreased in the cortex and the hippocampus of mice treated with scFv-Bsec or scFv-Diab compared with the GFP control group (Fig. 3b, *p < 0.05).\", \"Treatment with scFv-Bsec or scFv-Diab did not significantly decrease the number of Congo red–positive deposits in the cortex (Fig. 3e, p > 0.05) or the hippocampus (Fig. 3f, p > 0.05), indicating that the scFv-Bsec and scFv-Diab reduce formation of soluble amyloid aggregates but not insoluble fibrillar formation.\", \"Figure 3\",  \"Both scFv-Diab and scFv-Bsec Lowered Oligomeric Aβ Levels in APP/PS1 Mice\", \"Results showed a significant elevation in the levels of A4- and C6T-specific oligomers in the cortex and the hippocampus of transgenic vehicle mice compared with age-matched WT mice (Fig. 4a, b, ###p < 0.001). Treatment with scFv-Bsec and scFv-Diab lowered A4-reactive oligomeric Aβ levels in the cortex and the hippocampus, compared with vehicle transgenic mice (Fig. 4a, *p < 0.05). Similarly, C6T-recognized oligomeric Aβ levels were reduced in the mice treated with scFv-Diab and scFv-Bsec (Fig. 4b, *p < 0.05).\", \"Figure 4\", \"Consistent with the decreased levels of sAPPβ, we found decreased 6E10-positive Aβ deposits in both the scFv-Bsec- and scFv-Diab-treated mice, although insoluble Congo red–stained amyloid deposits did not decrease.\", \"It is not clear why soluble Aβ aggregates are decreased with treatment, but not insoluble aggregates, though various scenarios such as different aggregation pathways or locations could account for the difference. \", \"Both scFv-Bsec and scFv-Diab reduce β-site cleavage of APP, resulting in similar decreases in sAPPβ, A4- and C6T-recognizing Aβ oligomers, 6E10-positive Aβ deposit, and microgliosis.\",",
    "Curator Statement": "Not a statistical significant decrease, but decrease in plaque number"
  },
  "AMGAB0072": {
    "Interaction ID": "AMGAB0072",
    "Antibody ID": "ABID0254",
    "Antibody name": "scFv-Diab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s12035-019-1597-z",
    "PMID": 31041656.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other: Congo Red staining,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The diabody increased levels of sAPPα, decreased Aβ deposits and levels of oligomeric Aβ, increased neuronal health as indicated by MAP2 and synaptophysin staining, increased hippocampal neurogenesis, and most importantly dramatically increased survival rates compared with untreated mice or mice treated only with the β-secretase inhibitor.\", \"While both the iBsec1 and Diab constructs reduced plaque loads to similar extents, the Diab also increased sAPPα levels, improved neuronal health, and dramatically increased survival compared with iBsec1 by itself suggesting that tailoring APP processing by simultaneously inhibiting β-secretase processing of APP and promoting α-secretase processing is a promising therapeutic approach for treating both AD and other diseases such as Down’s syndrome which overexpress APP.\", \"Both scFv-Diab and scFv-Bsec Decrease Aβ Deposits in APP/PS1 Mice\", \"The number of 6E10-positive plaques was decreased in the cortex and the hippocampus of mice treated with scFv-Bsec or scFv-Diab compared with the GFP control group (Fig. 3b, *p < 0.05).\", \"Treatment with scFv-Bsec or scFv-Diab did not significantly decrease the number of Congo red–positive deposits in the cortex (Fig. 3e, p > 0.05) or the hippocampus (Fig. 3f, p > 0.05), indicating that the scFv-Bsec and scFv-Diab reduce formation of soluble amyloid aggregates but not insoluble fibrillar formation.\", \"Figure 3\", \"Both scFv-Diab and scFv-Bsec Lowered Oligomeric Aβ Levels in APP/PS1 Mice\", \"Results showed a significant elevation in the levels of A4- and C6T-specific oligomers in the cortex and the hippocampus of transgenic vehicle mice compared with age-matched WT mice (Fig. 4a, b, ###p < 0.001). Treatment with scFv-Bsec and scFv-Diab lowered A4-reactive oligomeric Aβ levels in the cortex and the hippocampus, compared with vehicle transgenic mice (Fig. 4a, *p < 0.05). Similarly, C6T-recognized oligomeric Aβ levels were reduced in the mice treated with scFv-Diab and scFv-Bsec (Fig. 4b, *p < 0.05).\", \"Figure 4\", \"Consistent with the decreased levels of sAPPβ, we found decreased 6E10-positive Aβ deposits in both the scFv-Bsec- and scFv-Diab-treated mice, although insoluble Congo red–stained amyloid deposits did not decrease.\", \"It is not clear why soluble Aβ aggregates are decreased with treatment, but not insoluble aggregates, though various scenarios such as different aggregation pathways or locations could account for the difference. \",  \"Both scFv-Bsec and scFv-Diab reduce β-site cleavage of APP, resulting in similar decreases in sAPPβ, A4- and C6T-recognizing Aβ oligomers, 6E10-positive Aβ deposit, and microgliosis.\", \"However, treatment with scFv-Diab, which simultaneously decreases amyloidogenic processing by inhibiting β-secretase activity while also promoting neuroprotective processing by promoting α-secretase activity, similarly decreased plaques and inflammation, and also restored neuronal health and dramatically increased survival rates.\",",
    "Curator Statement": "Not a statistical significant decrease, but decrease in plaque number"
  },
  "AMGAB0073": {
    "Interaction ID": "AMGAB0073",
    "Antibody ID": "ABID0291",
    "Antibody name": "SynTC1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1007/s12035-023-03211-3",
    "PMID": 36707462.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Immunocytochemistry",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Additionally, we found SynTCs differentially reduce α-Syn oligomeric polymorph-mediated neurotoxicity and propagation in primary cortical neurons in a polymorph-specific manner.\", \"When α-Syn oligomers are immunodepleted by SynTCs, cells exhibit differential reduction in toxicity and endogenous aggregation of α-Syn aggregates.\", \"SynTCs Differentially Reduce α-Syn Oligomeric Seeding in Primary Neurons\", \"We quantified average fluorescent intensity of α-Syn detected by Syn10842 (Fig. 4c, f, i) and LB509 (Fig. 4b, e, h) to evaluate total α-Syn propagation. SynODA exhibited the highest seeding propensity among the three polymorphs (Fig. 4a, d, g). SynOaCSF (Fig. 4a–c), SynODA (Fig. 4d–f), and SynODHA (Fig. 4g–i) were all differentially immunodepleted by all three SynTCs.\", \"Figure 4\", \"While multiple antibodies that target α-Syn are being developed and investigated, these antibodies target all forms of α-Syn rather than specific aggregates or polymorphisms of α-Syn aggregates [37– 39].\",",
    "Curator Statement": "The authors refer to α-Syn oligomeric polymorphs by their method of preparation: SynODA - in presence of Dopamine, SynODHA - in presence of Docosahexanoic acid, and SynOaCSF - in presence of artificial cerebrospinal fluid."
  },
  "AMGAB0074": {
    "Interaction ID": "AMGAB0074",
    "Antibody ID": "ABID0292",
    "Antibody name": "SynTC2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1007/s12035-023-03211-3",
    "PMID": 36707462.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Immunocytochemistry",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Additionally, we found SynTCs differentially reduce α-Syn oligomeric polymorph-mediated neurotoxicity and propagation in primary cortical neurons in a polymorph-specific manner.\", \"When α-Syn oligomers are immunodepleted by SynTCs, cells exhibit differential reduction in toxicity and endogenous aggregation of α-Syn aggregates.\", \"SynTCs Differentially Reduce α-Syn Oligomeric Seeding in Primary Neurons\", \"We quantified average fluorescent intensity of α-Syn detected by Syn10842 (Fig. 4c, f, i) and LB509 (Fig. 4b, e, h) to evaluate total α-Syn propagation. SynODA exhibited the highest seeding propensity among the three polymorphs (Fig. 4a, d, g). SynOaCSF (Fig. 4a–c), SynODA (Fig. 4d–f), and SynODHA (Fig. 4g–i) were all differentially immunodepleted by all three SynTCs.\", \"Figure 4\", \"While multiple antibodies that target α-Syn are being developed and investigated, these antibodies target all forms of α-Syn rather than specific aggregates or polymorphisms of α-Syn aggregates [37– 39].\",",
    "Curator Statement": "The authors refer to α-Syn oligomeric polymorphs by their method of preparation: SynODA - in presence of Dopamine, SynODHA - in presence of Docosahexanoic acid, and SynOaCSF - in presence of artificial cerebrospinal fluid."
  },
  "AMGAB0075": {
    "Interaction ID": "AMGAB0075",
    "Antibody ID": "ABID0293",
    "Antibody name": "SynTC3",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1007/s12035-023-03211-3",
    "PMID": 36707462.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Immunocytochemistry",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"SynTC3-immunodepleted neurons exhibiting the highest reduction in total α-Syn.\", \"Additionally, we found SynTCs differentially reduce α-Syn oligomeric polymorph-mediated neurotoxicity and propagation in primary cortical neurons in a polymorph-specific manner.\", \"When α-Syn oligomers are immunodepleted by SynTCs, cells exhibit differential reduction in toxicity and endogenous aggregation of α-Syn aggregates.\", \"SynTCs Differentially Reduce α-Syn Oligomeric Seeding in Primary Neurons\", \"We quantified average fluorescent intensity of α-Syn detected by Syn10842 (Fig. 4c, f, i) and LB509 (Fig. 4b, e, h) to evaluate total α-Syn propagation. SynODA exhibited the highest seeding propensity among the three polymorphs (Fig. 4a, d, g). SynOaCSF (Fig. 4a–c), SynODA (Fig. 4d–f), and SynODHA (Fig. 4g–i) were all differentially immunodepleted by all three SynTCs.\", \"Figure 4\", \"While multiple antibodies that target α-Syn are being developed and investigated, these antibodies target all forms of α-Syn rather than specific aggregates or polymorphisms of α-Syn aggregates [37– 39].\",",
    "Curator Statement": "The authors refer to α-Syn oligomeric polymorphs by their method of preparation: SynODA - in presence of Dopamine, SynODHA - in presence of Docosahexanoic acid, and SynOaCSF - in presence of artificial cerebrospinal fluid."
  },
  "AMGAB0076": {
    "Interaction ID": "AMGAB0076",
    "Antibody ID": "ABID0267",
    "Antibody name": "HS72",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s12035-023-03406-8",
    "PMID": 37326904.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, Immunohistochemistry, Histological (HE) staining, Enzyme-Linked Immunosorbent Assay (ELISA), Western Blot, HPLC,",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "VH-CDR1: SYGIS, VH-CDR2: GINTNTGNPAYAPGFTG, VH-CDR3: ARSSSGYQGSSYYFDMDV, VL-CDR1: RASRTISSYLN, VL-CDR2: AASILQS, VL-CDR3: QQSSSTP",
    "Quote of the interaction": "\"Degradation of Aβ42 aggregates by HS72 triggered a considerable disassembly or breakdown of the Aβ42 aggregates and greatly reduced their neurotoxicity. Aβ deposit/plaque load in the hippocampus of AD mice was reduced by approximately 27% after 7 days (once daily) of intravenous HS72 administration, while brain neural cells were greatly restored and their morphology was drastically improved. The above efficacies of HS72 were all greater than those of HT7, a simple anti-oligomeric Aβ42 scFv antibody.\", \"Although a catalytic anti-oligomeric Aβ42 antibody may have a slightly lower affinity for Aβ42 aggregates than a simple anti-oligomeric Aβ42 antibody, the former may display a stronger overall efficacy (dual efficacy of induction and catalysis) than the latter (induction alone) in clearing Aβ42 aggregates and improving histopathological changes in AD brain.\", \"Degradation of Aβ42 Aggregates Catalyzed by HS72\", \"In addition to its high binding specificity for Aβ42O, scFv HS72 was also able to catalyze the progressive degradation of Aβ42 species.\", \"Figure 2\", \"Nevertheless, Aβ42 levels gradually decreased over time in all three HS72-incubated groups, with a significant difference in the remaining Aβ42 levels between the HS72-catalyzed and their respective control groups from a certain time point onwards (*p < 0.05, **p < 0.01, and ***p < 0.001). This indicated that more and more Aβ42 molecules in these groups were catalytically degraded by HS72 over time. This was particularly the case for the Aβ42O group (Fig. 2B). For example, after 1 and 10 days of incubation of Aβ42O with HS72, the levels of Aβ42 decreased by about 4.8% and 11.2%, respectively. Precisely, the difference in mean levels of the remaining Aβ42 between the corresponding groups incubated with HT7 and HS72 was what accounted for the true share of proteolytic degradation of Aβ42 catalyzed by HS72 (Fig. 2C). Evidently, HS72 catalyzed the degradation of Aβ42 chains in an Aβ42 aggregate unit in a catalytic duration-dependent way, which was identical to the catalytic properties of typical enzymes. For example, after 1 and 10 days of incubation with HS72, about 4.3% and 9.4% of Aβ42O were degraded, respectively. Further, the capability and efficacy of HS72 in catalyzing Aβ42O degradation were significantly higher than its capability and efficacy in catalyzing Aβ42F degradation, indicating that although Aβ42O tended to further aggregate into Aβ42F during the incubation, the target binding and catalytic effect of HS72 greatly reduced further aggregation of Aβ42O. As a result, in the presence of HS72, the degradation rate of Aβ42O was almost always substantially higher than that of Aβ42F (Fig. 2C). \", \"Analysis of Aβ42-associated components in the degradation of Aβ42 aggregates catalyzed by HS72 by western blotting, and HPLC.\", \"Figure 3\", \"Finally, HS72 catalyzed the degradation of Aβ42 chain(s) in Aβ42O* and yielded free ΔAβ or small ΔAβ-Aβ42 oligomers (Aβ42O#); and (2) the release of the product ΔAβ from Aβ42O* after HS72 catalysis, either in the free form or as small ΔAβ-Aβ42 oligomers, was accompanied by the dissociation of a corresponding amount of Aβ42M from Aβ42O*. It could thus be proposed that the degradation of (large) Aβ42O and Aβ42F catalyzed by HS72 yielded ΔAβ, Aβ42M, and Aβ42O# but no intact small Aβ42O.\",  \"Additionally, almost no components with longer retention durations than small Aβ42O were found in the 1−10-day Aβ42M catalytic system (Fig. 3G), indicating that the induction and catalytic efficacy of HS72 together effectively inhibited or disrupted the greater aggregation of Aβ42.\", \"Overall, these results demonstrated that HS72 had a catalytic effect on Aβ42 aggregates, especially on Aβ42O, which was presumably attributed to two different residues in HS72: Asp45 and His241 (Fig. S1A).\", \"HS72 Significantly Reduces the Degree and Extent of Aβ42 Aggregation and Triggers a Specific Breakdown of Aβ42 Aggregates\", \"HS72 degraded approximately 5.6% of Aβ42 in the Aβ42O group within 48 h (Fig. 2C).\", \"Figure 5\", \"The fluorescence intensity in all four groups considerably decreased in the presence of scFv HT7 (gray diamonds), DS1 (black circles), and HS72 (black triangles) compared with the control (gray square), suggesting that scFv HT7, DS1, and HS72 could inhibit and/or prevent the assembly or aggregation of Aβ42 to some extent. HS72 inhibited Aβ42 assembly or aggregation more than HT7 and DS1, although no significant difference in the Aβ42 assembly inhibition was observed between the latter two groups. Evidently, the combination of antibody induction and catalysis by HS72 worked better than antibody induction alone by HT7 and DS1 in delaying or attenuating Aβ42 aggregation while also facilitating the initiation of the breakdown of Aβ42 aggregates.\", \"HS72 Improves Cell Morphology and Reduces Aβ Burden in the Brain of AD Mice\", \"Given that HS72 effectively degraded and disassembled Aβ42 aggregates (Figs. 3 and 5) and effectively protected neural cells from the neurotoxic effects of Aβ42 aggregates (Fig. 6), we used AD model mice to further analyze the effect of HS72 on the brain Aβ load using HE and IHC staining to determine the contribution of HS72 to reducing brain Aβ burden and maintaining a normal brain microenvironment in vivo.\",  \"Figure 7\", \"The hippocampal region in the positive control group had darker and larger Aβ spots (a in Fig. 7B, arrows), whereas in the HT7 (c in Fig. 7B) and HS72 (d in Fig. 7B) groups, the level of hippocampal Aβ deposits/plaques decreased, and the spots were lighter in color and smaller in size. Furthermore, the level of Aβ deposits/plaques was lower in the HS72 group than in the HT7 group (c and d in Fig. 7B).\",\"Both HS72 and HT7 reduced the amount of Aβ deposits and plaques. More specifically, HT7 and HS72 reduced the load of Aβ deposits and plaques in the hippocampal region by 5.6% and 27.4%, respectively, compared with the positive control group (100%) (**p < 0.01). There was also a significant difference in the amount of Aβ42 deposits and plaques between HS72 and HT7 groups (#p < 0.05). The quantity of Aβ deposits/plaques in the hippocampal region was also reduced in the HS72 and HT7 groups (Fig. 7D) (**p < 0.01), and the difference was more pronounced than the difference in the Aβ-positive area (##p < 0.01). These results showed that after 7 days of peripheral administration, scFv HS72 significantly induced a reduction in the level of Aβ deposits/plaques in the brains of AD mice, including a decrease in the Aβ42 deposit/plaque-positive areas, as well as a decrease in their number, demonstrating the efficacy of HS72 in reducing the brain Aβ42 burden. While the difference in this level was not significant between the HT7 and control groups after 7 days of HT7 administration, scFv HT7 induced a reduction in the level of Aβ deposits/plaques in the brains of AD mice.\", \"However, the significant differences in term of the Aβ-positive areas and Aβ deposit/plaque numbers between the HS72 and HT7 groups (Fig. 7C and D) consistently showed that the catalytic scFv antibody HS72 promoted the clearance of Aβ42 aggregates more efficiently than the simple scFv antibody HT7 in vivo. The dual effect of HS72-induced disassembly of Aβ aggregates and HS72-catalyzed degradation of Aβ aggregates resulted in the high efficacy of HS72 (Fig. 7B–D).\",",
    "Curator Statement": "Authors refer to monomers as Aβ42M, oligomers as Aβ42O , protofibrils as Aβ42P and fibrils as Aβ42F."
  },
  "AMGAB0077": {
    "Interaction ID": "AMGAB0077",
    "Antibody ID": "ABID0268",
    "Antibody name": "HT7",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s12035-023-03406-8",
    "PMID": 37326904.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, Immunohistochemistry, Histological (HE) staining",
    "Amyloid species identified": "Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "VH-CDR1: SYGIS, VH-CDR2: GINTNTGNPAYAPGFTG, VH-CDR3: ARSSSGYQGSSYYFDMDV, VL-CDR1: RASRTISSYLN, VL-CDR2: AASILQS, VL-CDR3: QQSSSTP",
    "Quote of the interaction": "\"The above efficacies of HS72 were all greater than those of HT7, a simple anti-oligomeric Aβ42 scFv antibody.\", \"Although a catalytic anti-oligomeric Aβ42 antibody may have a slightly lower affinity for Aβ42 aggregates than a simple anti-oligomeric Aβ42 antibody, the former may display a stronger overall efficacy (dual efficacy of induction and catalysis) than the latter (induction alone) in clearing Aβ42 aggregates and improving histopathological changes in AD brain.\", \"Figure 2\", \" While scFv HT7 was able to block the aggregation of some Aβ42M and induce the disassembly of some Aβ42O, the modest decrease in the immunoreactive signal of Aβ42 in these HT7-incubated groups is attributed to the slightly increased aggregation of Aβ42 molecules during incubation at 37 °C [16]. \", \"Figure 5\", \"The fluorescence intensity in all four groups considerably decreased in the presence of scFv HT7 (gray diamonds), DS1 (black circles), and HS72 (black triangles) compared with the control (gray square), suggesting that scFv HT7, DS1, and HS72 could inhibit and/or prevent the assembly or aggregation of Aβ42 to some extent. HS72 inhibited Aβ42 assembly or aggregation more than HT7 and DS1, although no significant difference in the Aβ42 assembly inhibition was observed between the latter two groups. Evidently, the combination of antibody induction and catalysis by HS72 worked better than antibody induction alone by HT7 and DS1 in delaying or attenuating Aβ42 aggregation while also facilitating the initiation of the breakdown of Aβ42 aggregates.\", \"Figure 7\", \"The hippocampal region in the positive control group had darker and larger Aβ spots (a in Fig. 7B, arrows), whereas in the HT7 (c in Fig. 7B) and HS72 (d in Fig. 7B) groups, the level of hippocampal Aβ deposits/plaques decreased, and the spots were lighter in color and smaller in size. Furthermore, the level of Aβ deposits/plaques was lower in the HS72 group than in the HT7 group (c and d in Fig. 7B).\", \"However, the significant differences in term of the Aβ-positive areas and Aβ deposit/plaque numbers between the HS72 and HT7 groups (Fig. 7C and D) consistently showed that the catalytic scFv antibody HS72 promoted the clearance of Aβ42 aggregates more efficiently than the simple scFv antibody HT7 in vivo. The dual effect of HS72-induced disassembly of Aβ aggregates and HS72-catalyzed degradation of Aβ aggregates resulted in the high efficacy of HS72 (Fig. 7B–D).\",",
    "Curator Statement": "Authors refer to monomers as Aβ42M, oligomers as Aβ42O , protofibrils as Aβ42P and fibrils as Aβ42F."
  },
  "AMGAB0078": {
    "Interaction ID": "AMGAB0078",
    "Antibody ID": "ABID0269",
    "Antibody name": "DS1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s12035-023-03406-8",
    "PMID": 37326904.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The purified DS1 (Fig. S1C) was incubated with Aβ42M, Aβ42O, and Aβ42F to confirm the necessity of residues Asp45 and His241 for HS72 catalysis. It was found that the effect of DS1 on Aβ42M, Aβ42O, and Aβ42F was almost identical to that of HT7 (data not shown). This demonstrates that residues Asp45 and His241 were both essential for the catalytic activity of HS72.\", \"Figure 5\", \"The fluorescence intensity in all four groups considerably decreased in the presence of scFv HT7 (gray diamonds), DS1 (black circles), and HS72 (black triangles) compared with the control (gray square), suggesting that scFv HT7, DS1, and HS72 could inhibit and/or prevent the assembly or aggregation of Aβ42 to some extent. HS72 inhibited Aβ42 assembly or aggregation more than HT7 and DS1, although no significant difference in the Aβ42 assembly inhibition was observed between the latter two groups. Evidently, the combination of antibody induction and catalysis by HS72 worked better than antibody induction alone by HT7 and DS1 in delaying or attenuating Aβ42 aggregation while also facilitating the initiation of the breakdown of Aβ42 aggregates.\", \"Both HS72 and HT7 reduced the amount of Aβ deposits and plaques. More specifically, HT7 and HS72 reduced the load of Aβ deposits and plaques in the hippocampal region by 5.6% and 27.4%, respectively, compared with the positive control group (100%) (**p < 0.01). There was also a significant difference in the amount of Aβ42 deposits and plaques between HS72 and HT7 groups (#p < 0.05). The quantity of Aβ deposits/plaques in the hippocampal region was also reduced in the HS72 and HT7 groups (Fig. 7D) (**p < 0.01), and the difference was more pronounced than the difference in the Aβ-positive area (##p < 0.01). These results showed that after 7 days of peripheral administration, scFv HS72 significantly induced a reduction in the level of Aβ deposits/plaques in the brains of AD mice, including a decrease in the Aβ42 deposit/plaque-positive areas, as well as a decrease in their number, demonstrating the efficacy of HS72 in reducing the brain Aβ42 burden. While the difference in this level was not significant between the HT7 and control groups after 7 days of HT7 administration, scFv HT7 induced a reduction in the level of Aβ deposits/plaques in the brains of AD mice.\",",
    "Curator Statement": "Authors refer to monomers as Aβ42M, oligomers as Aβ42O , protofibrils as Aβ42P and fibrils as Aβ42F."
  },
  "AMGAB0079": {
    "Interaction ID": "AMGAB0079",
    "Antibody ID": "ABID0268",
    "Antibody name": "HT7",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s12640-018-9955-6",
    "PMID": 30229545.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody",
    "Amyloid species identified": "Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Here, we obtained and characterized a novel anti-oligomeric Aβ42 aggregate scFv antibody, HT7, which could induce the significant disaggregation of Aβ42 aggregates through the release of stable and non-cytotoxic hexameric complexes that were composed of three scFv HT7s and one Aβ42 trimer, the latter being found to serve as the assembled subunit within larger Aβ42 aggregates in addition to existing freely between the cells.\", \"Our findings revealed that it was not sufficient for an anti-oligomeric Aβ42 antibody to exhibit high specificity and high affinity to the oligomeric Aβ42 aggregates in order to promote Aβ42 aggregate clearance and neutralize their cytotoxic effects.\", \"ScFv HT7 Inhibits Aβ42 Aggregation In Vitro\", \"The aggregations of the four Aβ42 species were clearly significantly repressed in the presence of scFv HT7, which differed somewhat from the case using scFv MO6 (Zhang et al. 2015a).\", \"Figure 3\", \"Firstly, despite the overall decrease in the aggregation of Aβ42 monomers in the presence of scFv HT7, the aggregation still occurred to some extent during the initial period (0–24 h), after which the aggregation tended to be stabilized by scFv HT7 to a constant level.\", \" Secondly, in the presence of scFv HT7, the primary Αβ42 oligomers and immature protofibrils were disaggregated to a certain degree into smaller Αβ42 oligomers during the initial 12-h period for Aβ42 oligomers or 48-h period for Aβ42 protofibrils (Fig. 3a(b, c)), whereas their further aggregation was significantly reduced. This showed that scFv HT7 could not only strongly inhibit further aggregation of the primary oligomeric Αβ42 aggregates, but also to a certain extent effectively reverse the formation, i.e., induced the disaggregation, of these Αβ42 aggregates, especially immature protofibrils.\", \" Finally, and strikingly, similar aggregation-inhibiting and disaggregation-inducing efficacy of scFv HT7 was also observed in Aβ42 fibrils. Although this did not reach significance (Fig. 3a(d)), it suggested that HT7 could also inhibit or even reduce the growth of Aβ42 fibrils to a certain extent, an effect that was barely observed for scFv MO6 (Zhang et al. 2015a).\", \"Electron microscopy further confirmed the inhibitory effect of scFv HT7 on Aβ42 aggregation 24 h after co-incubation with the four Aβ42 species (Fig. 3b). Aβ42 particles in the co-incubated Aβ42 monomer or oligomer reactions with scFv HT7 (Fig. 3b(b or d)) were much smaller than those in the corresponding controls (Fig. 3b(a or c)), indicating that scFv HT7 effectively repressed Aβ42 aggregation, while inducing their disaggregation into smaller oligomers.\", \"Taken together, the results shown in Fig. 3a, b demonstrated that scFv HT7 was not only able to inhibit Aβ42 aggregation but also to facilitate the gradual disassembly of oligomeric and even fibrillar Aβ42 aggregates into small Aβ42 oligomers in vitro.\", \"This enabled scFv HT7 to gradually induce the disaggregation of the larger Aβ42 aggregates as well as fibrils, while effectively inhibiting their further aggregation after recognizing and binding to the Aβ42 aggregates or fibrils. In particular, the specific recognition and the fitted binding of scFv HT7 to Aβ42 aggregates appeared to be a prerequisite for all the above effects of scFv HT7.\", \"This presumably occurred owing to the higher binding affinity of scFv HT7 to Aβ42 oligomers and protofibrils (Fig. 2) and the greater efficacy of scFv HT7 in inducing the disaggregation of Aβ42 oligomers and protofibrils (Fig. 3a, b).\", \"The presence of the hexameric complexes further indicated that once three scFv HT7 bound respectively to the three N-terminal regions of an Aβ42 trimer subunit, thus reaching scFv HT7 binding saturation, the bound scFv HT7s greatly attenuated the interaction of this Aβ42 trimer subunit with others and eventually led to the disassociation of the scFv HT7-saturated Aβ42 trimer subunit from larger Aβ42 aggregates or fibrils to release the non-cytotoxic hexameric complexes.\", \"In addition, in respect to scFv-induced disaggregation of Aβ42 aggregates, the manner of dissociating Aβ42 aggregates initially as Aβ42 trimer subunits, then into individual Aβ42 molecules appeared much more efficacious than that of dissociating Aβ42 aggregates directly into individual Aβ42 molecules one after another. Therefore, the efficacies of scFv HT7 in inducing the dissociation of Aβ42 aggregates as well as inhibiting Aβ42 aggregation, as shown in Fig. 3a, were significantly higher than those of scFv MO6 (Zhang et al. 2015a).\", \"In conclusion, this study revealed the subunit-assembly characteristics of Aβ42 aggregates and the post-saturation dissociation mechanism of the protective efficacy of an anti-oligomeric Aβ42 scFv antibody against the formation and cytotoxicity of oligomeric Aβ42 aggregates.\",",
    "Curator Statement": false
  },
  "AMGAB0080": {
    "Interaction ID": "AMGAB0080",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s13346-022-01117-6",
    "PMID": 35015254.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Accumulation of Aβ (1–42) was induced in the brain of 15-month-old App KI mice; however, obvious changes in Aβ (1–42) disposition were not observed after intranasal or i.v. administration.\", \"Figure 4\",",
    "Curator Statement": "The authors refer to the antibody as A594-AntiAβ. The insoluble levels of Aβ-42 after antibody administration intranasally show a non-significant decrease."
  },
  "AMGAB0081": {
    "Interaction ID": "AMGAB0081",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1007/s13346-022-01117-6",
    "PMID": 35015254.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\",",
    "Curator Statement": "The authors refer to the antibody as A594-AntiAβ. The insoluble levels of Aβ-42 after antibody administration intranasally show a non-significant decrease."
  },
  "AMGAB0082": {
    "Interaction ID": "AMGAB0082",
    "Antibody ID": "ABID0031",
    "Antibody name": "6C5",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.ajpath.2017.01.022",
    "PMID": 28408124.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay, Microfluidic-based Tau aggregate spreading assay",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The antibodies reduced tau uptake in an epitope-dependent manner: N-terminal (Tau13) and middomain (6C5 and HT7) antibodies successfully prevented uptake of tau species, whereas the distal C-terminal-specific antibody (Tau46) had little effect. Phosphorylation-dependent (40E8 and p396) and C-terminal half (4E4) tau antibodies also reduced tau uptake despite removing less total tau by immunodepletion, suggesting specific interactions with species involved in uptake. Among the seven antibodies evaluated, 6C5 most efficiently blocked uptake and subsequent aggregation.\", \"More important, 6C5 also blocked neuron-to-neuron spreading of tau in a unique three-chamber microfluidic device. Furthermore, 6C5 slowed down the progression of tau aggregation even after uptake had begun.\", \" The 6C5 or control IgG antibody was incubated with rTg4510 brain extracts and then directly added to primary neurons. At day 2, 6C5 significantly reduced neuronal tau uptake by 44% compared to control IgG (Figure 7).\", \"Figure 7\", \"Figure 8\", \"Figure 9\", \"The number of tau-aggregate positive neurons in the second chamber was significantly lower in the 6C5-treated neurons than in the control IgG (Figure 8), suggesting that 6C5 can block the interneuron propagation of tau.\", \"Furthermore, we examined whether the 6C5 antibody can slow down the progression of tau pathology: 6C5 or control IgG antibody was added to the neuron culture a day after the initiation of the tau-seed treatment (rTg4510 brain extract). The number of tau aggregate–positive neurons increases over time; however, treatment with 6C5 antibody had significantly less evidence of tau uptake by day 2 (a day after initiation of the antibody treatment) as compared to the control IgG-treated neurons (Figure 9).\", \"More important, the 6C5 antibody affected neuronal tau aggregations even after the uptake process had been initiated (Figure 9).\", \"Antibody D also shows full neutralization activity against Tau seeds from PSP\",",
    "Curator Statement": false
  },
  "AMGAB0083": {
    "Interaction ID": "AMGAB0083",
    "Antibody ID": "ABID0377",
    "Antibody name": "W20",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.bbapap.2011.09.005",
    "PMID": 21979582.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point), ELISA, Dot blot",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" Approximately 75% and 90% of Aβ40 aggregation was inhibited over the entire time-frame upon the addition of W8 and W20, respectively, at the molar ratio of 4:1 (Fig. 2D).\", \"Figure 2\", \"W8 and W20 completely inhibited the fibrillization of α-synuclein and amylin at the molar ratio of 4:1 (amyloid/scFv) (Fig. 3B, C, E, F), resulting in the formation of a substantial number of oligomeric species, while both oligomers and a few protofibrils appeared in the insulin and Aβ40 samples co-incubated with scFv antibodies at the same ratio (Fig. 3H, I, K, L).\", \"Figure 3\",\"In contrast, in the presence of W8 or W20, the ThT signal from the fibrils of α-synuclein, amylin, Aβ40, insulin and PrP dramatically decreased. W8 and W20 exhibited a similar ability to reduce the fluorescence intensity of amylin, Aβ40 and PrP, while W8 decreased the ThT signal from α-synuclein fibrils more efficiently than W20 (Fig. 4A). TEM imaging was consistent with the above fluorescence results. After 48-h incubation, the preformed fibrils of α-synuclein, amylin, insulin, Aβ40 and PrP remained as large fibrils (Fig. 4B, F, J, N, R). However, when the fibrils were co-incubated with W8 or W20, few fibrils but numerous oligomers in variety of sizes were observed in all samples except PrP (Fig. 4C, D, G, H, K, L, O, P). Fewer fibrils were observed in the PrP samples co-incubated with W8 or W20 compared with PrP alone (Fig. 4R, S, T). W8 and W20 exhibited a similar ability to disassociate preformed fibrils to oligomers.\", \"Figure 4\", \"The scFv inhibited fibrillization and cytotoxicity of various amyloids.\", \"The scFvs disaggregated preformed amyloid fibrils.\"",
    "Curator Statement": false
  },
  "AMGAB0084": {
    "Interaction ID": "AMGAB0084",
    "Antibody ID": "ABID0377",
    "Antibody name": "W20",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.bbapap.2011.09.005",
    "PMID": 21979582.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point), ELISA, Plot blot",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"When incubated with W8 or W20, 90% of α-synuclein (100 μM) and insulin (20 μM) fibrillization was inhibited at the molar ratio of 50:1 (amyloid/scFv) (Fig. 2A, C).\", \"Figure 2\", \"W8 and W20 completely inhibited the fibrillization of α-synuclein and amylin at the molar ratio of 4:1 (amyloid/scFv) (Fig. 3B, C, E, F), resulting in the formation of a substantial number of oligomeric species, while both oligomers and a few protofibrils appeared in the insulin and Aβ40 samples co-incubated with scFv antibodies at the same ratio (Fig. 3H, I, K, L).\", \"Figure 3\",\"In contrast, in the presence of W8 or W20, the ThT signal from the fibrils of α-synuclein, amylin, Aβ40, insulin and PrP dramatically decreased. W8 and W20 exhibited a similar ability to reduce the fluorescence intensity of amylin, Aβ40 and PrP, while W8 decreased the ThT signal from α-synuclein fibrils more efficiently than W20 (Fig. 4A). TEM imaging was consistent with the above fluorescence results. After 48-h incubation, the preformed fibrils of α-synuclein, amylin, insulin, Aβ40 and PrP remained as large fibrils (Fig. 4B, F, J, N, R). However, when the fibrils were co-incubated with W8 or W20, few fibrils but numerous oligomers in variety of sizes were observed in all samples except PrP (Fig. 4C, D, G, H, K, L, O, P). Fewer fibrils were observed in the PrP samples co-incubated with W8 or W20 compared with PrP alone (Fig. 4R, S, T). W8 and W20 exhibited a similar ability to disassociate preformed fibrils to oligomers.\", \"Figure 4\", \"The scFv inhibited fibrillization and cytotoxicity of various amyloids.\", \"The scFvs disaggregated preformed amyloid fibrils.\"",
    "Curator Statement": false
  },
  "AMGAB0085": {
    "Interaction ID": "AMGAB0085",
    "Antibody ID": "ABID0377",
    "Antibody name": "W20",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1016/j.bbapap.2011.09.005",
    "PMID": 21979582.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point), ELISA, Dot blot",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Around 90% of fibril formation of amylin and PrP 106–126 was inhibited at the molar ratio of 4:1 (amyloid/scFv) (Fig. 2B, E) while fibrillization of α-synuclein and insulin was completely inhibited at the same molar ratio of 4:1 (data not shown).\", \"Figure 2\", \"W8 and W20 completely inhibited the fibrillization of α-synuclein and amylin at the molar ratio of 4:1 (amyloid/scFv) (Fig. 3B, C, E, F), resulting in the formation of a substantial number of oligomeric species, while both oligomers and a few protofibrils appeared in the insulin and Aβ40 samples co-incubated with scFv antibodies at the same ratio (Fig. 3H, I, K, L).\", \"Figure 3\", \"In contrast, in the presence of W8 or W20, the ThT signal from the fibrils of α-synuclein, amylin, Aβ40, insulin and PrP dramatically decreased. W8 and W20 exhibited a similar ability to reduce the fluorescence intensity of amylin, Aβ40 and PrP, while W8 decreased the ThT signal from α-synuclein fibrils more efficiently than W20 (Fig. 4A). TEM imaging was consistent with the above fluorescence results. After 48-h incubation, the preformed fibrils of α-synuclein, amylin, insulin, Aβ40 and PrP remained as large fibrils (Fig. 4B, F, J, N, R). However, when the fibrils were co-incubated with W8 or W20, few fibrils but numerous oligomers in variety of sizes were observed in all samples except PrP (Fig. 4C, D, G, H, K, L, O, P). Fewer fibrils were observed in the PrP samples co-incubated with W8 or W20 compared with PrP alone (Fig. 4R, S, T). W8 and W20 exhibited a similar ability to disassociate preformed fibrils to oligomers.\", \"Figure 4\", \"The scFv inhibited fibrillization and cytotoxicity of various amyloids.\", \"The scFvs disaggregated preformed amyloid fibrils.\"",
    "Curator Statement": false
  },
  "AMGAB0086": {
    "Interaction ID": "AMGAB0086",
    "Antibody ID": "ABID0377",
    "Antibody name": "W20",
    "Amyloid ID": "AGAMYID0019",
    "Amyloid name": "Insulin",
    "DOI": "10.1016/j.bbapap.2011.09.005",
    "PMID": 21979582.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point), Dot blot, ELISA",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"When incubated with W8 or W20, 90% of α-synuclein (100 μM) and insulin (20 μM) fibrillization was inhibited at the molar ratio of 50:1 (amyloid/scFv) (Fig. 2A, C).\", \"Figure 2\", \"W8 and W20 completely inhibited the fibrillization of α-synuclein and amylin at the molar ratio of 4:1 (amyloid/scFv) (Fig. 3B, C, E, F), resulting in the formation of a substantial number of oligomeric species, while both oligomers and a few protofibrils appeared in the insulin and Aβ40 samples co-incubated with scFv antibodies at the same ratio (Fig. 3H, I, K, L).\", \"Figure 3\",\"In contrast, in the presence of W8 or W20, the ThT signal from the fibrils of α-synuclein, amylin, Aβ40, insulin and PrP dramatically decreased. W8 and W20 exhibited a similar ability to reduce the fluorescence intensity of amylin, Aβ40 and PrP, while W8 decreased the ThT signal from α-synuclein fibrils more efficiently than W20 (Fig. 4A). TEM imaging was consistent with the above fluorescence results. After 48-h incubation, the preformed fibrils of α-synuclein, amylin, insulin, Aβ40 and PrP remained as large fibrils (Fig. 4B, F, J, N, R). However, when the fibrils were co-incubated with W8 or W20, few fibrils but numerous oligomers in variety of sizes were observed in all samples except PrP (Fig. 4C, D, G, H, K, L, O, P). Fewer fibrils were observed in the PrP samples co-incubated with W8 or W20 compared with PrP alone (Fig. 4R, S, T). W8 and W20 exhibited a similar ability to disassociate preformed fibrils to oligomers.\", \"Figure 4\", \"The scFv inhibited fibrillization and cytotoxicity of various amyloids.\", \"The scFvs disaggregated preformed amyloid fibrils.\"",
    "Curator Statement": false
  },
  "AMGAB0087": {
    "Interaction ID": "AMGAB0087",
    "Antibody ID": "ABID0377",
    "Antibody name": "W20",
    "Amyloid ID": "AGAMYID0020",
    "Amyloid name": "Major prion protein",
    "DOI": "10.1016/j.bbapap.2011.09.005",
    "PMID": 21979582.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point), ELISA, Dot blot",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Around 90% of fibril formation of amylin and PrP 106–126 was inhibited at the molar ratio of 4:1 (amyloid/scFv) (Fig. 2B, E) while fibrillization of α-synuclein and insulin was completely inhibited at the same molar ratio of 4:1 (data not shown).\", \"Figure 2\", \"W8 and W20 also inhibited PrP aggregation, resulting in the formation of numerous oligomers and a few short fibrils (Fig. 3N, O).\", \"Figure 3\", \"In contrast, in the presence of W8 or W20, the ThT signal from the fibrils of α-synuclein, amylin, Aβ40, insulin and PrP dramatically decreased. W8 and W20 exhibited a similar ability to reduce the fluorescence intensity of amylin, Aβ40 and PrP, while W8 decreased the ThT signal from α-synuclein fibrils more efficiently than W20 (Fig. 4A). TEM imaging was consistent with the above fluorescence results. After 48-h incubation, the preformed fibrils of α-synuclein, amylin, insulin, Aβ40 and PrP remained as large fibrils (Fig. 4B, F, J, N, R). However, when the fibrils were co-incubated with W8 or W20, few fibrils but numerous oligomers in variety of sizes were observed in all samples except PrP (Fig. 4C, D, G, H, K, L, O, P). Fewer fibrils were observed in the PrP samples co-incubated with W8 or W20 compared with PrP alone (Fig. 4R, S, T). W8 and W20 exhibited a similar ability to disassociate preformed fibrils to oligomers.\", \"Figure 4\", \"The scFv inhibited fibrillization and cytotoxicity of various amyloids.\", \"The scFvs disaggregated preformed amyloid fibrils.\"",
    "Curator Statement": false
  },
  "AMGAB0088": {
    "Interaction ID": "AMGAB0088",
    "Antibody ID": "ABID0377",
    "Antibody name": "W20",
    "Amyloid ID": "AGAMYID0021",
    "Amyloid name": "Lysozyme C",
    "DOI": "10.1016/j.bbapap.2011.09.005",
    "PMID": 21979582.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point), ELISA, dot blot",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"However, the fluorescence intensity of lysozyme co-incubated with W8 and W20 (molar ratio of 4:1, amyloid/scFv) was significantly increased, indicating that W8 and W20 promoted fibril formation for lysozyme amyloids (Fig. 2F).\", \"Figure 2\", \"Consistent with the ThT results, the fibrillization of lysozyme was significantly promoted upon the addition of W8 and W20 (Fig. 3P–R).\", \"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0089": {
    "Interaction ID": "AMGAB0089",
    "Antibody ID": "ABID0474",
    "Antibody name": "W8",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.bbapap.2011.09.005",
    "PMID": 21979582.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point)",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" Approximately 75% and 90% of Aβ40 aggregation was inhibited over the entire time-frame upon the addition of W8 and W20, respectively, at the molar ratio of 4:1 (Fig. 2D).\", \"Figure 2\", \"W8 and W20 completely inhibited the fibrillization of α-synuclein and amylin at the molar ratio of 4:1 (amyloid/scFv) (Fig. 3B, C, E, F), resulting in the formation of a substantial number of oligomeric species, while both oligomers and a few protofibrils appeared in the insulin and Aβ40 samples co-incubated with scFv antibodies at the same ratio (Fig. 3H, I, K, L).\", \"Figure 3\", \"In contrast, in the presence of W8 or W20, the ThT signal from the fibrils of α-synuclein, amylin, Aβ40, insulin and PrP dramatically decreased. W8 and W20 exhibited a similar ability to reduce the fluorescence intensity of amylin, Aβ40 and PrP, while W8 decreased the ThT signal from α-synuclein fibrils more efficiently than W20 (Fig. 4A). TEM imaging was consistent with the above fluorescence results. After 48-h incubation, the preformed fibrils of α-synuclein, amylin, insulin, Aβ40 and PrP remained as large fibrils (Fig. 4B, F, J, N, R). However, when the fibrils were co-incubated with W8 or W20, few fibrils but numerous oligomers in variety of sizes were observed in all samples except PrP (Fig. 4C, D, G, H, K, L, O, P). Fewer fibrils were observed in the PrP samples co-incubated with W8 or W20 compared with PrP alone (Fig. 4R, S, T). W8 and W20 exhibited a similar ability to disassociate preformed fibrils to oligomers.\", \"Figure 4\", \"The scFv inhibited fibrillization and cytotoxicity of various amyloids.\", \"The scFvs disaggregated preformed amyloid fibrils.\"",
    "Curator Statement": false
  },
  "AMGAB0090": {
    "Interaction ID": "AMGAB0090",
    "Antibody ID": "ABID0474",
    "Antibody name": "W8",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.bbapap.2011.09.005",
    "PMID": 21979582.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point), ELISA, Dot - bot",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"When incubated with W8 or W20, 90% of α-synuclein (100 μM) and insulin (20 μM) fibrillization was inhibited at the molar ratio of 50:1 (amyloid/scFv) (Fig. 2A, C).\", \"Figure 2\", \"W8 and W20 completely inhibited the fibrillization of α-synuclein and amylin at the molar ratio of 4:1 (amyloid/scFv) (Fig. 3B, C, E, F), resulting in the formation of a substantial number of oligomeric species, while both oligomers and a few protofibrils appeared in the insulin and Aβ40 samples co-incubated with scFv antibodies at the same ratio (Fig. 3H, I, K, L).\", \"Figure 3\",\"In contrast, in the presence of W8 or W20, the ThT signal from the fibrils of α-synuclein, amylin, Aβ40, insulin and PrP dramatically decreased. W8 and W20 exhibited a similar ability to reduce the fluorescence intensity of amylin, Aβ40 and PrP, while W8 decreased the ThT signal from α-synuclein fibrils more efficiently than W20 (Fig. 4A). TEM imaging was consistent with the above fluorescence results. After 48-h incubation, the preformed fibrils of α-synuclein, amylin, insulin, Aβ40 and PrP remained as large fibrils (Fig. 4B, F, J, N, R). However, when the fibrils were co-incubated with W8 or W20, few fibrils but numerous oligomers in variety of sizes were observed in all samples except PrP (Fig. 4C, D, G, H, K, L, O, P). Fewer fibrils were observed in the PrP samples co-incubated with W8 or W20 compared with PrP alone (Fig. 4R, S, T). W8 and W20 exhibited a similar ability to disassociate preformed fibrils to oligomers.\", \"Figure 4\", \"The scFv inhibited fibrillization and cytotoxicity of various amyloids.\", \"The scFvs disaggregated preformed amyloid fibrils.\"",
    "Curator Statement": false
  },
  "AMGAB0091": {
    "Interaction ID": "AMGAB0091",
    "Antibody ID": "ABID0474",
    "Antibody name": "W8",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1016/j.bbapap.2011.09.005",
    "PMID": 21979582.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Light scattering - aggregation kinetics, TEM image in presence/absence of the antibody, ELISA, Dot blot",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Around 90% of fibril formation of amylin and PrP 106–126 was inhibited at the molar ratio of 4:1 (amyloid/scFv) (Fig. 2B, E) while fibrillization of α-synuclein and insulin was completely inhibited at the same molar ratio of 4:1 (data not shown).\", \"Figure 2\", \"W8 and W20 completely inhibited the fibrillization of α-synuclein and amylin at the molar ratio of 4:1 (amyloid/scFv) (Fig. 3B, C, E, F), resulting in the formation of a substantial number of oligomeric species, while both oligomers and a few protofibrils appeared in the insulin and Aβ40 samples co-incubated with scFv antibodies at the same ratio (Fig. 3H, I, K, L).\", \"Figure 3\", \"In contrast, in the presence of W8 or W20, the ThT signal from the fibrils of α-synuclein, amylin, Aβ40, insulin and PrP dramatically decreased. W8 and W20 exhibited a similar ability to reduce the fluorescence intensity of amylin, Aβ40 and PrP, while W8 decreased the ThT signal from α-synuclein fibrils more efficiently than W20 (Fig. 4A). TEM imaging was consistent with the above fluorescence results. After 48-h incubation, the preformed fibrils of α-synuclein, amylin, insulin, Aβ40 and PrP remained as large fibrils (Fig. 4B, F, J, N, R). However, when the fibrils were co-incubated with W8 or W20, few fibrils but numerous oligomers in variety of sizes were observed in all samples except PrP (Fig. 4C, D, G, H, K, L, O, P). Fewer fibrils were observed in the PrP samples co-incubated with W8 or W20 compared with PrP alone (Fig. 4R, S, T). W8 and W20 exhibited a similar ability to disassociate preformed fibrils to oligomers.\", \"Figure 4\", \"The scFv inhibited fibrillization and cytotoxicity of various amyloids.\", \"The scFvs disaggregated preformed amyloid fibrils.\"",
    "Curator Statement": false
  },
  "AMGAB0092": {
    "Interaction ID": "AMGAB0092",
    "Antibody ID": "ABID0474",
    "Antibody name": "W8",
    "Amyloid ID": "AGAMYID0019",
    "Amyloid name": "Insulin",
    "DOI": "10.1016/j.bbapap.2011.09.005",
    "PMID": 21979582.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Light scattering - aggregation kinetics, TEM image in presence/absence of the antibody, ELISA, Dot blot",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"When incubated with W8 or W20, 90% of α-synuclein (100 μM) and insulin (20 μM) fibrillization was inhibited at the molar ratio of 50:1 (amyloid/scFv) (Fig. 2A, C).\", \"Figure 2\", \"W8 and W20 completely inhibited the fibrillization of α-synuclein and amylin at the molar ratio of 4:1 (amyloid/scFv) (Fig. 3B, C, E, F), resulting in the formation of a substantial number of oligomeric species, while both oligomers and a few protofibrils appeared in the insulin and Aβ40 samples co-incubated with scFv antibodies at the same ratio (Fig. 3H, I, K, L).\", \"Figure 3\",\"In contrast, in the presence of W8 or W20, the ThT signal from the fibrils of α-synuclein, amylin, Aβ40, insulin and PrP dramatically decreased. W8 and W20 exhibited a similar ability to reduce the fluorescence intensity of amylin, Aβ40 and PrP, while W8 decreased the ThT signal from α-synuclein fibrils more efficiently than W20 (Fig. 4A). TEM imaging was consistent with the above fluorescence results. After 48-h incubation, the preformed fibrils of α-synuclein, amylin, insulin, Aβ40 and PrP remained as large fibrils (Fig. 4B, F, J, N, R). However, when the fibrils were co-incubated with W8 or W20, few fibrils but numerous oligomers in variety of sizes were observed in all samples except PrP (Fig. 4C, D, G, H, K, L, O, P). Fewer fibrils were observed in the PrP samples co-incubated with W8 or W20 compared with PrP alone (Fig. 4R, S, T). W8 and W20 exhibited a similar ability to disassociate preformed fibrils to oligomers.\", \"Figure 4\", \"The scFv inhibited fibrillization and cytotoxicity of various amyloids.\", \"The scFvs disaggregated preformed amyloid fibrils.\"",
    "Curator Statement": false
  },
  "AMGAB0093": {
    "Interaction ID": "AMGAB0093",
    "Antibody ID": "ABID0474",
    "Antibody name": "W8",
    "Amyloid ID": "AGAMYID0020",
    "Amyloid name": "Major prion protein",
    "DOI": "10.1016/j.bbapap.2011.09.005",
    "PMID": 21979582.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point)",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Around 90% of fibril formation of amylin and PrP 106–126 was inhibited at the molar ratio of 4:1 (amyloid/scFv) (Fig. 2B, E) while fibrillization of α-synuclein and insulin was completely inhibited at the same molar ratio of 4:1 (data not shown).\", \"Figure 2\", \"W8 and W20 also inhibited PrP aggregation, resulting in the formation of numerous oligomers and a few short fibrils (Fig. 3N, O).\", \"Figure 3\",\"In contrast, in the presence of W8 or W20, the ThT signal from the fibrils of α-synuclein, amylin, Aβ40, insulin and PrP dramatically decreased. W8 and W20 exhibited a similar ability to reduce the fluorescence intensity of amylin, Aβ40 and PrP, while W8 decreased the ThT signal from α-synuclein fibrils more efficiently than W20 (Fig. 4A). TEM imaging was consistent with the above fluorescence results. After 48-h incubation, the preformed fibrils of α-synuclein, amylin, insulin, Aβ40 and PrP remained as large fibrils (Fig. 4B, F, J, N, R). However, when the fibrils were co-incubated with W8 or W20, few fibrils but numerous oligomers in variety of sizes were observed in all samples except PrP (Fig. 4C, D, G, H, K, L, O, P). Fewer fibrils were observed in the PrP samples co-incubated with W8 or W20 compared with PrP alone (Fig. 4R, S, T). W8 and W20 exhibited a similar ability to disassociate preformed fibrils to oligomers.\", \"Figure 4\", \"The scFv inhibited fibrillization and cytotoxicity of various amyloids.\", \"The scFvs disaggregated preformed amyloid fibrils.\"",
    "Curator Statement": false
  },
  "AMGAB0094": {
    "Interaction ID": "AMGAB0094",
    "Antibody ID": "ABID0474",
    "Antibody name": "W8",
    "Amyloid ID": "AGAMYID0021",
    "Amyloid name": "Lysozyme C",
    "DOI": "10.1016/j.bbapap.2011.09.005",
    "PMID": 21979582.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point), ELISA, Dot blot",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"However, the fluorescence intensity of lysozyme co-incubated with W8 and W20 (molar ratio of 4:1, amyloid/scFv) was significantly increased, indicating that W8 and W20 promoted fibril formation for lysozyme amyloids (Fig. 2F).\", \"Figure 2\", \"Consistent with the ThT results, the fibrillization of lysozyme was significantly promoted upon the addition of W8 and W20 (Fig. 3P–R).\", \"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0095": {
    "Interaction ID": "AMGAB0095",
    "Antibody ID": "ABID0512",
    "Antibody name": "Anti-Aβ scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.bbi.2010.05.010",
    "PMID": 20595065.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Intramuscular delivery of a single chain antibody gene prevents brain Aβ deposition and cognitive impairment in a mouse model of Alzheimer's disease\", \"Brain Aβ plaque formation, Aβ accumulation, AD-type pathologies and cognitive impairment were significantly attenuated in scFv-treated APPSwe/PS1dE9 transgenic mice relative to EGFP-treated mice.\", \"Intramuscular delivery of scFv gene prevents Aβ deposition in the brain\", \"Compared with EGFP-treated mice (Fig. 3A and C), scFv-treated mice had a significantly lower area fraction and plaque density of both IHC (Fig. 3B) and Congo red (Fig. 3C) plaques in overall brain region (neocortex plus hippocampus), neocortex and hippocampus (Fig. 3E–G). ScFv-treated mice also had a smaller sized IHC and Congo red plaques than EGFP-treated mice.\", \"Figure 3\", \"Compared with EGFP-treated mice, scFv-treated mice had significantly lower levels of total Aβ, Aβ40, Aβ42, soluble and insoluble Aβ (Fig. 4A).\", \"Figure 4\", \"In the present study, we have demonstrated that intramuscular delivery of the gene encoding for a scFv against Aβ isolated from a human scFv library (Cai et al., 2003) is capable of preventing the Aβ accumulation and deposition in the brain, attenuating AD-type pathologies, and improving the cognitive functions of the APPSwe/PS1dE9 transgenic mice. \", \"In the present study we further confirmed the efficacy of intramuscular delivery of scFv gene by preventing the accumulation and deposition of Aβ in the brain and by functionally attenuating Aβ-related cognitive decline without eliciting microgliosis, microhemorrhage, systemic or local inflammatory responses.\",",
    "Curator Statement": false
  },
  "AMGAB0096": {
    "Interaction ID": "AMGAB0096",
    "Antibody ID": "ABID0571",
    "Antibody name": "m3.2",
    "Amyloid ID": "AGAMYID0022",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.bbr.2012.09.019",
    "PMID": 23000537.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Immunized Tg2576 mice had significantly less β-amyloid immunolabeling in the olfactory bulb and entorhinal cortex, yet showed elevations in Thioflavin-S labeled plaques in the piriform cortex.\", \"Table 1\", \"Figure 2\", \"In contrast, significant decreases in 4G8 staining within the OB (p<0.01) and EC (p<0.01) were observed in Tg2576+m3.2 mice compared to Tg2576+Ctl and Tg2576 mice. As a `non-olfactory' comparison, we additionally measured 4G8 and separately Thioflavin-S staining within the primary somatosensory and motor cortices (S1 and M1). Compared to Tg2576+Ctl mice, we found a significant decrease in 4G8 (p<0.05, 0.36 ± 0.15 [Ctl] vs 0.04 ± 0.01 [m3.2], mean ± SEM) and Thioflavin-S staining (p<0.01, 0.7 ± 0.09 [Ctl] vs 0.36 ± 0.07 [m3.2], mean ± SEM) in S1 and M1, consistent with our prior finding of a reduction in cortical β-amyloid following acute m3.2 immunization [31] (see Table 1).\", \"In contrast, we did find that 4G8 positive Aβ deposits were reduced within the OB and EC of Tg2576+m3.2 mice.\",",
    "Curator Statement": false
  },
  "AMGAB0097": {
    "Interaction ID": "AMGAB0097",
    "Antibody ID": "ABID0571",
    "Antibody name": "m3.2",
    "Amyloid ID": "AGAMYID0022",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.bbr.2012.09.019",
    "PMID": 23000537.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Immunized Tg2576 mice had significantly less β-amyloid immunolabeling in the olfactory bulb and entorhinal cortex, yet showed elevations in Thioflavin-S labeled plaques in the piriform cortex.\", \"Figure 2\", \"No effects of m3.2 immunization on Thioflavin-S staining in the other 3 structures analyzed were found (p>0.05, Tg2576+m3.2 vs. Tg2576+Ctl mice).\", \"Somewhat surprisingly, here we did not find that the remediation of olfactory habituation deficits in Tg2576 mice matched a reduction in Aβ deposition within the PCX (Figure 2), a region highly implicated in odor habituation [40]. Instead, Thioflavin-S positive Aβ actually increased in the PCX with chronic m3.2 immunization, despite the improvements in habituation behavior.\",",
    "Curator Statement": false
  },
  "AMGAB0098": {
    "Interaction ID": "AMGAB0098",
    "Antibody ID": "ABID0572",
    "Antibody name": "NT1",
    "Amyloid ID": "AGAMYID0022",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.bbr.2012.09.019",
    "PMID": 23000537.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0099": {
    "Interaction ID": "AMGAB0099",
    "Antibody ID": "ABID0013",
    "Antibody name": "PRX002",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.biopha.2025.118262",
    "PMID": 40554286.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Table 2\", \"α-syn Ab PRX002 led to a dose-dependent inhibition of the response achieving 98% inhibition at  10µg/ml. \", \"Although the 12F4 variants were not as effective as PRX002 in this model, they achieved levels of inhibition seen with other α-syn antibodies shown that will be discussed in detail in the following section.\", \" The five antibodies inhibited α-syn self-association at levels that ranged from 29 % to 98 %. 12F4 was least potent leading to only 29 % inhibition at 100 µg/ml. Each of the other 4 antibodies led to robust inhibition: 95 % at 10 µg/ml and 90 % at 100 µg/ml for Ab47, 54 % at 10 µg/ml and 65 % at 100 µg/ml for GM37, and 70 % at 10 µg/ml and 80 % at 100 µg/ ml for aslo0452, with PRX002 being the most potent with 98 % inhibition at 10 µg/ml. In this aggregation assay, the C-terminal antibodies appear to approach a maximum inhibition of > 95 % although GM37 and aslo0452 were less effective.\", \"For example, while Ab47 and aslo0452 showed  generally  similar  activity  across  the  three  assays,  GM37  was most  potent  in  blocking  uptake  and  reducing  pS129  formation  while PRX002  was most  potent  in blocking uptake and  reducing α-syn self-association.\", \"Table 3\", \"In this simplified system, PRX002 and Ab47 inhibited aggregation by > 95 %, levels that were not seen in any of the other models by any of the  antibodies.\", \"Since  PRX002  and  Ab47  bind  an  overlapping  epitope (aa118–126  vs  aa121–127),  one  can  hypothesize  that  this  sequence within  the  acidic  domain  of  α-syn  is  particularly  important  and  that preventing binding of the acidic domain to its cellular targets with the antibodies  accounts  for  the  near  quantitative  inhibition  seen  in  the model.\",",
    "Curator Statement": false
  },
  "AMGAB0100": {
    "Interaction ID": "AMGAB0100",
    "Antibody ID": "ABID0014.5",
    "Antibody name": "12F4",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.biopha.2025.118262",
    "PMID": 40554286.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Table 2\", \" By contrast, 12F4 treatment led to a 10% inhibition of α-syn aggregation at 10µg/ml and a 29% inhibition at 100µg/ml, while  treatment with the high affinity 12F4 HAM1 led to ~55% and Tetra1  and 2 led to 70–78% inhibition at 10 and 100µg/ml.\", \"Although the 12F4 variants were not as effective as PRX002 in this model, they achieved levels of inhibition seen with other α-syn antibodies shown that will be discussed in detail in the following section.\", \" The five antibodies inhibited α-syn self-association at levels that ranged from 29 % to 98 %. 12F4 was least potent leading to only 29 % inhibition at 100 µg/ml. Each of the other 4 antibodies led to robust inhibition: 95 % at 10 µg/ml and 90 % at 100 µg/ml for Ab47, 54 % at 10 µg/ml and 65 % at 100 µg/ml for GM37, and 70 % at 10 µg/ml and 80 % at 100 µg/ ml for aslo0452, with PRX002 being the most potent with 98 % inhibition at 10 µg/ml. In this aggregation assay, the C-terminal antibodies appear to approach a maximum inhibition of > 95 % although GM37 and aslo0452 were less effective.\", \"Table 3\", \"Treatment with 12F4 only led to 29 % inhibition.\"",
    "Curator Statement": false
  },
  "AMGAB0101": {
    "Interaction ID": "AMGAB0101",
    "Antibody ID": "ABID0014.9",
    "Antibody name": "HAM1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.biopha.2025.118262",
    "PMID": 40554286.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Table 2\", \" By contrast, 12F4 treatment led to a 10% inhibition of α-syn aggregation at 10µg/ml and a 29% inhibition at 100µg/ml, while  treatment with the high affinity 12F4 HAM1 led to ~55% and Tetra1  and 2 led to 70–78% inhibition at 10 and 100µg/ml.\", \"Although the 12F4 variants were not as effective as PRX002 in this model, they achieved levels of inhibition seen with other α-syn antibodies shown that will be discussed in detail in the following section.\", \"The engineering efforts we applied  to  12F4,  which  led  to  molecules  with  greater  affinity  and/or avidity  and  improved  the  performance  of  the  variants  in  the  assays compared  to  12F4,  but  they  were  largely  inferior  to  the  C-terminal targeted antibodies.\", \"Table 3\", \"HAM1 and the tetravalent 12F4 led to significant functional improvements in all three of the functional assays, but interestingly, HAM1 was most effective in the uptake assay whereas the tetravalent version was more active in the pS129 and aggregation assays. The weaker activity of HAM1 in the pS129 and aggregation assays was surprising since the binding characteristics resembled that of the PRX002, GM37, and aslo0452 C-terminal antibodies, suggesting that binding affinity alone is not a good predictor of activity.\"",
    "Curator Statement": false
  },
  "AMGAB0102": {
    "Interaction ID": "AMGAB0102",
    "Antibody ID": "ABID0014.9.2",
    "Antibody name": "Tetra1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.biopha.2025.118262",
    "PMID": 40554286.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Table 2\", \" By contrast, 12F4 treatment led to a 10% inhibition of α-syn aggregation at 10µg/ml and a 29% inhibition at 100µg/ml, while  treatment with the high affinity 12F4 HAM1 led to ~55% and Tetra1  and 2 led to 70–78% inhibition at 10 and 100µg/ml.\", \"Although the 12F4 variants were not as effective as PRX002 in this model, they achieved levels of inhibition seen with other α-syn antibodies shown that will be discussed in detail in the following section.\", \"The engineering efforts we applied  to  12F4,  which  led  to  molecules  with  greater  affinity  and/or avidity  and  improved  the  performance  of  the  variants  in  the  assays compared  to  12F4,  but  they  were  largely  inferior  to  the  C-terminal targeted antibodies.\", \"Table 3\", \"HAM1 and the tetravalent 12F4 led to significant functional improvements in all three of the functional assays, but interestingly, HAM1 was most effective in the uptake assay whereas the tetravalent version was more active in the pS129 and aggregation assays. The weaker activity of HAM1 in the pS129 and aggregation assays was surprising since the binding characteristics resembled that of the PRX002, GM37, and aslo0452 C-terminal antibodies, suggesting that binding affinity alone is not a good predictor of activity.\"",
    "Curator Statement": false
  },
  "AMGAB0103": {
    "Interaction ID": "AMGAB0103",
    "Antibody ID": "ABID0014.9.3",
    "Antibody name": "Tetra2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.biopha.2025.118262",
    "PMID": 40554286.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Table 2\", \" By contrast, 12F4 treatment led to a 10% inhibition of α-syn aggregation at 10µg/ml and a 29% inhibition at 100µg/ml, while  treatment with the high affinity 12F4 HAM1 led to ~55% and Tetra1  and 2 led to 70–78% inhibition at 10 and 100µg/ml.\", \"Although the 12F4 variants were not as effective as PRX002 in this model, they achieved levels of inhibition seen with other α-syn antibodies shown that will be discussed in detail in the following section.\", \"The engineering efforts we applied  to  12F4,  which  led  to  molecules  with  greater  affinity  and/or avidity  and  improved  the  performance  of  the  variants  in  the  assays compared  to  12F4,  but  they  were  largely  inferior  to  the  C-terminal targeted antibodies.\", \"Table 3\", \"HAM1 and the tetravalent 12F4 led to significant functional improvements in all three of the functional assays, but interestingly, HAM1 was most effective in the uptake assay whereas the tetravalent version was more active in the pS129 and aggregation assays. The weaker activity of HAM1 in the pS129 and aggregation assays was surprising since the binding characteristics resembled that of the PRX002, GM37, and aslo0452 C-terminal antibodies, suggesting that binding affinity alone is not a good predictor of activity.\"",
    "Curator Statement": false
  },
  "AMGAB0104": {
    "Interaction ID": "AMGAB0104",
    "Antibody ID": "ABID0015.6",
    "Antibody name": "GM37",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.biopha.2025.118262",
    "PMID": 40554286.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Table 2\", \" The five antibodies inhibited α-syn self-association at levels that ranged from 29 % to 98 %. 12F4 was least potent leading to only 29 % inhibition at 100 µg/ml. Each of the other 4 antibodies led to robust inhibition: 95 % at 10 µg/ml and 90 % at 100 µg/ml for Ab47, 54 % at 10 µg/ml and 65 % at 100 µg/ml for GM37, and 70 % at 10 µg/ml and 80 % at 100 µg/ ml for aslo0452, with PRX002 being the most potent with 98 % inhibition at 10 µg/ml. In this aggregation assay, the C-terminal antibodies appear to approach a maximum inhibition of > 95 % although GM37 and aslo0452 were less effective.\", \"By  contrast,  GM37  was  not  very  effective  in  reducing α-syn self-association and PRX002 was not very effective in lowering the formation of pS129.\", \"Table 3\", \" The GM37 antibody treatment was less effective and led to 65 % inhibition.\",",
    "Curator Statement": false
  },
  "AMGAB0105": {
    "Interaction ID": "AMGAB0105",
    "Antibody ID": "ABID0016.5",
    "Antibody name": "Ab47",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.biopha.2025.118262",
    "PMID": 40554286.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Table 2\", \" The five antibodies inhibited α-syn self-association at levels that ranged from 29 % to 98 %. 12F4 was least potent leading to only 29 % inhibition at 100 µg/ml. Each of the other 4 antibodies led to robust inhibition: 95 % at 10 µg/ml and 90 % at 100 µg/ml for Ab47, 54 % at 10 µg/ml and 65 % at 100 µg/ml for GM37, and 70 % at 10 µg/ml and 80 % at 100 µg/ ml for aslo0452, with PRX002 being the most potent with 98 % inhibition at 10 µg/ml. In this aggregation assay, the C-terminal antibodies appear to approach a maximum inhibition of > 95 % although GM37 and aslo0452 were less effective.\", \"For  instance,  aslo0452  showed  dose dependent  reduction  of  pS129  formation  and  α-syn  self-association, while  Ab47  showed  no  dose  dependence  in  reducing  pS129  signals and was less potent at the higher dose to reduce the self-association of α-syn.\", \"Table 3\", \"In this simplified system, PRX002 and Ab47 inhibited aggregation by > 95 %, levels that were not seen in any of the other models by any of the  antibodies.\", \"Since  PRX002  and  Ab47  bind  an  overlapping  epitope (aa118–126  vs  aa121–127),  one  can  hypothesize  that  this  sequence within  the  acidic  domain  of  α-syn  is  particularly  important  and  that preventing binding of the acidic domain to its cellular targets with the antibodies  accounts  for  the  near  quantitative  inhibition  seen  in  the model.\",",
    "Curator Statement": false
  },
  "AMGAB0106": {
    "Interaction ID": "AMGAB0106",
    "Antibody ID": "ABID0017.9",
    "Antibody name": "aslo0452",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.biopha.2025.118262",
    "PMID": 40554286.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Table 2\", \" The five antibodies inhibited α-syn self-association at levels that ranged from 29 % to 98 %. 12F4 was least potent leading to only 29 % inhibition at 100 µg/ml. Each of the other 4 antibodies led to robust inhibition: 95 % at 10 µg/ml and 90 % at 100 µg/ml for Ab47, 54 % at 10 µg/ml and 65 % at 100 µg/ml for GM37, and 70 % at 10 µg/ml and 80 % at 100 µg/ ml for aslo0452, with PRX002 being the most potent with 98 % inhibition at 10 µg/ml. In this aggregation assay, the C-terminal antibodies appear to approach a maximum inhibition of > 95 % although GM37 and aslo0452 were less effective.\", \"For  instance,  aslo0452  showed  dose dependent  reduction  of  pS129  formation  and  α-syn  self-association, while  Ab47  showed  no  dose  dependence  in  reducing  pS129  signals and was less potent at the higher dose to reduce the self-association of α-syn.\", \"Table 3\",",
    "Curator Statement": false
  },
  "AMGAB0107": {
    "Interaction ID": "AMGAB0107",
    "Antibody ID": "ABID0371",
    "Antibody name": "A1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.bpc.2016.11.002",
    "PMID": 27863716.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In the presence of the two best binders from the dot blot analysis, A1 and A2, aSN only forms few fibrils; instead, the images are dominated by amorphous aggregates. With A1 and A2, these aggregates tend to associate in contiguous networks and the overall amount of aggregated material is comparable to that of antibody-free aSN control.\", \"Figure 3\", \"Table 1\", \"In summary, our TEM data indicate that A1, A2 and A4 can all direct aggregation of aSN largely into non-fibrillar species and A4 in addition keeps most aSN soluble (i.e. non-aggregated). A5 and A3 show a weaker ability to redirect aSN to amorphous aggregates, but still have a significant impact compared to the low-binding antibody A6 as well as the negative control.\",\" Two C-terminal antibodies, A1, A2, which bind all aSN species well (Fig. 1), also inhibit fibrillation according to TEM, rerouting aSN to largely amorphous aggregates.\", \"Antibodies A1 and A2 showing strong binding to the monomer, affected the fibrillation of aSN. A3 and A4 only showed weak binding to monomeric aSN according to dot blots. Nevertheless, A4 showed good inhibition of fibrillation, in contrast to A3.\",\"Antibodies against the C-terminus of α-synuclein modulate its fibrillation\", \"Generally, the antibodies with strongest binding to aggregated aSN in dot blot, also inhibited fibrillation and membrane permeabilization the most, and promoted formation of amorphous aggregates surrounded by small and thin fibers.\", \"Antibodies targeting the C-terminus of alpha synuclein inhibit its fibrillation.\", \"Furthermore, C-terminal targeting antibodies affect the fibrillation and the ability of the oligomers to permeabilize membranes to some extent.\",\"Several of the antibodies inhibited fibrillation in vitro, and the inhibition appeared to depend on the apparent binding affinity evaluated by dot blot analysis\",",
    "Curator Statement": false
  },
  "AMGAB0108": {
    "Interaction ID": "AMGAB0108",
    "Antibody ID": "ABID0372",
    "Antibody name": "A2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.bpc.2016.11.002",
    "PMID": 27863716.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In the presence of the two best binders from the dot blot analysis, A1 and A2, aSN only forms few fibrils; instead, the images are dominated by amorphous aggregates. With A1 and A2, these aggregates tend to associate in contiguous networks and the overall amount of aggregated material is comparable to that of antibody-free aSN control.\", \"Figure 3\", \"Table 1\", \"In summary, our TEM data indicate that A1, A2 and A4 can all direct aggregation of aSN largely into non-fibrillar species and A4 in addition keeps most aSN soluble (i.e. non-aggregated). A5 and A3 show a weaker ability to redirect aSN to amorphous aggregates, but still have a significant impact compared to the low-binding antibody A6 as well as the negative control.\",\" Two C-terminal antibodies, A1, A2, which bind all aSN species well (Fig. 1), also inhibit fibrillation according to TEM, rerouting aSN to largely amorphous aggregates.\", \"Antibodies A1 and A2 showing strong binding to the monomer, affected the fibrillation of aSN. A3 and A4 only showed weak binding to monomeric aSN according to dot blots. Nevertheless, A4 showed good inhibition of fibrillation, in contrast to A3.\",\"Antibodies against the C-terminus of α-synuclein modulate its fibrillation\", \"Generally, the antibodies with strongest binding to aggregated aSN in dot blot, also inhibited fibrillation and membrane permeabilization the most, and promoted formation of amorphous aggregates surrounded by small and thin fibers.\", \"Antibodies targeting the C-terminus of alpha synuclein inhibit its fibrillation.\", \"Furthermore, C-terminal targeting antibodies affect the fibrillation and the ability of the oligomers to permeabilize membranes to some extent.\",\"Several of the antibodies inhibited fibrillation in vitro, and the inhibition appeared to depend on the apparent binding affinity evaluated by dot blot analysis\",",
    "Curator Statement": false
  },
  "AMGAB0109": {
    "Interaction ID": "AMGAB0109",
    "Antibody ID": "ABID0373",
    "Antibody name": "A3",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.bpc.2016.11.002",
    "PMID": 27863716.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" In contrast, A4 leads to an overall low density of aggregates, which means that the amorphous aggregates (and the few fibrils observed) tend to be more isolated.\", \"Figure 3\", \"Table 1\", \"In summary, our TEM data indicate that A1, A2 and A4 can all direct aggregation of aSN largely into non-fibrillar species and A4 in addition keeps most aSN soluble (i.e. non-aggregated). A5 and A3 show a weaker ability to redirect aSN to amorphous aggregates, but still have a significant impact compared to the low-binding antibody A6 as well as the negative control.\",\"Antibodies A3 and A4, which showed weaker binding, also have an effect on fibrillation.\", \"Antibodies A1 and A2 showing strong binding to the monomer, affected the fibrillation of aSN. A3 and A4 only showed weak binding to monomeric aSN according to dot blots. Nevertheless, A4 \"Antibodies against the C-terminus of α-synuclein modulate its fibrillation\", \"Generally, the antibodies with strongest binding to aggregated aSN in dot blot, also inhibited fibrillation and membrane permeabilization the most, and promoted formation of amorphous aggregates surrounded by small and thin fibers.\", \"Antibodies targeting the C-terminus of alpha synuclein inhibit its fibrillation.\", \"Furthermore, C-terminal targeting antibodies affect the fibrillation and the ability of the oligomers to permeabilize membranes to some extent.\",showed good inhibition of fibrillation, in contrast to A3.\",\"Several of the antibodies inhibited fibrillation in vitro, and the inhibition appeared to depend on the apparent binding affinity evaluated by dot blot analysis\", \"Several of the antibodies inhibited fibrillation in vitro, and the inhibition appeared to depend on the apparent binding affinity evaluated by dot blot analysis\",",
    "Curator Statement": false
  },
  "AMGAB0110": {
    "Interaction ID": "AMGAB0110",
    "Antibody ID": "ABID0374",
    "Antibody name": "A4",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.bpc.2016.11.002",
    "PMID": 27863716.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" In contrast, A4 leads to an overall low density of aggregates, which means that the amorphous aggregates (and the few fibrils observed) tend to be more isolated.\", \"Figure 3\", \"Table 1\", \"In summary, our TEM data indicate that A1, A2 and A4 can all direct aggregation of aSN largely into non-fibrillar species and A4 in addition keeps most aSN soluble (i.e. non-aggregated). A5 and A3 show a weaker ability to redirect aSN to amorphous aggregates, but still have a significant impact compared to the low-binding antibody A6 as well as the negative control.\",\"Antibodies A3 and A4, which showed weaker binding, also have an effect on fibrillation. Remarkably, antibody A4 was able to retain most of aSN in a soluble state (Fig. 3, Table 1).\",\"Antibodies A1 and A2 showing strong binding to the monomer, affected the fibrillation of aSN. A3 and A4 only showed weak binding to monomeric aSN according to dot blots. Nevertheless, A4 showed good inhibition of fibrillation, in contrast to A3.\",\"Antibodies against the C-terminus of α-synuclein modulate its fibrillation\", \"Generally, the antibodies with strongest binding to aggregated aSN in dot blot, also inhibited fibrillation and membrane permeabilization the most, and promoted formation of amorphous aggregates surrounded by small and thin fibers.\", \"Antibodies targeting the C-terminus of alpha synuclein inhibit its fibrillation.\", \"Furthermore, C-terminal targeting antibodies affect the fibrillation and the ability of the oligomers to permeabilize membranes to some extent.\",\"Several of the antibodies inhibited fibrillation in vitro, and the inhibition appeared to depend on the apparent binding affinity evaluated by dot blot analysis\",",
    "Curator Statement": false
  },
  "AMGAB0111": {
    "Interaction ID": "AMGAB0111",
    "Antibody ID": "ABID0375",
    "Antibody name": "A5",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.bpc.2016.11.002",
    "PMID": 27863716.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" In contrast, A4 leads to an overall low density of aggregates, which means that the amorphous aggregates (and the few fibrils observed) tend to be more isolated.\", \"Figure 3\", \"Table 1\", \"In summary, our TEM data indicate that A1, A2 and A4 can all direct aggregation of aSN largely into non-fibrillar species and A4 in addition keeps most aSN soluble (i.e. non-aggregated). A5 and A3 show a weaker ability to redirect aSN to amorphous aggregates, but still have a significant impact compared to the low-binding antibody A6 as well as the negative control.\",\"Antibodies against the C-terminus of α-synuclein modulate its fibrillation\", \"Generally, the antibodies with strongest binding to aggregated aSN in dot blot, also inhibited fibrillation and membrane permeabilization the most, and promoted formation of amorphous aggregates surrounded by small and thin fibers.\", \"Antibodies targeting the C-terminus of alpha synuclein inhibit its fibrillation.\", \"Furthermore, C-terminal targeting antibodies affect the fibrillation and the ability of the oligomers to permeabilize membranes to some extent.\",\"Several of the antibodies inhibited fibrillation in vitro, and the inhibition appeared to depend on the apparent binding affinity evaluated by dot blot analysis\",",
    "Curator Statement": false
  },
  "AMGAB0112": {
    "Interaction ID": "AMGAB0112",
    "Antibody ID": "ABID0376",
    "Antibody name": "A6",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.bpc.2016.11.002",
    "PMID": 27863716.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"Table 1\", \"In summary, our TEM data indicate that A1, A2 and A4 can all direct aggregation of aSN largely into non-fibrillar species and A4 in addition keeps most aSN soluble (i.e. non-aggregated). A5 and A3 show a weaker ability to redirect aSN to amorphous aggregates, but still have a significant impact compared to the low-binding antibody A6 as well as the negative control.\",",
    "Curator Statement": false
  },
  "AMGAB0113": {
    "Interaction ID": "AMGAB0113",
    "Antibody ID": "ABID0458",
    "Antibody name": "Anti-pS409",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.celrep.2016.06.099",
    "PMID": 27475227.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Western blot,",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Both antibodies reduced accumulation of tau pathology in Tau-P301L transgenic mice and protected cultured neurons against extracellular tau-induced toxicity.\", \"Full effector and effectorless tau antibodies slow the spread of tau pathology in vivo\", \"To biochemically assess the effect of antibody treatment on tau pathology, hippocampi from the left hemispheres were homogenized and fractionated for western blot analysis of insoluble phospho-tau. Both WT and DANG anti-pS409-Tau variants significantly lowered insoluble levels of phospho-tau, with no significant difference between the antibodies (Figures 3C–3E).\", \"Figure 3\", \"Reduction in Hippocampal Tau Pathology in P301L-Tg Mice following 3 Months Weekly Intraperitoneal Dosing with Anti-pS409\", \" In vivo, we show that tau antibodies can slow the accumulation of tau pathology when it is still building up and spreading, but not at an older age when pathology has plateaued.\",",
    "Curator Statement": false
  },
  "AMGAB0114": {
    "Interaction ID": "AMGAB0114",
    "Antibody ID": "ABID0458",
    "Antibody name": "Anti-pS409",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.celrep.2016.06.099",
    "PMID": 27475227.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Western blot,",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Importantly, 3-month dosing of older animals starting at 11.5 months of age, when pathology is already maximally established (see Figure 1B) did not reduce hippocampal tau pathology (Figure S3). Taken together, these results suggest that in vivo, tau antibodies do not clear existing intra-neuronal pathology but rather slow down the spread of pathology in earlier stages of propagation.\", \" pS409-tau antibodies do not clear existing tau pathology in aged Tau P301L-Tg mice, related to Figure 3.\", \" In vivo, we show that tau antibodies can slow the accumulation of tau pathology when it is still building up and spreading, but not at an older age when pathology has plateaued.\",",
    "Curator Statement": "The antibody did not clear pre-existing insoluble tau in aged mice."
  },
  "AMGAB0115": {
    "Interaction ID": "AMGAB0115",
    "Antibody ID": "ABID0459",
    "Antibody name": "Anti-pS409 DANG",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.celrep.2016.06.099",
    "PMID": 27475227.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Western blot,",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Both antibodies reduced accumulation of tau pathology in Tau-P301L transgenic mice and protected cultured neurons against extracellular tau-induced toxicity.\", \"Full effector and effectorless tau antibodies slow the spread of tau pathology in vivo\", \"To biochemically assess the effect of antibody treatment on tau pathology, hippocampi from the left hemispheres were homogenized and fractionated for western blot analysis of insoluble phospho-tau. Both WT and DANG anti-pS409-Tau variants significantly lowered insoluble levels of phospho-tau, with no significant difference between the antibodies (Figures 3C–3E).\", \"Figure 3\", \"Reduction in Hippocampal Tau Pathology in P301L-Tg Mice following 3 Months Weekly Intraperitoneal Dosing with Anti-pS409\", \" In vivo, we show that tau antibodies can slow the accumulation of tau pathology when it is still building up and spreading, but not at an older age when pathology has plateaued.\",",
    "Curator Statement": false
  },
  "AMGAB0116": {
    "Interaction ID": "AMGAB0116",
    "Antibody ID": "ABID0459",
    "Antibody name": "Anti-pS409 DANG",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.celrep.2016.06.099",
    "PMID": 27475227.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Western blot,",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Importantly, 3-month dosing of older animals starting at 11.5 months of age, when pathology is already maximally established (see Figure 1B) did not reduce hippocampal tau pathology (Figure S3). Taken together, these results suggest that in vivo, tau antibodies do not clear existing intra-neuronal pathology but rather slow down the spread of pathology in earlier stages of propagation.\", \" pS409-tau antibodies do not clear existing tau pathology in aged Tau P301L-Tg mice, related to Figure 3.\", \" In vivo, we show that tau antibodies can slow the accumulation of tau pathology when it is still building up and spreading, but not at an older age when pathology has plateaued.\",",
    "Curator Statement": "The antibody did not clear pre-existing insoluble tau in aged mice."
  },
  "AMGAB0117": {
    "Interaction ID": "AMGAB0117",
    "Antibody ID": "ABID0199",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"Figure S2\", \"We found that the T138cysteamine variant displays a potentiated ability to inhibit specifically the k+kn parameter compared with the unaltered DesAb-Aβ(3–9) (Figures 2B and 2C).\", \"fIGURE 3\", \"Using the kinetic model further shows that the captamine mutant has, again, an enhanced inhibition of the k+kn parameter by several orders of magnitude compared with the original DesAb-Aβ(3–9) (Figures 3E and 3F).\", \"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0118": {
    "Interaction ID": "AMGAB0118",
    "Antibody ID": "ABID0200",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(T138captamine)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"Figure 3\", \"Figure S3\", \"We found that the T138cysteamine variant displays a potentiated ability to inhibit specifically the k+kn parameter compared with the unaltered DesAb-Aβ(3–9) (Figures 2B and 2C).\", \"We note that, while the resulting cysteamine derivative is very similar to lysine, mutating T138 to lysine using conventional site-directed mutagenesis does not potentiate the antibody activity in the same way as the chemical mutation, even when subjected to the same treatment as the chemically derived cysteamine mutant (Figure S3).\",",
    "Curator Statement": false
  },
  "AMGAB0119": {
    "Interaction ID": "AMGAB0119",
    "Antibody ID": "ABID0201",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(T138cysteamine)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S3\", \"The results revealed that one of the derivatives, T138captamine, had a further potentiated activity compared with the starting cysteamine mutant (Figure 3D). Using the kinetic model further shows that the captamine mutant has, again, an enhanced inhibition of the k+kn parameter by several orders of magnitude compared with the original DesAb-Aβ(3–9) (Figures 3E and 3F).\"",
    "Curator Statement": false
  },
  "AMGAB0120": {
    "Interaction ID": "AMGAB0120",
    "Antibody ID": "ABID0202",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(L139-1-thiobutane)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0121": {
    "Interaction ID": "AMGAB0121",
    "Antibody ID": "ABID0203",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(E137[4-Nitrobenzyl]mercaptan)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0122": {
    "Interaction ID": "AMGAB0122",
    "Antibody ID": "ABID0204",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(E137cysteamine)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0123": {
    "Interaction ID": "AMGAB0123",
    "Antibody ID": "ABID0205",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(L139cysteamine)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0124": {
    "Interaction ID": "AMGAB0124",
    "Antibody ID": "ABID0206",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(E137MESNA)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0125": {
    "Interaction ID": "AMGAB0125",
    "Antibody ID": "ABID0207",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(E137LCys)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0126": {
    "Interaction ID": "AMGAB0126",
    "Antibody ID": "ABID0208",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(L139-β-mercaptoethanol)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0127": {
    "Interaction ID": "AMGAB0127",
    "Antibody ID": "ABID0209",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(L139Tertbutanethiol)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0128": {
    "Interaction ID": "AMGAB0128",
    "Antibody ID": "ABID0210",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(L139Cyclohexanethiol)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0129": {
    "Interaction ID": "AMGAB0129",
    "Antibody ID": "ABID0211",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(T138-β-mercaptoethanol)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S3\",",
    "Curator Statement": false
  },
  "AMGAB0130": {
    "Interaction ID": "AMGAB0130",
    "Antibody ID": "ABID0212",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(T138-1-thioglycerol)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S3\",",
    "Curator Statement": false
  },
  "AMGAB0131": {
    "Interaction ID": "AMGAB0131",
    "Antibody ID": "ABID0213",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(T138MESNA)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S3\",",
    "Curator Statement": false
  },
  "AMGAB0132": {
    "Interaction ID": "AMGAB0132",
    "Antibody ID": "ABID0214",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(T138N,N,N-trimethylcysteamine)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S3\",",
    "Curator Statement": false
  },
  "AMGAB0133": {
    "Interaction ID": "AMGAB0133",
    "Antibody ID": "ABID0215",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(T138N-acetylcysteamine)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S3\",",
    "Curator Statement": false
  },
  "AMGAB0134": {
    "Interaction ID": "AMGAB0134",
    "Antibody ID": "ABID0216",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(T138-4-morpholinethanethiol)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S3\",",
    "Curator Statement": false
  },
  "AMGAB0135": {
    "Interaction ID": "AMGAB0135",
    "Antibody ID": "ABID0217",
    "Antibody name": "DesAb-Aβ(3–9)-FETLTLR(T138K)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.chembiol.2020.11.002",
    "PMID": 33217338.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S3\", \"We note that, while the resulting cysteamine derivative is very similar to lysine, mutating T138 to lysine using conventional site-directed mutagenesis does not potentiate the antibody activity in the same way as the chemical mutation, even when subjected to the same treatment as the chemically derived cysteamine mutant (Figure S3).\",",
    "Curator Statement": false
  },
  "AMGAB0136": {
    "Interaction ID": "AMGAB0136",
    "Antibody ID": "ABID0377",
    "Antibody name": "W20",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.febslet.2008.12.064",
    "PMID": 19162022.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"When 10 μM Aβ42 co-incubated with 0.1, 0.25 and 1 μM of W20, Aβ42 fibrillation was strongly inhibited in a dose-dependent manner (Fig. 2 A). At the highest concentration of W20 (1 μM), around 80% inhibition of fibrillation was observed.\", \"These conformation-dependent scFv antibodies inhibit both Aβ fibrillation and cytotoxicity and bind to the same type of eptitope displayed on the Aβ oligomers.\",",
    "Curator Statement": false
  },
  "AMGAB0137": {
    "Interaction ID": "AMGAB0137",
    "Antibody ID": "ABID0377",
    "Antibody name": "W20",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.febslet.2008.12.064",
    "PMID": 19162022.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"When 10 μM Aβ42 co-incubated with 0.1, 0.25 and 1 μM of W20, Aβ42 fibrillation was strongly inhibited in a dose-dependent manner (Fig. 2 A). At the highest concentration of W20 (1 μM), around 80% inhibition of fibrillation was observed.\", \"These conformation-dependent scFv antibodies inhibit both Aβ fibrillation and cytotoxicity and bind to the same type of eptitope displayed on the Aβ oligomers.\", \" To study the ability of 4 scFv's to dissolve preformed amyloid aggregates, 1 μM of different scFv's were added to a 28 h preincubated sample of Aβ42 respectively. ScFv's dramatically decrease the fluorescence intensity of the preformed Aβ42 aggregates after their co-incubation for 24 h and 48 h (Fig. 2C).\",",
    "Curator Statement": false
  },
  "AMGAB0138": {
    "Interaction ID": "AMGAB0138",
    "Antibody ID": "ABID0474",
    "Antibody name": "W8",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.febslet.2008.12.064",
    "PMID": 19162022.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"These conformation-dependent scFv antibodies inhibit both Aβ fibrillation and cytotoxicity and bind to the same type of eptitope displayed on the Aβ oligomers.\", \"W8, W9 and WC2 also showed the similar ability to inhibit fibrillation of Aβ42 sample, while WC2 had smaller effects on Aβ42 fibrillation when the same concentrations of scFv's were used (Fig. 2B).\",",
    "Curator Statement": false
  },
  "AMGAB0139": {
    "Interaction ID": "AMGAB0139",
    "Antibody ID": "ABID0474",
    "Antibody name": "W8",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.febslet.2008.12.064",
    "PMID": 19162022.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"These conformation-dependent scFv antibodies inhibit both Aβ fibrillation and cytotoxicity and bind to the same type of eptitope displayed on the Aβ oligomers.\", \"W8, W9 and WC2 also showed the similar ability to inhibit fibrillation of Aβ42 sample, while WC2 had smaller effects on Aβ42 fibrillation when the same concentrations of scFv's were used (Fig. 2B).\", \" To study the ability of 4 scFv's to dissolve preformed amyloid aggregates, 1 μM of different scFv's were added to a 28 h preincubated sample of Aβ42 respectively. ScFv's dramatically decrease the fluorescence intensity of the preformed Aβ42 aggregates after their co-incubation for 24 h and 48 h (Fig. 2C).\",",
    "Curator Statement": false
  },
  "AMGAB0140": {
    "Interaction ID": "AMGAB0140",
    "Antibody ID": "ABID0526",
    "Antibody name": "W9",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.febslet.2008.12.064",
    "PMID": 19162022.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"These conformation-dependent scFv antibodies inhibit both Aβ fibrillation and cytotoxicity and bind to the same type of eptitope displayed on the Aβ oligomers.\", \"W8, W9 and WC2 also showed the similar ability to inhibit fibrillation of Aβ42 sample, while WC2 had smaller effects on Aβ42 fibrillation when the same concentrations of scFv's were used (Fig. 2B).\",",
    "Curator Statement": false
  },
  "AMGAB0141": {
    "Interaction ID": "AMGAB0141",
    "Antibody ID": "ABID0526",
    "Antibody name": "W9",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.febslet.2008.12.064",
    "PMID": 19162022.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"These conformation-dependent scFv antibodies inhibit both Aβ fibrillation and cytotoxicity and bind to the same type of eptitope displayed on the Aβ oligomers.\", \"W8, W9 and WC2 also showed the similar ability to inhibit fibrillation of Aβ42 sample, while WC2 had smaller effects on Aβ42 fibrillation when the same concentrations of scFv's were used (Fig. 2B).\", \" To study the ability of 4 scFv's to dissolve preformed amyloid aggregates, 1 μM of different scFv's were added to a 28 h preincubated sample of Aβ42 respectively. ScFv's dramatically decrease the fluorescence intensity of the preformed Aβ42 aggregates after their co-incubation for 24 h and 48 h (Fig. 2C).\",",
    "Curator Statement": false
  },
  "AMGAB0142": {
    "Interaction ID": "AMGAB0142",
    "Antibody ID": "ABID0527",
    "Antibody name": "WC.2",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.febslet.2008.12.064",
    "PMID": 19162022.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"These conformation-dependent scFv antibodies inhibit both Aβ fibrillation and cytotoxicity and bind to the same type of eptitope displayed on the Aβ oligomers.\", \"W8, W9 and WC2 also showed the similar ability to inhibit fibrillation of Aβ42 sample, while WC2 had smaller effects on Aβ42 fibrillation when the same concentrations of scFv's were used (Fig. 2B).\",",
    "Curator Statement": false
  },
  "AMGAB0143": {
    "Interaction ID": "AMGAB0143",
    "Antibody ID": "ABID0527",
    "Antibody name": "WC.2",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.febslet.2008.12.064",
    "PMID": 19162022.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"These conformation-dependent scFv antibodies inhibit both Aβ fibrillation and cytotoxicity and bind to the same type of eptitope displayed on the Aβ oligomers.\", \"W8, W9 and WC2 also showed the similar ability to inhibit fibrillation of Aβ42 sample, while WC2 had smaller effects on Aβ42 fibrillation when the same concentrations of scFv's were used (Fig. 2B).\", \" To study the ability of 4 scFv's to dissolve preformed amyloid aggregates, 1 μM of different scFv's were added to a 28 h preincubated sample of Aβ42 respectively. ScFv's dramatically decrease the fluorescence intensity of the preformed Aβ42 aggregates after their co-incubation for 24 h and 48 h (Fig. 2C).\",",
    "Curator Statement": false
  },
  "AMGAB0144": {
    "Interaction ID": "AMGAB0144",
    "Antibody ID": "ABID0129",
    "Antibody name": "10D5-scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.imlet.2020.07.009",
    "PMID": 32781005.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Western Blot, ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The results showed that both the 10D5-scFv and 12B4-scFv have high affinities for Aβ monomers, oligomers, and fibers. Moreover, scFvs could prevent the formation of Aβ oligomers and fibers, and block their cellular toxicity.\", \"Single chain antibodies prevent the formation of Aβ oligomers and blocks their toxicity in vitro\", \"Aβ42 peptides could self-assemble into oligomers, and the MWs were about 16 kDa (Fig. 3). When 10D5-scFv or 12B4-scFv was added into the preparation of oligomers, the amount of oligomers was significantly reduced.\", \"Figure 3\", \"Single chain antibodies reduce the formation rate of Aβ aggregates\", \"Aβ42 peptides could form fibrils within 6 h, and the addition of 10D5-scFv and 12B4-scFv efficiently inhibited the formation of Aβ fibers and remarkably reduced the formation rate of Aβ aggregates compared with the control and AT8-scFv-negative control groups (Fig. 5). The inhibitory effect of 10D5-scFv was superior to 12B4-scFv, but there was no significant difference between the two groups.\", \"Figure 5\", \"Furthermore, our results showed that 10D5-scFv could better prevent the formation of Aβ oligomers and inhibit the formation rate of Aβ aggregates, which is consistent with the above results.\"",
    "Curator Statement": false
  },
  "AMGAB0145": {
    "Interaction ID": "AMGAB0145",
    "Antibody ID": "ABID0130",
    "Antibody name": "12B4-scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.imlet.2020.07.009",
    "PMID": 32781005.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Western Blot, ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The results showed that both the 10D5-scFv and 12B4-scFv have high affinities for Aβ monomers, oligomers, and fibers. Moreover, scFvs could prevent the formation of Aβ oligomers and fibers, and block their cellular toxicity.\", \"Single chain antibodies prevent the formation of Aβ oligomers and blocks their toxicity in vitro\", \"Aβ42 peptides could self-assemble into oligomers, and the MWs were about 16 kDa (Fig. 3). When 10D5-scFv or 12B4-scFv was added into the preparation of oligomers, the amount of oligomers was significantly reduced.\", \"Figure 3\", \"Single chain antibodies reduce the formation rate of Aβ aggregates\", \"Aβ42 peptides could form fibrils within 6 h, and the addition of 10D5-scFv and 12B4-scFv efficiently inhibited the formation of Aβ fibers and remarkably reduced the formation rate of Aβ aggregates compared with the control and AT8-scFv-negative control groups (Fig. 5). The inhibitory effect of 10D5-scFv was superior to 12B4-scFv, but there was no significant difference between the two groups.\", \"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0146": {
    "Interaction ID": "AMGAB0146",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.imlet.2020.07.009",
    "PMID": 32781005.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Western Blot",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"When 10D5-scFv or 12B4-scFv was added into the preparation of oligomers, the amount of oligomers was significantly reduced. The effect of the scFvs was similar to the 6E10 positive control, indicating scFvs could inhibit the formation of Aβ oligomers.\"",
    "Curator Statement": false
  },
  "AMGAB0147": {
    "Interaction ID": "AMGAB0147",
    "Antibody ID": "ABID0132",
    "Antibody name": "AT8-scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.imlet.2020.07.009",
    "PMID": 32781005.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 5\", \"Aβ42 peptides could form fibrils within 6 h, and the addition of 10D5-scFv and 12B4-scFv efficiently inhibited the formation of Aβ fibers and remarkably reduced the formation rate of Aβ aggregates compared with the control and AT8-scFv-negative control groups (Fig. 5).\"",
    "Curator Statement": false
  },
  "AMGAB0148": {
    "Interaction ID": "AMGAB0148",
    "Antibody ID": "ABID0329",
    "Antibody name": "HT6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.intimp.2018.12.014",
    "PMID": 30553911.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody",
    "Amyloid species identified": "Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"This ability allowed scFv HT6 to induce the gradual disassembly of large Aβ42 aggregates into small Aβ42 oligomers while simultaneously effectively inhibiting the further development of Aβ42 aggregates. Moreover, the scFv HT6-targeted conformational region on Aβ42 aggregates was found to be more local and relatively close to the N-terminus of Aβ42; thus, scFv HT6 significantly delayed or even prevented the aggregation of Aβ42 protofibrils, while significantly reducing the cytotoxicity of Aβ42 oligomers.\", \"Figure 2\", \"Figure 3\", \"As shown in Fig. 2, in the presence of scFv HT6, the aggregation extents of all four Aβ42 species were distinctly reduced.\", \"Similarly, scFv HT6 not only suppressed the further aggregation of Αβ42 oligomers but also reversed their formation to some extent during the first 3 h of the reaction (Fig. 2b). This indicated that the specific binding of scFv HT6 to Aβ42 oligomers not only effectively inhibited the development of Αβ42 oligomers but also induced their disassembly into smaller Αβ42 oligomers. However, scFv HT6 showed the greatest efficacy in terms of both inhibiting development and inducing disassembly of aggregates in the Aβ42 protofibrils system within the first 3 h, despite a light increase in their aggregation after 3 h (Fig. 2c). Finally, scFv HT6 had a similar but weaker effect on Aβ42 fibrils as observed on Aβ42 oligomers (Fig. 2d), suggesting that scFv HT6 could also slightly inhibit the growth of Aβ42 fibers or even induce a slight decrease in their aggregation, especially during the first 12 h.\", \" Aβ42 particles derived from co-incubation of Aβ42 monomers or oligomers with scFv HT6 (Fig. 3b or d) were much smaller than their corresponding controls (Fig. 3a or c), indicating that scFv HT6 effectively repressed Aβ42 aggregation while inducing the disassembly of the aggregates into smaller oligomers to a certain extent. Similar to the results of the ThT-F assay, even shorter or finer Aβ42 protofibrils, along with some Aβ42 oligomers, were observed when Aβ42 protofibrils were co-incubated with scFv HT6 (Fig. 3f) compared to the unique state of the corresponding controls (Fig. 3e). This further demonstrated the greater efficacy of scFv HT6 in preventing the formation and stability of Aβ42 protofibrils. However, a mixture of diffuse and shorter or fine fibrillar states was observed when the Aβ42 fibrils were co-incubated with scFv HT6 (Fig. 3h) compared to their corresponding controls (Fig. 3g). These diffuse Aβ42 fibrils might represent the larger Aβ42–scFv HT6 complexes, from which the small Aβ42 oligomers might be subsequently dissociated out.\", \"For example, scFv HT6 had a slightly weaker effect on the aggregation of Aβ42 oligomers but had a stronger effect on the aggregation of Aβ42 protofibrils or even fibrils (Fig. 1c, Fig. 2) compared with scFv MO6. \", \"Moreover, scFv HT6 had greater potency than scFv MO6 in restraining the development of Aβ42 aggregates, although both antibodies reduced the aggregation of Aβ42 monomer with the same efficacy [8]. In particular, scFv HT6 more effectively suppressed the development of Aβ42 protofibrils rather than Aβ42 oligomers, indicating that the hydrophobic interaction between the C-terminal regions of smaller Aβ42 oligomer subunits (such as the trimer (3-mer)) was stronger for larger Aβ42 oligomer particles (such as octadecamer (18-mer)) than in Aβ42 protofibrils. Consequently, separation of the smaller Aβ42 oligomer subunits induced by scFv HT6 was more readily achieved from Aβ42 protofibrils than from larger Aβ42 oligomers because the scFv HT6-targeted region is relatively further from the C-terminus of Aβ42, even though scFv HT6 exhibited higher binding affinity for Aβ42 oligomers than scFv MO6.\", \"Figure 7\", \"This study demonstrated that the efficacy of an anti-oligomeric Aβ42 antibody to reduce the cytotoxicity of Aβ42 aggregates appears to be mainly related not only to its affinity for the Aβ42 aggregates, or to its efficacy of slowing or blocking the development of Aβ42 aggregates, but also, and potentially more importantly, to the specific antibody-targeted site or region on the Aβ42 aggregate and to the antibody's binding mode toward the Aβ42 aggregates based on their conformation fit.\",",
    "Curator Statement": false
  },
  "AMGAB0149": {
    "Interaction ID": "AMGAB0149",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.jalz.2012.11.010",
    "PMID": 23583235.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "VH-CDR1: GFSLSTSGMGVS, VH-CDR2: DNDRYYNPSLKS, VH-CDR3: PMNTWGDY, VL-CDR1: RSSQSLVHSNGNTYLH, VL-CDR2: KVSNRFSVL-CDR3: SQNTHVPLT",
    "Quote of the interaction": "\" After passive immunotherapy with 3D6, parenchymal Aβ and VAβ deposits were cleared in a time-dependent manner (Table 1). Of note, parenchymal and vascular endpoints appeared to follow a similar time course of clearance, with 70% to 80% removal observed at 12 weeks (Table 1). Although the prevalence of vascular deposits was not significantly reduced after 7 weeks of treatment, we observed examples of “patchy” Aβ morphology suggesting partial clearance at that time point (Fig. 2B).\", \"Table 1\", \"An extended passive immunotherapy study with 3D6, the murine antibody form of bapineuzumab, in PDAPP transgenic mice and with analysis at several time points (12, 24, and 36 weeks) allowed for a characterization of the spatiotemporal relationship of VAβ clearance and the appearance of microhemorrhages. Much of the VAβ clearance occurred within the first 12 weeks of treatment (86% reduction). By 36 weeks, near complete clearance of parenchymal and VAβ was noted as compared with the control group. Thus, passive immunotherapy with 3D6 induced parenchymal and vascular amyloid clearance in PDAPP mice with a similar time course. \",",
    "Curator Statement": false
  },
  "AMGAB0150": {
    "Interaction ID": "AMGAB0150",
    "Antibody ID": "ABID0256",
    "Antibody name": "Fab 4",
    "Amyloid ID": "AGAMYID0013",
    "Amyloid name": "Mutation D187N",
    "DOI": "10.1016/j.jbc.2024.107507",
    "PMID": 38944121.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Other: Size-exclusion chromatography (SEC) combined with multiangle light scattering (SEC-MALS)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "CDRs: L1 SQSVSSSSLN, L2 YGASSRATGV, L3 QQHTYDPP, H1 GFTFSSYWMN, H2 EINPSGGSTH, H3 ASDAFDY",
    "Quote of the interaction": "\"Importantly, all four Fabs selected for functional studies efficiently inhibited the amyloid formation of full-length AGelD187N as examined by thioflavin fluorescence assay and transmission electron microscopy. Two Fabs, neither of which bound to the previously proposed fibril-forming region of AGelD187N, completely blocked the amyloid formation of AGelD187N.\", \"Moreover, no small soluble aggregates, which are considered pathogenic species in protein misfolding diseases, were formed after successful inhibition of amyloid formation by the most promising aggregation inhibitor, as investigated by size-exclusion chromatography combined with multiangle light scattering.\", \"We showed that the developed Fabs binding to different epitopes efficiently inhibited amyloid formation as monitored by thioflavin T (ThT) fluorescence and electron microscopy.\", \"We also confirmed by size-exclusion chromatography (SEC) combined with multiangle light scattering (SEC-MALS) that no small, possibly non-ThT binding, aggregates were formed after successful inhibition of amyloid formation by the most promising aggregation inhibitor, Fab 4.\", \"At 10 μM concentration, all tested Fabs inhibited amyloid formation effectively (Figs. 3C and S2).\", \"Figure 3\", \"Figure S2\", \"Fab 4, which binds to the C-terminal region of AGelD187N, and Fab 19, which binds to the N-terminal region of AGelD187N, both arrested the amyloid formation fully.\", \"In the TEM images, there were only a few short (<0.5 μm) fibrils present in Fab 4 (Fig. 3D) and Fab 19 samples (Fig. S3A).\", \"Fabs 4, 19, and 21 showed concentration-dependent inhibition of amyloid formation (Fig. 4). Both the aggregation rates (Fig. 4, B, D and F) and the maximum ThT fluorescence intensities (Fig. S4, A–C) decreased in a concentration-dependent manner.\", \"Figure 4\", \"Fab 4 was the most potent aggregation inhibitor as it had a significant effect on both the aggregation rate (Fig. 4B) and maximum signal (Fig. S4A) even at the lowest 2.5 μM concentration.\", \"Fab 4, Fab 19, and Fab 21 inhibit AGelD187N amyloid formation in a concentration-dependent manner.\", \"In the sample with Fab 4, no free monomers or low-molecular-weight soluble aggregates were detected after the aggregation reaction. Instead, a main peak of 55 kDa and a second, minor peak of 70 kDa were detected (Fig. 5B). As the molecular weights of the Fab 4 and AGelD187N monomers are 47 kDa and 8 kDa, respectively, these results clearly indicate that Fab 4 formed 1:1 complexes with AGelD187N monomers. The peak of 70 kDa could indicate the formation of a small number of complexes between Fab 4 and AGelD187N trimers. In addition to the formed antibody complexes, the high-molecular weight soluble aggregates were reduced to 29% when comparing LS peak areas. The above results were consistent with the kinetic curves that showed the blocking of aggregation in the presence of 10 μM Fab 4.\", \"Figure 5\", \" We also have shown that the antibody fragments efficiently inhibited the aggregation of the disease-relevant full-length AGelD187N in vitro, although only one of the antibody fragments was known to bind to the previously proposed amyloidogenic region of AGelD187N.\", \"The best and second-best aggregation inhibitors, Fabs 4 and 19, completely blocked amyloid formation at a stoichiometric ratio to full-length AGelD187N, although neither of them targeted the previously proposed amyloidogenic region of the peptide.\", \"At a stoichiometric ratio of 1:1 to AGelD187N peptide, the highest-affinity Fab fragment, Fab 4, blocked amyloid formation fully; at a 1:0.5 ratio, the maximum fluorescence intensity decreased by approximately 50%, and at a 1:0.25 ratio, by approximately 25%.\", \"We conclude that this study provides the first demonstration of high-affinity binders and aggregation inhibitors to the aberrant amyloidogenic AGelD187 peptide, which causes gelsolin amyloidosis. The discovered antibody fragments bind to different epitopes in the disease-relevant full-length monomeric AGelD187N and efficiently inhibit its aggregation in vitro.\",",
    "Curator Statement": false
  },
  "AMGAB0151": {
    "Interaction ID": "AMGAB0151",
    "Antibody ID": "ABID0257",
    "Antibody name": "Fab 14",
    "Amyloid ID": "AGAMYID0013",
    "Amyloid name": "Mutation D187N",
    "DOI": "10.1016/j.jbc.2024.107507",
    "PMID": 38944121.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": false,
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "CDRs: L1 SQSVSSSNLN, L2 YGASSRATGV, L3 LQNNYAPR, H1 GFTFSSYLMT, H2 GIAPSGGSTY, H3 ARPRWRRDASDY",
    "Quote of the interaction": "\"Importantly, all four Fabs selected for functional studies efficiently inhibited the amyloid formation of full-length AGelD187N as examined by thioflavin fluorescence assay and transmission electron microscopy. Two Fabs, neither of which bound to the previously proposed fibril-forming region of AGelD187N, completely blocked the amyloid formation of AGelD187N.\", \"We showed that the developed Fabs binding to different epitopes efficiently inhibited amyloid formation as monitored by thioflavin T (ThT) fluorescence and electron microscopy.\", \"At 10 μM concentration, all tested Fabs inhibited amyloid formation effectively (Figs. 3C and S2).\", \"Figure 3\", \"Figure S2\", \"Figure S3\", \"Fab 21, which binds to the proposed fibril-forming region of AGelD187N, caused the fluorescence intensity to decrease by over 50%, and Fab 14, which was panned against full-length AGelD187N and therefore its binding region is unknown, caused the fluorescence intensity to decrease by over 30%. The decrease in amyloid quantity was also clearly visible in the TEM images (Fig. S3, B and C).\", \"The fourth investigated clone, Fab 14, which showed aggregation inhibition at the highest concentration, surprisingly seemed to induce aggregation at lower concentrations (Fig. S5).\", \"Figure S5\", \" We also have shown that the antibody fragments efficiently inhibited the aggregation of the disease-relevant full-length AGelD187N in vitro, although only one of the antibody fragments was known to bind to the previously proposed amyloidogenic region of AGelD187N.\", \"In addition, the two other Fabs, Fab 21 binding to the proposed fibril-forming region and Fab 14 binding to an unknown region, clearly inhibited amyloid formation at a stoichiometric ratio.\", \" Surprisingly, Fab 14 appeared to induce amyloid formation at lower concentrations. However, this was unlikely, as the aggregation reaction was run to completion without an inhibitor, which was confirmed by measuring the free AGelD187N concentration remaining in the solution after the assay. The most probable explanation for this is that at lower doses, Fab interferes with the aggregation process in a way that changes the fibril morphology and consequently, ThT binding and fluorescence (53, 54, 55).\", \"We conclude that this study provides the first demonstration of high-affinity binders and aggregation inhibitors to the aberrant amyloidogenic AGelD187 peptide, which causes gelsolin amyloidosis. The discovered antibody fragments bind to different epitopes in the disease-relevant full-length monomeric AGelD187N and efficiently inhibit its aggregation in vitro.\",",
    "Curator Statement": false
  },
  "AMGAB0152": {
    "Interaction ID": "AMGAB0152",
    "Antibody ID": "ABID0257",
    "Antibody name": "Fab 14",
    "Amyloid ID": "AGAMYID0013",
    "Amyloid name": "Mutation D187N",
    "DOI": "10.1016/j.jbc.2024.107507",
    "PMID": 38944121.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "CDRs: L1 SQSVSSSNLN, L2 YGASSRATGV, L3 LQNNYAPR, H1 GFTFSSYLMT, H2 GIAPSGGSTY, H3 ARPRWRRDASDY",
    "Quote of the interaction": "\"The fourth investigated clone, Fab 14, which showed aggregation inhibition at the highest concentration, surprisingly seemed to induce aggregation at lower concentrations (Fig. S5).\", \"Figure S5\", \" Surprisingly, Fab 14 appeared to induce amyloid formation at lower concentrations. However, this was unlikely, as the aggregation reaction was run to completion without an inhibitor, which was confirmed by measuring the free AGelD187N concentration remaining in the solution after the assay. The most probable explanation for this is that at lower doses, Fab interferes with the aggregation process in a way that changes the fibril morphology and consequently, ThT binding and fluorescence (53, 54, 55).\",",
    "Curator Statement": "At low concentrations Fab14 seemed to enhance the aggregation. The authors argue that this could be the effect of an off pathway aggregation side effect, in which the material interacts in a different way with ThT."
  },
  "AMGAB0153": {
    "Interaction ID": "AMGAB0153",
    "Antibody ID": "ABID0258",
    "Antibody name": "Fab 19",
    "Amyloid ID": "AGAMYID0013",
    "Amyloid name": "Mutation D187N",
    "DOI": "10.1016/j.jbc.2024.107507",
    "PMID": 38944121.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "CDRs:  L1:SQSVSSSYLN  L2:YGASSRATGV  L3:QQGYSSPP         H1:GFTFSSYWMS        H2:SISSSGGSTH         H3:ARVLGDY",
    "Quote of the interaction": "\"Importantly, all four Fabs selected for functional studies efficiently inhibited the amyloid formation of full-length AGelD187N as examined by thioflavin fluorescence assay and transmission electron microscopy. Two Fabs, neither of which bound to the previously proposed fibril-forming region of AGelD187N, completely blocked the amyloid formation of AGelD187N.\", \"We showed that the developed Fabs binding to different epitopes efficiently inhibited amyloid formation as monitored by thioflavin T (ThT) fluorescence and electron microscopy.\", \"At 10 μM concentration, all tested Fabs inhibited amyloid formation effectively (Figs. 3C and S2).\", \"Figure 3\", \"Figure S2\", \"Fab 4, which binds to the C-terminal region of AGelD187N, and Fab 19, which binds to the N-terminal region of AGelD187N, both arrested the amyloid formation fully.\", \"In the TEM images, there were only a few short (<0.5 μm) fibrils present in Fab 4 (Fig. 3D) and Fab 19 samples (Fig. S3A).\", \"Figure S3\", \"Fabs 4, 19, and 21 showed concentration-dependent inhibition of amyloid formation (Fig. 4). Both the aggregation rates (Fig. 4, B, D and F) and the maximum ThT fluorescence intensities (Fig. S4, A–C) decreased in a concentration-dependent manner.\", \"Figure 4\", \"Fabs 19 and 21 had significant effects on the aggregation rate at 5 μM concentration, with the effect of Fab 19 being greater than that of Fab 21 (Fig. 4, D and F). At 2.5 μM concentration, these two Fabs did not show significant effects compared with the aggregation process of AGelD187N without inhibitor.\", \"Fab 4, Fab 19, and Fab 21 inhibit AGelD187N amyloid formation in a concentration-dependent manner.\", \" We also have shown that the antibody fragments efficiently inhibited the aggregation of the disease-relevant full-length AGelD187N in vitro, although only one of the antibody fragments was known to bind to the previously proposed amyloidogenic region of AGelD187N.\", \"The best and second-best aggregation inhibitors, Fabs 4 and 19, completely blocked amyloid formation at a stoichiometric ratio to full-length AGelD187N, although neither of them targeted the previously proposed amyloidogenic region of the peptide.\", \"We conclude that this study provides the first demonstration of high-affinity binders and aggregation inhibitors to the aberrant amyloidogenic AGelD187 peptide, which causes gelsolin amyloidosis. The discovered antibody fragments bind to different epitopes in the disease-relevant full-length monomeric AGelD187N and efficiently inhibit its aggregation in vitro.\",",
    "Curator Statement": false
  },
  "AMGAB0154": {
    "Interaction ID": "AMGAB0154",
    "Antibody ID": "ABID0259",
    "Antibody name": "Fab 21",
    "Amyloid ID": "AGAMYID0013",
    "Amyloid name": "Mutation D187N",
    "DOI": "10.1016/j.jbc.2024.107507",
    "PMID": 38944121.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "CDRs: L1:SQSVSSSYLN  L2:YGASSRATGV  L3:LQGNYNPP        H1:GFTFSSYLMD  H2:RIDPSGGSTY H3:VLGGFYY",
    "Quote of the interaction": "\"Importantly, all four Fabs selected for functional studies efficiently inhibited the amyloid formation of full-length AGelD187N as examined by thioflavin fluorescence assay and transmission electron microscopy. Two Fabs, neither of which bound to the previously proposed fibril-forming region of AGelD187N, completely blocked the amyloid formation of AGelD187N.\", \"We showed that the developed Fabs binding to different epitopes efficiently inhibited amyloid formation as monitored by thioflavin T (ThT) fluorescence and electron microscopy.\", \"At 10 μM concentration, all tested Fabs inhibited amyloid formation effectively (Figs. 3C and S2).\", \"Figure 3\", \"Figure S2\", \"Figure S3\", \"Fab 21, which binds to the proposed fibril-forming region of AGelD187N, caused the fluorescence intensity to decrease by over 50%, and Fab 14, which was panned against full-length AGelD187N and therefore its binding region is unknown, caused the fluorescence intensity to decrease by over 30%. The decrease in amyloid quantity was also clearly visible in the TEM images (Fig. S3, B and C).\",\"Fabs 4, 19, and 21 showed concentration-dependent inhibition of amyloid formation (Fig. 4). Both the aggregation rates (Fig. 4, B, D and F) and the maximum ThT fluorescence intensities (Fig. S4, A–C) decreased in a concentration-dependent manner.\", \"Figure 4\", \"Fabs 19 and 21 had significant effects on the aggregation rate at 5 μM concentration, with the effect of Fab 19 being greater than that of Fab 21 (Fig. 4, D and F). At 2.5 μM concentration, these two Fabs did not show significant effects compared with the aggregation process of AGelD187N without inhibitor.\", \"Fab 4, Fab 19, and Fab 21 inhibit AGelD187N amyloid formation in a concentration-dependent manner.\", \" We also have shown that the antibody fragments efficiently inhibited the aggregation of the disease-relevant full-length AGelD187N in vitro, although only one of the antibody fragments was known to bind to the previously proposed amyloidogenic region of AGelD187N.\", \"In addition, the two other Fabs, Fab 21 binding to the proposed fibril-forming region and Fab 14 binding to an unknown region, clearly inhibited amyloid formation at a stoichiometric ratio.\", \"We conclude that this study provides the first demonstration of high-affinity binders and aggregation inhibitors to the aberrant amyloidogenic AGelD187 peptide, which causes gelsolin amyloidosis. The discovered antibody fragments bind to different epitopes in the disease-relevant full-length monomeric AGelD187N and efficiently inhibit its aggregation in vitro.\",",
    "Curator Statement": false
  },
  "AMGAB0155": {
    "Interaction ID": "AMGAB0155",
    "Antibody ID": "ABID0404",
    "Antibody name": "16B12",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1016/j.jbc.2026.111221",
    "PMID": 41643771.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro, In cellulo",
    "Experimental method(s)": "ThT - Aggregation kinetics, FRET-based biosensor-cell assay.",
    "Amyloid species identified": "Oligomers, Protofibrils,",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The conformation-specific antibody, 16B12, targeting the R1–R3 regions, showed high sensitivity in detecting early Tau structures and inhibited seed-induced aggregation in vitro.\", \"16B12 also inhibits seed-induced Tau aggregation in vitro.\", \"Nucleation and seeding-preventing effect of the 16B12 in AD\", \"As shown in Figure 5A, our results demonstrated that 16B12 effectively prevented Tau aggregation in a dose-dependent manner.\", \"Figure 5\", \"16B12 significantly inhibited seed elongation of rTau and Tau from two of the three AD samples, compared with the isotype control (Fig. 5, B–D).\", \"B) Representative images of Tau biosensor cells treated with the complex of human Tau seeds-mAb indicating the presence of positive puncta in all conditions, but a reduced number of puncta for the 16B12 treated cells (scale 50 μm).\", \"Figure S4\", \"Furthermore, brain-derived Tau seeds from two AD individuals preincubated with 16B12 were no longer able to seed and elongate properly.\", \"The 16B12 antibody, which binds both R1 and R3 repeats, effectively inhibited in vitro Tau aggregation and seeding, indicating its potential as a prototype Tau immunotherapy.\",",
    "Curator Statement": false
  },
  "AMGAB0156": {
    "Interaction ID": "AMGAB0156",
    "Antibody ID": "ABID0404",
    "Antibody name": "16B12",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1016/j.jbc.2026.111221",
    "PMID": 41643771.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro, In cellulo",
    "Experimental method(s)": "ThT - Aggregation kinetics, FRET-based biosensor-cell assay.",
    "Amyloid species identified": "Oligomers, Protofibrils,",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The conformation-specific antibody, 16B12, targeting the R1–R3 regions, showed high sensitivity in detecting early Tau structures and inhibited seed-induced aggregation in vitro.\", \"16B12 also inhibits seed-induced Tau aggregation in vitro.\", \"Nucleation and seeding-preventing effect of the 16B12 in AD\", \"As shown in Figure 5A, our results demonstrated that 16B12 effectively prevented Tau aggregation in a dose-dependent manner. Specifically, at 1:1 and 1:2 M ratios (mAb:Tau), 16B12 completely abolished the ThT fluorescence signal over the entire time course of the experiment, indicating full inhibition of nucleation and fibril formation.\", \"Figure 5\", \"16B12 significantly inhibited seed elongation of rTau and Tau from two of the three AD samples, compared with the isotype control (Fig. 5, B–D).\", \"Furthermore, brain-derived Tau seeds from two AD individuals preincubated with 16B12 were no longer able to seed and elongate properly.\", \"The 16B12 antibody, which binds both R1 and R3 repeats, effectively inhibited in vitro Tau aggregation and seeding, indicating its potential as a prototype Tau immunotherapy.\",",
    "Curator Statement": false
  },
  "AMGAB0157": {
    "Interaction ID": "AMGAB0157",
    "Antibody ID": "ABID0405",
    "Antibody name": "9H6F2",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1016/j.jbc.2026.111221",
    "PMID": 41643771.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "Monomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Another antibody, 9H6F2, detects the P1–P2 proline-rich segment interaction, distinguishing tauopathies but lacking seeding inhibition\", \" We also tested the remaining mAbs for their ability to inhibit human Tau seeding; however, none of them produced a significant reduction (Fig. S4, B and C).\", \"Similarly, 9H6F2, which targets early structural changes in the proline-rich region, also did not block seeding (Fig. S4C), reinforcing the essential role of the repeat region in Tau propagation (45).\", \" However, since 9H6F2 did not inhibit Tau seeding in vitro, it appears unsuitable for therapeutic use, highlighting the importance of targeting APRs for preventing Tau seeding.\",",
    "Curator Statement": false
  },
  "AMGAB0158": {
    "Interaction ID": "AMGAB0158",
    "Antibody ID": "ABID0406",
    "Antibody name": "11E12E10",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1016/j.jbc.2026.111221",
    "PMID": 41643771.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"Figure S4\",  \"We also tested the remaining mAbs for their ability to inhibit human Tau seeding; however, none of them produced a significant reduction (Fig. S4, B and C).\", \"Yet, such a scenario can be inferred by the observation that 11E12E1, which shares partial R1 epitope overlap with 16B12 but lacks R3 binding, failed to reduce the elongation of Tau seeds (Fig. 5, B and C).\",",
    "Curator Statement": false
  },
  "AMGAB0159": {
    "Interaction ID": "AMGAB0159",
    "Antibody ID": "ABID0407",
    "Antibody name": "Villin1E1",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1016/j.jbc.2026.111221",
    "PMID": 41643771.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative Control",
    "Quote of the interaction": "\"Importantly, the isotype control antibody (Villin1E1) showed no effect on Tau aggregation, confirming the specificity of 16B12’s inhibitory action.\", \"Figure 5\", \"16B12 significantly inhibited seed elongation of rTau and Tau from two of the three AD samples, compared with the isotype control (Fig. 5, B–D).\", \"Figure S4\",",
    "Curator Statement": false
  },
  "AMGAB0160": {
    "Interaction ID": "AMGAB0160",
    "Antibody ID": "ABID0408",
    "Antibody name": "ADx215",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1016/j.jbc.2026.111221",
    "PMID": 41643771.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" We also tested the remaining mAbs for their ability to inhibit human Tau seeding; however, none of them produced a significant reduction (Fig. S4, B and C).\", \"Figure S4\",",
    "Curator Statement": false
  },
  "AMGAB0161": {
    "Interaction ID": "AMGAB0161",
    "Antibody ID": "ABID0409",
    "Antibody name": "18F12",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1016/j.jbc.2026.111221",
    "PMID": 41643771.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" We also tested the remaining mAbs for their ability to inhibit human Tau seeding; however, none of them produced a significant reduction (Fig. S4, B and C).\", \"Figure S4\",",
    "Curator Statement": false
  },
  "AMGAB0162": {
    "Interaction ID": "AMGAB0162",
    "Antibody ID": "ABID0410",
    "Antibody name": "15A10",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1016/j.jbc.2026.111221",
    "PMID": 41643771.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" We also tested the remaining mAbs for their ability to inhibit human Tau seeding; however, none of them produced a significant reduction (Fig. S4, B and C).\", \"Figure S4\",",
    "Curator Statement": false
  },
  "AMGAB0163": {
    "Interaction ID": "AMGAB0163",
    "Antibody ID": "ABID0411",
    "Antibody name": "ADx201",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1016/j.jbc.2026.111221",
    "PMID": 41643771.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" We also tested the remaining mAbs for their ability to inhibit human Tau seeding; however, none of them produced a significant reduction (Fig. S4, B and C).\", \"Figure S4\",",
    "Curator Statement": false
  },
  "AMGAB0164": {
    "Interaction ID": "AMGAB0164",
    "Antibody ID": "ABID0412",
    "Antibody name": "ADx202",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1016/j.jbc.2026.111221",
    "PMID": 41643771.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" We also tested the remaining mAbs for their ability to inhibit human Tau seeding; however, none of them produced a significant reduction (Fig. S4, B and C).\", \"Figure S4\",",
    "Curator Statement": false
  },
  "AMGAB0165": {
    "Interaction ID": "AMGAB0165",
    "Antibody ID": "ABID0413",
    "Antibody name": "20G10",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1016/j.jbc.2026.111221",
    "PMID": 41643771.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" We also tested the remaining mAbs for their ability to inhibit human Tau seeding; however, none of them produced a significant reduction (Fig. S4, B and C).\", \"Figure S4\",",
    "Curator Statement": false
  },
  "AMGAB0166": {
    "Interaction ID": "AMGAB0166",
    "Antibody ID": "ABID0414",
    "Antibody name": "Villin9H11",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1016/j.jbc.2026.111221",
    "PMID": 41643771.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative Control",
    "Quote of the interaction": "\"Figure S4\",",
    "Curator Statement": false
  },
  "AMGAB0167": {
    "Interaction ID": "AMGAB0167",
    "Antibody ID": "ABID0415",
    "Antibody name": "COV4F11",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1016/j.jbc.2026.111221",
    "PMID": 41643771.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative Control",
    "Quote of the interaction": "\"Figure S4\",",
    "Curator Statement": false
  },
  "AMGAB0168": {
    "Interaction ID": "AMGAB0168",
    "Antibody ID": "ABID0475",
    "Antibody name": "IgV 2E6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.jbiotec.2014.03.026",
    "PMID": 24698848.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point)",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\", \"(g) Reduced fibrillar Aβ disaggregation by EDTA-pretreated paIgV 2E6. Following EDTA pretreatment as in panel C, the EDTA was removed by dialysis, and fibrillar Aβ42 (20 μM) was incubated for 24 h with the EDTA-pretreated paIgV 2E6 (+ bar), control paIgV pretreated with diluent (− bar) or non-catalytic paIgV MMF6 (4 μg/mL). Residual fibrillar Aβ42 was measured by the ThT fluorescence method\", \"Treatment with the hydrolytically active paIgV 2E6 solubilized pre-aggregated fibrillar Aβ42 compared to the diluent and non-catalytic MMF6 controls, evident from reduced Thioflavin-T binding to the IgV-treated fibrillar Aβ42\"",
    "Curator Statement": false
  },
  "AMGAB0169": {
    "Interaction ID": "AMGAB0169",
    "Antibody ID": "ABID0172",
    "Antibody name": "07/2a",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.jconrel.2021.06.037",
    "PMID": 34186148.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"a-e. Aβ42 immunoreactivity within the region-of-interest (ROI) showed reduced plaque burden in mice in the Tg:mAb+FUS group vs. Tg:PBS group (a, top row). No such reduction was observed in sections stained for Aβ40 immunoreactivity (a, bottom row). Quantification of the area of Aβ42-positive plaques showed a significant lowering in the hippocampus (b), but not the prefrontal cortex (PFC, c), in mice in the Tg:mAb+FUS group compared to mice in the Tg:PBS group. No significant difference among treatment groups was observed in the area of Aβ40 plaques in either hippocampus (d) or PFC (e). Scale bar = 100 μm. f-h. pGlu3 Aβ immunoreactivity in sections stained with K17 showed significantly decreased plaque load in the hippocampus RO1 in mice in the Tg:mAb+FUS group compared mice in the Tg:PBS group (f, g). No significant difference was found in pGlu3-Aβ immunoreactivities in the PFC (h). Scale bar = 100 μm.\", \" In addition, no significant difference was observed between any group in Aβx-42 plaque deposition in the PFC or in Aβx-40 plaque deposition in the hippocampus or PFC.\",",
    "Curator Statement": "The authors compare the antibody therapy with and without focused ultrasound blood brain barrier (FUS-BBB) disruption."
  },
  "AMGAB0170": {
    "Interaction ID": "AMGAB0170",
    "Antibody ID": "ABID0172",
    "Antibody name": "07/2a",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.jconrel.2021.06.037",
    "PMID": 34186148.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Mice given the combination treatment had reduced hippocampal plaque burden compared to PBS-treated controls.\", \"Decreased hippocampal plaque deposition in APP/PS1dE9 mice co-treated with anti-pGlu3 Aβ mAb and FUS-BBBD\", \"A significant decrease in Aβx-42 plaque deposition in the hippocampus was found in the Tg:mAb+FUS mice (p < 0.05, Fig. 3a, b). No significant differences in Aβx-42 plaque burden were observed between mice treated with PBS, 07/2a alone, or FUS alone (Fig. 3a–e).\", \"Figure 3\", \"a-e. Aβ42 immunoreactivity within the region-of-interest (ROI) showed reduced plaque burden in mice in the Tg:mAb+FUS group vs. Tg:PBS group (a, top row). No such reduction was observed in sections stained for Aβ40 immunoreactivity (a, bottom row). Quantification of the area of Aβ42-positive plaques showed a significant lowering in the hippocampus (b), but not the prefrontal cortex (PFC, c), in mice in the Tg:mAb+FUS group compared to mice in the Tg:PBS group. No significant difference among treatment groups was observed in the area of Aβ40 plaques in either hippocampus (d) or PFC (e). Scale bar = 100 μm. f-h. pGlu3 Aβ immunoreactivity in sections stained with K17 showed significantly decreased plaque load in the hippocampus RO1 in mice in the Tg:mAb+FUS group compared mice in the Tg:PBS group (f, g). No significant difference was found in pGlu3-Aβ immunoreactivities in the PFC (h). Scale bar = 100 μm.\", \" In addition, no significant difference was observed between any group in Aβx-42 plaque deposition in the PFC or in Aβx-40 plaque deposition in the hippocampus or PFC.\", \"However, plaque-lowering in hippocampus suggests that combining the pGlu-Aβ mAb with FUS-BBBD exerted an additive effect to reduce Aβ plaque deposition in the sonicated hippocampus of APP/PS1dE9 mice.\", \"Our results revealed that the effects of the anti-pGlu3 Aβ 07/2a mAb in aged APP/PS1dE9 mice are improved when combined with MB-enhanced FUS-BBBD, leading to improved learning ability, slowing of cognitive decline, and preserved synapses in the hippocampus, possibly by engaging microglia and monocytes, thereby promoting clearance of Aβ and reducing the plaque load.\", \"In conclusion, three weekly sessions of MB-enhanced FUS BBBD in the hippocampus improved the effects of an anti-pGlu3 Aβ mAb, selectively reducing plaque burden and synapse loss in the targeted area and improving spatial memory more quickly and in a greater percentage of animals.\",",
    "Curator Statement": "The authors compare the antibody therapy with and without focused ultrasound blood brain barrier (FUS-BBB) disruption. The plaque reduction is not seen in all brain zones."
  },
  "AMGAB0171": {
    "Interaction ID": "AMGAB0171",
    "Antibody ID": "ABID0172",
    "Antibody name": "07/2a",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.jconrel.2021.06.037",
    "PMID": 34186148.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Mice given the combination treatment had reduced hippocampal plaque burden compared to PBS-treated controls.\", \"Decreased hippocampal plaque deposition in APP/PS1dE9 mice co-treated with anti-pGlu3 Aβ mAb and FUS-BBBD\", \"A significant decrease in Aβx-42 plaque deposition in the hippocampus was found in the Tg:mAb+FUS mice (p < 0.05, Fig. 3a, b). No significant differences in Aβx-42 plaque burden were observed between mice treated with PBS, 07/2a alone, or FUS alone (Fig. 3a–e).\", \"Figure 3\", \"a-e. Aβ42 immunoreactivity within the region-of-interest (ROI) showed reduced plaque burden in mice in the Tg:mAb+FUS group vs. Tg:PBS group (a, top row). No such reduction was observed in sections stained for Aβ40 immunoreactivity (a, bottom row). Quantification of the area of Aβ42-positive plaques showed a significant lowering in the hippocampus (b), but not the prefrontal cortex (PFC, c), in mice in the Tg:mAb+FUS group compared to mice in the Tg:PBS group. No significant difference among treatment groups was observed in the area of Aβ40 plaques in either hippocampus (d) or PFC (e). Scale bar = 100 μm. f-h. pGlu3 Aβ immunoreactivity in sections stained with K17 showed significantly decreased plaque load in the hippocampus RO1 in mice in the Tg:mAb+FUS group compared mice in the Tg:PBS group (f, g). No significant difference was found in pGlu3-Aβ immunoreactivities in the PFC (h). Scale bar = 100 μm.\", \" In addition, no significant difference was observed between any group in Aβx-42 plaque deposition in the PFC or in Aβx-40 plaque deposition in the hippocampus or PFC.\", \"However, plaque-lowering in hippocampus suggests that combining the pGlu-Aβ mAb with FUS-BBBD exerted an additive effect to reduce Aβ plaque deposition in the sonicated hippocampus of APP/PS1dE9 mice.\", \"Our results revealed that the effects of the anti-pGlu3 Aβ 07/2a mAb in aged APP/PS1dE9 mice are improved when combined with MB-enhanced FUS-BBBD, leading to improved learning ability, slowing of cognitive decline, and preserved synapses in the hippocampus, possibly by engaging microglia and monocytes, thereby promoting clearance of Aβ and reducing the plaque load.\", \"In conclusion, three weekly sessions of MB-enhanced FUS BBBD in the hippocampus improved the effects of an anti-pGlu3 Aβ mAb, selectively reducing plaque burden and synapse loss in the targeted area and improving spatial memory more quickly and in a greater percentage of animals.\",",
    "Curator Statement": "The authors compare the antibody therapy with and without focused ultrasound blood brain barrier (FUS-BBB) disruption. The plaque reduction is not seen in all brain zones."
  },
  "AMGAB0172": {
    "Interaction ID": "AMGAB0172",
    "Antibody ID": "ABID0172",
    "Antibody name": "07/2a",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1016/j.jconrel.2021.06.037",
    "PMID": 34186148.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", f-h. pGlu3 Aβ immunoreactivity in sections stained with K17 showed significantly decreased plaque load in the hippocampus RO1 in mice in the Tg:mAb+FUS group compared mice in the Tg:PBS group (f, g). No significant difference was found in pGlu3-Aβ immunoreactivities in the PFC (h). Scale bar = 100 μm.\", \"PyroGlu3 Aβ plaque deposition in the hippocampus was reduced in both the Tg:mAb and the Tg:mAb+FUS groups but only reached significance in the Tg:mAb+FUS group compared to the PBS-treated mice (Fig. 3f, g). No significant differences in pGlu3 Aβ plaque deposition were seen in PFC (Fig. 3h), indicating that the effect was localized to the sonicated area.\", \"Our current results differ slightly from our previous work [22] in that we did not see a reduction of pGlu3 Aβ plaque deposition in prefrontal cortex following the combination treatment in aged APP/PS1dE9 mice. This is likely due to the fact that the mice in this study were immunized only 3 times, compared to 16 times in the previous study, and the plaque-lowering was better in the sonicated hippocampal region, as expected.\",",
    "Curator Statement": "The authors compare the antibody therapy with and without focused ultrasound blood brain barrier (FUS-BBB) disruption. The reduction is not seen in all brain zones."
  },
  "AMGAB0173": {
    "Interaction ID": "AMGAB0173",
    "Antibody ID": "ABID0172",
    "Antibody name": "07/2a",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1016/j.jconrel.2021.06.037",
    "PMID": 34186148.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", f-h. pGlu3 Aβ immunoreactivity in sections stained with K17 showed significantly decreased plaque load in the hippocampus RO1 in mice in the Tg:mAb+FUS group compared mice in the Tg:PBS group (f, g). No significant difference was found in pGlu3-Aβ immunoreactivities in the PFC (h). Scale bar = 100 μm.\", \"PyroGlu3 Aβ plaque deposition in the hippocampus was reduced in both the Tg:mAb and the Tg:mAb+FUS groups but only reached significance in the Tg:mAb+FUS group compared to the PBS-treated mice (Fig. 3f, g). No significant differences in pGlu3 Aβ plaque deposition were seen in PFC (Fig. 3h), indicating that the effect was localized to the sonicated area.\", \"Our current results differ slightly from our previous work [22] in that we did not see a reduction of pGlu3 Aβ plaque deposition in prefrontal cortex following the combination treatment in aged APP/PS1dE9 mice. This is likely due to the fact that the mice in this study were immunized only 3 times, compared to 16 times in the previous study, and the plaque-lowering was better in the sonicated hippocampal region, as expected.\",",
    "Curator Statement": "The authors compare the antibody therapy with and without focused ultrasound blood brain barrier (FUS-BBB) disruption. The reduction is not seen in all brain zones."
  },
  "AMGAB0174": {
    "Interaction ID": "AMGAB0174",
    "Antibody ID": "ABID0005.9",
    "Antibody name": "266.2",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.jmb.2003.11.019",
    "PMID": 14698294.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Inhibition of fibril formation by both antibodies was also confirmed by thioflavin-T (ThT) fluorescence experiments carried out with Aβ1–40 incubated for five days.\", \"Inhibition of Aβ aggregation by co-incubation for five days with anti-Aβ antibodies was confirmed by measuring ThT fluorescence changes that result from the formation of Aβ fibrils.18., 29. Compared to the effects of an irrelevant IgG control, m266.2 and m3D6 inhibited Aβ aggregation in a concentration-dependent manner (Figure 8), showing significant effects at 3 μM and 9 μM m266.2 and m3D6 (p<0.01 and p<0.05, respectively).\", \"Figure 8\",\"The inhibition of fibril formation by both m3D6 and m266.2 was further supported spectroscopically by ThT fluorescence.\",",
    "Curator Statement": false
  },
  "AMGAB0175": {
    "Interaction ID": "AMGAB0175",
    "Antibody ID": "ABID0005.9",
    "Antibody name": "266.2",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.jmb.2003.11.019",
    "PMID": 14698294.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" However, m266.2, which is directed against the central domain of Aβ (amino acid residues 13–28) appeared to completely prevent the formation of fibrils over the course of the experiment.\", \"Anti-Aβ antibodies inhibit fibrillogenesis\", \"Figure 4\", \"Figure 5\", \"However, throughout the entire incubation (five days), Aβ1–42 did not form fibrils in the presence of m266.2.\", \"m3D6 appeared to inhibit fibril growth, and m266.2 appeared to completely suppress the growth of fibrils meeting the criteria.\",\" The term particle is used because some images (especially images from the first two days for all samples and on all days for m266.2 containing samples) did not contain any fibrils. The number of particles taken for these averages was 150 (b) and 10 (c).\", \"Samples incubated with m266.2 appeared to completely suppress the formation of fibrils.\", \"(a) The number of fibrils per μm2 (N=135) for Aβ1–42+mAbαE was not significantly different than the control Aβ1–42 alone sample; however, samples incubated with m3D6 and m266.2 both displayed a significantly fewer number of fibrils per μm2. (b) When 150 largest particles for three different experiments were compiled (N=450), samples containing Aβ1–42+m3D6 or m266.2, but not mAbαE showed a significant decrease in the average length of the 150 largest particles by day 5. (c) When ten largest particles for three different experiments were compiled (N=30), samples containing Aβ1–42+m3D6 and m266.2, but not mAbαE, showed a significant decrease in the average length of the ten largest particles by day 5.\", \" Most remarkably, no fibrils were detected in Aβ1–42+m266.2 incubated up to five days (Figure 4, Figure 5, Figure 6). Only small (volume <500 nm3), relatively uniform aggregates of Aβ and m266.2 were observed in this case. These aggregates did not appear to increase in size or to form any protofibrillar species.\", \"Since fibrils were not actually observed in these samples, these aggregate lengths do not represent fibrils, but short protofibrils (on earlier days) and then aggregates that are comprised of antibodies and Aβ1–42.\", \"While m3D6 was able to inhibit fibril formation compared to the control incubations of Aβ1–42 alone and Aβ1–42+mAbαE, m266.2 was much more effective in its ability to prevent the formation of amyloid fibrils, most likely by arresting the growth of protofibrillar precursors. Interestingly, although some protofibrils were observed in Aβ1–42+m266.2 up to the third day, they later disappeared, suggesting that m266.2 may effectively block and reverse their formation.\",\" As a control, m266.2 was added to solutions of preformed fibrils and deposited on mica. The preformed fibrils were present, indicating that m266.2 did not prevent mature fibrils from depositing on mica.\",",
    "Curator Statement": false
  },
  "AMGAB0176": {
    "Interaction ID": "AMGAB0176",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.jmb.2003.11.019",
    "PMID": 14698294.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Inhibition of fibril formation by both antibodies was also confirmed by thioflavin-T (ThT) fluorescence experiments carried out with Aβ1–40 incubated for five days.\", \"Inhibition of Aβ aggregation by co-incubation for five days with anti-Aβ antibodies was confirmed by measuring ThT fluorescence changes that result from the formation of Aβ fibrils.18., 29. Compared to the effects of an irrelevant IgG control, m266.2 and m3D6 inhibited Aβ aggregation in a concentration-dependent manner (Figure 8), showing significant effects at 3 μM and 9 μM m266.2 and m3D6 (p<0.01 and p<0.05, respectively).\", \"Figure 8\",\"The inhibition of fibril formation by both m3D6 and m266.2 was further supported spectroscopically by ThT fluorescence.\",",
    "Curator Statement": false
  },
  "AMGAB0177": {
    "Interaction ID": "AMGAB0177",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.jmb.2003.11.019",
    "PMID": 14698294.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"m3D6, which is directed against an N-terminal domain of Aβ (amino acid residues 1–5) slowed down fibril formation.\", \"Anti-Aβ antibodies inhibit fibrillogenesis\", \"Figure 3\", \"Figure 5\", \"On day 3 (c), fibril appeared, but fewer fibrils were present in incubations containing m3D6 when compared to the control studies. These fibrils were also decorated by a “halo” of antibodies that is seen more clearly in Figure 7. On day 4 (d) and day 5 (e), the fibrils gradually increased in size and number, but at a slower rate than observed in the control studies.\", \"m3D6 appeared to inhibit fibril growth, and m266.2 appeared to completely suppress the growth of fibrils meeting the criteria.\",\" The term particle is used because some images (especially images from the first two days for all samples and on all days for m266.2 containing samples) did not contain any fibrils. The number of particles taken for these averages was 150 (b) and 10 (c).\", \"m3D6 appears to inhibit fibril growth without completely suppressing it. By comparing the plots for N=150 and N=10, it can be seen that the longest fibrils in samples containing m3D6 are similar to those found in the control samples, but there are fewer fibrils present.\",\"(a) The number of fibrils per μm2 (N=135) for Aβ1–42+mAbαE was not significantly different than the control Aβ1–42 alone sample; however, samples incubated with m3D6 and m266.2 both displayed a significantly fewer number of fibrils per μm2. (b) When 150 largest particles for three different experiments were compiled (N=450), samples containing Aβ1–42+m3D6 or m266.2, but not mAbαE showed a significant decrease in the average length of the 150 largest particles by day 5. (c) When ten largest particles for three different experiments were compiled (N=30), samples containing Aβ1–42+m3D6 and m266.2, but not mAbαE, showed a significant decrease in the average length of the ten largest particles by day 5.\", \"Aβ1–42 samples incubated with m3D6 often displayed fibrils as well. However, these fibrils were found less frequently and their number did not increase as quickly on subsequent days as in the control samples (Figure 3). By the third day, the number of fibrils per μm2 for samples with m3D6 was significantly smaller than the control sample of Aβ1–42 alone (Figure 5, Figure 6). Even though there were fewer fibrils formed in the presence of m3D6, their lengths were still similar to those of fibrils formed in the two controls; mature fibrils were present as early as on the third day. In contrast to control samples, however, the fibrils and globular aggregates formed in the presence of m3D6 displayed a characteristic “halo” around their periphery (Figure 7). Such halos were never observed in control samples, and they were most likely formed upon drying, by the collapse of m3D6 antibodies surrounding the Aβ1–42 aggregate onto mica. Apparently, the presence of such an antibody sheath around the aggregates did not prevent Aβ1–42 from forming fibrils, and only slowed down the rate at which they appeared.\", \"While m3D6 was able to inhibit fibril formation compared to the control incubations of Aβ1–42 alone and Aβ1–42+mAbαE, m266.2 was much more effective in its ability to prevent the formation of amyloid fibrils, most likely by arresting the growth of protofibrillar precursors.\",",
    "Curator Statement": false
  },
  "AMGAB0178": {
    "Interaction ID": "AMGAB0178",
    "Antibody ID": "ABID0403",
    "Antibody name": "mAbαE",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.jmb.2003.11.019",
    "PMID": 14698294.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative Control",
    "Quote of the interaction": "\"Figure 2\", \"Figure 5\", \"Using this method, the control antibody mAbαE did not appreciably inhibit the formation of fibrils.\", \"The control antibody, mAbαE did not inhibit fibril length.\", \"(a) The number of fibrils per μm2 (N=135) for Aβ1–42+mAbαE was not significantly different than the control Aβ1–42 alone sample; however, samples incubated with m3D6 and m266.2 both displayed a significantly fewer number of fibrils per μm2. (b) When 150 largest particles for three different experiments were compiled (N=450), samples containing Aβ1–42+m3D6 or m266.2, but not mAbαE showed a significant decrease in the average length of the 150 largest particles by day 5. (c) When ten largest particles for three different experiments were compiled (N=30), samples containing Aβ1–42+m3D6 and m266.2, but not mAbαE, showed a significant decrease in the average length of the ten largest particles by day 5.\", \"The AFM images of Aβ1–42 alone and Aβ1–42+mAbαE showed similar fibril growth over the five-day period (Figure 1, Figure 2). Fibrils became present on the third or second day of most experiments for these control groups and continued to increase in number (Figure 5(a)) and length on the subsequent days of the study. The number of fibrils present in these two samples was not statistically different to the 0.05 confidence level (Figure 6(a)).\", \"While m3D6 was able to inhibit fibril formation compared to the control incubations of Aβ1–42 alone and Aβ1–42+mAbαE, m266.2 was much more effective in its ability to prevent the formation of amyloid fibrils, most likely by arresting the growth of protofibrillar precursors.\",",
    "Curator Statement": false
  },
  "AMGAB0179": {
    "Interaction ID": "AMGAB0179",
    "Antibody ID": "ABID0140",
    "Antibody name": "NbSyn2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1016/j.jmb.2010.07.001",
    "PMID": 20620148.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody, ThT - Aggregation kinetics, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Protofibrils, Mature fibrils, Oligomers, Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" The aggregation behavior of α-synuclein at physiological pH, including the morphology of the resulting fibrillar structures, is remarkably unaffected by the presence of NbSyn2 and indeed we show that NbSyn2 binds strongly to the aggregated as well as to the soluble forms of α-synuclein.\", \"Finally, the aggregation behavior of α-synuclein in vitro was found to be unaffected by the binding of the nanobody, a result that sheds light on the likely structure of the fibrils and their precursors and on the mechanism by which proteins bind to IDPs.\", \"Figure 5\", \"NbSyn2 does not significantly affect the conversion of α-synuclein into amyloid fibrils\", \"Figure 6\", \"Figure 6a shows that the addition of a 1 molar equivalent of NbSyn2 to a  70-μM sample of α-synuclein in phosphate-buffered saline (PBS) buffer at 37 °C, under conditions of continuous stirring, only minimally perturbs the time course of the increase in the fluorescence of thioflavin T (ThT),57 a dye that binds to amyloid fibrils; a slightly shorter lag phase is observed for the NbSyn:α-synuclein sample.\",  \"In a parallel set of experiments, however, we monitored the time course of the change in the fluorescence of 1-anilino-8-naphthalene sulfonate (ANS),58 a dye that binds to exposed hydrophobic patches on the surface of proteins (Fig. 6b). No significant differences for a series of solutions containing different ratios of NbSyn2 and α-synuclein were observed.\", \"This evidence therefore points to the conclusion that NbSyn2 does not significantly influence the formation of amyloid fibrils by α-synuclein, even at a 1:1 stoichiometry, suggesting that it is not involved in any of the rate-limiting steps of the aggregation reaction under the conditions studied in this work, and that the binding process is highly dynamic. In support of these conclusions, TEM was used to image all the fibrils at the endpoint of the reaction and no significant differences in fibril morphology could be detected. However, in the samples containing an equimolar mixture of α-synuclein and NbSyn2, a higher number of shorter fibrils observed (Fig. 6d), suggesting a higher rate of fragmentation and therefore a shorter lag phase in the aggregation reaction probed by ThT fluorescence.\", \"The finding that NbSyn2 has no major influence on the aggregation kinetics of α-synuclein, for example, suggests that the C-terminal region plays no part in the structure or stability of any intermediate species whose formation affects the aggregation kinetics. \",",
    "Curator Statement": false
  },
  "AMGAB0180": {
    "Interaction ID": "AMGAB0180",
    "Antibody ID": "ABID0424",
    "Antibody name": "C4 scFv",
    "Amyloid ID": "AGAMYID0008",
    "Amyloid name": "Huntingtin",
    "DOI": "10.1016/j.jmb.2015.03.021",
    "PMID": 25861763.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro,",
    "Experimental method(s)": "In vitro aggregation/solubility assay,",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Structure of a single-chain Fv bound to the 17 N-terminal residues of huntingtin provides insights into pathogenic amyloid formation and suppression\", \"We show in this paper that C4 scFv inhibits amyloid formation by exon1 fragments of huntingtin in vitro and elucidate the structural basis for this inhibition and protection by determining the crystal structure of the complex of C4 scFv and HTT(1-17).\", \" The results provide insights into the manner in which C4 scFv inhibits the aggregation of HTT, and hence into its therapeutic potential, and suggests a structural basis for the initial interactions that underlie the formation of disease-associated amyloid fibrils by HTT.\", \"C4 scFv specific for HTT(1-17) inhibits mHTT aggregation in vitro.\", \" In this manuscript, we describe the effects of C4 scFv on the in vitro aggregation properties of mHTT protein fragments and report the crystal structure of the antibody fragment in complex with the 17-residue peptide at 2.5 Å resolution, as well as the characteristics of the binding of these two species in solution using NMR spectroscopy.\", \"Inhibition of the in vitro aggregation of mHTT-exon1 huntingtin fragments by the intrabody C4 scFv\", \"C4 scFv specifically inhibits the aggregation of the exon1 of mHTT in vitro.\", \"When C4 scFv was added after the proteolytic cleavage of MBP, effectively all of the HTT-Ex1-Q46 peptide remained soluble for incubation times of at least 76 h, an effect similar to that of the well-known peptide inhibitor of polyQ aggregation, polyglutamine binding peptide 1, QBP1 [27], which we included in our experimental strategy as a positive control (Fig. 1).\", \"Figure 1\", \"C4 scFv inhibition of mHTT-exon1 aggregation\", \"In the present study, we have found that C4 scFv inhibits the aggregation of HTT-Ex1-Q72 peptides in vitro (Fig. 1), a result that is consistent with observations from in situ and in vivo studies [24,25].\", \"Furthermore, C4 scFv increases the solubility of the peptide by interacting with the residues Leu4HTT, Leu8HTT and Phe11HTT, which adopt helical conformations resulting in the formation of a hydrophobic surface. This surface is thus shielded from the solvent and protected from self-association with other HTT fragments, as well as from interactions with cellular membranes that have been suggested to be an important factor in the nucleation of toxic mHTT aggregates [18,32–35].\",",
    "Curator Statement": false
  },
  "AMGAB0181": {
    "Interaction ID": "AMGAB0181",
    "Antibody ID": "ABID0425",
    "Antibody name": "scFvR19",
    "Amyloid ID": "AGAMYID0008",
    "Amyloid name": "Huntingtin",
    "DOI": "10.1016/j.jmb.2015.03.021",
    "PMID": 25861763.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro,",
    "Experimental method(s)": "In vitro aggregation/solubility assay,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 1\", \"To evaluate the specificity of the inhibition of mHTT by C4 scFv, we incorporated a gankyrin-specific scFv, scFvR19 [28], into the experimental design. As expected, this antibody fragment had no detectable effect on the extent of aggregation by HTT-Ex1-Q46 when it was added at the beginning of the aggregation reaction (Fig. 1).\",",
    "Curator Statement": false
  },
  "AMGAB0182": {
    "Interaction ID": "AMGAB0182",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.jneuroim.2010.03.023",
    "PMID": 20451261.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In these experiments, phage 1.27 was almost as effective as a control Aβ-specific monoclonal antibody (6E10) in amyloid clearance, while negative control phage did not reduce amyloid load (Fig. 8)\", \"Figure 8\",",
    "Curator Statement": false
  },
  "AMGAB0183": {
    "Interaction ID": "AMGAB0183",
    "Antibody ID": "ABID0260",
    "Antibody name": "VH1.27",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.jneuroim.2010.03.023",
    "PMID": 20451261.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We demonstrated that these antibody fragments recognize in a specific manner amyloid beta deposits in APP/Tg mouse brains, inhibit toxicity of oligomeric Aβ1-42 in neuroblastoma cell cultures in a concentration-dependently manner and reduced amyloid deposits in APP/Tg2576 mice after intracranial administration.\", \"Aβ-specific VH recombinant antibody fragment clears amyloid deposits after intracranial delivery\", \"In these experiments, phage 1.27 was almost as effective as a control Aβ-specific monoclonal antibody (6E10) in amyloid clearance, while negative control phage did not reduce amyloid load (Fig. 8)\", \"Figure 8\", \"Purified phage bearing anti-Aβ antibody fragment efficiently clears amyloid deposits after intracranial delivery.\",",
    "Curator Statement": false
  },
  "AMGAB0184": {
    "Interaction ID": "AMGAB0184",
    "Antibody ID": "ABID0447",
    "Antibody name": "72D9",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.lfs.2012.04.038",
    "PMID": 22579764.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunohistochemistry, ELISA, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Monoclonal 72D9 immunotherapy protects 3x-Tg AD mice from intraneuronal AβO and phosphorylated tau accumulation or neurofibrillary tangle formation\", \"(right half of panel) Double-staining experiment also revealed that the accumulation of A11-positive intraneuronal AβOs was reduced in 72D9-treated mice: A11 (red)/DAPI (blue).\", \"Figure 2\", \"Passive immunization protects 3xTg-AD mice from memory deficits, intraneuronal AβOs and/or phosphorylated tau accumulation, and neurofibrillary tangle formation.\", \"At 26 months of age (Mastrangelo and Bowers, 2008; extracellular and intracellular AβOs, intraneuronal phosphorylated tau, and NFTs as well as memory loss are well established), intraneuronal accumulation of AT8-(left panel of Fig. 2B) or A11-positive immunofluorescence (right panel of Fig. 2B) was effectively blocked by 72D9 immunization as compared with control IgG2b immunization. Gallyas–Braak staining revealed that 72D9 immunotherapy (left panel of Fig. 2C) markedly inhibited NFT formation and senile plaque accumulation as compared with control IgG2b immunization (right panel of Fig. 2C).\", \"Furthermore, our in vivo investigation demonstrated that 72D9-immunized mice with improved cognition showed less intraneuronal accumulation of A11-positive AβOs, indicating that extracellular and intraneuronal AβOs are indeed related. We also found that microglial responses to 72D9 immunization remained unchanged compared with those to control IgG2b immunization despite the dramatic reduction of the number of plaques in 72D9-treated mice, suggesting that plaques may be formed as a protective reservoir to maintain AβOs at the sufficient concentration that does not affect synaptic function.\",",
    "Curator Statement": false
  },
  "AMGAB0185": {
    "Interaction ID": "AMGAB0185",
    "Antibody ID": "ABID0006.5",
    "Antibody name": "mAb158",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.mcn.2024.103950",
    "PMID": 38901655.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Other: MesoScale Discovery (MSD) assay using Electrochemiluminescence (ECL),",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\", No significant differences in insoluble Aβ40 levels were observed between mAb158- and vehicle-treated mice.\", \"Figure 2\", \"(A) No statistically significant differences in total insoluble Aβ40 levels were observed in mice treated with mAb158 or vehicle.\", \"Figure 6\", \"Although the levels of Aβ40 in the insoluble fraction showed no significant differences in mAb158-treated and vehicle groups (Fig. 6A), mAb158 treatment had a significant effect on insoluble Aβ42 levels.\",",
    "Curator Statement": false
  },
  "AMGAB0186": {
    "Interaction ID": "AMGAB0186",
    "Antibody ID": "ABID0006.5",
    "Antibody name": "mAb158",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.mcn.2024.103950",
    "PMID": 38901655.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Other: MesoScale Discovery (MSD) assay using Electrochemiluminescence (ECL),",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Aβ protofibril levels were significantly lower in mAb158-treated animals at both 4 and 18 weeks, while longer treatment duration (18 weeks) was required to observe significantly lower Aβ42 levels in insoluble brain fractions and lower Aβ plaque load. Following the off-treatment period, comparison of the vehicle- and mAb158-treated mice demonstrated that the Aβ protofibril levels, insoluble Aβ42 levels and Aβ plaque load remained significantly lower in mAb158-treated animals, as compared with age-matched controls. However, there was a significant increase of brain accumulation of both the Aβ protofibril levels, insoluble Aβ42 levels and Aβ plaque load after treatment cessation. Thus, repeated mAb158 treatment of aged Tg2576 mice first reduced Aβ protofibril levels within 4 weeks of treatment, which then was followed by a reduction of amyloid plaque pathology within 18 weeks of treatment. These effects were maintained 12 weeks after the final dose, indicating that mAb158 had a disease-modifying effect on the Aβ pathology in this mouse model. In addition, brain accumulation of both Aβ protofibril levels and amyloid pathology progressed after discontinuation of the treatment which supports the importance of continued treatment with mAb158 to maintain the effects on Aβ pathology.\", \"mAb158 reduced soluble and insoluble Aβ levels in Tg2576 mice at different time-points\", \"Soluble Aβ and protofibril levels were reduced by mAb158 treatment for 4 weeks\", \"Figure 1\", \"Compared to controls, mice treated with mAb158 for 4 weeks had a 62 % lower level of Aβ protofibrils; this difference was statistically significant (4.9 ± 0.9 vs. 13.0 ± 2.0 ng/g; p < 0.001). This efficacy was enhanced in animals treated for 18 weeks, despite the robust age-associated increase in Aβ protofibril levels in this model. Tg2576 mice treated with mAb158 for 18 weeks had an 87 % lower level of Aβ protofibrils, as compared to controls (13.1 ± 1.9 vs. 103.2 ± 15.2 ng/g; p < 0.0001).\", \"(A) Treatment with mAb158 resulted in significantly lower Aβ protofibril levels at 4 and 18 weeks, compared to the respective vehicle control group.\", \"Insoluble Aβ levels were reduced by mAb158 treatment for 18 weeks\", \"To evaluate the effects of mAb158 on aggregated Aβ, the levels of Aβ40 and Αβ42 were measured in the insoluble brain fraction (Fig. 2). Mice treated with mAb158 for 4 weeks showed a trend towards a lower level of insoluble Aβ42 (22 % below the level in control mice), but this difference did not reach statistical significance. Mice treated with mAb158 for 18 weeks had 31 % less insoluble Aβ42, as compared to controls (5529 ± 368 vs. 7969 ± 543 ng/g; p < 0.001). No significant differences in insoluble Aβ40 levels were observed between mAb158- and vehicle-treated mice.\", \"Figure 2\", \"(B) Mice treated with mAb158 for 18 weeks had significantly lower levels of total insoluble Aβ42, as compared to the vehicle control group.\", \"The Aβ-positive plaque load was reduced by mAb158 treatment for 18 weeks\", \"Quantification of Aβ-positive plaques in the cerebral cortex showed a higher plaque load in the vehicle-treated 18-week group, as compared to the 4-week group (Fig. 3).\", \"Figure 3\", \"Quantification of the Aβ-positive (6E10) immunoreactive area (B) and object density (C) showed statistically significant differences between mice treated with mAb158 or vehicle for 18 weeks.\", \"Mice treated with mAb158 or vehicle for 4 weeks showed no statistically significant difference in plaque load. In contrast, mice treated with mAb158 for 18 weeks had significantly lower plaque loads than vehicle-treated animals, with 56 % less immunoreactive area (0.310 ± 0.026 vs. 0.701 ± 0.079 %; p < 0.0001; Fig. 3B) and a 66 % lower object density (14.0 ± 1.1 vs. 40.9 ± 4.4 objects/mm2; p < 0.0001; Fig. 3C).\", \"As was evident from representative immunofluorescence images of mice treated with mAb158 or vehicle for 18 weeks (Fig. 3A) and confirmed by the size distribution analysis, mAb158 treatment primarily affected the number of smaller plaques (Fig. 3D), suggesting that mAb158 slowed the formation of new plaques while vehicle treatment still allowed plaques to form. \", \"ThioS staining of β-sheets was used to quantify dense core plaques in the cerebral cortex (Supplementary Information, Fig. S1). Consistent with the Aβ-positive plaque analysis above, a higher total signal was detected in the 18-week vehicle-treated group than in the 4-week vehicle group, indicating a growth of dense core plaques between the ages of 13 months (4-week group) and 16.5 months (18-week group). However, we found no statistically significant differences in the levels of ThioS-positive plaques in Tg2576 mice treated with mAb158 or vehicle for 4 or 18 weeks, although a trend to an effect on ThioS-positive object density was observed at 18 weeks (p = 0.09; Fig. S1B).\", \"Supplementary Figure S1\",  \"Comparisons of Aβ protofibril levels in the soluble brain fractions of all groups using a two-way factorial ANOVA identified a significantly higher level of Aβ protofibrils in the vehicle group that lived 12 weeks longer (off-treatment period), as compared to the vehicle group that was euthanized after 18 weeks (p < 0.001). Aβ protofibril levels were 86 % lower in mAb158-treated mice than in the respective controls after the 18-week treatment period (22.5 ± 0.8 vs. 163.6 ± 18.3 ng/g; p < 0.001), and after the 12-week off-treatment period (45.2 ± 3.8 vs. 328.8 ± 24.0 ng; p < 0.001) (Fig. 5A).\", \"Figure 5\", \"Mice treated with mAb158 had significantly lower Aβ protofibril levels both before and after the 12-week off-treatment period, as compared to the respective vehicle controls.\", \"Figure 6\",\"Although the levels of Aβ40 in the insoluble fraction showed no significant differences in mAb158-treated and vehicle groups (Fig. 6A), mAb158 treatment had a significant effect on insoluble Aβ42 levels.\", \"The mAb158-treated group had 41 % less Aβ42 at 18 weeks (5592 ± 432 vs. 9525 ± 505 ng/g, p < 0.001), and 34 % less Aβ42 following the 12-week off-treatment period (11,527 ± 529 vs. 17,598 ± 1095 ng/g, p < 0.001), as compared to the respective control groups (Fig. 6B).\", \"Aβ42 levels were significantly lower in mice treated with mAb158 for 18 weeks, both before and after the off-treatment period, as compared to the respective vehicle controls.\",  \"Mice treated with mAb158 for 18 weeks had significantly less Aβ-positive plaque pathology, both before and after the 12-week off-treatment period, as compared to the respective vehicle control group. At 18 weeks, these mice had 59 % less immunoreactive area (0.399 ± 0.039 vs. 0.966 ± 0.049 %, p < 0.001) and 52 % lower object density (42.1 ± 2.2 vs. 87.1 ± 4.1 objects/mm2, p < 0.001); after the off-treatment period, these values were 41 % (0.790 ± 0.063 vs. 1.340 ± 0.084 %, p < 0.001) and 40 % (63.4 ± 3.4 vs. 105.0 ± 5.1 objects/mm2, p < 0.001) lower, respectively (Fig. 7). Although plaque pathology was more pronounced after the off-treatment period, there was no significant interaction between treatment and treatment duration for either the immunoreactive area (F1,74 = 0.020, p = 0.888) or the object density (F1,74 = 0.196, p = 0.659), showing that the effect of mAb158 treatment persisted following the 12-week off-treatment period.\", \"Figure 7\", \"Animals treated with mAb158 for 18 weeks had a significantly smaller Aβ-positive area both before and after the off-treatment period, as compared with the relevant vehicle controls. (B) The Aβ-positive object density also increased significantly during the off-treatment period. Animals treated with mAb158 for 18 weeks showed a significantly lower object density, both before and after the off-treatment period, as compared to the relevant vehicle controls.\", \"However, different mAb158 treatment durations were required to achieve these effects, with lower levels of Aβ protofibrils observed after 4 weeks, while the Aβ-positive cortical plaque load was only reduced after 18 weeks. This finding suggests that Aβ protofibril clearance precedes plaque clearance in Tg2576 mice treated with mAb158.\", \" In contrast to the effects seen in older Tg-ArcSwe mice with established plaque pathology, treatment of Tg2576 mice with mAb158 at an age when plaque formation had indeed begun, but when Aβ pathology still was increasing exponentially, resulted in effective reduction of both Aβ protofibrils and diffuse Aβ-positive plaques after long-term treatment.\", \"The lower Aβ-positive plaque burden in Tg2576 mice treated with mAb158 was associated with a significantly lower Aβ42 level in the insoluble brain fraction.\",",
    "Curator Statement": false
  },
  "AMGAB0187": {
    "Interaction ID": "AMGAB0187",
    "Antibody ID": "ABID0565",
    "Antibody name": "anti-hTAU-mIgG2a",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.medj.2022.09.007",
    "PMID": 36257298.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Meso scale discovery,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"Figure 3J shows significantly higher potency of both anti-tau mAbs at slowing tau seeding since the tau concentration in both anti-tau mAb-treated groups was lower than the isotype IgG-treated group.\",",
    "Curator Statement": false
  },
  "AMGAB0188": {
    "Interaction ID": "AMGAB0188",
    "Antibody ID": "ABID0566",
    "Antibody name": "anti-hTAU-mIgG2σ",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.medj.2022.09.007",
    "PMID": 36257298.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Meso scale discovery,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"Figure 3J shows significantly higher potency of both anti-tau mAbs at slowing tau seeding since the tau concentration in both anti-tau mAb-treated groups was lower than the isotype IgG-treated group.\",",
    "Curator Statement": false
  },
  "AMGAB0189": {
    "Interaction ID": "AMGAB0189",
    "Antibody ID": "ABID0567",
    "Antibody name": "anti-hTAU-mIgG2a/chim",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.medj.2022.09.007",
    "PMID": 36257298.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Meso scale discovery,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"Eight weeks after dosing, both anti-hTAU mAb-treated groups had significantly less PHF-tau in brain homogenates than the isotype control group, indicating both mAbs neutralized tau seeding (Figure 3K).\",",
    "Curator Statement": false
  },
  "AMGAB0190": {
    "Interaction ID": "AMGAB0190",
    "Antibody ID": "ABID0568",
    "Antibody name": "anti-hTAU-hIgG1-mut-mTfR",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.medj.2022.09.007",
    "PMID": 36257298.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Meso scale discovery,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"Eight weeks after dosing, both anti-hTAU mAb-treated groups had significantly less PHF-tau in brain homogenates than the isotype control group, indicating both mAbs neutralized tau seeding (Figure 3K).\",",
    "Curator Statement": false
  },
  "AMGAB0191": {
    "Interaction ID": "AMGAB0191",
    "Antibody ID": "ABID0528",
    "Antibody name": "V31-1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.molimm.2008.09.008",
    "PMID": 18930548.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Dynamic light scattering (DLS),  ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Two were able to recognize selectively intraneuronal Aβ oligomers; furthermore, one of them, V31-1, prevented Aβ-induced neurotoxicity and inhibited fibril formation.\", \"VHH V31-1 inhibits the formation of fibrils\", \"When Aβ42 was co-incubated with an equimolar concentration of VHH V31-1, we observed two peaks, at 10–25 nm and at 150–200 nm. Noticeably, the 600–800 nm peak could never be detected for this complex, suggesting that high molecular weight aggregates could not form in the presence of VHH V31-1. The average light scattering intensity of VHHs alone was much lower than that of Aβ42, and could therefore be neglected in the VHH-Aβ42 mixture (data not shown).\", \"Table 1\", \"The absence of fibril formation in the presence of VHH V31-1 was confirmed by the ThT assay: fluorescence significantly decreased when Aβ42 was co-incubated with an equimolar concentration of VHH V31-1, while it increased when Aβ42 was alone (Table 2). No significant decrease of fluorescence was observed when Aβ42 was co-incubated with an equimolar concentration of VHH L35\", \"The binding of VHH V31-1 to Aβ42 samples taken at different times was the strongest at t = 1 h and then steadily decreased suggesting that VHH V31-1 preferentially recognized a non-fibrillar conformation of Aβ.\", \"Here we demonstrate that VHH V31-1 is able to inhibit the aggregation of Aβ42 while an irrelevant VHH has no effect on the aggregation.\",",
    "Curator Statement": false
  },
  "AMGAB0192": {
    "Interaction ID": "AMGAB0192",
    "Antibody ID": "ABID0529",
    "Antibody name": "VHH L35",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.molimm.2008.09.008",
    "PMID": 18930548.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Dynamic light scattering (DLS),  ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Table 1\", \"The absence of fibril formation in the presence of VHH V31-1 was confirmed by the ThT assay: fluorescence significantly decreased when Aβ42 was co-incubated with an equimolar concentration of VHH V31-1, while it increased when Aβ42 was alone (Table 2). No significant decrease of fluorescence was observed when Aβ42 was co-incubated with an equimolar concentration of VHH L35.\", \"Here we demonstrate that VHH V31-1 is able to inhibit the aggregation of Aβ42 while an irrelevant VHH has no effect on the aggregation.\", \" When Aβ42 was co-incubated with an equimolar concentration of VHH L35, a similar pattern of aggregation was observed with the formation of two main peaks around 100–150 nm and 600–700 nm. Interestingly, VHH L35 appeared to accelerate the rate of fibril formation of Aβ42, as the 600–800 nm peak appeared as early as day 4.\",",
    "Curator Statement": false
  },
  "AMGAB0193": {
    "Interaction ID": "AMGAB0193",
    "Antibody ID": "ABID0135",
    "Antibody name": "C4",
    "Amyloid ID": "AGAMYID0008",
    "Amyloid name": "Huntingtin (htt) 97Q (GFP-tagged)",
    "DOI": "10.1016/j.nbd.2004.11.003",
    "PMID": 15837560.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Flourescence microscopy",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Immunoblot analysis of transiently transfected HEK-293T cells indicated that C4 dramatically lowered steady-state levels of both normal (25Q) and mutant (97Q) httex1pGFP, as compared to levels in the presence of control sFv (ML3.9), by 78% and 89%, respectively (Fig. 2; quantified P < 0.001). GFP positive aggregates were visualized in cells co-expressing ML3.9 control sFv with mutant httex1p(97Q)-GFP, but not in cells coexpressing C4 sFv with mutant httex1p(97Q)-GFP, or in cells expressing normal httex1p(25Q)-GFP (not shown); this pattern is in agreement with previous observations (Lecerf et al., 2001).\"",
    "Curator Statement": false
  },
  "AMGAB0194": {
    "Interaction ID": "AMGAB0194",
    "Antibody ID": "ABID0136",
    "Antibody name": "ML3.9",
    "Amyloid ID": "AGAMYID0008",
    "Amyloid name": "Huntingtin (htt) 97Q (GFP-tagged)",
    "DOI": "10.1016/j.nbd.2004.11.003",
    "PMID": 15837560.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Flourescence microscopy",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Immunoblot analysis of transiently transfected HEK-293T cells indicated that C4 dramatically lowered steady-state levels of both normal (25Q) and mutant (97Q) httex1pGFP, as compared to levels in the presence of control sFv (ML3.9), by 78% and 89%, respectively (Fig. 2; quantified P < 0.001). GFP positive aggregates were visualized in cells co-expressing ML3.9 control sFv with mutant httex1p(97Q)-GFP, but not in cells coexpressing C4 sFv with mutant httex1p(97Q)-GFP, or in cells expressing normal httex1p(25Q)-GFP (not shown); this pattern is in agreement with previous observations (Lecerf et al., 2001).\"",
    "Curator Statement": false
  },
  "AMGAB0195": {
    "Interaction ID": "AMGAB0195",
    "Antibody ID": "ABID0416",
    "Antibody name": "scFv59",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.nbd.2006.04.012",
    "PMID": 16766200.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"AD mouse models subjected to AAV injection had much less amyloid deposits at the injection sites than the mouse models subjected to PBS injection.\", \"The β-amyloid loads (average percentage of area showing Aβ immunoreactivity) in the hippocampus and neocortex were on average 3.09 ± 0.718% and 5.97 ± 1.08% for rAAV-CAscFv59 injected and PBS injected Tg2576 mice, respectively (P < 0.05) (Fig. 3C). Thus, Tg2576 mice subjected to rAAV-CAscFv59 injection had fewer Aβ deposits than Tg2576 mice injected with PBS.\", \"Figure 3\", \"rAAV-CAscFv59 injection reduces Aβ deposits in the brain of Tg2576 mice. \", \"Six months after corticohippocampal injection of rAAV-CAscFv59, less amyloid deposits were found at the injection sites in Tg2576 mice compared with Tg2576 mice subjected to PBS injection.\", \"scFv59 is immunoreactive with oligomeric Aβ and inhibits Aβ aggregation and probably cytotoxicity in vitro (Fukuchi et al., 2006).\",",
    "Curator Statement": false
  },
  "AMGAB0196": {
    "Interaction ID": "AMGAB0196",
    "Antibody ID": "ABID0006.5",
    "Antibody name": "mAb158",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.nbd.2009.08.007",
    "PMID": 19703562.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry,",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"However, Aβ burden in the cerebral cortex, assessed with 6E10 immunostaining, was much lower in young tg-ArcSwe mice treated with the mAb158 antibody as compared to mice treated with control IgG (P < 0.05; Figs. 4C, D; Supplementary Table 1). Similar results were obtained when an Aβ40-specific antibody was used for immunohistochemistry (data not shown).\"",
    "Curator Statement": "Actic mutation"
  },
  "AMGAB0197": {
    "Interaction ID": "AMGAB0197",
    "Antibody ID": "ABID0006.5",
    "Antibody name": "mAb158",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.nbd.2009.08.007",
    "PMID": 19703562.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Quantification of sedimented particles (ultracentrifugation), SDS-PAGE",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The highly protofibril-selective monoclonal antibody mAb158 inhibited in vitro fibril formation and protected cells from Aβ protofibril-induced toxicity.\", \"mAb158 prevents Aβ fibrillogenesis in vitro\", \"Figure 2\",\"Both mAb158 and mAb1C3 inhibited Aβ fibrillogenesis (Fig. 2A) as compared to a control IgG, although mAb1C3 seemed to stop the aggregation process at an earlier stage than mAb158.\", \"Antibodies with conformational and linear N-terminal Aβ epitopes both halt in vitro Aβ1–42 fibrillogenesis. \", \"Both mAb158 and mAb1C3 diminished fibril formation.\", \"In addition, both antibodies inhibited Aβ fibrillogenesis as assessed with ThT fluorescence in vitro, although mAb158 interfered at a later stage in the process. The moderate increase in ThT fluorescence seen over 5 days with mAb158 likely reflects its selective preference for larger oligomers, whereas mAb1C3 halted aggregation early on, at the monomer/low molecular weight-Aβ stage resulting in a weaker ThT signal.\",",
    "Curator Statement": false
  },
  "AMGAB0198": {
    "Interaction ID": "AMGAB0198",
    "Antibody ID": "ABID0006.5",
    "Antibody name": "mAb158",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.nbd.2009.08.007",
    "PMID": 19703562.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"When the mAb158 antibody was administered for 4 months to plaque-bearing transgenic mice with both the Arctic and Swedish mutations (tg-ArcSwe), Aβ protofibril levels were lowered while measures of insoluble Aβ were unaffected.\", \"In contrast, when treatment began before the appearance of senile plaques, amyloid deposition was prevented and Aβ protofibril levels diminished.\", \"Soluble Aβ protofibrils were efficiently cleared by the mAb158 antibody, while amyloid burden was only reduced with preventive treatment.\", \"Treatment of young tg-ArcSwe mice with mAb158 prevents accumulation of soluble Aβ protofibrils and insoluble Aβ\", \"At the end of the study, animals treated with mAb158 had lower levels of soluble Aβ protofibrils as compared to animals treated with an irrelevant antibody (Fig. 3A; Supplementary Table 1).\", \"Figure 3\", \" Supplementary Table 1\", \" When the insoluble Aβ pool in the FA-extracts was analyzed, levels were much lower in mAb158 treated animals in all assays, as compared to mice given the control IgG (Fig. 3C; Supplementary Table 1).\", \"(A) Levels of soluble Aβ protofibrils (pg/mg tissue) were analyzed at the end of treatment and found to be significantly lower in mAb158 immunized mice as compared to mice given control IgG or mAb1C3. ⁎⁎P < 0.01.\", \"(C) Levels of total Aβ, Aβx-40 and Aβx-42 (ng/mg tissue) in formic acid extracts were all significantly lower in mAb158 treated mice as compared to control IgG and mAb1C3 treated mice. These Aβ ELISA measures mainly represent insoluble Aβ. ⁎⁎P < 0.01; ⁎P < 0.05.\", \"Passive immunization with mAb158 does not alter intraneuronal Aβ accumulation but prevents senile plaque formation in young tg-ArcSwe mice\", \"However, Aβ burden in the cerebral cortex, assessed with 6E10 immunostaining, was much lower in young tg-ArcSwe mice treated with the mAb158 antibody as compared to mice treated with control IgG (P < 0.05; Figs. 4C, D; Supplementary Table 1). Similar results were obtained when an Aβ40-specific antibody was used for immunohistochemistry (data not shown).\", \" Amyloid burden, the area stained by Congo Red in cerebral cortex, was significantly lower in mAb158 treated mice compared to mice given control IgG (P <  0.05; Figs. 4E, F; Supplementary Table 1), results consistent with the biochemical measures of insoluble Aβ (Figs. 3C; Supplementary Table 1). We found highly significant correlations between a biochemical measure of total Aβ levels in formic acid extracts and histological measures of Aβ burden or Congo burden among individual mice (r = 0.93, P <  0.001 and r = 0.92, P <  0.001, respectively), suggesting that we could reliably estimate the level of insoluble Aβ.\", \"Aβ burden was lower in mAb158 immunized animals, as compared to mice treated with control IgG or mAb1C3.\", \"Congo burden was significantly lower in mAb158 immunized mice than in mice given control IgG, while Congo burden in mAb1C3 immunized mice were similar to the control group. ⁎P < 0.05.\", \"mAb158 reduces levels of soluble Aβ protofibrils but does not clear insoluble Aβ in plaque-bearing tg-ArcSwe mice\", \"Animals treated with the antibody had approximately 75% lower levels of Aβ protofibrils in TBS extracts of brain as compared to placebo-treated animals, when measured with the mAb158 ELISA (Fig. 5A; Supplementary Table 2).\", \"Supplementary Table 2\", \"Figure 5\", \"Consistent with these findings, there were no significant differences in immunohistochemical Aβ burden or Congo burden between the groups (Figs. 5C, D; Supplementary Table 2).\", \"(A) Levels of soluble Aβ protofibrils (pg/mg tissue), measured by ELISA, were significantly lower at the end of treatment ⁎⁎⁎P < 0.001.\", \"This is the first report where an Aβ protofibril-selective antibody, mAb158, has been tested therapeutically and shown to prevent the accumulation of amyloid in APP transgenic mice.\", \"Passive immunization was associated with lower levels of Aβ protofibrils in both plaque-free and plaque-bearing animals, while effects on Aβ plaque deposition and insoluble Aβ were only seen with preventive treatment when animals were devoid of senile plaques when the therapy began.\", \"Lower levels of soluble Aβ protofibrils in tg-ArcSwe mice were accompanied by a halt in the development of Aβ plaque pathology in young mice, but not by clearance of pre-existing Aβ plaques in older mice. It is therefore likely that the mAb158 antibody prevented plaque formation by reducing Aβ protofibrils, suggesting that protofibrils are intermediates in the Aβ aggregation process in the brain.\", \"However, with a conformation-dependent antibody we here show that it is possible to selectively clear soluble Aβ species when the brain contains substantial amounts of insoluble Aβ.\",",
    "Curator Statement": "Actic mutation"
  },
  "AMGAB0199": {
    "Interaction ID": "AMGAB0199",
    "Antibody ID": "ABID0006.5",
    "Antibody name": "mAb158",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.nbd.2009.08.007",
    "PMID": 19703562.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"When the mAb158 antibody was administered for 4 months to plaque-bearing transgenic mice with both the Arctic and Swedish mutations (tg-ArcSwe), Aβ protofibril levels were lowered while measures of insoluble Aβ were unaffected.\", \"Soluble Aβ protofibrils were efficiently cleared by the mAb158 antibody, while amyloid burden was only reduced with preventive treatment.\", \"Passive immunization with mAb158 does not alter intraneuronal Aβ accumulation but prevents senile plaque formation in young tg-ArcSwe mice\", \"Administration of mAb158 antibodies between 4 and 8 months of age did not lower the amount of accumulated Aβ inside neurons. When stained with the 82E1 antibody no differences in punctate Aβ staining within the CA1 pyramidal cells were observed in animals treated with mAb158 (1.17 ± 0.23%; n =  11), control IgG (1.25 ± 0.14%; n =  12) or mAb1C3 (1.73 ± 0.21%; n =  12; Figs. 4A, B).\", \"Figure 4\", \"Neither treatment with mAb158, nor with mAb1C3, was associated with less accumulation of intraneuronal Aβ as compared to control IgG treatment.\", \"mAb158 reduces levels of soluble Aβ protofibrils but does not clear insoluble Aβ in plaque-bearing tg-ArcSwe mice\", \"Consistent with these findings, there were no significant differences in immunohistochemical Aβ burden or Congo burden between the groups (Figs. 5C, D; Supplementary Table 2).\", \"(B) Total levels of Aβ (ng/mg tissue) in formic acid extracts representing the insoluble Aβ pool did not differ between placebo and mAb158 treated mice, when analyzed with Aβ ELISA.\", \"The curative treatment with mAb158 immunization did not alter plaque load.\",",
    "Curator Statement": "Actic mutation. Insoluble Aβ was unnafected on plaque-bearing mice."
  },
  "AMGAB0200": {
    "Interaction ID": "AMGAB0200",
    "Antibody ID": "ABID0448",
    "Antibody name": "mAb1C3",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.nbd.2009.08.007",
    "PMID": 19703562.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",\"Both mAb158 and mAb1C3 inhibited Aβ fibrillogenesis (Fig. 2A) as compared to a control IgG, although mAb1C3 seemed to stop the aggregation process at an earlier stage than mAb158.\", \"Antibodies with conformational and linear N-terminal Aβ epitopes both halt in vitro Aβ1–42 fibrillogenesis. \",\"Both mAb158 and mAb1C3 diminished fibril formation.\", \"In addition, both antibodies inhibited Aβ fibrillogenesis as assessed with ThT fluorescence in vitro, although mAb158 interfered at a later stage in the process. The moderate increase in ThT fluorescence seen over 5 days with mAb158 likely reflects its selective preference for larger oligomers, whereas mAb1C3 halted aggregation early on, at the monomer/low molecular weight-Aβ stage resulting in a weaker ThT signal.\",",
    "Curator Statement": false
  },
  "AMGAB0201": {
    "Interaction ID": "AMGAB0201",
    "Antibody ID": "ABID0448",
    "Antibody name": "mAb1C3",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.nbd.2009.08.007",
    "PMID": 19703562.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry, ELISA",
    "Amyloid species identified": "Protein monomer, Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Table 1\", \"Soluble and insoluble Aβ levels in mice treated with mAb1C3 were essentially equal to that of mice treated with control IgG (Figs. 3A–C; Supplementary Table 1).\", \"Figure 3\", \"(A) Levels of soluble Aβ protofibrils (pg/mg tissue) were analyzed at the end of treatment and found to be significantly lower in mAb158 immunized mice as compared to mice given control IgG or mAb1C3. ⁎⁎P < 0.01.\", \"(C) Levels of total Aβ, Aβx-40 and Aβx-42 (ng/mg tissue) in formic acid extracts were all significantly lower in mAb158 treated mice as compared to control IgG and mAb1C3 treated mice. These Aβ ELISA measures mainly represent insoluble Aβ. ⁎⁎P < 0.01; ⁎P < 0.05.\", \"Administration of mAb158 antibodies between 4 and 8 months of age did not lower the amount of accumulated Aβ inside neurons. When stained with the 82E1 antibody no differences in punctate Aβ staining within the CA1 pyramidal cells were observed in animals treated with mAb158 (1.17 ± 0.23%; n =  11), control IgG (1.25 ± 0.14%; n =  12) or mAb1C3 (1.73 ± 0.21%; n =  12; Figs. 4A, B).\", \"Figure 4\", \"Young tg-ArcSwe mice treated with mAb1C3 did not show lower Aβ burden (Figs. 4C–D; Supplementary Table 1) or Congo burden (Figs. 4E, F; Supplementary Table 1), than mice treated with control IgG.\", \"Neither treatment with mAb158, nor with mAb1C3, was associated with less accumulation of intraneuronal Aβ as compared to control IgG treatment.\", \"Aβ burden was lower in mAb158 immunized animals, as compared to mice treated with control IgG or mAb1C3.\", \"Congo burden was significantly lower in mAb158 immunized mice than in mice given control IgG, while Congo burden in mAb1C3 immunized mice were similar to the control group. ⁎P < 0.05.\", \"Antibody mAb1C3, an Aβ antibody with an N-terminal epitope lacking Aβ protofibril-conformational selectivity, showed no therapeutic efficacy in tg-ArcSwe mice.\", \"Based on these in vitro studies, it was rather surprising that preventive treatment with mAb1C3 had no impact on Aβ pathology in tg-ArcSwe mice.\",",
    "Curator Statement": "Actic mutation"
  },
  "AMGAB0202": {
    "Interaction ID": "AMGAB0202",
    "Antibody ID": "ABID0449",
    "Antibody name": "Ly-128",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.nbd.2009.08.007",
    "PMID": 19703562.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry, ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"At the end of the study, animals treated with mAb158 had lower levels of soluble Aβ protofibrils as compared to animals treated with an irrelevant antibody (Fig. 3A; Supplementary Table 1).\", \"Figure 3\", \" Supplementary Table 1\", \" When the insoluble Aβ pool in the FA-extracts was analyzed, levels were much lower in mAb158 treated animals in all assays, as compared to mice given the control IgG (Fig. 3C; Supplementary Table 1).\", \"(A) Levels of soluble Aβ protofibrils (pg/mg tissue) were analyzed at the end of treatment and found to be significantly lower in mAb158 immunized mice as compared to mice given control IgG or mAb1C3. ⁎⁎P < 0.01.\", \"(C) Levels of total Aβ, Aβx-40 and Aβx-42 (ng/mg tissue) in formic acid extracts were all significantly lower in mAb158 treated mice as compared to control IgG and mAb1C3 treated mice. These Aβ ELISA measures mainly represent insoluble Aβ. ⁎⁎P < 0.01; ⁎P < 0.05.\", \"Administration of mAb158 antibodies between 4 and 8 months of age did not lower the amount of accumulated Aβ inside neurons. When stained with the 82E1 antibody no differences in punctate Aβ staining within the CA1 pyramidal cells were observed in animals treated with mAb158 (1.17 ± 0.23%; n =  11), control IgG (1.25 ± 0.14%; n =  12) or mAb1C3 (1.73 ± 0.21%; n =  12; Figs. 4A, B).\", \"Figure 4\", \"Neither treatment with mAb158, nor with mAb1C3, was associated with less accumulation of intraneuronal Aβ as compared to control IgG treatment.\", \"Aβ burden was lower in mAb158 immunized animals, as compared to mice treated with control IgG or mAb1C3.\", \"Congo burden was significantly lower in mAb158 immunized mice than in mice given control IgG, while Congo burden in mAb1C3 immunized mice were similar to the control group. ⁎P < 0.05.\", \"Animals treated with the antibody had approximately 75% lower levels of Aβ protofibrils in TBS extracts of brain as compared to placebo-treated animals, when measured with the mAb158 ELISA (Fig. 5A; Supplementary Table 2).\", \"Supplementary Table 2\", \"Figure 5\", \"Consistent with these findings, there were no significant differences in immunohistochemical Aβ burden or Congo burden between the groups (Figs. 5C, D; Supplementary Table 2).\", \"(B) Total levels of Aβ (ng/mg tissue) in formic acid extracts representing the insoluble Aβ pool did not differ between placebo and mAb158 treated mice, when analyzed with Aβ ELISA.\",",
    "Curator Statement": "Actic mutation"
  },
  "AMGAB0203": {
    "Interaction ID": "AMGAB0203",
    "Antibody ID": "ABID0449",
    "Antibody name": "Ly-128",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.nbd.2009.08.007",
    "PMID": 19703562.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 2\", \"Both mAb158 and mAb1C3 inhibited Aβ fibrillogenesis (Fig. 2A) as compared to a control IgG, although mAb1C3 seemed to stop the aggregation process at an earlier stage than mAb158.\",",
    "Curator Statement": false
  },
  "AMGAB0204": {
    "Interaction ID": "AMGAB0204",
    "Antibody ID": "ABID0473",
    "Antibody name": "P4D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.nbd.2013.09.001",
    "PMID": 24021662.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Intracerebral injection of P4D6, an SDPM1 peptide-mimotope antibody, also lowered brain amyloid plaque burden in APPswePSEN1dE9 mice.\", \"Co-staining for P4D6 and Thioflavin S showed reduced Thioflavin S staining in P4D6-injected brain regions. Amyloid plaque burden (Fig. 7C) and plaque number (Fig. 7D) were both significantly reduced in P4D6-injected areas. Interestingly, the size of remaining plaques (Fig. 7E), most of which were present at the edges of the injection sites, was unchanged, suggesting a local therapeutic effect at the site of injection. These data demonstrate that an SDPM1 peptide-mimotope antibody can directly affect brain Aβ amyloid plaque burden.\", \"Figure 7\", \"An SDPM1 peptide-mimotope antibody, P4D6, can lower brain Aβ amyloid plaque burden in the APPswePSENde9 mouse\",",
    "Curator Statement": false
  },
  "AMGAB0205": {
    "Interaction ID": "AMGAB0205",
    "Antibody ID": "ABID0018",
    "Antibody name": "Gosuranemab",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.nbd.2020.105120",
    "PMID": 32991997.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Tau seeding assay",
    "Amyloid species identified": "Available from the crystal structure deposited in the PDB: 6PXR",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Gosuranemab inhibited pathologic tau–induced tau aggregation in cells.\", \"Preincubation of seed-competent AD-tau with gosuranemab significantly inhibited tau aggregation in mouse primary cortical neurons. \", \"Gosuranemab inhibited tau seeding activity from brain homogenates and ISF in cell models and exhibited near-complete target engagement in ISF and CSF.\", \"Gosuranemab prevents tau aggregation in mouse primary cortical neurons\", \"Preincubation of AD-tau with gosuranemab resulted in a concentration-dependent reduction in tau aggregation, with the highest concentrations (4 and 8 μg/mL) resulting in a maximum ~50% reduction in aggregation compared with AD-tau alone, which was the maximal inhibition observed in this assay. \", \"Figure 6\", \"Gosuranemab binds extracellular tau in rTg4510 model\", \"Gosuranemab blocks tau aggregation induced by AD-tau in primary mouse neurons.\", \"Indeed, the seeding activity of AD brain homogenate is completely removed by gosuranemab, indicating that pathological tau seeds are not modified at T17 or Y18.\", \"Here we have shown for the first time that ISF derived from rTg4510 mice contains seed-competent tau [previously demonstrated for transgenic CSF (Takeda et al., 2016)] and that gosuranemab can completely thwart cellular tau aggregation induced by ISF.\", \"The ability of gosuranemab to prevent the induction of tau aggregation is not unique to the biosensor cell system because gosuranemab was also able to impede the aggregation of endogenous tau in wildtype mouse primary cortical neurons.\", \"Notably, in this assay the inhibitory effect of gosuranemab treatment appears to reach a maximum of 50%, a similar extent of inhibition as that resulting from treatment with the mid-region recognizing anti-tau Tau5 antibody. \", \"Importantly, the ability of AD-tau to seed tau aggregation in mouse neuronal cells was reduced in the presence of tau–gosuranemab complexes, suggesting that the effect of gosuranemab does not rely on the removal of the immune complex. \", \"Taken together, along with our biosensor and mouse neuron experiments, our data show that gosuranemab can efficiently bind extracellular tau seeds and potentially block tau spreading.\", \"The ability of gosuranemab to impede extracellular tau seeds and prevent intracellular tau aggregation, and the tolerability and safety of the antibody observed in clinical trials, provide continued optimism for ongoing trials of gosuranemab and other tau-targeted immunotherapies in AD.\",",
    "Curator Statement": false
  },
  "AMGAB0206": {
    "Interaction ID": "AMGAB0206",
    "Antibody ID": "ABID0418",
    "Antibody name": "Tau5",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.nbd.2020.105120",
    "PMID": 32991997.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Tau seeding assay",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Preincubation of AD-tau with gosuranemab resulted in a concentration-dependent reduction in tau aggregation, with the highest concentrations (4 and 8 μg/mL) resulting in a maximum ~50% reduction in aggregation compared with AD-tau alone, which was the maximal inhibition observed in this assay. Preincubation with Tau5 at 4 μg/mL had a similar degree of effect (Fig. 6B).\", \"Figure 6\", \"Notably, in this assay the inhibitory effect of gosuranemab treatment appears to reach a maximum of 50%, a similar extent of inhibition as that resulting from treatment with the mid-region recognizing anti-tau Tau5 antibody. \",",
    "Curator Statement": false
  },
  "AMGAB0207": {
    "Interaction ID": "AMGAB0207",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.nbd.2021.105365",
    "PMID": 33848635.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Analysis of the percentage area of the cortex (Fig. 6A and Supplementary Fig. S5) and the hippocampus (Fig. 6B and Supplementary Fig. S5) covered by amyloid staining revealed significant reductions close to baseline levels for all monotherapy treatment groups compared to the control group (treated with the isotype control antibody and Methocel vehicle).\", \"3D6 treatment reduced amyloid burden with 32% in both cortex and hippocampus (p < 0.0001).\", \"Figure 6\", \"Supplementary Figure S5\",",
    "Curator Statement": false
  },
  "AMGAB0208": {
    "Interaction ID": "AMGAB0208",
    "Antibody ID": "ABID0171",
    "Antibody name": "BAMB31",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.nbd.2021.105365",
    "PMID": 33848635.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other: Histology",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We have developed a novel, high affinity antibody against Aβ peptides bearing a pyroglutamate residue at amino acid position 3 (3pE), an Aβ species abundantly present in plaque deposits in AD brains. Here, we describe the preclinical characterization of this antibody, and demonstrate a significant reduction in amyloid burden in the absence of microhemorrhages in different mouse models with established plaque deposition. Moreover, we combined antibody treatment with chronic BACE1 inhibitor treatment and demonstrate significant clearance of pre-existing amyloid deposits in transgenic mouse brain, without induction of microhemorrhages and other histopathological findings.\", \"Chronic combination treatment with BAMB31 antibody and BACEi clears pre-existing deposited amyloid\", \"Analysis of the percentage area of the cortex (Fig. 6A and Supplementary Fig. S5) and the hippocampus (Fig. 6B and Supplementary Fig. S5) covered by amyloid staining revealed significant reductions close to baseline levels for all monotherapy treatment groups compared to the control group (treated with the isotype control antibody and Methocel vehicle).\", \"Combining BAMB31 with BACEi treatment significantly lowered existing plaque load below baseline levels in the cortex (57% reduction compared to isotype control antibody, p < 0.0001), and hippocampus (44% reduction compared to isotype control antibody, p < 0.0001) of aged APPLon mice (Fig. 6A and B, Supplementary Fig. S5).\", \"Figure 6\", \"Combining BAMB31 with BACEi treatment significantly lowered existing plaque load below baseline levels in the cortex (57% reduction compared to isotype control antibody, p < 0.0001), and hippocampus (44% reduction compared to isotype control antibody, p < 0.0001) of aged APPLon mice (Fig. 6A and B, Supplementary Fig. S5).\", \"Supplementary Figure S5\", \"In summary, BAMB31 treatment lowered amyloid burden versus isotype control antibody while combination treatment of BAMB31 with atabecestat lowered total amyloid levels below baseline levels indicative of clearance of pre-existing amyloid deposits.\", \"Plaque lowering in the brain occurs without inducing microhemorrhages after treatment with BAMB31\", \" In contrast, treatment with BAMB31, BACEi or the combination therapy did not induce a significant formation of microhemorrhages in these brain regions, while these treatments did cause reduction of amyloid burden as described above. In summary, these data confirm that combination treatment of BACEi with BAMB31 is able to reduce existing deposited Aβ load in transgenic animals without formation of microhemorrhages.\", \"Chronic administration of BAMB31 reduces amyloid deposition in the brain of PDAPP mice.\",  \"Supplementary Figure S6\", \"4G8 IHC illustrated a mean 37% and 23% reduction of plaque load by BAMB31 treatment compared to isotype control antibody treatment in cortical (p < 0.0001) and hippocampal (p = 0.0003) regions, respectively (Fig. 8B and Supplementary Fig. S6).\", \"Figure 8\",  \"Amyloid burden was reduced to approximately baseline levels by BAMB31 treatment.\", \"In our data set, we demonstrate consistent lowering of amyloid burden in APPLon and PDAPP mice to approximately baseline levels, both on biochemical and immunohistochemical measures.\",",
    "Curator Statement": false
  },
  "AMGAB0209": {
    "Interaction ID": "AMGAB0209",
    "Antibody ID": "ABID0432",
    "Antibody name": "AT8",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neulet.2014.05.047",
    "PMID": 24887583.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Intrahippocampal injection of AT8 reduces total tau levels without affecting Aβ load\", \"Figure 2\", \"In contrast, AT8 immunotherapy had no effect on Aβ levels: at any time point (Fig. 2).\", \"Tau immunization does not affect Aβ pathology.\", \"(A) In contrast to what was observed for tau, immunohistochemical analysis against Aβ (6E10) detected no differences between AT8 and control IgG treated hippocampi at either time point analyzed.\", \"Here, we demonstrate that a single intrahippocampal injection of AT8 significantly reduces early and late tau pathology in 3xTg-AD mice: within 7 days post-injection. In contrast, there were no changes in Aβ pathology.\", \"In the same study, we found that immunotherapy against normal human tau was ineffective in reducing tau or Aβ pathology: supporting the idea that antibody specificity is critical in determining immunization effectiveness.\", \"Unfortunately, a single injection of the AT8 did not affect pre-established Aβ pathology. \", \"Tau immunization does not affect established amyloid-β pathology.\",",
    "Curator Statement": false
  },
  "AMGAB0210": {
    "Interaction ID": "AMGAB0210",
    "Antibody ID": "ABID0432",
    "Antibody name": "AT8",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.neulet.2014.05.047",
    "PMID": 24887583.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"p-Tau immunotherapy reduces soluble and insoluble tau in aged 3xTg-AD mice\", , \"We report the novel findings that a single intrahippocampal injection of AT8, targeting phosphorylated Ser202, and Thr205 residues of tau [20], significantly reduces somatodendritic tau; without affecting Aβ.\", \"Intrahippocampal injection of AT8 reduces total tau levels without affecting Aβ load\", \"After one week, immunohistochemical analysis revealed a significant reduction in somatodendritic tau levels in AT8 treated vs. control hemispheres (Fig. 1).\", \"Figure 1\", \"Immunization with the AT8-antibody reduces somatodendritic tau immunoreactivity.\", \"Single injection with AT8 reduces both early and late pathological tau\", \"To investigate whether AT8 injection would diminish pathological tau, we conducted an assessment of early and late tau pathology. We found that treated hemispheres had significantly less AT8 reactivity in the CA1 subfield. This observation was only significant at one week post-injection (Fig. 4). To determine if there was a similar effect on more advance stages of tau pathology, we used the Gallyas silver stain method to stain for NFTs. The number of Gallyas positive neurons, within CA1, was reduced one week after AT8 injection compared to control hemispheres (Fig. 5). These findings show proof of concept that immunotherapy targeting p-tau can reduce different pools of pathological tau.\", \"Figure 4\", \"Figure 5\", \"Targeting p-tau via immunization significantly reduces early AT8 immunoreactivity.\", \"(A) Staining for phosphorylated residues Ser199 and Thr202 (AT8) show a large decreased in reactive at 7 days post-injection.\", \"(B) Statistical analysis of AT8 immunoreactivity, at post injection day 7, reveals a significant decrease in AT8 treated vs. control IgG treated sections (t-test, ***P < 0.0001, N = 7). \", \"3xTg-AD mice immunized with AT8 have reduced Gallyas positive neurons one week post-injection.\", \"A) Using the Gallyas silver stain method, we observed fewer Gallyas positive neurons in hemispheres treated with AT8 at 7 days.\", \"Here, we demonstrate that a single intrahippocampal injection of AT8 significantly reduces early and late tau pathology in 3xTg-AD mice: within 7 days post-injection.\", \"Overall, we found that a single intrahippocampal injection of AT8 significantly reduces total tau levels, and early and late pathological tau, in just one-weeks time.\", \"Nevertheless, a single administration of AT8 was able to reduce total tau, and early pathological tau; and attenuate the generation of any new tau pathology for several days.\", \"Targeting phosphorylated tau decreases both soluble and insoluble tau levels.\",",
    "Curator Statement": false
  },
  "AMGAB0211": {
    "Interaction ID": "AMGAB0211",
    "Antibody ID": "ABID0433",
    "Antibody name": "4G8",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neulet.2014.05.047",
    "PMID": 24887583.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"4G8 treatment resulted in a reduction of intra- and extracellular Aβ, corroborating our previous results (Fig. 3) [8].\", \"Figure 3\", \"Immunization with the 4G8-antibody reduces intra- and extracellular Aβ.\",",
    "Curator Statement": false
  },
  "AMGAB0212": {
    "Interaction ID": "AMGAB0212",
    "Antibody ID": "ABID0250",
    "Antibody name": "A4",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.neurobiolaging.2010.09.020",
    "PMID": 21067847.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Atomic force microscopy (AFM),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Similar to A4, E1 does not bind monomeric or fibrillar Aβ forms and inhibits Aβ aggregation and fibril formation, however the E1 nanobody stabilizes formation of a small nontoxic low-n Aβ species, whereas A4 binds a larger oligomeric form.\", \"Table 1\", \"When Aβ is coincubated with A4, Aβ particle heights between 3 and 4 nm aggregate species are predominantly generated after 2 days (Table 1C).\",",
    "Curator Statement": false
  },
  "AMGAB0213": {
    "Interaction ID": "AMGAB0213",
    "Antibody ID": "ABID0417",
    "Antibody name": "E4",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.neurobiolaging.2010.09.020",
    "PMID": 21067847.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Atomic force microscopy (AFM),",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"While E1, like A4, blocks assembly of Aβ into larger oligomeric and fibrillar forms and prevents any Aβ induced toxicity toward neuronal cells, it does so by binding a small Aβ oligomeric species, directing its assembly toward a stable nontoxic conformation.\", \"Similar to A4, E1 does not bind monomeric or fibrillar Aβ forms and inhibits Aβ aggregation and fibril formation, however the E1 nanobody stabilizes formation of a small nontoxic low-n Aβ species, whereas A4 binds a larger oligomeric form.\", \"Table 1\", \"E1 blocks aggregation of preformed Aβ oligomers into fibrils\", \"Addition of E1 to a 1-day preincubated Aβ sample completely inhibited further aggregation (Fig. 3A) similar to the ThT aggregation profile obtained when E1 was coincubated with monomeric Aβ (Fig. 1A).\", \"Figure 3\", \"When 1-day preincubated Aβ aggregates were incubated with E1, only small 1–2 nm Aβ aggregate species were observed even after incubation for 7 days (Fig. 3C). In contrast to the results obtained with 1 day preaggregated Aβ, E1 did not inhibit an increase in particle size when incubated with a 3-day preaggregated Aβ sample which contains predominantly 2–4-nm particle sizes (Fig. 3D–E).\", \"Because E1 blocks fibrillar aggregate formation by Aβ, but stabilizes a small, early oligomeric species and oligomeric Aβ forms have been implicated in toxicity, we studied how E1 alters cytotoxicity of Aβ aggregates toward SH-SY5Y neuroblastoma cells.\", \"Here, we describe a second nanobody E1, isolated by biopanning against in vitro generated Aβ oligomers, which also blocked Aβ aggregation and Aβ induced cytotoxicity toward neuronal cells.\", \" E1 inhibits further aggregation of preformed 1–2 nm Aβ aggregates (Fig. 3) but not of larger 2–3 nm Aβ aggregates.\", \"While both E1 and A4 prevent aggregation of Aβ into fibrils and prevent Aβ oligomer induced cytotoxicity to neuronal cells, height distribution analysis of AFM images indicate that E1 binds and stabilizes a small nontoxic oligomeric Aβ species (height 1–2 nm, Table 1) corresponding to a tetrameric form of Aβ (Ono et al., 2009), effectively blocking further aggregation of this early Aβ species.\", \"E1 can also bind to previously formed small 1–2 nm Aβ aggregates and either prevents their further assembly into toxic morphologies and fibrils or directs their assembly toward a stable nontoxic species.\",",
    "Curator Statement": false
  },
  "AMGAB0214": {
    "Interaction ID": "AMGAB0214",
    "Antibody ID": "ABID0510",
    "Antibody name": "m3.2",
    "Amyloid ID": "AGAMYID0022",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neurobiolaging.2012.04.007",
    "PMID": 22608241.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In the human APP transgenic mice Tg2576, passive immunization for eight weeks with a murine-Aβ-specific antibody reduced β-plaque pathology, robustly decreasing both murine and human Aβ levels.\", \"We conclude that passive anti-murine-Aβ immunization clears β-amyloid plaque pathology – including the major human Aβ component – and decreases behavioral deficits, arguing that targeting minor, endogenous brain plaque constituents can be beneficial, broadening the range of plaque-associated targets for AD therapeutics.\", \"Immunization targeting a minor plaque constituent clears β-amyloid and rescues behavioral deficits in an Alzheimer's disease mouse model\", \" Additionally, ELISA measurements of formic acid-extracted murine Aβ40, murine Aβ42, human Aβ40 and human Aβ42 showed significantly decreased levels of both human and murine Aβ in the m3.2-injected Tg2576 mice compared to control-antibody injected mice: murine Aβ40 levels decreased 65.3% +/− 10.2%, murine Aβ42 levels decreased 40.7% +/− 6.8%, human Aβ40 levels decreased 58.0% +/− 8.7% and human Aβ42 levels decreased 57.9% +/− 9.2% (Figure 2B).\", \"Figure 2\", \"Thioflavin S staining of brain tissue sections showed significant clearance of amyloid plaques in both cortex (Figure 2C, upper panels) and hippocampus (Figure 2C, lower panels) when comparing m3.2-injected mice (right panels) with controls (left panels). Quantification of amyloid area of brain coronal sections is shown in Figure 2D: amyloid plaque area decreased 54.4% +/− 15.0% in cortex and decreased 71.0% +/− 19.0% in hippocampus in m3.2-injected mice compared to controls.\",",
    "Curator Statement": false
  },
  "AMGAB0215": {
    "Interaction ID": "AMGAB0215",
    "Antibody ID": "ABID0510",
    "Antibody name": "m3.2",
    "Amyloid ID": "AGAMYID0026",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.neurobiolaging.2012.04.007",
    "PMID": 22608241.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" Additionally, ELISA measurements of formic acid-extracted murine Aβ40, murine Aβ42, human Aβ40 and human Aβ42 showed significantly decreased levels of both human and murine Aβ in the m3.2-injected Tg2576 mice compared to control-antibody injected mice: murine Aβ40 levels decreased 65.3% +/− 10.2%, murine Aβ42 levels decreased 40.7% +/− 6.8%, human Aβ40 levels decreased 58.0% +/− 8.7% and human Aβ42 levels decreased 57.9% +/− 9.2% (Figure 2B).\", \"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0216": {
    "Interaction ID": "AMGAB0216",
    "Antibody ID": "ABID0511",
    "Antibody name": "NT1",
    "Amyloid ID": "AGAMYID0022",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neurobiolaging.2012.04.007",
    "PMID": 22608241.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0217": {
    "Interaction ID": "AMGAB0217",
    "Antibody ID": "ABID0511",
    "Antibody name": "NT1",
    "Amyloid ID": "AGAMYID0026",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.neurobiolaging.2012.04.007",
    "PMID": 22608241.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0218": {
    "Interaction ID": "AMGAB0218",
    "Antibody ID": "ABID0322",
    "Antibody name": "β1",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.neurobiolaging.2013.06.013",
    "PMID": 23870837.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Beta1_HCDR1: GFSLSTSGMGVS, Beta1_HCDR2: DNDYYNIPSLKS, Beta1_HCDR3: PMNTWGDY, Beta1_LCDR1: RSSQSLVHSNGNTYLH, Beta1_LCDR2: KVSNRFS, Beta1_LCDR3: SQNTHVPLT",
    "Quote of the interaction": "\" As expected, parenchymal CAA was not detected in 11-month-old APP23 mice, however, all animals showed CAA in the meninges (Fig. 8). No CAA was found in APP23 × BIN66 mice (both lines) indicating that β1 blocked its formation as much as amyloid plaque deposition.\", \"Figure 8\" , \"These data suggest that the robust reduction in the amyloid plaque load observed in older mice was primarily mediated by a complex of β1 with soluble Aβ.\",",
    "Curator Statement": false
  },
  "AMGAB0219": {
    "Interaction ID": "AMGAB0219",
    "Antibody ID": "ABID0322",
    "Antibody name": "β1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neurobiolaging.2013.06.013",
    "PMID": 23870837.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Beta1_HCDR1: GFSLSTSGMGVS, Beta1_HCDR2: DNDYYNIPSLKS, Beta1_HCDR3: PMNTWGDY, Beta1_LCDR1: RSSQSLVHSNGNTYLH, Beta1_LCDR2: KVSNRFS, Beta1_LCDR3: SQNTHVPLT",
    "Quote of the interaction": "\"At 11 months of age, β1 expression reduced amyloid by 97% compared with age-matched APP23 mice.\", \" Aβ42 in the single APP23 transgenic littermates accumulated to 975 ± 131 pmol/g and was reduced to 42 ± 2 pmol/g in the presence of the β1 transgene (−95.7%, pooled data; Fig. 7B). This was further supported by immune histological quantification of the plaque load. In the APP23 × BIN/66 mice, the cortical plaque load was significantly reduced, for BIN66/2 from 0.32 ± 0.15% to 0.02 ± 0.02% (−94.4%), and for the BIN66/3 mice from 0.52 ± 0.11% to 0.01 ± 0.01% (−98.9%) (Fig. 7C). Combined data for both BIN66 lines demonstrated a decrease of −97.2% in the double transgenic mice when compared with the single transgenic controls (Table 2). Reduced plaque area in the β1-expressing mice correlated highly significantly with the amount of total Aβ40 (Table 2) and Aβ42 (not shown) determined biochemically. \", \"Figure 7\", \"Substantial formation of Aβ-antibody complexes caused a dramatic reduction of amyloid plaque deposition suggestive of a chaperone-type mechanism. Our study represents the first proof of concept for a gene therapy designed to increase the amount of an intact Aβ antibody in the brain, which dramatically reduces age-related Aβ accumulation. \",",
    "Curator Statement": false
  },
  "AMGAB0220": {
    "Interaction ID": "AMGAB0220",
    "Antibody ID": "ABID0322",
    "Antibody name": "β1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neurobiolaging.2013.06.013",
    "PMID": 23870837.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Beta1_HCDR1: GFSLSTSGMGVS, Beta1_HCDR2: DNDYYNIPSLKS, Beta1_HCDR3: PMNTWGDY, Beta1_LCDR1: RSSQSLVHSNGNTYLH, Beta1_LCDR2: KVSNRFS, Beta1_LCDR3: SQNTHVPLT",
    "Quote of the interaction": "\"Analysis of Aβ oligomers using a specific single-epitope 4G8/4G8 immune assay showed a small (23.8%), nonsignificant increase in Aβ oligomers in APP23 × BIN66/3 mice when compared with their APP23 siblings (Fig. 6B).\", \"Figure 6\",",
    "Curator Statement": false
  },
  "AMGAB0221": {
    "Interaction ID": "AMGAB0221",
    "Antibody ID": "ABID0387",
    "Antibody name": "07/1 mAb",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neurobiolaging.2015.08.021",
    "PMID": 26453001.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"An anti-pyroglutamate-3 Aβ vaccine reduces plaques and improves cognition in APPswe/PS1ΔE9 mice\", \"After 28 weeks of treatment, plaque burden was reduced and cognitive performance of 07/1-immunized Tg mice, especially at the higher dose, was normalized to wild-type (Wt) levels in two hippocampal-dependent tests and partially spared compared to PBS-treated Tg mice.\", \"In hippocampus, R1282 IR was reduced by 35% in 500μg 07/1-immunized Tg mice (p<0.05), 45% in 150μg 07/1-immunized Tg mice (p<0.01) and 58% in 3A1-immunized Tg mice (p<0.001) compared to PBS-treated Tg mice (Fig 3A-D, Q).\", \"Figure 3\", \"Similar treatment-specific reductions were observed for Aβ(1-x) deposition in the hippocampus (Fig 3E-H). APPswe/PS1ΔE9 mice immunized with either 150μg or 500μg 07/1 mAb exhibited reductions in 82E1 IR of 35% (p<0.001) and 32% (p<0.001), respectively, compared to PBS-treated Tg mice, while 3A1-immunized Tg mice showed a 42% reduction (p<0.001) of Aβ1-x deposition compared to PBS-treated Tg mice (Fig 3Q). Dramatic reductions in pGlu-3 Aβ depositions were observed in all vaccinated mice in the hippocampus (Fig 3J-L). Image analysis revealed that 500μg 07/1-immunized Tg mice had a 50% reduction (p<0.001), 150μg 07/1-immunized Tg mice had a 58% reduction (p<0.001) and 3A1-immunized Tg mice had a 48% reduction in pGlu-3 Aβ deposition compared to PBS-treated Tg mice (Fig 3I,Q). Changes in Thioflavin S-positive plaques were less robust, as only 150μg 07/1-immunized and 3A1-immuned Tg mice had significant reductions of 22% (p<0.05) and 29%, respectively (p<0.01), relative to PBS-treated Tg mice (Fig 3Q).\", \"Prophylactic passive immunization with 07/1 mAb at 150 and 500μg doses significantly lowered pGlu-3 Aβ deposition as well as general Aβ and Aβ1-x species but not Thioflavin S-positive plaques (ThioS) in the brains of APPswe/PS1ΔE9 Tg mice.\",\"In hippocampus, significant reductions in general Aβ, Aβ 1-x and pGlu-3 deposition we appreciated in 150 and 500μg 07/1-immunized mice as well as 200μg 3A1-immunized Tg mice compared to PBS-treated Tg controls (Q). In addition, significant reductions in general and pGlu-3 Aβ deposition were found in the frontal cortex in 150μg and 500μg 07/1-immunized mice and also in 3A1-immunized mice compared to PBS-treated Tg controls (R). In frontal cortex, no significant differences in Aβ1-x deposition or ThioS-positive plaques at either dose of the 07/1 antibody was observed, however, there were significant reductions in Aβ1-x and Thio S plaque burden in the frontal cortex of 3A1-immunized mice (R). In cerebellum, a significant reduction in general Aβ staining was observed in both 150μg and 500μg 07/1-immunized Tg mice and 3A1-immunized Tg mice compared to PBS-controls (S). When quantifying Aβ1-x deposition, significant reductions were noted in 150μg 07/1-immunized and 3A1-immunized Tg mice compared to PBS-treated Tg controls. No significant changes in pGlu-3 Aβ deposition were found in the hippocampus with any treatment and only 3A1-immunized mice showed reductions in Thio S staining in cerebellum compared PBS controls (S). \",\"In parallel to significant plaque reduction in hippocampus, similar results were also observed in both the frontal cortex and cerebellum. In frontal cortex, general Aβ IR was reduced 20% (p<0.05) in 150μg 07/1-immunized and 25% (p<0.01) in 500μg 07/1-immunized Tg mice and 44% (p<0.001) in 3A1-immunized Tg mice compared to PBS-treated Tg controls (Fig 3R). Complementary to general Aβ reductions, Aβ(1-x) deposition was reduced by 23% (n.s.) in 500μg 07/1-immunized Tg and 22% (n.s) in 150μg 07/1-immunized Tg mice, while 3A1-immunized Tg mice displayed a 46% reduction (p<0.05) in Aβ1-x relative to PBS-treated Tg controls (Fig 3R). Pyroglutamate-3 Aβ deposition was reduced by a 30% (p<0.05) in 500μg 07/1-immunized Tg mice and 37% (p<0.01) in 150μg 07/1-immunized Tg mice, while 3A1-immunized Tg mice had a 40% reduction in pGlu-3 Aβ (p<0.01) compared to PBS-treated Tg mice. As in the hippocampus, Thioflavin S-positive plaques were less effectively cleared in the frontal cortex, and only 3A1-immunized Tg mice exhibited a significant 27% reduction of 07/2 IR (p<0.05; Fig 3R).\",\"In the cerebellum, the greatest reductions were observed in general Aβ and Aβ1-x IR in which 150μg 07/1-immunized and 500μg 07/1-immunized Tg mice had reductions of 27% (p<0.05) and 43% (p<0.001) in general Aβ deposition and 52% (p<0.01) and 36% (n.s.) of Aβ(1-x) IR, respectively (Fig 3S). 3A1-immunized Tg mice also showed a 47% reduction in general Aβ (p<0.001) and a 45% reduction in Aβ(1-x) deposition (p<0.05) compared to PBS-treated Tg mice (Fig 3S). No significant differences in pGlu-3 Aβ deposition in cerebellum were noted in any immunization group and only 3A1-immunized Tg mice exhibited a significant 29% reduction in Thioflavin S-positive plaques (p<0.05; Fig 3S).\",\"Although there was a trend for reduction in all immunizations groups, compared to PBS-treated Tg controls, no significant differences were observed (data not show).\",\"Biochemical analyses from hippocampal, cortical and cerebellar soluble and insoluble brain homogenates did not confirm reductions in cerebral Aβ levels observed by neuropathological analyses. \", \"There were no significant changes in Aβ(x-42) or pGlu-3 Aβ(42) levels in either the SDS (soluble) or formic acid (insoluble) fractions from hippocampus or cortex in any immunization group compared PBS-treated Tg mice (Table 1). \",\"Here, we tested the 07/1 mAb at two different doses, 150 and 500μg, to investigate whether there would be a dose-dependent clearance of cerebral Aβ and/or cognitive benefits. Importantly, we confirmed our previous results and observed a significant lowering of total Aβ plaque deposition in the absence of microhemorrhage and, for the first time, demonstrate rescue of cognitive deficits with anti-pGlu-3 Aβ passive immunotherapy in a preclinical AD-like mouse model.\", \"Detailed neuropathological analyses and accompanying quantitative image analysis, demonstrated significant reductions in the deposition of general Aβ, Aβ(1-x) and pGlu-3 Aβ species in several brain regions, particularly the hippocampus. Overall, there was not a dose-dependent clearance when comparing 150μg 07/1-immunized and 500μg 07/1-immunized Tg mice to PBS-treated Tg controls as both doses prevented cerebral Aβ deposition similarly.\", \"Moreover, the 07/1 mAb appeared not as effective as the 3A1 mAb in preventing deposition of fibrillar amyloid, general Aβ and Aβ(1-x).\",\"Alternatively, the 07/1 mAb may have prevented aggregation of pGlu-3 Aβ, resulting in increased levels of soluble Aβ (as observed in cerebellum). \",",
    "Curator Statement": "The amyloid deposition was not widespread throughout regions, especially for the lower dose treatments, and the ThioS staining."
  },
  "AMGAB0222": {
    "Interaction ID": "AMGAB0222",
    "Antibody ID": "ABID0387",
    "Antibody name": "07/1 mAb",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neurobiolaging.2015.08.021",
    "PMID": 26453001.0,
    "Impact of the antibody on amyloid formation": "No effect,",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\",Changes in Thioflavin S-positive plaques were less robust, as only 150μg 07/1-immunized and 3A1-immuned Tg mice had significant reductions of 22% (p<0.05) and 29%, respectively (p<0.01), relative to PBS-treated Tg mice (Fig 3Q).\", \"Prophylactic passive immunization with 07/1 mAb at 150 and 500μg doses significantly lowered pGlu-3 Aβ deposition as well as general Aβ and Aβ1-x species but not Thioflavin S-positive plaques (ThioS) in the brains of APPswe/PS1ΔE9 Tg mice.\",\"In frontal cortex, no significant differences in Aβ1-x deposition or ThioS-positive plaques at either dose of the 07/1 antibody was observed, however, there were significant reductions in Aβ1-x and Thio S plaque burden in the frontal cortex of 3A1-immunized mice (R).\", \"No significant differences in pGlu-3 Aβ deposition in cerebellum were noted in any immunization group and only 3A1-immunized Tg mice exhibited a significant 29% reduction in Thioflavin S-positive plaques (p<0.05; Fig 3S).\",\"Although there was a trend for reduction in all immunizations groups, compared to PBS-treated Tg controls, no significant differences were observed (data not show).\",\"There were no significant changes in Aβ(x-42) or pGlu-3 Aβ(42) levels in either the SDS (soluble) or formic acid (insoluble) fractions from hippocampus or cortex in any immunization group compared PBS-treated Tg mice (Table 1). \", \"Moreover, the 07/1 mAb appeared not as effective as the 3A1 mAb in preventing deposition of fibrillar amyloid, general Aβ and Aβ(1-x).\",\"Alternatively, the 07/1 mAb may have prevented aggregation of pGlu-3 Aβ, resulting in increased levels of soluble Aβ (as observed in cerebellum). \",",
    "Curator Statement": "The amyloid deposition was not widespread throughout regions, especially for the lower dose treatments, and the ThioS staining."
  },
  "AMGAB0223": {
    "Interaction ID": "AMGAB0223",
    "Antibody ID": "ABID0387",
    "Antibody name": "07/1 mAb",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1016/j.neurobiolaging.2015.08.021",
    "PMID": 26453001.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"Dramatic reductions in pGlu-3 Aβ depositions were observed in all vaccinated mice in the hippocampus (Fig 3J-L). Image analysis revealed that 500μg 07/1-immunized Tg mice had a 50% reduction (p<0.001), 150μg 07/1-immunized Tg mice had a 58% reduction (p<0.001) and 3A1-immunized Tg mice had a 48% reduction in pGlu-3 Aβ deposition compared to PBS-treated Tg mice (Fig 3I,Q). Changes in Thioflavin S-positive plaques were less robust, as only 150μg 07/1-immunized and 3A1-immuned Tg mice had significant reductions of 22% (p<0.05) and 29%, respectively (p<0.01), relative to PBS-treated Tg mice (Fig 3Q).\", \"Prophylactic passive immunization with 07/1 mAb at 150 and 500μg doses significantly lowered pGlu-3 Aβ deposition as well as general Aβ and Aβ1-x species but not Thioflavin S-positive plaques (ThioS) in the brains of APPswe/PS1ΔE9 Tg mice.\",\"In hippocampus, significant reductions in general Aβ, Aβ 1-x and pGlu-3 deposition we appreciated in 150 and 500μg 07/1-immunized mice as well as 200μg 3A1-immunized Tg mice compared to PBS-treated Tg controls (Q). In addition, significant reductions in general and pGlu-3 Aβ deposition were found in the frontal cortex in 150μg and 500μg 07/1-immunized mice and also in 3A1-immunized mice compared to PBS-treated Tg controls (R). No significant changes in pGlu-3 Aβ deposition were found in the hippocampus with any treatment and only 3A1-immunized mice showed reductions in Thio S staining in cerebellum compared PBS controls (S). \",\"In parallel to significant plaque reduction in hippocampus, similar results were also observed in both the frontal cortex and cerebellum. In frontal cortex, general Aβ IR was reduced 20% (p<0.05) in 150μg 07/1-immunized and 25% (p<0.01) in 500μg 07/1-immunized Tg mice and 44% (p<0.001) in 3A1-immunized Tg mice compared to PBS-treated Tg controls (Fig 3R). Complementary to general Aβ reductions, Aβ(1-x) deposition was reduced by 23% (n.s.) in 500μg 07/1-immunized Tg and 22% (n.s) in 150μg 07/1-immunized Tg mice, while 3A1-immunized Tg mice displayed a 46% reduction (p<0.05) in Aβ1-x relative to PBS-treated Tg controls (Fig 3R). Pyroglutamate-3 Aβ deposition was reduced by a 30% (p<0.05) in 500μg 07/1-immunized Tg mice and 37% (p<0.01) in 150μg 07/1-immunized Tg mice, while 3A1-immunized Tg mice had a 40% reduction in pGlu-3 Aβ (p<0.01) compared to PBS-treated Tg mice. As in the hippocampus, Thioflavin S-positive plaques were less effectively cleared in the frontal cortex, and only 3A1-immunized Tg mice exhibited a significant 27% reduction of 07/2 IR (p<0.05; Fig 3R).\",\"In the cerebellum, the greatest reductions were observed in general Aβ and Aβ1-x IR in which 150μg 07/1-immunized and 500μg 07/1-immunized Tg mice had reductions of 27% (p<0.05) and 43% (p<0.001) in general Aβ deposition and 52% (p<0.01) and 36% (n.s.) of Aβ(1-x) IR, respectively (Fig 3S). 3A1-immunized Tg mice also showed a 47% reduction in general Aβ (p<0.001) and a 45% reduction in Aβ(1-x) deposition (p<0.05) compared to PBS-treated Tg mice (Fig 3S). No significant differences in pGlu-3 Aβ deposition in cerebellum were noted in any immunization group and only 3A1-immunized Tg mice exhibited a significant 29% reduction in Thioflavin S-positive plaques (p<0.05; Fig 3S).\",\"Although there was a trend for reduction in all immunizations groups, compared to PBS-treated Tg controls, no significant differences were observed (data not show).\",\"Biochemical analyses from hippocampal, cortical and cerebellar soluble and insoluble brain homogenates did not confirm reductions in cerebral Aβ levels observed by neuropathological analyses. \", \"There were no significant changes in Aβ(x-42) or pGlu-3 Aβ(42) levels in either the SDS (soluble) or formic acid (insoluble) fractions from hippocampus or cortex in any immunization group compared PBS-treated Tg mice (Table 1). \", \"Detailed neuropathological analyses and accompanying quantitative image analysis, demonstrated significant reductions in the deposition of general Aβ, Aβ(1-x) and pGlu-3 Aβ species in several brain regions, particularly the hippocampus.  \"Alternatively, the 07/1 mAb may have prevented aggregation of pGlu-3 Aβ, resulting in increased levels of soluble Aβ (as observed in cerebellum). \",",
    "Curator Statement": "The amyloid deposition was not widespread throughout regions, especially for the lower dose treatments, and the ThioS staining."
  },
  "AMGAB0224": {
    "Interaction ID": "AMGAB0224",
    "Antibody ID": "ABID0387",
    "Antibody name": "07/1 mAb",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1016/j.neurobiolaging.2015.08.021",
    "PMID": 26453001.0,
    "Impact of the antibody on amyloid formation": "No effect,",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"No significant changes in pGlu-3 Aβ deposition were found in the hippocampus with any treatment and only 3A1-immunized mice showed reductions in Thio S staining in cerebellum compared PBS controls (S). \",\"No significant differences in pGlu-3 Aβ deposition in cerebellum were noted in any immunization group and only 3A1-immunized Tg mice exhibited a significant 29% reduction in Thioflavin S-positive plaques (p<0.05; Fig 3S).\",\"Although there was a trend for reduction in all immunizations groups, compared to PBS-treated Tg controls, no significant differences were observed (data not show).\",\"Biochemical analyses from hippocampal, cortical and cerebellar soluble and insoluble brain homogenates did not confirm reductions in cerebral Aβ levels observed by neuropathological analyses. \", \"There were no significant changes in Aβ(x-42) or pGlu-3 Aβ(42) levels in either the SDS (soluble) or formic acid (insoluble) fractions from hippocampus or cortex in any immunization group compared PBS-treated Tg mice (Table 1). \",",
    "Curator Statement": "The amyloid deposition was not widespread throughout regions, especially for the lower dose treatments, and the ThioS staining."
  },
  "AMGAB0225": {
    "Interaction ID": "AMGAB0225",
    "Antibody ID": "ABID0388",
    "Antibody name": "3A1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neurobiolaging.2015.08.021",
    "PMID": 26453001.0,
    "Impact of the antibody on amyloid formation": "No effect,",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"Changes in Thioflavin S-positive plaques were less robust, as only 150μg 07/1-immunized and 3A1-immuned Tg mice had significant reductions of 22% (p<0.05) and 29%, respectively (p<0.01), relative to PBS-treated Tg mice (Fig 3Q).\",\"Although there was a trend for reduction in all immunizations groups, compared to PBS-treated Tg controls, no significant differences were observed (data not show).\",\"Biochemical analyses from hippocampal, cortical and cerebellar soluble and insoluble brain homogenates did not confirm reductions in cerebral Aβ levels observed by neuropathological analyses. \",\"There were no significant changes in Aβ(x-42) or pGlu-3 Aβ(42) levels in either the SDS (soluble) or formic acid (insoluble) fractions from hippocampus or cortex in any immunization group compared PBS-treated Tg mice (Table 1). \",",
    "Curator Statement": "The amyloid deposition was not widespread throughout regions, especially for the lower dose treatments, and the ThioS staining."
  },
  "AMGAB0226": {
    "Interaction ID": "AMGAB0226",
    "Antibody ID": "ABID0388",
    "Antibody name": "3A1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neurobiolaging.2015.08.021",
    "PMID": 26453001.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Mice that received 3A1 had reduced plaque burden but showed no cognitive benefit.\", \"In hippocampus, R1282 IR was reduced by 35% in 500μg 07/1-immunized Tg mice (p<0.05), 45% in 150μg 07/1-immunized Tg mice (p<0.01) and 58% in 3A1-immunized Tg mice (p<0.001) compared to PBS-treated Tg mice (Fig 3A-D, Q).\", \"Figure 3\", \"Similar treatment-specific reductions were observed for Aβ(1-x) deposition in the hippocampus (Fig 3E-H).\", \"APPswe/PS1ΔE9 mice immunized with either 150μg or 500μg 07/1 mAb exhibited reductions in 82E1 IR of 35% (p<0.001) and 32% (p<0.001), respectively, compared to PBS-treated Tg mice, while 3A1-immunized Tg mice showed a 42% reduction (p<0.001) of Aβ1-x deposition compared to PBS-treated Tg mice (Fig 3Q).\", \"Changes in Thioflavin S-positive plaques were less robust, as only 150μg 07/1-immunized and 3A1-immuned Tg mice had significant reductions of 22% (p<0.05) and 29%, respectively (p<0.01), relative to PBS-treated Tg mice (Fig 3Q).\",\"In hippocampus, significant reductions in general Aβ, Aβ 1-x and pGlu-3 deposition we appreciated in 150 and 500μg 07/1-immunized mice as well as 200μg 3A1-immunized Tg mice compared to PBS-treated Tg controls (Q).\", \"In cerebellum, a significant reduction in general Aβ staining was observed in both 150μg and 500μg 07/1-immunized Tg mice and 3A1-immunized Tg mice compared to PBS-controls (S). When quantifying Aβ1-x deposition, significant reductions were noted in 150μg 07/1-immunized and 3A1-immunized Tg mice compared to PBS-treated Tg controls.\", \"In parallel to significant plaque reduction in hippocampus, similar results were also observed in both the frontal cortex and cerebellum. In frontal cortex, general Aβ IR was reduced 20% (p<0.05) in 150μg 07/1-immunized and 25% (p<0.01) in 500μg 07/1-immunized Tg mice and 44% (p<0.001) in 3A1-immunized Tg mice compared to PBS-treated Tg controls (Fig 3R). Complementary to general Aβ reductions, Aβ(1-x) deposition was reduced by 23% (n.s.) in 500μg 07/1-immunized Tg and 22% (n.s) in 150μg 07/1-immunized Tg mice, while 3A1-immunized Tg mice displayed a 46% reduction (p<0.05) in Aβ1-x relative to PBS-treated Tg controls (Fig 3R).\", \"As in the hippocampus, Thioflavin S-positive plaques were less effectively cleared in the frontal cortex, and only 3A1-immunized Tg mice exhibited a significant 27% reduction of 07/2 IR (p<0.05; Fig 3R).\",\"In the cerebellum, the greatest reductions were observed in general Aβ and Aβ1-x IR in which 150μg 07/1-immunized and 500μg 07/1-immunized Tg mice had reductions of 27% (p<0.05) and 43% (p<0.001) in general Aβ deposition and 52% (p<0.01) and 36% (n.s.) of Aβ(1-x) IR, respectively (Fig 3S). 3A1-immunized Tg mice also showed a 47% reduction in general Aβ (p<0.001) and a 45% reduction in Aβ(1-x) deposition (p<0.05) compared to PBS-treated Tg mice (Fig 3S).\",\"Although there was a trend for reduction in all immunizations groups, compared to PBS-treated Tg controls, no significant differences were observed (data not show).\",\"Biochemical analyses from hippocampal, cortical and cerebellar soluble and insoluble brain homogenates did not confirm reductions in cerebral Aβ levels observed by neuropathological analyses. \", \"Moreover, the 07/1 mAb appeared not as effective as the 3A1 mAb in preventing deposition of fibrillar amyloid, general Aβ and Aβ(1-x).\",",
    "Curator Statement": "The amyloid deposition was not widespread throughout regions, especially for the lower dose treatments, and the ThioS staining."
  },
  "AMGAB0227": {
    "Interaction ID": "AMGAB0227",
    "Antibody ID": "ABID0388",
    "Antibody name": "3A1",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1016/j.neurobiolaging.2015.08.021",
    "PMID": 26453001.0,
    "Impact of the antibody on amyloid formation": "No effect,",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\",  \"No significant changes in pGlu-3 Aβ deposition were found in the hippocampus with any treatment and only 3A1-immunized mice showed reductions in Thio S staining in cerebellum compared PBS controls (S). \",\"No significant differences in pGlu-3 Aβ deposition in cerebellum were noted in any immunization group and only 3A1-immunized Tg mice exhibited a significant 29% reduction in Thioflavin S-positive plaques (p<0.05; Fig 3S).\",\"Although there was a trend for reduction in all immunizations groups, compared to PBS-treated Tg controls, no significant differences were observed (data not show).\",\"Biochemical analyses from hippocampal, cortical and cerebellar soluble and insoluble brain homogenates did not confirm reductions in cerebral Aβ levels observed by neuropathological analyses. \",\"There were no significant changes in Aβ(x-42) or pGlu-3 Aβ(42) levels in either the SDS (soluble) or formic acid (insoluble) fractions from hippocampus or cortex in any immunization group compared PBS-treated Tg mice (Table 1). \",",
    "Curator Statement": "The amyloid deposition was not widespread throughout regions, especially for the lower dose treatments, and the ThioS staining."
  },
  "AMGAB0228": {
    "Interaction ID": "AMGAB0228",
    "Antibody ID": "ABID0388",
    "Antibody name": "3A1",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1016/j.neurobiolaging.2015.08.021",
    "PMID": 26453001.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"Dramatic reductions in pGlu-3 Aβ depositions were observed in all vaccinated mice in the hippocampus (Fig 3J-L). Image analysis revealed that 500μg 07/1-immunized Tg mice had a 50% reduction (p<0.001), 150μg 07/1-immunized Tg mice had a 58% reduction (p<0.001) and 3A1-immunized Tg mice had a 48% reduction in pGlu-3 Aβ deposition compared to PBS-treated Tg mice (Fig 3I,Q). Changes in Thioflavin S-positive plaques were less robust, as only 150μg 07/1-immunized and 3A1-immuned Tg mice had significant reductions of 22% (p<0.05) and 29%, respectively (p<0.01), relative to PBS-treated Tg mice (Fig 3Q).\",\"In hippocampus, significant reductions in general Aβ, Aβ 1-x and pGlu-3 deposition we appreciated in 150 and 500μg 07/1-immunized mice as well as 200μg 3A1-immunized Tg mice compared to PBS-treated Tg controls (Q). In addition, significant reductions in general and pGlu-3 Aβ deposition were found in the frontal cortex in 150μg and 500μg 07/1-immunized mice and also in 3A1-immunized mice compared to PBS-treated Tg controls (R).\", \" Pyroglutamate-3 Aβ deposition was reduced by a 30% (p<0.05) in 500μg 07/1-immunized Tg mice and 37% (p<0.01) in 150μg 07/1-immunized Tg mice, while 3A1-immunized Tg mice had a 40% reduction in pGlu-3 Aβ (p<0.01) compared to PBS-treated Tg mice. As in the hippocampus, Thioflavin S-positive plaques were less effectively cleared in the frontal cortex, and only 3A1-immunized Tg mice exhibited a significant 27% reduction of 07/2 IR (p<0.05; Fig 3R).\",\"In the cerebellum, the greatest reductions were observed in general Aβ and Aβ1-x IR in which 150μg 07/1-immunized and 500μg 07/1-immunized Tg mice had reductions of 27% (p<0.05) and 43% (p<0.001) in general Aβ deposition and 52% (p<0.01) and 36% (n.s.) of Aβ(1-x) IR, respectively (Fig 3S).\", \"Moreover, the 07/1 mAb appeared not as effective as the 3A1 mAb in preventing deposition of fibrillar amyloid, general Aβ and Aβ(1-x).\",",
    "Curator Statement": "The amyloid deposition was not widespread throughout regions, especially for the lower dose treatments, and the ThioS staining."
  },
  "AMGAB0229": {
    "Interaction ID": "AMGAB0229",
    "Antibody ID": "ABID0003.6",
    "Antibody name": "mE8-IgG2a",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuron.2012.10.029",
    "PMID": 23217740.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We developed a plaque-specific antibody that targets a modified Aβ peptide (Aβp3-42), which showed robust clearance of pre-existing plaque without causing microhemorrhage.\", \"Plaque-specific anti-Aβp3-42 antibody removes pre-existing plaque\", \" These antibodies robustly labeled deposited plaque in both AD and PDAPP brain sections and led to a significant reduction of deposited Aβ in an ex vivo phagocytosis assay.\", \"Therapeutic plaque-lowering studies performed with the anti-Aβp3-42 antibodies in extremely aged PDAPP mice (23 to 26 months of age) demonstrated that mE8 on either maximal or minimal effector function significantly lowered deposited Aβ, whereas mice treated with the N-terminal antibody 3D6 (mIgG2b), which binds both soluble and insoluble Aβ, lacked efficacy.\", \"Analysis of the remaining Aβ1-42 present in the tissue sections demonstrated that the 3D6 and mE8 (minimal or maximal effector function) amino-terminal antibodies significantly facilitated clearance of deposited plaque (p < 0.001).\", \"The Aβp3-x antibody with maximal effector function (mE8, IgG2a) cleared significantly (p < 0.001) more plaque than the Aβp3-x antibody with minimal effector function (mE8, IgG1).\", \" In contrast, treatment with either Aβp3-x antibody, minimal or maximal effector function, resulted in significant Aβ lowering as compared to the IgG control antibody (p < 0.01 and p < 0.001, respectively). The mE8-IgG1 and mE8-IgG2a lowered the Aβ42 by ∼38% and ∼53%, respectively. The Aβp3-x antibody with maximal effector function trended to being more efficacious than the minimal effector function antibody; however, this difference did not reach statistical significance. Importantly, the mE8-IgG2a antibody significantly lowered Aβ42 by ∼30% in the hippocampus as compared to the time zero mice (t test; p < 0.0066), thus demonstrating clearance of existing Aβ deposits.\", \"The analyses of the cortical guanidine lysates yielded very similar outcomes with the exception that only the mE8-IgG2a with maximal effector function significantly decreased Aβ42 deposition (Figure 3B). \", \"Figure 2\", \"Figure 3\", \"Morphological differences in the deposited plaque were observed in the animals treated with the Aβp3-x antibodies when brain sections were immunostained with multiple anti-Aβ antibodies (Figure 4A). Animals treated with mE8-IgG2a consistently had areas of plaque deposition in the CA1 and CA3 regions that histologically appeared blurred and less defined; a similar but less dramatic effect was observed in mE8-IgG1-treated animals. However, an analysis of the percent area of the hippocampus covered by Aβ immunostaining showed no significant difference among the treatment groups (Figure 4B). Likewise, analysis of the total amyloid load or microglia counts revealed no significant treatment effects (Figures S2 and S3). Note that the PDAPP transgenic model mainly develops diffuse plaque. Thus, in this model, the anti-Aβp3-x antibodies predominantly reduced Aβ as pre-existing diffuse plaque.\", \"Figure 4\", \"A significant dose-dependent decrease in Aβ42 was observed for the mE8-IgG2a treatment in both hippocampus (p < 0.0001, Figure 5A) and cortex (p < 0.0073, Figure 5B). In hippocampus, the 4 and 12.5 mg/kg doses significantly lowered deposited Aβ42 by 31% (p < 0.001) and 39% (p < 0.001), respectively. The 1.5 mg/kg dose of mE8-IgG2a was a nonsignificant 15% lower.\", \"Figure 5\", \"In contrast, treatment with either mE8-IgG1 or mE8-IgG2a did not significantly increase microhemorrhage, even though these Aβp3-x antibodies were able to reduce deposited Aβ.\", \"These results demonstrate that treatment with the Aβp3-x antibodies in aged PDAPP mice with maximal plaque loads was able to reduce existing deposited Aβ without CAA-related microhemorrhage liability.\", \"Consistent with previous reports for similar N-terminal antibodies, treatment with 3D6 resulted in a significant ∼68% decrease of hippocampal Aβ42 (p < 0.001) as compared to the control IgG, although levels were higher than the untreated animals sacrificed at 10.5 months of age. The mE8-IgG2a treatment resulted in a nonsignificant ∼30% decrease in Aβ42 as compared to the control IgG-treated mice. Similar results were observed in the cortical extracts from these mice (Figure 5D).\", \"Figure 5\", \"Utilizing Aβp3-x antibodies with isotypes of varying effector potency, we demonstrated that robust clearance of existing plaque was in agreement with reported ability to engage activating Fc receptors. Additionally, the plaque-lowering ability of the Aβp3-x antibody was shown to be highly repeatable in a dose-response study. Differences were observed in the efficacy of plaque lowering between hippocampus and cortex for the anti-Aβp3-x antibodies that may be a result of the lower net levels of deposited Aβ or possibly the delay in deposition in this tissue relative to hippocampus (and thus less modified Aβ species).\", \" Interestingly, in contrast to 3D6 and other N-terminal antibodies, the Aβp3-x antibody failed to show significant plaque lowering when used as a preventative measure.\", \"The current anti-Aβp3-x results clearly demonstrate that plaque can be removed without this adverse event.\", \"In summary, these studies have demonstrated that the development of plaque-specific Aβp3-x antibodies that lack binding to soluble Aβ peptides leads to significant engagement of Aβ deposits (i.e., plaque binding) and to the subsequent removal of existing plaque without a microhemorrhage liability.\",",
    "Curator Statement": false
  },
  "AMGAB0230": {
    "Interaction ID": "AMGAB0230",
    "Antibody ID": "ABID0003.6",
    "Antibody name": "mE8-IgG2a",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuron.2012.10.029",
    "PMID": 23217740.0,
    "Impact of the antibody on amyloid formation": "No effect,",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\",",
    "Curator Statement": "Although most indicators were diminished, the immunoreactive plaque area did not change with the application of the antibody."
  },
  "AMGAB0231": {
    "Interaction ID": "AMGAB0231",
    "Antibody ID": "ABID0003.9",
    "Antibody name": "mE8-IgG1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuron.2012.10.029",
    "PMID": 23217740.0,
    "Impact of the antibody on amyloid formation": "No effect,",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\",",
    "Curator Statement": "Although most indicators were diminished, the immunoreactive plaque area did not change with the application of the antibody."
  },
  "AMGAB0232": {
    "Interaction ID": "AMGAB0232",
    "Antibody ID": "ABID0003.9",
    "Antibody name": "mE8-IgG1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuron.2012.10.029",
    "PMID": 23217740.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We developed a plaque-specific antibody that targets a modified Aβ peptide (Aβp3-42), which showed robust clearance of pre-existing plaque without causing microhemorrhage.\", \"Plaque-specific anti-Aβp3-42 antibody removes pre-existing plaque\", \" These antibodies robustly labeled deposited plaque in both AD and PDAPP brain sections and led to a significant reduction of deposited Aβ in an ex vivo phagocytosis assay.\", \"Therapeutic plaque-lowering studies performed with the anti-Aβp3-42 antibodies in extremely aged PDAPP mice (23 to 26 months of age) demonstrated that mE8 on either maximal or minimal effector function significantly lowered deposited Aβ, whereas mice treated with the N-terminal antibody 3D6 (mIgG2b), which binds both soluble and insoluble Aβ, lacked efficacy.\", \"Analysis of the remaining Aβ1-42 present in the tissue sections demonstrated that the 3D6 and mE8 (minimal or maximal effector function) amino-terminal antibodies significantly facilitated clearance of deposited plaque (p < 0.001).\", \"The Aβp3-x antibody with maximal effector function (mE8, IgG2a) cleared significantly (p < 0.001) more plaque than the Aβp3-x antibody with minimal effector function (mE8, IgG1).\", \" In contrast, treatment with either Aβp3-x antibody, minimal or maximal effector function, resulted in significant Aβ lowering as compared to the IgG control antibody (p < 0.01 and p < 0.001, respectively). The mE8-IgG1 and mE8-IgG2a lowered the Aβ42 by ∼38% and ∼53%, respectively. The Aβp3-x antibody with maximal effector function trended to being more efficacious than the minimal effector function antibody; however, this difference did not reach statistical significance. Importantly, the mE8-IgG2a antibody significantly lowered Aβ42 by ∼30% in the hippocampus as compared to the time zero mice (t test; p < 0.0066), thus demonstrating clearance of existing Aβ deposits.\", \"Figure 2\", \"Figure 3\", \"Morphological differences in the deposited plaque were observed in the animals treated with the Aβp3-x antibodies when brain sections were immunostained with multiple anti-Aβ antibodies (Figure 4A). Animals treated with mE8-IgG2a consistently had areas of plaque deposition in the CA1 and CA3 regions that histologically appeared blurred and less defined; a similar but less dramatic effect was observed in mE8-IgG1-treated animals. However, an analysis of the percent area of the hippocampus covered by Aβ immunostaining showed no significant difference among the treatment groups (Figure 4B). Likewise, analysis of the total amyloid load or microglia counts revealed no significant treatment effects (Figures S2 and S3). Note that the PDAPP transgenic model mainly develops diffuse plaque. Thus, in this model, the anti-Aβp3-x antibodies predominantly reduced Aβ as pre-existing diffuse plaque.\", \"Figure 4\", \"In contrast, treatment with either mE8-IgG1 or mE8-IgG2a did not significantly increase microhemorrhage, even though these Aβp3-x antibodies were able to reduce deposited Aβ.\", \"These results demonstrate that treatment with the Aβp3-x antibodies in aged PDAPP mice with maximal plaque loads was able to reduce existing deposited Aβ without CAA-related microhemorrhage liability.\", \"Utilizing Aβp3-x antibodies with isotypes of varying effector potency, we demonstrated that robust clearance of existing plaque was in agreement with reported ability to engage activating Fc receptors. Additionally, the plaque-lowering ability of the Aβp3-x antibody was shown to be highly repeatable in a dose-response study. Differences were observed in the efficacy of plaque lowering between hippocampus and cortex for the anti-Aβp3-x antibodies that may be a result of the lower net levels of deposited Aβ or possibly the delay in deposition in this tissue relative to hippocampus (and thus less modified Aβ species).\", \" Interestingly, in contrast to 3D6 and other N-terminal antibodies, the Aβp3-x antibody failed to show significant plaque lowering when used as a preventative measure.\", \"The current anti-Aβp3-x results clearly demonstrate that plaque can be removed without this adverse event.\", \"In summary, these studies have demonstrated that the development of plaque-specific Aβp3-x antibodies that lack binding to soluble Aβ peptides leads to significant engagement of Aβ deposits (i.e., plaque binding) and to the subsequent removal of existing plaque without a microhemorrhage liability.\",",
    "Curator Statement": false
  },
  "AMGAB0233": {
    "Interaction ID": "AMGAB0233",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuron.2012.10.029",
    "PMID": 23217740.0,
    "Impact of the antibody on amyloid formation": "No effect,",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "Mature fibrils, Protofilaments, Protofibrils, Oligomers, Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Interestingly, a comparator N-terminal Aβ antibody 3D6, which binds both soluble and insoluble Aβ1-42, lacked efficacy for lowering existing plaque but manifested a significant microhemorrhage liability. Mechanistic studies suggested that the lack of efficacy for 3D6 was attributed to poor target engagement in plaques.\", \"Therapeutic plaque-lowering studies performed with the anti-Aβp3-42 antibodies in extremely aged PDAPP mice (23 to 26 months of age) demonstrated that mE8 on either maximal or minimal effector function significantly lowered deposited Aβ, whereas mice treated with the N-terminal antibody 3D6 (mIgG2b), which binds both soluble and insoluble Aβ, lacked efficacy.\", \"An analysis of the 9-month-old PDAPP mice treated for 3 months with 3D6 demonstrated a significant prevention of Aβ deposition in hippocampus (40%, p < 0.0161, Figure 1A) and cortex (69%, p < 0.0001, Figure 1B).\", \"In contrast, the aged PDAPP mice treated from 18 to 21 months showed no effect on levels of existing deposited Aβ in either the hippocampus (p = 0.7441, Figure 1C) or cortex (p = 0.5959, Figure 1D).\", \"Figure 1\", \"Analysis of the remaining Aβ1-42 present in the tissue sections demonstrated that the 3D6 and mE8 (minimal or maximal effector function) amino-terminal antibodies significantly facilitated clearance of deposited plaque (p < 0.001).\", \"Similar to our previous studies, treatment with the 3D6 antibody had no effect on amyloid levels in hippocampal lysates.\", \"Figure 1\", \"Figure 4\", \"Consistent with previous reports for similar N-terminal antibodies, treatment with 3D6 resulted in a significant ∼68% decrease of hippocampal Aβ42 (p < 0.001) as compared to the control IgG, although levels were higher than the untreated animals sacrificed at 10.5 months of age. The mE8-IgG2a treatment resulted in a nonsignificant ∼30% decrease in Aβ42 as compared to the control IgG-treated mice. Similar results were observed in the cortical extracts from these mice (Figure 5D).\", \"Figure 5\", \"In contrast, the N-terminal antibody 3D6, which binds soluble and insoluble Aβ, reveals an opposite pattern of efficacy (no clearance of established plaque and strong prevention of deposition), thereby suggesting that the major mechanism of action for these two antibodies is different.\", \"Our studies with the N-terminal antibody 3D6, the murine equivalent of bapineuzumab, replicated the literature wherein 3D6 significantly prevented plaque deposition yet consistently failed to alter deposition when administered to mice with extensive pre-existing Aβ plaque.\", \" Interestingly, in contrast to 3D6 and other N-terminal antibodies, the Aβp3-x antibody failed to show significant plaque lowering when used as a preventative measure.\", \"The same 3D6 antibody was successful in an ex vivo phagocytosis model in which exogenous antibody facilitated plaque removal; however, in this experimental paradigm, high levels of antibody (10 μg/ml) were added to a static system in which soluble Aβ effects would be negated. Additionally, 3D6 was efficacious when administered in a prevention paradigm, a scenario that would precede the establishment of high concentrations of soluble monomer associated with plaque and indeed a paradigm that previous reports (Das et al., 2003) have suggested may not primarily involve a phagocytic mechanism.\", \"Strikingly, the 3D6 antibody induced a clear increase in microhemorrhage; however, the antibody did not remove plaque.\",",
    "Curator Statement": "3D6 was mostly innefective, although for young mice it did have an anti-amyloid effect."
  },
  "AMGAB0234": {
    "Interaction ID": "AMGAB0234",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuron.2012.10.029",
    "PMID": 23217740.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "Mature fibrils, Protofilaments, Protofibrils, Oligomers, Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"An analysis of the 9-month-old PDAPP mice treated for 3 months with 3D6 demonstrated a significant prevention of Aβ deposition in hippocampus (40%, p < 0.0161, Figure 1A) and cortex (69%, p < 0.0001, Figure 1B).\", \"Figure 1\", \"Analysis of the remaining Aβ1-42 present in the tissue sections demonstrated that the 3D6 and mE8 (minimal or maximal effector function) amino-terminal antibodies significantly facilitated clearance of deposited plaque (p < 0.001).\", \"Figure 4\", \"Consistent with previous reports for similar N-terminal antibodies, treatment with 3D6 resulted in a significant ∼68% decrease of hippocampal Aβ42 (p < 0.001) as compared to the control IgG, although levels were higher than the untreated animals sacrificed at 10.5 months of age.\", \"Figure 5\", \"In contrast, the N-terminal antibody 3D6, which binds soluble and insoluble Aβ, reveals an opposite pattern of efficacy (no clearance of established plaque and strong prevention of deposition), thereby suggesting that the major mechanism of action for these two antibodies is different.\", \"Our studies with the N-terminal antibody 3D6, the murine equivalent of bapineuzumab, replicated the literature wherein 3D6 significantly prevented plaque deposition yet consistently failed to alter deposition when administered to mice with extensive pre-existing Aβ plaque.\",",
    "Curator Statement": "3D6 was mostly innefective, although for young mice it did have an anti-amyloid effect."
  },
  "AMGAB0235": {
    "Interaction ID": "AMGAB0235",
    "Antibody ID": "ABID0019.6",
    "Antibody name": "HJ8.5",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.neuron.2013.07.046",
    "PMID": 24075978.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo\", \" We infused 3 effective antibodies or controls into the lateral ventricle of P301S mice for 3 months. The antibodies markedly reduced hyperphosphorylated, aggregated, and insoluble tau. They also blocked development of tau seeding activity detected in brain lysates using the biosensor assay, reduced microglial activation, and improved cognitive deficits.\", \"Figure 2\", \"Tau-antibodies block the uptake and seeding activity of P301S tau aggregates as detected by a FRET assay.\", \"We found all the tau antibodies incubated with P301S brain lysates significantly blocked seeding activity.\", \"Out of all tau-antibodies we used, HJ8.5 was the most potent in blocking the uptake and seeding activity of P301S brain lysates. \", \" The HJ8.5 antibody blocked seeding activity at concentrations as low as 0.25 μg/ml compared to controls.\", \" At 0.5 μg/ml, both HJ8.5 and HJ9.3 antibody significantly blocked uptake and seeding activity compared to control.\", \" Treatment with HJ8.5, the most potent antibody in vitro, profoundly reduced tau pathology.\",",
    "Curator Statement": false
  },
  "AMGAB0236": {
    "Interaction ID": "AMGAB0236",
    "Antibody ID": "ABID0019.6",
    "Antibody name": "HJ8.5",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.neuron.2013.07.046",
    "PMID": 24075978.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo,",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), ELISA, Western Blot,",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-tau antibody treatment reduces abnormally phosphorylated tau\", \" HJ8.5 treatment strongly reduced AT8 staining (Figure 4C), especially in the neuropil.\", \" Quantitative analysis of AT8 staining in piriform cortex (Figure 5A), entorhinal cortex (Figure 5B), and amygdala (Figure 5C) demonstrated a strong but variable reduction in phospho-tau in all anti-tau antibody treated mice.\", \"HJ8.5 antibody markedly reduced AT8 staining in piriform cortex, entorhinal cortex, and amygdala.\", \"HJ9.3 had slightly decreased effects compared to HJ8.5, and HJ9.4 had significant effects in both entorhinal cortex and amygdala but not in the piriform cortex (Figure 5).\", \"Anti-tau antibodies strongly decreased AT8 staining in P301S mouse brain.\", \"Figure 5\", \"Certain anti-tau antibodies strongly decrease AT8 staining in P301S mouse brain\", \"There was reduced AT8 staining in several different brain regions in the anti-tau antibody treated mice compared to PBS or HJ3.4 antibody treated mice. HJ8.5 had the largest effects.\", \"Supplementary Figure S6\", \"ThioS staining of neurofibrillary tangles was reduced in HJ8.5antibody treated mice compared to the PBS or HJ3.4 antibody treated mice. \", \" HJ8.5 antibody treated mice had significantly less ThioS staining compared to PBS or HJ3.4 antibody treated mice.\", \"Insoluble tau levels are reduced by antibodies HJ8.5 and HJ9.3 in P301S mice.\", \" However, there was a significant decrease of insoluble tau levels in 70% FA fractions in the HJ8.5 and HJ9.3 anti-tau antibodies treated mice compared to the PBS or HJ3.4 antibody treated groups.\", \"Figure 6\", \"In 70% FA fractions, we also found that phospho tau at Ser202 and Thr205 as detected by AT8 reactivity was reduced in anti-tau antibody treated mice compared to controls, similar to total human tau.\", \"Anti-tau antibodies reduce detergent-insoluble tau and seeding activity\", \"We analyzed every animal studied and found that HJ8.5 and HJ9.3 decreased detergent-insoluble tau by >50% vs. controls (Figure 6C). \", \"Supplementary Figure S7\", \" Treatment with HJ8.5, the most potent antibody in vitro, profoundly reduced tau pathology.\", \" While the model of aggregate flux requires further testing, our results here are consistent with this idea, since antibody treatment profoundly reduced intracellular tau pathology.\",",
    "Curator Statement": false
  },
  "AMGAB0237": {
    "Interaction ID": "AMGAB0237",
    "Antibody ID": "ABID0452",
    "Antibody name": "HJ9.3",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.neuron.2013.07.046",
    "PMID": 24075978.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.,",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo\", \" We infused 3 effective antibodies or controls into the lateral ventricle of P301S mice for 3 months. The antibodies markedly reduced hyperphosphorylated, aggregated, and insoluble tau. They also blocked development of tau seeding activity detected in brain lysates using the biosensor assay, reduced microglial activation, and improved cognitive deficits.\", \"Figure 2\", \"Tau-antibodies block the uptake and seeding activity of P301S tau aggregates as detected by a FRET assay.\", \"We found all the tau antibodies incubated with P301S brain lysates significantly blocked seeding activity.\", \" At 0.5 μg/ml, both HJ8.5 and HJ9.3 antibody significantly blocked uptake and seeding activity compared to control.\",",
    "Curator Statement": false
  },
  "AMGAB0238": {
    "Interaction ID": "AMGAB0238",
    "Antibody ID": "ABID0452",
    "Antibody name": "HJ9.3",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.neuron.2013.07.046",
    "PMID": 24075978.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo,",
    "Experimental method(s)": "Immunohistochemistry, , ELISA, Western Blot,",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-tau antibody treatment reduces abnormally phosphorylated tau\", \"HJ8.5 treatment strongly reduced AT8 staining (Figure 4C), especially in the neuropil. HJ9.3 and HJ9.4 also decreased AT8 staining but the effects were slightly less (Figure 4D and 4E). \",\" Quantitative analysis of AT8 staining in piriform cortex (Figure 5A), entorhinal cortex (Figure 5B), and amygdala (Figure 5C) demonstrated a strong but variable reduction in phospho-tau in all anti-tau antibody treated mice.\", \"HJ9.3 had slightly decreased effects compared to HJ8.5, and HJ9.4 had significant effects in both entorhinal cortex and amygdala but not in the piriform cortex (Figure 5).\", \"Anti-tau antibodies strongly decreased AT8 staining in P301S mouse brain.\", \"Figure 5\", \"Certain anti-tau antibodies strongly decrease AT8 staining in P301S mouse brain\", \"There was reduced AT8 staining in several different brain regions in the anti-tau antibody treated mice compared to PBS or HJ3.4 antibody treated mice. HJ8.5 had the largest effects.\",  \"Insoluble tau levels are reduced by antibodies HJ8.5 and HJ9.3 in P301S mice.\", \" However, there was a significant decrease of insoluble tau levels in 70% FA fractions in the HJ8.5 and HJ9.3 anti-tau antibodies treated mice compared to the PBS or HJ3.4 antibody treated groups.\", \"Figure 6\", \"In 70% FA fractions, we also found that phospho tau at Ser202 and Thr205 as detected by AT8 reactivity was reduced in anti-tau antibody treated mice compared to controls, similar to total human tau.\",\"Anti-tau antibodies reduce detergent-insoluble tau and seeding activity\",\"We analyzed every animal studied and found that HJ8.5 and HJ9.3 decreased detergent-insoluble tau by >50% vs. controls (Figure 6C). \",\"Supplementary Figure S7\", \" While the model of aggregate flux requires further testing, our results here are consistent with this idea, since antibody treatment profoundly reduced intracellular tau pathology.\",",
    "Curator Statement": false
  },
  "AMGAB0239": {
    "Interaction ID": "AMGAB0239",
    "Antibody ID": "ABID0452",
    "Antibody name": "HJ9.3",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.neuron.2013.07.046",
    "PMID": 24075978.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo,",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-tau antibody treatment reduces abnormally phosphorylated tau\", \"HJ8.5 treatment strongly reduced AT8 staining (Figure 4C), especially in the neuropil. HJ9.3 and HJ9.4 also decreased AT8 staining but the effects were slightly less (Figure 4D and 4E). \",\" Quantitative analysis of AT8 staining in piriform cortex (Figure 5A), entorhinal cortex (Figure 5B), and amygdala (Figure 5C) demonstrated a strong but variable reduction in phospho-tau in all anti-tau antibody treated mice.\", \"HJ9.3 had slightly decreased effects compared to HJ8.5, and HJ9.4 had significant effects in both entorhinal cortex and amygdala but not in the piriform cortex (Figure 5).\", \"Anti-tau antibodies strongly decreased AT8 staining in P301S mouse brain.\", \"Figure 5\", \"Certain anti-tau antibodies strongly decrease AT8 staining in P301S mouse brain\", \"There was reduced AT8 staining in several different brain regions in the anti-tau antibody treated mice compared to PBS or HJ3.4 antibody treated mice. HJ8.5 had the largest effects.\", \"Supplementary Figure S6\", \"Insoluble tau levels are reduced by antibodies HJ8.5 and HJ9.3 in P301S mice.\",",
    "Curator Statement": "Semi quantitative Thio-S staining showed no difference between negative controls and HJ9.3 antibody."
  },
  "AMGAB0240": {
    "Interaction ID": "AMGAB0240",
    "Antibody ID": "ABID0453",
    "Antibody name": "HJ9.4",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.neuron.2013.07.046",
    "PMID": 24075978.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.,",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo\", \" We infused 3 effective antibodies or controls into the lateral ventricle of P301S mice for 3 months. The antibodies markedly reduced hyperphosphorylated, aggregated, and insoluble tau. They also blocked development of tau seeding activity detected in brain lysates using the biosensor assay, reduced microglial activation, and improved cognitive deficits.\", \"Figure 2\", \"Tau-antibodies block the uptake and seeding activity of P301S tau aggregates as detected by a FRET assay.\", \"We found all the tau antibodies incubated with P301S brain lysates significantly blocked seeding activity.\", \"HJ9.4 was least potent in blocking the uptake and seeding activity, consistent with its higher affinity for mouse tau.\",",
    "Curator Statement": false
  },
  "AMGAB0241": {
    "Interaction ID": "AMGAB0241",
    "Antibody ID": "ABID0453",
    "Antibody name": "HJ9.4",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.neuron.2013.07.046",
    "PMID": 24075978.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo,",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-tau antibody treatment reduces abnormally phosphorylated tau\", \"HJ8.5 treatment strongly reduced AT8 staining (Figure 4C), especially in the neuropil. HJ9.3 and HJ9.4 also decreased AT8 staining but the effects were slightly less (Figure 4D and 4E). \",\" Quantitative analysis of AT8 staining in piriform cortex (Figure 5A), entorhinal cortex (Figure 5B), and amygdala (Figure 5C) demonstrated a strong but variable reduction in phospho-tau in all anti-tau antibody treated mice.\", \"HJ9.3 had slightly decreased effects compared to HJ8.5, and HJ9.4 had significant effects in both entorhinal cortex and amygdala but not in the piriform cortex (Figure 5).\", \"Anti-tau antibodies strongly decreased AT8 staining in P301S mouse brain.\", \"Figure 5\", \"Certain anti-tau antibodies strongly decrease AT8 staining in P301S mouse brain\", \"There was reduced AT8 staining in several different brain regions in the anti-tau antibody treated mice compared to PBS or HJ3.4 antibody treated mice. HJ8.5 had the largest effects.\", \"Supplementary Figure S6\",\"In 70% FA fractions, we also found that phospho tau at Ser202 and Thr205 as detected by AT8 reactivity was reduced in anti-tau antibody treated mice compared to controls, similar to total human tau.\",\"Anti-tau antibodies reduce detergent-insoluble tau and seeding activity\", \" While the model of aggregate flux requires further testing, our results here are consistent with this idea, since antibody treatment profoundly reduced intracellular tau pathology.\",",
    "Curator Statement": false
  },
  "AMGAB0242": {
    "Interaction ID": "AMGAB0242",
    "Antibody ID": "ABID0453",
    "Antibody name": "HJ9.4",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.neuron.2013.07.046",
    "PMID": 24075978.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo,",
    "Experimental method(s)": "ELISA, Western Blot,",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 6\", \"Insoluble tau levels in the HJ9.4 antibody treated mice were not different from the control groups.\", \"Supplementary Figure S7\", \"Insoluble tau levels were no different in HJ9.4-treated groups versus PBS or HJ3.4.\",",
    "Curator Statement": "Insoluble tau levels for antibody HJ9.4 weer not different from the control groups."
  },
  "AMGAB0243": {
    "Interaction ID": "AMGAB0243",
    "Antibody ID": "ABID0454",
    "Antibody name": "HJ3.4",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.neuron.2013.07.046",
    "PMID": 24075978.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0244": {
    "Interaction ID": "AMGAB0244",
    "Antibody ID": "ABID0454",
    "Antibody name": "HJ3.4",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.neuron.2013.07.046",
    "PMID": 24075978.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo,",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), ELISA, Western Blot,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"In mice treated with PBS and HJ3.4, AT8 strongly stained neuronal cell bodies and the neuropil in multiple brain regions, particularly in the piriform cortex, entorhinal cortex, amygdala, and hippocampus (Figure 4A and 4B).\", \"Figure 4\",\"Figure 5\", \"There was reduced AT8 staining in several different brain regions in the anti-tau antibody treated mice compared to PBS or HJ3.4 antibody treated mice. HJ8.5 had the largest effects.\", \"Supplementary Figure S6\", \"ThioS staining of neurofibrillary tangles was reduced in HJ8.5antibody treated mice compared to the PBS or HJ3.4 antibody treated mice. \", \" HJ8.5 antibody treated mice had significantly less ThioS staining compared to PBS or HJ3.4 antibody treated mice.\", \" However, there was a significant decrease of insoluble tau levels in 70% FA fractions in the HJ8.5 and HJ9.3 anti-tau antibodies treated mice compared to the PBS or HJ3.4 antibody treated groups.\", \"Figure 6\", \"We analyzed every animal studied and found that HJ8.5 and HJ9.3 decreased detergent-insoluble tau by >50% vs. controls (Figure 6C). \", \"Supplementary Figure S7\", \"Insoluble tau levels were no different in HJ9.4-treated groups versus PBS or HJ3.4.\",",
    "Curator Statement": false
  },
  "AMGAB0245": {
    "Interaction ID": "AMGAB0245",
    "Antibody ID": "ABID0002.9.2",
    "Antibody name": "mAb31",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuron.2013.10.061",
    "PMID": 24411731.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunohistochemistry, Quantitative Morphometric Analysis,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The degree of amyloidosis in the APPPS2 double-transgenic mice was quantified at baseline, and following vehicle, low-dose parent mAb31 and low-dose sFab construct treatment (Figures 6E–6H). At these low doses, no in vivo effect was detected with the parent mAb31 (Figure 6I), which was anticipated based on a previous long-term study over 5 months (Bohrmann et al., 2012).\", \"Figure 6\",",
    "Curator Statement": false
  },
  "AMGAB0246": {
    "Interaction ID": "AMGAB0246",
    "Antibody ID": "ABID0026.1",
    "Antibody name": "sFab Brain Shuttle",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuron.2013.10.061",
    "PMID": 24411731.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Quantitative Morphometric Analysis,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 6\", \" In contrast, a significant reduction in plaque numbers both in cortex and hippocampus was observed with the middose of 2.67 mg/kg of the sFab construct. Even at the much lower dose of 0.53 mg/kg (Figure 6I), a trend was seen in favor of the sFab construct, especially in the cortex, although it did not reach statistical significance. A secondary analysis of plaque sizes revealed a more pronounced reduction of numbers for small plaques (Figure S8), in agreement with the mode of action for mAb31 (Bohrmann et al., 2012).\", \"Supplementary Figure S8\", \"The sFab construct predominantly and significantly reduces the number of small to medium size plagues both in cortex and hippocampus, in accordance with the mode of action of mAb31.\"",
    "Curator Statement": false
  },
  "AMGAB0247": {
    "Interaction ID": "AMGAB0247",
    "Antibody ID": "ABID0463",
    "Antibody name": "mO6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuropharm.2015.07.038",
    "PMID": 26256421.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "VH-CDR1: GYTVTSYG, VH-CDR2: GINTNTGNP, VH-CDR3: ARSSSGYQGSSYYFDMDV, VL-CDR1: QGISKY, VL-CDR2: AAS, VL-CDR3: LQDD SYP--",
    "Quote of the interaction": "\"ScFv MO6 specifically recognized and bound to the oligomeric Aβ42 (Aβ42 oligomers and immature protofibrils; 18–37 kDa), and reduced their levels mainly by blocking their formation, although scFv MO6 also induced disaggregation of Aβ42 aggregates.\", \"ScFv MO6 inhibited the aggregation of Aβ42 and induced the disaggregation of preformed Aβ42 aggregates in vitro\", \"All Aβ42 species co-incubated with scFv MO6 exhibited significantly lower fluorescence intensities than the corresponding Aβ42 species alone, especially in the case of Aβ42 oligomers and protofibrils, at any given time point (1–48 h). This result indicated that scFv MO6 effectively inhibits further aggregation of Aβ42 species, especially in the case of Aβ42 oligomers or protofibrils.\", \"Figure 3\", \"The effects of scFv MO6 on Aβ42 aggregation were further confirmed by electron microscopy after 24 h of co-incubation of scFv MO6 with different Aβ42 species (Fig. 4). After 24 h of co-incubation with scFv MO6 at 37 °C, Aβ42 monomers and oligomers (Fig. 4d and e) grew remarkable more slowly than in the absence of scFv MO6 (Fig. 4a and c), indicating that scFv MO6 inhibited the assembly of Aβ42 monomer into oligomers, and induced the disaggregation of medium-sized Aβ42 oligomers into much smaller globular units. Amorphous or diffuse state of the incubated Aβ42 protofibrils and Aβ42 fibrils was discernable upon incubation with scFv MO6 (Fig. 4f and h); these amorphous structures might represent large Aβ42-MO6 complexes.\", \"Nevertheless, almost immediately, the co-incubated scFv MO6 bound to the nascent oligomers, and inhibited further aggregation. Furthermore, binding of scFv MO6 induced disaggregation of the oligomers to a certain extent (Fig. 3b).\", \"Together, the results shown in Fig. 3, Fig. 4 demonstrated that scFv MO6 could inhibit the aggregation of Aβ42 and induce the disaggregation of preformed oligomeric Aβ42 aggregates such as Aβ42 oligomers or immature protofibrils in vitro. These results are consistent with the binding specificity of scFv MO6 (Fig. 2).\", \"Consequently, scFv MO6 ameliorated or attenuated Aβ42-mediated cytotoxicity (Fig. 5).\",",
    "Curator Statement": false
  },
  "AMGAB0248": {
    "Interaction ID": "AMGAB0248",
    "Antibody ID": "ABID0463",
    "Antibody name": "mO6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuropharm.2015.07.038",
    "PMID": 26256421.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "VH-CDR1: GYTVTSYG, VH-CDR2: GINTNTGNP, VH-CDR3: ARSSSGYQGSSYYFDMDV, VL-CDR1: QGISKY, VL-CDR2: AAS, VL-CDR3: LQDD SYP--",
    "Quote of the interaction": "\"Furthermore, presence of scFv MO6 in the Aβ42 oligomers or protofibrils significantly reduced their fluorescence intensity to values even lower than their own baseline level during the first 3 h (for Aβ42 oligomers) or 24 h (for Aβ42 protofibrils) (Fig. 3b and c). This result indicated that scFv MO6 not only effectively prevented further aggregation of Aβ42 oligomers and protofibrils, but also reversed their formation, i.e., induced their disaggregation, to a certain degree. However, no significant decrease in fluorescence intensity was observed in Aβ42 fibrils incubated with scFv MO6 over 48 h (Fig. 3d). Together, these results indicated that scFv MO6 inhibited Aβ42 aggregation more efficiently than it induced the disaggregation of Aβ42 aggregates.\", \"Figure 3\", \"Figure 4\", \"The effects of scFv MO6 on Aβ42 aggregation were further confirmed by electron microscopy after 24 h of co-incubation of scFv MO6 with different Aβ42 species (Fig. 4). After 24 h of co-incubation with scFv MO6 at 37 °C, Aβ42 monomers and oligomers (Fig. 4d and e) grew remarkable more slowly than in the absence of scFv MO6 (Fig. 4a and c), indicating that scFv MO6 inhibited the assembly of Aβ42 monomer into oligomers, and induced the disaggregation of medium-sized Aβ42 oligomers into much smaller globular units. Amorphous or diffuse state of the incubated Aβ42 protofibrils and Aβ42 fibrils was discernable upon incubation with scFv MO6 (Fig. 4f and h); these amorphous structures might represent large Aβ42-MO6 complexes.\", \"Nevertheless, almost immediately, the co-incubated scFv MO6 bound to the nascent oligomers, and inhibited further aggregation. Furthermore, binding of scFv MO6 induced disaggregation of the oligomers to a certain extent (Fig. 3b).\", \"Together, the results shown in Fig. 3, Fig. 4 demonstrated that scFv MO6 could inhibit the aggregation of Aβ42 and induce the disaggregation of preformed oligomeric Aβ42 aggregates such as Aβ42 oligomers or immature protofibrils in vitro. These results are consistent with the binding specificity of scFv MO6 (Fig. 2).\", \"Consequently, scFv MO6 ameliorated or attenuated Aβ42-mediated cytotoxicity (Fig. 5).\",",
    "Curator Statement": false
  },
  "AMGAB0249": {
    "Interaction ID": "AMGAB0249",
    "Antibody ID": "ABID0195",
    "Antibody name": "HS72",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuropharm.2023.109775",
    "PMID": 37913984.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo, In cellulo,",
    "Experimental method(s)": "ThT - Aggregation kinetics, Immunohistochemistry, ELISA, Western blot, HPLC,",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The synergy of matrine with the catalytic antibody HS72 makes HS72 more effective than HS72 alone in reducing or removing Aβ42 aggregates or plaques and protecting neural cells.\", \"The study's results suggest a natural synergy between Mat-like small molecules and the catalytic anti-oligomeric Aβ42 antibody HS72, enabling more effective reduction or removal of Aβ42 aggregates or plaques than the antibody alone.\", \"According to Fig. 1A, although the overall pattern of change in Aβ42 levels was similar to that in the absence of Mat (Song et al., 2023), with the gradual decrease of the remaining Aβ42 levels in all three groups, the Aβ42 levels in all three groups at the corresponding time points were marginally lower in all three groups, particularly in the Aβ42O and Aβ42F groups, than those in the corresponding groups in the absence of Mat. For example, when HS72 acted in combination with Mat, Aβ42 levels decreased by 4.8%, 12.9%, and 9.6% in the Aβ42M, Aβ42O, and Aβ42F groups, respectively, whereas when HS72 acted alone, they decreased by 4%, 11.2%, and 5.8%, respectively. Clearly, Mat increased HS72's catalytic effectiveness for Aβ42 aggregates. The differences in the remaining Aβ42 levels in the three groups in the presence and absence of Mat are shown in Fig. 1B. The differences in all three groups increased with increasing catalytic duration, especially in the Aβ42F group, indicating that Mat synergized the catalytic effect of HS72 on Aβ42 aggregates, particularly Aβ42F.\", \"Figure 1\", \"In the Aβ42M group (Fig. 1C and D), in the presence of HS72 with Mat, the levels of the HS72−Aβ42 complex (c in Fig. 1C and D) and Aβ42M (including free Aβ42M and Aβ42M−Mat complexes, denoted by Aβ42M*) (f in Fig. 1C) remained constant during incubation from days 1–10 at 37 °C, whereas the levels of small Aβ42O, including free Aβ42O and Aβ42O−Mat complexes (e in Fig. 1C), gradually decreased with increasing catalytic duration.\", \"In contrast, in the Aβ42M incubation system without Mat, the level of the HS72−Aβ42 complex gradually decreased, and the level of Aβ42O gradually increased with increasing catalytic duration (Song et al., 2023). This implied that although Aβ42M tends to aggregate into Aβ42O during incubation at 37 °C, under the synergistic action of Mat, the newly formed Aβ42O were efficiently digested by HS72 and the degradation products (N-terminal and C-terminal Aβ fragments, denoted by NAβ and AβC, respectively, and not recognized by the used anti-Aβ42 primary antibody) were quickly released from the active site of HS72, which inevitably caused the disassembly or release of the remaining Aβ42 chains from the involved Aβ42O units.\", \"In contrast to when HS72 was used alone (gray triangles in Fig. 2A–D), the fluorescence intensity in all four groups significantly decreased in the presence of both HS72 and Mat (black circles). These results demonstrate that HS72 was more effective at blocking and reducing Aβ42 aggregation or assembly in the four groups when Mat was present, particularly in Aβ42O and Aβ42F groups where the degree of Aβ42 aggregation remained lower than that in their initial stage within this 48 h. Apparently, Mat's intervention in the integrated conformation of Aβ42 aggregates by inserting Aβ42 aggregate units as previously reported (Yang et al., 2020) considerably aided HS72's induction of Aβ42 aggregate disassembly or breakdown while aiding in Aβ42 aggregate degradation. This demonstrated that the degradation of the Aβ42 aggregate was accompanied by their disassembly or breakdown.\",  \"Figure 2\", \"The presence of Mat promotes HS72-induced clearance of Aβ plaques in the brain of AD model mice\", \"Figure 5\", \"In the HS72 and HS72 with Mat groups (c and d in Fig. 5B), the level of hippocampus Aβ deposits/plaques decreased, and the spots were lighter in color and smaller in size. In contrast, the positive control group showed hippocampal regions with darker and larger Aβ spots (a in Fig. 5B, arrows). Furthermore, the HS72 with Mat group exhibited a reduced level of Aβ deposits/plaques than the HS72 group (c and d in Fig. 5B).\", \"HS72 and HS72 with Mat reduced a load of Aβ deposits and plaques in the hippocampal region by 27.4% and 34.3%, respectively, compared to the positive control (100%) (**p < 0.01, ***p < 0.001). Further, there was a significant difference in the load of Aβ42 deposits and plaques between the HS72 and HS72 with Mat groups (#p < 0.05) (Fig. 5C). However, there was no significant difference in the number of Aβ42 deposits and plaques between them (Fig. 5D), although there was a significant difference in the number of Aβ42 deposit/plaque spots between HS72 or HS72 with Mat group and the positive control group (**p < 0.01) (Fig. 5D). These results showed that after 7 days of peripheral administration, scFv HS72 combined with Mat was as effective as scFv HS72 alone in reducing the number of Aβ42 deposit/plaque spots in the brains of AD mice, and was also marginally superior to scFv HS72 alone in reducing the area or quantity of positive Aβ42 deposits/plaques. \",  \"In addition, the results of Fig. 5 showed that the synergistic effect of Mat on scFv HS72 can increase the efficacy of HS72 in reducing the level of large Aβ42 aggregates, such as Aβ42F, besides enhancing the efficacy of HS72 in removing Aβ42O or small aggregates, which is consistent with the results shown in Fig. 1B.\", \"Therefore, the presence of Mat increased the efficiency of HS72 in degrading Aβ42 aggregates and altered the nature of the degradation products. \", \"In conclusion, Mat synergistically enhanced the ability of HS72, an catalytic anti-oligomeric Aβ42 scFv antibody, to degrade Aβ42 aggregates and protect neural cells by increasing HS72's turnover number (or molecular activity). The combination of scFv HS72 with Mat reduced or removed Aβ42 aggregates or plaques more effectively than HS72 alone, which will increase scFv HS72's potency in AD immunotherapy.\"",
    "Curator Statement": "Authors refer to monomers as Aβ42M, oligomers as Aβ42O , protofibrils as Aβ42P and fibrils as Aβ42F."
  },
  "AMGAB0250": {
    "Interaction ID": "AMGAB0250",
    "Antibody ID": "ABID0310",
    "Antibody name": "B06 IgG",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuroscience.2021.03.006",
    "PMID": 33958140.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 6\", \"However, SPR measurements revealed insufficient binding affinity of each recombinant antibody B06, B07 and C06. Further assays confirmed that the observed low affinity to Aβ seemed to be responsible for the low inhibited fibrillation and the low microglial uptake of BV-2 cells in vitro (Fig. 6). In fibrillation assay, we found significant differences between the mentioned groups via Kruskal-Wallis test. The post-hoc pairwise Dunn’s test yielded only one significant effect, namely between B07 scFv-Fc and Aβ. No other pairwise differences were found.\",",
    "Curator Statement": false
  },
  "AMGAB0251": {
    "Interaction ID": "AMGAB0251",
    "Antibody ID": "ABID0311",
    "Antibody name": "B07 IgG",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuroscience.2021.03.006",
    "PMID": 33958140.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 6\", \"However, SPR measurements revealed insufficient binding affinity of each recombinant antibody B06, B07 and C06. Further assays confirmed that the observed low affinity to Aβ seemed to be responsible for the low inhibited fibrillation and the low microglial uptake of BV-2 cells in vitro (Fig. 6). In fibrillation assay, we found significant differences between the mentioned groups via Kruskal-Wallis test. The post-hoc pairwise Dunn’s test yielded only one significant effect, namely between B07 scFv-Fc and Aβ. No other pairwise differences were found.\",",
    "Curator Statement": false
  },
  "AMGAB0252": {
    "Interaction ID": "AMGAB0252",
    "Antibody ID": "ABID0312",
    "Antibody name": "C06 IgG",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuroscience.2021.03.006",
    "PMID": 33958140.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 6\", \"However, SPR measurements revealed insufficient binding affinity of each recombinant antibody B06, B07 and C06. Further assays confirmed that the observed low affinity to Aβ seemed to be responsible for the low inhibited fibrillation and the low microglial uptake of BV-2 cells in vitro (Fig. 6). In fibrillation assay, we found significant differences between the mentioned groups via Kruskal-Wallis test. The post-hoc pairwise Dunn’s test yielded only one significant effect, namely between B07 scFv-Fc and Aβ. No other pairwise differences were found.\",",
    "Curator Statement": false
  },
  "AMGAB0253": {
    "Interaction ID": "AMGAB0253",
    "Antibody ID": "ABID0313",
    "Antibody name": "B07 scFv--Fc",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.neuroscience.2021.03.006",
    "PMID": 33958140.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Monomers, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The multimeric scFv-Fc antibody exhibited thereby strong impact on amyloid-β clearance and inhibition of oligomerization.\", \"Multimerization improved Aβ-toxicity neutralization and clearance significantly in vitro.\", \"Figure 5\",  \"Figure 6\", \"However, SPR measurements revealed insufficient binding affinity of each recombinant antibody B06, B07 and C06. Further assays confirmed that the observed low affinity to Aβ seemed to be responsible for the low inhibited fibrillation and the low microglial uptake of BV-2 cells in vitro (Fig. 6). In fibrillation assay, we found significant differences between the mentioned groups via Kruskal-Wallis test. The post-hoc pairwise Dunn’s test yielded only one significant effect, namely between B07 scFv-Fc and Aβ. No other pairwise differences were found.\",",
    "Curator Statement": false
  },
  "AMGAB0254": {
    "Interaction ID": "AMGAB0254",
    "Antibody ID": "ABID0012.5",
    "Antibody name": "13C3",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.omtm.2020.08.014",
    "PMID": 33005703.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry,",
    "Amyloid species identified": "Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"No significant difference could be evidenced between the three antibodies, suggesting that TBTI3a and TBTI6a antibodies used at a five times lower dose (15 nmol/kg) are as effective at decreasing Aβ levels in the cortex as the 13C3a antibody at a dose of 70 nmol/kg. A further analysis of each total, insoluble and soluble fractions for Aβ38, 40, and 42, was also performed on the cortical samples from TBTI6a-treated mice in comparison with 13C3a, confirming the effect in all three fractions (data not shown).\", \"Using quantitative image analysis of cortical and hippocampal Aβ peptide immunolabeling, significant preventive activities of all three administered antibodies (ranging from −28% to −63%) against total positive staining surface or total positive deposit number were also demonstrated (Figure 7). In the cortex, TBTI6a had a similar efficacy as 13C3a, while TBTI3a appeared less effective, but there was no statistically significant difference between TBTI3a and TBTI6a (Figures 7A and 7B).\", \"Figure 7\", \" The results in the hippocampus confirmed the trends seen with biochemistry, with only TBTI6a and 13C3a showing marked similar significant protective activity, ranging from −51% to −63%, against Aβ deposition (total surface and deposit number) (Figures 7C and 7D).\", \"Consistent with the increase in brain exposure, both TBTI3a and TBTI6a significantly reduced the cortical amount of Aβ and cortical Aβ deposition to the same extent as the higher dose of 13C3a. To our knowledge, this is the first report of anti-TfR-anti-Aβ antibodies reducing both Aβ plaques and the cerebral pool of Aβ peptides at a lower dose and at the same administration frequency as the control monospecific antibody. \", \"TBTI6a reduced cortical and hippocampal Aβ deposition to the same level as 13C3a. Even though not statistically significant, TBTI3a was less effective than TBTI6a in reducing the cortical Aβ deposition, while no effect could be seen in the hippocampus. The reduced effect of TBTI3a compared to TBTI6a might be due to its higher clearance rate, especially in plasma. With a repeated weekly low-dose regimen, the accumulation factor of TBTI3a in APPSL mice is therefore smaller than for TBTI6a, as shown by their plasma exposures of 0.32 and 49.5 nM, respectively, 1 week after the last administration. However, the terminal brain exposures, 0.28 and 0.37 nM, respectively, did not confirm such accumulation.\",\" The best candidates were selected for a chronic study in an amyloid precursor protein (APP) Tg mouse model showing efficacy at reducing brain amyloid load at a lower dose than the corresponding monospecific antibody.\", \"Tetravalent bispecific tandem immunoglobulin Gs (IgGs) (TBTIs) containing two paratopes for both transferrin receptor (TfR) and amyloid-beta (Aβ) peptide were constructed and shown to display higher brain penetration than the parent Aβ antibody, parenchymal target engagement, and efficacy at reducing brain amyloid load in a chronic study in an amyloid precursor protein (APP) transgenic (Tg) mouse model.\",",
    "Curator Statement": false
  },
  "AMGAB0255": {
    "Interaction ID": "AMGAB0255",
    "Antibody ID": "ABID0330",
    "Antibody name": "TBTI3",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.omtm.2020.08.014",
    "PMID": 33005703.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry,",
    "Amyloid species identified": "Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"No significant difference could be evidenced between the three antibodies, suggesting that TBTI3a and TBTI6a antibodies used at a five times lower dose (15 nmol/kg) are as effective at decreasing Aβ levels in the cortex as the 13C3a antibody at a dose of 70 nmol/kg. A further analysis of each total, insoluble and soluble fractions for Aβ38, 40, and 42, was also performed on the cortical samples from TBTI6a-treated mice in comparison with 13C3a, confirming the effect in all three fractions (data not shown).\", \"Figure 7\", \"Using quantitative image analysis of cortical and hippocampal Aβ peptide immunolabeling, significant preventive activities of all three administered antibodies (ranging from −28% to −63%) against total positive staining surface or total positive deposit number were also demonstrated (Figure 7). In the cortex, TBTI6a had a similar efficacy as 13C3a, while TBTI3a appeared less effective, but there was no statistically significant difference between TBTI3a and TBTI6a (Figures 7A and 7B).\", \" The results in the hippocampus confirmed the trends seen with biochemistry, with only TBTI6a and 13C3a showing marked similar significant protective activity, ranging from −51% to −63%, against Aβ deposition (total surface and deposit number) (Figures 7C and 7D).\",\"Consistent with the increase in brain exposure, both TBTI3a and TBTI6a significantly reduced the cortical amount of Aβ and cortical Aβ deposition to the same extent as the higher dose of 13C3a. To our knowledge, this is the first report of anti-TfR-anti-Aβ antibodies reducing both Aβ plaques and the cerebral pool of Aβ peptides at a lower dose and at the same administration frequency as the control monospecific antibody. \", \"TBTI6a reduced cortical and hippocampal Aβ deposition to the same level as 13C3a. Even though not statistically significant, TBTI3a was less effective than TBTI6a in reducing the cortical Aβ deposition, while no effect could be seen in the hippocampus. The reduced effect of TBTI3a compared to TBTI6a might be due to its higher clearance rate, especially in plasma. With a repeated weekly low-dose regimen, the accumulation factor of TBTI3a in APPSL mice is therefore smaller than for TBTI6a, as shown by their plasma exposures of 0.32 and 49.5 nM, respectively, 1 week after the last administration. However, the terminal brain exposures, 0.28 and 0.37 nM, respectively, did not confirm such accumulation.\", \" The best candidates were selected for a chronic study in an amyloid precursor protein (APP) Tg mouse model showing efficacy at reducing brain amyloid load at a lower dose than the corresponding monospecific antibody.\", \"Tetravalent bispecific tandem immunoglobulin Gs (IgGs) (TBTIs) containing two paratopes for both transferrin receptor (TfR) and amyloid-beta (Aβ) peptide were constructed and shown to display higher brain penetration than the parent Aβ antibody, parenchymal target engagement, and efficacy at reducing brain amyloid load in a chronic study in an amyloid precursor protein (APP) transgenic (Tg) mouse model.\",",
    "Curator Statement": false
  },
  "AMGAB0256": {
    "Interaction ID": "AMGAB0256",
    "Antibody ID": "ABID0331",
    "Antibody name": "TBTI6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.omtm.2020.08.014",
    "PMID": 33005703.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry,",
    "Amyloid species identified": "Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"No significant difference could be evidenced between the three antibodies, suggesting that TBTI3a and TBTI6a antibodies used at a five times lower dose (15 nmol/kg) are as effective at decreasing Aβ levels in the cortex as the 13C3a antibody at a dose of 70 nmol/kg. A further analysis of each total, insoluble and soluble fractions for Aβ38, 40, and 42, was also performed on the cortical samples from TBTI6a-treated mice in comparison with 13C3a, confirming the effect in all three fractions (data not shown).\", \"Figure 7\", \"Using quantitative image analysis of cortical and hippocampal Aβ peptide immunolabeling, significant preventive activities of all three administered antibodies (ranging from −28% to −63%) against total positive staining surface or total positive deposit number were also demonstrated (Figure 7). In the cortex, TBTI6a had a similar efficacy as 13C3a, while TBTI3a appeared less effective, but there was no statistically significant difference between TBTI3a and TBTI6a (Figures 7A and 7B).\", \" The results in the hippocampus confirmed the trends seen with biochemistry, with only TBTI6a and 13C3a showing marked similar significant protective activity, ranging from −51% to −63%, against Aβ deposition (total surface and deposit number) (Figures 7C and 7D).\",\"Consistent with the increase in brain exposure, both TBTI3a and TBTI6a significantly reduced the cortical amount of Aβ and cortical Aβ deposition to the same extent as the higher dose of 13C3a. To our knowledge, this is the first report of anti-TfR-anti-Aβ antibodies reducing both Aβ plaques and the cerebral pool of Aβ peptides at a lower dose and at the same administration frequency as the control monospecific antibody. \", \"TBTI6a reduced cortical and hippocampal Aβ deposition to the same level as 13C3a. Even though not statistically significant, TBTI3a was less effective than TBTI6a in reducing the cortical Aβ deposition, while no effect could be seen in the hippocampus. The reduced effect of TBTI3a compared to TBTI6a might be due to its higher clearance rate, especially in plasma. With a repeated weekly low-dose regimen, the accumulation factor of TBTI3a in APPSL mice is therefore smaller than for TBTI6a, as shown by their plasma exposures of 0.32 and 49.5 nM, respectively, 1 week after the last administration. However, the terminal brain exposures, 0.28 and 0.37 nM, respectively, did not confirm such accumulation.\", \" The best candidates were selected for a chronic study in an amyloid precursor protein (APP) Tg mouse model showing efficacy at reducing brain amyloid load at a lower dose than the corresponding monospecific antibody.\", \"Tetravalent bispecific tandem immunoglobulin Gs (IgGs) (TBTIs) containing two paratopes for both transferrin receptor (TfR) and amyloid-beta (Aβ) peptide were constructed and shown to display higher brain penetration than the parent Aβ antibody, parenchymal target engagement, and efficacy at reducing brain amyloid load in a chronic study in an amyloid precursor protein (APP) transgenic (Tg) mouse model.\",",
    "Curator Statement": false
  },
  "AMGAB0257": {
    "Interaction ID": "AMGAB0257",
    "Antibody ID": "ABID0314",
    "Antibody name": "scFv9",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.omtm.2023.101146",
    "PMID": 38027063.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA, biochemical extraction",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 7\", \"As expected, mice expressing scFv9 had significantly less RIPA-soluble Aβ42, SDS-soluble Aβ40 and Aβ42, and FA-extracted Aβ40 and Aβ42 compared to controls (Figures 7B–7F).\",",
    "Curator Statement": false
  },
  "AMGAB0258": {
    "Interaction ID": "AMGAB0258",
    "Antibody ID": "ABID0314",
    "Antibody name": "scFv9",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.omtm.2023.101146",
    "PMID": 38027063.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA, biochemical extraction",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 6\",\"Figure 7\", \"Concomitantly, with our previous findings,11 scFv9 significantly reduced amyloid deposition; however, fusion of CD to scFv9 did not augment the ability of scFv9 to prevent amyloid aggregation because there was no difference in the number of amyloid plaques between scFv9 and scFv9-CD (Figures 6A and 6B).\", \"As expected, mice expressing scFv9 had significantly less RIPA-soluble Aβ42, SDS-soluble Aβ40 and Aβ42, and FA-extracted Aβ40 and Aβ42 compared to controls (Figures 7B–7F).\", \"Proof of concept studies using rAAV vectors to express three different anti-Aβ scFvs either alone or fused to the CD as modulators of amyloid deposition in TgCRND8 mice demonstrated modest effects on the efficacy of a modest affinity anti-Aβ scFv (scFv12), but did not affect the efficacy of a high-affinity anti-Aβ scFv (scFv9).\", \"Another lower-affinity anti-Aβ scFv12 showed slightly improved efficacy in terms of amyloid reduction when expressed as a CD fusion, but neither the parent scFv nor the CD fusion were as effective as scFv9.\",",
    "Curator Statement": false
  },
  "AMGAB0259": {
    "Interaction ID": "AMGAB0259",
    "Antibody ID": "ABID0315",
    "Antibody name": "scFv9-CD",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.omtm.2023.101146",
    "PMID": 38027063.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA, biochemical extraction",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 7\", \"Mice expressing scFv9-CD also had significantly lower levels of SDS-soluble Aβ40 and Aβ42 and FA-soluble Aβ40 and Aβ42 compared to controls (Figures 7B, 7C, 7E, and 7F).\", \"The resulting scFv-CD improved binding and prevention of Aβ aggregation.\",",
    "Curator Statement": false
  },
  "AMGAB0260": {
    "Interaction ID": "AMGAB0260",
    "Antibody ID": "ABID0315",
    "Antibody name": "scFv9-CD",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.omtm.2023.101146",
    "PMID": 38027063.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA, biochemical extraction",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 6\",\"Figure 7\", \"Concomitantly, with our previous findings,11 scFv9 significantly reduced amyloid deposition; however, fusion of CD to scFv9 did not augment the ability of scFv9 to prevent amyloid aggregation because there was no difference in the number of amyloid plaques between scFv9 and scFv9-CD (Figures 6A and 6B).\", \"Mice expressing scFv9-CD also had significantly lower levels of SDS-soluble Aβ40 and Aβ42 and FA-soluble Aβ40 and Aβ42 compared to controls (Figures 7B, 7C, 7E, and 7F).\", \"Proof of concept studies using rAAV vectors to express three different anti-Aβ scFvs either alone or fused to the CD as modulators of amyloid deposition in TgCRND8 mice demonstrated modest effects on the efficacy of a modest affinity anti-Aβ scFv (scFv12), but did not affect the efficacy of a high-affinity anti-Aβ scFv (scFv9).\", \"The resulting scFv-CD improved binding and prevention of Aβ aggregation.\",",
    "Curator Statement": false
  },
  "AMGAB0261": {
    "Interaction ID": "AMGAB0261",
    "Antibody ID": "ABID0316",
    "Antibody name": "scFvB11",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.omtm.2023.101146",
    "PMID": 38027063.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ELISA, biochemical extraction",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 7\",",
    "Curator Statement": false
  },
  "AMGAB0262": {
    "Interaction ID": "AMGAB0262",
    "Antibody ID": "ABID0316",
    "Antibody name": "scFvB11",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.omtm.2023.101146",
    "PMID": 38027063.0,
    "Impact of the antibody on amyloid formation": "No effect, Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), ELISA, biochemical extraction",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 6\", \"Figure 7\", \"CD fusion to scFvB11 reduced amyloid plaques by 17.6% compared to scFvB11 alone; however, scFvB11 with or without CD fusion did not significantly affect the plaque count in TgCRND8 mice as compared to controls.\", \"A fibril-selective scFvB11 derived from the aducanumab sequence had limited impact on amyloid loads in this study.\",",
    "Curator Statement": false
  },
  "AMGAB0263": {
    "Interaction ID": "AMGAB0263",
    "Antibody ID": "ABID0317",
    "Antibody name": "scFvB11-CD",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.omtm.2023.101146",
    "PMID": 38027063.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ELISA, biochemical extraction",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 7\",\"The resulting scFv-CD improved binding and prevention of Aβ aggregation.\",",
    "Curator Statement": false
  },
  "AMGAB0264": {
    "Interaction ID": "AMGAB0264",
    "Antibody ID": "ABID0317",
    "Antibody name": "scFvB11-CD",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.omtm.2023.101146",
    "PMID": 38027063.0,
    "Impact of the antibody on amyloid formation": "No effect, Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA, biochemical extraction",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 6\", \"Figure 7\", \"CD fusion to scFvB11 reduced amyloid plaques by 17.6% compared to scFvB11 alone; however, scFvB11 with or without CD fusion did not significantly affect the plaque count in TgCRND8 mice as compared to controls.\", \"A fibril-selective scFvB11 derived from the aducanumab sequence had limited impact on amyloid loads in this study.\", \"The resulting scFv-CD improved binding and prevention of Aβ aggregation.\",",
    "Curator Statement": false
  },
  "AMGAB0265": {
    "Interaction ID": "AMGAB0265",
    "Antibody ID": "ABID0318",
    "Antibody name": "scFv12",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.omtm.2023.101146",
    "PMID": 38027063.0,
    "Impact of the antibody on amyloid formation": "No effect, Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ELISA, biochemical extraction",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"CD fusion to scFv12 reduced the levels of Aβ40 in FA fraction (32.4% as compared to control) (Figure 7C), whereas only a trend to the reduction of SDS-soluble Aβ40 (18.3%) and Aβ42 (12.3%) levels and FA-extracted Aβ42 levels (13.2%) was achieved with scFv12 alone.\", \"Figure 7\",",
    "Curator Statement": false
  },
  "AMGAB0266": {
    "Interaction ID": "AMGAB0266",
    "Antibody ID": "ABID0318",
    "Antibody name": "scFv12",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.omtm.2023.101146",
    "PMID": 38027063.0,
    "Impact of the antibody on amyloid formation": "No effect,  Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), ELISA, biochemical extraction",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"It is interesting to note that the fusion of CD to scFv12 improved the efficacy of scFv12 and further reduced the number of amyloid plaques by 26.2% compared to scFv12 alone.\", \"CD fusion to scFv12 reduced the levels of Aβ40 in FA fraction (32.4% as compared to control) (Figure 7C), whereas only a trend to the reduction of SDS-soluble Aβ40 (18.3%) and Aβ42 (12.3%) levels and FA-extracted Aβ42 levels (13.2%) was achieved with scFv12 alone.\", \"Figure 7\", \"Figure 6\", \"Proof of concept studies using rAAV vectors to express three different anti-Aβ scFvs either alone or fused to the CD as modulators of amyloid deposition in TgCRND8 mice demonstrated modest effects on the efficacy of a modest affinity anti-Aβ scFv (scFv12), but did not affect the efficacy of a high-affinity anti-Aβ scFv (scFv9).\", \"Another lower-affinity anti-Aβ scFv12 showed slightly improved efficacy in terms of amyloid reduction when expressed as a CD fusion, but neither the parent scFv nor the CD fusion were as effective as scFv9.\",",
    "Curator Statement": false
  },
  "AMGAB0267": {
    "Interaction ID": "AMGAB0267",
    "Antibody ID": "ABID0319",
    "Antibody name": "scFv12-CD",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.omtm.2023.101146",
    "PMID": 38027063.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ELISA, Biochemical extraction",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Mice expressing scFv12-CD had significant reductions in SDS-soluble Aβ40 and FA-extracted Aβ40 and Aβ42 compared to controls (Figures 7B, 7C, and 7F). CD fusion to scFv12 reduced the levels of Aβ40 in FA fraction (32.4% as compared to control) (Figure 7C), whereas only a trend to the reduction of SDS-soluble Aβ40 (18.3%) and Aβ42 (12.3%) levels and FA-extracted Aβ42 levels (13.2%) was achieved with scFv12 alone.\", \"Figure 7\", \"The resulting scFv-CD improved binding and prevention of Aβ aggregation.\",",
    "Curator Statement": false
  },
  "AMGAB0268": {
    "Interaction ID": "AMGAB0268",
    "Antibody ID": "ABID0319",
    "Antibody name": "scFv12-CD",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.omtm.2023.101146",
    "PMID": 38027063.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), ELISA, biochemical extraction",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"It is interesting to note that the fusion of CD to scFv12 improved the efficacy of scFv12 and further reduced the number of amyloid plaques by 26.2% compared to scFv12 alone. Also, mice expressing scFv12-CD had significantly fewer plaques than controls (Figure 6B). Mice expressing scFv12-CD had significant reductions in SDS-soluble Aβ40 and FA-extracted Aβ40 and Aβ42 compared to controls (Figures 7B, 7C, and 7F). CD fusion to scFv12 reduced the levels of Aβ40 in FA fraction (32.4% as compared to control) (Figure 7C), whereas only a trend to the reduction of SDS-soluble Aβ40 (18.3%) and Aβ42 (12.3%) levels and FA-extracted Aβ42 levels (13.2%) was achieved with scFv12 alone.\", \"Figure 7\", \"Figure 6\", \"Proof of concept studies using rAAV vectors to express three different anti-Aβ scFvs either alone or fused to the CD as modulators of amyloid deposition in TgCRND8 mice demonstrated modest effects on the efficacy of a modest affinity anti-Aβ scFv (scFv12), but did not affect the efficacy of a high-affinity anti-Aβ scFv (scFv9).\", \"Another lower-affinity anti-Aβ scFv12 showed slightly improved efficacy in terms of amyloid reduction when expressed as a CD fusion, but neither the parent scFv nor the CD fusion were as effective as scFv9.\", \"The resulting scFv-CD improved binding and prevention of Aβ aggregation.\",",
    "Curator Statement": false
  },
  "AMGAB0269": {
    "Interaction ID": "AMGAB0269",
    "Antibody ID": "ABID0169",
    "Antibody name": "NU1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.taap.2009.07.018",
    "PMID": 19631677.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"These changes have been found to facilitate the clearance of oAβs from synapses using oligomer-specific antibodies.\", \"Figure 8\", \"This may provide a way to enhance immunotherapy, as ADDLs will be more easily detected and removed by the antibodies.\", \"The enhanced immunoreactivity and removal of ADDLs by the oligomer-specific antibody NU1 imply that OC could be a potential enhancer of AD immunotherapy.\",",
    "Curator Statement": false
  },
  "AMGAB0270": {
    "Interaction ID": "AMGAB0270",
    "Antibody ID": "ABID0021",
    "Antibody name": "Sabirnetug",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/j.tjpad.2024.100005",
    "PMID": 39800458.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Over three months, approximately 25% and 20% reduction in amyloid plaques, respectively, were observed in participants receiving three infusions of sabirnetug 60 mg/kg every four weeks and 25 mg/kg every two weeks.\", \"Pooled values for participants in cohorts 1, 2, 3, and 4 who received placebo were 48.5 Centiloids at baseline and 49.5 Centiloids at day 42 (change from baseline, +1.0 Centiloids, +2.2%). Participants in cohorts 1, 2, 3, and 4 who received sabirnetug had mean baseline Centiloid values of 65.3, 70.0, 63.7, and 60.2, respectively, and mean values at day 42 of 62.7 Centiloids (mean change from baseline, −2.6 Centiloids, −4.0%), 84.9 Centiloids (mean change, +14.9 Centiloids, +21.4%), 62.9 (mean change, −0.8 Centiloids, −1.3%), and 50.3 (mean change, −9.9 Centiloids, −16.5%), respectively.\",\"The pooled value for participants in cohorts 5 and 6 who received placebo was 37.3 Centiloids at baseline. At day 70, mean value for cohort 5 was 44.6 Centiloids (change from baseline, 7.3 Centiloids, 19.5%). At day 63, mean value for cohort 6 was 28.6 Centiloids (mean change, −8.7 Centiloids, −23.2%). For sabirnetug-treated participants in cohort 5, mean baseline value was 55.8 Centiloids and day 70 value was 59.2 Centiloids (mean change from baseline, +3.4 Centiloids, +6.1%, p=0.746). For sabirnetug-treated participants in cohort 6, baseline value was 71.9 Centiloids and day 63 value was 53.7 Centiloids (mean change, −18.2 Centiloids, −23.2%; p=0.01). For sabirnetug-treated participants in cohort 7, baseline value was 66.8 Centiloids and day 70 value was 53.0 Centiloids (mean change, −18.3 Centiloids, −25.6%; p=0.01).\", \"However, plaque reduction was observed over three months treatment in the MAD portion of the study. This represented approximate reductions of 25% and 20% Centiloids in the 60 mg/kg Q4W and 25 mg/kg Q2W cohorts, respectively.\", \"However, the data indicate central target engagement and amyloid plaque reduction consistent with an effect of sabirnetug on the AD pathologic process after only three administrations.\", \"Although the decrease in amyloid plaque was not anticipated, these preliminary findings suggest sabirnetug may facilitate simultaneous clearance of multiple forms of Aβ.\",",
    "Curator Statement": false
  },
  "AMGAB0271": {
    "Interaction ID": "AMGAB0271",
    "Antibody ID": "ABID0023",
    "Antibody name": "Ponezumab",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1016/j.trci.2017.05.003",
    "PMID": 29067345.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Plasma Aβ increased dose dependently with ponezumab, but CSF biomarkers, brain amyloid burden, cognition, and function were not affected.\", \"Minimal changes from baseline to month 13 were observed in brain amyloid burden in cohort M, and there were no discernible differences between treatment arms in any region or for the overall brain (Fig. 2). For the overall brain, the LS means and 90% CIs for percent change from baseline in SUVR were −2.48 (−6.47, 1.68) for ponezumab and −1.07 (−6.76, 4.97) for placebo. The between-group difference (ponezumab vs. placebo) in LS means was −1.43 and the 90% CI overlapped zero (−8.35, 6.02; P = .734).\", \"No differences between ponezumab and placebo in brain amyloid burden were discernible by PIB for any individual brain region or overall. \", \"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0272": {
    "Interaction ID": "AMGAB0272",
    "Antibody ID": "ABID0028.5",
    "Antibody name": "C10.2",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.trci.2018.09.005",
    "PMID": 30386817.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"C10.2 significantly reduced tau seeding of P301L human tau in HEK293 cells, murine cortical neurons, and mice.\", \"C10.2 treatment reduced the seeding by 74% (P < .01) and D1.2 treatment reduced the seeding by 66% (P < .05).\", \"Furthermore, we explored the mechanism of inhibition by C10.2 in rTg4510 mice seeded with AD crude extracts by applying three different dosing paradigms (Fig. 6C). We compared dosing throughout (1) the entire seeding period (14 weeks, full), (2) start 4 weeks after seeding (post), and (3) C10.2 treatment only for 3 weeks, starting 2 weeks before injection (pre). Prevention of seeding and development of pathology was only observed when there was antibody (C10.2) exposure at the time of seed injection (full and pre) (Fig. 6D). Dosing of C10.2 4 weeks after seeding with AD brain material (post) had no effect. These data suggest that the antibody interacts with extracellular seeds and thereby prevents seeding and further development of tau pathology.\", \"Figure 6\", \"pS396-tau antibodies prevent in vivo tau seeding\", \"Our studies demonstrate that C10.2 and D1.2 antibodies effectively prevent the development of the tau pathology induced by injection of crude rTg4510 or AD brain extracts into the hippocampus.\", \"This is supported by the observation that prevention is only possible when there is C10.2 exposure at the time of seed injection and not when the antibody is dosed after the tau seeds have been taken up.\",",
    "Curator Statement": false
  },
  "AMGAB0273": {
    "Interaction ID": "AMGAB0273",
    "Antibody ID": "ABID0028.5",
    "Antibody name": "C10.2",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.trci.2018.09.005",
    "PMID": 30386817.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Furthermore, we explored the mechanism of inhibition by C10.2 in rTg4510 mice seeded with AD crude extracts by applying three different dosing paradigms (Fig. 6C). We compared dosing throughout (1) the entire seeding period (14 weeks, full), (2) start 4 weeks after seeding (post), and (3) C10.2 treatment only for 3 weeks, starting 2 weeks before injection (pre). Prevention of seeding and development of pathology was only observed when there was antibody (C10.2) exposure at the time of seed injection (full and pre) (Fig. 6D). Dosing of C10.2 4 weeks after seeding with AD brain material (post) had no effect. These data suggest that the antibody interacts with extracellular seeds and thereby prevents seeding and further development of tau pathology.\", \"Figure 6\", \" Thus, the effect on pathology observed in vivo may reflect inability of antibody-decorated brain extracts to induce seeding and aggregation in the host cell. This is supported by the observation that prevention is only possible when there is C10.2 exposure at the time of seed injection and not when the antibody is dosed after the tau seeds have been taken up.\",",
    "Curator Statement": "C10.2 showed prevention of tau aggregation, but not significant clearance of preformed aggregates."
  },
  "AMGAB0274": {
    "Interaction ID": "AMGAB0274",
    "Antibody ID": "ABID0461",
    "Antibody name": "D1.2",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1016/j.trci.2018.09.005",
    "PMID": 30386817.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"C10.2 treatment reduced the seeding by 74% (P < .01) and D1.2 treatment reduced the seeding by 66% (P < .05).\", \"Figure 6\", \"pS396-tau antibodies prevent in vivo tau seeding\", \"Our studies demonstrate that C10.2 and D1.2 antibodies effectively prevent the development of the tau pathology induced by injection of crude rTg4510 or AD brain extracts into the hippocampus.\", \"C10.2 potently prevents tau seeding in cellular and in vivo assays.\",",
    "Curator Statement": false
  },
  "AMGAB0275": {
    "Interaction ID": "AMGAB0275",
    "Antibody ID": "ABID0007",
    "Antibody name": "Bapineuzumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1016/S1474-4422(10)70043-0",
    "PMID": 20189881.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Estimated mean (11)C-PiB retention ratio change from baseline to week 78 was -0.09 (95% CI -0.16 to -0.02; p=0.014) in the bapineuzumab group and 0.15 (95% CI 0.02 to 0.28; p=0.022) in the placebo group. Estimated mean difference in (11)C-PiB retention ratio change from baseline to week 78 between the bapineuzumab group and the placebo group was -0.24 (95% CI -0.39 to -0.09; p=0.003). Differences between the bapineuzumab group and the placebo group in the individual regions of interest were similar to the overall mean difference.\", \"Treatment with bapineuzumab for 78 weeks reduced cortical (11)C-PiB retention compared with both baseline and placebo.\", \"Figure 4\", \"Estimated mean ¹¹C-PiB retention ratio decreased by 0·09 in the bapineuzumab group (95% CI –0·16 to –0·02; p=0·014) and increased by 0·15 in the placebo group (95% CI 0·02 to 0·28; p=0·022) from baseline to week 78 (estimated difference –0·24 [95% CI –0·39 to –0·09], p=0·003; table 2). The estimated treatment difference between the bapineuzumab group and the placebo group increased over time (p=0·06 for treatment-by-visit interaction; figure 2).\", \"Figure 2\", \"Across the six regions of interest, changes from baseline to week 78 showed reductions in ¹¹C-PiB retention ratio in the bapineuzumab group and increases in the placebo group (table 2). The difference in the mean ¹¹C-PiB retention ratio between the bapineuzumab group and the placebo group was −0·24 for the 0·5mg/kg dose group (p=0·009), −0·18 for the 1·0 mg/kg dose group (p=0·051), and −0·29 for the 2·0 mg/kg dose group (p=0·003).\", \"Table 2\", \"Figure 3 shows ¹¹C-PiB PET retention for individual patients by treatment group at baseline and at their last available visit, as well as the change from baseline to last available visit. Figure 4 shows ¹¹C-PiB scans for individual patients before and after 78 weeks of treatment with bapineuzumab or placebo.\", \"Figure 3\", \"The estimated mean ¹¹C-PiB treatment difference between the bapineuzumab group and placebo group was –0·25 (95% CI –0·47 to –0·03) after adjusting for baseline neuropsychological test battery score, clinical dementia rating sum of boxes score, and mean ¹¹C-PiB retention (p=0·025; table 3). The mean ¹¹C-PiB change from baseline to week 78 in the bapineuzumab group was –0·08 for nine patients with the apolipoprotein E (APOE)ε4 allele and –0·10 for six patients without.\", \"There was a significant difference in change from baseline in the ¹¹C-PiB PET mean retention from six targeted regions of interest in patients in the bapineuzumab group compared with those in the placebo group. A reduction in ¹¹C-PiB retention relative to baseline was noted for the bapineuzumab group, while an increase was observed in the placebo group.\", \"The difference in ¹¹C-PiB retention between the bapineuzumab and placebo groups was similar for each of the three doses tested, and the treatment difference increased over time.\", \"The –0·09 ratio units for bapineuzumab over 78 weeks represents an 8·5% decline from the baseline value of 2·06, whereas the 0·15 ratio units for placebo represents a 16·9% increase over the baseline value of 1·89. By use of this percentage approach, one can estimate that bapineuzumab treatment was associated with an approximate 25% reduction in cortical fibrillar amyloid βover 78 weeks compared with placebo.\", \"After adjustment for imbalances in baseline ¹¹C-PiB PET retention and clinical scores, the difference in ¹¹C-PiB PET retention between the bapineuzumab group and the placebo group remained, whereas no differences were noted on the clinical or other biomarker outcomes.\", \"Table 3\",",
    "Curator Statement": false
  },
  "AMGAB0276": {
    "Interaction ID": "AMGAB0276",
    "Antibody ID": "ABID0262",
    "Antibody name": "αSP1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/acs.jmedchem.3c02408",
    "PMID": 38842931.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Finally, to assess the specificity of αSP1 for α-syn, the ThT assays were performed against another target known to form amyloid, the 42-residue variant of Aβ (Aβ42)50 at a 1:10 αSP1:Aβ42 molar ratio (the maximum molar ratio tested for α-syn) (Figure 5A). The results showed no inhibitory effect of αSP1 on the in vitro aggregation of Aβ42, confirming that αSP1 inhibits the amyloid formation of α-syn in a specific manner. \". \"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0277": {
    "Interaction ID": "AMGAB0277",
    "Antibody ID": "ABID0262",
    "Antibody name": "αSP1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1021/acs.jmedchem.3c02408",
    "PMID": 38842931.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "CDR1: RHQWME, CDR2: SSFGQWTK, CDR3: CVVEVGYEYY",
    "Quote of the interaction": "\"A Potent Sybody Selectively Inhibits α-Synuclein Amyloid Formation by Binding to the P1 Region\", \"We discovered a sybody, named αSP1, that inhibits amyloid formation of α-synuclein at substoichiometric concentrations in a specific manner, even within highly crowded heterogeneous mixtures. Fluorescence resonance energy transfer-based binding assays and seeding experiments with and without αSP1 further demonstrate the importance of the P1 region for both primary and secondary nucleation mechanisms of amyloid assembly.\", \"Using seeding assays and experiments involving time-dependent sybody binding, we show that the sybody can inhibit α-syn amyloid formation in a specific and substoichiometric manner by binding to α-syn oligomers formed during the assembly process and to fibrils, preventing secondary nucleation processes.\", \"Figure 2\", \" The results showed that amyloid formation of α-syn is almost fully inhibited by αSP1, with a 1:10 αSP1:α-syn molar ratio, increasing the length of the lag phase by ∼2-fold, consistent with the sybody affecting early stages of amyloid formation that include primary nucleation of the assembly reaction (Figure 3A).\", \"Figure 3\", \"The inhibitory effect by αSP1 was confirmed by negative stain transmission electron microscopy, which showed fibrillar aggregates at the end of the incubation in the absence of αSP1, and notably fewer fibrils found when α-syn is incubated in the presence of αSP1 at a 1:100 (αSP1:α-syn) molar ratio (Figure 3B).\", \"Inhibition of α-syn amyloid aggregation by αSP1.\", \"The experiments described above show that αSP1 is effective at inhibiting amyloid formation of α-syn at low substoichiometric concentrations (even at a 1:100 αSP1:α-syn molar ratio). This observation suggests that inhibition is achieved via preferential interaction of the sybody with α-syn aggregates.\", \"Finally, we investigated the effect of αSP1 on one of the key modes of oligomer formation, secondary nucleation.45 To do so, ThT fluorescence assays were performed at pH 4.8 and a low molar ratio of preformed fibrils (PFFs) of α-syn to monomers, i.e., 1:1000, conditions under which amyloid formation is dominated by secondary nucleation on the fibril surface.45In vitro, this pH disrupts electrostatic interactions within the fuzzy coat surrounding α-syn fibrils, exposing their β-sheet core, and favoring interaction of the monomer with the fibril surface.46 Furthermore, this pH is biologically relevant as it mimics that of lysosomes, which are important in PD.47 Under these conditions, αSP1 showed a clear inhibitory effect on α-syn amyloid formation at substoichiometric concentrations of αSP1 to α-syn as low as 1:20 (Figure 3D), consistent with aSP1 inhibiting secondary nucleation processes.\",  \"Our data support the conclusion that the antiaggregation activity of the sybody is achieved via interaction with aggregated α-syn species, particularly with the oligomers. \", \"Finally, to assess the specificity of αSP1 for α-syn, the ThT assays were performed against another target known to form amyloid, the 42-residue variant of Aβ (Aβ42)50 at a 1:10 αSP1:Aβ42 molar ratio (the maximum molar ratio tested for α-syn) (Figure 5A). The results showed no inhibitory effect of αSP1 on the in vitro aggregation of Aβ42, confirming that αSP1 inhibits the amyloid formation of α-syn in a specific manner. \". \"Figure 5\", \"Finally, we assessed the ability of αSP1 to affect WT α-syn amyloid formation in the presence of an E. coli protein extract (Figure 5B) instead of buffer. We found that, even under this condition, αSP1 still inhibits the aggregation of α-syn into amyloid at substoichiometric concentrations, i.e., a 1:100 αSP1:α-syn molar ratio.\", \"In summary, the results presented show that αSP1 inhibits the self-assembly of α-syn by binding to α-syn oligomers and fibrils, potentially at the surface.\",",
    "Curator Statement": false
  },
  "AMGAB0278": {
    "Interaction ID": "AMGAB0278",
    "Antibody ID": "ABID0006",
    "Antibody name": "Lecanemab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/acs.nanolett.3c00187",
    "PMID": 37141711.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Atomic force microscopy (AFM)",
    "Amyloid species identified": "Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Lecanemab remained stable in binding to PFs and to globular oligomers, inhibiting the formation of large aggregates.\", \"These aggregates remained covered with lecanemab molecules (Figures 4a,d and S12d). We observed few MFs in the presence of lecanemab (Figures S11b and S12a). This result suggested that lecanemab bound oligomers like the shortest PFs in Figure S7 and inhibited their assembling to longer PFs.\", \"These results indicate that lecanemab covered the oligomer and inhibited the formation of larger PF and other aggregates (Figures 4, S11 and S12), thereby lowering the toxicity of large aggregates and oligomers.\", \"Figure S11\", Lecanemab kept the aggregate size small and spherical (Figures 4b,c and S12b,c). These aggregates remained covered with lecanemab molecules (Figures 4a,d and S12d). We observed few MFs in the presence of lecanemab (Figures S11b and S12a). This result suggested that lecanemab bound oligomers like the shortest PFs in Figure S7 and inhibited their assembling to longer PFs.\", \"Figure 4\", \"Figure S12\", \" Aggregates in the presence of lecanemab are denser (Table S1) but smaller in size (Figures 4b and S12b). \",",
    "Curator Statement": false
  },
  "AMGAB0279": {
    "Interaction ID": "AMGAB0279",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/acs.nanolett.3c00187",
    "PMID": 37141711.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Atomic force microscopy (AFM)",
    "Amyloid species identified": "Monomers, Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure S11\", \"In the presence of 6E10, LMW Aβ42 formed larger aggregates than those without antibody (Figures 4b and S12b). The sphericity of these aggregates was lower than that in lecanemab and larger than those without antibody (Figures 4c and S12c). The 6E10-covered area was not as large as lecanemab and no longer covered the periphery of the aggregates over the incubation time (Figures 4a,d and S12d). These results indicated that the binding of 6E10 to its epitope altered the aggregation pathway. Further growth of the newly formed aggregates by 6E10 would not expose the 6E10 epitope, suggesting that 6E10 was no longer able to bind.\", \"The number of aggregates in the presence of 6E10 is smaller than the number of aggregates without antibody (Table S1), although the presence of antibody may prevent adsorption to the well surface.\",",
    "Curator Statement": false
  },
  "AMGAB0280": {
    "Interaction ID": "AMGAB0280",
    "Antibody ID": "ABID0271",
    "Antibody name": "4G8",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/acs.nanolett.3c00187",
    "PMID": 37141711.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Movie S10\"",
    "Curator Statement": false
  },
  "AMGAB0281": {
    "Interaction ID": "AMGAB0281",
    "Antibody ID": "ABID0333",
    "Antibody name": "anti-AβOcSNK",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/acschemneuro.7b00469",
    "PMID": 29614860.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point), Immunohistochemistry",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"A mouse monoclonal antibody targeting AβOcSNK recognizes ∼50-60 kDa SDS-resistant soluble Aβ assemblages in AD brain and prolongs the lag phase of Aβ aggregation in vitro.\", \"Figure 5\", \"Anti-AβOcSNK binding delays synthetic AβO42 maturation.\", \"(c) At 5:1 and 10:1 Aβ/antibody molar ratios, anti-AβOcSNK significantly lengthens the lag phase compared to IgG1 control (** p < 0.01). (d) The elongation rate is not significantly impacted in the presence of anti-AβOcSNK compared to IgG1. (e) anti-AβOcSNK diminishes the final β-sheet content as measured by ThioT fluorescence, compared to Aβ alone and with IgG1 control, significantly at 5:1 and 10:1 Aβ/antibody molar ratios (**p < 0.01). Two-way ANOVA shows a significant difference between anti-AβOcSNK and IgG1 in their effect on the lag phase (p < 0.0001) and the maximum β-sheet levels (p = 0.003).\", \" When anti-AβOcSNK was added to Aβ monomer film reconstitution media, the maturation of all Aβ42 oligomers into smaller diameter forms was significantly delayed (Figure5a).\", \"We found that molar ratios of 50:1 and 100:1 Aβ/antibody had no effect on the accumulation of β-sheet content in the assay. However, at higher but still substoichiometric 5:1 and 10:1 Aβ/antibody molar ratios, anti-AβOcSNK β-sheet accumulation was significantly reduced from Aβ42 alone (p = 0.0001) and from Aβ42 incubated with a negative control IgG1 (p = 0.0001).\", \"Compared to Aβ42 monomer alone, anti-AβOcSNK antibody delays the lag phase of β-sheet accumulation by ∼1.75-fold at 5:1 and 10:1 Aβ/antibody ratio (p < 0.0001, Figure5c). This effect was statistically significant compared to IgG1 isotype control (p < 0.01), which has a nonstatistically significant increase in lag phase compared to Aβ42 monomer alone (Figure5b,c). The elongation rate showed a nonsignificant decrease, ∼0.5-fold, after incubation with anti-AβOcSNK antibody at 5:1 and 10:1 ratios (p < 0.5, Figure5d). The total β-sheet accumulated, as observed in the plateau phase, was significantly reduced by ∼0.25-fold with anti-AβOcSNK antibody (5:1 ratio) compared to Aβ42 alone and the IgG1 isotype control (both comparisons p < 0.05, Figure5e).\", \"This reduction in maximal β-sheet plateau suggests that the antibody is binding and stabilizing Aβ in its oligomeric, low β-sheet containing conformation, preventing a minority of Aβ from converting to high β-sheet containing fibrils. This was confirmed by TEM imaging (Supporting Figure 3b); by 30 h, oligomers are rarely observed in the Aβ42 sample, corresponding to the elongation phase, and only sparsely observed at 48 and 72 h, the plateau phase. In contrast, if Aβ42 is incubated with anti-AβOcSNK, oligomers are readily found at 48 h, the beginning of the plateau phase; by 72 h, oligomers are sparsely observed (Supporting Figure 3b). Similarly, when the presence of soluble versus insoluble aggregates in the assay was investigated through the time course, it was clear that anti-AβOcSNK delays the formation of insoluble aggregates by at least 20 h (Supporting Figure 3).\", \"Supporting Figure 3\", \"Anti-AβOcSNK markedly delays the aggregation of Aβ into an insoluble aggregate.\", \". Aβ gradually converts to its insoluble form starting at 30 h in the absence of antibody, while anti-AβOcSNK retains it in its soluble form for a longer time (> 48 h).  IgG1 seems to have an effect, but the delay is less pronounced than with anti-AβOcSNK (between 30 and 48 h)\", \"These TEM and ThioT analyses indicate that anti-AβOcSNK inhibits the aggregation of Aβ polymers in vitro, displaying its most prominent effects in early stages. In the lag phase as monomers begin to form oligomers, the cSNK epitope is exposed and is subsequently bound by anti-AβOcSNK. This binding slows the accumulation of β-sheet and oligomeric structures; likewise, this blockade slows the transition from oligomers to fibrils as the majority species in the population. However, once a critical concentration of oligomers (including protofibrils) has been reached, the elongation phase begins, in which fibrils recruit monomer at a faster rate than oligomers. (54) Thus, in the elongation phase, anti-AβOcSNK has a reduced impact because fibrils do not display the cSNK epitope. Finally, a significant reduction in plateau β-sheet structure suggests that, by maintaining some structures in an oligomeric form, the anti-AβOcSNK antibody has a negative downstream effect on total Aβ fibril content in vitro and perhaps even in vivo (Supporting Figure 5b).\", \"Figure 6\", \"Twelve month-old male Tg2576 and APP/PS1 mice were intraperitoneally injected weekly with 30 mg/kg of anti-AβOcSNK for 6 weeks. In both mouse models, anti-AβOcSNK treated animals had significantly lower levels of soluble Aβ aggregates in saline brain extracts compared to IgG1 treated controls (30% and 20% reduction, p = 0.012 and p = 0.012, respective, Figure6f). This indicates that 20–30% of the total brain AβO population can form AβOcSNK and are thus sensitive to engagement by anti-AβOcSNK and subsequent clearance. Notably, the murine IgG1 Fc subclass of the anti-AβOcSNK monoclonal antibody necessitates that clearance occur without the participation of Fc receptor-bearing brain cells, such as microglia.\", \"This is also supported by the in vitro aggregation study, which shows that anti-AβOcSNK (1) blocks formation of soluble oligomers from monomers, (2) has a nonsignificant effect on elongation of fibrils, and (3) reduces the maximal β-sheet produced (Figure5). These in vivo and in vitro studies allow us to conclude that the anti-AβOcSNK inhibits the oligomer–fibril transition of the Aβ population at large. (53)\", \"Our in vivo and in vitro studies suggest that anti-AβOcSNK inhibits the oligomer-fibril transition of Aβ, while neutralizing the toxic activity of AβOs.\",",
    "Curator Statement": false
  },
  "AMGAB0282": {
    "Interaction ID": "AMGAB0282",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/acschemneuro.9b00020",
    "PMID": 31042358.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Dot blot",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"The fiber inhibition experiment demonstrated that 1H7 could inhibit the formation of fiber at different concentrations (1.0, 0.5, and 0.1 μM) in a 3-h inhibition test, and the inhibitory efficiency was similar to that treated with 6E10 (Figure 4B).\", \"Figure 5\", \"Compared with polyclonal antibodies, 1H7 inhibited the formation of Aβ1–42 fibers but could not depolymerize Aβ1–42 fibers. The inhibitory effect was similar to that of 6E10, a classical anti-Aβ antibody.\",",
    "Curator Statement": false
  },
  "AMGAB0283": {
    "Interaction ID": "AMGAB0283",
    "Antibody ID": "ABID0187",
    "Antibody name": "1H7",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/acschemneuro.9b00020",
    "PMID": 31042358.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Dot blot",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"The fiber inhibition experiment demonstrated that 1H7 could inhibit the formation of fiber at different concentrations (1.0, 0.5, and 0.1 μM) in a 3-h inhibition test, and the inhibitory efficiency was similar to that treated with 6E10 (Figure 4B).\", \" After 3 h, the fluorescence intensity of the 1H7 treated group was decreased by about 50%, suggesting that 1H7 had a strong inhibitory effect on Aβ fiber formation.\", \"Figure 5\", \"Importantly, after incubation with 0.1 μM 1H7 for 160 h, no obvious fibers were observed.\", \"Compared with polyclonal antibodies, 1H7 inhibited the formation of Aβ1–42 fibers but could not depolymerize Aβ1–42 fibers. The inhibitory effect was similar to that of 6E10, a classical anti-Aβ antibody.\", \"Additionally, a monoclonal antibody 1H7 inhibiting fiber formation was also characterized and could be applied in future diagnostics and therapy.\"",
    "Curator Statement": false
  },
  "AMGAB0284": {
    "Interaction ID": "AMGAB0284",
    "Antibody ID": "ABID0443",
    "Antibody name": "N3Y",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1021/acsnano.1c03083",
    "PMID": 34293858.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro,",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Nanobody's CDR3 grafted a trityrosine 3xY motif (DED–3Y–DED, AGS/AAA) presumably responsible for the inhibition.",
    "Quote of the interaction": "\"Supplementary Figure S7\", \" In addition, we also expressed two more nanobodies, N3Y and N6Y, with the CDR3 regions being grafted by oligotyrosines 3Y and 6Y, respectively. The results of the ThT fluorescence kinetics indicated that N3Y and N6Y also showed an enhanced inhibitory effect compared to the corresponding 3Y and 6Y (Figure S7A,B), further evidencing that the conformation constraint of oligotyrosines was generally applicable.\", \"Compared with N3Y, N4Y showed a better inhibitory effect, whereas N6Y could even completely mitigate the aggregation of hIAPP (Figure S7C), suggesting that an increase in the number of Y in oligotyrosine was helpful in achieving an efficient inhibitor of hIAPP aggregation (Figure S7D).\",",
    "Curator Statement": false
  },
  "AMGAB0285": {
    "Interaction ID": "AMGAB0285",
    "Antibody ID": "ABID0443",
    "Antibody name": "N3Y",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1021/acsnano.1c03083",
    "PMID": 34293858.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro,",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Nanobody's CDR3 grafted a trityrosine 3xY motif (DED–3Y–DED, AGS/AAA) presumably responsible for the inhibition.",
    "Quote of the interaction": "\"Supplementary Figure S7\", \" In addition, we also expressed two more nanobodies, N3Y and N6Y, with the CDR3 regions being grafted by oligotyrosines 3Y and 6Y, respectively. The results of the ThT fluorescence kinetics indicated that N3Y and N6Y also showed an enhanced inhibitory effect compared to the corresponding 3Y and 6Y (Figure S7A,B), further evidencing that the conformation constraint of oligotyrosines was generally applicable.\", \"Compared with N3Y, N4Y showed a better inhibitory effect, whereas N6Y could even completely mitigate the aggregation of hIAPP (Figure S7C), suggesting that an increase in the number of Y in oligotyrosine was helpful in achieving an efficient inhibitor of hIAPP aggregation (Figure S7D).\",",
    "Curator Statement": false
  },
  "AMGAB0286": {
    "Interaction ID": "AMGAB0286",
    "Antibody ID": "ABID0444",
    "Antibody name": "N4Y",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1021/acsnano.1c03083",
    "PMID": 34293858.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro,",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Dynamic light scattering (DLS)",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "Nanobody's CDR3 grafted a tetratyrosine 4xY motif (DED–4Y–DED, AGS/AAA) presumably responsible for the inhibition.",
    "Quote of the interaction": "\"Figure 1\", \" At very low stoichiometric concentrations, 4Y failed to inhibit the hIAPP aggregation, whereas N4Y effectively delayed the hIAPP aggregation and partially mitigated the hIAPP amyloidogenesis.\", \"When the same concentration of N4Y was present, the lag phase of the hIAPP kinetics curve was significantly extended (416 min, Figure4C), and the final fluorescence intensity was reduced ∼70% (blue curve, Figure4A), indicating that N4Y could effectively inhibit the amyloidogenesis of hIAPP.\", \"Supplementary Figure S7\", \"Figure 4\", \"Compared with N3Y, N4Y showed a better inhibitory effect, whereas N6Y could even completely mitigate the aggregation of hIAPP (Figure S7C), suggesting that an increase in the number of Y in oligotyrosine was helpful in achieving an efficient inhibitor of hIAPP aggregation (Figure S7D).\", \"With an addition of N4Y in the hIAPP sample, the lag phase of hIAPP increased to 343 min, and the final fluorescence intensity decreased ∼65% (blue curve, Figure4B).\", \"Supplementary Figure S9\",",
    "Curator Statement": false
  },
  "AMGAB0287": {
    "Interaction ID": "AMGAB0287",
    "Antibody ID": "ABID0444",
    "Antibody name": "N4Y",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1021/acsnano.1c03083",
    "PMID": 34293858.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro,",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Dynamic light scattering (DLS),  Circular dichroism (CD),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Nanobody's CDR3 grafted a tetratyrosine 4xY motif (DED–4Y–DED, AGS/AAA) presumably responsible for the inhibition.",
    "Quote of the interaction": "\"Supplementary Figure S7\", \"Supplementary Figure S8\", \"Figure 4\", \"Compared with N3Y, N4Y showed a better inhibitory effect, whereas N6Y could even completely mitigate the aggregation of hIAPP (Figure S7C), suggesting that an increase in the number of Y in oligotyrosine was helpful in achieving an efficient inhibitor of hIAPP aggregation (Figure S7D).\", \"With an addition of N4Y in the hIAPP sample, the lag phase of hIAPP increased to 343 min, and the final fluorescence intensity decreased ∼65% (blue curve, Figure4B).\", \"Supplementary Figure S9\", \"As a comparison, the increase of particle size was impaired when N4Y was present (hIAPP/inhibitor molar ratio of 20:1), showing the effective inhibition of N4Y (Figure5E). \", \"Figure 5\", \"Supplementary Figure S12\", \"Similar results were observed when the concentration of added inhibitors was reduced to an hIAPP/inhibitor molar ratio of 40:1 (Figure S12), confirming the increased inhibitory effect on hIAPP amyloidogenesis by the three inhibitors.\",",
    "Curator Statement": false
  },
  "AMGAB0288": {
    "Interaction ID": "AMGAB0288",
    "Antibody ID": "ABID0445",
    "Antibody name": "N6Y",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1021/acsnano.1c03083",
    "PMID": 34293858.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro,",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Nanobody's CDR3 grafted a hexatyrosine 6xY motif (DED–6Y–DED, AGS/AAA) presumably responsible for the inhibition.",
    "Quote of the interaction": "\"Supplementary Figure S7\", \" In addition, we also expressed two more nanobodies, N3Y and N6Y, with the CDR3 regions being grafted by oligotyrosines 3Y and 6Y, respectively. The results of the ThT fluorescence kinetics indicated that N3Y and N6Y also showed an enhanced inhibitory effect compared to the corresponding 3Y and 6Y (Figure S7A,B), further evidencing that the conformation constraint of oligotyrosines was generally applicable.\", \"Compared with N3Y, N4Y showed a better inhibitory effect, whereas N6Y could even completely mitigate the aggregation of hIAPP (Figure S7C), suggesting that an increase in the number of Y in oligotyrosine was helpful in achieving an efficient inhibitor of hIAPP aggregation (Figure S7D).\",",
    "Curator Statement": false
  },
  "AMGAB0289": {
    "Interaction ID": "AMGAB0289",
    "Antibody ID": "ABID0558",
    "Antibody name": "anti-Aβ",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1021/bc060349x",
    "PMID": 17315944.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Mature fibrils, Protein monomer,",
    "Quote of the interaction": "\"Following a 4 hour incubation of the fusion antibody and the Abeta fibrils, most of the fibrils were disaggregated (Figure 9b).\", \"Figure 9\", \"The data show that the fusion antibody binds to Aβ1–40 plaque, and that this binding causes fibril disaggregation over a 4-hour period.\", \"After a 4-hour incubation with Abeta fibrils, the fusion antibody causes a time-dependent disaggregation of Abeta fibrils (Figure 9b).\",",
    "Curator Statement": false
  },
  "AMGAB0290": {
    "Interaction ID": "AMGAB0290",
    "Antibody ID": "ABID0558",
    "Antibody name": "anti-Aβ",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/bc060349x",
    "PMID": 17315944.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Mature fibrils, Protein monomer,",
    "Quote of the interaction": "\"Fusion antibody for Alzheimer's disease with bidirectional transport across the blood-brain barrier and abeta fibril disaggregation\", \"The fusion antibody also disaggregates Abeta amyloid in vivo in transgenic mouse brain.\", \"Figure 9\", \"Quantitation of the percent of either frontal cortex or hippocampus occupied by the the amyloid plaque showed that approximately 5% of the brain was amyloid. A single intra-cerebral injection of the fusion antibody into the hippocampus or the frontal cortex caused a 39 ± 3% and 38 ± 2% decrease, respectively, in the Abeta amyloid burden in brain in vivo at 48 hours after injection in the side ipsilateral to the injection, relative to the amyloid burden in the contralateral hippocampus or frontal cortex (Figure 9d).\", \"Fusion antibody disaggregates Abeta amyloid fibrils in vitro and in vivo.\", \"The decrease in amyloid content in either frontal cortex or hippocampus on the side of the fusion antibody injection, relative to the saline control, is statistically significant (*p<0.01).\", \"The fusion antibody also causes disaggregation of amyloid plaque in vivo in double transgenic APPswe/PS1dE9 mice (Figure 9d).\", \"A single intra-cerebral injection of 20 pmol of fusion antibody into either the frontal cortex or the hippocampus causes a 38–39% reduction in brain amyloid burden at 48 hours after fusion antibody administration (Figure 9d).\",",
    "Curator Statement": false
  },
  "AMGAB0291": {
    "Interaction ID": "AMGAB0291",
    "Antibody ID": "ABID0530",
    "Antibody name": "D4",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/bi060601o",
    "PMID": 16981713.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Atomic force microscopy (AFM),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Two scFvs with differing affinities for Aβ were studied, and both inhibited aggregation of Aβ42 as determined by thioflavin T binding assay and atomic force microscopy analysis and blocked Aβ-induced toxicity toward human neuroblastoma SH-SY5Y cells as determined by MTT and LDH release assays.\", \"We show that these scFvs are effective in inhibiting the aggregation of Aβ42 in vitro as well as reducing Aβ42-induced neurotoxicity in cell culture studies.\", \" When co-incubated with equimolar D4 or B6, however, Aβ42 aggregation was strongly inhibited (Figure 3). When incubated alone at similar concentrations, D4 and B6 did not increase fluorescence (Figure 3). The Aβ42 sample alone contained small aggregates at 0 h, forming larger spherical aggregates after 3 and 6 h of incubation and, finally, a mixture of Aβ fibrils and large aggregates after 50 h as visualized by AFM imaging (Figure 4). When Aβ42 was co-incubated with D4 and B6, however, only small aggregates were obtained even after prolonged incubation times (Figure 4), although the B6 sample formed larger aggregates compared to D4.\", \"Figure 3\", \"Figure 4\", \"Addition of B6 or D4 scFvs to the 3 h preincubated sample completely inhibited any further aggregation although neither sample dissolved the preexisting aggregates (data not shown).\", \"Both scFvs also inhibit further aggregation of preexisting Aβ oligomers, indicating that these scFvs can bind the early Aβ aggregate morphologies.\", \"ScFvs against the Aβ 25−35 fragment can successfully inhibit Aβ42 aggregation and reduce toxicity induced by Aβ42 toward neuronal cells.\",",
    "Curator Statement": false
  },
  "AMGAB0292": {
    "Interaction ID": "AMGAB0292",
    "Antibody ID": "ABID0530",
    "Antibody name": "D4",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/bi060601o",
    "PMID": 16981713.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Atomic force microscopy (AFM),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"However, when the B6 or D4 scFvs were added to the 50 h preincubated sample, no inhibition or dissolution of aggregation compared to Aβ42 alone was observed (data not shown).\", \"AFM image analyses indicated the presence of small aggregates in the 3 h preincubated samples treated with scFvs and a mixture of large aggregates and fibrils in the 50 h preincubated samples treated with scFvs (data not shown).\", \"The scFvs did not reduce or dissolve preexisting Aβ fibrillar samples.\",",
    "Curator Statement": "No dissagregation of pre-formed amyloid was seen."
  },
  "AMGAB0293": {
    "Interaction ID": "AMGAB0293",
    "Antibody ID": "ABID0531",
    "Antibody name": "B6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/bi060601o",
    "PMID": 16981713.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Atomic force microscopy (AFM),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Two scFvs with differing affinities for Aβ were studied, and both inhibited aggregation of Aβ42 as determined by thioflavin T binding assay and atomic force microscopy analysis and blocked Aβ-induced toxicity toward human neuroblastoma SH-SY5Y cells as determined by MTT and LDH release assays.\", \"We show that these scFvs are effective in inhibiting the aggregation of Aβ42 in vitro as well as reducing Aβ42-induced neurotoxicity in cell culture studies.\", \" When co-incubated with equimolar D4 or B6, however, Aβ42 aggregation was strongly inhibited (Figure 3). When incubated alone at similar concentrations, D4 and B6 did not increase fluorescence (Figure 3). The Aβ42 sample alone contained small aggregates at 0 h, forming larger spherical aggregates after 3 and 6 h of incubation and, finally, a mixture of Aβ fibrils and large aggregates after 50 h as visualized by AFM imaging (Figure 4). When Aβ42 was co-incubated with D4 and B6, however, only small aggregates were obtained even after prolonged incubation times (Figure 4), although the B6 sample formed larger aggregates compared to D4.\", \"Figure 3\", \"Figure 4\", \"Addition of B6 or D4 scFvs to the 3 h preincubated sample completely inhibited any further aggregation although neither sample dissolved the preexisting aggregates (data not shown).\", \"Both scFvs also inhibit further aggregation of preexisting Aβ oligomers, indicating that these scFvs can bind the early Aβ aggregate morphologies.\", \"ScFvs against the Aβ 25−35 fragment can successfully inhibit Aβ42 aggregation and reduce toxicity induced by Aβ42 toward neuronal cells.\",",
    "Curator Statement": false
  },
  "AMGAB0294": {
    "Interaction ID": "AMGAB0294",
    "Antibody ID": "ABID0531",
    "Antibody name": "B6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/bi060601o",
    "PMID": 16981713.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Atomic force microscopy (AFM),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"However, when the B6 or D4 scFvs were added to the 50 h preincubated sample, no inhibition or dissolution of aggregation compared to Aβ42 alone was observed (data not shown).\", \"AFM image analyses indicated the presence of small aggregates in the 3 h preincubated samples treated with scFvs and a mixture of large aggregates and fibrils in the 50 h preincubated samples treated with scFvs (data not shown).\", \"The scFvs did not reduce or dissolve preexisting Aβ fibrillar samples.\",",
    "Curator Statement": "No dissagregation of pre-formed amyloid was seen."
  },
  "AMGAB0295": {
    "Interaction ID": "AMGAB0295",
    "Antibody ID": "ABID0261",
    "Antibody name": "Asec-1A",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1021/bi902030m",
    "PMID": 20429609.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In cellulo",
    "Experimental method(s)": "ThT - Aggregation kinetics, Atomic force microscopy (AFM), SDS-PAGE",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The Asec-1A proteolytic nanobody, derived from a parent catalytic light chain antibody, prevents aggregation of monomeric Aβ, inhibits further aggregation of preformed Aβ aggregates, and reduces Aβ-induced cytotoxicity toward a human neuroblastoma cell line.\", \"Asec-1A prevents aggregation of Aβ in vitro and reduces Aβ-induced cytotoxicity toward SH-SY5Y neuroblastoma cells. The proteolytic nanobody can cleave early stage Aβ oligomers which have been implicated as the toxic species in AD but does not cleave late stage oligomers and fibrils.\", \"Figure 1\", \"Figure 2\", \"Figure 6\", \"Asec-1A Blocks Further Aggregation of Preaggregated Aβ\", \"We added aliquots of 1/200 molar ratio Asec-1A to 1, 2, and 4 day preincubated Aβ samples, and in each case the proteolytic nanobody inhibited any further aggregation of Aβ but did not result in dissolution of existing aggregates as determined by ThT (Figure 6). Image analysis by AFM confirms these results, indicating that the preaggregated Aβ particles do not increase in size when incubated with Asec-1A (Figure 7).\", \"Figure 7\",  \"Figure 9\", \"Our results show that when Aβ is incubated alone, the aggregates show a continual increase in height with time, starting with heights <0.5 nm corresponding to monomeric Aβ, and increasing steadily with time where heights >4 nm corresponding to fibrillar Aβ predominate after 7 days (Figure 9A). When Aβ is coincubated with Asec-1A, the particle heights remain essentially constant between 1 and 2 nm over the first 2 days of aggregation (Figure 9B), which correspond to trimeric and/or tetrameric forms of cross-linked Aβ (30).\", \"Figure 10\", \"While Aβ alone at 2, 4, and 7 days had predominant particle heights of 2−2.5, 2.5−3, and 3.5−4 nm, respectively, the heights of the corresponding samples incubated with Asec-1A were 1.5−2, 2−3, and 2.5−3.5 nm, indicating the nanobody delays but does not block Aβ aggregation at this concentration (Figure 10).\", \"Here we show that the Asec-1A proteolytic nanobody that has been affinity matured to have increased specificity for the α-secretase site of Aβ can potentially inhibit aggregation of monomeric and preaggregated Aβ forms. Whereas the parent c23.5 proteolytic scFv was previously shown to increase aggregation of Aβ (35), the affinity-matured variant decreases aggregation, suggesting that the increased aggregation previously observed with the c23.5 scFv was likely due to coaggregation of Aβ with the scFv itself.\", \"Incubation of monomeric or preformed aggregates of Aβ with Asec-1A inhibits formation of the 2.5−3 nm aggregates and inhibits subsequent toxicity toward mammalian neuronal cells.\", \"Asec-1A, even at 1/1000 (w/w) ratio, effectively inhibits Aβ aggregation and toxicity in vitro.\", \"The proteolytic nanobody can reduce toxicity both by cleaving APP at the α-secretase site preventing generation of Aβ and by cleaving Aβ monomers and low-n oligomers before they can aggregate into toxic species.\", \"The Asec1A nanobody described here both blocks aggregation of monomeric Aβ and prevents further aggregation of small aggregate species, both of which inhibit the formation of more toxic oligomeric Aβ aggregates.\",",
    "Curator Statement": false
  },
  "AMGAB0296": {
    "Interaction ID": "AMGAB0296",
    "Antibody ID": "ABID0281",
    "Antibody name": "Nb484",
    "Amyloid ID": "AGAMYID0024",
    "Amyloid name": "Major prion protein",
    "DOI": "10.1021/ja407527p",
    "PMID": 24400836.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), No aggregation (complete inhibition), Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Amyloid Seeding Assay, Protease-K resistance",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The addition of Nb484 to MoPrP(23–230) extended the lag phase of fibrillization by about 40 h in amyloid seeding assay (ASA).\", \"This indicates that the interaction of Nb484 with the full-length MoPrP inhibits the formation of PrPSc-like aggregates (Figure 1A,B).\", \"Figure 1\", \"To further confirm that Nb484 inhibits prion propagation, we treated scrapie infected murine cells (ScGT1) with different concentrations of Nb484. We evaluated the effect of the treatment measuring PrPSc level by PK assay and Western blotting. We observed that, compared with nontreated cells, the PrPSc levels in the ScGT1 cells treated with Nb484 were dramatically reduced in a dose-dependent manner. After adding 3.5 μM of Nb484, PrPSc levels were no longer detectable (Figure 1C). We also tested whether PrPSc remained undetectable after removing Nb484 from the medium. Cells previously treated with 3.5 μM of Nb484 exhibited PrPSc clearance upon its withdrawal (Figure 1D).\", \" Nb484 inhibits prion propagation.\", \"(C) Dose-dependent inhibition of PrPSc formation in ScGT1 cells treated with Nb484.\",",
    "Curator Statement": "Authors refer to Mouse PrP as MoPrP"
  },
  "AMGAB0297": {
    "Interaction ID": "AMGAB0297",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/jacs.4c08841",
    "PMID": 39445702.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "TEM image in presence/absence of the antibody, Atomic force microscopy (AFM)",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Notably, fibril elongation did not occur while 4396C was bound to its growing end, a phenomenon not observed with 6E10 and 4G8, which bind to the lateral surfaces of the fibrils (Figure 3).\",\"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0298": {
    "Interaction ID": "AMGAB0298",
    "Antibody ID": "ABID0251",
    "Antibody name": "4396C",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/jacs.4c08841",
    "PMID": 39445702.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Atomic force microscopy (AFM),",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We highlight the distinctive interaction of antibody 4396C, which specifically binds to the fibril ends in the paused state, suggesting a unique mechanism to hinder fibril elongation.\", \"(d) HS-AFM snapshots at 2.5, 5, 7.5, and 10 min of events where 4396C continuously bound to the end of Aβ fibrils for several minutes without dissociation within the observation time, thereby inhibiting elongation.\", \"Notably, fibril elongation did not occur while 4396C was bound to its growing end, a phenomenon not observed with 6E10 and 4G8, which bind to the lateral surfaces of the fibrils (Figure 3).\", \"Figure 3\", \"Figure 5\", \"Inhibitory effect of 4396C on fibril formation.\", \"The ThT assay provides a macroscopic perspective on the inhibitory effect of 4396C on Aβ fibril formation. The data revealed that 4396C had minimal impact on the lag time for the increase in fluorescence intensity but significantly reduced the steepness of the curve (Figure 5), indicating that the antibody inhibited fibril elongation rather than the primary nucleation process.\", \"In many instances, when 4396C bound to the fibril end, there was an observable increase in fibril image length corresponding to the size of the antibody, and fibril growth ceased both before and after binding (as illustrated in Figure S2). Consequently, the HS-AFM data revealed that 87% of the binding events of 4396C occurred at least 0.1 s after the spontaneous cessation of fibril elongation (Figure 6a), indicating that 4396C preferentially binds the fibril end during the pause state. Statistical analysis of HS-AFM data suggested that the pause period of fibril extension was significantly extended in the presence of 4396C, averaging 54.6 s compared to an average of 5.5 s in the absence of 4396C. Moreover, 4396C often remained bound to the fibril edge for more than 100 s, effectively arresting the fibril elongation (Figure 6b). Increasing the 4396C concentration led to a more potent inhibition of overall Aβ fibril growth (Figure S3).\", \"Figure 6\", \"Figure S2\", \"Figure S3\", \"Inhibition of Aβ fibril growth dependent on 4396C concentration.\", \"Antibody 4396C targets the edge of Aβ42 fibrils in the pause state, wherein most fibrils exhibit an even edge. This observation suggests that the fibril edge in the pause phase is trapped in a distinct conformational state, which bears an epitope recognized by 4396C (Figure 7)\", \"Antibody 4396C binds to the edge of the fibril in this state, thereby delaying or virtually halting the fibril elongation (Figures 3 and 6). \",",
    "Curator Statement": false
  },
  "AMGAB0299": {
    "Interaction ID": "AMGAB0299",
    "Antibody ID": "ABID0252",
    "Antibody name": "4G8",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/jacs.4c08841",
    "PMID": 39445702.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody, Atomic force microscopy (AFM)",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Notably, fibril elongation did not occur while 4396C was bound to its growing end, a phenomenon not observed with 6E10 and 4G8, which bind to the lateral surfaces of the fibrils (Figure 3).\",\"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0300": {
    "Interaction ID": "AMGAB0300",
    "Antibody ID": "ABID0476",
    "Antibody name": "cTfRMAb-ScFv",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1021/mp400348n",
    "PMID": 23924247.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \" In the present study, daily sc injections of the cTfRMAb-ScFv fusion protein causes no reduction in the brain concentration of urea-soluble immunoreactive Aβ1–40 or Aβ1–42 amyloid peptide (Table 2).\",",
    "Curator Statement": "Table 2 brain immunoreactivity was obtained through urea-mediated solubilization."
  },
  "AMGAB0301": {
    "Interaction ID": "AMGAB0301",
    "Antibody ID": "ABID0476",
    "Antibody name": "cTfRMAb-ScFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/mp400348n",
    "PMID": 23924247.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, Confocal microscopy",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Disaggregation of amyloid plaque in brain of Alzheimer's disease transgenic mice with daily subcutaneous administration of a tetravalent bispecific antibody that targets the transferrin receptor and the Abeta amyloid peptide\", \"Fusion protein treatment caused a 57% and 61% reduction in amyloid plaque in the cortex and hippocampus, respectively.\", \"Figure 2\", \"The percent of brain area occupied by Abeta plaque was reduced 57% and 49% in cortex as determined by 6E10 labeling and Thioflavin-S labeling, respectively. The percent of brain area occupied by Abeta plaque was reduced 61% and 43% in hippocampus as determined by 6E10 labeling and Thioflavin-S labeling, respectively. Significant reductions in amyloid burden were observed for all parameters for both cortex and hippocampus and for both 6E10 and Thioflavin-S labeling (Table 1).\", \"Table 1\", \" First, daily sc administration of the cTfRMAb-ScFv fusion protein to 12–15 month old PSAPP AD transgenic mice results in up to a 57%–61% decrease in the Abeta amyloid plaque burden in the cortex and hippocampus (Table 1).\", \"Daily sc treatment of the PSAPP mice with the cTfRMAb-ScFv fusion protein causes a 57% and 61% decrease in the Abeta amyloid plaque area of cortex and hippocampus, respectively (Table 1).\",",
    "Curator Statement": false
  },
  "AMGAB0302": {
    "Interaction ID": "AMGAB0302",
    "Antibody ID": "ABID0476",
    "Antibody name": "cTfRMAb-ScFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1021/mp400348n",
    "PMID": 23924247.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \" In the present study, daily sc injections of the cTfRMAb-ScFv fusion protein causes no reduction in the brain concentration of urea-soluble immunoreactive Aβ1–40 or Aβ1–42 amyloid peptide (Table 2).\",",
    "Curator Statement": "Table 2 brain immunoreactivity was obtained through urea-mediated solubilization."
  },
  "AMGAB0303": {
    "Interaction ID": "AMGAB0303",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/78682",
    "PMID": 10932230.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo, In cellulo",
    "Experimental method(s)": "Immunohistochemistry, ELISA, Quantitative Histomorphometry, Confocal microscopy,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\",\"Treatment with 3D6 was equally effective, producing an 86% reduction in plaque burden (P = 0.003). In contrast, 16C11 failed to have any effect on plaque burden.\", \"Figure 2\", \"After peripheral administration, 10D5 and 3D6 enter the CNS, bind to Aβ plaques and trigger amyloid clearance.\", \" After peripheral administration, 10D5 and 3D6 had gained access to most plaques within the CNS where they may have directly triggered amyloid clearance.\", \"The plaque burden is greatly reduced by 3D6 and 10D5 compared with that of 16C11.\", \"We undertook a separate study to determine if antibody treatment resulted in the clearance of preexisting amyloid or simply prevented formation of new plaques. We administered 3D6 or control antibody to 13-month-old heterozygous PDAPP mice, then examined the brains for total plaque burden after 3 and 35 days of treatment. Although there was no obvious change in the number of large plaques over the short treatment period (Fig. 2b), there seemed to be a reduction in diffuse amyloid and small aggregates of Aβ (Fig. 2b, inset). By image analysis of the frontal cortex, nearly 60% of the small plaques and diffuse amyloid, corresponding to pixels with intermediate to low intensity, had been eliminated during the intervening 32 days of treatment (Fig. 2c; P = 0.001). These results confirm that the antibody treatment triggered clearance of preexisting amyloid.\", \"Table 1\", \"Antibodies 10D5, 3D6 and pabAβ1–42 were all active in the ex vivo assay and demonstrated efficacy in vivo. In contrast, 16C11, 21F12 and the control antibody TM2a were inactive in both assays.\", \"Here we report that peripheral administration of antibodies against amyloid beta-peptide, was sufficient to reduce amyloid burden. Despite their relatively modest serum levels, the passively administered antibodies were able to enter the central nervous system, decorate plaques and induce clearance of preexisting amyloid. When examined in an ex vivo assay with sections of PDAPP or Alzheimer disease brain tissue, antibodies against amyloid beta-peptide triggered microglial cells to clear plaques through Fc receptor-mediated phagocytosis and subsequent peptide degradation.\", \"In summary, we have shown that passively administered antibodies against Aβ peptide reduced the extent of plaque deposition in a mouse model of Alzheimer disease.\",",
    "Curator Statement": false
  },
  "AMGAB0304": {
    "Interaction ID": "AMGAB0304",
    "Antibody ID": "ABID0434",
    "Antibody name": "10D5",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/78682",
    "PMID": 10932230.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo, In cellulo",
    "Experimental method(s)": "Immunohistochemistry, ELISA, Quantitative Histomorphometry, Confocal microscopy,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Relative to control-treated mice, the polyclonal immunoglobulin fraction against Aβ and one of the monoclonal antibodies (10D5) reduced plaque burden by 93% and 81%, respectively (Fig. 1a, P < 0.005).\", \"Figure 1\", \"There were similar reductions in cortical levels of Aβ42 by ELISA measurements (6200, 4890 and 13800 ng/g tissue for 10D5, pabAβ1–42 and PBS, respectively).\", \"Once again, after 6 months of treatment, 10D5 reduced plaque burden by greater than 80% compared with that of either the PBS or isotype-matched antibody controls (P = 0.003).\", \"Figure 2\", \" After peripheral administration, 10D5 and 3D6 had gained access to most plaques within the CNS where they may have directly triggered amyloid clearance.\", \"The plaque burden is greatly reduced by 3D6 and 10D5 compared with that of 16C11.\", \"In PDAPP brain sections assayed in the presence of 16C11 (one of the antibodies against Aβ that was not efficacious in vivo), amyloid β-protein plaques remained intact and there was no phagocytosis. In contrast, after culture of adjacent sections in the presence of 10D5, amyloid deposits were mostly eliminated and the microglial cells showed many phagocytic vesicles containing Aβ (Fig. 3a, top). We obtained identical results with AD brain sections: 10D5 induced phagocytosis of AD plaques, whereas 16C11 was inactive (Fig. 3a, bottom).\", \"Figure 3\", \"Table 1\", \"Antibodies 10D5, 3D6 and pabAβ1–42 were all active in the ex vivo assay and demonstrated efficacy in vivo. In contrast, 16C11, 21F12 and the control antibody TM2a were inactive in both assays.\", \"Here we report that peripheral administration of antibodies against amyloid beta-peptide, was sufficient to reduce amyloid burden. Despite their relatively modest serum levels, the passively administered antibodies were able to enter the central nervous system, decorate plaques and induce clearance of preexisting amyloid. When examined in an ex vivo assay with sections of PDAPP or Alzheimer disease brain tissue, antibodies against amyloid beta-peptide triggered microglial cells to clear plaques through Fc receptor-mediated phagocytosis and subsequent peptide degradation.\", \"In summary, we have shown that passively administered antibodies against Aβ peptide reduced the extent of plaque deposition in a mouse model of Alzheimer disease.\",",
    "Curator Statement": false
  },
  "AMGAB0305": {
    "Interaction ID": "AMGAB0305",
    "Antibody ID": "ABID0455",
    "Antibody name": "21F12",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/78682",
    "PMID": 10932230.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro, In vivo, In cellulo",
    "Experimental method(s)": "Immunohistochemistry, ELISA,Quantitative Histomorphometry, Confocal microscopy",
    "Amyloid species identified": "Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\", \"Although 21F12 seemed to have a relatively modest effect on plaque burden, there was no substantial reduction as determined by ELISA measurements (13,580 ng/g). \", \"After peripheral administration, 10D5 and 3D6 enter the CNS, bind to Aβ plaques and trigger amyloid clearance.\", \"Table 1\",\"Antibodies 10D5, 3D6 and pabAβ1–42 were all active in the ex vivo assay and demonstrated efficacy in vivo. In contrast, 16C11, 21F12 and the control antibody TM2a were inactive in both assays.\",",
    "Curator Statement": false
  },
  "AMGAB0306": {
    "Interaction ID": "AMGAB0306",
    "Antibody ID": "ABID0456",
    "Antibody name": "16C11",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/78682",
    "PMID": 10932230.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro, In vivo, In cellulo",
    "Experimental method(s)": "Immunohistochemistry, ELISA, Quantitative Histomorphometry, Confocal microscopy",
    "Amyloid species identified": "Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\", \"The plaque burden is greatly reduced by 3D6 and 10D5 compared with that of 16C11.\",  \"In PDAPP brain sections assayed in the presence of 16C11 (one of the antibodies against Aβ that was not efficacious in vivo), amyloid β-protein plaques remained intact and there was no phagocytosis. In contrast, after culture of adjacent sections in the presence of 10D5, amyloid deposits were mostly eliminated and the microglial cells showed many phagocytic vesicles containing Aβ (Fig. 3a, top). We obtained identical results with AD brain sections: 10D5 induced phagocytosis of AD plaques, whereas 16C11 was inactive (Fig. 3a, bottom).\", \"Figure 3\", \"In the presence of 10D5, Aβ (red) localizes to vesicles within the membrane boundaries of microglial cells; in the presence of 16C11, plaques remain intact and there is no evidence of cellular staining.\", \"Table 1\", \"Antibodies 10D5, 3D6 and pabAβ1–42 were all active in the ex vivo assay and demonstrated efficacy in vivo. In contrast, 16C11, 21F12 and the control antibody TM2a were inactive in both assays.\",",
    "Curator Statement": false
  },
  "AMGAB0307": {
    "Interaction ID": "AMGAB0307",
    "Antibody ID": "ABID0162",
    "Antibody name": "Aβ-scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/mt.2010.111",
    "PMID": 20551911.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"22 Treatment of 3-month-old 3xTg-AD mice resulted in decreased amyloid burden, decreased tau hyperphosphorylation, and improved spatial learning by 12 months of age.\", \"Although there was no reduction of total soluble Aβ, levels of soluble oligomeric Aβ, as measured via NU-4 dot blot, were reduced in mice treated with rAAV1-Aβ-scFv as compared to mice receiving no injection (Figure 5c). Mice receiving rAAV1-Phe-scFv possessed an intermediate level of soluble oligomeric Aβ.\", \"Figure 5\", \"Mice treated with rAAV1-Aβ-scFv exhibited >75% reduction in numbers of Congo red-stained plaques (Figure 5g).\", \"Mice receiving rAAV1-Phe-scFv or no injection showed elevated Aβ/APP staining as compared to mice receiving rAAV1-Aβ-scFv (Figure 7i)\", \"Figure 7\", \"AAV1 vector-mediated expression of Aβ-scFv antibody decreases levels of insoluble Aβ in the hippocampus of 3xTg-AD mice.\", \"Our results demonstrate that sustained hippocampal expression of an Aβ-specific scFv decreased amyloid burden, diminished hyperphosphorylation of tau, increased numbers of microglia, and enhanced learning behavior.\", \"The levels of insoluble Aβ42, oligomeric Aβ by NU-4 and numbers of congophillic plaques were significantly reduced in 3xTg-AD mice receiving rAAV1-Aβ-scFv, suggesting that this third option could at least partially account for the effects observed on amyloid pathology.\", \"35,36 Hence, the Aβ-scFv mediated decrease in insoluble Aβ that we observe in 3xTg-AD mice are consistent with prevention of senescence of resident microglia, thereby enhancing the abilities of these cells to participate in Aβ clearance.\"",
    "Curator Statement": false
  },
  "AMGAB0308": {
    "Interaction ID": "AMGAB0308",
    "Antibody ID": "ABID0163",
    "Antibody name": "Phe-scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/mt.2010.111",
    "PMID": 20551911.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Although there was no reduction of total soluble Aβ, levels of soluble oligomeric Aβ, as measured via NU-4 dot blot, were reduced in mice treated with rAAV1-Aβ-scFv as compared to mice receiving no injection (Figure 5c). Mice receiving rAAV1-Phe-scFv possessed an intermediate level of soluble oligomeric Aβ.\",\"Figure 5\", \"Mice receiving rAAV1-Phe-scFv or no injection showed elevated Aβ/APP staining as compared to mice receiving rAAV1-Aβ-scFv (Figure 7i)\", \"Figure 7\",",
    "Curator Statement": false
  },
  "AMGAB0309": {
    "Interaction ID": "AMGAB0309",
    "Antibody ID": "ABID0532",
    "Antibody name": "SAP-5",
    "Amyloid ID": "AGAMYID0017",
    "Amyloid name": "Serum amyloid P-component",
    "DOI": "10.1038/nature09494",
    "PMID": 20962779.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Radio-labelled Tracer Qunatification, Histological quantification,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" Here we show that administration of anti-human-SAP antibodies to mice with amyloid deposits containing human SAP triggers a potent, complement-dependent, macrophage-derived giant cell reaction that swiftly removes massive visceral amyloid deposits without adverse effect\", \"Supplementary information Section 11\", \"Supplementary information Section 12\", \"Only one of the monoclonal antibodies in this panel, the IgG2a SAP-5, was effective in eliminating amyloid deposits, despite several of the IgG1 antibodies having similar affinity and avidity. The ineffective IgG2a antibody was less avid than SAP-5.\", \"SAP-5 and Abp1 recognized different epitopes on human SAP (Supplementary Information, section 10) but were each as potent as the polyclonal sheep anti-SAP in eliminating amyloid in vivo (Supplementary Information, sections 11 and 12).\",",
    "Curator Statement": false
  },
  "AMGAB0310": {
    "Interaction ID": "AMGAB0310",
    "Antibody ID": "ABID0533",
    "Antibody name": "Abp1",
    "Amyloid ID": "AGAMYID0017",
    "Amyloid name": "Serum amyloid P-component",
    "DOI": "10.1038/nature09494",
    "PMID": 20962779.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Radio-labelled Tracer Qunatification,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" Here we show that administration of anti-human-SAP antibodies to mice with amyloid deposits containing human SAP triggers a potent, complement-dependent, macrophage-derived giant cell reaction that swiftly removes massive visceral amyloid deposits without adverse effect\", \"Supplementary information Section 11\", \"SAP-5 and Abp1 recognized different epitopes on human SAP (Supplementary Information, section 10) but were each as potent as the polyclonal sheep anti-SAP in eliminating amyloid in vivo (Supplementary Information, sections 11 and 12).\",",
    "Curator Statement": false
  },
  "AMGAB0311": {
    "Interaction ID": "AMGAB0311",
    "Antibody ID": "ABID0534",
    "Antibody name": "SAP-1",
    "Amyloid ID": "AGAMYID0017",
    "Amyloid name": "Serum amyloid P-component",
    "DOI": "10.1038/nature09494",
    "PMID": 20962779.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Histological quantification,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary information Section 12\", \"Only one of the monoclonal antibodies in this panel, the IgG2a SAP-5, was effective in eliminating amyloid deposits, despite several of the IgG1 antibodies having similar affinity and avidity. The ineffective IgG2a antibody was less avid than SAP-5. \"",
    "Curator Statement": false
  },
  "AMGAB0312": {
    "Interaction ID": "AMGAB0312",
    "Antibody ID": "ABID0535",
    "Antibody name": "SAP-2",
    "Amyloid ID": "AGAMYID0017",
    "Amyloid name": "Serum amyloid P-component",
    "DOI": "10.1038/nature09494",
    "PMID": 20962779.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Histological quantification,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary information Section 12\", \"Only one of the monoclonal antibodies in this panel, the IgG2a SAP-5, was effective in eliminating amyloid deposits, despite several of the IgG1 antibodies having similar affinity and avidity. The ineffective IgG2a antibody was less avid than SAP-5. \"",
    "Curator Statement": false
  },
  "AMGAB0313": {
    "Interaction ID": "AMGAB0313",
    "Antibody ID": "ABID0536",
    "Antibody name": "SAP-3",
    "Amyloid ID": "AGAMYID0017",
    "Amyloid name": "Serum amyloid P-component",
    "DOI": "10.1038/nature09494",
    "PMID": 20962779.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Histological quantification,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary information Section 12\", \"Only one of the monoclonal antibodies in this panel, the IgG2a SAP-5, was effective in eliminating amyloid deposits, despite several of the IgG1 antibodies having similar affinity and avidity. The ineffective IgG2a antibody was less avid than SAP-5. \"",
    "Curator Statement": false
  },
  "AMGAB0314": {
    "Interaction ID": "AMGAB0314",
    "Antibody ID": "ABID0537",
    "Antibody name": "SAP-4",
    "Amyloid ID": "AGAMYID0017",
    "Amyloid name": "Serum amyloid P-component",
    "DOI": "10.1038/nature09494",
    "PMID": 20962779.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Histological quantification,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary information Section 12\", \"Only one of the monoclonal antibodies in this panel, the IgG2a SAP-5, was effective in eliminating amyloid deposits, despite several of the IgG1 antibodies having similar affinity and avidity. The ineffective IgG2a antibody was less avid than SAP-5. \"",
    "Curator Statement": false
  },
  "AMGAB0315": {
    "Interaction ID": "AMGAB0315",
    "Antibody ID": "ABID0538",
    "Antibody name": "SAP-6",
    "Amyloid ID": "AGAMYID0017",
    "Amyloid name": "Serum amyloid P-component",
    "DOI": "10.1038/nature09494",
    "PMID": 20962779.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Histological quantification,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary information Section 12\", \"Only one of the monoclonal antibodies in this panel, the IgG2a SAP-5, was effective in eliminating amyloid deposits, despite several of the IgG1 antibodies having similar affinity and avidity. The ineffective IgG2a antibody was less avid than SAP-5. \"",
    "Curator Statement": false
  },
  "AMGAB0316": {
    "Interaction ID": "AMGAB0316",
    "Antibody ID": "ABID0539",
    "Antibody name": "SAP-7",
    "Amyloid ID": "AGAMYID0017",
    "Amyloid name": "Serum amyloid P-component",
    "DOI": "10.1038/nature09494",
    "PMID": 20962779.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Histological quantification,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary information Section 12\", \"Only one of the monoclonal antibodies in this panel, the IgG2a SAP-5, was effective in eliminating amyloid deposits, despite several of the IgG1 antibodies having similar affinity and avidity. The ineffective IgG2a antibody was less avid than SAP-5. \"",
    "Curator Statement": false
  },
  "AMGAB0317": {
    "Interaction ID": "AMGAB0317",
    "Antibody ID": "ABID0001",
    "Antibody name": "Aducanumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/nature19323",
    "PMID": 27582220.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The antibody aducanumab reduces Aβ plaques in Alzheimer's disease\", \"Together, our data support further development of aducanumab as an Aβ-removing, disease-modifying therapy for AD.\", \"Treatment with aducanumab reduced brain Aβ plaques as measured by florbetapir PET imaging in a dose- and time-dependent fashion (Fig. 1, 2a).\", \"The mean PET standard uptake value ratio (SUVR) composite score at baseline was 1.44. After 54 weeks of treatment, this had decreased significantly (P < 0.001) in the 3, 6 and 10 mg kg−1 dose groups; whereas change for the placebo group was minimal (Fig. 2a, Extended Data Table 1).\", \"Figure 1\", \"Figure 2\", \"In the 10 mg kg−1 dose group, the SUVR composite score was 1.16 after 54 weeks of treatment, a value near the purported quantitative cut-point of 1.10 that discriminates between positive and negative scans (Fig. 2b)10. The adjusted mean changes in SUVR composite scores in the 6 and 10 mg kg−1 groups treated for 26 weeks were similar in magnitude to the dose group below (3 and 6 mg kg−1, respectively) treated for 54 weeks (Fig. 2a). Reductions in amyloid PET SUVR composite score in aducanumab-treated patients were similar in patients with mild and prodromal AD, and apolipoprotein E (ApoE) ε4 carriers and non-carriers (Extended Data Fig. 2a, b). Pre-specified regional analyses of SUVR changes demonstrated statistically significant dose-dependent reductions in all brain regions, except for the pons and sub-cortical white matter, two areas in which Aβ plaques are not expected to accumulate (Extended Data Fig. 3).\", \"Amyloid plaque reduction with aducanumab: example amyloid PET images at baseline and week 54.\", \"Amyloid plaque reduction with aducanumab.\", \"Extended Data Table 1\", \"Extended Data Figure 2\", \"Amyloid plaque reduction with aducanumab by baseline clinical stage and baseline ApoE ε4 status.\", \"Extended Data Figure 3\",  \"Amyloid plaque reduction- regional analysis SUVR at week 54. \", \"The PRIME study shows that aducanumab penetrates the brain and decreases Aβ in patients with AD in a time- and dose-dependent manner. Within 54 weeks of treatment, 3, 6 and 10 mg kg−1 doses of aducanumab significantly decreased the amyloid PET SUVR. Patients receiving placebo showed virtually no change in their mean PET SUVR composite scores over one year, indicating that Aβ pathology had already reached an asymptote of accumulation.\", \"The minimal effective dose upon repeated systemic administration of chaducanumab in transgenic mice was 3 mg kg−1 (corresponding to minimally effective concentrations of 13.8 ± 1.9 μg ml−1 in plasma and 99.8 ± 30.0 ng g−1 in brain) with reductions of Aβ42 in soluble and insoluble brain fractions of approximately 50%, and reductions in Aβ plaque of approximately 40%. Since exposure at 3 mg kg−1 in animals and humans is approximately equivalent, the observed dose-response in the model was consistent with the clinical doses that led to reductions in amyloid PET SUVR. chaducanumab cleared plaques of all sizes, suggesting that aducanumab triggered clearance of pre-existing Aβ plaques and prevented formation of new plaques.\",\"Several mechanisms may be involved in aducanumab’s Aβ-lowering activity. The clearance of Aβ deposits was accompanied by enhanced recruitment of microglia. Together with the reduced potency of the aglycosylated form of chaducanumab (data not shown), and the ex vivo phagocytosis data, this suggests that FcγR-mediated microglial recruitment and phagocytosis played an important role in Aβ clearance in these models.\",",
    "Curator Statement": false
  },
  "AMGAB0318": {
    "Interaction ID": "AMGAB0318",
    "Antibody ID": "ABID0001.6.4",
    "Antibody name": "chaducanumab",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1038/nature19323",
    "PMID": 27582220.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Reduction of amyloid burden following weekly dosing with chaducanumab in 9.5- to 15.5-month-old Tg2576 transgenic mice.\", \"Quantitative 6E10 immunohistochemistry showed significant reductions in all forms of Aβ deposits by up to 70% (Fig. 4c, d).\",",
    "Curator Statement": false
  },
  "AMGAB0319": {
    "Interaction ID": "AMGAB0319",
    "Antibody ID": "ABID0001.6.4",
    "Antibody name": "chaducanumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/nature19323",
    "PMID": 27582220.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Reduction of brain Aβ in transgenic mice\", \"chaducanumab, a murine IgG2a/κ chimaeric analogue, dose-dependently reduced Aβ measured in brain homogenates by up to 50% relative to the vehicle control in the diethylamine (DEA) fraction that extracted soluble monomeric and oligomeric forms of Aβ40 and Aβ42, and in the guanidine hydrochloride (GuHCl) fraction that extracted insoluble Aβ fibrils (Fig. 4a, b).\",\"Figure 4\", \"Reduction of amyloid burden following weekly dosing with chaducanumab in 9.5- to 15.5-month-old Tg2576 transgenic mice.\", \"Quantitative 6E10 immunohistochemistry showed significant reductions in all forms of Aβ deposits by up to 70% (Fig. 4c, d).\", \"Thioflavin S (ThioS) staining of compact Aβ plaques showed dose-dependent and statistically significant reductions in the cortex and hippocampus by up to 63% (Fig. 4c, d). Quantitative histology indicated that chaducanumab significantly reduced the number of plaques of all sizes, including plaques >500 μm2 and plaques <125 μm2 (Extended Data Fig. 6a–c). Quantification of ThioS-positive vascular and parenchymal Aβ plaques separately showed that chaducanumab did not affect vascular Aβ in either cortex or hippocampus (Fig. 4e–h).\", \"Extended Data Figure 6\", \"Treatment with chaducanumab affects plaques of all sizes.\", \"The minimal effective dose upon repeated systemic administration of chaducanumab in transgenic mice was 3 mg kg−1 (corresponding to minimally effective concentrations of 13.8 ± 1.9 μg ml−1 in plasma and 99.8 ± 30.0 ng g−1 in brain) with reductions of Aβ42 in soluble and insoluble brain fractions of approximately 50%, and reductions in Aβ plaque of approximately 40%. Since exposure at 3 mg kg−1 in animals and humans is approximately equivalent, the observed dose-response in the model was consistent with the clinical doses that led to reductions in amyloid PET SUVR. chaducanumab cleared plaques of all sizes, suggesting that aducanumab triggered clearance of pre-existing Aβ plaques and prevented formation of new plaques.\",",
    "Curator Statement": false
  },
  "AMGAB0320": {
    "Interaction ID": "AMGAB0320",
    "Antibody ID": "ABID0309",
    "Antibody name": "TAP01_04",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41380-021-01385-7",
    "PMID": 34776512.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Studies in two established mouse models of AD (5XFAD [17] and Tg4-42 [18]) showed substantial therapeutic benefits from either active immunisation with cyclised Aβ1-14 or passive immunisation with a humanised variant of TAP01, which reveals two attractive new options for AD treatment, including a potentially transformative vaccination approach.\", \" The beneficial treatment effect achieved by active immunisation with cyclised Aβ1-14 and by passive immunisation with TAP01_04 antibody was similar across these imaging investigations, which clearly suggests that both approaches target the pseudo β-hairpin conformation of Aβ (Fig. 2).\", \"Fig. 2: Active and passive immunisation reduced amyloid plaque load in 5XFAD mice.\", \"Figure 2\", \"PET images with amyloid-plaque tracer florbetaben reveal a reduction in plaque load induced by either active immunisation with cyclised Aβ1-14 or treatment with the antibody TAP01_04 (passive immunisation).\",",
    "Curator Statement": false
  },
  "AMGAB0321": {
    "Interaction ID": "AMGAB0321",
    "Antibody ID": "ABID0188",
    "Antibody name": "3H3",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41467-020-14685-3",
    "PMID": 32081907.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Dynamic light scattering (DLS)",
    "Amyloid species identified": "Monomers, oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"3H3 inhibits polymerization of Aβ and other amyloid precursors in vitro and reduces amyloid deposition in transgenic mouse models of AD and familial Danish dementia.\", \"Supplementary Figure 2\", \"In addition, 3H3 and 4G1 mAbs inhibited both curli and Aβ fibrillization, whereas 4A6 did not (Supplementary Fig. 2).\",  \"The ability of 3H3 to inhibit polymerization of curli monomers suggests that some of its anti-biofilm activity may involve inhibiting the development of full-length curli fibrils. The observation that 3H3 binds and inhibits polymerization of amyloids with dramatically different primary sequences suggests that it binds a pre-fibrillar intermediate conformation that is shared by diverse amyloids. In the case of curli, these structures may consist of curli monomers or low molecular weight oligomers32.\",",
    "Curator Statement": false
  },
  "AMGAB0322": {
    "Interaction ID": "AMGAB0322",
    "Antibody ID": "ABID0188",
    "Antibody name": "3H3",
    "Amyloid ID": "AGAMYID0025",
    "Amyloid name": "Curli",
    "DOI": "10.1038/s41467-020-14685-3",
    "PMID": 32081907.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro, in vivo",
    "Experimental method(s)": "Confocal microscopy of Congo Red-stained biofilms,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We show that 3H3 inhibits the polymerization of curli, leading to alteration of the biofilm architecture and rendering the biofilm bacteria more sensitive to antibiotic treatment and to macrophage uptake. In addition, 3H3 inhibits biofilm formation on a vascular catheter in vivo and collaborates with an antibiotic to clear an established, catheter-associated biofilm.\", \"Anti-Aβ mAb inhibits formation of S. Typhimurium biofilms\", \"Biofilms formed in cultures containing the other mAbs were substantially thinner, approaching the value for the csgBA mutant (5.5 µm): 4A6, 10.9 µm; 4G1, 7.3 µm; 2C10, 9.5 µm; and 3H3, 7.5 µm (Fig. 1b), with less surface coverage and CR staining (Fig. 1a).\", \"Figure 1\", \" Three of the four mAb-exposed samples had significantly reduced CR staining: 4G1 (23.9 RFU), 2C10 (22.1 RFU), and 3H3 (23.2 RFU), compared to the control and 6A samples (47.1 RFU and 48.1 RFU, respectively), although these were greater than the csgBA biofilm (7.91 RFU) (Fig. 1c).\", \"3H3 inhibits the fibrillization of curli\", \"To test whether 3H3 affects curli fibrillization, we tested the synthetic peptides CsgAR4-5 and CsgAR4-5N122A and the protein BSA in vitro using the Thioflavin T (ThT) assay41. CsgAR4-5, which has the sequence of the fourth and fifth repeats of CsgA, self-associates and forms fibrils, whereas CsgAR4-5N122A contains a single amino acid substitution that prevents fibrillization42. Incubation of CsgAR4-5 in the presence of 3H3 significantly reduced the polymerization of CsgAR4-5 alone or incubated with the control antibody 6A (Supplementary Fig. 5A).\", \"Supplementary Figure 5\", \"We also evaluated the lag time (t0) of fibrillization, the time required for monomers to self-associate and begin to fibrillize43. There was a significant increase in the lag time required for CsgAR4-5 to self-associate when incubated with 3H3 in comparison to the calculated lag time for CsgAR4-5 alone. Overall these data suggest that 3H3 inhibits initiation of CsgA fibrillization as well as elongation of curli fibrils (Supplementary Fig. 5B).\", \" In contrast, catheters treated with ampicillin and 3H3 in combination were virtually free of biofilm, with only minimal levels of Congo Red staining (Fig. 5b, lower right).\", \"Figure 5\", \"Upon incubation of synthetic CsgA peptides with 3H3, we observed a reduction in curli fibrillization\", \"In addition, 3H3 and 4G1 mAbs inhibited both curli and Aβ fibrillization, whereas 4A6 did not (Supplementary Fig. 2).\", \"The ability of 3H3 to inhibit polymerization of curli monomers suggests that some of its anti-biofilm activity may involve inhibiting the development of full-length curli fibrils. The observation that 3H3 binds and inhibits polymerization of amyloids with dramatically different primary sequences suggests that it binds a pre-fibrillar intermediate conformation that is shared by diverse amyloids. In the case of curli, these structures may consist of curli monomers or low molecular weight oligomers32.\",",
    "Curator Statement": "UniProt Accession assigned to A0A0F6AZX4, as the strain used is derived from the 14028."
  },
  "AMGAB0323": {
    "Interaction ID": "AMGAB0323",
    "Antibody ID": "ABID0189",
    "Antibody name": "4G1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41467-020-14685-3",
    "PMID": 32081907.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Dynamic light scattering (DLS)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure 2\", \"4G1 also inhibits Aβ fibril formation in vitro (Supplementary Fig. 2).\", \"In addition, 3H3 and 4G1 mAbs inhibited both curli and Aβ fibrillization, whereas 4A6 did not (Supplementary Fig. 2).\",",
    "Curator Statement": false
  },
  "AMGAB0324": {
    "Interaction ID": "AMGAB0324",
    "Antibody ID": "ABID0189",
    "Antibody name": "4G1",
    "Amyloid ID": "AGAMYID0025",
    "Amyloid name": "Curli",
    "DOI": "10.1038/s41467-020-14685-3",
    "PMID": 32081907.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Confocal microscopy of Congo Red-stained biofilms,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-Aβ mAb inhibits formation of S. Typhimurium biofilms\", \"Biofilms formed in cultures containing the other mAbs were substantially thinner, approaching the value for the csgBA mutant (5.5 µm): 4A6, 10.9 µm; 4G1, 7.3 µm; 2C10, 9.5 µm; and 3H3, 7.5 µm (Fig. 1b), with less surface coverage and CR staining (Fig. 1a).\", \"Figure 1\", \" Three of the four mAb-exposed samples had significantly reduced CR staining: 4G1 (23.9 RFU), 2C10 (22.1 RFU), and 3H3 (23.2 RFU), compared to the control and 6A samples (47.1 RFU and 48.1 RFU, respectively), although these were greater than the csgBA biofilm (7.91 RFU) (Fig. 1c).\", \"In addition, 3H3 and 4G1 mAbs inhibited both curli and Aβ fibrillization, whereas 4A6 did not (Supplementary Fig. 2).\",",
    "Curator Statement": "UniProt Accession assigned to A0A0F6AZX4, as the strain used is derived from the 14028."
  },
  "AMGAB0325": {
    "Interaction ID": "AMGAB0325",
    "Antibody ID": "ABID0190",
    "Antibody name": "4A6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41467-020-14685-3",
    "PMID": 32081907.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Dynamic light scattering (DLS)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure 2\", \"4G1 also inhibits Aβ fibril formation in vitro (Supplementary Fig. 2).\", \"In addition, 3H3 and 4G1 mAbs inhibited both curli and Aβ fibrillization, whereas 4A6 did not (Supplementary Fig. 2).\",",
    "Curator Statement": false
  },
  "AMGAB0326": {
    "Interaction ID": "AMGAB0326",
    "Antibody ID": "ABID0190",
    "Antibody name": "4A6",
    "Amyloid ID": "AGAMYID0025",
    "Amyloid name": "Curli",
    "DOI": "10.1038/s41467-020-14685-3",
    "PMID": 32081907.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Confocal microscopy of Congo Red-stained biofilms,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-Aβ mAb inhibits formation of S. Typhimurium biofilms\", \"Biofilms formed in cultures containing the other mAbs were substantially thinner, approaching the value for the csgBA mutant (5.5 µm): 4A6, 10.9 µm; 4G1, 7.3 µm; 2C10, 9.5 µm; and 3H3, 7.5 µm (Fig. 1b), with less surface coverage and CR staining (Fig. 1a).\", \"Figure 1\", \" Three of the four mAb-exposed samples had significantly reduced CR staining: 4G1 (23.9 RFU), 2C10 (22.1 RFU), and 3H3 (23.2 RFU), compared to the control and 6A samples (47.1 RFU and 48.1 RFU, respectively), although these were greater than the csgBA biofilm (7.91 RFU) (Fig. 1c).\",  \"In addition, 3H3 and 4G1 mAbs inhibited both curli and Aβ fibrillization, whereas 4A6 did not (Supplementary Fig. 2).\"",
    "Curator Statement": "UniProt Accession assigned to A0A0F6AZX4, as the strain used is derived from the 14028."
  },
  "AMGAB0328": {
    "Interaction ID": "AMGAB0328",
    "Antibody ID": "ABID0191",
    "Antibody name": "2C10",
    "Amyloid ID": "AGAMYID0025",
    "Amyloid name": "Curli",
    "DOI": "10.1038/s41467-020-14685-3",
    "PMID": 32081907.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Confocal microscopy of Congo Red-stained biofilms,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-Aβ mAb inhibits formation of S. Typhimurium biofilms\", \"Biofilms formed in cultures containing the other mAbs were substantially thinner, approaching the value for the csgBA mutant (5.5 µm): 4A6, 10.9 µm; 4G1, 7.3 µm; 2C10, 9.5 µm; and 3H3, 7.5 µm (Fig. 1b), with less surface coverage and CR staining (Fig. 1a).\", \"Figure 1\", \" Three of the four mAb-exposed samples had significantly reduced CR staining: 4G1 (23.9 RFU), 2C10 (22.1 RFU), and 3H3 (23.2 RFU), compared to the control and 6A samples (47.1 RFU and 48.1 RFU, respectively), although these were greater than the csgBA biofilm (7.91 RFU) (Fig. 1c).\",",
    "Curator Statement": "UniProt Accession assigned to A0A0F6AZX4, as the strain used is derived from the 14028."
  },
  "AMGAB0329": {
    "Interaction ID": "AMGAB0329",
    "Antibody ID": "ABID0192",
    "Antibody name": "6A",
    "Amyloid ID": "AGAMYID0025",
    "Amyloid name": "Curli",
    "DOI": "10.1038/s41467-020-14685-3",
    "PMID": 32081907.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro, in vivo",
    "Experimental method(s)": "Confocal microscopy of Congo Red-stained biofilms, crystal violet pellicle assay",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"The biofilm exposed to the control 6A antibody was similar to the untreated control, 18.21 µm thick and essentially confluent, although the depth of CR staining was reduced.\", \" Three of the four mAb-exposed samples had significantly reduced CR staining: 4G1 (23.9 RFU), 2C10 (22.1 RFU), and 3H3 (23.2 RFU), compared to the control and 6A samples (47.1 RFU and 48.1 RFU, respectively), although these were greater than the csgBA biofilm (7.91 RFU) (Fig. 1c).\", \"To test whether 3H3 affects curli fibrillization, we tested the synthetic peptides CsgAR4-5 and CsgAR4-5N122A and the protein BSA in vitro using the Thioflavin T (ThT) assay41. CsgAR4-5, which has the sequence of the fourth and fifth repeats of CsgA, self-associates and forms fibrils, whereas CsgAR4-5N122A contains a single amino acid substitution that prevents fibrillization42. Incubation of CsgAR4-5 in the presence of 3H3 significantly reduced the polymerization of CsgAR4-5 alone or incubated with the control antibody 6A (Supplementary Fig. 5A).\", \"Supplementary Figure 5\",",
    "Curator Statement": "UniProt Accession assigned to A0A0F6AZX4, as the strain used is derived from the 14028."
  },
  "AMGAB0330": {
    "Interaction ID": "AMGAB0330",
    "Antibody ID": "ABID0263",
    "Antibody name": "α-IAPP-O",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "Islet amyloid polypeptide (IAPP)",
    "DOI": "10.1038/s41467-023-41986-0",
    "PMID": 37813862.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro, In cellulo",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Dynamic Light Scattering, Immunohistochemistry",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Antibody treatment in male rats and mice transgenic for human IAPP, and human islet-engrafted mouse models of type 2 diabetes triggers clearance of IAPP oligomers resulting in beta cell protection and improved glucose control.\", \"In male rats and mice transgenic for human IAPP, and human islet-engrafted mouse models of T2D, α-IAPP-O triggers clearance of IAPP oligomers resulting in beta cell protection and improved glucose control.\", \"In both cases, model analysis indicates that α-IAPP-O concentration-dependently delayed fibril formation by inhibiting primary nucleation, with minimal effects on fibril-dependent processes such as elongation, secondary nucleation, and fragmentation (Fig. 2d,e and Supplementary Figs. 5 and 6).\", \"Figure 2\", \"Supplementary Figure 5\", \" Supplementary Figure 6\", \"α-IAPP-O concentration-dependently inhibits hIAPP assembly into amyloid fibrils.\", \"Fitting represented by solid lines is consistent with an effect of αIAPP-O on the product of fibril elongation and primary nucleation rate (k+kn) under both fragmentation- and secondary nucleation-dominated regimes (see also Figure 2d), but not on k+k and k+k2.\", \"α-IAPP-O inhibits primary nucleation.\", \"Consistent with selective inhibition of primary nucleation, a higher substoichiometric concentration of α-IAPP-O (10 hIAPP: 1 α-IAPP-O ratio) fully inhibited the formation of amyloid fibrils (Fig. 2g) by complexing pre-fibrillar oligomers with sizes ranging from 60 to 500 nm (Fig. 2h and Supplementary Fig. 7). Taken together, these data indicate that α-IAPP-O selectively targets hIAPP oligomers built at an early stage of the aggregation process (Supplementary Fig. 6e).\", \"Human islets were exposed to high glucose leading to the accumulation of extracellular ThioS-positive amyloid deposits and to beta cell apoptosis (Fig. 3h). Co-incubation with α-IAPP-O (0.5 µM) reduced ThioS-positive amyloid load and apoptotic beta cell death compared to IgG control.\",  \"Supplementary Figure 8\",  \"α-IAPP-O prevents the deposition of toxic hIAPP oligomers on INS-1 beta cells.\", \"α-IAPP-O variants inhibit hIAPP amyloid fibril formation.\", \"Supplementary Figure 10\", \"Neutralization of hIAPP oligomers by α-IAPP-O, a human monoclonal IgG1 antibody selectively binding extracellular hIAPP deposits in the pancreas of T2D patients and hIAPP intermediates produced during amyloid formation, prevented accumulation of amyloid fibrils, lipid membrane disruption and beta cell toxicity.\", \"We have also shown that α-IAPP-O interacts with the N-terminus of IAPP when self-assembled into oligomers and inhibits the formation of amyloid fibril end-product, supporting a key role of IAPP N-terminal residues in the initial aggregation process facilitating membrane interaction and permeation51.\", \"Although α-IAPP-O promoted the recruitment of macrophages at sites of amyloid deposition, we did not observe any effect on amyloid load, consistent with the selective binding of α-IAPP-O toward hIAPP oligomers but not amyloid fibrils.\", \"α-IAPP-O and its chimeric derivatives inhibited ThioS-positive amyloid fibril formation in vitro and prevented amyloid deposition on cultured INS-1 beta cells and human islets.\"",
    "Curator Statement": false
  },
  "AMGAB0331": {
    "Interaction ID": "AMGAB0331",
    "Antibody ID": "ABID0264",
    "Antibody name": "chα-IAPP-O",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "Islet amyloid polypeptide (IAPP)",
    "DOI": "10.1038/s41467-023-41986-0",
    "PMID": 37813862.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Histological Differentiation, Enzyme-Linked Immunosorbent Assay (ELISA)",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Antibody treatment had no effect on islet size, beta cell area and islet amyloid deposition as compared to vehicle-treated glucose intolerant rats (Supplementary Fig. 9d).\", \"Applying an isotype control antibody had no impact on glycemia in transgenic or wild-type rats (Supplementary Fig. 9e/f).\", \"chα-IAPP-O treatment was also associated with an increase in soluble IAPP levels and a decrease in insoluble IAPP aggregates in pancreas homogenates (Fig. 4l) that did not translate into reduced islet amyloid deposits stained by thioflavin-S (Supplementary Fig. 11h).\", \"α-IAPP-O removes extracellular hIAPP oligomers in transgenic rat islets\", \"α-IAPP-O and its chimeric derivatives inhibited ThioS-positive amyloid fibril formation in vitro and prevented amyloid deposition on cultured INS-1 beta cells and human islets.\",",
    "Curator Statement": false
  },
  "AMGAB0332": {
    "Interaction ID": "AMGAB0332",
    "Antibody ID": "ABID0196",
    "Antibody name": "VH14*PEST",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-018-0062-4",
    "PMID": 30155513.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"This study validates the proposition that both engineered nanobodies can reduce aggregation of α-syn and limit the expression of α-syn species phosphorylated at Serine-129 (p-S129) correlative of pathological aggregation.\", \"VH14*PEST and NbSyn87*PEST expression reduces pathologic aggregation of α-syn\", \"Figure 2\", \"Intrabody treatment also reduces the overall level of mature Lewy body-like cellular aggregates (inset) (scale bars: 100 and 25 μm).\", \"With Thioflavin-S staining of β-sheet aggregation, we confirmed p-S129-labeled species to be indicative of toxic aggregates and a representative marker for histopathology (Fig. 2c). Due to limited tissue material we were unable to appropriately quantify reductions in Thioflavin-S staining by stereology, although we were able to qualitatively observe reductions in aggregation in both intrabody-treated cohorts.\", \"We determined in previous in situ characterizations of these two candidate intrabodies that although NbSyn87*PEST clears α-syn more effectively than VH14*PEST, VH14*PEST modifies cellular stress associated with multi-factorial proteostasis to a greater extent, particularly in the case of α-syn promotion of mutant huntingtin proteinopathy.22 \",",
    "Curator Statement": false
  },
  "AMGAB0333": {
    "Interaction ID": "AMGAB0333",
    "Antibody ID": "ABID0197",
    "Antibody name": "NbSyn87*PEST",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-018-0062-4",
    "PMID": 30155513.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"This study validates the proposition that both engineered nanobodies can reduce aggregation of α-syn and limit the expression of α-syn species phosphorylated at Serine-129 (p-S129) correlative of pathological aggregation.\", \"VH14*PEST and NbSyn87*PEST expression reduces pathologic aggregation of α-syn\", \"Figure 2\", \"Intrabody treatment also reduces the overall level of mature Lewy body-like cellular aggregates (inset) (scale bars: 100 and 25 μm).\", \"With Thioflavin-S staining of β-sheet aggregation, we confirmed p-S129-labeled species to be indicative of toxic aggregates and a representative marker for histopathology (Fig. 2c). Due to limited tissue material we were unable to appropriately quantify reductions in Thioflavin-S staining by stereology, although we were able to qualitatively observe reductions in aggregation in both intrabody-treated cohorts.\", \"We determined in previous in situ characterizations of these two candidate intrabodies that although NbSyn87*PEST clears α-syn more effectively than VH14*PEST, VH14*PEST modifies cellular stress associated with multi-factorial proteostasis to a greater extent, particularly in the case of α-syn promotion of mutant huntingtin proteinopathy.22 \",",
    "Curator Statement": false
  },
  "AMGAB0334": {
    "Interaction ID": "AMGAB0334",
    "Antibody ID": "ABID0335",
    "Antibody name": "03-9H9",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Protofilaments, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0335": {
    "Interaction ID": "AMGAB0335",
    "Antibody ID": "ABID0335",
    "Antibody name": "03-9H9",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Protofilaments, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0336": {
    "Interaction ID": "AMGAB0336",
    "Antibody ID": "ABID0335",
    "Antibody name": "03-9H9",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Protofilaments, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0337": {
    "Interaction ID": "AMGAB0337",
    "Antibody ID": "ABID0336",
    "Antibody name": "06-10H11-B2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0338": {
    "Interaction ID": "AMGAB0338",
    "Antibody ID": "ABID0336",
    "Antibody name": "06-10H11-B2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0339": {
    "Interaction ID": "AMGAB0339",
    "Antibody ID": "ABID0336",
    "Antibody name": "06-10H11-B2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0340": {
    "Interaction ID": "AMGAB0340",
    "Antibody ID": "ABID0337",
    "Antibody name": "06-3A10-A1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0341": {
    "Interaction ID": "AMGAB0341",
    "Antibody ID": "ABID0337",
    "Antibody name": "06-3A10-A1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0342": {
    "Interaction ID": "AMGAB0342",
    "Antibody ID": "ABID0338",
    "Antibody name": "08-9E4-E3",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0343": {
    "Interaction ID": "AMGAB0343",
    "Antibody ID": "ABID0338",
    "Antibody name": "08-9E4-E3",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0344": {
    "Interaction ID": "AMGAB0344",
    "Antibody ID": "ABID0338",
    "Antibody name": "08-9E4-E3",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0345": {
    "Interaction ID": "AMGAB0345",
    "Antibody ID": "ABID0339",
    "Antibody name": "10-4A2-A2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"Of the 28 mAbs we tested (summarized in Table 2 columns I & J), 11 had no significant effect on α-syn fibrillation (t½ values 30–40 h within error), while 12 accelerated fibrillation to some extent (t½ values down to 13 ± 1 h) and five (antibodies 10-4A2-A2, 13-1F10-A2, 14-2B8-G1, 14-9E7-A1, 18-4G9-E3) slowed down fibrillation (t½ values up to 61 ± 12 h).\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",\"Figure 4\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0346": {
    "Interaction ID": "AMGAB0346",
    "Antibody ID": "ABID0339",
    "Antibody name": "10-4A2-A2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"Of the 28 mAbs we tested (summarized in Table 2 columns I & J), 11 had no significant effect on α-syn fibrillation (t½ values 30–40 h within error), while 12 accelerated fibrillation to some extent (t½ values down to 13 ± 1 h) and five (antibodies 10-4A2-A2, 13-1F10-A2, 14-2B8-G1, 14-9E7-A1, 18-4G9-E3) slowed down fibrillation (t½ values up to 61 ± 12 h).\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",\"Figure 4\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0347": {
    "Interaction ID": "AMGAB0347",
    "Antibody ID": "ABID0340",
    "Antibody name": "10-9C8-C1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0348": {
    "Interaction ID": "AMGAB0348",
    "Antibody ID": "ABID0340",
    "Antibody name": "10-9C8-C1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0349": {
    "Interaction ID": "AMGAB0349",
    "Antibody ID": "ABID0340",
    "Antibody name": "10-9C8-C1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0350": {
    "Interaction ID": "AMGAB0350",
    "Antibody ID": "ABID0341",
    "Antibody name": "13-1B2-B1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, seeded with preformed fibrils",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0351": {
    "Interaction ID": "AMGAB0351",
    "Antibody ID": "ABID0342",
    "Antibody name": "13-3H6-D2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, seeded with preformed fibrils",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0352": {
    "Interaction ID": "AMGAB0352",
    "Antibody ID": "ABID0342",
    "Antibody name": "13-3H6-D2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, seeded with preformed fibrils",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0353": {
    "Interaction ID": "AMGAB0353",
    "Antibody ID": "ABID0343",
    "Antibody name": "13-1F10-A2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"Of the 28 mAbs we tested (summarized in Table 2 columns I & J), 11 had no significant effect on α-syn fibrillation (t½ values 30–40 h within error), while 12 accelerated fibrillation to some extent (t½ values down to 13 ± 1 h) and five (antibodies 10-4A2-A2, 13-1F10-A2, 14-2B8-G1, 14-9E7-A1, 18-4G9-E3) slowed down fibrillation (t½ values up to 61 ± 12 h).\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0354": {
    "Interaction ID": "AMGAB0354",
    "Antibody ID": "ABID0344",
    "Antibody name": "14-1A6-F3",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0355": {
    "Interaction ID": "AMGAB0355",
    "Antibody ID": "ABID0344",
    "Antibody name": "14-1A6-F3",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0356": {
    "Interaction ID": "AMGAB0356",
    "Antibody ID": "ABID0344",
    "Antibody name": "14-1A6-F3",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0357": {
    "Interaction ID": "AMGAB0357",
    "Antibody ID": "ABID0345",
    "Antibody name": "14-1E2-E1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0358": {
    "Interaction ID": "AMGAB0358",
    "Antibody ID": "ABID0346",
    "Antibody name": "14-2B8-G1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"Of the 28 mAbs we tested (summarized in Table 2 columns I & J), 11 had no significant effect on α-syn fibrillation (t½ values 30–40 h within error), while 12 accelerated fibrillation to some extent (t½ values down to 13 ± 1 h) and five (antibodies 10-4A2-A2, 13-1F10-A2, 14-2B8-G1, 14-9E7-A1, 18-4G9-E3) slowed down fibrillation (t½ values up to 61 ± 12 h).\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0359": {
    "Interaction ID": "AMGAB0359",
    "Antibody ID": "ABID0346",
    "Antibody name": "14-2B8-G1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"Of the 28 mAbs we tested (summarized in Table 2 columns I & J), 11 had no significant effect on α-syn fibrillation (t½ values 30–40 h within error), while 12 accelerated fibrillation to some extent (t½ values down to 13 ± 1 h) and five (antibodies 10-4A2-A2, 13-1F10-A2, 14-2B8-G1, 14-9E7-A1, 18-4G9-E3) slowed down fibrillation (t½ values up to 61 ± 12 h).\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0360": {
    "Interaction ID": "AMGAB0360",
    "Antibody ID": "ABID0347",
    "Antibody name": "14-9E7-A1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"Of the 28 mAbs we tested (summarized in Table 2 columns I & J), 11 had no significant effect on α-syn fibrillation (t½ values 30–40 h within error), while 12 accelerated fibrillation to some extent (t½ values down to 13 ± 1 h) and five (antibodies 10-4A2-A2, 13-1F10-A2, 14-2B8-G1, 14-9E7-A1, 18-4G9-E3) slowed down fibrillation (t½ values up to 61 ± 12 h).\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0361": {
    "Interaction ID": "AMGAB0361",
    "Antibody ID": "ABID0347",
    "Antibody name": "14-9E7-A1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"Of the 28 mAbs we tested (summarized in Table 2 columns I & J), 11 had no significant effect on α-syn fibrillation (t½ values 30–40 h within error), while 12 accelerated fibrillation to some extent (t½ values down to 13 ± 1 h) and five (antibodies 10-4A2-A2, 13-1F10-A2, 14-2B8-G1, 14-9E7-A1, 18-4G9-E3) slowed down fibrillation (t½ values up to 61 ± 12 h).\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0362": {
    "Interaction ID": "AMGAB0362",
    "Antibody ID": "ABID0348",
    "Antibody name": "16-3B1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, seeded with preformed fibrils",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0363": {
    "Interaction ID": "AMGAB0363",
    "Antibody ID": "ABID0348",
    "Antibody name": "16-3B1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, seeded with preformed fibrils",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0364": {
    "Interaction ID": "AMGAB0364",
    "Antibody ID": "ABID0349",
    "Antibody name": "16-7B2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, seeded with preformed fibrils",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0365": {
    "Interaction ID": "AMGAB0365",
    "Antibody ID": "ABID0349",
    "Antibody name": "16-7B2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, seeded with preformed fibrils",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0366": {
    "Interaction ID": "AMGAB0366",
    "Antibody ID": "ABID0350",
    "Antibody name": "16-9E5",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0367": {
    "Interaction ID": "AMGAB0367",
    "Antibody ID": "ABID0350",
    "Antibody name": "16-9E5",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0368": {
    "Interaction ID": "AMGAB0368",
    "Antibody ID": "ABID0350",
    "Antibody name": "16-9E5",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0369": {
    "Interaction ID": "AMGAB0369",
    "Antibody ID": "ABID0351",
    "Antibody name": "17-5A8-H1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0370": {
    "Interaction ID": "AMGAB0370",
    "Antibody ID": "ABID0351",
    "Antibody name": "17-5A8-H1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0371": {
    "Interaction ID": "AMGAB0371",
    "Antibody ID": "ABID0351",
    "Antibody name": "17-5A8-H1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0372": {
    "Interaction ID": "AMGAB0372",
    "Antibody ID": "ABID0352",
    "Antibody name": "17-9D12-A1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0373": {
    "Interaction ID": "AMGAB0373",
    "Antibody ID": "ABID0352",
    "Antibody name": "17-9D12-A1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0374": {
    "Interaction ID": "AMGAB0374",
    "Antibody ID": "ABID0352",
    "Antibody name": "17-9D12-A1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0375": {
    "Interaction ID": "AMGAB0375",
    "Antibody ID": "ABID0353",
    "Antibody name": "18-3A5-H2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0376": {
    "Interaction ID": "AMGAB0376",
    "Antibody ID": "ABID0353",
    "Antibody name": "18-3A5-H2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0377": {
    "Interaction ID": "AMGAB0377",
    "Antibody ID": "ABID0353",
    "Antibody name": "18-3A5-H2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0378": {
    "Interaction ID": "AMGAB0378",
    "Antibody ID": "ABID0354",
    "Antibody name": "18-7B9-C10",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",\"In all cases, most of the α-syn was incorporated into fibrils, but several mAbs, in particular 18-4-G9, 18-7-B9, 19-1D2 and 20-9E2, retained a substantial amount of α-syn in solution (according to densitometric analysis with ImageJ, this corresponded to 0.15–0.2 mg/ml, i.e. 30-40% of the initial amount of α-syn) and also showed the lowest levels of ThT fluorescence. In other words, the two sets of observations are internally consistent: the antibodies that most reduce the level of fibrillation (according to ThT fluorescence) also lead to the highest amount of soluble α-syn.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0379": {
    "Interaction ID": "AMGAB0379",
    "Antibody ID": "ABID0354",
    "Antibody name": "18-7B9-C10",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",\"In all cases, most of the α-syn was incorporated into fibrils, but several mAbs, in particular 18-4-G9, 18-7-B9, 19-1D2 and 20-9E2, retained a substantial amount of α-syn in solution (according to densitometric analysis with ImageJ, this corresponded to 0.15–0.2 mg/ml, i.e. 30-40% of the initial amount of α-syn) and also showed the lowest levels of ThT fluorescence. In other words, the two sets of observations are internally consistent: the antibodies that most reduce the level of fibrillation (according to ThT fluorescence) also lead to the highest amount of soluble α-syn.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0380": {
    "Interaction ID": "AMGAB0380",
    "Antibody ID": "ABID0354",
    "Antibody name": "18-7B9-C10",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",\"In all cases, most of the α-syn was incorporated into fibrils, but several mAbs, in particular 18-4-G9, 18-7-B9, 19-1D2 and 20-9E2, retained a substantial amount of α-syn in solution (according to densitometric analysis with ImageJ, this corresponded to 0.15–0.2 mg/ml, i.e. 30-40% of the initial amount of α-syn) and also showed the lowest levels of ThT fluorescence. In other words, the two sets of observations are internally consistent: the antibodies that most reduce the level of fibrillation (according to ThT fluorescence) also lead to the highest amount of soluble α-syn.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0381": {
    "Interaction ID": "AMGAB0381",
    "Antibody ID": "ABID0355",
    "Antibody name": "18-9E10-B1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\", \"Figure 4\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0382": {
    "Interaction ID": "AMGAB0382",
    "Antibody ID": "ABID0355",
    "Antibody name": "18-9E10-B1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\", \"Figure 4\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0383": {
    "Interaction ID": "AMGAB0383",
    "Antibody ID": "ABID0355",
    "Antibody name": "18-9E10-B1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\", \"Figure 4\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0384": {
    "Interaction ID": "AMGAB0384",
    "Antibody ID": "ABID0356",
    "Antibody name": "19-1D2-F9",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",\"In all cases, most of the α-syn was incorporated into fibrils, but several mAbs, in particular 18-4-G9, 18-7-B9, 19-1D2 and 20-9E2, retained a substantial amount of α-syn in solution (according to densitometric analysis with ImageJ, this corresponded to 0.15–0.2 mg/ml, i.e. 30-40% of the initial amount of α-syn) and also showed the lowest levels of ThT fluorescence. In other words, the two sets of observations are internally consistent: the antibodies that most reduce the level of fibrillation (according to ThT fluorescence) also lead to the highest amount of soluble α-syn.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0385": {
    "Interaction ID": "AMGAB0385",
    "Antibody ID": "ABID0356",
    "Antibody name": "19-1D2-F9",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",\"In all cases, most of the α-syn was incorporated into fibrils, but several mAbs, in particular 18-4-G9, 18-7-B9, 19-1D2 and 20-9E2, retained a substantial amount of α-syn in solution (according to densitometric analysis with ImageJ, this corresponded to 0.15–0.2 mg/ml, i.e. 30-40% of the initial amount of α-syn) and also showed the lowest levels of ThT fluorescence. In other words, the two sets of observations are internally consistent: the antibodies that most reduce the level of fibrillation (according to ThT fluorescence) also lead to the highest amount of soluble α-syn.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0386": {
    "Interaction ID": "AMGAB0386",
    "Antibody ID": "ABID0356",
    "Antibody name": "19-1D2-F9",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",\"In all cases, most of the α-syn was incorporated into fibrils, but several mAbs, in particular 18-4-G9, 18-7-B9, 19-1D2 and 20-9E2, retained a substantial amount of α-syn in solution (according to densitometric analysis with ImageJ, this corresponded to 0.15–0.2 mg/ml, i.e. 30-40% of the initial amount of α-syn) and also showed the lowest levels of ThT fluorescence. In other words, the two sets of observations are internally consistent: the antibodies that most reduce the level of fibrillation (according to ThT fluorescence) also lead to the highest amount of soluble α-syn.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0387": {
    "Interaction ID": "AMGAB0387",
    "Antibody ID": "ABID0357",
    "Antibody name": "19-2C3-F10",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",\"Figure 4\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0388": {
    "Interaction ID": "AMGAB0388",
    "Antibody ID": "ABID0357",
    "Antibody name": "19-2C3-F10",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",\"Figure 4\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0389": {
    "Interaction ID": "AMGAB0389",
    "Antibody ID": "ABID0357",
    "Antibody name": "19-2C3-F10",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",\"Figure 4\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0390": {
    "Interaction ID": "AMGAB0390",
    "Antibody ID": "ABID0358",
    "Antibody name": "20-5H12-C10",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0391": {
    "Interaction ID": "AMGAB0391",
    "Antibody ID": "ABID0358",
    "Antibody name": "20-5H12-C10",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0392": {
    "Interaction ID": "AMGAB0392",
    "Antibody ID": "ABID0358",
    "Antibody name": "20-5H12-C10",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0393": {
    "Interaction ID": "AMGAB0393",
    "Antibody ID": "ABID0359",
    "Antibody name": "21-4G12-C12",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "No effect,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0394": {
    "Interaction ID": "AMGAB0394",
    "Antibody ID": "ABID0359",
    "Antibody name": "21-4G12-C12",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0395": {
    "Interaction ID": "AMGAB0395",
    "Antibody ID": "ABID0359",
    "Antibody name": "21-4G12-C12",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0396": {
    "Interaction ID": "AMGAB0396",
    "Antibody ID": "ABID0360",
    "Antibody name": "21-9H11-D11",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "No effect,",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0397": {
    "Interaction ID": "AMGAB0397",
    "Antibody ID": "ABID0360",
    "Antibody name": "21-9H11-D11",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0398": {
    "Interaction ID": "AMGAB0398",
    "Antibody ID": "ABID0360",
    "Antibody name": "21-9H11-D11",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0399": {
    "Interaction ID": "AMGAB0399",
    "Antibody ID": "ABID0361",
    "Antibody name": "18-4G9-E3",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"Of the 28 mAbs we tested (summarized in Table 2 columns I & J), 11 had no significant effect on α-syn fibrillation (t½ values 30–40 h within error), while 12 accelerated fibrillation to some extent (t½ values down to 13 ± 1 h) and five (antibodies 10-4A2-A2, 13-1F10-A2, 14-2B8-G1, 14-9E7-A1, 18-4G9-E3) slowed down fibrillation (t½ values up to 61 ± 12 h).\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\", \"In all cases, most of the α-syn was incorporated into fibrils, but several mAbs, in particular 18-4-G9, 18-7-B9, 19-1D2 and 20-9E2, retained a substantial amount of α-syn in solution (according to densitometric analysis with ImageJ, this corresponded to 0.15–0.2 mg/ml, i.e. 30-40% of the initial amount of α-syn) and also showed the lowest levels of ThT fluorescence. In other words, the two sets of observations are internally consistent: the antibodies that most reduce the level of fibrillation (according to ThT fluorescence) also lead to the highest amount of soluble α-syn.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0400": {
    "Interaction ID": "AMGAB0400",
    "Antibody ID": "ABID0361",
    "Antibody name": "18-4G9-E3",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"Of the 28 mAbs we tested (summarized in Table 2 columns I & J), 11 had no significant effect on α-syn fibrillation (t½ values 30–40 h within error), while 12 accelerated fibrillation to some extent (t½ values down to 13 ± 1 h) and five (antibodies 10-4A2-A2, 13-1F10-A2, 14-2B8-G1, 14-9E7-A1, 18-4G9-E3) slowed down fibrillation (t½ values up to 61 ± 12 h).\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\", \"In all cases, most of the α-syn was incorporated into fibrils, but several mAbs, in particular 18-4-G9, 18-7-B9, 19-1D2 and 20-9E2, retained a substantial amount of α-syn in solution (according to densitometric analysis with ImageJ, this corresponded to 0.15–0.2 mg/ml, i.e. 30-40% of the initial amount of α-syn) and also showed the lowest levels of ThT fluorescence. In other words, the two sets of observations are internally consistent: the antibodies that most reduce the level of fibrillation (according to ThT fluorescence) also lead to the highest amount of soluble α-syn.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0401": {
    "Interaction ID": "AMGAB0401",
    "Antibody ID": "ABID0362",
    "Antibody name": "03-8C4",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, seeded  with preformed fibrils",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0402": {
    "Interaction ID": "AMGAB0402",
    "Antibody ID": "ABID0362",
    "Antibody name": "03-8C4",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": false,
    "Experimental method(s)": "ThT - Aggregation kinetics, seeded  with preformed fibrils",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0403": {
    "Interaction ID": "AMGAB0403",
    "Antibody ID": "ABID0363",
    "Antibody name": "20-9E2-B8",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, seeded with preformed fibrils",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\", \"In all cases, most of the α-syn was incorporated into fibrils, but several mAbs, in particular 18-4-G9, 18-7-B9, 19-1D2 and 20-9E2, retained a substantial amount of α-syn in solution (according to densitometric analysis with ImageJ, this corresponded to 0.15–0.2 mg/ml, i.e. 30-40% of the initial amount of α-syn) and also showed the lowest levels of ThT fluorescence. In other words, the two sets of observations are internally consistent: the antibodies that most reduce the level of fibrillation (according to ThT fluorescence) also lead to the highest amount of soluble α-syn.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0404": {
    "Interaction ID": "AMGAB0404",
    "Antibody ID": "ABID0363",
    "Antibody name": "20-9E2-B8",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/s41531-024-00747-6",
    "PMID": 39075088.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, seeded with preformed fibrils",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"However, the modest spread in effects suggests that the antibodies do not have strong affinity for species that are critical for fibrillation, e.g. monomers, nuclei, or growing ends of fibrils.\", \"In all cases, most of the α-syn was incorporated into fibrils, but several mAbs, in particular 18-4-G9, 18-7-B9, 19-1D2 and 20-9E2, retained a substantial amount of α-syn in solution (according to densitometric analysis with ImageJ, this corresponded to 0.15–0.2 mg/ml, i.e. 30-40% of the initial amount of α-syn) and also showed the lowest levels of ThT fluorescence. In other words, the two sets of observations are internally consistent: the antibodies that most reduce the level of fibrillation (according to ThT fluorescence) also lead to the highest amount of soluble α-syn.\",",
    "Curator Statement": "From Table 2: Column I and J are interpreted as reports of speed of aggregation (seeded and unseeded), and column K, plateau ThT flourescence, as amyloid quantity. Error margin of 10% in colimn I is considered."
  },
  "AMGAB0405": {
    "Interaction ID": "AMGAB0405",
    "Antibody ID": "ABID0001.6",
    "Antibody name": "mAducanumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41586-021-03489-0",
    "PMID": 33911285.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Treatments with mAducanumab or mAb158 proved to be efficient in reducing the density of Aβ plaques (Fig. 1b, c and Extended Data Fig. 3g, h).\", Figure 1\", \"Extended Data Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0406": {
    "Interaction ID": "AMGAB0406",
    "Antibody ID": "ABID0006.5",
    "Antibody name": "mAb158",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41586-021-03489-0",
    "PMID": 33911285.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Treatments with mAducanumab or mAb158 proved to be efficient in reducing the density of Aβ plaques (Fig. 1b, c and Extended Data Fig. 3g, h).\", Figure 1\", \"Extended Data Figure 3\", \"The reduction in Aβ load and microgliosis in 5xFAD mice treated with mVEGF-C and mAb158 was accompanied by an expansion of lymphatic vasculature around the transverse sinus (Extended Data Fig. 7h–m).\",",
    "Curator Statement": false
  },
  "AMGAB0407": {
    "Interaction ID": "AMGAB0407",
    "Antibody ID": "ABID0001.6.3",
    "Antibody name": "cmAducanumab",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "Mature fibrils, Protofibrils,",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"(c) Measurement of the Triton-soluble Aβx-40 and Aβx-42 did not indicate any differences among the groups (Kruskal-Wallis-Test; Aβx-40, H(3)=1.718; P=0.6329; Aβx-42, H(3)=0.4967; P=0.9196). In contrast, FA-soluble Aβx-40 and Aβx-42 appeared to be reduced in cmAdu-treated mice although the reduction did not reach statistical significance (one-way ANOVA: Aβx-40, F(3,29)=2.360, P=0.0920; Aβx-42, F(3,29)=3.0170, P=0.0459, subsequent post hoc Dunnettś multiple comparisons test did not indicate a difference between the combined Ctrl1/2 and any treatment group).\", \"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0408": {
    "Interaction ID": "AMGAB0408",
    "Antibody ID": "ABID0001.6.3",
    "Antibody name": "cmAducanumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "Mature fibrils, Protofibrils,",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"However, in the mice that received the chimeric murinized (cm) version of Aducanumab (cmAducanumab), Aβ was markedly reduced in the formic-acid soluble fraction (Fig. 1c). For Aβ42 (the Aβ species ending with amino acid 42) the reduction reached 50%. To probe whether cmAducanumab indeed removed early Aβ seeds, a well-established in vivo seeding assay was performed11, i.e., minute amounts of brain homogenates from the cmAducanumab- and control antibody-treated mice were infused into young, 3-month-old APP23 mice (Fig. 1d). While brain extract from the control antibody-treated mice strongly seeded Aβ deposition in the host mice 8 months later, seeding activity was reduced by more than 80% in the brain extract from the cmAducanumab-treated mice (Fig. 1d).\", \"Figure 1\", \"Kruskal-Wallis-Test indicated no group differences for the Triton-extracted Aβ (Aβx-40, H(6)=8.865, P=0.1813; Aβx-42, H(6)=14.84, P=0.0215; no significant group differences between controls and any other group with post hoc Dunn’s multiple comparison).\", \"For FA-extracted Aβ, group differences were found for Aβx-42 (H(6)=14.73; P=0.0225, post hoc Dunn’s multiple comparison test between cmAdu-injected mice and controls, P=0.006). \", \"(d) Brain homogenates from cmAdu- and Ctrl2-treated (7.5-month-old) mice were inoculated into the hippocampus of 3-month-old male APP23 hosts. After an 8-month incubation period, the brain homogenate of cmAdu-treated mice induced markedly less Aβ deposition (n=7 for both cmAdu and Ctrl2, two-tailed unpaired t-test; t(12)=3.726; P=0.003).\", \"Brain PBS homogenates of all 8 cmAdu- and 8 Ctrl2-treated mice were pooled. Homogenates were examined with ARPA (see Fig. 2 for a description of the ARPA methodology) using Beta1 antibody as capture antibody to pull down Aβ. Beta1 was used since it recognizes all Aβ species fairly equally in this assay (see Fig. 2). Note the faint bands in the higher molecular fractions in the Ctrl2-treated mice that appear diminished in the cmAdu-treated mice.\", \"Figure 3\",\"(c) Measurement of the Triton-soluble Aβx-40 and Aβx-42 did not indicate any differences among the groups (Kruskal-Wallis-Test; Aβx-40, H(3)=1.718; P=0.6329; Aβx-42, H(3)=0.4967; P=0.9196). In contrast, FA-soluble Aβx-40 and Aβx-42 appeared to be reduced in cmAdu-treated mice although the reduction did not reach statistical significance (one-way ANOVA: Aβx-40, F(3,29)=2.360, P=0.0920; Aβx-42, F(3,29)=3.0170, P=0.0459, subsequent post hoc Dunnettś multiple comparisons test did not indicate a difference between the combined Ctrl1/2 and any treatment group).\", \"Figure 5\", \" An even larger reduction was found for plaque number (ANOVA: F(3,29)=12.35; P<0.0001; post hoc Dunnettś multiple comparisons test: P=0.0007). Plaque size was also reduced, but to a lesser extent (ANOVA: F(3,29)=3.6320; P=0.0247; post hoc Dunnettś multiple comparisons test: P=0.0268). The amount of CAA was not significantly different in antibody-treated mice, although two mice treated with cmAdu and three treated with m266 had relatively high CAA counts.\", \"(f) Staining of amyloid with the combination of two (qFTAA and hFTAA) luminescent conjugated oligothiophenes (LCOs). The number of total LCO-positive cortical plaques was again lower in cmAdu-treated mice vs controls (Kruskal-Wallis-Test: H(3)=19,11; P=0.0003; Dunn’s multiple comparison P=0.0013)\",  \"Strikingly, while m266- and Beta1-treated animals did not differ in any measure relative to control antibody-treated mice, both FA-extracted Aβ and immunohistochemically-detected Aβ deposits were reduced (35% and 67%, respectively) in mice receiving a single, 5-day regimen of cmAducanumab 6 months earlier (Fig. 5c, d). Further quantitative histopathological analyses indicated that the treatment mainly reduced the number of Aβ plaques (86%), whereas the average size of plaques was only decreased by 17% (Fig. 5d, e). The deposition of Aβ in the vasculature (cerebral β-amyloid angiopathy, CAA) was not lowered by antibody treatment, and in some cmAducanumab- and m266-treated mice even appeared to have increased (Fig. 5d). However, no old or recent CAA-associated hemorrhages were detected in any of the groups using the Perls stain for iron or hematoxylin and eosin, respectively.\", \" While a similar reduction of cortical plaque number was found with these amyloid dyes compared to immunohistochemical staining, amyloid in the cmAducanumab-treated mice had different fluorescence emission characteristics, suggestive of less mature plaques compared to those in the control-antibody treated mice (Fig. 5f)21.\", \"The finding that acutely targeting such early Aβ seeds for only 5 days leads to a significant reduction of Aβ deposition and associated pathologies 6 months later suggests that the formation of Aβ seeds at this time already strongly influences the extent of cerebral β-amyloidosis much later in life.\", \"Of potential concern for the translation of the present results into clinical applications is the finding that cmAducanumab did not reduce CAA. The same was reported when amyloid-bearing APP-transgenic mice were passively immunized with cmAducanumab, i.e. a reduction of plaques but not CAA was found29.\",",
    "Curator Statement": false
  },
  "AMGAB0409": {
    "Interaction ID": "AMGAB0409",
    "Antibody ID": "ABID0001.6.3",
    "Antibody name": "cmAducanumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "Mature fibrils, Protofibrils,",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the tested antibodies altered Aβ levels in the Triton-soluble fraction.\", \"Figure 1\", \"Kruskal-Wallis-Test indicated no group differences for the Triton-extracted Aβ (Aβx-40, H(6)=8.865, P=0.1813; Aβx-42, H(6)=14.84, P=0.0215; no significant group differences between controls and any other group with post hoc Dunn’s multiple comparison).\", \"Figure 3\",\"(c) Measurement of the Triton-soluble Aβx-40 and Aβx-42 did not indicate any differences among the groups (Kruskal-Wallis-Test; Aβx-40, H(3)=1.718; P=0.6329; Aβx-42, H(3)=0.4967; P=0.9196). In contrast, FA-soluble Aβx-40 and Aβx-42 appeared to be reduced in cmAdu-treated mice although the reduction did not reach statistical significance (one-way ANOVA: Aβx-40, F(3,29)=2.360, P=0.0920; Aβx-42, F(3,29)=3.0170, P=0.0459, subsequent post hoc Dunnettś multiple comparisons test did not indicate a difference between the combined Ctrl1/2 and any treatment group).\",",
    "Curator Statement": "Overall decrease amyloid in most reporters, althoigh no difference in the Triton-soluble homogenate levels."
  },
  "AMGAB0410": {
    "Interaction ID": "AMGAB0410",
    "Antibody ID": "ABID0002.9",
    "Antibody name": "cmGantenerumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Protein monomer, Mature fibrils, Protofibrils,",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the tested antibodies altered Aβ levels in the Triton-soluble fraction.\", \"Figure 1\", \"Kruskal-Wallis-Test indicated no group differences for the Triton-extracted Aβ (Aβx-40, H(6)=8.865, P=0.1813; Aβx-42, H(6)=14.84, P=0.0215; no significant group differences between controls and any other group with post hoc Dunn’s multiple comparison).\", \" Whereas cmAducanumab and mE8 recognize almost exclusively larger Aβ assemblies, all other antibodies tested in the present study also recognize monomeric Aβ, which may explain why they failed to impede Aβ seeds in the present study (although we only tested the IgG1 version of cmGantenerumab, whose effector function is reduced in mice30,31).\",",
    "Curator Statement": false
  },
  "AMGAB0411": {
    "Interaction ID": "AMGAB0411",
    "Antibody ID": "ABID0003.5",
    "Antibody name": "mE8",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Mature fibrils, Protofibrils,",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the tested antibodies altered Aβ levels in the Triton-soluble fraction.\", \"Figure 1\", \"Kruskal-Wallis-Test indicated no group differences for the Triton-extracted Aβ (Aβx-40, H(6)=8.865, P=0.1813; Aβx-42, H(6)=14.84, P=0.0215; no significant group differences between controls and any other group with post hoc Dunn’s multiple comparison).\", \"This might explain why mE8 did not inhibit early seeds in the present study despite showing an ARPA profile almost identical to cmAducanumab in end-stage AD and transgenic mouse brains.\",",
    "Curator Statement": false
  },
  "AMGAB0412": {
    "Interaction ID": "AMGAB0412",
    "Antibody ID": "ABID0004.5",
    "Antibody name": "mC2",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Protein monomer, Mature fibrils, Protofibrils,",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the tested antibodies altered Aβ levels in the Triton-soluble fraction.\", \"Figure 1\", \"Kruskal-Wallis-Test indicated no group differences for the Triton-extracted Aβ (Aβx-40, H(6)=8.865, P=0.1813; Aβx-42, H(6)=14.84, P=0.0215; no significant group differences between controls and any other group with post hoc Dunn’s multiple comparison).\", \" Whereas cmAducanumab and mE8 recognize almost exclusively larger Aβ assemblies, all other antibodies tested in the present study also recognize monomeric Aβ, which may explain why they failed to impede Aβ seeds in the present study (although we only tested the IgG1 version of cmGantenerumab, whose effector function is reduced in mice30,31).\",",
    "Curator Statement": false
  },
  "AMGAB0413": {
    "Interaction ID": "AMGAB0413",
    "Antibody ID": "ABID0005.5",
    "Antibody name": "m266",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"(c) Measurement of the Triton-soluble Aβx-40 and Aβx-42 did not indicate any differences among the groups (Kruskal-Wallis-Test; Aβx-40, H(3)=1.718; P=0.6329; Aβx-42, H(3)=0.4967; P=0.9196). In contrast, FA-soluble Aβx-40 and Aβx-42 appeared to be reduced in cmAdu-treated mice although the reduction did not reach statistical significance (one-way ANOVA: Aβx-40, F(3,29)=2.360, P=0.0920; Aβx-42, F(3,29)=3.0170, P=0.0459, subsequent post hoc Dunnettś multiple comparisons test did not indicate a difference between the combined Ctrl1/2 and any treatment group).\", \"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0414": {
    "Interaction ID": "AMGAB0414",
    "Antibody ID": "ABID0005.5",
    "Antibody name": "m266",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "No effect, Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the tested antibodies altered Aβ levels in the Triton-soluble fraction.\", \"Figure 1\", \"Kruskal-Wallis-Test indicated no group differences for the Triton-extracted Aβ (Aβx-40, H(6)=8.865, P=0.1813; Aβx-42, H(6)=14.84, P=0.0215; no significant group differences between controls and any other group with post hoc Dunn’s multiple comparison).\", \"(c) Measurement of the Triton-soluble Aβx-40 and Aβx-42 did not indicate any differences among the groups (Kruskal-Wallis-Test; Aβx-40, H(3)=1.718; P=0.6329; Aβx-42, H(3)=0.4967; P=0.9196). In contrast, FA-soluble Aβx-40 and Aβx-42 appeared to be reduced in cmAdu-treated mice although the reduction did not reach statistical significance (one-way ANOVA: Aβx-40, F(3,29)=2.360, P=0.0920; Aβx-42, F(3,29)=3.0170, P=0.0459, subsequent post hoc Dunnettś multiple comparisons test did not indicate a difference between the combined Ctrl1/2 and any treatment group).\", \"Figure 5\", \"Strikingly, while m266- and Beta1-treated animals did not differ in any measure relative to control antibody-treated mice, both FA-extracted Aβ and immunohistochemically-detected Aβ deposits were reduced (35% and 67%, respectively) in mice receiving a single, 5-day regimen of cmAducanumab 6 months earlier (Fig. 5c, d). Further quantitative histopathological analyses indicated that the treatment mainly reduced the number of Aβ plaques (86%), whereas the average size of plaques was only decreased by 17% (Fig. 5d, e). The deposition of Aβ in the vasculature (cerebral β-amyloid angiopathy, CAA) was not lowered by antibody treatment, and in some cmAducanumab- and m266-treated mice even appeared to have increased (Fig. 5d). However, no old or recent CAA-associated hemorrhages were detected in any of the groups using the Perls stain for iron or hematoxylin and eosin, respectively.\", \" Whereas cmAducanumab and mE8 recognize almost exclusively larger Aβ assemblies, all other antibodies tested in the present study also recognize monomeric Aβ, which may explain why they failed to impede Aβ seeds in the present study (although we only tested the IgG1 version of cmGantenerumab, whose effector function is reduced in mice30,31).\",",
    "Curator Statement": false
  },
  "AMGAB0415": {
    "Interaction ID": "AMGAB0415",
    "Antibody ID": "ABID0320",
    "Antibody name": "anti-wheat auxin",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"(c) Measurement of the Triton-soluble Aβx-40 and Aβx-42 did not indicate any differences among the groups (Kruskal-Wallis-Test; Aβx-40, H(3)=1.718; P=0.6329; Aβx-42, H(3)=0.4967; P=0.9196). In contrast, FA-soluble Aβx-40 and Aβx-42 appeared to be reduced in cmAdu-treated mice although the reduction did not reach statistical significance (one-way ANOVA: Aβx-40, F(3,29)=2.360, P=0.0920; Aβx-42, F(3,29)=3.0170, P=0.0459, subsequent post hoc Dunnettś multiple comparisons test did not indicate a difference between the combined Ctrl1/2 and any treatment group).\", \"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0416": {
    "Interaction ID": "AMGAB0416",
    "Antibody ID": "ABID0320",
    "Antibody name": "anti-wheat auxin",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"None of the tested antibodies altered Aβ levels in the Triton-soluble fraction.\", \"Figure 1\", \"Kruskal-Wallis-Test indicated no group differences for the Triton-extracted Aβ (Aβx-40, H(6)=8.865, P=0.1813; Aβx-42, H(6)=14.84, P=0.0215; no significant group differences between controls and any other group with post hoc Dunn’s multiple comparison).\", \"(c) Measurement of the Triton-soluble Aβx-40 and Aβx-42 did not indicate any differences among the groups (Kruskal-Wallis-Test; Aβx-40, H(3)=1.718; P=0.6329; Aβx-42, H(3)=0.4967; P=0.9196). In contrast, FA-soluble Aβx-40 and Aβx-42 appeared to be reduced in cmAdu-treated mice although the reduction did not reach statistical significance (one-way ANOVA: Aβx-40, F(3,29)=2.360, P=0.0920; Aβx-42, F(3,29)=3.0170, P=0.0459, subsequent post hoc Dunnettś multiple comparisons test did not indicate a difference between the combined Ctrl1/2 and any treatment group).\", \"Figure 5\", \" An even larger reduction was found for plaque number (ANOVA: F(3,29)=12.35; P<0.0001; post hoc Dunnettś multiple comparisons test: P=0.0007). Plaque size was also reduced, but to a lesser extent (ANOVA: F(3,29)=3.6320; P=0.0247; post hoc Dunnettś multiple comparisons test: P=0.0268). The amount of CAA was not significantly different in antibody-treated mice, although two mice treated with cmAdu and three treated with m266 had relatively high CAA counts.\", \"(f) Staining of amyloid with the combination of two (qFTAA and hFTAA) luminescent conjugated oligothiophenes (LCOs). The number of total LCO-positive cortical plaques was again lower in cmAdu-treated mice vs controls (Kruskal-Wallis-Test: H(3)=19,11; P=0.0003; Dunn’s multiple comparison P=0.0013)\", \"Strikingly, while m266- and Beta1-treated animals did not differ in any measure relative to control antibody-treated mice, both FA-extracted Aβ and immunohistochemically-detected Aβ deposits were reduced (35% and 67%, respectively) in mice receiving a single, 5-day regimen of cmAducanumab 6 months earlier (Fig. 5c, d). Further quantitative histopathological analyses indicated that the treatment mainly reduced the number of Aβ plaques (86%), whereas the average size of plaques was only decreased by 17% (Fig. 5d, e). The deposition of Aβ in the vasculature (cerebral β-amyloid angiopathy, CAA) was not lowered by antibody treatment, and in some cmAducanumab- and m266-treated mice even appeared to have increased (Fig. 5d). However, no old or recent CAA-associated hemorrhages were detected in any of the groups using the Perls stain for iron or hematoxylin and eosin, respectively.\",",
    "Curator Statement": false
  },
  "AMGAB0417": {
    "Interaction ID": "AMGAB0417",
    "Antibody ID": "ABID0321",
    "Antibody name": "P1.17",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"(c) Measurement of the Triton-soluble Aβx-40 and Aβx-42 did not indicate any differences among the groups (Kruskal-Wallis-Test; Aβx-40, H(3)=1.718; P=0.6329; Aβx-42, H(3)=0.4967; P=0.9196). In contrast, FA-soluble Aβx-40 and Aβx-42 appeared to be reduced in cmAdu-treated mice although the reduction did not reach statistical significance (one-way ANOVA: Aβx-40, F(3,29)=2.360, P=0.0920; Aβx-42, F(3,29)=3.0170, P=0.0459, subsequent post hoc Dunnettś multiple comparisons test did not indicate a difference between the combined Ctrl1/2 and any treatment group).\", \"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0418": {
    "Interaction ID": "AMGAB0418",
    "Antibody ID": "ABID0321",
    "Antibody name": "P1.17",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"None of the tested antibodies altered Aβ levels in the Triton-soluble fraction.\", \"Figure 1\", \"Kruskal-Wallis-Test indicated no group differences for the Triton-extracted Aβ (Aβx-40, H(6)=8.865, P=0.1813; Aβx-42, H(6)=14.84, P=0.0215; no significant group differences between controls and any other group with post hoc Dunn’s multiple comparison).\", \"(c) Measurement of the Triton-soluble Aβx-40 and Aβx-42 did not indicate any differences among the groups (Kruskal-Wallis-Test; Aβx-40, H(3)=1.718; P=0.6329; Aβx-42, H(3)=0.4967; P=0.9196). In contrast, FA-soluble Aβx-40 and Aβx-42 appeared to be reduced in cmAdu-treated mice although the reduction did not reach statistical significance (one-way ANOVA: Aβx-40, F(3,29)=2.360, P=0.0920; Aβx-42, F(3,29)=3.0170, P=0.0459, subsequent post hoc Dunnettś multiple comparisons test did not indicate a difference between the combined Ctrl1/2 and any treatment group).\", \"Figure 5\", \" An even larger reduction was found for plaque number (ANOVA: F(3,29)=12.35; P<0.0001; post hoc Dunnettś multiple comparisons test: P=0.0007). Plaque size was also reduced, but to a lesser extent (ANOVA: F(3,29)=3.6320; P=0.0247; post hoc Dunnettś multiple comparisons test: P=0.0268). The amount of CAA was not significantly different in antibody-treated mice, although two mice treated with cmAdu and three treated with m266 had relatively high CAA counts.\", \"(f) Staining of amyloid with the combination of two (qFTAA and hFTAA) luminescent conjugated oligothiophenes (LCOs). The number of total LCO-positive cortical plaques was again lower in cmAdu-treated mice vs controls (Kruskal-Wallis-Test: H(3)=19,11; P=0.0003; Dunn’s multiple comparison P=0.0013)\", \"Strikingly, while m266- and Beta1-treated animals did not differ in any measure relative to control antibody-treated mice, both FA-extracted Aβ and immunohistochemically-detected Aβ deposits were reduced (35% and 67%, respectively) in mice receiving a single, 5-day regimen of cmAducanumab 6 months earlier (Fig. 5c, d). Further quantitative histopathological analyses indicated that the treatment mainly reduced the number of Aβ plaques (86%), whereas the average size of plaques was only decreased by 17% (Fig. 5d, e). The deposition of Aβ in the vasculature (cerebral β-amyloid angiopathy, CAA) was not lowered by antibody treatment, and in some cmAducanumab- and m266-treated mice even appeared to have increased (Fig. 5d). However, no old or recent CAA-associated hemorrhages were detected in any of the groups using the Perls stain for iron or hematoxylin and eosin, respectively.\",",
    "Curator Statement": false
  },
  "AMGAB0419": {
    "Interaction ID": "AMGAB0419",
    "Antibody ID": "ABID0322",
    "Antibody name": "β1",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Protein monomer, Mature fibrils, Protofibrils, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the tested antibodies altered Aβ levels in the Triton-soluble fraction.\", \"Figure 1\", \"Kruskal-Wallis-Test indicated no group differences for the Triton-extracted Aβ (Aβx-40, H(6)=8.865, P=0.1813; Aβx-42, H(6)=14.84, P=0.0215; no significant group differences between controls and any other group with post hoc Dunn’s multiple comparison).\", \"(c) Measurement of the Triton-soluble Aβx-40 and Aβx-42 did not indicate any differences among the groups (Kruskal-Wallis-Test; Aβx-40, H(3)=1.718; P=0.6329; Aβx-42, H(3)=0.4967; P=0.9196). In contrast, FA-soluble Aβx-40 and Aβx-42 appeared to be reduced in cmAdu-treated mice although the reduction did not reach statistical significance (one-way ANOVA: Aβx-40, F(3,29)=2.360, P=0.0920; Aβx-42, F(3,29)=3.0170, P=0.0459, subsequent post hoc Dunnettś multiple comparisons test did not indicate a difference between the combined Ctrl1/2 and any treatment group).\", \"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0420": {
    "Interaction ID": "AMGAB0420",
    "Antibody ID": "ABID0322",
    "Antibody name": "β1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41593-020-00737-w",
    "PMID": 33199898.0,
    "Impact of the antibody on amyloid formation": "No effect, Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Protein monomer, Mature fibrils, Protofibrils, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the tested antibodies altered Aβ levels in the Triton-soluble fraction.\", \"Figure 1\", \"Kruskal-Wallis-Test indicated no group differences for the Triton-extracted Aβ (Aβx-40, H(6)=8.865, P=0.1813; Aβx-42, H(6)=14.84, P=0.0215; no significant group differences between controls and any other group with post hoc Dunn’s multiple comparison).\", \"(c) Measurement of the Triton-soluble Aβx-40 and Aβx-42 did not indicate any differences among the groups (Kruskal-Wallis-Test; Aβx-40, H(3)=1.718; P=0.6329; Aβx-42, H(3)=0.4967; P=0.9196). In contrast, FA-soluble Aβx-40 and Aβx-42 appeared to be reduced in cmAdu-treated mice although the reduction did not reach statistical significance (one-way ANOVA: Aβx-40, F(3,29)=2.360, P=0.0920; Aβx-42, F(3,29)=3.0170, P=0.0459, subsequent post hoc Dunnettś multiple comparisons test did not indicate a difference between the combined Ctrl1/2 and any treatment group).\", \"Figure 5\", \"Strikingly, while m266- and Beta1-treated animals did not differ in any measure relative to control antibody-treated mice, both FA-extracted Aβ and immunohistochemically-detected Aβ deposits were reduced (35% and 67%, respectively) in mice receiving a single, 5-day regimen of cmAducanumab 6 months earlier (Fig. 5c, d). Further quantitative histopathological analyses indicated that the treatment mainly reduced the number of Aβ plaques (86%), whereas the average size of plaques was only decreased by 17% (Fig. 5d, e). The deposition of Aβ in the vasculature (cerebral β-amyloid angiopathy, CAA) was not lowered by antibody treatment, and in some cmAducanumab- and m266-treated mice even appeared to have increased (Fig. 5d). However, no old or recent CAA-associated hemorrhages were detected in any of the groups using the Perls stain for iron or hematoxylin and eosin, respectively.\", \" Whereas cmAducanumab and mE8 recognize almost exclusively larger Aβ assemblies, all other antibodies tested in the present study also recognize monomeric Aβ, which may explain why they failed to impede Aβ seeds in the present study (although we only tested the IgG1 version of cmGantenerumab, whose effector function is reduced in mice30,31).\", \"The reasons that Beta1 inactivates exogenously applied seeds efficiently (e.g.14), but was ineffective against endogenous seeds, could then also be explained by a much higher ratio of seeds to monomeric Aβ in the infusion paradigm.\",",
    "Curator Statement": false
  },
  "AMGAB0421": {
    "Interaction ID": "AMGAB0421",
    "Antibody ID": "ABID0001.6.4",
    "Antibody name": "chaducanumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41594-020-0505-6",
    "PMID": 32989305.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Mass Spectrometry",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\", \"Extended Data Figure 6\", \"Extended Data Figure 7\",  \"Extended Data Figure 8\", \"We found that chaducanumab selectively reduces the secondary nucleation rate of Aβ42 (Fig. 1a), lowering the effective rate constant for this process by approximately 40% even at the lowest concentration of antibody tested (250 pM, Extended Data Fig. 4). The maximum reduction, by a factor of 3, is observed at concentrations of approximately 100 nM chaducanumab corresponding to a substoichiometric molar ratio of 0.03:1 antibody:Aβ42.\", \"To extend these findings to physiological conditions, we used CSF in the aggregation assay. In this case, Aβ42 displayed an extended lag phase consistent with earlier findings (Extended Data Fig. 6)35,36. However, each antibody was found to predominantly inhibit the same step as in buffer (Fig. 1 and Extended Data Figs. 6 and 7), with variations in the values of the rate constants reflecting the change of environment from buffer to CSF.\", \"The results reveal that chaducanumab causes a clear reduction of the free oligomer concentration, in direct agreement with the observed reduction in secondary nucleation, while a smaller reduction is observed with 3D6 and in particular with chgantenerumab, neither of which significantly inhibits secondary nucleation. We also observed that a fraction of Aβ42 elutes together with chaducanumab in the void.\",  \"Extended Data Figure 9\",\"Figure 2\",\"The specific inhibition of secondary nucleation (Fig. 1), and the corresponding reduction in free oligomer concentration identified in the presence of chaducanumab (Fig. 2), indicates that the activity of this antibody is likely to be driven predominantly by interactions with species unique to secondary nucleation, that is the fibril surface, rather than interactions with smaller species that are involved in both primary and secondary nucleation.\", \" We observed that pristine fibrils that had not been exposed to chaducanumab at any stage enhance the process of secondary nucleation and increase the rate of aggregation, whereas preformed fibrils that had been generated in the presence of 0.1 molar equivalents of chaducanumab accelerate aggregation to a significantly smaller extent. Kinetic analysis (Extended Data Fig. 8f) reveals a reduction of approximately 33% in the apparent rate constant for secondary nucleation in this latter case, a value that is similar to that identified from the analysis in Fig. 1 (see also Extended Data Fig. 4), showing that a substantial fraction of the inhibitory effect on secondary nucleation originates from interaction of chaducanumab with Aβ42 fibrils.\", \"In particular, the kinetic fingerprints shown in Fig. 4a reveal that only chaducanumab specifically reduces the rate of the secondary nucleation pathway. Similar results were obtained in both buffer and CSF.\", \"Figure 4\",\"To demonstrate the highly specific nature of the inhibition of secondary nucleation by chaducanumab, we also investigated the combined effect of the antibodies together with Brichos. Since the kinetic fingerprints showed that both chaducanumab and the molecular chaperone inhibit secondary nucleation specifically, the analysis predicted that no effect on the aggregation kinetics would be observed on the addition of chaducanumab in the presence of excess Brichos. By contrast, since the kinetic fingerprints for chgantenerumab and 3D6 show that these antibodies inhibit processes other than secondary nucleation, an additive inhibitory effect was expected even in the presence of excess molecular chaperone. These predictions were verified by the data probing the aggregation process in the presence of each of the antibodies and Brichos (Fig. 4b), demonstrating the specific activity of chaducanumab in inhibiting the secondary nucleation pathway.\", \"The reduction of the free oligomer concentration in the presence of chaducanumab is in agreement with the observed inhibition of secondary nucleation and in contrast to the smaller reduction observed in the presence of 3D6 or chgantenerumab, neither of which significantly inhibits secondary nucleation.\",  \"For example, chaducanumab displays a highly similar kinetic fingerprint to the Brichos chaperone, a profile that is not shared by any of the other antibodies tested here (Fig. 4) but that is known to correspond to highly efficient oligomer suppression through inhibition of secondary nucleation5 (Fig. 2).\", \"Taken together, our results demonstrate the power of the chemical kinetics approach and reveal that chaducanumab can highly effectively directly inhibit the key molecular process, secondary nucleation, through which oligomers form, as well as bind amyloid fibrils even at low concentrations, thus targeting them for microglia-mediated removal13,18 and eliminating the catalyst for this reaction.\",",
    "Curator Statement": false
  },
  "AMGAB0422": {
    "Interaction ID": "AMGAB0422",
    "Antibody ID": "ABID0002.6",
    "Antibody name": "chgantenerumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41594-020-0505-6",
    "PMID": 32989305.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Mass Spectrometry",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\", \"Extended Data Figure 6\", \"Extended Data Figure 7\",  \"Extended Data Figure 8\", \"We also found that 3D6 and chgantenerumab act predominantly by reducing the growth of the fibrillar aggregates under both preseeded and unseeded reaction conditions (Fig. 1b,d). \", \"To extend these findings to physiological conditions, we used CSF in the aggregation assay. In this case, Aβ42 displayed an extended lag phase consistent with earlier findings (Extended Data Fig. 6)35,36. However, each antibody was found to predominantly inhibit the same step as in buffer (Fig. 1 and Extended Data Figs. 6 and 7), with variations in the values of the rate constants reflecting the change of environment from buffer to CSF.\",\"The results reveal that chaducanumab causes a clear reduction of the free oligomer concentration, in direct agreement with the observed reduction in secondary nucleation, while a smaller reduction is observed with 3D6 and in particular with chgantenerumab, neither of which significantly inhibits secondary nucleation. We also observed that a fraction of Aβ42 elutes together with chaducanumab in the void.\",  \"Extended Data Figure 9\", \"Figure 2\", \" To verify this mode of action, we benchmarked the activity of chaducanumab against the effect of a known and highly specific secondary nucleation inhibitor, the chaperone domain Brichos from pro-SPC5. While chaducanumab reduces the rate of secondary nucleation by up to a factor of three, at high concentrations Brichos is able to completely suppress secondary nucleation5. Considered together, our data reveal that chaducanumab has the same kinetic fingerprint as Brichos, while the other antibodies exhibit different types of behavior (Fig. 4a).\", \"Figure 4\", \"The reduction of the free oligomer concentration in the presence of chaducanumab is in agreement with the observed inhibition of secondary nucleation and in contrast to the smaller reduction observed in the presence of 3D6 or chgantenerumab, neither of which significantly inhibits secondary nucleation.\",",
    "Curator Statement": false
  },
  "AMGAB0423": {
    "Interaction ID": "AMGAB0423",
    "Antibody ID": "ABID0005.5",
    "Antibody name": "m266",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41594-020-0505-6",
    "PMID": 32989305.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Mass Spectrometry",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\", \"Extended Data Figure 6\", \"Extended Data Figure 7\",  \"Extended Data Figure 8\", \"Extended Data Figure 9\", \"By contrast, the data show that m266 selectively inhibits primary nucleation (Fig. 1c).\", \"To extend these findings to physiological conditions, we used CSF in the aggregation assay. In this case, Aβ42 displayed an extended lag phase consistent with earlier findings (Extended Data Fig. 6)35,36. However, each antibody was found to predominantly inhibit the same step as in buffer (Fig. 1 and Extended Data Figs. 6 and 7), with variations in the values of the rate constants reflecting the change of environment from buffer to CSF.\", \" For m266 we observe a very large amount of Aβ42 eluting in early SEC fractions (Extended Data Fig. 9), consistent with the observation that this antibody binds with high affinity to Aβ42 monomers19.\", \"\"Figure 2\", \"Figure 4\",",
    "Curator Statement": false
  },
  "AMGAB0424": {
    "Interaction ID": "AMGAB0424",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41594-020-0505-6",
    "PMID": 32989305.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Mass Spectrometry",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\", \"Extended Data Figure 6\", \"Extended Data Figure 7\",  \"Extended Data Figure 8\", \"We also found that 3D6 and chgantenerumab act predominantly by reducing the growth of the fibrillar aggregates under both preseeded and unseeded reaction conditions (Fig. 1b,d). \", \"To extend these findings to physiological conditions, we used CSF in the aggregation assay. In this case, Aβ42 displayed an extended lag phase consistent with earlier findings (Extended Data Fig. 6)35,36. However, each antibody was found to predominantly inhibit the same step as in buffer (Fig. 1 and Extended Data Figs. 6 and 7), with variations in the values of the rate constants reflecting the change of environment from buffer to CSF.\",\"The results reveal that chaducanumab causes a clear reduction of the free oligomer concentration, in direct agreement with the observed reduction in secondary nucleation, while a smaller reduction is observed with 3D6 and in particular with chgantenerumab, neither of which significantly inhibits secondary nucleation. We also observed that a fraction of Aβ42 elutes together with chaducanumab in the void.\",  \"Extended Data Figure 9\", \"Figure 2\", \"Figure 4\", \"The reduction of the free oligomer concentration in the presence of chaducanumab is in agreement with the observed inhibition of secondary nucleation and in contrast to the smaller reduction observed in the presence of 3D6 or chgantenerumab, neither of which significantly inhibits secondary nucleation.\",",
    "Curator Statement": false
  },
  "AMGAB0425": {
    "Interaction ID": "AMGAB0425",
    "Antibody ID": "ABID0028.5",
    "Antibody name": "C10.2",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1038/s41598-019-41105-4",
    "PMID": 30874605.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Immunocytochemistry",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0426": {
    "Interaction ID": "AMGAB0426",
    "Antibody ID": "ABID0028.9",
    "Antibody name": "C10.2_D265A",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1038/s41598-019-41105-4",
    "PMID": 30874605.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Immunocytochemistry",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0427": {
    "Interaction ID": "AMGAB0427",
    "Antibody ID": "ABID0328",
    "Antibody name": "muPMN310",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41598-019-46306-5",
    "PMID": 31285517.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, ThT - Total aggregation (final point), Immunoblotting",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \" The addition of muPMN310 at an antibody:Aβ42 molar ratio of 1:5 (an excess molar ratio of Aβ to assess the blocking potential of PMN310) completely inhibited accumulation of β-sheet structure (Fig. 4a).\", \" The immunoblots show that addition of muPMN310 to Aβ42 peptides maintained a pool of soluble Aβ in the supernatant at assay endpoint, whereas no soluble Aβ remained for Aβ42 incubated alone or with an isotype control (Fig. 4b). Correspondingly, strong Aβ signals were observed in the pelleted insoluble fractions from Aβ42 incubated alone or with isotype control, while a reduced insoluble Aβ signal was obtained with the Aβ42 + muPMN310 sample (Fig. 4b, uncropped immunoblots provided in Supplementary Fig. 4a). Together these results suggest that muPMN310 inhibits aggregation of Aβ42.\", \"In vitro, muPMN310 prevented propagation of Aβ42 aggregation and inhibited the neurotoxicity of synthetic oligomers in primary neuronal cultures (Fig. 4a–c).\",",
    "Curator Statement": false
  },
  "AMGAB0428": {
    "Interaction ID": "AMGAB0428",
    "Antibody ID": "ABID0176",
    "Antibody name": "STAB-MAb",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1038/s41598-019-47626-2",
    "PMID": 31439854.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point)",
    "Amyloid species identified": "Monomers. Mature fibers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The NMR derived epitope supports the observed results from ThT-monitored fluorescence and electron microscopy experiments, in which STAB-MAb was shown to inhibit the formation of aggregates and promote disruption of pre-formed fibrils.\", \"ThT-monitored fluorescence experiments indicate that STAB-MAb can inhibit Aβ(1–42) aggregation\", \"The aggregation kinetics of Aβ in the presence of STAB-Mab were monitored by the Thioflavin T (ThT) assay.\", \"Figure 1\", \"ThT curves indicated an immediate inhibition of Aβ(1–42) fibrillation, both in the presence of phenol red and STAB-MAb, with a more pronounced effect being observed in the latter case, in which fluorescence decreased approximately 2000 RFU during the first 60 minutes of experiment (Fig. 1B).\",  \"In a third and final experiment, a new Aβ(1–42) aliquot was resuspended in buffer at 4 °C and incubated for 24 hours at 37 °C to promote self-assembly. STAB-MAb was then added and aggregation monitored by ThT fluorescence. Remarkably, in this case RFU values decreased approximately 30% of their initial value in the following 2 hours, with curves for both control and antibody exhibiting a similar shape (Fig. 1C). Together, these results are a first indication that STAB-MAb can both inhibit Aβ aggregation and induce fibril disassociation.\", \"Electron microscopy analysis confirms that STAB-MAb can inhibit the formation of aggregates and induce fibril disassembly\", \"Transmission electron microscopy (TEM) experiments further confirmed the ability of STAB-MAb to inhibit the in vitro formation of amyloid-organized aggregates and promote the disruption of pre-formed fibrils. \", \"Figure 2\", \"However, with concomitant antibody incubation, no organized Aβ(1–42) structures were visible, but regular, small globulomers were found (Fig. 2C,D). Moreover, when the formation of Aβ(1–42) fibrillar assemblies was followed by a 24-hour incubation with STAB-MAb, no organized aggregates were observed (Fig. 2E), with micrographs unusually resembling those of the freshly resuspended peptide (Fig. 2A).\", \" In this context, we demonstrated that STAB-MAb can completely inhibit the formation of fibril structures when present at a 1:1 molar concentration with Aβ. However, the ThT assay is not well-suited to establish whether the antibody is also capable of binding and disrupting pre-assembled Aβ aggregates. For this reason, we performed TEM analysis of several samples containing pre-formed fibrils of Aβ incubated with STAB-MAb. These experiments demonstrated that the antibody can disaggregate fibrils. In addition, we also observed that the antibody can interfere with the formation of Aβ aggregates.\", \"Together, the data provided by the ThT and TEM experiments reveals that STAB-MAb may exert its therapeutic effect through a dual mechanism, since it can both inhibit the formation of highly organized Aβ structures and also inducing the disruption of fibrils.\",",
    "Curator Statement": false
  },
  "AMGAB0429": {
    "Interaction ID": "AMGAB0429",
    "Antibody ID": "ABID0018",
    "Antibody name": "Gosuranemab",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1038/s43587-023-00523-w",
    "PMID": 38012285.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"No significant differences were observed between the gosuranemab and placebo groups (P > 0.05) in the adjusted mean change in the tau positron emission tomography (PET) standardized uptake value ratio (SUVR) in each brain composite region corresponding to Braak stages I–II (–0.012 (95% CI −0.055, 0.031) in the high-dose group, 0.054 (95% CI −0.008, 0.115) in the intermediate-dose group, 0.033 (95% CI −0.028, 0.094) in the low-dose group and 0.047 (95% CI 0.002, 0.091) in the placebo group), Braak stages III–IV (0.129 (95% CI 0.082, 0.176) in the high-dose group, 0.178 (95% CI 0.110, 0.246) in the intermediate-dose group, 0.142 (95% CI 0.075, 0.209) in the low-dose group and 0.177 (95% CI 0.128, 0.227) in the placebo group) and Braak stages V–VI (0.135 (95% CI 0.087, 0.183) in the high-dose group, 0.175 (95% CI 0.106, 0.244) in the intermediate-dose group, 0.168 (95% CI 0.100, 0.237) in the low-dose group and 0.180 (95% CI 0.130, 0.230) in the placebo group; Fig. 4a–c).\", \"Figure 4\", \"Extended Data Figure 3\", \" As expected, the placebo group demonstrated increased tau PET SUVR over 78 weeks. Similar results were obtained for the medial temporal, lateral temporal and frontal cortices (Extended Data Fig. 3).\", \"Analysis of the tau PET substudy—the largest [18F]MK-6240 tau PET dataset collected to date in the context of a well-controlled clinical trial—demonstrated measurable longitudinal increases in tau PET SUVR over time, as expected, yet no effect of treatment on cerebral tau accumulation in the target brain regions (for example, composite regions corresponding to Braak stages I–VI). Thus, gosuranemab effectively bound extracellular N-terminal tau, but this binding did not reduce the accumulation of pathological tau as detected by tau PET.\",",
    "Curator Statement": "Although not significant, the data shows reduction in amyloid accumulation vs the placebo."
  },
  "AMGAB0430": {
    "Interaction ID": "AMGAB0430",
    "Antibody ID": "ABID0018",
    "Antibody name": "Gosuranemab",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1038/s43587-023-00523-w",
    "PMID": 38012285.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"No significant differences were observed between the gosuranemab and placebo groups (P > 0.05) in the adjusted mean change in the tau positron emission tomography (PET) standardized uptake value ratio (SUVR) in each brain composite region corresponding to Braak stages I–II (–0.012 (95% CI −0.055, 0.031) in the high-dose group, 0.054 (95% CI −0.008, 0.115) in the intermediate-dose group, 0.033 (95% CI −0.028, 0.094) in the low-dose group and 0.047 (95% CI 0.002, 0.091) in the placebo group), Braak stages III–IV (0.129 (95% CI 0.082, 0.176) in the high-dose group, 0.178 (95% CI 0.110, 0.246) in the intermediate-dose group, 0.142 (95% CI 0.075, 0.209) in the low-dose group and 0.177 (95% CI 0.128, 0.227) in the placebo group) and Braak stages V–VI (0.135 (95% CI 0.087, 0.183) in the high-dose group, 0.175 (95% CI 0.106, 0.244) in the intermediate-dose group, 0.168 (95% CI 0.100, 0.237) in the low-dose group and 0.180 (95% CI 0.130, 0.230) in the placebo group; Fig. 4a–c).\", \"Figure 4\", \"Extended Data Figure 3\", \" As expected, the placebo group demonstrated increased tau PET SUVR over 78 weeks. Similar results were obtained for the medial temporal, lateral temporal and frontal cortices (Extended Data Fig. 3).\", \"Analysis of the tau PET substudy—the largest [18F]MK-6240 tau PET dataset collected to date in the context of a well-controlled clinical trial—demonstrated measurable longitudinal increases in tau PET SUVR over time, as expected, yet no effect of treatment on cerebral tau accumulation in the target brain regions (for example, composite regions corresponding to Braak stages I–VI). Thus, gosuranemab effectively bound extracellular N-terminal tau, but this binding did not reduce the accumulation of pathological tau as detected by tau PET.\",",
    "Curator Statement": "Although not significant, the data shows reduction in amyloid accumulation vs the placebo."
  },
  "AMGAB0431": {
    "Interaction ID": "AMGAB0431",
    "Antibody ID": "ABID0377",
    "Antibody name": "W20",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1038/srep36631",
    "PMID": 27824125.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"W20-treated mice showed 13.6% (Fig. 3e) and 32.1% (Fig. 3f) reductions in levels of α-synuclein oligomers, as detected by OC and A11 antibodies, respectively, compared with vehicle-treated A53T α-synuclein mice.\", \"Supplementary Figure 8\", \"W20 disassociated preformed amyloid deposits.\", \"In this study, we firstly showed that an oligomer-specific single-chain variable fragment antibody, W20 simultaneously improved motor and cognitive function in Parkinson’s disease and Huntington’s disease mouse models, and attenuated a number of neuropathological features by reducing α-synuclein and mutant huntingtin protein aggregate load and preventing synaptic degeneration.\", \"W20 penetrated neurons and dissociated performed amyloid deposits\", \"The results showed that both α-synuclein and mHTT aggregates were significantly decreased in the brain slides, suggesting W20 may decrease intracellular amyloid deposits in transgenic mouse models by penetrating neurons and disassociating preformed amyloid aggregates (Supplementary Fig. 8).\", \"W20 not only significantly reduced the levels of both types of α-synuclein oligomers, but also decreased α-synuclein deposits in the brainstem of A53T α-synuclein mice.\", \"W20 treatment markedly attenuated astrocytic and microglial activation by decreasing levels of α-synuclein and mHTT aggregates.\",",
    "Curator Statement": false
  },
  "AMGAB0432": {
    "Interaction ID": "AMGAB0432",
    "Antibody ID": "ABID0377",
    "Antibody name": "W20",
    "Amyloid ID": "AGAMYID0008",
    "Amyloid name": "Huntingtin",
    "DOI": "10.1038/srep36631",
    "PMID": 27824125.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot, Dot blot,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Treating BACHD mice with W20 markedly decreased both soluble and insoluble mHTT levels in the BACHD mice brains. While neither ns-scFv affected the mHTT levels in the brains of BACHD mice nor W20 had any effects in WT mice, suggesting W20 had specific therapeutic function on HD mice (Supplementary Fig. 3).\", \"Supplementary Figure 8\", \"W20 disassociated preformed amyloid deposits.\", \"Figure 6\", \"W20 reduced mHTT levels in BACHD mouse brains\",\"In this study, we firstly showed that an oligomer-specific single-chain variable fragment antibody, W20 simultaneously improved motor and cognitive function in Parkinson’s disease and Huntington’s disease mouse models, and attenuated a number of neuropathological features by reducing α-synuclein and mutant huntingtin protein aggregate load and preventing synaptic degeneration.\", \"We also determined the levels of mHTT oligomers in the mouse brain lysates by dot-blot using oligomer-specific antibodies OC and A11 (Fig. 6b). W20-treated mice showed 36.5% (Fig. 6e) and 31.1% (Fig. 6h) reductions in the levels of mHTT oligomers, as detected by OC and A11 antibodies, respectively, compared with vehicle-treated BACHD mice.\", \"The results showed that mHTT aggregates dramatically decreased in the cortex and striatum of W20-treated BACHD mice compared with those in the vehicle-treated BACHD control by 26% (Fig. 7a, Supplementary Fig. 4a) and 49.5% (Fig. 7b, Supplementary Fig. 4b), respectively.\", \"W20 penetrated neurons and dissociated performed amyloid deposits\", \"The results showed that both α-synuclein and mHTT aggregates were significantly decreased in the brain slides, suggesting W20 may decrease intracellular amyloid deposits in transgenic mouse models by penetrating neurons and disassociating preformed amyloid aggregates (Supplementary Fig. 8).\", \"Similarly, our findings showed that W20 treatment significantly reduced levels of soluble and insoluble mHTT, mHTT oligomers as well as EM48-positive mHTT aggregate accumulation in the brains of BACHD mice.\", \"W20 treatment markedly attenuated astrocytic and microglial activation by decreasing levels of α-synuclein and mHTT aggregates.\",",
    "Curator Statement": false
  },
  "AMGAB0433": {
    "Interaction ID": "AMGAB0433",
    "Antibody ID": "ABID0218",
    "Antibody name": "DesAb9–17",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Our results indicated that all DesAbs except DesAb22–29 were effective in delaying IAPP aggregation in a concentration dependent manner, while the negative control DesAb did not show any activity against IAPP aggregation (Fig. S5)\",",
    "Curator Statement": false
  },
  "AMGAB0434": {
    "Interaction ID": "AMGAB0434",
    "Antibody ID": "ABID0219",
    "Antibody name": "DesAb12–18",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Our results indicated that all DesAbs except DesAb22–29 were effective in delaying IAPP aggregation in a concentration dependent manner, while the negative control DesAb did not show any activity against IAPP aggregation (Fig. S5)\",",
    "Curator Statement": false
  },
  "AMGAB0435": {
    "Interaction ID": "AMGAB0435",
    "Antibody ID": "ABID0220",
    "Antibody name": "DesAb15–22",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Our results indicated that all DesAbs except DesAb22–29 were effective in delaying IAPP aggregation in a concentration dependent manner, while the negative control DesAb did not show any activity against IAPP aggregation (Fig. S5)\",",
    "Curator Statement": false
  },
  "AMGAB0436": {
    "Interaction ID": "AMGAB0436",
    "Antibody ID": "ABID0221",
    "Antibody name": "DesAb19–26",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Our results indicated that all DesAbs except DesAb22–29 were effective in delaying IAPP aggregation in a concentration dependent manner, while the negative control DesAb did not show any activity against IAPP aggregation (Fig. S5)\",",
    "Curator Statement": false
  },
  "AMGAB0437": {
    "Interaction ID": "AMGAB0437",
    "Antibody ID": "ABID0222",
    "Antibody name": "DesAb20–28",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Our results indicated that all DesAbs except DesAb22–29 were effective in delaying IAPP aggregation in a concentration dependent manner, while the negative control DesAb did not show any activity against IAPP aggregation (Fig. S5)\",",
    "Curator Statement": false
  },
  "AMGAB0438": {
    "Interaction ID": "AMGAB0438",
    "Antibody ID": "ABID0223",
    "Antibody name": "DesAb22–29",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Our results indicated that all DesAbs except DesAb22–29 were effective in delaying IAPP aggregation in a concentration dependent manner, while the negative control DesAb did not show any activity against IAPP aggregation (Fig. S5)\",",
    "Curator Statement": false
  },
  "AMGAB0439": {
    "Interaction ID": "AMGAB0439",
    "Antibody ID": "ABID0224",
    "Antibody name": "DesAb26–32",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Our results indicated that all DesAbs except DesAb22–29 were effective in delaying IAPP aggregation in a concentration dependent manner, while the negative control DesAb did not show any activity against IAPP aggregation (Fig. S5)\",",
    "Curator Statement": false
  },
  "AMGAB0440": {
    "Interaction ID": "AMGAB0440",
    "Antibody ID": "ABID0225",
    "Antibody name": "DesAb26–34",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Our results indicated that all DesAbs except DesAb22–29 were effective in delaying IAPP aggregation in a concentration dependent manner, while the negative control DesAb did not show any activity against IAPP aggregation (Fig. S5)\",",
    "Curator Statement": false
  },
  "AMGAB0441": {
    "Interaction ID": "AMGAB0441",
    "Antibody ID": "ABID0226",
    "Antibody name": "DesAb30–37",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Our results indicated that all DesAbs except DesAb22–29 were effective in delaying IAPP aggregation in a concentration dependent manner, while the negative control DesAb did not show any activity against IAPP aggregation (Fig. S5)\",",
    "Curator Statement": false
  },
  "AMGAB0442": {
    "Interaction ID": "AMGAB0442",
    "Antibody ID": "ABID0227",
    "Antibody name": "Monobody9–17",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"Our findings demonstrate that all monobodies were capable of delaying IAPP aggregation in a concentration-dependent manner while the negative control monobody did not show activity against IAPP aggregation (Fig. 5d).\"",
    "Curator Statement": false
  },
  "AMGAB0443": {
    "Interaction ID": "AMGAB0443",
    "Antibody ID": "ABID0228",
    "Antibody name": "Monobody19–26",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"Our findings demonstrate that all monobodies were capable of delaying IAPP aggregation in a concentration-dependent manner while the negative control monobody did not show activity against IAPP aggregation (Fig. 5d).\"",
    "Curator Statement": false
  },
  "AMGAB0444": {
    "Interaction ID": "AMGAB0444",
    "Antibody ID": "ABID0229",
    "Antibody name": "Monobody20–28",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"Our findings demonstrate that all monobodies were capable of delaying IAPP aggregation in a concentration-dependent manner while the negative control monobody did not show activity against IAPP aggregation (Fig. 5d).\"",
    "Curator Statement": false
  },
  "AMGAB0445": {
    "Interaction ID": "AMGAB0445",
    "Antibody ID": "ABID0230",
    "Antibody name": "Monobody26–34",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"Our findings demonstrate that all monobodies were capable of delaying IAPP aggregation in a concentration-dependent manner while the negative control monobody did not show activity against IAPP aggregation (Fig. 5d).\"",
    "Curator Statement": false
  },
  "AMGAB0446": {
    "Interaction ID": "AMGAB0446",
    "Antibody ID": "ABID0231",
    "Antibody name": "Monobodyneg",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 5\", \"Our findings demonstrate that all monobodies were capable of delaying IAPP aggregation in a concentration-dependent manner while the negative control monobody did not show activity against IAPP aggregation (Fig. 5d).\"",
    "Curator Statement": false
  },
  "AMGAB0447": {
    "Interaction ID": "AMGAB0447",
    "Antibody ID": "ABID0232",
    "Antibody name": "DesAb-Aβ(3-9)-FETLTLR(C23AC97V)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\", \"The results indicated that both constructs were effective in inhibiting Aβ42 aggregation, as previously shown for the parent DesAb.28\"",
    "Curator Statement": false
  },
  "AMGAB0448": {
    "Interaction ID": "AMGAB0448",
    "Antibody ID": "ABID0233",
    "Antibody name": "DesAb-Aβ(3-9)-FETLTLR(C23AC97A)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\", \"The results indicated that both constructs were effective in inhibiting Aβ42 aggregation, as previously shown for the parent DesAb.28\"",
    "Curator Statement": false
  },
  "AMGAB0449": {
    "Interaction ID": "AMGAB0449",
    "Antibody ID": "ABID0233",
    "Antibody name": "DesAb-Aβ(3-9)-FETLTLR(C23AC97A)",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"We tested the specificity of FETLTLR_C23A_C97A by performing a kinetics aggregation assay against α-synuclein (aS), a different misfolding protein. Since the FETLTLR sequence was designed for Aβ42, a specific DesAb should not inhibit the aggregation of aS, as indeed we found (Fig. S1).\", \"Figure S1\"",
    "Curator Statement": false
  },
  "AMGAB0450": {
    "Interaction ID": "AMGAB0450",
    "Antibody ID": "ABID0234",
    "Antibody name": "DesAbneg",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 4\", \"Our results indicated that all DesAbs except DesAb22–29 were effective in delaying IAPP aggregation in a concentration dependent manner, while the negative control DesAb did not show any activity against IAPP aggregation (Fig. S5)\", \"Figure S5\", \"We also measured the binding affinity of DesAbneg as negative control, and it did not show binding signal to IAPP monomers (Fig. S7).\",",
    "Curator Statement": false
  },
  "AMGAB0451": {
    "Interaction ID": "AMGAB0451",
    "Antibody ID": "ABID0235",
    "Antibody name": "FETLTLR(BC)-wt(FG)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0452": {
    "Interaction ID": "AMGAB0452",
    "Antibody ID": "ABID0236",
    "Antibody name": "GSFETLTLREEE(BC)-wt(FG)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0453": {
    "Interaction ID": "AMGAB0453",
    "Antibody ID": "ABID0237",
    "Antibody name": "wt(BC)-FETLTLR(FG)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0454": {
    "Interaction ID": "AMGAB0454",
    "Antibody ID": "ABID0238",
    "Antibody name": "wt(BC)-GSFETLTLREEE(FG)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0455": {
    "Interaction ID": "AMGAB0455",
    "Antibody ID": "ABID0239",
    "Antibody name": "N-4-FETLTLR(BC)-wt(FG)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0456": {
    "Interaction ID": "AMGAB0456",
    "Antibody ID": "ABID0240",
    "Antibody name": "N-8-FETLTLR(BC)-AAAAS(FG)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"Kinetics aggregation assays were applied to test their activity against the aggregation of Aβ42 under (Fig. 2d, red dashed box), and observed that only N-8-FETLTLR(BC)-AAAAS(FG) exhibited good activity against the aggregation of Aβ42, suggesting that simultaneous shortening of the N-terminus and FG loop may help maintain binding of the designed BC loop sequence.\",",
    "Curator Statement": false
  },
  "AMGAB0457": {
    "Interaction ID": "AMGAB0457",
    "Antibody ID": "ABID0241",
    "Antibody name": "N-8-GSFETLTLREEE(BC)-AAAAS(FG)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0458": {
    "Interaction ID": "AMGAB0458",
    "Antibody ID": "ABID0242",
    "Antibody name": "N-8-FETLTLR(BC)-EGYYSSY(FG)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \" We then tested their activity against the aggregation of Aβ42 (Fig. 2d, red dashed box), and observed that both monobody variants showed good activity against the aggregation of Aβ42.\",",
    "Curator Statement": false
  },
  "AMGAB0459": {
    "Interaction ID": "AMGAB0459",
    "Antibody ID": "ABID0243",
    "Antibody name": "N-8-FETLTLR(BC)-PTSDYG(FG)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1039/d5sc01427a",
    "PMID": 41395543.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \" We then tested their activity against the aggregation of Aβ42 (Fig. 2d, red dashed box), and observed that both monobody variants showed good activity against the aggregation of Aβ42.\",",
    "Curator Statement": false
  },
  "AMGAB0460": {
    "Interaction ID": "AMGAB0460",
    "Antibody ID": "ABID0007.1",
    "Antibody name": "ScFv-h3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1042/BJ20101712",
    "PMID": 21501114.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody, ThT - Total aggregation (final point), Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The addition of an equimolar ratio of scFv-h3D6 to the Aβ1–42 peptide prevented the formation of Aβ oligomers and, in its place, initiated the formation of WL fibrils immediately after mixing (Figure 3D).\", \"Figure 3\", \"Taking into account that WL fibrils are kinetically trapped species, the temperature has depopulated this state, allowing the actual amyloid-fibril pathway by the Aβ1–42 peptide to proceed.\", \"In contrast with the behaviour of the scFv-h3D6 alone, when mixing Aβ1–42 –scFv-h3D6, the binding of ThT and ANS is apparent from zero time and becomes more evident upon heating (especially at 90 ◦C) (Figures 4A and 4B).\", \"Figure 4A\", \"Apart from the details of the aggregation pathways, the most relevant conclusion of the present study is that, in native conditions, scFv-h3D6 inhibits Aβ-peptide amyloid fibril formation and cytotoxicity by pulling its oligomers towards the WL pathway.\"",
    "Curator Statement": false
  },
  "AMGAB0461": {
    "Interaction ID": "AMGAB0461",
    "Antibody ID": "ABID0007",
    "Antibody name": "Bapineuzumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1056/NEJMoa1304839",
    "PMID": 24450891.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Among carriers, the mean (±SE) SUVR increased in the placebo group (by 0.102±0.026), but remained almost unchanged in the bapineuzumab group (an increase of only 0.001±0.021) over the course of 71 weeks (difference in change, bapineuzumab minus placebo, −0.101; P=0.004).\", \"Between-group differences were observed with respect to PIB-PET and cerebrospinal fluid phospho-tau concentrations in APOE ε4 allele carriers but not in noncarriers.\", \"4–8 In phase 2 clinical studies involving patients with mild-to-moderate Alzheimer’s disease, patients who received bapineuzumab, as compared with those who received placebo, had a greater reduction in amyloid on positron-emission tomographic amyloid imaging with the use of Pittsburgh compound B (PIB-PET) and reduced cerebrospinal fluid phosphorylated tau (phospho-tau), suggesting target engagement and attenuated neurodegeneration.\", \"Figure 2\", \"Table S3\", \"A decreased rate of accumulation of amyloid in the brain on PIB-PET was seen in APOE ε4 carriers who received bapineuzumab, but the difference was smaller than that seen in phase 2 studies, which included the 2.0-mg-per-kilogram dose.\", \"Although biomarker results in the carrier study suggest that bapineuzumab may modify Aβ accumulation and a downstream biomarker (phospho-tau), neither trial showed a benefit of bapineuzumab with respect to clinical outcomes\"",
    "Curator Statement": false
  },
  "AMGAB0462": {
    "Interaction ID": "AMGAB0462",
    "Antibody ID": "ABID0022",
    "Antibody name": "Dezamizumab",
    "Amyloid ID": "AGAMYID0017",
    "Amyloid name": "Serum amyloid P-component",
    "DOI": "10.1056/NEJMoa1504942",
    "PMID": 26176329.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "SAP scintigraphy (123I-SAP)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\", \"Table 1\", \"At 45 days after the start of CPHPC treatment and 42 days after anti-SAP antibody treatment, when SAP distribution had fully re-equilibrated between the soluble and amyloid-bound compartments, whole-body 123I-SAP scintigraphy scans revealed substantial reductions in hepatic amyloid load in four patients (Table 1 and Figure 1). In Patient 13, who had macroglobulinemia in clonal relapse throughout the study and in whom AL amyloidosis had been diagnosed by biopsy of a greatly enlarged amyloid-laden cervical lymph node, the mass shrank from approximately 5 cm in diameter immediately before anti-SAP treatment to approximately 1 cm at day 42. In Patient 12, who had no hepatic amyloid, renal function and proteinuria were unchanged at day 42, but SAP scintigraphy revealed a modest reduction in renal amyloid load.\", \". Indeed, after treatment with anti-SAP antibody, a reduction in amyloid load was most sensitively detected as decreased liver stiffness. Major clearance of hepatic amyloid was also revealed by means of SAP scintigraphy1,8,23 in some patients and was independently confirmed when equilibrium MRI showed a reduction in liver extracellular volume toward normal in these patients.\", \"A modest but definite reduction in renal SAP scintigraphy signal was also seen in Patient 12, and there was impressive shrinkage of the amyloid-laden cervical lymph node in Patient 13. The amyloid regression in Patients 9, 13, and 14 was particularly notable, because the respective amyloidogenic precursors were still being produced in these patients (Table S1 in the Supplementary Appendix), and the patients would have been expected to continue to have accumulation of amyloid.\",",
    "Curator Statement": false
  },
  "AMGAB0463": {
    "Interaction ID": "AMGAB0463",
    "Antibody ID": "ABID0022",
    "Antibody name": "Dezamizumab",
    "Amyloid ID": "AGAMYID0017",
    "Amyloid name": "Serum amyloid P-component",
    "DOI": "10.1056/NEJMoa1504942",
    "PMID": 26176329.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "SAP scintigraphy (123I-SAP)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\", \"Table 1\",",
    "Curator Statement": "The amyloid reduction was not detected in all patients form the trial."
  },
  "AMGAB0464": {
    "Interaction ID": "AMGAB0464",
    "Antibody ID": "ABID0003",
    "Antibody name": "Donanemab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1056/NEJMoa2100708",
    "PMID": 33720637.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" At 76 weeks, the reductions in the amyloid plaque level and the global tau load were 85.06 centiloids and 0.01 greater, respectively, with donanemab than with placebo.\", \"At 76 weeks, the reduction in the amyloid plaque level as assessed by florbetapir PET was 85.06 centiloids greater in the donanemab group than in the placebo group (−84.13 vs. 0.93 centiloids) (Figure 3A). By 24 weeks, the reduction was 67.83 centiloids greater with donanemab than with placebo (−69.64 vs. −1.82 centiloids). The percentage of participants in the donanemab group who had amyloid-negative status (defined as an amyloid plaque level of <24.10 centiloids) at 24, 52, and 76 weeks was 40.0%, 59.8%, and 67.8%, respectively (Figure 3A). In addition, approximately 27.4% and 54.7% of participants in the donanemab group had sufficient lowering of the amyloid plaque level to switch to placebo infusion at 28 and 56 weeks, respectively. \", \"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0465": {
    "Interaction ID": "AMGAB0465",
    "Antibody ID": "ABID0008.5",
    "Antibody name": "NI006",
    "Amyloid ID": "AGAMYID0010",
    "Amyloid name": "Transthyretin",
    "DOI": "10.1056/NEJMoa2303765",
    "PMID": 37212440.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other: Cardiac scintigraphy (Gamma scan), Other: Cardiac MRI (extracellular volume quantification)",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"At doses of at least 10 mg per kilogram, cardiac tracer uptake on scintigraphy and extracellular volume on cardiac magnetic resonance imaging, both of which are imaging-based surrogate markers of cardiac amyloid load, appeared to be reduced over a period of 12 months.\", \"Figure 1\", \"Figure 2\", \"By contrast, patients who received NI006 at doses of at least 10 mg per kilogram seemed to have reductions in cardiac tracer uptake on scintigraphy and in extracellular volume on cardiac MRI after 4 months and 12 months of treatment. These findings may support the proof-of-concept regarding the use of NI006 for the treatment of patients with ATTR cardiomyopathy and appear to be consistent with preclinical data showing activity of NI006 for inducing removal of ATTR.18\",",
    "Curator Statement": false
  },
  "AMGAB0466": {
    "Interaction ID": "AMGAB0466",
    "Antibody ID": "ABID0002",
    "Antibody name": "Gantenerumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1056/NEJMoa2304430",
    "PMID": 37966285.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"At week 116, the difference in the amyloid level on PET between the gantenerumab group and the placebo group was −66.44 and −56.46 centiloids in the GRADUATE I and II trials, respectively, and amyloid-negative status was attained in 28.0% and 26.8% of the participants receiving gantenerumab in the two trials.\", \"Among persons with early Alzheimer’s disease, the use of gantenerumab led to a lower amyloid plaque burden than placebo at 116 weeks but was not associated with slower clinical decline.\", \"The amyloid level on PET at week 116 among participants receiving gantenerumab was lower than the level among those receiving placebo (Fig. 3A). The difference in the adjusted mean (±SE) amyloid level between the gantenerumab group and the placebo group was −66.44±4.17 centiloids (95% CI, −74.71 to −58.16) in the GRADUATE I trial and −56.46±3.98 centiloids (95% CI, −64.36 to −48.56) in the GRADUATE II trial. The mean (±SD) amyloid level at week 116 was 40.68±27.39 and 104.44±33.15 centiloids in the gantenerumab and placebo groups, respectively, in the GRADUATE I trial and 44.85±26.67 and 99.52±27.72 centiloids in the gantenerumab and placebo groups, respectively, in the GRADUATE II trial.\", \"Figure 3\", \"At week 116, amyloid-negative status (amyloid level, ≤24 centiloids) was attained in 28.0% and 2.4% of the participants receiving gantenerumab and placebo, respectively, in the GRADUATE I trial and in 26.8% and none of the participants receiving gantenerumab and placebo, respectively, in the GRADUATE II trial (Table S4). \", \"Table S4\", \"The use of gantenerumab led to partial removal of amyloid plaques and improvement in some soluble biomarkers of Alzheimer’s disease. \"",
    "Curator Statement": false
  },
  "AMGAB0467": {
    "Interaction ID": "AMGAB0467",
    "Antibody ID": "ABID0002",
    "Antibody name": "Gantenerumab",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1056/NEJMoa2304430",
    "PMID": 37966285.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \" Across both trials, participants receiving gantenerumab had lower CSF levels of phosphorylated tau 181 and higher levels of Aβ42 than those receiving placebo; the accumulation of aggregated tau on PET was similar in the two groups. \", \"There was no appreciable difference between the gantenerumab group and the placebo group in the tau level assessed in any of the four composite regions on PET at week 116 (Fig. 3B and Fig. S6). For example, the between-group difference in the median SUVR assessed in the medial temporal composite region, which did not include the hippocampus, was −0.02 (95% CI, −0.06 to 0.03) in the GRADUATE I trial and 0.04 (95% CI, −0.03 to 0.09) in the GRADUATE II trial.\",  \"However, there was no treatment effect with respect to the accumulation of tau in the brain on PET; the absence of such an effect may be due to the limited amyloid plaque removal observed.\",",
    "Curator Statement": false
  },
  "AMGAB0468": {
    "Interaction ID": "AMGAB0468",
    "Antibody ID": "ABID0166",
    "Antibody name": "MW1 scFv",
    "Amyloid ID": "AGAMYID0008",
    "Amyloid name": "Huntingtin (htt) Exon 1",
    "DOI": "10.1073/pnas.022631799",
    "PMID": 11792860.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Other: High-speed centrifugation, Western blotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Here we report that intracellular expression of some of these mAbs as recombinant, single-chain variable region fragments (scFvs) targeted to different regions of htt exon 1 can either block or enhance aggregation as well as the cell death induced by a mutant htt.\"",
    "Curator Statement": false
  },
  "AMGAB0469": {
    "Interaction ID": "AMGAB0469",
    "Antibody ID": "ABID0167",
    "Antibody name": "MW2 scFv",
    "Amyloid ID": "AGAMYID0008",
    "Amyloid name": "Huntingtin (htt) Exon 1",
    "DOI": "10.1073/pnas.022631799",
    "PMID": 11792860.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "High-speed centrifugation, Western blotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Here we report that intracellular expression of some of these mAbs as recombinant, single-chain variable region fragments (scFvs) targeted to different regions of htt exon 1 can either block or enhance aggregation as well as the cell death induced by a mutant htt.\"",
    "Curator Statement": false
  },
  "AMGAB0470": {
    "Interaction ID": "AMGAB0470",
    "Antibody ID": "ABID0168",
    "Antibody name": "MW7 scFv",
    "Amyloid ID": "AGAMYID0008",
    "Amyloid name": "Huntingtin (htt) Exon 1",
    "DOI": "10.1073/pnas.022631799",
    "PMID": 11792860.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "High-speed centrifugation, Western blotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In perturbation experiments, MW7 scFv, recognizing the polyP domains of htt, significantly inhibits aggregation as well as the cell death induced by mutant htt protein.\", \"Here we report that intracellular expression of some of these mAbs as recombinant, single-chain variable region fragments (scFvs) targeted to different regions of htt exon 1 can either block or enhance aggregation as well as the cell death induced by a mutant htt.\", \"MW7 scFv inhibits aggregation of mutant htt exon 1.\", \"Figure 6\", \" The htt in the pellet that can be solubilized by SDS treatment is ≈80 kDa, whereas the htt that cannot be solubilized does not enter the gel and is visualized as a band at the top of the gel. Very little of either form of htt is found in lysates from cells transfected with MW7 scFv. In contrast, these forms of htt appear to be greater in lysates from cells transfected with MW1 or -2 scFvs than in lysates from control cells. \", \"Biochemical assays show that WM7 coexpression also strongly inhibits htt aggregation. \", \" Biochemical analysis clearly shows, however, that mutant htt does aggregate in these cells and that expression of MW7 scFv strikingly reduces this aggregation.\",",
    "Curator Statement": false
  },
  "AMGAB0471": {
    "Interaction ID": "AMGAB0471",
    "Antibody ID": "ABID0434",
    "Antibody name": "10D5",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.0436286100",
    "PMID": 12566568.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The studies showed that: (i) of the purified or elicited antibodies tested, only antibodies against the N-terminal regions of Aβ were able to invoke plaque clearance; (ii) plaque binding correlated with a clearance response and neuronal protection, whereas the ability of antibodies to capture soluble Aβ was not necessarily correlated with efficacy; (iii) the isotype of the antibody dramatically influenced the degree of plaque clearance and neuronal protection; (iv) high affinity of the antibody for Fc receptors on microglial cells seemed more important than high affinity for Aβ itself; and (v) complement activation was not required for plaque clearance. \", \"These findings also illustrate that, of the five antibodies previously examined in vivo, those against N-terminal epitopes were effective in reducing plaque burden (pAb1–42, 3D6, and 10D5), whereas those against C-terminal epitopes were inactive (16C11 and 21F12) (7).\",  \"Figure 3\", \"As shown in Fig. 3, the two IgG2a antibodies against Aβ reduced peptide levels in the cultures more efficiently (73% and 69%, P < 0.001) than the IgG1 (28% and 35%, not significant) or IgG2b (48% and 59%, P < 0.05 and 0.001, respectively) antibodies. Because previous studies showed that ex vivo plaque clearance depends on Fc-receptor activity (7) and can occur in the presence of heat-inactivated serum, it is unlikely that complement played a significant role in mediating the effects observed in the ex vivo assay.\", \"The two anti-Aβ IgG2a antibodies reduced Aβ levels in the cultures (69% for 2C1 and 73% for 12B4; P < 0.001) more efficiently than the IgG2b isotype antibodies (48% for 12A11, P < 0.05, and 59% for 3A3, P < 0.001). The anti-Aβ IgG1 antibodies did not significantly reduce Aβ levels.\", \"Although all the antibodies triggered plaque clearance, only the IgG2a antibodies provided significant reduction in neuritic dystrophy (12B4, P < 0.05, and 2C1, P < 0.001) (Fig. 4 b and c).\", \"Interestingly, the antibody 10D5 (IgG1) was less effective than either of the IgG2a antibodies even though it exhibited higher avidity for aggregated Aβ1–42 (Table 2) as well as amyloid plaques (data not shown) and maintained significantly higher serum titers than the other antibodies.\", \"IgG2a antibodies, which exhibit higher affinity than other isotypes for phagocytic Fc receptors (in particular FcγRI), provided the highest level of plaque clearance and were the only anti-Aβ antibodies to provide neuronal protection under the conditions tested. Plaque clearance seemed independent of complement activation, because IgG1 antibodies, which cannot fix complement, were as effective as the complement-fixing IgG2b antibodies.\",",
    "Curator Statement": false
  },
  "AMGAB0472": {
    "Interaction ID": "AMGAB0472",
    "Antibody ID": "ABID0435",
    "Antibody name": "6C6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.0436286100",
    "PMID": 12566568.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The studies showed that: (i) of the purified or elicited antibodies tested, only antibodies against the N-terminal regions of Aβ were able to invoke plaque clearance; (ii) plaque binding correlated with a clearance response and neuronal protection, whereas the ability of antibodies to capture soluble Aβ was not necessarily correlated with efficacy; (iii) the isotype of the antibody dramatically influenced the degree of plaque clearance and neuronal protection; (iv) high affinity of the antibody for Fc receptors on microglial cells seemed more important than high affinity for Aβ itself; and (v) complement activation was not required for plaque clearance. \", \"These findings also illustrate that, of the five antibodies previously examined in vivo, those against N-terminal epitopes were effective in reducing plaque burden (pAb1–42, 3D6, and 10D5), whereas those against C-terminal epitopes were inactive (16C11 and 21F12) (7).\",  \"Figure 3\", \"As shown in Fig. 3, the two IgG2a antibodies against Aβ reduced peptide levels in the cultures more efficiently (73% and 69%, P < 0.001) than the IgG1 (28% and 35%, not significant) or IgG2b (48% and 59%, P < 0.05 and 0.001, respectively) antibodies. Because previous studies showed that ex vivo plaque clearance depends on Fc-receptor activity (7) and can occur in the presence of heat-inactivated serum, it is unlikely that complement played a significant role in mediating the effects observed in the ex vivo assay.\", \"The two anti-Aβ IgG2a antibodies reduced Aβ levels in the cultures (69% for 2C1 and 73% for 12B4; P < 0.001) more efficiently than the IgG2b isotype antibodies (48% for 12A11, P < 0.05, and 59% for 3A3, P < 0.001). The anti-Aβ IgG1 antibodies did not significantly reduce Aβ levels.\", \"Although all the antibodies triggered plaque clearance, only the IgG2a antibodies provided significant reduction in neuritic dystrophy (12B4, P < 0.05, and 2C1, P < 0.001) (Fig. 4 b and c).\", \"IgG2a antibodies, which exhibit higher affinity than other isotypes for phagocytic Fc receptors (in particular FcγRI), provided the highest level of plaque clearance and were the only anti-Aβ antibodies to provide neuronal protection under the conditions tested. Plaque clearance seemed independent of complement activation, because IgG1 antibodies, which cannot fix complement, were as effective as the complement-fixing IgG2b antibodies.\",",
    "Curator Statement": false
  },
  "AMGAB0473": {
    "Interaction ID": "AMGAB0473",
    "Antibody ID": "ABID0436",
    "Antibody name": "2C1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.0436286100",
    "PMID": 12566568.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The studies showed that: (i) of the purified or elicited antibodies tested, only antibodies against the N-terminal regions of Aβ were able to invoke plaque clearance; (ii) plaque binding correlated with a clearance response and neuronal protection, whereas the ability of antibodies to capture soluble Aβ was not necessarily correlated with efficacy; (iii) the isotype of the antibody dramatically influenced the degree of plaque clearance and neuronal protection; (iv) high affinity of the antibody for Fc receptors on microglial cells seemed more important than high affinity for Aβ itself; and (v) complement activation was not required for plaque clearance. \", \"These findings also illustrate that, of the five antibodies previously examined in vivo, those against N-terminal epitopes were effective in reducing plaque burden (pAb1–42, 3D6, and 10D5), whereas those against C-terminal epitopes were inactive (16C11 and 21F12) (7).\",  \"Figure 3\", \"As shown in Fig. 3, the two IgG2a antibodies against Aβ reduced peptide levels in the cultures more efficiently (73% and 69%, P < 0.001) than the IgG1 (28% and 35%, not significant) or IgG2b (48% and 59%, P < 0.05 and 0.001, respectively) antibodies. Because previous studies showed that ex vivo plaque clearance depends on Fc-receptor activity (7) and can occur in the presence of heat-inactivated serum, it is unlikely that complement played a significant role in mediating the effects observed in the ex vivo assay.\", \"The two anti-Aβ IgG2a antibodies reduced Aβ levels in the cultures (69% for 2C1 and 73% for 12B4; P < 0.001) more efficiently than the IgG2b isotype antibodies (48% for 12A11, P < 0.05, and 59% for 3A3, P < 0.001). The anti-Aβ IgG1 antibodies did not significantly reduce Aβ levels.\", \"Although all the antibodies triggered plaque clearance, only the IgG2a antibodies provided significant reduction in neuritic dystrophy (12B4, P < 0.05, and 2C1, P < 0.001) (Fig. 4 b and c).\", \"IgG2a antibodies, which exhibit higher affinity than other isotypes for phagocytic Fc receptors (in particular FcγRI), provided the highest level of plaque clearance and were the only anti-Aβ antibodies to provide neuronal protection under the conditions tested. Plaque clearance seemed independent of complement activation, because IgG1 antibodies, which cannot fix complement, were as effective as the complement-fixing IgG2b antibodies.\",",
    "Curator Statement": false
  },
  "AMGAB0474": {
    "Interaction ID": "AMGAB0474",
    "Antibody ID": "ABID0437",
    "Antibody name": "12B4",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.0436286100",
    "PMID": 12566568.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The studies showed that: (i) of the purified or elicited antibodies tested, only antibodies against the N-terminal regions of Aβ were able to invoke plaque clearance; (ii) plaque binding correlated with a clearance response and neuronal protection, whereas the ability of antibodies to capture soluble Aβ was not necessarily correlated with efficacy; (iii) the isotype of the antibody dramatically influenced the degree of plaque clearance and neuronal protection; (iv) high affinity of the antibody for Fc receptors on microglial cells seemed more important than high affinity for Aβ itself; and (v) complement activation was not required for plaque clearance. \", \"These findings also illustrate that, of the five antibodies previously examined in vivo, those against N-terminal epitopes were effective in reducing plaque burden (pAb1–42, 3D6, and 10D5), whereas those against C-terminal epitopes were inactive (16C11 and 21F12) (7).\",  \"Figure 3\", \"As shown in Fig. 3, the two IgG2a antibodies against Aβ reduced peptide levels in the cultures more efficiently (73% and 69%, P < 0.001) than the IgG1 (28% and 35%, not significant) or IgG2b (48% and 59%, P < 0.05 and 0.001, respectively) antibodies. Because previous studies showed that ex vivo plaque clearance depends on Fc-receptor activity (7) and can occur in the presence of heat-inactivated serum, it is unlikely that complement played a significant role in mediating the effects observed in the ex vivo assay.\", \"The two anti-Aβ IgG2a antibodies reduced Aβ levels in the cultures (69% for 2C1 and 73% for 12B4; P < 0.001) more efficiently than the IgG2b isotype antibodies (48% for 12A11, P < 0.05, and 59% for 3A3, P < 0.001). The anti-Aβ IgG1 antibodies did not significantly reduce Aβ levels.\", \"Although all the antibodies triggered plaque clearance, only the IgG2a antibodies provided significant reduction in neuritic dystrophy (12B4, P < 0.05, and 2C1, P < 0.001) (Fig. 4 b and c).\", \"IgG2a antibodies, which exhibit higher affinity than other isotypes for phagocytic Fc receptors (in particular FcγRI), provided the highest level of plaque clearance and were the only anti-Aβ antibodies to provide neuronal protection under the conditions tested. Plaque clearance seemed independent of complement activation, because IgG1 antibodies, which cannot fix complement, were as effective as the complement-fixing IgG2b antibodies.\",",
    "Curator Statement": false
  },
  "AMGAB0475": {
    "Interaction ID": "AMGAB0475",
    "Antibody ID": "ABID0438",
    "Antibody name": "3A3",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.0436286100",
    "PMID": 12566568.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The studies showed that: (i) of the purified or elicited antibodies tested, only antibodies against the N-terminal regions of Aβ were able to invoke plaque clearance; (ii) plaque binding correlated with a clearance response and neuronal protection, whereas the ability of antibodies to capture soluble Aβ was not necessarily correlated with efficacy; (iii) the isotype of the antibody dramatically influenced the degree of plaque clearance and neuronal protection; (iv) high affinity of the antibody for Fc receptors on microglial cells seemed more important than high affinity for Aβ itself; and (v) complement activation was not required for plaque clearance. \", \"These findings also illustrate that, of the five antibodies previously examined in vivo, those against N-terminal epitopes were effective in reducing plaque burden (pAb1–42, 3D6, and 10D5), whereas those against C-terminal epitopes were inactive (16C11 and 21F12) (7).\",  \"Figure 3\", \"As shown in Fig. 3, the two IgG2a antibodies against Aβ reduced peptide levels in the cultures more efficiently (73% and 69%, P < 0.001) than the IgG1 (28% and 35%, not significant) or IgG2b (48% and 59%, P < 0.05 and 0.001, respectively) antibodies. Because previous studies showed that ex vivo plaque clearance depends on Fc-receptor activity (7) and can occur in the presence of heat-inactivated serum, it is unlikely that complement played a significant role in mediating the effects observed in the ex vivo assay.\", \"The two anti-Aβ IgG2a antibodies reduced Aβ levels in the cultures (69% for 2C1 and 73% for 12B4; P < 0.001) more efficiently than the IgG2b isotype antibodies (48% for 12A11, P < 0.05, and 59% for 3A3, P < 0.001). The anti-Aβ IgG1 antibodies did not significantly reduce Aβ levels.\", \"Although all the antibodies triggered plaque clearance, only the IgG2a antibodies provided significant reduction in neuritic dystrophy (12B4, P < 0.05, and 2C1, P < 0.001) (Fig. 4 b and c).\", \"IgG2a antibodies, which exhibit higher affinity than other isotypes for phagocytic Fc receptors (in particular FcγRI), provided the highest level of plaque clearance and were the only anti-Aβ antibodies to provide neuronal protection under the conditions tested. Plaque clearance seemed independent of complement activation, because IgG1 antibodies, which cannot fix complement, were as effective as the complement-fixing IgG2b antibodies.\",",
    "Curator Statement": false
  },
  "AMGAB0476": {
    "Interaction ID": "AMGAB0476",
    "Antibody ID": "ABID0439",
    "Antibody name": "12A11",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.0436286100",
    "PMID": 12566568.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The studies showed that: (i) of the purified or elicited antibodies tested, only antibodies against the N-terminal regions of Aβ were able to invoke plaque clearance; (ii) plaque binding correlated with a clearance response and neuronal protection, whereas the ability of antibodies to capture soluble Aβ was not necessarily correlated with efficacy; (iii) the isotype of the antibody dramatically influenced the degree of plaque clearance and neuronal protection; (iv) high affinity of the antibody for Fc receptors on microglial cells seemed more important than high affinity for Aβ itself; and (v) complement activation was not required for plaque clearance. \", \"These findings also illustrate that, of the five antibodies previously examined in vivo, those against N-terminal epitopes were effective in reducing plaque burden (pAb1–42, 3D6, and 10D5), whereas those against C-terminal epitopes were inactive (16C11 and 21F12) (7).\",  \"Figure 3\", \"As shown in Fig. 3, the two IgG2a antibodies against Aβ reduced peptide levels in the cultures more efficiently (73% and 69%, P < 0.001) than the IgG1 (28% and 35%, not significant) or IgG2b (48% and 59%, P < 0.05 and 0.001, respectively) antibodies. Because previous studies showed that ex vivo plaque clearance depends on Fc-receptor activity (7) and can occur in the presence of heat-inactivated serum, it is unlikely that complement played a significant role in mediating the effects observed in the ex vivo assay.\", \"The two anti-Aβ IgG2a antibodies reduced Aβ levels in the cultures (69% for 2C1 and 73% for 12B4; P < 0.001) more efficiently than the IgG2b isotype antibodies (48% for 12A11, P < 0.05, and 59% for 3A3, P < 0.001). The anti-Aβ IgG1 antibodies did not significantly reduce Aβ levels.\", \"Although all the antibodies triggered plaque clearance, only the IgG2a antibodies provided significant reduction in neuritic dystrophy (12B4, P < 0.05, and 2C1, P < 0.001) (Fig. 4 b and c).\", \"IgG2a antibodies, which exhibit higher affinity than other isotypes for phagocytic Fc receptors (in particular FcγRI), provided the highest level of plaque clearance and were the only anti-Aβ antibodies to provide neuronal protection under the conditions tested. Plaque clearance seemed independent of complement activation, because IgG1 antibodies, which cannot fix complement, were as effective as the complement-fixing IgG2b antibodies.\",",
    "Curator Statement": false
  },
  "AMGAB0477": {
    "Interaction ID": "AMGAB0477",
    "Antibody ID": "ABID0523",
    "Antibody name": "AB10",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1073/pnas.0703793104",
    "PMID": 18042730.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody, Ultracentrifugation,",
    "Amyloid species identified": "Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The antibody domain possesses functional activity in preventing the formation of mature amyloid fibrils by stabilizing Aβ protofibrils.\", \"Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils\", \"B10 Prevents the Formation of Mature Amyloid Fibrils by Stabilizing Aβ Protofibrils.\", \"Figure 4\", \"B10AP prevents mature fibril formation by stabilization of Aβ(1–40) protofibrils. \", \" However, dot blot experiments with B10AP measure a shorter lag phase (5.9 h) than fluorescence measurements with ThT (7.3 h). These data demonstrate the formation of B10-epitopes at significant level before the formation of ThT-positive fibrils. TEM analysis demonstrates small amounts of nonfibrillar aggregates after 4 h, large quantities of fibrils after 18 h, and both fibrils and nonfibrillar structures after 7 h (Fig. 4a). The apparent quantity of the nonfibrillar aggregates declines progressively upon incubation.\", \"Addition of B10AP to Aβ(1–40) at 1:10 (B10:Aβ) molar ratio potently blocks the formation of ThT-positive fibrils (Fig. 4b) and leads, instead, to the stabilization of much more irregular, curvilinear fibrils, similar to what has been described as protofibrils (35, 36). The presently analyzed fibrils possess amyloid-like characteristics, evident from an ATR-FTIR peak at 1,624 cm−1 (Fig. 4c) and x-ray diffraction (Fig. 4d). Fully hydrated protofibril-B10AP complexes show reflections at 4.62 ± 0.02 and 9.88 ± 0.05 Å, the characteristic spacings of an amyloid-like core structure (5). Nevertheless, protofibril-B10AP complexes show only small interactions with amyloid-specific dyes, such as ThT or CR (Fig. 4 e and f), consistent with previous reports about Aβ protofibrils (37). Control reactions show that their small ThT and CR affinities cannot be explained with a steric hindrance due to B10AP or with a short fibril length, because B10AP-decorated mature fibrils and fragmented mature fibrils (Fig. 4g) produce significant interactions with both dyes (Fig. 4 e and f). Protofibril-B10AP complexes are more susceptible toward proteolytic digestion than mature fibrils (Fig. 4h), consistent with a lower structural compactness. Taken together, we conclude that B10AP prevents the formation of mature Aβ amyloid fibrils by arresting fibril formation at the protofibril stage.\", \"Experiments in which B10AP is added to Aβ peptide under the conditions of fibril formation show that B10AP possesses functional activity in abrogating the formation of mature amyloid fibrils (Fig. 4).\",",
    "Curator Statement": false
  },
  "AMGAB0478": {
    "Interaction ID": "AMGAB0478",
    "Antibody ID": "ABID0523",
    "Antibody name": "AB10",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1073/pnas.0703793104",
    "PMID": 18042730.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Digestion experiments by proteinase K, X-ray fiber diffraction pattern, Increase in beta content by Fourier transform infrared (FTIR) spectroscopy, Ultracentrifugation, Congo Red (CR) red shift,",
    "Amyloid species identified": "Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Finally, centrifugation (Fig. 4i) and TEM analysis (not presented) do not provide evidence that B10AP binding leads to a significant disaggregation of preformed Aβ fibrils. \", \"Figure 4\", \"Consistent with this, we do not observe any significant dissociation of preformed amyloid fibrils in the presence of B10AP (Fig. 4i).\",",
    "Curator Statement": "The AB10 construct does not dissagregate preformed fibrils."
  },
  "AMGAB0479": {
    "Interaction ID": "AMGAB0479",
    "Antibody ID": "ABID0135",
    "Antibody name": "C4",
    "Amyloid ID": "AGAMYID0008",
    "Amyloid name": "Huntingtin (htt) Fusion construct",
    "DOI": "10.1073/pnas.071058398",
    "PMID": 11296304.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Flourescence microscopy",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Coexpression of anti-huntingtin sFv intrabodies with the abnormal huntingtin-GFP fusion protein dramatically reduced the number of aggregates, compared with controls lacking the intrabody. \", \"Figure 4\", \"\"Up to 86% fewer aggregates were present in intrabody cotransfectants, compared with control levels\", \"When this HD model is examined in transfected cells, the huntingtin analogues with expanded polyglutamine (polyQ) repeats exhibit visible aggregate formation that increases proportionately with the number of glutamine residues in the polyQ segment. Using this model, we have found that intrabody association with huntingtin via its N-terminal residues (1–17) can significantly reduce in situ aggregation of expanded-repeat exon 1 analogues.\", \"Aggregate formation by HD-Q72-GFP or HD-Q103-GFP was observed to qualitatively decrease at an intrabody-to-antigen plasmid ratio of 3:1, but for quantitative analysis, the effects were counted at a ratio of 5:1. Up to 86% fewer aggregates were present in intrabody cotransfectants, compared with control levels (note BHK-21 cells, Fig. 4A). In contrast, control transfections with nonspecific intrabody plasmids (anti-erbB-2 ML3–9 sFv) showed little or no statistically significant reduction in aggregate formation compared with the parent empty vector. \", \"Inhibition of aggregate formation of pathogenic HD-polyQ-GFP in the presence of cotransfected anti-HD C4 sFv. (A) Quantitation of aggregate numbers at 48 h after cotransfection (5:1 ratio) with anti-HD C4 sFv-HA, negative control ML3–9 sFv-HA, or parent vector (pcDNA) and HD-Q72-GFP in COS-7, BHK-21, or HEK 293 cells, as indicated. After lysis with 2% SDS/2% Triton X-100/50 mM Tris, the number of insoluble fluorescent aggregates in six or eight random fields was counted. Bars represent means of six cotransfections ± SEM. C4 sFv-HA significantly reduced the number of aggregates when compared with control ML3–9 sFv-HA or pcDNA (P < 0.005). Similar results seen with HD-Q103-GFP (not shown). \", \"Double-label immunofluorescence studies confirmed that BHK-21 cells expressing HD-Q72-GFP or HD-Q103-GFP (green label, Fig. 3 A and B) plus anti-HD C4 sFv (red label, Fig. 3B) showed substantial diffuse GFP label, with only an occasional fluorescent aggregate (usually labeled with HA as well; note arrow in Fig. 3B). Those cells that failed to express the intrabody showed evidence of large aggregates (Fig. 3B, arrowheads).\", \"We have discovered that huntingtin-specific intrabodies can reduce aggregate formation in cellular models of HD. \"",
    "Curator Statement": false
  },
  "AMGAB0480": {
    "Interaction ID": "AMGAB0480",
    "Antibody ID": "ABID0136",
    "Antibody name": "ML3.9",
    "Amyloid ID": "AGAMYID0008",
    "Amyloid name": "Huntingtin (htt) Fusion construct",
    "DOI": "10.1073/pnas.071058398",
    "PMID": 11296304.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Flourescence microscopy",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 4\", \"\"Up to 86% fewer aggregates were present in intrabody cotransfectants, compared with control levels\", \"Aggregate formation by HD-Q72-GFP or HD-Q103-GFP was observed to qualitatively decrease at an intrabody-to-antigen plasmid ratio of 3:1, but for quantitative analysis, the effects were counted at a ratio of 5:1. Up to 86% fewer aggregates were present in intrabody cotransfectants, compared with control levels (note BHK-21 cells, Fig. 4A). In contrast, control transfections with nonspecific intrabody plasmids (anti-erbB-2 ML3–9 sFv) showed little or no statistically significant reduction in aggregate formation compared with the parent empty vector. \", \"Inhibition of aggregate formation of pathogenic HD-polyQ-GFP in the presence of cotransfected anti-HD C4 sFv. (A) Quantitation of aggregate numbers at 48 h after cotransfection (5:1 ratio) with anti-HD C4 sFv-HA, negative control ML3–9 sFv-HA, or parent vector (pcDNA) and HD-Q72-GFP in COS-7, BHK-21, or HEK 293 cells, as indicated. After lysis with 2% SDS/2% Triton X-100/50 mM Tris, the number of insoluble fluorescent aggregates in six or eight random fields was counted. Bars represent means of six cotransfections ± SEM. C4 sFv-HA significantly reduced the number of aggregates when compared with control ML3–9 sFv-HA or pcDNA (P < 0.005). Similar results seen with HD-Q103-GFP (not shown). \"",
    "Curator Statement": false
  },
  "AMGAB0481": {
    "Interaction ID": "AMGAB0481",
    "Antibody ID": "ABID0153",
    "Antibody name": "Nb24",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Mutant ΔN6",
    "DOI": "10.1073/pnas.1008560108",
    "PMID": 21220305.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In this study, we selected nanobodies that block the fibrillogenesis of a proteolytic amyloidogenic ΔN6 variant of β2m.\", \"Nanobodies Efficiently Block β2m Fibrillogenesis.\", \"Figure 1\", \"Nb24 Disrupts β2-Microglobulin Aggregates in Vitro but Does not Disrupt the Fibrils.\", \"Addition of Nb24 to preformed nonamorphous ΔN6β2m aggregates (obtained after 5 h of incubation at 37 °C and pH 5.0) caused a significant decrease of the ThT fluorescence (Fig. S4B) concomitant with an increase of resolubilized ΔN6β2m as shown by SDS-PAGE analysis of the soluble fraction (Fig. S4C).\", \"To investigate the stoichiometry of this reaction, ΔN6β2m aggregates were mixed with Nb24 at ΔN6β2m:Nb ratios of 1∶1 and 4∶1. Equimolar amounts of ΔN6β2m and nanobody were needed to completely disrupt the preformed ΔN6β2m fibrils, as indicated by the reduction of the ThT fluorescence to background levels. \",",
    "Curator Statement": false
  },
  "AMGAB0482": {
    "Interaction ID": "AMGAB0482",
    "Antibody ID": "ABID0154",
    "Antibody name": "Nb108",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Mutant ΔN6",
    "DOI": "10.1073/pnas.1008560108",
    "PMID": 21220305.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 1\", \"The β2m-unrelated Nb108 did not interfere with ΔN6β2m aggregation (Fig. S4B).\", \"Figure S4\",",
    "Curator Statement": false
  },
  "AMGAB0483": {
    "Interaction ID": "AMGAB0483",
    "Antibody ID": "ABID0155",
    "Antibody name": "Nb23",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Mutant ΔN6",
    "DOI": "10.1073/pnas.1008560108",
    "PMID": 21220305.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In this study, we selected nanobodies that block the fibrillogenesis of a proteolytic amyloidogenic ΔN6 variant of β2m.\", \"Nanobodies Efficiently Block β2m Fibrillogenesis.\", \"Figure 1\",",
    "Curator Statement": false
  },
  "AMGAB0484": {
    "Interaction ID": "AMGAB0484",
    "Antibody ID": "ABID0156",
    "Antibody name": "Nb30",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Mutant ΔN6",
    "DOI": "10.1073/pnas.1008560108",
    "PMID": 21220305.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In this study, we selected nanobodies that block the fibrillogenesis of a proteolytic amyloidogenic ΔN6 variant of β2m.\", \"Nanobodies Efficiently Block β2m Fibrillogenesis.\", \"Figure 1\",",
    "Curator Statement": false
  },
  "AMGAB0485": {
    "Interaction ID": "AMGAB0485",
    "Antibody ID": "ABID0157",
    "Antibody name": "Nb272",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Mutant ΔN6",
    "DOI": "10.1073/pnas.1008560108",
    "PMID": 21220305.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In this study, we selected nanobodies that block the fibrillogenesis of a proteolytic amyloidogenic ΔN6 variant of β2m.\", \"Nanobodies Efficiently Block β2m Fibrillogenesis.\", \"Figure 1\",",
    "Curator Statement": false
  },
  "AMGAB0486": {
    "Interaction ID": "AMGAB0486",
    "Antibody ID": "ABID0158",
    "Antibody name": "Nb22",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Mutant ΔN6",
    "DOI": "10.1073/pnas.1008560108",
    "PMID": 21220305.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In this study, we selected nanobodies that block the fibrillogenesis of a proteolytic amyloidogenic ΔN6 variant of β2m.\", \"Nanobodies Efficiently Block β2m Fibrillogenesis.\", \"Figure 1\",",
    "Curator Statement": false
  },
  "AMGAB0487": {
    "Interaction ID": "AMGAB0487",
    "Antibody ID": "ABID0159",
    "Antibody name": "Nb21",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Mutant ΔN6",
    "DOI": "10.1073/pnas.1008560108",
    "PMID": 21220305.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\",",
    "Curator Statement": false
  },
  "AMGAB0488": {
    "Interaction ID": "AMGAB0488",
    "Antibody ID": "ABID0160",
    "Antibody name": "Nb20",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Mutant ΔN6",
    "DOI": "10.1073/pnas.1008560108",
    "PMID": 21220305.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\",",
    "Curator Statement": false
  },
  "AMGAB0489": {
    "Interaction ID": "AMGAB0489",
    "Antibody ID": "ABID0161",
    "Antibody name": "Nb31",
    "Amyloid ID": "AGAMYID0011",
    "Amyloid name": "Mutant ΔN6",
    "DOI": "10.1073/pnas.1008560108",
    "PMID": 21220305.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point), TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\",",
    "Curator Statement": false
  },
  "AMGAB0490": {
    "Interaction ID": "AMGAB0490",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Importantly, none of these antibodies inhibit Aβ fibrillization at substoichiometric concentrations (1:10 antibody:Aβ molar ratio).\", \"Supplementary Figure S7\", \"Conventional sequence- and conformation-specific antibodies fail to inhibit Aβ fibrillization at substoichiometric concentrations despite that they bind to Aβ.\",",
    "Curator Statement": false
  },
  "AMGAB0491": {
    "Interaction ID": "AMGAB0491",
    "Antibody ID": "ABID0433",
    "Antibody name": "4G8",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Importantly, none of these antibodies inhibit Aβ fibrillization at substoichiometric concentrations (1:10 antibody:Aβ molar ratio).\", \"Supplementary Figure S7\", \"Conventional sequence- and conformation-specific antibodies fail to inhibit Aβ fibrillization at substoichiometric concentrations despite that they bind to Aβ.\",",
    "Curator Statement": false
  },
  "AMGAB0492": {
    "Interaction ID": "AMGAB0492",
    "Antibody ID": "ABID0477",
    "Antibody name": "Aβ12–21",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,  immunoblotting,  Atomic force microscopy (AFM), Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Grafted AMyloid-Motif AntiBODIES (gammabodies) presenting hydrophobic peptides from Aβ (Alzheimer’s disease), α-Synuclein (Parkinson's disease), and islet amyloid polypeptide (type 2 diabetes) inhibit fibril assembly of each corresponding polypeptide at low substoichiometric concentrations (1:10 gammabody:monomer molar ratio).\", \"Figure 2\", \"We find that Aβ gammabodies inhibit amyloid formation, which we first evaluated at substoichiometric gammabody concentrations (1:10 gammabody:Aβ molar ratio; Fig. 2A).\", \"The Aβ12–21 and Aβ15–24 gammabodies also fail to inhibit the formation of prefibrillar oligomers (day 1) and fibrillar conformers (day 2) but convert fibrillar Aβ conformers into nonfibrillar ones (days 3–6).\", \"This inhibitory activity is unchanged at higher gammabody concentrations (1:1 gammabody:Aβ molar ratio), whereas each active gammabody is inactive at a molar ratio of 1:100 gammabody:Aβ (Fig. S2).\", \"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0493": {
    "Interaction ID": "AMGAB0493",
    "Antibody ID": "ABID0477",
    "Antibody name": "Aβ12–21",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"This inhibitory activity is unchanged at higher gammabody concentrations (1:1 gammabody:Aβ molar ratio), whereas each active gammabody is inactive at a molar ratio of 1:100 gammabody:Aβ (Fig. S2).\", \"Supplementary Figure S2\", \"Although the inhibitory Aβ gammabodies eliminated A11- and/or OC-immunoreactivity, we sought additional evidence of their antiaggregation activity. Atomic force microscopy (AFM) imaging and fluorescence analysis using two dyes sensitive to the conformation of Aβ (8-anilino-1-naphthalene sulfonate, ANS; thioflavin T, ThT) confirmed that the Aβ12–21 and Aβ15–24 gammabodies fail to prevent formation of prefibrillar oligomers (day 1) or fibrillar intermediates (day 2), but both prevent fibril formation (days 3–6; Fig. 2 B–D and Fig. S3).\",",
    "Curator Statement": "The antibody (gammabody) does not show Inhibitory activity at a molar ratio of 1:100 gammabody:Aβ."
  },
  "AMGAB0494": {
    "Interaction ID": "AMGAB0494",
    "Antibody ID": "ABID0478",
    "Antibody name": "Aβ15–24",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Secondary structure composition by Circular dichroism (CD), Atomic force microscopy (AFM), Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), immunoblotting",
    "Amyloid species identified": "Protein monomer, Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Grafted AMyloid-Motif AntiBODIES (gammabodies) presenting hydrophobic peptides from Aβ (Alzheimer’s disease), α-Synuclein (Parkinson's disease), and islet amyloid polypeptide (type 2 diabetes) inhibit fibril assembly of each corresponding polypeptide at low substoichiometric concentrations (1:10 gammabody:monomer molar ratio).\", \"Figure 2\", \"We find that Aβ gammabodies inhibit amyloid formation, which we first evaluated at substoichiometric gammabody concentrations (1:10 gammabody:Aβ molar ratio; Fig. 2A).\", \"The Aβ12–21 and Aβ15–24 gammabodies also fail to inhibit the formation of prefibrillar oligomers (day 1) and fibrillar conformers (day 2) but convert fibrillar Aβ conformers into nonfibrillar ones (days 3–6).\", \"This inhibitory activity is unchanged at higher gammabody concentrations (1:1 gammabody:Aβ molar ratio), whereas each active gammabody is inactive at a molar ratio of 1:100 gammabody:Aβ (Fig. S2).\", \"Supplementary Figure S2\", \"Finally, circular dichroism spectroscopy revealed that the Aβ15–24 gammabody converts β-sheet fibrillar intermediates (day 2) into unstructured Aβ conformers (days 3–6), whereas the Aβ33–42 gammabody maintains Aβ monomers (day 0) as unstructured conformers (days 1–6; Fig. S4).\", \"Supplementary Figure S4\",",
    "Curator Statement": false
  },
  "AMGAB0495": {
    "Interaction ID": "AMGAB0495",
    "Antibody ID": "ABID0478",
    "Antibody name": "Aβ15–24",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting,  Atomic force microscopy (AFM),",
    "Amyloid species identified": "Protein monomer, Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"This inhibitory activity is unchanged at higher gammabody concentrations (1:1 gammabody:Aβ molar ratio), whereas each active gammabody is inactive at a molar ratio of 1:100 gammabody:Aβ (Fig. S2).\", \"Supplementary Figure S2\", \"Supplementary Figure S3\", \"Finally, Aβ gammabodies that are inhibitory when added before Aβ oligomerization (day 0) are noninhibitory when added after Aβ oligomerization (Fig. S3).\", \"Although the inhibitory Aβ gammabodies eliminated A11- and/or OC-immunoreactivity, we sought additional evidence of their antiaggregation activity. Atomic force microscopy (AFM) imaging and fluorescence analysis using two dyes sensitive to the conformation of Aβ (8-anilino-1-naphthalene sulfonate, ANS; thioflavin T, ThT) confirmed that the Aβ12–21 and Aβ15–24 gammabodies fail to prevent formation of prefibrillar oligomers (day 1) or fibrillar intermediates (day 2), but both prevent fibril formation (days 3–6; Fig. 2 B–D and Fig. S3).\",",
    "Curator Statement": "The antibody (gammabody) does not show Inhibitory activity at a molar ratio of 1:100 gammabody:Aβ. The gammabody was not able to inhibit once the oligomerization of beta peptide had already started."
  },
  "AMGAB0496": {
    "Interaction ID": "AMGAB0496",
    "Antibody ID": "ABID0478",
    "Antibody name": "Aβ15–24",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM), immunoblotting,  Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...) ,ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 7\",\"Supplementary Figure S8\", \"Supplementary Figure S9\",",
    "Curator Statement": false
  },
  "AMGAB0497": {
    "Interaction ID": "AMGAB0497",
    "Antibody ID": "ABID0478",
    "Antibody name": "Aβ15–24",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM), immunoblotting,  Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...) ,ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 7\",\"Supplementary Figure S9\",",
    "Curator Statement": false
  },
  "AMGAB0498": {
    "Interaction ID": "AMGAB0498",
    "Antibody ID": "ABID0479",
    "Antibody name": "Aβ30–39",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, immunoblotting,  Atomic force microscopy (AFM), Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Grafted AMyloid-Motif AntiBODIES (gammabodies) presenting hydrophobic peptides from Aβ (Alzheimer’s disease), α-Synuclein (Parkinson's disease), and islet amyloid polypeptide (type 2 diabetes) inhibit fibril assembly of each corresponding polypeptide at low substoichiometric concentrations (1:10 gammabody:monomer molar ratio).\", \"Figure 2\", \"We find that Aβ gammabodies inhibit amyloid formation, which we first evaluated at substoichiometric gammabody concentrations (1:10 gammabody:Aβ molar ratio; Fig. 2A).\", \"In contrast, the Aβ30–39 and Aβ33–42 gammabodies prevent formation of both oligomer and fibrillar Aβ conformers (days 0–6; Fig. 2A).\", \"This inhibitory activity is unchanged at higher gammabody concentrations (1:1 gammabody:Aβ molar ratio), whereas each active gammabody is inactive at a molar ratio of 1:100 gammabody:Aβ (Fig. S2).\", \"Supplementary Figure S2\", \"AFM and fluorescence analysis also confirmed that the Aβ30–39 and Aβ33–42 gammabodies prevent both Aβ oligomerization and fibrillization (Fig. 2 B–D and Fig. S3).\",",
    "Curator Statement": false
  },
  "AMGAB0499": {
    "Interaction ID": "AMGAB0499",
    "Antibody ID": "ABID0479",
    "Antibody name": "Aβ30–39",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"This inhibitory activity is unchanged at higher gammabody concentrations (1:1 gammabody:Aβ molar ratio), whereas each active gammabody is inactive at a molar ratio of 1:100 gammabody:Aβ (Fig. S2).\", \"Supplementary Figure S2\",",
    "Curator Statement": "The antibody (gammabody) does not show Inhibitory activity at a molar ratio of 1:100 gammabody:Aβ."
  },
  "AMGAB0500": {
    "Interaction ID": "AMGAB0500",
    "Antibody ID": "ABID0480",
    "Antibody name": "Aβ33–42",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Atomic force microscopy (AFM), Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunoblotting",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Grafted AMyloid-Motif AntiBODIES (gammabodies) presenting hydrophobic peptides from Aβ (Alzheimer’s disease), α-Synuclein (Parkinson's disease), and islet amyloid polypeptide (type 2 diabetes) inhibit fibril assembly of each corresponding polypeptide at low substoichiometric concentrations (1:10 gammabody:monomer molar ratio).\", \"Figure 2\", \"We find that Aβ gammabodies inhibit amyloid formation, which we first evaluated at substoichiometric gammabody concentrations (1:10 gammabody:Aβ molar ratio; Fig. 2A).\", \"In contrast, the Aβ30–39 and Aβ33–42 gammabodies prevent formation of both oligomer and fibrillar Aβ conformers (days 0–6; Fig. 2A).\", \"This inhibitory activity is unchanged at higher gammabody concentrations (1:1 gammabody:Aβ molar ratio), whereas each active gammabody is inactive at a molar ratio of 1:100 gammabody:Aβ (Fig. S2).\", \"Supplementary Figure S2\",\"AFM and fluorescence analysis also confirmed that the Aβ30–39 and Aβ33–42 gammabodies prevent both Aβ oligomerization and fibrillization (Fig. 2 B–D and Fig. S3).\",",
    "Curator Statement": false
  },
  "AMGAB0501": {
    "Interaction ID": "AMGAB0501",
    "Antibody ID": "ABID0480",
    "Antibody name": "Aβ33–42",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting,  Atomic force microscopy (AFM),",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"This inhibitory activity is unchanged at higher gammabody concentrations (1:1 gammabody:Aβ molar ratio), whereas each active gammabody is inactive at a molar ratio of 1:100 gammabody:Aβ (Fig. S2).\", \"Supplementary Figure S2\", \"Supplementary Figure S3\", \"Finally, Aβ gammabodies that are inhibitory when added before Aβ oligomerization (day 0) are noninhibitory when added after Aβ oligomerization (Fig. S3).\",",
    "Curator Statement": "The antibody (gammabody) does not show Inhibitory activity at a molar ratio of 1:100 gammabody:Aβ. The gammabody was not able to inhibit once the oligomerization of beta peptide had already started."
  },
  "AMGAB0502": {
    "Interaction ID": "AMGAB0502",
    "Antibody ID": "ABID0480",
    "Antibody name": "Aβ33–42",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM), immunoblotting,  Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...) ,ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 7\",\"Supplementary Figure S8\", \"Supplementary Figure S9\",",
    "Curator Statement": false
  },
  "AMGAB0503": {
    "Interaction ID": "AMGAB0503",
    "Antibody ID": "ABID0480",
    "Antibody name": "Aβ33–42",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM), immunoblotting,  Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...) ,ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 7\",\"Supplementary Figure S9\",",
    "Curator Statement": false
  },
  "AMGAB0504": {
    "Interaction ID": "AMGAB0504",
    "Antibody ID": "ABID0481",
    "Antibody name": "IAPP22–31",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM), immunoblotting,  Secondary structure composition by Circular dichroism (CD), Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...) ,ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Supplementary Figure S8\",\"Supplementary Figure S9\",",
    "Curator Statement": false
  },
  "AMGAB0505": {
    "Interaction ID": "AMGAB0505",
    "Antibody ID": "ABID0481",
    "Antibody name": "IAPP22–31",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM), immunoblotting,  Secondary structure composition by Circular dichroism (CD), Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...) ,ThT - Aggregation kinetics,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Grafted AMyloid-Motif AntiBODIES (gammabodies) presenting hydrophobic peptides from Aβ (Alzheimer’s disease), α-Synuclein (Parkinson's disease), and islet amyloid polypeptide (type 2 diabetes) inhibit fibril assembly of each corresponding polypeptide at low substoichiometric concentrations (1:10 gammabody:monomer molar ratio).\", \"Strikingly, the IAPP and α-Synuclein gammabodies inhibit fibrillization in a sequence-specific manner at both 1:10 (Fig. 7) and 1:1 (Fig. S8) gammabody:monomer molar ratios.\", \"Supplementary Figure S8\", \"Figure 7\", \"IAPP and α-Synuclein Gammabodies Potently Inhibit Amyloid Formation in a Sequence-Specific Manner.\", \"Supplementary Figure S8\", \"Supplementary Figure S9\",",
    "Curator Statement": false
  },
  "AMGAB0506": {
    "Interaction ID": "AMGAB0506",
    "Antibody ID": "ABID0481",
    "Antibody name": "IAPP22–31",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S8\",",
    "Curator Statement": "The antibody (gammabody) does not show Inhibitory activity at a molar ratio of 1:100 gammabody:IAPP."
  },
  "AMGAB0507": {
    "Interaction ID": "AMGAB0507",
    "Antibody ID": "ABID0482",
    "Antibody name": "αSyn69–78",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM), immunoblotting,  Secondary structure composition by Circular dichroism (CD), Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...) ,ThT - Aggregation kinetics,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Grafted AMyloid-Motif AntiBODIES (gammabodies) presenting hydrophobic peptides from Aβ (Alzheimer’s disease), α-Synuclein (Parkinson's disease), and islet amyloid polypeptide (type 2 diabetes) inhibit fibril assembly of each corresponding polypeptide at low substoichiometric concentrations (1:10 gammabody:monomer molar ratio).\", \"Strikingly, the IAPP and α-Synuclein gammabodies inhibit fibrillization in a sequence-specific manner at both 1:10 (Fig. 7) and 1:1 (Fig. S8) gammabody:monomer molar ratios.\", \"Supplementary Figure S8\", \"Figure 7\", \"IAPP and α-Synuclein Gammabodies Potently Inhibit Amyloid Formation in a Sequence-Specific Manner.\", \"Supplementary Figure S9\",",
    "Curator Statement": false
  },
  "AMGAB0508": {
    "Interaction ID": "AMGAB0508",
    "Antibody ID": "ABID0482",
    "Antibody name": "αSyn69–78",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S8\",\"Supplementary Figure S9\",",
    "Curator Statement": "The antibody (gammabody) does not show Inhibitory activity at a molar ratio of 1:100 gammabody:amyloid."
  },
  "AMGAB0509": {
    "Interaction ID": "AMGAB0509",
    "Antibody ID": "ABID0482",
    "Antibody name": "αSyn69–78",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM), immunoblotting,  Secondary structure composition by Circular dichroism (CD), Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...) ,ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 7\",",
    "Curator Statement": false
  },
  "AMGAB0510": {
    "Interaction ID": "AMGAB0510",
    "Antibody ID": "ABID0483",
    "Antibody name": "Scrambled Aβ15–24",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 2\", \"Moreover, scrambling the grafted Aβ peptides (Fig. 2A) or mutating them with single proline substitutions or glycine insertions (Fig. S2) eliminates the inhibitory activity of gammabodies.\",",
    "Curator Statement": false
  },
  "AMGAB0511": {
    "Interaction ID": "AMGAB0511",
    "Antibody ID": "ABID0484",
    "Antibody name": "Scrambled Aβ33–42",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 2\", \"Moreover, scrambling the grafted Aβ peptides (Fig. 2A) or mutating them with single proline substitutions or glycine insertions (Fig. S2) eliminates the inhibitory activity of gammabodies.\",",
    "Curator Statement": false
  },
  "AMGAB0512": {
    "Interaction ID": "AMGAB0512",
    "Antibody ID": "ABID0485",
    "Antibody name": "Aβ1–10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"As expected, the Aβ1–10 gammabody (which fails to bind to Aβ) is noninhibitory.\", \"This inhibitory activity is unchanged at higher gammabody concentrations (1:1 gammabody:Aβ molar ratio), whereas each active gammabody is inactive at a molar ratio of 1:100 gammabody:Aβ (Fig. S2).\", \"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0513": {
    "Interaction ID": "AMGAB0513",
    "Antibody ID": "ABID0486",
    "Antibody name": "Aβ16–21",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We also find that gammabodies presenting 6mer Aβ peptides (Aβ residues 16–21, 34–39, and 37–42) within CDR3 are as inhibitory as their parent gammabodies presenting 10mer Aβ peptides, whereas gammabodies presenting 4mer Aβ peptides (Aβ residues 36–39 and 39–42) are inactive (Fig. S2).\", \"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0514": {
    "Interaction ID": "AMGAB0514",
    "Antibody ID": "ABID0487",
    "Antibody name": "Aβ34–39",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We also find that gammabodies presenting 6mer Aβ peptides (Aβ residues 16–21, 34–39, and 37–42) within CDR3 are as inhibitory as their parent gammabodies presenting 10mer Aβ peptides, whereas gammabodies presenting 4mer Aβ peptides (Aβ residues 36–39 and 39–42) are inactive (Fig. S2).\", \"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0515": {
    "Interaction ID": "AMGAB0515",
    "Antibody ID": "ABID0488",
    "Antibody name": "Aβ37–42",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We also find that gammabodies presenting 6mer Aβ peptides (Aβ residues 16–21, 34–39, and 37–42) within CDR3 are as inhibitory as their parent gammabodies presenting 10mer Aβ peptides, whereas gammabodies presenting 4mer Aβ peptides (Aβ residues 36–39 and 39–42) are inactive (Fig. S2).\", \"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0516": {
    "Interaction ID": "AMGAB0516",
    "Antibody ID": "ABID0489",
    "Antibody name": "Aβ36–39",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We also find that gammabodies presenting 6mer Aβ peptides (Aβ residues 16–21, 34–39, and 37–42) within CDR3 are as inhibitory as their parent gammabodies presenting 10mer Aβ peptides, whereas gammabodies presenting 4mer Aβ peptides (Aβ residues 36–39 and 39–42) are inactive (Fig. S2).\", \"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0517": {
    "Interaction ID": "AMGAB0517",
    "Antibody ID": "ABID0490",
    "Antibody name": "Aβ39–42",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We also find that gammabodies presenting 6mer Aβ peptides (Aβ residues 16–21, 34–39, and 37–42) within CDR3 are as inhibitory as their parent gammabodies presenting 10mer Aβ peptides, whereas gammabodies presenting 4mer Aβ peptides (Aβ residues 36–39 and 39–42) are inactive (Fig. S2).\", \"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0518": {
    "Interaction ID": "AMGAB0518",
    "Antibody ID": "ABID0491",
    "Antibody name": "Aβ15–24 V18P mutant",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Moreover, scrambling the grafted Aβ peptides (Fig. 2A) or mutating them with single proline substitutions or glycine insertions (Fig. S2) eliminates the inhibitory activity of gammabodies.\", \"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0519": {
    "Interaction ID": "AMGAB0519",
    "Antibody ID": "ABID0492",
    "Antibody name": "Aβ15–24 19G mutant",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Moreover, scrambling the grafted Aβ peptides (Fig. 2A) or mutating them with single proline substitutions or glycine insertions (Fig. S2) eliminates the inhibitory activity of gammabodies.\", \"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0520": {
    "Interaction ID": "AMGAB0520",
    "Antibody ID": "ABID0493",
    "Antibody name": "Aβ15–24 20G mutant",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Moreover, scrambling the grafted Aβ peptides (Fig. 2A) or mutating them with single proline substitutions or glycine insertions (Fig. S2) eliminates the inhibitory activity of gammabodies.\", \"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0521": {
    "Interaction ID": "AMGAB0521",
    "Antibody ID": "ABID0494",
    "Antibody name": "Aβ33–42 V39P mutant",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Moreover, scrambling the grafted Aβ peptides (Fig. 2A) or mutating them with single proline substitutions or glycine insertions (Fig. S2) eliminates the inhibitory activity of gammabodies.\", \"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0522": {
    "Interaction ID": "AMGAB0522",
    "Antibody ID": "ABID0495",
    "Antibody name": "Aβ33–42 40G mutant",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Moreover, scrambling the grafted Aβ peptides (Fig. 2A) or mutating them with single proline substitutions or glycine insertions (Fig. S2) eliminates the inhibitory activity of gammabodies.\", \"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0523": {
    "Interaction ID": "AMGAB0523",
    "Antibody ID": "ABID0496",
    "Antibody name": "Aβ33–42 41G mutant",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Moreover, scrambling the grafted Aβ peptides (Fig. 2A) or mutating them with single proline substitutions or glycine insertions (Fig. S2) eliminates the inhibitory activity of gammabodies.\", \"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0524": {
    "Interaction ID": "AMGAB0524",
    "Antibody ID": "ABID0497",
    "Antibody name": "Wild-type VH",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Supplementary Figure S2\",",
    "Curator Statement": false
  },
  "AMGAB0525": {
    "Interaction ID": "AMGAB0525",
    "Antibody ID": "ABID0498",
    "Antibody name": "9F1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Importantly, none of these antibodies inhibit Aβ fibrillization at substoichiometric concentrations (1:10 antibody:Aβ molar ratio).\", \"Supplementary Figure S7\", \"Conventional sequence- and conformation-specific antibodies fail to inhibit Aβ fibrillization at substoichiometric concentrations despite that they bind to Aβ.\",",
    "Curator Statement": false
  },
  "AMGAB0526": {
    "Interaction ID": "AMGAB0526",
    "Antibody ID": "ABID0499",
    "Antibody name": "αSyn69-78_G73P",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S8\", \"Single proline substitution or glycine insertion mutations in the grafted peptide segments eliminate the inhibitory activity of each gammabody (Fig. S8). \",",
    "Curator Statement": false
  },
  "AMGAB0527": {
    "Interaction ID": "AMGAB0527",
    "Antibody ID": "ABID0500",
    "Antibody name": "αSyn69-78_V74P",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S8\", \"Single proline substitution or glycine insertion mutations in the grafted peptide segments eliminate the inhibitory activity of each gammabody (Fig. S8). \",",
    "Curator Statement": false
  },
  "AMGAB0528": {
    "Interaction ID": "AMGAB0528",
    "Antibody ID": "ABID0501",
    "Antibody name": "αSyn69-78_72-G-73",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S8\", \"Single proline substitution or glycine insertion mutations in the grafted peptide segments eliminate the inhibitory activity of each gammabody (Fig. S8). \",",
    "Curator Statement": false
  },
  "AMGAB0529": {
    "Interaction ID": "AMGAB0529",
    "Antibody ID": "ABID0502",
    "Antibody name": "αSyn69-78_74-G-75",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S8\", \"Single proline substitution or glycine insertion mutations in the grafted peptide segments eliminate the inhibitory activity of each gammabody (Fig. S8). \",",
    "Curator Statement": false
  },
  "AMGAB0530": {
    "Interaction ID": "AMGAB0530",
    "Antibody ID": "ABID0503",
    "Antibody name": "IAPP22-31_26-G-27",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S8\", \"Single proline substitution or glycine insertion mutations in the grafted peptide segments eliminate the inhibitory activity of each gammabody (Fig. S8). \",",
    "Curator Statement": false
  },
  "AMGAB0531": {
    "Interaction ID": "AMGAB0531",
    "Antibody ID": "ABID0504",
    "Antibody name": "IAPP22-31_25-G-26",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S8\", \"Single proline substitution or glycine insertion mutations in the grafted peptide segments eliminate the inhibitory activity of each gammabody (Fig. S8). \",",
    "Curator Statement": false
  },
  "AMGAB0532": {
    "Interaction ID": "AMGAB0532",
    "Antibody ID": "ABID0505",
    "Antibody name": "IAPP22-31_I26P",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S8\", \"Single proline substitution or glycine insertion mutations in the grafted peptide segments eliminate the inhibitory activity of each gammabody (Fig. S8). \",",
    "Curator Statement": false
  },
  "AMGAB0533": {
    "Interaction ID": "AMGAB0533",
    "Antibody ID": "ABID0506",
    "Antibody name": "IAPP22-31_L27P",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Immunoblotting,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S8\", \"Single proline substitution or glycine insertion mutations in the grafted peptide segments eliminate the inhibitory activity of each gammabody (Fig. S8). \",",
    "Curator Statement": false
  },
  "AMGAB0534": {
    "Interaction ID": "AMGAB0534",
    "Antibody ID": "ABID0507",
    "Antibody name": "5C2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM), Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...) ,ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 7\", \"Importantly, conventional sequence- and conformation-specific antibodies against α-Synuclein and IAPP that were obtained via immunization are noninhibitory at substoichiometric concentrations (1:10 antibody:monomer molar ratio; Fig. 7 and Fig. S9).\", \"Supplementary Figure S9\",",
    "Curator Statement": false
  },
  "AMGAB0535": {
    "Interaction ID": "AMGAB0535",
    "Antibody ID": "ABID0507",
    "Antibody name": "5C2",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 7\", \"Importantly, conventional sequence- and conformation-specific antibodies against α-Synuclein and IAPP that were obtained via immunization are noninhibitory at substoichiometric concentrations (1:10 antibody:monomer molar ratio; Fig. 7 and Fig. S9).\",",
    "Curator Statement": false
  },
  "AMGAB0536": {
    "Interaction ID": "AMGAB0536",
    "Antibody ID": "ABID0508",
    "Antibody name": "R10/99",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 7\", \"Importantly, conventional sequence- and conformation-specific antibodies against α-Synuclein and IAPP that were obtained via immunization are noninhibitory at substoichiometric concentrations (1:10 antibody:monomer molar ratio; Fig. 7 and Fig. S9).\",",
    "Curator Statement": false
  },
  "AMGAB0537": {
    "Interaction ID": "AMGAB0537",
    "Antibody ID": "ABID0508",
    "Antibody name": "R10/99",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1073/pnas.1208797109",
    "PMID": 23161913.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Atomic force microscopy (AFM), Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...) ,ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 7\", \"Importantly, conventional sequence- and conformation-specific antibodies against α-Synuclein and IAPP that were obtained via immunization are noninhibitory at substoichiometric concentrations (1:10 antibody:monomer molar ratio; Fig. 7 and Fig. S9).\", \"Supplementary Figure S9\",",
    "Curator Statement": false
  },
  "AMGAB0538": {
    "Interaction ID": "AMGAB0538",
    "Antibody ID": "ABID0532",
    "Antibody name": "SAP-5",
    "Amyloid ID": "AGAMYID0017",
    "Amyloid name": "Serum amyloid P-component",
    "DOI": "10.1073/pnas.1306621110",
    "PMID": 23959890.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We recently showed that administration of anti-human SAP antibodies to AA amyloidotic mice in which the amyloid deposits had been loaded with human SAP leads to macrophage-mediated elimination of hepatic and splenic amyloid (25). In contrast to the standard mouse AA amyloidosis model, cardiac amyloid is consistently present in the new SAA transgenic model. SAA transgenic mice with abundant amyloid after exposure to doxycycline were therefore given three daily parenteral injections of human SAP to load up the amyloid deposits, and 5 d after the last injection, when all human SAP had left the circulation, they were treated with monoclonal mouse IgG2a anti-human SAP antibodies. After a single dose of anti-SAP, spleen and liver amyloid deposits were, as usual, substantially reduced (both P < 0.001 compared with amyloidotic controls not given the antibody), but there was no significant difference in extent of cardiac amyloid. However, after a second treatment with SAP and anti-SAP 1 mo later, the cardiac amyloid deposits were substantially diminished (P = 0.014; Fig. 5).\", \"Figure 5\", \"The development of cardiac amyloidosis in the transgenic model allowed us to show that our recently developed antibody therapy (25) effectively reduces cardiac amyloid load, as it does amyloid in the spleen and liver. \",",
    "Curator Statement": false
  },
  "AMGAB0539": {
    "Interaction ID": "AMGAB0539",
    "Antibody ID": "ABID0518",
    "Antibody name": "DesAb-F",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1422401112",
    "PMID": 26216991.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Sedimentation Assay, ThT - Aggregation kinetics,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"By monitoring soluble α-synuclein over four-day aggregation (SI Materials and Methods), we found that DesAb-F has a strong inhibitory effect, even at a substoichiometric concentration (1:10) (Fig. 5A). \", \"Figure 5\", \"Supplementary Figure S7\",",
    "Curator Statement": false
  },
  "AMGAB0540": {
    "Interaction ID": "AMGAB0540",
    "Antibody ID": "ABID0518",
    "Antibody name": "DesAb-F",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1422401112",
    "PMID": 26216991.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"To support this conclusion, we performed seeded aggregation assays at increasing concentrations of DesAb-F (SI Materials and Methods). We found a specific concentration-dependent effect of the antibody on the elongation phase of α-synuclein aggregation (Fig. 5 B and C), and we also detected a strong dependence on the concentration of α-synuclein seeds (Fig. 5D).\", \"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0541": {
    "Interaction ID": "AMGAB0541",
    "Antibody ID": "ABID0541",
    "Antibody name": "DesAb-IAPP",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1073/pnas.1422401112",
    "PMID": 26216991.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Besides, the fact that DesAb-IAPP only shows a negligible effect on the aggregation of α-synuclein, even at a 1:2 DesAb-monomer ratio (Fig. S7), suggests that the observed inhibition specifically comes from the grafted complementary peptide.\", \"Supplementary Figure S7\",",
    "Curator Statement": false
  },
  "AMGAB0542": {
    "Interaction ID": "AMGAB0542",
    "Antibody ID": "ABID0364",
    "Antibody name": "I2",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1700407114",
    "PMID": 28584111.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "Heavy Chain: CDR1: SYAMS, CDR2: XIYNYGYTTNYADSVKG, CDR3: TAYGFDY,  Light Chain: CDR1: RASQSISSYLN, CDR2: NASTLQS, CDR3: QQNNSSPTT",
    "Quote of the interaction": "\"For four of the candidate scFvs—I2, I48, J44, and J57—we found that the main effect of their presence in Aβ42 solutions was a change in the slope of the growth region (Fig. 3). The data are well fitted assuming a selective reduction of k2 (Fig. 3) but cannot be fitted at all if only kn (SI Appendix, Fig. S2), or only k+ (SI Appendix, Fig. S3), is varied. The strongest inhibitory effect of these scFvs is thus likely to be on secondary nucleation, whereas primary nucleation and elongation remain essentially unaffected, in agreement with the scenario shown in Fig. 2B. The fits to the data at the higher scFv concentrations indicate a very low value of k2. The effect saturates at ∼1–2 µM scFv in solutions containing initially 3 µM Aβ42 monomers, suggesting that secondary nucleation is effectively completely suppressed in the presence of high concentration of these scFvs, and the secondary nucleation rate is much lower than the primary nucleation rate essentially during the full time course of the aggregation reaction.\", \" The scFv I2 appears to have somewhat lower affinity (SI Appendix, Fig. S1), and at the highest concentrations used, its inhibitory effect corresponds to ca. 20-fold reduction in k2, thus some secondary nucleation still occurs at a detectable rate. \", \"We find that the fibril-specific scFvs from clones I2, I48, J44, and J57 most likely inhibit Aβ42 aggregation through selective reduction of the rate constant for secondary nucleation. In the presence of scFvs I48, J44, and J57 at molar ratios above ca. 1:2 scFv:Aβ42, secondary nucleation has no detectable kinetic significance, although for I2 there is a residual contribution from this microscopic step.\", \"Figure 5\", \" However, scFvs I2, I48, J57, and J44 diminish this seeding effect (Fig. 5 A–D) and 1% and 3% seeds have much lower catalytic effect than for Aβ42 alone. The aggregation in the presence of these scFvs is dominated by primary nucleation and still very strongly retarded relative to the behavior observed in the absence of scFv. At 30% seed, the aggregation kinetics of Aβ42 in the absence of scFv is greatly accelerated due to rapid elongation of the seeds, seen as the emergence of observable growth from time 0 (Fig. 5 E and F). The growth rate at early times can reveal effects on the elongation rate constant, and we find that I2, I48, J57, and J44 cause at most a factor of 1.3 change in this rate (Fig. 5 F and G), compared with the more than 10-fold (I2) or more than 100-fold (I48, J44, and J57) reduction in the rate constant for secondary nucleation (Figs. 3 E and F and 5G).\",\"Indeed, if the sites for secondary nucleation and elongation were to be identical, it would not be possible to block selectively secondary nucleation without affecting elongation and vice versa. The scFvs I2, I48, J44, and J57 act in a manner similar to Brichos, which binds along the fibril surface (21) and blocks selectively secondary nucleation. These scFvs are likely to bind to epitopes presented along the sides of the fibrils in a manner that prevents Aβ42 monomer binding or nucleation. The scFvs I68 and J7 are intriguing in that they seem to show a duality of behaviors, with selective inhibition of secondary nucleation processes at low concentration, whereas at higher concentrations the elongation step also appears to be affected (Fig. 4 A and B and SI Appendix, Fig. S5).\",\"Starting from large phage display libraries of single-chain antibody fragments (scFvs), the three-stage approach that we describe includes (i) selection of scFvs with high affinity for Aβ42 fibrils after removal of scFvs that bind Aβ42 in its monomeric form; (ii) ranking, by surface plasmon resonance affinity measurements, of the resulting candidate scFvs that bind to the Aβ42 fibrils; and (iii) kinetic screening and analysis to find the scFvs that inhibit selectively the fibril-catalyzed secondary nucleation process in Aβ42 aggregation.\", \"By applying this approach, we have identified four scFvs that inhibit specifically the fibril-dependent secondary nucleation process.\", \"These macroscopic aggregation curves are clearly affected by all four scFvs but not by randomly selected scFvs from the initial pool (Fig. 4 D and E).\", \"Figure 3\", \"Figure 4\", \"As a consequence of secondary nucleation inhibition, the reactive flux is redirected to a pathway including primary nucleation and elongation only. This means that a much smaller number of new aggregates are created (Fig. 2E) and a larger fraction of monomers are consumed in elongation of those fewer aggregates, leading to longer fibrils on average.\", \"Secondary nucleation is a positive feedback mechanism that can lead to the rapid amplification of the number of aggregates once an initial population has been formed (20, 22) and also be very effective in the production of toxic oligomers (20, 21). Inhibition of secondary nucleation, therefore, appears likely to be an important approach to reduce the pathogenicity associated with protein aggregation (34)\", \"We have shown in this study that screening of phage display libraries for antibody fragments (scFvs) that bind to amyloid fibrils, combined with affinity ranking and kinetic screening, enables the identification of antibodies with the capacity to inhibit fibril-dependent secondary nucleation processes. Importantly, our approach allows scFvs that inhibit elongation to be detected and eliminated from further investigations, as such species can cause significant apparent inhibition of the overall aggregation reaction but are unlikely to result in a significant reduction of toxic species and could even lead to an increase in the overall production of oligomers.\", \"Figure S3\",\"Figure S2\", \"Alternative kinetic analyses of scFvs found to selectively inhibit secondary nucleation. Aggregation kinetics of solutions of 3 µM Aβ42 monomer in the absence (black) and presence of four different scFvs from the phage display selection at concentrations ranging from 0.3 to 3.0 µM: scFv-I48 (A), scFv-I2 (B), scFv-J44 (C) and scFv-J57 (D).\"",
    "Curator Statement": false
  },
  "AMGAB0543": {
    "Interaction ID": "AMGAB0543",
    "Antibody ID": "ABID0365",
    "Antibody name": "I48",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1700407114",
    "PMID": 28584111.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "Heavy Chain: CDR1: SYAMS, CDR2: GINTTGSNTSYADSVKG, CDR3: SDSDFDY,  Light Chain: CDR1: RASQSISSYLN, CDR2: DASSLQS, CDR3: QQSNATPAT",
    "Quote of the interaction": "\"For four of the candidate scFvs—I2, I48, J44, and J57—we found that the main effect of their presence in Aβ42 solutions was a change in the slope of the growth region (Fig. 3). The data are well fitted assuming a selective reduction of k2 (Fig. 3) but cannot be fitted at all if only kn (SI Appendix, Fig. S2), or only k+ (SI Appendix, Fig. S3), is varied. The strongest inhibitory effect of these scFvs is thus likely to be on secondary nucleation, whereas primary nucleation and elongation remain essentially unaffected, in agreement with the scenario shown in Fig. 2B. The fits to the data at the higher scFv concentrations indicate a very low value of k2. The effect saturates at ∼1–2 µM scFv in solutions containing initially 3 µM Aβ42 monomers, suggesting that secondary nucleation is effectively completely suppressed in the presence of high concentration of these scFvs, and the secondary nucleation rate is much lower than the primary nucleation rate essentially during the full time course of the aggregation reaction.\", \"We find that the fibril-specific scFvs from clones I2, I48, J44, and J57 most likely inhibit Aβ42 aggregation through selective reduction of the rate constant for secondary nucleation. In the presence of scFvs I48, J44, and J57 at molar ratios above ca. 1:2 scFv:Aβ42, secondary nucleation has no detectable kinetic significance, although for I2 there is a residual contribution from this microscopic step.\", \"Figure 5\", \" However, scFvs I2, I48, J57, and J44 diminish this seeding effect (Fig. 5 A–D) and 1% and 3% seeds have much lower catalytic effect than for Aβ42 alone. The aggregation in the presence of these scFvs is dominated by primary nucleation and still very strongly retarded relative to the behavior observed in the absence of scFv. At 30% seed, the aggregation kinetics of Aβ42 in the absence of scFv is greatly accelerated due to rapid elongation of the seeds, seen as the emergence of observable growth from time 0 (Fig. 5 E and F). The growth rate at early times can reveal effects on the elongation rate constant, and we find that I2, I48, J57, and J44 cause at most a factor of 1.3 change in this rate (Fig. 5 F and G), compared with the more than 10-fold (I2) or more than 100-fold (I48, J44, and J57) reduction in the rate constant for secondary nucleation (Figs. 3 E and F and 5G).\", \"Indeed, if the sites for secondary nucleation and elongation were to be identical, it would not be possible to block selectively secondary nucleation without affecting elongation and vice versa. The scFvs I2, I48, J44, and J57 act in a manner similar to Brichos, which binds along the fibril surface (21) and blocks selectively secondary nucleation. These scFvs are likely to bind to epitopes presented along the sides of the fibrils in a manner that prevents Aβ42 monomer binding or nucleation. The scFvs I68 and J7 are intriguing in that they seem to show a duality of behaviors, with selective inhibition of secondary nucleation processes at low concentration, whereas at higher concentrations the elongation step also appears to be affected (Fig. 4 A and B and SI Appendix, Fig. S5).\",\"Starting from large phage display libraries of single-chain antibody fragments (scFvs), the three-stage approach that we describe includes (i) selection of scFvs with high affinity for Aβ42 fibrils after removal of scFvs that bind Aβ42 in its monomeric form; (ii) ranking, by surface plasmon resonance affinity measurements, of the resulting candidate scFvs that bind to the Aβ42 fibrils; and (iii) kinetic screening and analysis to find the scFvs that inhibit selectively the fibril-catalyzed secondary nucleation process in Aβ42 aggregation.\", \"By applying this approach, we have identified four scFvs that inhibit specifically the fibril-dependent secondary nucleation process.\", \"These macroscopic aggregation curves are clearly affected by all four scFvs but not by randomly selected scFvs from the initial pool (Fig. 4 D and E).\", \"Figure 3\", \"Figure 4\", \"As a consequence of secondary nucleation inhibition, the reactive flux is redirected to a pathway including primary nucleation and elongation only. This means that a much smaller number of new aggregates are created (Fig. 2E) and a larger fraction of monomers are consumed in elongation of those fewer aggregates, leading to longer fibrils on average.\", \"Secondary nucleation is a positive feedback mechanism that can lead to the rapid amplification of the number of aggregates once an initial population has been formed (20, 22) and also be very effective in the production of toxic oligomers (20, 21). Inhibition of secondary nucleation, therefore, appears likely to be an important approach to reduce the pathogenicity associated with protein aggregation (34)\", \"We have shown in this study that screening of phage display libraries for antibody fragments (scFvs) that bind to amyloid fibrils, combined with affinity ranking and kinetic screening, enables the identification of antibodies with the capacity to inhibit fibril-dependent secondary nucleation processes. Importantly, our approach allows scFvs that inhibit elongation to be detected and eliminated from further investigations, as such species can cause significant apparent inhibition of the overall aggregation reaction but are unlikely to result in a significant reduction of toxic species and could even lead to an increase in the overall production of oligomers.\", \"Figure S3\",\"Figure S2\", \"Alternative kinetic analyses of scFvs found to selectively inhibit secondary nucleation. Aggregation kinetics of solutions of 3 µM Aβ42 monomer in the absence (black) and presence of four different scFvs from the phage display selection at concentrations ranging from 0.3 to 3.0 µM: scFv-I48 (A), scFv-I2 (B), scFv-J44 (C) and scFv-J57 (D).\"",
    "Curator Statement": false
  },
  "AMGAB0544": {
    "Interaction ID": "AMGAB0544",
    "Antibody ID": "ABID0366",
    "Antibody name": "J44",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1700407114",
    "PMID": 28584111.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "Heavy Chain: CDR1: SYAMS, CDR2: AINKGGYKTYYADSVKG, CDR3: TPKPFDY,  Light Chain: CDR1: RASQSISSYLN, CDR2: GASVLQS, CDR3: QQANTKPAT",
    "Quote of the interaction": "\"For four of the candidate scFvs—I2, I48, J44, and J57—we found that the main effect of their presence in Aβ42 solutions was a change in the slope of the growth region (Fig. 3). The data are well fitted assuming a selective reduction of k2 (Fig. 3) but cannot be fitted at all if only kn (SI Appendix, Fig. S2), or only k+ (SI Appendix, Fig. S3), is varied. The strongest inhibitory effect of these scFvs is thus likely to be on secondary nucleation, whereas primary nucleation and elongation remain essentially unaffected, in agreement with the scenario shown in Fig. 2B. The fits to the data at the higher scFv concentrations indicate a very low value of k2. The effect saturates at ∼1–2 µM scFv in solutions containing initially 3 µM Aβ42 monomers, suggesting that secondary nucleation is effectively completely suppressed in the presence of high concentration of these scFvs, and the secondary nucleation rate is much lower than the primary nucleation rate essentially during the full time course of the aggregation reaction.\", \"We find that the fibril-specific scFvs from clones I2, I48, J44, and J57 most likely inhibit Aβ42 aggregation through selective reduction of the rate constant for secondary nucleation. In the presence of scFvs I48, J44, and J57 at molar ratios above ca. 1:2 scFv:Aβ42, secondary nucleation has no detectable kinetic significance, although for I2 there is a residual contribution from this microscopic step.\", \"Figure 5\", \" However, scFvs I2, I48, J57, and J44 diminish this seeding effect (Fig. 5 A–D) and 1% and 3% seeds have much lower catalytic effect than for Aβ42 alone. The aggregation in the presence of these scFvs is dominated by primary nucleation and still very strongly retarded relative to the behavior observed in the absence of scFv. At 30% seed, the aggregation kinetics of Aβ42 in the absence of scFv is greatly accelerated due to rapid elongation of the seeds, seen as the emergence of observable growth from time 0 (Fig. 5 E and F). The growth rate at early times can reveal effects on the elongation rate constant, and we find that I2, I48, J57, and J44 cause at most a factor of 1.3 change in this rate (Fig. 5 F and G), compared with the more than 10-fold (I2) or more than 100-fold (I48, J44, and J57) reduction in the rate constant for secondary nucleation (Figs. 3 E and F and 5G).\", \"Indeed, if the sites for secondary nucleation and elongation were to be identical, it would not be possible to block selectively secondary nucleation without affecting elongation and vice versa. The scFvs I2, I48, J44, and J57 act in a manner similar to Brichos, which binds along the fibril surface (21) and blocks selectively secondary nucleation. These scFvs are likely to bind to epitopes presented along the sides of the fibrils in a manner that prevents Aβ42 monomer binding or nucleation. The scFvs I68 and J7 are intriguing in that they seem to show a duality of behaviors, with selective inhibition of secondary nucleation processes at low concentration, whereas at higher concentrations the elongation step also appears to be affected (Fig. 4 A and B and SI Appendix, Fig. S5).\",\"Starting from large phage display libraries of single-chain antibody fragments (scFvs), the three-stage approach that we describe includes (i) selection of scFvs with high affinity for Aβ42 fibrils after removal of scFvs that bind Aβ42 in its monomeric form; (ii) ranking, by surface plasmon resonance affinity measurements, of the resulting candidate scFvs that bind to the Aβ42 fibrils; and (iii) kinetic screening and analysis to find the scFvs that inhibit selectively the fibril-catalyzed secondary nucleation process in Aβ42 aggregation.\", \"By applying this approach, we have identified four scFvs that inhibit specifically the fibril-dependent secondary nucleation process.\", \"These macroscopic aggregation curves are clearly affected by all four scFvs but not by randomly selected scFvs from the initial pool (Fig. 4 D and E).\", \"Figure 3\", \"Figure 4\", \"As a consequence of secondary nucleation inhibition, the reactive flux is redirected to a pathway including primary nucleation and elongation only. This means that a much smaller number of new aggregates are created (Fig. 2E) and a larger fraction of monomers are consumed in elongation of those fewer aggregates, leading to longer fibrils on average.\", \"Secondary nucleation is a positive feedback mechanism that can lead to the rapid amplification of the number of aggregates once an initial population has been formed (20, 22) and also be very effective in the production of toxic oligomers (20, 21). Inhibition of secondary nucleation, therefore, appears likely to be an important approach to reduce the pathogenicity associated with protein aggregation (34)\", \"We have shown in this study that screening of phage display libraries for antibody fragments (scFvs) that bind to amyloid fibrils, combined with affinity ranking and kinetic screening, enables the identification of antibodies with the capacity to inhibit fibril-dependent secondary nucleation processes. Importantly, our approach allows scFvs that inhibit elongation to be detected and eliminated from further investigations, as such species can cause significant apparent inhibition of the overall aggregation reaction but are unlikely to result in a significant reduction of toxic species and could even lead to an increase in the overall production of oligomers.\", \"Figure S3\",\"Figure S2\", \"Alternative kinetic analyses of scFvs found to selectively inhibit secondary nucleation. Aggregation kinetics of solutions of 3 µM Aβ42 monomer in the absence (black) and presence of four different scFvs from the phage display selection at concentrations ranging from 0.3 to 3.0 µM: scFv-I48 (A), scFv-I2 (B), scFv-J44 (C) and scFv-J57 (D).\"",
    "Curator Statement": false
  },
  "AMGAB0545": {
    "Interaction ID": "AMGAB0545",
    "Antibody ID": "ABID0367",
    "Antibody name": "J57",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1700407114",
    "PMID": 28584111.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "Heavy Chain: CDR1: SYAMS, CDR2: AINKGGYKTYYADSVKG, CDR3: TPKPFDY,  Light Chain: CDR1: RASQSISSYLN, CDR2: GASVLQS, CDR3: QQANTKPAT",
    "Quote of the interaction": "\"For four of the candidate scFvs—I2, I48, J44, and J57—we found that the main effect of their presence in Aβ42 solutions was a change in the slope of the growth region (Fig. 3). The data are well fitted assuming a selective reduction of k2 (Fig. 3) but cannot be fitted at all if only kn (SI Appendix, Fig. S2), or only k+ (SI Appendix, Fig. S3), is varied. The strongest inhibitory effect of these scFvs is thus likely to be on secondary nucleation, whereas primary nucleation and elongation remain essentially unaffected, in agreement with the scenario shown in Fig. 2B. The fits to the data at the higher scFv concentrations indicate a very low value of k2. The effect saturates at ∼1–2 µM scFv in solutions containing initially 3 µM Aβ42 monomers, suggesting that secondary nucleation is effectively completely suppressed in the presence of high concentration of these scFvs, and the secondary nucleation rate is much lower than the primary nucleation rate essentially during the full time course of the aggregation reaction.\", \"We find that the fibril-specific scFvs from clones I2, I48, J44, and J57 most likely inhibit Aβ42 aggregation through selective reduction of the rate constant for secondary nucleation. In the presence of scFvs I48, J44, and J57 at molar ratios above ca. 1:2 scFv:Aβ42, secondary nucleation has no detectable kinetic significance, although for I2 there is a residual contribution from this microscopic step.\", \"Figure 5\", \" However, scFvs I2, I48, J57, and J44 diminish this seeding effect (Fig. 5 A–D) and 1% and 3% seeds have much lower catalytic effect than for Aβ42 alone. The aggregation in the presence of these scFvs is dominated by primary nucleation and still very strongly retarded relative to the behavior observed in the absence of scFv. At 30% seed, the aggregation kinetics of Aβ42 in the absence of scFv is greatly accelerated due to rapid elongation of the seeds, seen as the emergence of observable growth from time 0 (Fig. 5 E and F). The growth rate at early times can reveal effects on the elongation rate constant, and we find that I2, I48, J57, and J44 cause at most a factor of 1.3 change in this rate (Fig. 5 F and G), compared with the more than 10-fold (I2) or more than 100-fold (I48, J44, and J57) reduction in the rate constant for secondary nucleation (Figs. 3 E and F and 5G).\", \"Indeed, if the sites for secondary nucleation and elongation were to be identical, it would not be possible to block selectively secondary nucleation without affecting elongation and vice versa. The scFvs I2, I48, J44, and J57 act in a manner similar to Brichos, which binds along the fibril surface (21) and blocks selectively secondary nucleation. These scFvs are likely to bind to epitopes presented along the sides of the fibrils in a manner that prevents Aβ42 monomer binding or nucleation. The scFvs I68 and J7 are intriguing in that they seem to show a duality of behaviors, with selective inhibition of secondary nucleation processes at low concentration, whereas at higher concentrations the elongation step also appears to be affected (Fig. 4 A and B and SI Appendix, Fig. S5).\",\"Starting from large phage display libraries of single-chain antibody fragments (scFvs), the three-stage approach that we describe includes (i) selection of scFvs with high affinity for Aβ42 fibrils after removal of scFvs that bind Aβ42 in its monomeric form; (ii) ranking, by surface plasmon resonance affinity measurements, of the resulting candidate scFvs that bind to the Aβ42 fibrils; and (iii) kinetic screening and analysis to find the scFvs that inhibit selectively the fibril-catalyzed secondary nucleation process in Aβ42 aggregation.\", \"By applying this approach, we have identified four scFvs that inhibit specifically the fibril-dependent secondary nucleation process.\", \"These macroscopic aggregation curves are clearly affected by all four scFvs but not by randomly selected scFvs from the initial pool (Fig. 4 D and E).\", \"Figure 3\", \"Figure 4\", \"As a consequence of secondary nucleation inhibition, the reactive flux is redirected to a pathway including primary nucleation and elongation only. This means that a much smaller number of new aggregates are created (Fig. 2E) and a larger fraction of monomers are consumed in elongation of those fewer aggregates, leading to longer fibrils on average.\", \"Secondary nucleation is a positive feedback mechanism that can lead to the rapid amplification of the number of aggregates once an initial population has been formed (20, 22) and also be very effective in the production of toxic oligomers (20, 21). Inhibition of secondary nucleation, therefore, appears likely to be an important approach to reduce the pathogenicity associated with protein aggregation (34)\", \"We have shown in this study that screening of phage display libraries for antibody fragments (scFvs) that bind to amyloid fibrils, combined with affinity ranking and kinetic screening, enables the identification of antibodies with the capacity to inhibit fibril-dependent secondary nucleation processes. Importantly, our approach allows scFvs that inhibit elongation to be detected and eliminated from further investigations, as such species can cause significant apparent inhibition of the overall aggregation reaction but are unlikely to result in a significant reduction of toxic species and could even lead to an increase in the overall production of oligomers.\", \"Figure S3\", \"Figure S2\", \"Alternative kinetic analyses of scFvs found to selectively inhibit secondary nucleation. Aggregation kinetics of solutions of 3 µM Aβ42 monomer in the absence (black) and presence of four different scFvs from the phage display selection at concentrations ranging from 0.3 to 3.0 µM: scFv-I48 (A), scFv-I2 (B), scFv-J44 (C) and scFv-J57 (D).\"",
    "Curator Statement": false
  },
  "AMGAB0546": {
    "Interaction ID": "AMGAB0546",
    "Antibody ID": "ABID0368",
    "Antibody name": "I68",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1700407114",
    "PMID": 28584111.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "Heavy Chain: CDR1: SYAMS, CDR2: GIDYTGSTAYAYADSVKG, CDR3: SDNDFDY,   Light Chain: CDR1: RASQSISSYLN, CDR2: TASALQS, CDR3: QQYNNGPAT",
    "Quote of the interaction": "\"In the presence of scFvs J7, J46, and I68, the aggregation kinetics indicate that the elongation rate constant may also be affected (Fig. 4). The curves at low concentration of scFvs J7 and I68 can be fitted if only k2 is reduced (Fig. 4 A and B). The data at a higher concentration of scFv J7 and I68 can only be fitted by assuming that k+ or kn are reduced as well (SI Appendix, Fig. S5), suggesting that elongation may be affected. J46 appears to affect the elongation rate at all concentrations (Fig. 4C).\", \"Indeed, if the sites for secondary nucleation and elongation were to be identical, it would not be possible to block selectively secondary nucleation without affecting elongation and vice versa. The scFvs I2, I48, J44, and J57 act in a manner similar to Brichos, which binds along the fibril surface (21) and blocks selectively secondary nucleation. These scFvs are likely to bind to epitopes presented along the sides of the fibrils in a manner that prevents Aβ42 monomer binding or nucleation. The scFvs I68 and J7 are intriguing in that they seem to show a duality of behaviors, with selective inhibition of secondary nucleation processes at low concentration, whereas at higher concentrations the elongation step also appears to be affected (Fig. 4 A and B and SI Appendix, Fig. S5).\", \"Starting from large phage display libraries of single-chain antibody fragments (scFvs), the three-stage approach that we describe includes (i) selection of scFvs with high affinity for Aβ42 fibrils after removal of scFvs that bind Aβ42 in its monomeric form; (ii) ranking, by surface plasmon resonance affinity measurements, of the resulting candidate scFvs that bind to the Aβ42 fibrils; and (iii) kinetic screening and analysis to find the scFvs that inhibit selectively the fibril-catalyzed secondary nucleation process in Aβ42 aggregation.\", \"By applying this approach, we have identified four scFvs that inhibit specifically the fibril-dependent secondary nucleation process.\", \"These macroscopic aggregation curves are clearly affected by all four scFvs but not by randomly selected scFvs from the initial pool (Fig. 4 D and E).\", \"Figure 3\", \"Figure 4\", \"As a consequence of secondary nucleation inhibition, the reactive flux is redirected to a pathway including primary nucleation and elongation only. This means that a much smaller number of new aggregates are created (Fig. 2E) and a larger fraction of monomers are consumed in elongation of those fewer aggregates, leading to longer fibrils on average.\", \"Secondary nucleation is a positive feedback mechanism that can lead to the rapid amplification of the number of aggregates once an initial population has been formed (20, 22) and also be very effective in the production of toxic oligomers (20, 21). Inhibition of secondary nucleation, therefore, appears likely to be an important approach to reduce the pathogenicity associated with protein aggregation (34)\", \"We have shown in this study that screening of phage display libraries for antibody fragments (scFvs) that bind to amyloid fibrils, combined with affinity ranking and kinetic screening, enables the identification of antibodies with the capacity to inhibit fibril-dependent secondary nucleation processes. Importantly, our approach allows scFvs that inhibit elongation to be detected and eliminated from further investigations, as such species can cause significant apparent inhibition of the overall aggregation reaction but are unlikely to result in a significant reduction of toxic species and could even lead to an increase in the overall production of oligomers.\", \"Figure S5\",",
    "Curator Statement": false
  },
  "AMGAB0547": {
    "Interaction ID": "AMGAB0547",
    "Antibody ID": "ABID0369",
    "Antibody name": "J7",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1700407114",
    "PMID": 28584111.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "Heavy Chain: CDR1: SYAMS, CDR2: TIKSKGNH TVYADSVKG, CDR3: RNRPFDY,  Light Chain: CDR1: RASQSISSYLN, CDR2: SASELQS, CDR3: QQQKYPPT",
    "Quote of the interaction": "\"In the presence of scFvs J7, J46, and I68, the aggregation kinetics indicate that the elongation rate constant may also be affected (Fig. 4). The curves at low concentration of scFvs J7 and I68 can be fitted if only k2 is reduced (Fig. 4 A and B). The data at a higher concentration of scFv J7 and I68 can only be fitted by assuming that k+ or kn are reduced as well (SI Appendix, Fig. S5), suggesting that elongation may be affected. J46 appears to affect the elongation rate at all concentrations (Fig. 4C).\", \"Indeed, if the sites for secondary nucleation and elongation were to be identical, it would not be possible to block selectively secondary nucleation without affecting elongation and vice versa. The scFvs I2, I48, J44, and J57 act in a manner similar to Brichos, which binds along the fibril surface (21) and blocks selectively secondary nucleation. These scFvs are likely to bind to epitopes presented along the sides of the fibrils in a manner that prevents Aβ42 monomer binding or nucleation. The scFvs I68 and J7 are intriguing in that they seem to show a duality of behaviors, with selective inhibition of secondary nucleation processes at low concentration, whereas at higher concentrations the elongation step also appears to be affected (Fig. 4 A and B and SI Appendix, Fig. S5).\", \"Starting from large phage display libraries of single-chain antibody fragments (scFvs), the three-stage approach that we describe includes (i) selection of scFvs with high affinity for Aβ42 fibrils after removal of scFvs that bind Aβ42 in its monomeric form; (ii) ranking, by surface plasmon resonance affinity measurements, of the resulting candidate scFvs that bind to the Aβ42 fibrils; and (iii) kinetic screening and analysis to find the scFvs that inhibit selectively the fibril-catalyzed secondary nucleation process in Aβ42 aggregation.\", \"By applying this approach, we have identified four scFvs that inhibit specifically the fibril-dependent secondary nucleation process.\", \"These macroscopic aggregation curves are clearly affected by all four scFvs but not by randomly selected scFvs from the initial pool (Fig. 4 D and E).\", \"Figure 3\", \"Figure 4\", \"As a consequence of secondary nucleation inhibition, the reactive flux is redirected to a pathway including primary nucleation and elongation only. This means that a much smaller number of new aggregates are created (Fig. 2E) and a larger fraction of monomers are consumed in elongation of those fewer aggregates, leading to longer fibrils on average.\", \"Secondary nucleation is a positive feedback mechanism that can lead to the rapid amplification of the number of aggregates once an initial population has been formed (20, 22) and also be very effective in the production of toxic oligomers (20, 21). Inhibition of secondary nucleation, therefore, appears likely to be an important approach to reduce the pathogenicity associated with protein aggregation (34)\", \"We have shown in this study that screening of phage display libraries for antibody fragments (scFvs) that bind to amyloid fibrils, combined with affinity ranking and kinetic screening, enables the identification of antibodies with the capacity to inhibit fibril-dependent secondary nucleation processes. Importantly, our approach allows scFvs that inhibit elongation to be detected and eliminated from further investigations, as such species can cause significant apparent inhibition of the overall aggregation reaction but are unlikely to result in a significant reduction of toxic species and could even lead to an increase in the overall production of oligomers.\", \"Figure S5\",",
    "Curator Statement": false
  },
  "AMGAB0548": {
    "Interaction ID": "AMGAB0548",
    "Antibody ID": "ABID0370",
    "Antibody name": "J46",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1073/pnas.1700407114",
    "PMID": 28584111.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "Heavy Chain: CDR1: SYAMS, CDR2: TISNXGVQTXYADSVKG, CDR3: RLHRFDY,  Light Chain: CDR1: RASQSISSYLN, CDR2: RASSLQS, CDR3: QQRGHSPPT",
    "Quote of the interaction": "\"In the presence of scFvs J7, J46, and I68, the aggregation kinetics indicate that the elongation rate constant may also be affected (Fig. 4). The curves at low concentration of scFvs J7 and I68 can be fitted if only k2 is reduced (Fig. 4 A and B). The data at a higher concentration of scFv J7 and I68 can only be fitted by assuming that k+ or kn are reduced as well (SI Appendix, Fig. S5), suggesting that elongation may be affected. J46 appears to affect the elongation rate at all concentrations (Fig. 4C).\", \"Starting from large phage display libraries of single-chain antibody fragments (scFvs), the three-stage approach that we describe includes (i) selection of scFvs with high affinity for Aβ42 fibrils after removal of scFvs that bind Aβ42 in its monomeric form; (ii) ranking, by surface plasmon resonance affinity measurements, of the resulting candidate scFvs that bind to the Aβ42 fibrils; and (iii) kinetic screening and analysis to find the scFvs that inhibit selectively the fibril-catalyzed secondary nucleation process in Aβ42 aggregation.\", \"By applying this approach, we have identified four scFvs that inhibit specifically the fibril-dependent secondary nucleation process.\", \"These macroscopic aggregation curves are clearly affected by all four scFvs but not by randomly selected scFvs from the initial pool (Fig. 4 D and E).\", \"Figure 3\", \"Figure 4\", \"As a consequence of secondary nucleation inhibition, the reactive flux is redirected to a pathway including primary nucleation and elongation only. This means that a much smaller number of new aggregates are created (Fig. 2E) and a larger fraction of monomers are consumed in elongation of those fewer aggregates, leading to longer fibrils on average.\", \"Secondary nucleation is a positive feedback mechanism that can lead to the rapid amplification of the number of aggregates once an initial population has been formed (20, 22) and also be very effective in the production of toxic oligomers (20, 21). Inhibition of secondary nucleation, therefore, appears likely to be an important approach to reduce the pathogenicity associated with protein aggregation (34)\", \"We have shown in this study that screening of phage display libraries for antibody fragments (scFvs) that bind to amyloid fibrils, combined with affinity ranking and kinetic screening, enables the identification of antibodies with the capacity to inhibit fibril-dependent secondary nucleation processes. Importantly, our approach allows scFvs that inhibit elongation to be detected and eliminated from further investigations, as such species can cause significant apparent inhibition of the overall aggregation reaction but are unlikely to result in a significant reduction of toxic species and could even lead to an increase in the overall production of oligomers.\", \"Figure S5\"",
    "Curator Statement": false
  },
  "AMGAB0549": {
    "Interaction ID": "AMGAB0549",
    "Antibody ID": "ABID0009.9",
    "Antibody name": "m11-1F4",
    "Amyloid ID": "AGAMYID0009",
    "Amyloid name": "Antibody Light chain",
    "DOI": "10.1073/pnas.1805515115",
    "PMID": 30377267.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Fluorescence microscopy, Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Pretreatment with the peptope induced 11-1F4 mAb accumulation in serum amyloid A deposits in vivo and enhanced 11-1F4–mediated dissolution of a human AL amyloid extract implanted in mice.\", \"Finally, we demonstrate enhancement of 11-1F4 mAb-mediated clearance of implanted human AL amyloid extract in a model of localized AL amyloid in the presence of peptope.\", \"Female NU/NU mice (∼8 wk of age) were injected subcutaneously on day 0 with 2 mg of human AL λ2BAL amyloid labeled covalently with Dylight800 (DL) NIR fluorophore and with (n = 5) or without (n = 4) preincubation in 200 µg of p66. Fluorescence emission from the subcutaneous amyloidoma was readily visualized on the flank of the mice by optical imaging (Fig. 4A). The rate at which the fluorescence emission, associated with the human amyloid extract, decreased was significantly enhanced in mice administered p66-pretreated material in response to m11-1F4 therapy, compared with m11-1F4 treatment alone (Fig. 4B).\", \"Figure 4\", \"(B) Pretreatment with p66 enhanced the therapeutic activity of 11-1F4.\", \"Figure 5\", \"The DL fluorescence intensity correlated positively with amyloid load, based on ThT fluorescence in the untreated and p66-treated samples (Fig. 5 B and C) and as a single population (Fig. 5D). No significant difference in the DL:ThT fluorescence ratio in the treated and untreated populations was observed (Fig. 5E), indicating that the reduction in DL fluorescence emission measured in vivo is associated with amyloid dissolution.\", \"Using this system, we were able to generate data amenable to a mixed-effect analysis, which demonstrated that 11-1F4 treatment of p66-coated λ2BAL amyloid extract was significantly more effective than 11-1F4 treatment alone, as evidenced by a more rapid decrease in amyloid-associated fluorescence in the lesion (Fig. 4).\",",
    "Curator Statement": "The antibody is pre-bound with an amyloid-binding peptide p5+14: 6(–KxxxKxx–), where x is Ala or Gln."
  },
  "AMGAB0550": {
    "Interaction ID": "AMGAB0550",
    "Antibody ID": "ABID0272",
    "Antibody name": "VDW (first generation)",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Tau",
    "DOI": "10.1073/pnas.2300258120",
    "PMID": 37801475.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Cell-based quantitative fluorescence tau seeding inhibition assay",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "CDR3: SVWIWYEPVDWSE",
    "Quote of the interaction": "\"Figure 1\", \"The VDW and W3 nanobodies failed to block tau seeding by brain extracts from AD1, but inhibited tau seeding by brain extracts from AD2, suggesting lower potency of the VDW and W3 nanobody designs.\", \"Our evidence suggests that inhibition exhibited by WIW is caused by the designed insert and not the scaffold. If the scaffold had been responsible for the inhibition exhibited by nanobody WIW (Fig. 1G), then VDW and W3 would have exhibited the same level of inhibition as WIW since all three share the same scaffold.\", \"Seeding by tau-K18 oligomers was reduced by all nanobody designs.\", \"Supplementary Figure S1\", \"The nanobodies grafted with capping inhibitors blocked tau aggregation in biosensor cells seeded with postmortem brain extracts from AD and progressive supranuclear palsy (PSP) patients. The tau capping nanobody inhibitors also blocked seeding by recombinant tau oligomers.\", \"We designed two generations of synthetic camel antibodies that halt prion-like seeding.\" , \"Designed Nanobodies Block Seeding by tau Fibrils and Oligomers in HEK293 Biosensor Cells.\",",
    "Curator Statement": false
  },
  "AMGAB0551": {
    "Interaction ID": "AMGAB0551",
    "Antibody ID": "ABID0273",
    "Antibody name": "W3 (first generation)",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Tau",
    "DOI": "10.1073/pnas.2300258120",
    "PMID": 37801475.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Cell-based quantitative fluorescence tau seeding inhibition assay",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "CDR3: DVWIINKKLK",
    "Quote of the interaction": "\"Figure 1\", \"The VDW and W3 nanobodies failed to block tau seeding by brain extracts from AD1, but inhibited tau seeding by brain extracts from AD2, suggesting lower potency of the VDW and W3 nanobody designs.\", \"Our evidence suggests that inhibition exhibited by WIW is caused by the designed insert and not the scaffold. If the scaffold had been responsible for the inhibition exhibited by nanobody WIW (Fig. 1G), then VDW and W3 would have exhibited the same level of inhibition as WIW since all three share the same scaffold.\", \"Seeding by tau-K18 oligomers was reduced by all nanobody designs.\", \"Supplementary Figure S1\", \"The nanobodies grafted with capping inhibitors blocked tau aggregation in biosensor cells seeded with postmortem brain extracts from AD and progressive supranuclear palsy (PSP) patients. The tau capping nanobody inhibitors also blocked seeding by recombinant tau oligomers.\", \"We designed two generations of synthetic camel antibodies that halt prion-like seeding.\" , \"Designed Nanobodies Block Seeding by tau Fibrils and Oligomers in HEK293 Biosensor Cells.\",",
    "Curator Statement": false
  },
  "AMGAB0552": {
    "Interaction ID": "AMGAB0552",
    "Antibody ID": "ABID0274",
    "Antibody name": "WIW (first generation)",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Tau",
    "DOI": "10.1073/pnas.2300258120",
    "PMID": 37801475.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Cell-based quantitative fluorescence tau seeding inhibition assay",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "CDR3: SVWIWYE",
    "Quote of the interaction": "\"Figure 1\", \"As shown in Fig. 1 G–I, seeding by brain tissue extracts from donor 1 (AD1) and donor 2 (AD2) was inhibited by the WIW capping nanobody inhibitor (P < 0.0005).\", \"Our evidence suggests that inhibition exhibited by WIW is caused by the designed insert and not the scaffold. If the scaffold had been responsible for the inhibition exhibited by nanobody WIW (Fig. 1G), then VDW and W3 would have exhibited the same level of inhibition as WIW since all three share the same scaffold.\", \"Seeding by tau-K18 oligomers was reduced by all nanobody designs. Notably, the WIW nanobody inhibited aggregation seeded by both PHFs and oligomers (SI Appendix, Fig. S1 G and H).\", \"Supplementary Figure S1\", \"The nanobodies grafted with capping inhibitors blocked tau aggregation in biosensor cells seeded with postmortem brain extracts from AD and progressive supranuclear palsy (PSP) patients. The tau capping nanobody inhibitors also blocked seeding by recombinant tau oligomers.\", \"We designed two generations of synthetic camel antibodies that halt prion-like seeding.\" , \"Designed Nanobodies Block Seeding by tau Fibrils and Oligomers in HEK293 Biosensor Cells.\",",
    "Curator Statement": false
  },
  "AMGAB0553": {
    "Interaction ID": "AMGAB0553",
    "Antibody ID": "ABID0275",
    "Antibody name": "SV (second generation)",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Tau",
    "DOI": "10.1073/pnas.2300258120",
    "PMID": 37801475.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Cell-based quantitative fluorescence tau seeding inhibition assay",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "SVQIVYK",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Supplementary Figure S3\", \"We found that treating the AD brain extracts with the WIW or SV second-generation nanobody strongly reduced the seeding by all four AD samples (SI Appendix, Fig. S2 C–J).\", \"Figure 2\", \"All synthetic nanobodies strongly reduced seeding by AD3, AD4, and AD5 patient brain samples (Fig. 2 C–E and SI Appendix, Fig. S3 C–E).\", \"Supplementary Figure S4\",  \"In addition, all synthetic nanobodies strongly reduced seeding by AD6, AD7, AD8, AD9, and AD10 patient brain samples (SI Appendix, Fig. S4).\", \"SV and M4 nanobodies were more effective inhibitors of AD7 and AD8 than WIW (Fig. 2 C–E and SI Appendix, Fig. S4).\", \"We observed that seeded aggregation by tau-K18 oligomers was strongly inhibited in the presence of the second-generation WIW and SV nanobodies in tau biosensor cells (SI Appendix, Fig. S2 K and L).\", \"Figure 3\", \"As shown in Fig. 4 B and C, the designed nanobody inhibitors block seeding by purified tau fibrils, while the noncognate nanobody shows no effect on seeding inhibition. Our nanobody designs successfully inhibit seeding of both crude brain extract and purified tau fibrils from AD patients, revealing the potential relevance of our nanobody-based designs to AD.\", \"Figure 4\", \"Supplementary Figure S5\", \"We tested the inhibitory power of our synthetic nanobodies on crude brain extracts from two donors with PSP. Electron micrographs of brain extract from PSP donor 1 confirmed that the extract contained fibrils with a twisted filament morphology (SI Appendix, Fig. S5 A and B). As shown in SI Appendix, Fig. S5 C–E, all synthetic nanobodies blocked seeding by both PSP brain extracts. The noncognate nanobody showed no effect on seeding by either PSP extract.\", \"The second-generation nanobody inhibitors decrease seeding by AD patient brain extracts in biosensor cells (Fig. 2 and SI Appendix, Figs. S2–S4). In addition, the second-generation nanobody inhibitors decrease seeding by purified tau fibrils from AD and PSP patients (Fig. 4 and SI Appendix, Fig. S5), demonstrating that aggregation-prone interfaces of both AD and PSP tau are accessible and targeted by our designed nanobody inhibitors.\", \"The WIW and SV designed nanobodies potently inhibit seeding by tau oligomers (Fig. 3 and SI Appendix, Fig. S2).\", \"The nanobodies grafted with capping inhibitors blocked tau aggregation in biosensor cells seeded with postmortem brain extracts from AD and progressive supranuclear palsy (PSP) patients. The tau capping nanobody inhibitors also blocked seeding by recombinant tau oligomers.\", \"We designed two generations of synthetic camel antibodies that halt prion-like seeding.\" , \"Designed Nanobodies Block Seeding by tau Fibrils and Oligomers in HEK293 Biosensor Cells.\",",
    "Curator Statement": false
  },
  "AMGAB0554": {
    "Interaction ID": "AMGAB0554",
    "Antibody ID": "ABID0276",
    "Antibody name": "M4 (second generation)",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Tau",
    "DOI": "10.1073/pnas.2300258120",
    "PMID": 37801475.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Cell-based quantitative fluorescence tau seeding inhibition assay",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "CDR3: DVQMINKKLK",
    "Quote of the interaction": "\"Supplementary Figure S3\", \"Figure 2\", \"All synthetic nanobodies strongly reduced seeding by AD3, AD4, and AD5 patient brain samples (Fig. 2 C–E and SI Appendix, Fig. S3 C–E).\", \"Supplementary Figure S4\",  \"In addition, all synthetic nanobodies strongly reduced seeding by AD6, AD7, AD8, AD9, and AD10 patient brain samples (SI Appendix, Fig. S4).\", \"SV and M4 nanobodies were more effective inhibitors of AD7 and AD8 than WIW (Fig. 2 C–E and SI Appendix, Fig. S4).\", \"Figure 3\", \"As shown in Fig. 4 B and C, the designed nanobody inhibitors block seeding by purified tau fibrils, while the noncognate nanobody shows no effect on seeding inhibition. Our nanobody designs successfully inhibit seeding of both crude brain extract and purified tau fibrils from AD patients, revealing the potential relevance of our nanobody-based designs to AD.\", \"Figure 4\", \"Supplementary Figure S5\", \"We tested the inhibitory power of our synthetic nanobodies on crude brain extracts from two donors with PSP. Electron micrographs of brain extract from PSP donor 1 confirmed that the extract contained fibrils with a twisted filament morphology (SI Appendix, Fig. S5 A and B). As shown in SI Appendix, Fig. S5 C–E, all synthetic nanobodies blocked seeding by both PSP brain extracts. The noncognate nanobody showed no effect on seeding by either PSP extract.\", \"The second-generation nanobody inhibitors decrease seeding by AD patient brain extracts in biosensor cells (Fig. 2 and SI Appendix, Figs. S2–S4). In addition, the second-generation nanobody inhibitors decrease seeding by purified tau fibrils from AD and PSP patients (Fig. 4 and SI Appendix, Fig. S5), demonstrating that aggregation-prone interfaces of both AD and PSP tau are accessible and targeted by our designed nanobody inhibitors.\", \"The nanobodies grafted with capping inhibitors blocked tau aggregation in biosensor cells seeded with postmortem brain extracts from AD and progressive supranuclear palsy (PSP) patients. The tau capping nanobody inhibitors also blocked seeding by recombinant tau oligomers.\", \"We designed two generations of synthetic camel antibodies that halt prion-like seeding.\" , \"Designed Nanobodies Block Seeding by tau Fibrils and Oligomers in HEK293 Biosensor Cells.\",",
    "Curator Statement": false
  },
  "AMGAB0555": {
    "Interaction ID": "AMGAB0555",
    "Antibody ID": "ABID0277",
    "Antibody name": "R9 (second generation)",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Tau",
    "DOI": "10.1073/pnas.2300258120",
    "PMID": 37801475.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Cell-based quantitative fluorescence tau seeding inhibition assay",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "CDR3: DVQIINKKRK",
    "Quote of the interaction": "\"Supplementary Figure S3\", \"Figure 2\", \"All synthetic nanobodies strongly reduced seeding by AD3, AD4, and AD5 patient brain samples (Fig. 2 C–E and SI Appendix, Fig. S3 C–E).\", \"Supplementary Figure S4\",  \"In addition, all synthetic nanobodies strongly reduced seeding by AD6, AD7, AD8, AD9, and AD10 patient brain samples (SI Appendix, Fig. S4).\", \"Figure 3\", \"As shown in Fig. 4 B and C, the designed nanobody inhibitors block seeding by purified tau fibrils, while the noncognate nanobody shows no effect on seeding inhibition. Our nanobody designs successfully inhibit seeding of both crude brain extract and purified tau fibrils from AD patients, revealing the potential relevance of our nanobody-based designs to AD.\", \"Figure 4\", \"Supplementary Figure S5\", \"We tested the inhibitory power of our synthetic nanobodies on crude brain extracts from two donors with PSP. Electron micrographs of brain extract from PSP donor 1 confirmed that the extract contained fibrils with a twisted filament morphology (SI Appendix, Fig. S5 A and B). As shown in SI Appendix, Fig. S5 C–E, all synthetic nanobodies blocked seeding by both PSP brain extracts. The noncognate nanobody showed no effect on seeding by either PSP extract.\", \"The second-generation nanobody inhibitors decrease seeding by AD patient brain extracts in biosensor cells (Fig. 2 and SI Appendix, Figs. S2–S4). In addition, the second-generation nanobody inhibitors decrease seeding by purified tau fibrils from AD and PSP patients (Fig. 4 and SI Appendix, Fig. S5), demonstrating that aggregation-prone interfaces of both AD and PSP tau are accessible and targeted by our designed nanobody inhibitors.\", \"The nanobodies grafted with capping inhibitors blocked tau aggregation in biosensor cells seeded with postmortem brain extracts from AD and progressive supranuclear palsy (PSP) patients. The tau capping nanobody inhibitors also blocked seeding by recombinant tau oligomers.\", \"We designed two generations of synthetic camel antibodies that halt prion-like seeding.\" , \"Designed Nanobodies Block Seeding by tau Fibrils and Oligomers in HEK293 Biosensor Cells.\",",
    "Curator Statement": false
  },
  "AMGAB0556": {
    "Interaction ID": "AMGAB0556",
    "Antibody ID": "ABID0278",
    "Antibody name": "QIINK (second generation)",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Tau",
    "DOI": "10.1073/pnas.2300258120",
    "PMID": 37801475.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Cell-based quantitative fluorescence tau seeding inhibition assay",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "CDR3: KVQIINKKLD",
    "Quote of the interaction": "\"Supplementary Figure S3\", \"Figure 2\", \"All synthetic nanobodies strongly reduced seeding by AD3, AD4, and AD5 patient brain samples (Fig. 2 C–E and SI Appendix, Fig. S3 C–E).\", \"Supplementary Figure S4\",  \"In addition, all synthetic nanobodies strongly reduced seeding by AD6, AD7, AD8, AD9, and AD10 patient brain samples (SI Appendix, Fig. S4).\", \"Figure 3\", \"As shown in Fig. 4 B and C, the designed nanobody inhibitors block seeding by purified tau fibrils, while the noncognate nanobody shows no effect on seeding inhibition. Our nanobody designs successfully inhibit seeding of both crude brain extract and purified tau fibrils from AD patients, revealing the potential relevance of our nanobody-based designs to AD.\", \"Figure 4\", \"Supplementary Figure S5\", \"We tested the inhibitory power of our synthetic nanobodies on crude brain extracts from two donors with PSP. Electron micrographs of brain extract from PSP donor 1 confirmed that the extract contained fibrils with a twisted filament morphology (SI Appendix, Fig. S5 A and B). As shown in SI Appendix, Fig. S5 C–E, all synthetic nanobodies blocked seeding by both PSP brain extracts. The noncognate nanobody showed no effect on seeding by either PSP extract.\", \"The second-generation nanobody inhibitors decrease seeding by AD patient brain extracts in biosensor cells (Fig. 2 and SI Appendix, Figs. S2–S4). In addition, the second-generation nanobody inhibitors decrease seeding by purified tau fibrils from AD and PSP patients (Fig. 4 and SI Appendix, Fig. S5), demonstrating that aggregation-prone interfaces of both AD and PSP tau are accessible and targeted by our designed nanobody inhibitors.\", \"The nanobodies grafted with capping inhibitors blocked tau aggregation in biosensor cells seeded with postmortem brain extracts from AD and progressive supranuclear palsy (PSP) patients. The tau capping nanobody inhibitors also blocked seeding by recombinant tau oligomers.\", \"We designed two generations of synthetic camel antibodies that halt prion-like seeding.\" , \"Designed Nanobodies Block Seeding by tau Fibrils and Oligomers in HEK293 Biosensor Cells.\",",
    "Curator Statement": false
  },
  "AMGAB0557": {
    "Interaction ID": "AMGAB0557",
    "Antibody ID": "ABID0279",
    "Antibody name": "W3 (second generation)",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Tau",
    "DOI": "10.1073/pnas.2300258120",
    "PMID": 37801475.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Cell-based quantitative fluorescence tau seeding inhibition assay",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "CDR3: DVWIINKKLK",
    "Quote of the interaction": "\"Supplementary Figure S3\", \"Figure 2\", \"All synthetic nanobodies strongly reduced seeding by AD3, AD4, and AD5 patient brain samples (Fig. 2 C–E and SI Appendix, Fig. S3 C–E).\", \"Supplementary Figure S4\",  \"In addition, all synthetic nanobodies strongly reduced seeding by AD6, AD7, AD8, AD9, and AD10 patient brain samples (SI Appendix, Fig. S4).\", \"Figure 3\", \"As shown in Fig. 4 B and C, the designed nanobody inhibitors block seeding by purified tau fibrils, while the noncognate nanobody shows no effect on seeding inhibition. Our nanobody designs successfully inhibit seeding of both crude brain extract and purified tau fibrils from AD patients, revealing the potential relevance of our nanobody-based designs to AD.\", \"Figure 4\",  \"Supplementary Figure S5\", \"We tested the inhibitory power of our synthetic nanobodies on crude brain extracts from two donors with PSP. Electron micrographs of brain extract from PSP donor 1 confirmed that the extract contained fibrils with a twisted filament morphology (SI Appendix, Fig. S5 A and B). As shown in SI Appendix, Fig. S5 C–E, all synthetic nanobodies blocked seeding by both PSP brain extracts. The noncognate nanobody showed no effect on seeding by either PSP extract.\", \"The second-generation nanobody inhibitors decrease seeding by AD patient brain extracts in biosensor cells (Fig. 2 and SI Appendix, Figs. S2–S4). In addition, the second-generation nanobody inhibitors decrease seeding by purified tau fibrils from AD and PSP patients (Fig. 4 and SI Appendix, Fig. S5), demonstrating that aggregation-prone interfaces of both AD and PSP tau are accessible and targeted by our designed nanobody inhibitors.\", \"The nanobodies grafted with capping inhibitors blocked tau aggregation in biosensor cells seeded with postmortem brain extracts from AD and progressive supranuclear palsy (PSP) patients. The tau capping nanobody inhibitors also blocked seeding by recombinant tau oligomers.\", \"We designed two generations of synthetic camel antibodies that halt prion-like seeding.\" , \"Designed Nanobodies Block Seeding by tau Fibrils and Oligomers in HEK293 Biosensor Cells.\",",
    "Curator Statement": false
  },
  "AMGAB0558": {
    "Interaction ID": "AMGAB0558",
    "Antibody ID": "ABID0280",
    "Antibody name": "WIW (second generation)",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Tau",
    "DOI": "10.1073/pnas.2300258120",
    "PMID": 37801475.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Cell-based quantitative fluorescence tau seeding inhibition assay",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "CDR3: SVWIWYE",
    "Quote of the interaction": "\"Supplementary Figure S2\", \"Supplementary Figure S3\", \"We found that treating the AD brain extracts with the WIW or SV second-generation nanobody strongly reduced the seeding by all four AD samples (SI Appendix, Fig. S2 C–J).\", \"(F) Representative second-generation nanobody WIW inhibits seeding by brain extract AD3 at doses ranging from 1 to 10 μM.\", \"Figure 2\", \"All synthetic nanobodies strongly reduced seeding by AD3, AD4, and AD5 patient brain samples (Fig. 2 C–E and SI Appendix, Fig. S3 C–E).\", \"Supplementary Figure S4\",  \"In addition, all synthetic nanobodies strongly reduced seeding by AD6, AD7, AD8, AD9, and AD10 patient brain samples (SI Appendix, Fig. S4).\", \"WIW was the most potent inhibitor of seeding by AD3, AD4, and AD5 brain extracts but was less effective on AD7 and AD8 brain extracts (Fig. 2 C–E and SI Appendix, Fig. S4).\", \"WIW inhibits seeding by AD3 brain extract in a dose-dependent manner from 1 to 5 µM, and at 10 µM, there is a plateau in WIW’s inhibitory effect (Fig. 2F).\", \"We observed that seeded aggregation by tau-K18 oligomers was strongly inhibited in the presence of the second-generation WIW and SV nanobodies in tau biosensor cells (SI Appendix, Fig. S2 K and L).\", \"Figure 3\", \"(D) Representative second-generation nanobody WIW inhibits seeding by tau K18 oligomers at doses ranging from 1 to 10 μM.\", \" WIW inhibits seeding by oligomers in a dose-dependent manner from 1 to 10 µM (Fig. 3 D and E). We again used a noncognate nanobody to serve as a negative control. We observed nonspecific inhibition by the noncognate nanobody, but the inhibition from WIW at the same concentration was significantly greater than that of the noncognate (P < 0.0001).\", \"As shown in Fig. 4 B and C, the designed nanobody inhibitors block seeding by purified tau fibrils, while the noncognate nanobody shows no effect on seeding inhibition. Our nanobody designs successfully inhibit seeding of both crude brain extract and purified tau fibrils from AD patients, revealing the potential relevance of our nanobody-based designs to AD.\", \"Figure 4\", \"Supplementary Figure S5\", \"We tested the inhibitory power of our synthetic nanobodies on crude brain extracts from two donors with PSP. Electron micrographs of brain extract from PSP donor 1 confirmed that the extract contained fibrils with a twisted filament morphology (SI Appendix, Fig. S5 A and B). As shown in SI Appendix, Fig. S5 C–E, all synthetic nanobodies blocked seeding by both PSP brain extracts. The noncognate nanobody showed no effect on seeding by either PSP extract.\", \"The second-generation nanobody inhibitors decrease seeding by AD patient brain extracts in biosensor cells (Fig. 2 and SI Appendix, Figs. S2–S4). In addition, the second-generation nanobody inhibitors decrease seeding by purified tau fibrils from AD and PSP patients (Fig. 4 and SI Appendix, Fig. S5), demonstrating that aggregation-prone interfaces of both AD and PSP tau are accessible and targeted by our designed nanobody inhibitors.\", \"The WIW and SV designed nanobodies potently inhibit seeding by tau oligomers (Fig. 3 and SI Appendix, Fig. S2).\",  \"The nanobodies grafted with capping inhibitors blocked tau aggregation in biosensor cells seeded with postmortem brain extracts from AD and progressive supranuclear palsy (PSP) patients. The tau capping nanobody inhibitors also blocked seeding by recombinant tau oligomers.\", \"We designed two generations of synthetic camel antibodies that halt prion-like seeding.\" , \"Designed Nanobodies Block Seeding by tau Fibrils and Oligomers in HEK293 Biosensor Cells.\",",
    "Curator Statement": false
  },
  "AMGAB0559": {
    "Interaction ID": "AMGAB0559",
    "Antibody ID": "ABID0281",
    "Antibody name": "Nb484",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Tau",
    "DOI": "10.1073/pnas.2300258120",
    "PMID": 37801475.0,
    "Impact of the antibody on amyloid formation": "No effect, Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Cell-based quantitative fluorescence tau seeding inhibition assay",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Supplementary Figure S3\", \"Figure 2\", \"We observed some nonspecific inhibition by the noncognate nanobody toward AD3, but the inhibition from all designed nanobodies was significantly greater (P < 0.0001) than that of the noncognate.\", \"Supplementary Figure S4\", \"The noncognate nanobody showed no effect on seeding by AD6, AD7, AD9, and AD10. We observed nonspecific inhibition by the noncognate nanobody toward AD8.\", \"We again used a noncognate nanobody to serve as a negative control which showed no effect on seeding.\", \"Figure 3\", \" WIW inhibits seeding by oligomers in a dose-dependent manner from 1 to 10 µM (Fig. 3 D and E). We again used a noncognate nanobody to serve as a negative control. We observed nonspecific inhibition by the noncognate nanobody, but the inhibition from WIW at the same concentration was significantly greater than that of the noncognate (P < 0.0001).\", \"As shown in Fig. 4 B and C, the designed nanobody inhibitors block seeding by purified tau fibrils, while the noncognate nanobody shows no effect on seeding inhibition. Our nanobody designs successfully inhibit seeding of both crude brain extract and purified tau fibrils from AD patients, revealing the potential relevance of our nanobody-based designs to AD.\", \"Figure 4\", \"Supplementary Figure S5\", \"We tested the inhibitory power of our synthetic nanobodies on crude brain extracts from two donors with PSP. Electron micrographs of brain extract from PSP donor 1 confirmed that the extract contained fibrils with a twisted filament morphology (SI Appendix, Fig. S5 A and B). As shown in SI Appendix, Fig. S5 C–E, all synthetic nanobodies blocked seeding by both PSP brain extracts. The noncognate nanobody showed no effect on seeding by either PSP extract.\", \"In cases of patient AD3, AD8, and the recombinant K18 oligomers (Fig. 2, Fig. 3, and SI Appendix, Figs. S4 and S3), we observed some nonspecific inhibition by the noncognate nanobody. It is possible that the nonspecific inhibition comes from some nonspecific binding of tau from the nanobody scaffold. Based on the results of the unbiased docking experiment (SI Appendix, Fig. S1 D and E), we are aware of a few possible configurations of nonspecific binding. However, based on the finding that sequestering monomeric tau with an anti-tau antibody is not sufficient for inhibition (Fig. 2F), only nonspecific binding in aggregation-prone regions such as the fibril core or VQIINK could contribute to the nonspecific inhibition in biosensor cells. In future generations of nanobody design, we will select a scaffold with less nonspecific binding and nonspecific inhibition.\",",
    "Curator Statement": "Results show a significative non-specific inhibition."
  },
  "AMGAB0560": {
    "Interaction ID": "AMGAB0560",
    "Antibody ID": "ABID0282",
    "Antibody name": "43D",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Tau",
    "DOI": "10.1073/pnas.2300258120",
    "PMID": 37801475.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Other: Cell-based quantitative fluorescence tau seeding inhibition assay",
    "Amyloid species identified": "Monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In addition, we wanted to ensure that our capping nanobody does not simply bind and sequester tau monomer instead of blocking fibril growth. We included a monoclonal antibody that binds residues 6 to 18 of tau, called 43D, and found that it does not reduce seeding by AD3 brain extract. Because 43D can bind tau monomer with high affinity but still does not reduce seeding, we can assume that sequestering tau monomer is not sufficient for nanobody function.\",",
    "Curator Statement": false
  },
  "AMGAB0561": {
    "Interaction ID": "AMGAB0561",
    "Antibody ID": "ABID0524",
    "Antibody name": "HC F1",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1074/jbc.M109.044321",
    "PMID": 19889627.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "CDR3: AREKTMVRGAISGYSDY",
    "Quote of the interaction": "\"This fusion resulted in the cloning of a novel free human Ig heavy chain (HC), F1, which cross-reacted with amyloid fibrils and Aβ oligomers without binding to the native precursor proteins, inhibited Aβ fibril growth, and reduced soluble Aβ-induced impairment of a cellular mechanism of rodent memory and learning, hippocampal long term potentiation (LTP). Moreover, we have demonstrated that anti-amyloidogenic activity is a general property of free human Ig γ HCs.\", \"In a more stringent test of anti-amyloidogenic activity, F1 was the only protein that inhibited Aβ fibril elongation, albeit without inducing the formation of alternative Abeta assembly species, with a molar protein concentration that obtained half-maximum inhibition (IC50) of ∼1.0 μm (Fig. 7A). This indicated that the anti-amyloidogenic activity of a HC was partly dependent on its primary sequence.\",",
    "Curator Statement": false
  },
  "AMGAB0562": {
    "Interaction ID": "AMGAB0562",
    "Antibody ID": "ABID0525",
    "Antibody name": "13A",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1074/jbc.M109.044321",
    "PMID": 19889627.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Fig. 6 shows that subequimolar concentrations of HCs, F1, and 13A inhibited de novo Aβ fibril formation. However, the inhibitory potency of HC is not unique because similar inhibition was observed for the intact 13A antibody, BSA, and several other human mAbs that have no appreciable binding to Aβ (Fig. 6).\", \"Figure 6\",",
    "Curator Statement": false
  },
  "AMGAB0563": {
    "Interaction ID": "AMGAB0563",
    "Antibody ID": "ABID0525",
    "Antibody name": "13A",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1074/jbc.M109.044321",
    "PMID": 19889627.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" Electron micrographs of the reaction products indicated that HC F1 but not IgG 13A enhanced the formation of less ordered fibrillar-like Aβ aggregates (Fig. 6, C–E).\", \"Figure 6\", \"In a more stringent test of anti-amyloidogenic activity, F1 was the only protein that inhibited Aβ fibril elongation, albeit without inducing the formation of alternative Abeta assembly species, with a molar protein concentration that obtained half-maximum inhibition (IC50) of ∼1.0 μm (Fig. 7A). This indicated that the anti-amyloidogenic activity of a HC was partly dependent on its primary sequence.\",",
    "Curator Statement": false
  },
  "AMGAB0564": {
    "Interaction ID": "AMGAB0564",
    "Antibody ID": "ABID0334",
    "Antibody name": "9D5",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1074/jbc.M110.178707",
    "PMID": 20971852.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, Immunohistochemistry, ELISA,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" Using a novel sandwich ELISA significantly decreased levels of oligomers in plasma samples from patients with AD compared with healthy controls were identified. Moreover, passive immunization of 5XFAD mice with 9D5 significantly reduced overall Aβ plaque load and AβpE3 levels, and normalized behavioral deficits. These data indicate that 9D5 is a therapeutically and diagnostically effective monoclonal antibody targeting low molecular weight AβpE3 oligomers.\", \"9D5 treatment significantly reduced generic Aβ, Aβ42, Aβ40, and AβpE3 plaque load in hippocampus (HC) and cortex (Ctx) (Fig. 4, A and B).\", \"Figure 4\", \"B, plaque-load quantification showed a significant decrease for both total Aβ (4G8), Aβ40 (G2–10), Aβ42 (G2–11), and pyroglutamate-modified Aβ (2–48) in 9D5-injected mice compared with PBS-injected mice in both hippocampus (HC) and cortex (Ctx).\", \"The therapeutic potential of 9D5 was demonstrated in passively immunized 5XFAD mice as plaque load and Aβ levels were reduced and behavioral deficits were normalized.\",",
    "Curator Statement": false
  },
  "AMGAB0565": {
    "Interaction ID": "AMGAB0565",
    "Antibody ID": "ABID0334",
    "Antibody name": "9D5",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1074/jbc.M110.178707",
    "PMID": 20971852.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, Immunohistochemistry, ELISA,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" Using a novel sandwich ELISA significantly decreased levels of oligomers in plasma samples from patients with AD compared with healthy controls were identified. Moreover, passive immunization of 5XFAD mice with 9D5 significantly reduced overall Aβ plaque load and AβpE3 levels, and normalized behavioral deficits. These data indicate that 9D5 is a therapeutically and diagnostically effective monoclonal antibody targeting low molecular weight AβpE3 oligomers.\", \"9D5 recognized ΑβpΕ3 oligomers and inhibited ΑβpΕ3 aggregation in vitro\", \"Figure 1\", \"Notably, the presence of antibody 9D5 efficiently decreased the formation of higher aggregates of the AβpE3–42 peptide at a 1:76 (9D5:Aβ) ratio, but not the rapid formation of lower oligomers, further demonstrating the specificity of this antibody for lower oligomeric species of AβpE3 and its efficiency in the inhibition of further peptide aggregation (Fig. 1E).\", \"E, accelerated increase after the inflection point at 200 min was efficiently blocked by addition of 9D5 together with AβpE3–42.\", \"Supplementary Figure 5\", \"Reduction of intracellular signal in the subiculum after passive immunisation of 5XFAD mice with 9D5. (A) Reduction of intracellular 9D5 immunoreactivity after passive immunisation with 9D5.\",",
    "Curator Statement": false
  },
  "AMGAB0566": {
    "Interaction ID": "AMGAB0566",
    "Antibody ID": "ABID0024.5",
    "Antibody name": "MC1",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1074/jbc.M111.229633",
    "PMID": 21841002.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA, Western blot",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We show that peripheral administration of two antibodies against pathological Tau forms significantly reduces biochemical Tau pathology in the JNPL3 mouse model. We further demonstrate that peripheral administration of the same antibodies in the more rapidly progressive P301S tauopathy model not only reduces Tau pathology quantitated by biochemical assays and immunohistochemistry, but also significantly delays the onset of motor function decline and weight loss. This is accompanied by a reduction in neurospheroids, providing direct evidence of reduced neurodegeneration. Thus, passive immunotherapy is effective at preventing the buildup of intracellular Tau pathology, neurospheroids, and associated symptoms, although the exact mechanism remains uncertain.\", \"Figure 9\", \"A, AT8 ELISA analysis of the JNPL3 mouse P1 brain fraction shows strong reduction in AT8 signal in both antibody treatment groups compared with control antibody. B, statistical analysis of the log-transformed AT8 ELISA data shows that the reduction is highly significant for both PHF1 and MC1.\", \"Western blot analysis of this fraction using antibody AT8 (which recognizes Tau phosphorylated at Ser-202 and Thr-205 (17)) showed only the 64-kDa Tau band, which exhibited substantial animal-to-animal variability, but overall was reduced in both the PHF1- and MC1-treated groups versus control (Fig. 4A).\", \"Figure 4\", \"Biochemically detectable Tau pathology in JNPL3 mice is reduced after passive immunization with anti-Tau antibodies. A, AT8 Western blot of the P1 brain fraction from 6-month-old JNPL3 mice shows the specificity of the antibody for the 64-kDa band of hyperphosphorylated human Tau that comigrates with PHF Tau from AD brain (15) and correlates with functional deficits in several models of tauopathy (16). The 64-kDa band is weaker in the MC1 and PHF1 treatment groups compared with control antibody.\", \"Using this AT8 ELISA for the insoluble fraction of the brain we found that both antibodies reduced the biochemical pathology by >50% (Fig. 6A), which was highly statistically significant (p = 0.0006 for PHF1 and p = 0.0004 for MC1 by Dunnett's method (Fig. 6B)).\", \"Figure 6\", \"A, AT8 ELISA analysis of the JNPL3 mouse P1 brain fraction shows strong reduction in AT8 signal in both antibody treatment groups compared with control antibody. B, statistical analysis of the log-transformed AT8 ELISA data shows that the reduction is highly significant for both PHF1 and MC1.\",\"Therefore, we analyzed the effects of immunotherapy on both S1 and P1 fractions. ELISA analysis of the P1 fraction (Fig. 9B) revealed relative to control antibody a 45% reduction in biochemical pathology in the PHF1-treated mice, which was highly significant (p = 0.006) and a 33% reduction in the MC1 group, although this was not significant at the p = 0.05 level (p = 0.088).\", \"Applying the same analysis techniques to the spinal cord P1 fraction of the same mice we obtained similar results with reductions for both PHF1 (p = 0.086) and MC1 (p = 0.016) treatment versus control antibody (Fig. 9D). In summary, in the P301S model in all fractions, where it can be detected, biochemical Tau pathology was reduced by Tau immunotherapy, consistent with the results in the JNPL3 model (see above).\", \"Figure 10\",\"Figure 11\", \"Representative images taken from the spinal cord and brain stem (×20) from P301S mice treated with control, MC1, and PHF1 antibodies. The images show a reduction in PG5 staining in the MC1- and PHF1-treated mice compared with control antibody-treated mice.\", \"Quantitative analysis demonstrated reduction in pathology using three different detection antibodies: AT8, which recognizes Tau phosphorylated at Ser-202 and Thr-205 (Fig. 11A, significant reduction for both antibodies in both regions); PG5 (10) (Fig. 11B, significant reduction for both antibodies in both regions), and nY29, which detects Tau nitrated at position 29 (20) (Fig. 11C, strong trend for both antibodies in both regions). The PG5 and nY29 antibodies each recognize epitopes that are largely restricted to neurofibrillary inclusions (tangles and neuropil threads) (10, 20).\", \"A, quantitation of AT8-positive cells in brain stem shows a significant reduction for PHF1 and MC1 treatment compared with control antibody. There was also a significant reduction in of AT8 in the cord for PHF1-treated mice. B, quantitation of PG5 positive cells in brain stem and spinal cord shows a significant reduction for PHF1 and MC1 treatment compared with control antibody. C, quantitation of nY29-positive cells in spinal cord brain stem shows a trend toward reduction for PHF1 and MC1 treatment compared with control antibody.\", \"In summary, we have established that passive immunization with antibodies that selectively recognize pathological forms of Tau reduces the extent of biochemically detectable Tau pathology in two different mouse models and that this translates into a reduction in axonal degeneration, a preservation of motor function, and slowing of disease progression in the P301S model of tauopathy. The therapeutic effects observed in the P301S mice are all the more impressive given the aggressive disease course in this model. We observed strong effects on Tau pathology using both immunohistochemistry with antibodies that selectively recognize neurofibrillary inclusions and through analysis of a biochemical correlate of Tau pathology (64-kDa hyperphosphorylated tau).\", \"Indeed, insoluble Tau extracts from P301S transgenic mice containing the 64-kDa hyperphosphorylated Tau species, which was reduced by passive immunotherapy in this study, were necessary and sufficient to drive the propagation of neurofibrillary pathology in the brains of recipient mice (26).\",",
    "Curator Statement": "Authors refer to the insoluble fraction as P1."
  },
  "AMGAB0567": {
    "Interaction ID": "AMGAB0567",
    "Antibody ID": "ABID0457",
    "Antibody name": "PHF1",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1074/jbc.M111.229633",
    "PMID": 21841002.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA, Western blot",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We show that peripheral administration of two antibodies against pathological Tau forms significantly reduces biochemical Tau pathology in the JNPL3 mouse model. We further demonstrate that peripheral administration of the same antibodies in the more rapidly progressive P301S tauopathy model not only reduces Tau pathology quantitated by biochemical assays and immunohistochemistry, but also significantly delays the onset of motor function decline and weight loss. This is accompanied by a reduction in neurospheroids, providing direct evidence of reduced neurodegeneration. Thus, passive immunotherapy is effective at preventing the buildup of intracellular Tau pathology, neurospheroids, and associated symptoms, although the exact mechanism remains uncertain.\", \"A, AT8 ELISA analysis of the JNPL3 mouse P1 brain fraction shows strong reduction in AT8 signal in both antibody treatment groups compared with control antibody. B, statistical analysis of the log-transformed AT8 ELISA data shows that the reduction is highly significant for both PHF1 and MC1.\", \"Figure 9\", \"Western blot analysis of this fraction using antibody AT8 (which recognizes Tau phosphorylated at Ser-202 and Thr-205 (17)) showed only the 64-kDa Tau band, which exhibited substantial animal-to-animal variability, but overall was reduced in both the PHF1- and MC1-treated groups versus control (Fig. 4A).\", \"Figure 4\", \"Biochemically detectable Tau pathology in JNPL3 mice is reduced after passive immunization with anti-Tau antibodies. A, AT8 Western blot of the P1 brain fraction from 6-month-old JNPL3 mice shows the specificity of the antibody for the 64-kDa band of hyperphosphorylated human Tau that comigrates with PHF Tau from AD brain (15) and correlates with functional deficits in several models of tauopathy (16). The 64-kDa band is weaker in the MC1 and PHF1 treatment groups compared with control antibody.\", \"Using this AT8 ELISA for the insoluble fraction of the brain we found that both antibodies reduced the biochemical pathology by >50% (Fig. 6A), which was highly statistically significant (p = 0.0006 for PHF1 and p = 0.0004 for MC1 by Dunnett's method (Fig. 6B)).\", \"Figure 6\", \"A, AT8 ELISA analysis of the JNPL3 mouse P1 brain fraction shows strong reduction in AT8 signal in both antibody treatment groups compared with control antibody. B, statistical analysis of the log-transformed AT8 ELISA data shows that the reduction is highly significant for both PHF1 and MC1.\", \"Therefore, we analyzed the effects of immunotherapy on both S1 and P1 fractions. ELISA analysis of the P1 fraction (Fig. 9B) revealed relative to control antibody a 45% reduction in biochemical pathology in the PHF1-treated mice, which was highly significant (p = 0.006) and a 33% reduction in the MC1 group, although this was not significant at the p = 0.05 level (p = 0.088).\", \"Applying the same analysis techniques to the spinal cord P1 fraction of the same mice we obtained similar results with reductions for both PHF1 (p = 0.086) and MC1 (p = 0.016) treatment versus control antibody (Fig. 9D). In summary, in the P301S model in all fractions, where it can be detected, biochemical Tau pathology was reduced by Tau immunotherapy, consistent with the results in the JNPL3 model (see above).\", \"Figure 10\",\"Figure 11\", \"Representative images taken from the spinal cord and brain stem (×20) from P301S mice treated with control, MC1, and PHF1 antibodies. The images show a reduction in PG5 staining in the MC1- and PHF1-treated mice compared with control antibody-treated mice.\", \"Quantitative analysis demonstrated reduction in pathology using three different detection antibodies: AT8, which recognizes Tau phosphorylated at Ser-202 and Thr-205 (Fig. 11A, significant reduction for both antibodies in both regions); PG5 (10) (Fig. 11B, significant reduction for both antibodies in both regions), and nY29, which detects Tau nitrated at position 29 (20) (Fig. 11C, strong trend for both antibodies in both regions). The PG5 and nY29 antibodies each recognize epitopes that are largely restricted to neurofibrillary inclusions (tangles and neuropil threads) (10, 20).\", \"A, quantitation of AT8-positive cells in brain stem shows a significant reduction for PHF1 and MC1 treatment compared with control antibody. There was also a significant reduction in of AT8 in the cord for PHF1-treated mice. B, quantitation of PG5 positive cells in brain stem and spinal cord shows a significant reduction for PHF1 and MC1 treatment compared with control antibody. C, quantitation of nY29-positive cells in spinal cord brain stem shows a trend toward reduction for PHF1 and MC1 treatment compared with control antibody.\", \"In summary, we have established that passive immunization with antibodies that selectively recognize pathological forms of Tau reduces the extent of biochemically detectable Tau pathology in two different mouse models and that this translates into a reduction in axonal degeneration, a preservation of motor function, and slowing of disease progression in the P301S model of tauopathy. The therapeutic effects observed in the P301S mice are all the more impressive given the aggressive disease course in this model. We observed strong effects on Tau pathology using both immunohistochemistry with antibodies that selectively recognize neurofibrillary inclusions and through analysis of a biochemical correlate of Tau pathology (64-kDa hyperphosphorylated tau).\", \"Indeed, insoluble Tau extracts from P301S transgenic mice containing the 64-kDa hyperphosphorylated Tau species, which was reduced by passive immunotherapy in this study, were necessary and sufficient to drive the propagation of neurofibrillary pathology in the brains of recipient mice (26).\",",
    "Curator Statement": "Authors refer to the insoluble fraction as P1."
  },
  "AMGAB0568": {
    "Interaction ID": "AMGAB0568",
    "Antibody ID": "ABID0563",
    "Antibody name": "mIgM 1802",
    "Amyloid ID": "AGAMYID0010",
    "Amyloid name": "Transthyretin",
    "DOI": "10.1074/jbc.M114.557231",
    "PMID": 24648510.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Hydrolytic enzymatic assay, Turbidimetry, ThT - Total aggregation (final point),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Excess misTTR was dissolved by a hydrolytic mIgM.\", \"Figure 4\", \"E, time-dependent misTTR hydrolysis. mIgM 1802 treatment (120 μg/ml) depleted the 1-mer band derived from misTTR but not the 4-mer phyTTR band visualized by electrophoresis (assay conditions as in A).\", \"Like the pIgMs, the 12 misTTR-hydrolyzing mIgMs hydrolyzed misTTR but not phyTTR, shown by (a) the depleted 1-mer band of preaggregated 125I-TTR but not non-aggregated 125I-TTR in boiled reaction mixtures and (b) the depleted 1-mer TTR band originating from misTTR and the undepleted 4-mer phyTTR band in non-boiled reaction mixtures of pre-aggregated 125I-TTR (Fig. 4, D and E, shows the example of mIgM 1802). Moreover, the mIgMs generated the same 13-, 10-, and 7-kDa TTR product fragments observed for pIgMs (Fig. 4C, inset). The consistent selectivity and product fragment profiles suggest a shared structural basis for mIgM and pIgM catalysis.\", \"Treatment of a 10-fold molar excess of preaggregated TTR with the hydrolytic mIgM 1802 but not non-hydrolytic IgM 1819 resulted in time-dependent reduction of turbidity to the nearly basal value of non-aggregated TTR (Fig. 7A). \", \"Figure 7\", \"mIgM 1802 treatment reduced the ThT fluorescence value to the basal value observed for non-aggregated TTR treated with diluent.\", \"mIgM 1802 treatment reduced the ThT fluorescence value to the basal value observed for non-aggregated TTR treated with diluent.\",",
    "Curator Statement": false
  },
  "AMGAB0569": {
    "Interaction ID": "AMGAB0569",
    "Antibody ID": "ABID0564",
    "Antibody name": "mIgM 1819",
    "Amyloid ID": "AGAMYID0010",
    "Amyloid name": "Transthyretin",
    "DOI": "10.1074/jbc.M114.557231",
    "PMID": 24648510.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Hydrolytic enzymatic assay, Turbidimetry, ThT - Total aggregation (final point),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Excess misTTR was dissolved by a hydrolytic mIgM.\", \"Figure 4\", \"E, time-dependent misTTR hydrolysis. mIgM 1802 treatment (120 μg/ml) depleted the 1-mer band derived from misTTR but not the 4-mer phyTTR band visualized by electrophoresis (assay conditions as in A).\", \"Like the pIgMs, the 12 misTTR-hydrolyzing mIgMs hydrolyzed misTTR but not phyTTR, shown by (a) the depleted 1-mer band of preaggregated 125I-TTR but not non-aggregated 125I-TTR in boiled reaction mixtures and (b) the depleted 1-mer TTR band originating from misTTR and the undepleted 4-mer phyTTR band in non-boiled reaction mixtures of pre-aggregated 125I-TTR (Fig. 4, D and E, shows the example of mIgM 1802). Moreover, the mIgMs generated the same 13-, 10-, and 7-kDa TTR product fragments observed for pIgMs (Fig. 4C, inset). The consistent selectivity and product fragment profiles suggest a shared structural basis for mIgM and pIgM catalysis.\", \"Treatment of a 10-fold molar excess of preaggregated TTR with the hydrolytic mIgM 1802 but not non-hydrolytic IgM 1819 resulted in time-dependent reduction of turbidity to the nearly basal value of non-aggregated TTR (Fig. 7A). \", \"Figure 7\",",
    "Curator Statement": false
  },
  "AMGAB0570": {
    "Interaction ID": "AMGAB0570",
    "Antibody ID": "ABID0427",
    "Antibody name": "2E4",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1074/jbc.M115.641738",
    "PMID": 25724648.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\",",
    "Curator Statement": false
  },
  "AMGAB0571": {
    "Interaction ID": "AMGAB0571",
    "Antibody ID": "ABID0427",
    "Antibody name": "2E4",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1074/jbc.M115.641738",
    "PMID": 25724648.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Immunohistochemistry, Radiolabeled- SDS-electrophoresis, ELISA",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"A catabody engineered from innate immunity principles hydrolyzed amyloid β (Aβ) specifically, dissolved Aβ aggregates, and cleared brain Aβ deposits without evident toxicity.\", \" The catabody recognized the Aβ C terminus noncovalently and hydrolyzed Aβ rapidly, with no reactivity to the Aβ precursor protein, transthyretin amyloid aggregates, or irrelevant proteins containing the catabody-sensitive Aβ dipeptide unit.\", \"The catabody dissolved preformed Aβ aggregates and inhibited Aβ aggregation more potently than an Aβ-binding IgG.\", \"Intravenous catabody treatment reduced brain Aβ deposits in a mouse Alzheimer disease model without inducing microgliosis or microhemorrhages.\", \"Specific Aβ hydrolysis appears to be an innate immune function that could be applied for therapeutic Aβ removal.\", \"Here we present evidence showing that the IgV degrades and clears Aβ specifically with no evidence of microglial activation or microhemorrhages.\", \"Treatment of prefibrillized Aβ42 with tissue culture supernatants containing IgV 2E6 but not IgV MMF6 dissolved the peptide fibrils nearly completely in two repeat experiments, leaving only sparse individual fibrils visible by electron microscopy (Fig. 3A, images 1–4).\",  \"Figure 3\", \"Likewise, a small concentration of the catalytically efficient nIgV 2E6 preparation dissolved prefibrillized Aβ42, judged by the ThT-binding test for β-sheet-containing aggregates (Fig. 3B).\", \" The aIgV 2E6 with lesser Aβ40 hydrolytic activity also dissolved prefibrillized Aβ42 but with lower potency compared to nIgV 2E6 (Fig. 3C; 17-fold difference between dissolution potency, computed as the ratio of nIgV and aIgV concentrations needed to reduce ThT binding by 20 fluorescence units compared with the value prior to incubation with the IgV; difference in Aβ hydrolytic activity of the two IgV preparations, 36-fold).\", \"The EDTA-treated nIgV and aIgV 2E6 preparations without Aβ hydrolytic activity also failed to dissolve fibrillar Aβ, suggesting catalysis as the dissolution mechanism.\", \"Detection of SDS-stable aggregates in electrophoresis gels run is a diagnostic test for Aβ42 oligomerization (21) (Fig. 3E, inset, lane 1). Treatment with nIgV 2E6 reduced the content of the 3-mer Aβ42 band (13 kDa), 4-mer Aβ42 band (17 kDa), and higher mass Aβ42 bands (45 kDa, 64–84 kDa) in preoligomerized Aβ42, accompanied by the appearance of a 2.5-kDa product fragment stainable by anti-Aβ antibodies (Fig. 3E). \", \"Dissolution of preformed Aβ aggregates by IgV 2E6.\", \"The dense Aβ plaques visible after diluent or IgV MMF6 treatment were absent after IgV 2E6 treatment, and only rare individual Aβ fibrils were evident (image 4 shows a magnified solitary fibril).\", \" ThT binding was reduced to levels below the starting fibrillar Aβ42 prior to incubation with the nIgVs (dashed line, 103 ± 10 fluorescence units (FU)).\", \" ThT binding was reduced to levels below the starting fibrillar Aβ42 prior to incubation with the aIgVs (dashed line, 103 ± 10 fluorescence units).\", \"Treatment of preoligomerized Aβ42 with nIgV 2E6 but not nIgV MMF6 (3 μg/ml, 24 h) depleted the SDS-stable Aβ trimers, tetramers, and high mass oligomers (45 kDa band, 64–84 kDa region).\", \"The ThT binding values for Aβ42 treated with diluent or control IgV MMF6 for 48 h were similar, but ThT binding was reduced significantly by treatment with nIgV 2E6 for the same duration (Fig. 4A).\", \"Figure 4\", \"Likewise, the content of each SDS-stable oligomer species was reduced significantly by nIgV 2E6 treatment of Aβ42 that had not been subjected to prior oligomerization, accompanied by the appearance of the 2.5-kDa hydrolytic product (Fig. 4B).\", \"The amyloid inhibition effect was evident at 1 μg/ml nIgV 2E6, whereas a 30-fold larger concentration of the Aβ-binding IgG1 59 was without effect (Fig. 4C).\", \"Together, the data suggest catalytic Aβ degradation as the mechanism of IgV anti-amyloid effects without the participation of accessory phagocytic cells that clear immune complexes by the Fc receptor uptake pathway.\", \"Reduced Aβ aggregation in the presence of nIgV 2E6. A, inhibition of Aβ42 fibrillization.\", \"Freshly dissolved Aβ42 substrate treated with nIgV 2E6 (4 μg/ml) but not nIgV MMF6 showed reduced ThT binding after 48 h. *, p < 0.01 versus IgV MMF6.\", \"The intensities of the SDS-stable trimer and tetramer were reduced by nIgV 2E6 treatment (24 h) of Aβ42 that had not been subjected to prior oligomerization compared with an equivalent nIgV MMF6 concentration (3 μg/ml). Higher order SDS-stable oligomers were less abundant than in preoligomerized Aβ42 preparations. Only the 74-kDa high mass oligomer band was evident, which was reduced significantly by treatment with nIgV 2E6. **, p < 0.005; *, p < 0.03.\", \"C, superior inhibition of Aβ42 fibrillization by nIgV 2E6 compared with IgG1 59. Aβ42 fibrillization tested as in A was inhibited by nIgV 2E6 (1 μg/ml) but not the Aβ-binding IgG1 59 (1 or 30 μg/ml).\", \"Decreased Aβ plaque burden surrounding the nIgV 2E6 delivery site was evident compared with the non-injected left brain neocortex of the same mice (Fig. 5, A and B). The Aβ clearance effect was limited to the immediate vicinity of the injection site, consistent with administration of a small IgV volume (2 μl). \", \"Figure 5\", \"A, local plaque burden was reduced 7 days after nIgV 2E6 but not nIgV MMF6 or PBS injection into the right brain neocortex, determined by staining with anti-Aβ antibody (1 μg of nIgV; n = 7 5XFAD mice in the nIgV 2E6 group, n = 4 mice each in the nIgV MMF6 and PBS groups).\", \"Ten days after intravenous treatment with aIgV 2E6 (100 μg total IgV/mouse), the right hemisphere neocortical Aβ deposits were reduced significantly compared with the control aIgV MMF6 treatment, as judged by immunohistochemical staining of brain sections (28% reduction, p < 0.05; Fig. 6, B and C). The Aβ-clearing effect was confirmed from the reduced hippocampal Aβ deposits (Fig. 6D). ELISA measurements in whole left brain hemisphere extracts showed modest but significant reductions of the soluble and insoluble Aβ40 and Aβ42 levels in the aIgV 2E6-treated mice (Table 2), suggesting a widespread Aβ clearing effect.\", \"Figure 6\", \"Table 2\", \"Together, the studies suggest significant brain Aβ clearance by the brief intravenous aIgV 2E6 treatment. \", \"Reduced brain Aβ following intravenous aIgV 2E6 injection.\", \"B, the plaque burden in the brain neocortex was reduced on day 10 after intravenous aIgV 2E6 injections on days 0 and 3 (50 μg/injection) compared with mice treated equivalently with aIgV MMF6 (n = 8 TgSwDI mice/group).\",",
    "Curator Statement": false
  },
  "AMGAB0572": {
    "Interaction ID": "AMGAB0572",
    "Antibody ID": "ABID0428",
    "Antibody name": "MMF6",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1074/jbc.M115.641738",
    "PMID": 25724648.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Table 2\",",
    "Curator Statement": false
  },
  "AMGAB0573": {
    "Interaction ID": "AMGAB0573",
    "Antibody ID": "ABID0428",
    "Antibody name": "MMF6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1074/jbc.M115.641738",
    "PMID": 25724648.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Immunohistochemistry, Radiolabeled- SDS-electrophoresis, ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Treatment of prefibrillized Aβ42 with tissue culture supernatants containing IgV 2E6 but not IgV MMF6 dissolved the peptide fibrils nearly completely in two repeat experiments, leaving only sparse individual fibrils visible by electron microscopy (Fig. 3A, images 1–4).\",  \"Figure 3\", \"The control non-catalytic nIgV MMF6 and aIgV MMF6 preparations did not dissolve fibrillar Aβ. \", \"Increased ThT binding is observed over 24 h of diluent and IgV MMF6 treatment due to continued Aβ fibrillization.\", \"Treatment of preoligomerized Aβ42 with nIgV 2E6 but not nIgV MMF6 (3 μg/ml, 24 h) depleted the SDS-stable Aβ trimers, tetramers, and high mass oligomers (45 kDa band, 64–84 kDa region).\", \"Figure 4\", \"The ThT binding values for Aβ42 treated with diluent or control IgV MMF6 for 48 h were similar, but ThT binding was reduced significantly by treatment with nIgV 2E6 for the same duration (Fig. 4A).\", \"Freshly dissolved Aβ42 substrate treated with nIgV 2E6 (4 μg/ml) but not nIgV MMF6 showed reduced ThT binding after 48 h. *, p < 0.01 versus IgV MMF6. ThT fluorescence values of Aβ treated with nIgV MMF6 and diluent after 48 h were indistinguishable (p > 0.1).\", \"The intensities of the SDS-stable trimer and tetramer were reduced by nIgV 2E6 treatment (24 h) of Aβ42 that had not been subjected to prior oligomerization compared with an equivalent nIgV MMF6 concentration (3 μg/ml). Higher order SDS-stable oligomers were less abundant than in preoligomerized Aβ42 preparations. Only the 74-kDa high mass oligomer band was evident, which was reduced significantly by treatment with nIgV 2E6. **, p < 0.005; *, p < 0.03.\", \"There was no decrease of local Aβ burden following nIgV MMF6 or PBS injection into the right brain neocortex compared with the non-injected left brain neocortex.\", \"Figure 5\", \"Reduced brain Aβ following intrabrain nIgV 2E6 injection.\", \"A, local plaque burden was reduced 7 days after nIgV 2E6 but not nIgV MMF6 or PBS injection into the right brain neocortex, determined by staining with anti-Aβ antibody (1 μg of nIgV; n = 7 5XFAD mice in the nIgV 2E6 group, n = 4 mice each in the nIgV MMF6 and PBS groups).\", \"Figure 6\", \"Table 2\",  \"B, the plaque burden in the brain neocortex was reduced on day 10 after intravenous aIgV 2E6 injections on days 0 and 3 (50 μg/injection) compared with mice treated equivalently with aIgV MMF6 (n = 8 TgSwDI mice/group).\",",
    "Curator Statement": false
  },
  "AMGAB0574": {
    "Interaction ID": "AMGAB0574",
    "Antibody ID": "ABID0429",
    "Antibody name": "IgG1 59",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1074/jbc.M115.641738",
    "PMID": 25724648.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The amyloid inhibition effect was evident at 1 μg/ml nIgV 2E6, whereas a 30-fold larger concentration of the Aβ-binding IgG1 59 was without effect (Fig. 4C).\", \"Figure 4\", \"C, superior inhibition of Aβ42 fibrillization by nIgV 2E6 compared with IgG1 59. Aβ42 fibrillization tested as in A was inhibited by nIgV 2E6 (1 μg/ml) but not the Aβ-binding IgG1 59 (1 or 30 μg/ml).\",",
    "Curator Statement": false
  },
  "AMGAB0575": {
    "Interaction ID": "AMGAB0575",
    "Antibody ID": "ABID0378",
    "Antibody name": "T24",
    "Amyloid ID": "AGAMYID0010",
    "Amyloid name": "Transthyretin",
    "DOI": "10.1074/jbc.M116.738138",
    "PMID": 27758856.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"T24 inhibited TTR accumulation in FAP model rats, which expressed human ATTR V30M in various tissues and exhibited non-fibrillar deposits of ATTR in the gastrointestinal tracts.\", \"T24 Inhibited TTR Deposits in FAP Model Rats\", \"Using FAP model rats, we performed an efficacy evaluation test to test whether T24 suppresses the deposition of TTR amyloid. Comparing the stained images after administration of T24 or PBS, the group administered with T24 (T24 group, Fig. 10A) showed greater reduction of TTR-positive areas than that administered PBS (PBS group, Fig. 10B). Semi-quantitatively, the T24 group tended to have a greater reduction in the amount of TTR deposits than in the PBS group (Fig. 10C).\", \"Figure 10\", \"T24 inhibits TTR deposition in FAP model rats.\", \"In this study, a difference in TTR deposits in the muscle layer of the large intestine was observed between the groups that were administered T24 and PBS; however, it was not statistically significant (Fig. 10C).\",",
    "Curator Statement": false
  },
  "AMGAB0576": {
    "Interaction ID": "AMGAB0576",
    "Antibody ID": "ABID0379",
    "Antibody name": "RT24",
    "Amyloid ID": "AGAMYID0010",
    "Amyloid name": "Transthyretin",
    "DOI": "10.1074/jbc.M116.738138",
    "PMID": 27758856.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Western blot",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Additionally, humanized T24 (RT24) inhibited TTR fibrillation and promoted macrophage phagocytosis of aggregated TTR.\", \"RT24 Inhibited V30M TTR Fibrillization\", \"We found that RT24 significantly inhibited V30M TTR fibrillization in an antibody concentration-dependent manner (Fig. 8) and that IC50 of RT24 is ∼150 nm.\", \"Figure 8\", \"First, RT24 inhibited V30M TTR fibrillization in an antibody concentration-dependent manner (Fig. 8). \", \"Thus, RT24, which targets conformationally changed TTR via fibrils and TTR amyloids, is expected to not only inhibit deposition of mutated TTR but also remove amyloid deposits (Fig. 10); therefore, this antibody has the potential to be a novel therapeutic drug for FAP.\",",
    "Curator Statement": false
  },
  "AMGAB0577": {
    "Interaction ID": "AMGAB0577",
    "Antibody ID": "ABID0178",
    "Antibody name": "c#6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1074/jbc.M117.777839",
    "PMID": 28623233.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"AβpE3-specific antibodies inhibit AβpE3–42 but not Aβ1–42 fibrillation\", \"Fibril formation of full-length non-pE-modified Aβ1–42 was not inhibited by any of the AβpE3-specific antibodies (Fig. 1C), underlining their specificity for pyroglutamate-modified Aβ.\", \"Figure 1\", \"C, the antibodies have no influence on full-length Aβ1–42 peptide fibril formation (4 μm Ab, molar ratio of 1:5). \"",
    "Curator Statement": false
  },
  "AMGAB0578": {
    "Interaction ID": "AMGAB0578",
    "Antibody ID": "ABID0178",
    "Antibody name": "c#6",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1074/jbc.M117.777839",
    "PMID": 28623233.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "Light Chain (LC): CDR1: KSSQSLLYSDGKTYLN, CDR2: LVSKLDS, CDR3: VQGTHFPFT,  Heavy Chain (HC): CDR1: GYSFTGYTMN, CDR2: LINPYNGVTRYNQKFKG, DR3: REAKR---EWDETY",
    "Quote of the interaction": "\"Here we present three separate monoclonal antibodies that specifically recognize AβpE3 with affinities of 1–10 nm and inhibit AβpE3 fibril formation in vitro. \", \"AβpE3-specific antibodies inhibit AβpE3–42 but not Aβ1–42 fibrillation\", \"In a thioflavin T fibrillation assay, all three antibodies inhibit fibril formation of the (full-length) AβpE3–42-peptide (Fig. 1, A and B). \", \"Figure 1\",  \"AβpE3-specific antibodies inhibit fibril formation. A and B, fibril formation, monitored by thioflavin T (ThT) fluorescence (measured in relative fluorescence units (RFU)) as a function of time [h], is inhibited by addition of AβpE3-specific antibodies (c#6, c#24, c#17) to 10 μm AβpE3–42 peptide in a molar ratio of 1:2.5 (4 μm Ab) (A) and 1:5 (2 μm Ab) (B).\"",
    "Curator Statement": false
  },
  "AMGAB0579": {
    "Interaction ID": "AMGAB0579",
    "Antibody ID": "ABID0179",
    "Antibody name": "c#17",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1074/jbc.M117.777839",
    "PMID": 28623233.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"AβpE3-specific antibodies inhibit AβpE3–42 but not Aβ1–42 fibrillation\", \"Fibril formation of full-length non-pE-modified Aβ1–42 was not inhibited by any of the AβpE3-specific antibodies (Fig. 1C), underlining their specificity for pyroglutamate-modified Aβ.\", \"Figure 1\", \"C, the antibodies have no influence on full-length Aβ1–42 peptide fibril formation (4 μm Ab, molar ratio of 1:5). \"",
    "Curator Statement": false
  },
  "AMGAB0580": {
    "Interaction ID": "AMGAB0580",
    "Antibody ID": "ABID0179",
    "Antibody name": "c#17",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1074/jbc.M117.777839",
    "PMID": 28623233.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "Light Chain (LC): CDR1: RSSQSLVHSDGNTYLH, CDR2: KVSNRFS, CDR3: SQSTHVPPT, Heavy Chain (HC): CDR1: GFTFSDYGMA, CDR2: FISNLAYSIYYADTVTG, CDR3: YDYDNILDYVMDY",
    "Quote of the interaction": "\"Here we present three separate monoclonal antibodies that specifically recognize AβpE3 with affinities of 1–10 nm and inhibit AβpE3 fibril formation in vitro. \", \"AβpE3-specific antibodies inhibit AβpE3–42 but not Aβ1–42 fibrillation\", \"In a thioflavin T fibrillation assay, all three antibodies inhibit fibril formation of the (full-length) AβpE3–42-peptide (Fig. 1, A and B). \", \"Figure 1\",  \"AβpE3-specific antibodies inhibit fibril formation. A and B, fibril formation, monitored by thioflavin T (ThT) fluorescence (measured in relative fluorescence units (RFU)) as a function of time [h], is inhibited by addition of AβpE3-specific antibodies (c#6, c#24, c#17) to 10 μm AβpE3–42 peptide in a molar ratio of 1:2.5 (4 μm Ab) (A) and 1:5 (2 μm Ab) (B).\"",
    "Curator Statement": false
  },
  "AMGAB0581": {
    "Interaction ID": "AMGAB0581",
    "Antibody ID": "ABID0180",
    "Antibody name": "c#24",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1074/jbc.M117.777839",
    "PMID": 28623233.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"AβpE3-specific antibodies inhibit AβpE3–42 but not Aβ1–42 fibrillation\", \"Fibril formation of full-length non-pE-modified Aβ1–42 was not inhibited by any of the AβpE3-specific antibodies (Fig. 1C), underlining their specificity for pyroglutamate-modified Aβ.\", \"Figure 1\", \"C, the antibodies have no influence on full-length Aβ1–42 peptide fibril formation (4 μm Ab, molar ratio of 1:5). \"",
    "Curator Statement": false
  },
  "AMGAB0582": {
    "Interaction ID": "AMGAB0582",
    "Antibody ID": "ABID0180",
    "Antibody name": "c#24",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1074/jbc.M117.777839",
    "PMID": 28623233.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "Light Chain (LC): CDR1: KSSQSLLYSNGKTYLN, CDR2: VVSKLDS, CDR3: VQGTHFPFT, Heavy Chain (HC):CDR1: GYIFNNYWIN, CDR2: QIYPGDGDTNYNGKFKG, CDR3: REG-------YIVY",
    "Quote of the interaction": "\"Here we present three separate monoclonal antibodies that specifically recognize AβpE3 with affinities of 1–10 nm and inhibit AβpE3 fibril formation in vitro. \", \"AβpE3-specific antibodies inhibit AβpE3–42 but not Aβ1–42 fibrillation\", \"In a thioflavin T fibrillation assay, all three antibodies inhibit fibril formation of the (full-length) AβpE3–42-peptide (Fig. 1, A and B). \", \"Figure 1\",  \"AβpE3-specific antibodies inhibit fibril formation. A and B, fibril formation, monitored by thioflavin T (ThT) fluorescence (measured in relative fluorescence units (RFU)) as a function of time [h], is inhibited by addition of AβpE3-specific antibodies (c#6, c#24, c#17) to 10 μm AβpE3–42 peptide in a molar ratio of 1:2.5 (4 μm Ab) (A) and 1:5 (2 μm Ab) (B).\"",
    "Curator Statement": false
  },
  "AMGAB0583": {
    "Interaction ID": "AMGAB0583",
    "Antibody ID": "ABID0325",
    "Antibody name": "M204-scFv",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1074/jbc.RA120.013638",
    "PMID": 32493775.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "VH/CDR3: KYGSEWGGDL; VL/CDR3: QSTYENPTYVS",
    "Quote of the interaction": "\"Figure 5\", \"M204-scFv antibody delays in vitro aggregation.\", \"M204-scFv inhibits aggregation recombinant tau\", \"All of the M204-scFv antibodies delayed fibril formation at ratios of 1:1 and 1:0.5 (tau-K18:scFv) (Fig. 5, E–G). However, the M204-scFv dimer exhibited the most pronounced delay in lag time, whereas the M204-scFv monomer showed the smallest effect.\", \" Inhibition of IL15-induced tau aggregation by M204-scFv is shown for the M204-scFv monomer (E), dimer (F), and trimer (G). \",",
    "Curator Statement": "The authors identify \"ionic liquid 15\" as an inducer of tau aggregation to metastable oligomers, and use it's abbreviation, (IL15), throughout the text. The different outcomes seen for the aggregation inhibition are related to different human seeds."
  },
  "AMGAB0584": {
    "Interaction ID": "AMGAB0584",
    "Antibody ID": "ABID0325",
    "Antibody name": "M204-scFv",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1074/jbc.RA120.013638",
    "PMID": 32493775.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In cellulo",
    "Experimental method(s)": "ThT - Aggregation kinetics, Biosensor Cell Seeding Assay",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "VH/CDR3: KYGSEWGGDL; VL/CDR3: QSTYENPTYVS",
    "Quote of the interaction": "\"Crystal structure of a conformational antibody that binds tau oligomers and inhibits pathological seeding by extracts from donors with Alzheimer's disease\", \"M204 and an engineered single-chain variable fragment (scFv) inhibited seeding by IL15-induced tau oligomers and pathological extracts from donors with AD and chronic traumatic encephalopathy.\", \"We engineered a single-chain variable fragment (scFv) construct of M204 and found that it too forms oligomers of different molecular weights, and that M204-scFv inhibits seeding by isolates from the autopsied brains of human donors with AD and CTE.\", \"Nevertheless as shown in Fig. 6, B–F, dimers and trimers of M204-scFv block seeding by extracts from three different AD donors. M204-scFv monomer on the other hand is a poor inhibitor of seeding, and in one case, even stimulates seeding (Fig. 6C).\", \"Figure 6\", \"M204-scFv antibodies inhibit the seeding of tau aggregation by autopsied brain extracts from three human AD brain patients.\", \"Collectively our results suggest that although M204-scFv preferentially targets recombinant oligomers over recombinant fibrils of tau, the antibody somehow still inhibits seeding by pathological brain extracts that are enriched in tau fibrils.\", \"Figure 7\", \"As a further test of the inhibitory power of dimers and trimers of M204-scFv, we assayed inhibition of seeding by crude lysates from four additional donors with diagnosed tauopathies: two with CTE, one with CBD, and one with a familial (P301L) mutation. As shown in Fig. 7, M204-scFv blocked seeding by one of the two CTE donors, but not by extracts from donors with CBD or the P301L mutation. In fact seeding by CBD or the P301L extracts appeared to be marginally enhanced by M204-scFv. \", \"M204-scFv dimer and trimer inhibit seeding by extract from (A) CTE Donor 1, but not (B) CTE Donor 2, (C) CBD donor, or (D) a donor with a P301L familial mutation.\", \"The engineered M204-scFv antibody itself adopts three different self-associated species: a monomer, dimer, and trimer, all of which bind to recombinant tau oligomers, but with the dimer most effectively inhibiting seeding.\", \"The lack of inhibition by M204 for some tauopathy brain extracts suggests the presence of various polymorphisms across different tauopathies.\", \"In addition, our inhibitor studies using crude brain extracts highlight other factors that may antagonize inhibition of tau seeding by M204-scFv, such as: 1) the presence of cellular proteases that could potentially degrade the antibody, and 2) the reducing environment of the cell extract, which could convert the trimeric and dimeric M204-scFv back to monomer, which we know to be a poor inhibitor of seeding.\", \"In summary, we engineered a single-chain, conformational antibody that recognizes recombinant oligomers of tau, and inhibits cell-to-cell seeding by extracts from autopsy sections from human donors with tau pathology.\",",
    "Curator Statement": "The authors identify \"ionic liquid 15\" as an inducer of tau aggregation to metastable oligomers, and use it's abbreviation, (IL15), throughout the text. The different outcomes seen for the aggregation inhibition are related to different human seeds."
  },
  "AMGAB0585": {
    "Interaction ID": "AMGAB0585",
    "Antibody ID": "ABID0325",
    "Antibody name": "M204-scFv",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1074/jbc.RA120.013638",
    "PMID": 32493775.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation,",
    "Experimental Model(s)": "In cellulo, In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Biosensor Cell Seeding Assay",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "VH/CDR3: KYGSEWGGDL; VL/CDR3: QSTYENPTYVS",
    "Quote of the interaction": "\"Nevertheless as shown in Fig. 6, B–F, dimers and trimers of M204-scFv block seeding by extracts from three different AD donors. M204-scFv monomer on the other hand is a poor inhibitor of seeding, and in one case, even stimulates seeding (Fig. 6C).\", \"Figure 6\", \"Figure 7\", \"As shown in Fig. 7, M204-scFv blocked seeding by one of the two CTE donors, but not by extracts from donors with CBD or the P301L mutation. In fact seeding by CBD or the P301L extracts appeared to be marginally enhanced by M204-scFv. \", \"The lack of inhibition by M204 for some tauopathy brain extracts suggests the presence of various polymorphisms across different tauopathies.\"",
    "Curator Statement": "The authors identify \"ionic liquid 15\" as an inducer of tau aggregation to metastable oligomers, and use it's abbreviation, (IL15), throughout the text. The different outcomes seen for the aggregation inhibition are related to different human seeds."
  },
  "AMGAB0586": {
    "Interaction ID": "AMGAB0586",
    "Antibody ID": "ABID0326",
    "Antibody name": "M204",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1074/jbc.RA120.013638",
    "PMID": 32493775.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Biosensor Cell Seeding Assay",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "VH/CDR3: KYGSEWGGDL; VL/CDR3: QSTYENPTYVS",
    "Quote of the interaction": "\"Crystal structure of a conformational antibody that binds tau oligomers and inhibits pathological seeding by extracts from donors with Alzheimer's disease\", \"M204 and an engineered single-chain variable fragment (scFv) inhibited seeding by IL15-induced tau oligomers and pathological extracts from donors with AD and chronic traumatic encephalopathy.\", \"Figure 3\", \"B, seeding by IL15-mediated tau-K18 purified oligomers in HEK293 biosensor cells expressing YFP-tagged tau-K18. C, as in B, except following treatment of tau-K18 oligomer with 10 μm M204 antibody. Seeding inhibition by M204 is interpreted based on the appearance of fewer puncta compared with B.\", \"As shown in Fig. 3, B–D, IL15-induced tau-K18 oligomers strongly seeded aggregation in tau biosensor cells, and seeding was inhibited by the addition of purified 10 μm M204.\", \"Because M204 is an inhibitor of tau seeding and shows immunoreactivity with AD brain extract, we aimed to engineer a single-chain (scFv) version of the antibody, which because of its smaller size, may possess greater tissue penetration than the full-length antibody (35).\", \"In summary, we engineered a single-chain, conformational antibody that recognizes recombinant oligomers of tau, and inhibits cell-to-cell seeding by extracts from autopsy sections from human donors with tau pathology.\",",
    "Curator Statement": "The authors identify \"ionic liquid 15\" as an inducer of tau aggregation to metastable oligomers, and use it's abbreviation, (IL15), throughout the text."
  },
  "AMGAB0587": {
    "Interaction ID": "AMGAB0587",
    "Antibody ID": "ABID0249",
    "Antibody name": "C6T",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1074/jbc.RA120.015327",
    "PMID": 33376140.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA,  Immunohistochemistry, Other: Congo Red staining,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"While treatment with C6T only slightly decreased Aβ deposits and plaque-associated inflammation, it restored neuronal integrity to WT levels, significantly promoted growth of new neurons, and impressively rescued survival rates to WT levels.\", \"Figure 2\",  \"Furthermore, we observed that the brain sections of mice treated with the recombinant human adeno-associated virus (rAAV)-C6T showed greatly reduced staining of C6T-immunoreactive structures (Fig. 2B).\", \"In the mice treated with either rAAV-C6T or rAAV-A4, the levels of both A4-reactive oligomeric variants (Fig. 2C; ∗p < 0.05) and C6T-reactive variants (Fig. 2D; ∗p < 0.05) were lowered compared with the vehicle-treated mice.\", \" The number of plaques significantly decreased in the cortex (Fig. 3B; ∗∗p < 0.01, ∗p < 0.05) and the hippocampus (Fig. 3C; ∗p < 0.05) of mice receiving either rAAV-A4 and rAAV-C6T compared with the littermate GFP vehicle group. Interestingly, the number of 6E10-staining plaques in the cortex decreased significantly more in the rAAV-A4–treated mice compared with the rAAV-C6T–treated mice (Fig. 3B; &p < 0.05) and were lower, though not statistically significantly, in the hippocampus as well.\", \"Figure 3\", \"Both C6T and A4 decrease Aβ deposits in APP/PS1 mice\", \"A significant decrease in the number of Congo red deposits was observed in both the cortex (Fig. 3E; ∗p < 0.05) and hippocampus (Fig. 3F; ∗p < 0.05) in brain tissue of mice treated with rAAV-A4 and rAAV-C6T compared with littermate GFP vehicle-treated mice. Similar to the results obtained with the 6E10-labeled plaques (Fig. 3B), a significant decrease in the number of Congo red structures was observed in the cortex in mice treated with rAAV-A4 compared with rAAV-C6T (Fig. 3F; &p < 0.05), and levels were also lower in the hippocampus.\", \"However, when we analyze how the scFvs influence amyloid plaque levels, the results are quite different. Amyloid plaque levels as determined by 6E10 staining (Fig. 3, A–C) and Congo red staining (Fig. 3, D–F) showed significant reductions in the A4-treated mice but only modest reduction in the C6T-treated mice. Treatment with A4 lowered both C6T- and A4-recognized oligomeric Aβ levels in the cortex and hippocampus, whereas treatment with C6T lowered C6T-recognized Aβ variant levels to essentially WT levels but did not alter A4-recognized Aβ variant levels.\", \"Since treatment with C6T did not reduce plaque levels as effectively as treatment with A4, the results suggest a correlation of certain oligomeric Aβ variants (such as those recognized by A4) with the formation of Aβ plaques (36, 37, 46), whereas the smaller intracellularly brain-derived C6T-recognized oligomeric Aβ species play a more important role in synaptic toxicity consistent with previous reports (47, 48).\",",
    "Curator Statement": false
  },
  "AMGAB0588": {
    "Interaction ID": "AMGAB0588",
    "Antibody ID": "ABID0250",
    "Antibody name": "A4",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1074/jbc.RA120.015327",
    "PMID": 33376140.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA,  Immunohistochemistry, Other: Congo Red staining,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Treatment with A4 on the other hand significantly decreased Aβ deposits but did not significantly decrease neuroinflammation or promote neuronal integrity, neurogenesis, or survival rate.\", \"Figure 2\", \"In the mice treated with either rAAV-C6T or rAAV-A4, the levels of both A4-reactive oligomeric variants (Fig. 2C; ∗p < 0.05) and C6T-reactive variants (Fig. 2D; ∗p < 0.05) were lowered compared with the vehicle-treated mice.\", \" The number of plaques significantly decreased in the cortex (Fig. 3B; ∗∗p < 0.01, ∗p < 0.05) and the hippocampus (Fig. 3C; ∗p < 0.05) of mice receiving either rAAV-A4 and rAAV-C6T compared with the littermate GFP vehicle group. Interestingly, the number of 6E10-staining plaques in the cortex decreased significantly more in the rAAV-A4–treated mice compared with the rAAV-C6T–treated mice (Fig. 3B; &p < 0.05) and were lower, though not statistically significantly, in the hippocampus as well.\", \"Figure 3\", \"Both C6T and A4 decrease Aβ deposits in APP/PS1 mice\", \"A significant decrease in the number of Congo red deposits was observed in both the cortex (Fig. 3E; ∗p < 0.05) and hippocampus (Fig. 3F; ∗p < 0.05) in brain tissue of mice treated with rAAV-A4 and rAAV-C6T compared with littermate GFP vehicle-treated mice. Similar to the results obtained with the 6E10-labeled plaques (Fig. 3B), a significant decrease in the number of Congo red structures was observed in the cortex in mice treated with rAAV-A4 compared with rAAV-C6T (Fig. 3F; &p < 0.05), and levels were also lower in the hippocampus.\", \"However, when we analyze how the scFvs influence amyloid plaque levels, the results are quite different. Amyloid plaque levels as determined by 6E10 staining (Fig. 3, A–C) and Congo red staining (Fig. 3, D–F) showed significant reductions in the A4-treated mice but only modest reduction in the C6T-treated mice. Treatment with A4 lowered both C6T- and A4-recognized oligomeric Aβ levels in the cortex and hippocampus, whereas treatment with C6T lowered C6T-recognized Aβ variant levels to essentially WT levels but did not alter A4-recognized Aβ variant levels.\", \"Since treatment with C6T did not reduce plaque levels as effectively as treatment with A4, the results suggest a correlation of certain oligomeric Aβ variants (such as those recognized by A4) with the formation of Aβ plaques (36, 37, 46), whereas the smaller intracellularly brain-derived C6T-recognized oligomeric Aβ species play a more important role in synaptic toxicity consistent with previous reports (47, 48).\",",
    "Curator Statement": false
  },
  "AMGAB0589": {
    "Interaction ID": "AMGAB0589",
    "Antibody ID": "ABID0265",
    "Antibody name": "intra-scFv-SE21",
    "Amyloid ID": "AGAMYID0014",
    "Amyloid name": "Superoxide dismutase [Cu-Zn]",
    "DOI": "10.1093/brain/awad222",
    "PMID": 37394908.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo, In cellulo",
    "Experimental method(s)": "Immunohistochemistry, Immunoblotting, Immunoprecipitation",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The adeno-associated virus-mediated expression of scFv-SE21 in the CNS of hSOD1G37R mice rescued spinal motor neurons, reduced the accumulation of misfolded SOD1, decreased gliosis and thus delayed disease onset and extended survival by 90 days.\", \"Here, we demonstrated that scFv-SE21, a single-chain antibody derived from SE21 mAb, expressed in the CNS of ALS mice transgenic for human SOD1G37R mutant, rescued spinal motor neurons, reduced the accumulation of soluble and aggregated forms of misfolded SOD1, suppressed gliosis, and thus delayed disease onset and extended survival by ∼90 days.\", \"Consistent with the idea that the β6/β7 loop region, once exposed, is implicated in triggering SOD1 aggregation,16 scFv-SE21 intrabody efficiently inhibited the accumulation of insoluble (Triton X-resistant) aggregates of hSOD1G93A overexpressed in mouse NSC-34 cells (Fig. 1 and Supplementary Fig. 3A–C).\", \"Figure 1\", \"scFv-SE21 prevents the formation of insoluble aggregates of hSOD1G93A in NSC-34 cells.\", \"Supplementary Figure 3\", \"ScFv-SE21 expression prevents the formation of insoluble hSOD1 aggregates in NSC-34 cells.\",  \"Consistent with the proposed mechanism of action, the induction of scFv-SE21 expression failed to reduce the amount of hSOD1G93A aggregates present in the cell prior to doxycycline addition, but efficiently suppressed the accumulation of novel aggregates (Fig. 1B and C). Importantly, the magnitude of the inhibitory effect was proportional to the extent of scFv-SE21 expression, since less hSOD1G93A aggregates were formed in the cells expressing scFv-SE21 under strong CMV promoter, compared to those in which the expression was controlled by a weaker doxycycline-inducible promoter (Fig. 1B and C and Supplementary Fig. 3B–E).\", \"The scFv-SE21 expression was effective in blocking the accumulation of aggregated forms of all the SOD1 variants tested (Supplementary Fig. 3B and C).\", \"Intra-scFv-SE21 reduced the accumulation of misfolded SOD1 in spinal cord\", \"Immunoprecipitation analysis using B8H10 antibody specifically recognizing misfolded forms of SOD145,46 revealed a significant delay in the accumulation of soluble species of misfolded SOD1 in spinal cord of intra-scFv-SE21, but not extra-scFv-SE21 treated animals (Fig. 4A and B).\", \"Figure 4\", \"ScFv-SE21 intrabody suppressed the accumulation of misfolded SOD1 in spinal cord of hSOD1G37R ALS mice.\", \"The IP results were in qualitative agreement with the results of spinal cord tissue immunostaining, which demonstrated a significant attenuation of the accumulation of aggregated forms of misfolded SOD1 (measured as a total area of B8H10-positive inclusions) in intra-scFv-SE21 treated animals, as compared to control or extra-scFV-SE21 treated mice (Fig. 4C and D and Supplementary Fig. 4A). As with soluble species of misfolded SOD1 measured by IP (Fig. 4A and B), accumulation of aggregated forms of SOD1 in spinal cord of intra-scFv-SE21 treated and control animals reached similar levels at their respective disease end-stages (Fig. 4D).\",",
    "Curator Statement": false
  },
  "AMGAB0590": {
    "Interaction ID": "AMGAB0590",
    "Antibody ID": "ABID0266",
    "Antibody name": "extra-scFv-SE21",
    "Amyloid ID": "AGAMYID0014",
    "Amyloid name": "Superoxide dismutase [Cu-Zn]",
    "DOI": "10.1093/brain/awad222",
    "PMID": 37394908.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Immunoprecipitation, immunoblotting",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Immunoprecipitation analysis using B8H10 antibody specifically recognizing misfolded forms of SOD145,46 revealed a significant delay in the accumulation of soluble species of misfolded SOD1 in spinal cord of intra-scFv-SE21, but not extra-scFv-SE21 treated animals (Fig. 4A and B).\", \"Figure 4\",",
    "Curator Statement": false
  },
  "AMGAB0591": {
    "Interaction ID": "AMGAB0591",
    "Antibody ID": "ABID0025.5",
    "Antibody name": "MAb86",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1093/brain/awu213",
    "PMID": 25085375.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA,",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" Chronic, peripheral administration of anti-tau/pS422 antibody reduces the accumulation of tau pathology.\", \"We show that TauPS2APP transgenic mice develop less tau pathology than vehicle-treated controls if treated for 4 months with anti-tau/pS422 antibody.\", \"Chronic treatment of TauPS2APP mice with MAb86 reduces tau/pS422 pathology\", \" At the end of treatment, immunoassay of whole brain extracts showed a significant reduction in tau/pS422 levels in MAb86-treated mice compared to vehicle-treated mice (Fig. 6A–C).\", \"Figure 6\", \"(A) Quantitative immunohistochemistry  of  hippocampal and cortical regions from TauPS2APP using anti-Tau/pS422 (clone 2.10.3) for immunodetection  mice shows a significant increase in overall fluorescence between the start and end of experiment (***  P < 0.001) and a significant reduction in the hippocampus of antibody-treated mice  compared to vehicle treated mice (**  P < 0.01).\",",
    "Curator Statement": false
  },
  "AMGAB0592": {
    "Interaction ID": "AMGAB0592",
    "Antibody ID": "ABID0430",
    "Antibody name": "A-887755",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/brain/awu280",
    "PMID": 25281869.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Treatment of 12-month-old mice with oligomer-specific (A-887755) or conformation-unspecific (6G1) antibodies for 8 weeks did not affect fibrillar plaque density or growth.\", \"Pan-amyloid-β antibodies as well as oligomer-specific antibodies alleviated the synaptic pathology, while amyloid deposition was unaffected by the treatment regimen.\", \"Anti-amyloid immunotherapy with 6G1 and A-887755 antibodies has no effect on fibrillar plaque growth and density.\", \"Figure 1\", \"At the end of the treatment period, overall plaque densities did not differ significantly between groups (Kruskal-Wallis test, n = 4–8; Fig. 1C).  Because amyloid deposition is a gradual process, the majority of the plaques may have been deposited before the treatment had an effect. Therefore, we analysed the volumes of pre-existing plaques, i.e. plaques that had been present before the treatment was started (Fig. 1D) and newborn plaques, i.e. plaques that appeared during the treatment period, separately (Fig. 1E). Neither group were altered by immunotherapy (Kruskal-Wallis test, n = 4–8; Fig. 3B and C). Finally, we analysed the linear growth rate of pre-existing and newborn plaques, which is proportional to the cube root of the difference in volumes between two imaging sessions (Hefendehl et al., 2011; Burgold et al., 2014). Again, immunotherapy had no effect on the growth rates of fibrillar plaques (Kruskal-Wallis test, n = 4–8; Fig. 1 F and G).\", \"Neither the oligomer-specific antibody had an effect on amyloid plaques, nor the conformation-unspecific antibody (Fig. 1).\", \"Nevertheless, the lack of effect even on newly appearing plaques suggests that amyloid deposition was unaffected by both antibodies. \",  \"However, even in the absence of an amyloid clearing effect we found that synapse loss was alleviated in animals treated with either non-conformation specific or oligomer-specific antibodies (Fig. 2).\",",
    "Curator Statement": false
  },
  "AMGAB0593": {
    "Interaction ID": "AMGAB0593",
    "Antibody ID": "ABID0431",
    "Antibody name": "6G1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/brain/awu280",
    "PMID": 25281869.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Treatment of 12-month-old mice with oligomer-specific (A-887755) or conformation-unspecific (6G1) antibodies for 8 weeks did not affect fibrillar plaque density or growth.\", \"Pan-amyloid-β antibodies as well as oligomer-specific antibodies alleviated the synaptic pathology, while amyloid deposition was unaffected by the treatment regimen.\", \"Anti-amyloid immunotherapy with 6G1 and A-887755 antibodies has no effect on fibrillar plaque growth and density.\", \"Figure 1\", \"At the end of the treatment period, overall plaque densities did not differ significantly between groups (Kruskal-Wallis test, n = 4–8; Fig. 1C).  Because amyloid deposition is a gradual process, the majority of the plaques may have been deposited before the treatment had an effect. Therefore, we analysed the volumes of pre-existing plaques, i.e. plaques that had been present before the treatment was started (Fig. 1D) and newborn plaques, i.e. plaques that appeared during the treatment period, separately (Fig. 1E). Neither group were altered by immunotherapy (Kruskal-Wallis test, n = 4–8; Fig. 3B and C). Finally, we analysed the linear growth rate of pre-existing and newborn plaques, which is proportional to the cube root of the difference in volumes between two imaging sessions (Hefendehl et al., 2011; Burgold et al., 2014). Again, immunotherapy had no effect on the growth rates of fibrillar plaques (Kruskal-Wallis test, n = 4–8; Fig. 1 F and G).\", \"Neither the oligomer-specific antibody had an effect on amyloid plaques, nor the conformation-unspecific antibody (Fig. 1).\", \"However, we observed no effect of the conformation-unspecific antibody, 6G1, which has an intermediate affinity for fibrils (Hillen et al., 2010), though in contrast to most other studies we quantified only fibrillar amyloid, as only this can be visualized in vivo.\", \"Nevertheless, the lack of effect even on newly appearing plaques suggests that amyloid deposition was unaffected by both antibodies. \", \"However, even in the absence of an amyloid clearing effect we found that synapse loss was alleviated in animals treated with either non-conformation specific or oligomer-specific antibodies (Fig. 2).\",",
    "Curator Statement": false
  },
  "AMGAB0594": {
    "Interaction ID": "AMGAB0594",
    "Antibody ID": "ABID0023",
    "Antibody name": "Ponezumab",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1093/brain/awv313",
    "PMID": 26493635.0,
    "Impact of the antibody on amyloid formation": "No effect, Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry, Intravital Multiphoton Microscopy, ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Passive immunotherapy targeting amyloid-β reduces cerebral amyloid angiopathy and improves vascular reactivity \", \"Chronic administration of ponezumab to transgenic mice led to a significant reduction in amyloid and amyloid-β accumulation both in leptomeningeal and brain vessels when measured by intravital multiphoton imaging and immunohistochemistry.\", \"Taken together, the beneficial effects ponezumab administration has on reducing the rate of cerebral amyloid angiopathy deposition and restoring cerebral vascular health favours a mechanism that involves rapid removal and/or neutralization of amyloid-β species that may otherwise be detrimental to normal vessel function.\", \"Chronic administration of ponezumab to transgenic mice resulted in a significant reduction in the rate of CAA accumulation.\", \" Taken together, the rapid and robust effects ponezumab treatment has on cerebral vascular reactivity in addition to the significant decrease in CAA following chronic administration favours a mechanism that involves rapid removal and/or neutralization of amyloid-β species that are otherwise detrimental to normal vessel function.\", \"Reduction of cerebral amyloid angiopathy in PSAPP transgenic mice following ponezumab administration\", \"When 6-month-old PSAPP transgenic mice were administered ponezumab peripherally (weekly, 10 mg/kg, i.p.) over the same period of time, there was no significant increase in the amount of CAA that accumulated (Fig. 1).\", \"Figure 1\", \"Figure 2\", \"Following treatment with ponezumab, we quantified a significant decrease in the number of amyloid positive leptomeningeal and brain vessels with a greater decrease observed in the number of brain vessels that were amyloid positive (Fig. 2). Similarly, the number of amyloid-β40 positive leptomeningeal and brain vessels following administration of ponezumab for 6 months were also significantly reduced (Fig. 2).\", \" Significant reduction in Congo red-positive amyloid in leptomeningeal (A) and brain vessels (B). Significant reduction in the number of leptomeningeal (C) or brain vessels (D) immunoreactive for amyloid-β40 following administration of ponezumab.\", \" Similar to the results we observed when quantifying the individual CAA vessel burden using intravital multiphoton imaging and immunohistochemistry, we also quantified a significant decrease in detergent soluble amyloid-β40 and amyloid-β42 levels in samples that were enriched for cerebral vascular elements (Fig. 3B and C).\", \"Figure 3\", \"While there was also a decrease in the levels of both amyloid-β40 and amyloid-β42 (15–20%, respectively) in the insoluble guanidine fraction (Fig. 3D and E), the reduction did not reach significance. In the crude brain homogenate there was also a significant decrease in the levels of both amyloid-β40 and amyloid-β42 measured in the detergent soluble fraction following weekly administration of PSAPP mice with ponezumab for 3 months.\", \"The levels of both amyloid-β peptides in the insoluble guanidine brain extract were unchanged as was the amount of amyloid quantified when using immunohistochemistry (Fig. 4).\", \"Figure 4\", \" The distribution of area brain parenchymal plaques that are positive for A40 or amyloid is not affected by treatment. \", \"Supplementary Figure 2\", \"Supplementary Figure 3\", \"No  significant differences were detected between ponezumab-treated and vehicle groups based on one way ANOVA tests, performed independently for each endpoint and category of plaques.\", \"Significant reduction in detergent soluble amyloid-β40 (B) and amyloid-β42 (C) following 3 months treatment of PSAPP mice with ponezumab (6 months of age at study start; 10 mg/kg, weekly intraperitoneal), *P < 0.05.\", \"There was no significant reduction in amyloid-β40 (D) or amyloid-β42 (E) levels from the guanidine extractable pool measured from the cerebrovascular enriched fraction; n = 6–7 per group.\", \"Significant decrease in detergent soluble amyloid-β40 (A) and amyloid-β42 (B) levels that were extracted from brain tissue of PSAPP mice after weekly administration of ponezumab for 6 months (6 months of age at study start; 10 mg/kg, weekly intraperitoneal administration) There was no significant reduction in amyloid-β40 (C) or amyloid-β42 (D) in the guanidine extractable pool from brain homogenates or when quantifying the number of amyloid-β40 (E) or amyloid (thioflavin S) positive plaques (F) parenchymal plaques.\", \" Chronic administration of ponezumab to PSAPP mice resulted in a significant reduction in CAA accumulation assessed both by histology and via quantitative intravital multiphoton microscopy of individual cerebral vessels. The age-dependent reduction in amyloid accumulation was also reflected in our biochemical measurements of amyloid-β using tissue that was enriched for cerebral vascular elements and a sensitive ELISA that measured various amyloid-β peptides.\", \"While the levels of the less mobilizable and insoluble pool represented by the guanidine extractable amyloid-β species were decreased, the reduction did not reach significance (for amyloid-β42P = 0.0515).\", \"In a separate cohort of PSAPP mice we confirmed our multiphoton and biochemical measurements by quantifying a significant reduction in the number of vessels that were positive for amyloid or amyloid-β40 by immunohistochemistry.\", \" While our studies may have been underpowered to detect a robust decrease in parenchymal amyloid-β load we would anticipate that a longer treatment period would have a more profound effect on this particular biochemical pool of amyloid-β. Taken together, our results demonstrate that chronic administration of ponezumab to transgenic mice with considerable CAA at the beginning of the treatment paradigm results in a significant reduction in the rate of CAA accumulation.\", \"Furthermore, biochemical analysis of tissue enriched in cerebral vascular elements suggests that the significant reduction in amyloid-β40 specific accumulation may also have beneficial effects on the removal of amyloid-β42.\",",
    "Curator Statement": false
  },
  "AMGAB0595": {
    "Interaction ID": "AMGAB0595",
    "Antibody ID": "ABID0023",
    "Antibody name": "Ponezumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/brain/awv313",
    "PMID": 26493635.0,
    "Impact of the antibody on amyloid formation": "No effect, Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" Similar to the results we observed when quantifying the individual CAA vessel burden using intravital multiphoton imaging and immunohistochemistry, we also quantified a significant decrease in detergent soluble amyloid-β40 and amyloid-β42 levels in samples that were enriched for cerebral vascular elements (Fig. 3B and C).\", \"Figure 3\", \"While there was also a decrease in the levels of both amyloid-β40 and amyloid-β42 (15–20%, respectively) in the insoluble guanidine fraction (Fig. 3D and E), the reduction did not reach significance. In the crude brain homogenate there was also a significant decrease in the levels of both amyloid-β40 and amyloid-β42 measured in the detergent soluble fraction following weekly administration of PSAPP mice with ponezumab for 3 months.\", \"The levels of both amyloid-β peptides in the insoluble guanidine brain extract were unchanged as was the amount of amyloid quantified when using immunohistochemistry (Fig. 4).\", \"Figure 4\", \"There was no significant difference in the distribution or size of amyloid-β/amyloid brain parenchymal plaques following ponezumab administration (Supplementary Figs 2–5).\", \"Supplementary Figure 2\", \"Supplementary Figure 4\", \" No significant differences were detected between Ponezumab-treated and vehicle groups  based on one-way ANOVA tests, performed independently for each endpoint and category of  plaques.\", \"Supplementary Figure 5\", \" No significant differences were detected  between Ponezumab-treated and vehicle groups.\", \"Significant reduction in detergent soluble amyloid-β40 (B) and amyloid-β42 (C) following 3 months treatment of PSAPP mice with ponezumab (6 months of age at study start; 10 mg/kg, weekly intraperitoneal), *P < 0.05.\", \"There was no significant reduction in amyloid-β40 (D) or amyloid-β42 (E) levels from the guanidine extractable pool measured from the cerebrovascular enriched fraction; n = 6–7 per group.\", \"Significant decrease in detergent soluble amyloid-β40 (A) and amyloid-β42 (B) levels that were extracted from brain tissue of PSAPP mice after weekly administration of ponezumab for 6 months (6 months of age at study start; 10 mg/kg, weekly intraperitoneal administration) There was no significant reduction in amyloid-β40 (C) or amyloid-β42 (D) in the guanidine extractable pool from brain homogenates or when quantifying the number of amyloid-β40 (E) or amyloid (thioflavin S) positive plaques (F) parenchymal plaques.\", \"The age-dependent reduction in amyloid accumulation was also reflected in our biochemical measurements of amyloid-β using tissue that was enriched for cerebral vascular elements and a sensitive ELISA that measured various amyloid-β peptides.\", \"Interestingly in addition to a significant decrease in the level of detergent soluble amyloid-β40, we also quantified a significant decrease in the level of amyloid-β42 following administration of ponezumab for 3 months.\", \"While the levels of the less mobilizable and insoluble pool represented by the guanidine extractable amyloid-β species were decreased, the reduction did not reach significance (for amyloid-β42P = 0.0515).\", \"In a separate cohort of PSAPP mice we confirmed our multiphoton and biochemical measurements by quantifying a significant reduction in the number of vessels that were positive for amyloid or amyloid-β40 by immunohistochemistry.\", \"Furthermore, biochemical analysis of tissue enriched in cerebral vascular elements suggests that the significant reduction in amyloid-β40 specific accumulation may also have beneficial effects on the removal of amyloid-β42.\",",
    "Curator Statement": false
  },
  "AMGAB0596": {
    "Interaction ID": "AMGAB0596",
    "Antibody ID": "ABID0133",
    "Antibody name": "MAb-11",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/brain/aww036",
    "PMID": 26956423.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other: Quantitative morphometry, Other: gratings-based X-ray phase contrast tomographic microscopy,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"When encapsulated cells are implanted before the onset of amyloid plaque deposition in TauPS2APP mice, chronic exposure to anti-amyloid-β antibodies dramatically reduces amyloid-β 40 and amyloid-β 42 levels in the brain, decreases amyloid plaque burden, and most notably, prevents phospho-tau pathology in the hippocampus\", \"Passive immunization against toxic misfolded proteins could offer protection against neurodegenerative disease.\",  \"Passive immunization by ECT delivery of mAb-11 decreases amyloid brain pathology in 5XFAD mice\", \"Dense and widespread amyloidosis, mainly affecting the cortex, hippocampus and thalamus, was found in 5- to 6-month-old animals implanted with devices containing GFP-expressing C2C12 myoblasts ( Fig. 4 A and B). Amyloid pathology was reduced in the 5XFAD mice treated with the mAb-11 secreting devices ( Fig. 4 C and D). Quantitative morphometry showed a significant reduction of the percentage of area covered with amyloid-β plaques in the cortex (−31.0%, P = 0.0069), hippocampus (−18.1%, P = 0.018) and thalamus (−31.7%, P = 0.013) ( Fig. 4 E). Plaque density was decreased in the same brain regions (cortex: −37.8%, P = 0.00005; hippocampus: −20.1%, P = 0.002; thalamus: −30.3%, P = 0.007; Fig. 4 F). The median plaque area was significantly increased in the treated mice ( P = 0.012; Fig. 4 G), consistent with a clearance of small amyloid deposits revealed by the shift in the plaque size distribution ( Supplementary Fig. 1 ).\", \"Figure 4\", \"Figure 4 Continuous anti-amyloid-β antibody delivered by ECT reduces amyloid burden in 5XFAD mice. \",  \"In these 5- to 6-month-old mice, the staining reveals a robust amyloid pathology that is reduced in the treated animals ( C and D ). ( B and D ) Higher magnifications of the regions outlined in ( A ) and ( C ), respectively. ( E ) The quantification of amyloid-β burden shows a significant reduction in the plaque load (percentage of the section  surface occupied by plaques) in the cortex, hippocampus and thalamus of treated mice. ( F ) The density of amyloid plaques is significantly decreased in these brain regions.\", \"Briefly, ECT devices secreting mAb-11 IgG2a were implanted in 7-month-old TauPS2APP mice, leading to chronic antibody exposure for 39 weeks. Similarly to the previous experiment in 5XFAD mice, ECT-mediated passive immunization led to a significant decrease in amyloid deposition.\",  \"When initiated before plaque deposition occurred in TauPS2APP mice, the chronic subcutaneous delivery of mAb-11 IgG2a led to a dramatic reduction in amyloid burden detected by anti-amyloid-β immunohistochemistry, compared with the mice implanted with control devices ( Fig. 6 A). Plaque load was clearly reduced throughout the cortex (−79.9%, P = 0.004) and hippocampus (−78.5%, P = 0.017) ( Fig. 6 B). Similarly, the number of plaques was dramatically decreased in both regions (−94.5% and −92.7%, respectively; Fig. 6 C). There was minimal deposition of amyloid plaques in the thalamus of 12-month-old TauPS2APP mice. In contrast, the amyloid burden was reduced by only 15–20% with F(ab’) 2 -secreting devices, an effect that was not significant ( P > 0.2).\", \"Figure 6\", \"Figure 6 Preventive mAb-11 immunization using ECT delivery strongly reduces amyloid load in the brain of TauPS2APP mice. ( A ) Amyloid burden revealed by anti-amyloid-β immunostaining (6E10) in the frontal cortices of 12-month-old TauPS2APP mice. Note the decreased amyloid pathology in the cortex of the TauPS2APP mouse continuously treated with mAb-11 IgG2a. ( B ) Plaque load, expressed as the percentage of the brain area occupied by amyloid-β-positive plaques, is significantly reduced in the cortex and hippocampus of mice treated with mAb-11 IgG2a. ( C ) The density of amyloid plaques is significantly decreased in these brain regions.\", \"Strong reduction of plaque density throughout the whole cortex of ECT-mAb-11 treated mice \" , \" The density of plaques in the cortex (plaques/mm 3 ) was determined following threshold segmentation ( Fig. 7 A and B and Supplementary Videos 1–3 ). Coronal maximum-intensity maps show that plaque density was clearly reduced in the entire hemicortex of the mAb-11 IgG2a-treated mice ( Fig. 7 C). In contrast, the density and distribution of amyloid plaques were similar in control and F(ab’) 2 -treated mice. Volumetric information from the phase contrast CT datasets was used to determine the total number of plaques in the hemicortex of the mice in each group ( Fig. 7 D). The mAb-11 IgG2a treatment dramatically reduced the number of detectable plaques (−83%, P = 0.00013), whereas the effect of the F(ab’) 2 treatment was not significant (−25%, P = 0.0697).\", \"Figure 7\", \"Figure 7 ECT delivery of mAb-11 IgG2a prevents amyloid plaque deposition throughout the entire cortex of TauPS2APP mice.\", \"Note that IgG2a-treated mice have detectable plaques only in the most frontal part of the cortex. ( C ) Coronal maximum-intensity maps of the representative hemicortex. Note the overall reduction in plaque density in the IgG2a-treated mouse. \", \"Our results are consistent with previous reports, which have shown that the systemic administration of anti-amyloid-β antibodies can decrease brain amyloid burden in preclinical Alzheimer’s disease models ( Bard et al. , 2000 , 2003 ; DeMattos et al. , 2001 ; Wilcock et al. , 2004 a , b ; Buttini et al. , 2005 ; Adolfsson et al. , 2012 ).\",",
    "Curator Statement": false
  },
  "AMGAB0597": {
    "Interaction ID": "AMGAB0597",
    "Antibody ID": "ABID0134",
    "Antibody name": "mAb-11 F(ab’) 2",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/brain/aww036",
    "PMID": 26956423.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other: Quantitative morphometry, Other: gratings-based X-ray phase contrast tomographic microscopy,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Briefly, ECT devices secreting mAb-11 IgG2a were implanted in 7-month-old TauPS2APP mice, leading to chronic antibody exposure for 39 weeks. Similarly to the previous experiment in 5XFAD mice, ECT-mediated passive immunization led to a significant decrease in amyloid deposition.\",  \"When initiated before plaque deposition occurred in TauPS2APP mice, the chronic subcutaneous delivery of mAb-11 IgG2a led to a dramatic reduction in amyloid burden detected by anti-amyloid-β immunohistochemistry, compared with the mice implanted with control devices ( Fig. 6 A). Plaque load was clearly reduced throughout the cortex (−79.9%, P = 0.004) and hippocampus (−78.5%, P = 0.017) ( Fig. 6 B). Similarly, the number of plaques was dramatically decreased in both regions (−94.5% and −92.7%, respectively; Fig. 6 C). There was minimal deposition of amyloid plaques in the thalamus of 12-month-old TauPS2APP mice. In contrast, the amyloid burden was reduced by only 15–20% with F(ab’) 2 -secreting devices, an effect that was not significant ( P > 0.2).\", \"Figure 6\", \" The density of plaques in the cortex (plaques/mm 3 ) was determined following threshold segmentation ( Fig. 7 A and B and Supplementary Videos 1–3 ). Coronal maximum-intensity maps show that plaque density was clearly reduced in the entire hemicortex of the mAb-11 IgG2a-treated mice ( Fig. 7 C). In contrast, the density and distribution of amyloid plaques were similar in control and F(ab’) 2 -treated mice. Volumetric information from the phase contrast CT datasets was used to determine the total number of plaques in the hemicortex of the mice in each group ( Fig. 7 D). The mAb-11 IgG2a treatment dramatically reduced the number of detectable plaques (−83%, P = 0.00013), whereas the effect of the F(ab’) 2 treatment was not significant (−25%, P = 0.0697).\", \"Figure 7\",",
    "Curator Statement": false
  },
  "AMGAB0598": {
    "Interaction ID": "AMGAB0598",
    "Antibody ID": "ABID0520",
    "Antibody name": "Antibody D",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1093/brain/awz100",
    "PMID": 31038156.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"First, antibody D effectively prevented the induction of tau pathology in the brains of transgenic mice that had been injected with human Alzheimer’s disease brain extracts, showing that it could effectively neutralize the pathological species present in these extracts. Second, by using K18 P301L tau fibrils to induce pathology, we further demonstrated that antibody D was also capable of blocking the progression of tau pathology to distal brain regions.\", \"We injected K18-P301L in hTauP301L transgenic mice (Peeraer et al., 2015); tau fibrils that are not recognized by tau antibody D. We demonstrated in this model that antibody D is capable of blocking the progression of tau pathology to distal brain regions, as the therapeutic antibody cannot bind to the injected material, it unambiguously demonstrates an effect on spread, even though the seed is artificial.\", \"Immunization with a mid-region epitope tau antibody reduces human tau seeding\", \"Antibody D treatment strongly reduced AT8 (Figs 1C and 2A) and AT100 immunoreactivity (Fig. 1H and 2B) in the ipsilateral CA1 compared to control isotype antibody treatment.\", \"Figure 1\", \"Figure 2\", \"(A) Percentage of AT8 immunopositive areas (A) in the ipsi- and contralateral CA1 layer. Statistical values: antibody D versus isotype, in the ipsilateral side: Z = −4.22, P < 0.0001 and in the contralateral side: Z = −3.55, P = 0.0004; antibody A versus isotype, in the ipsilateral side: Z = 0.7, P = 0.482 and in the contralateral side: Z = −0.62, P = 0.535).\", \"(B) Percentage of AT100 immunopositive areas in the ipsi- and contralateral CA1 layer. Statistical values: antibody D versus isotype, in the ipsilateral side: Z = −3.27, P = 0.0011 and in the contralateral side: Z = −2.7, P = 0.0068; antibody A versus isotype, in the ipsilateral side: Z = −1.76, P = 0.0784 and in the contralateral side: Z = −2.25, P = 0.0243).\", \"(C) Number of AT8-positive cells in the CA1 layer Statistical values: antibody D versus isotype, in the ipsilateral side: Z = −4.16, P < 0.0001 and in the contralateral side: Z = −4.02, P < 0.0001; antibody A versus isotype, in the ipsilateral side: Z = 2.84, P = 0.0045 and in the contralateral side: Z = 1.61, P = 0.105).\", \"Conversely, in hAD-injected groups, sarkosyl-insoluble materials characterized by high molecular weight species, pS396 and AT100-immunoreactivities, were higher in control isotype and antibody A-treated mice than in the antibody D-treated mice. High molecular weight species were mainly labelled by pSer396 and AT100 antibodies, which recognize epitopes mostly found in PHF-like structures (Buée-Scherrer et al., 1996; Allen et al., 2002; Augustinack et al., 2002). Antibody D strongly reduced the level of sarkosyl-insoluble material detected by M19G antibody (highly aggregated tau species) compared to the control isotype antibody (Fig. 3M; 1.6-fold, P = 0.0028) and compared to antibody A groups (Fig. 3M; 2-fold, P = 0.0011).\", \"Figure 3\", \"Immunization with antibody D strongly prevented human tau propagation\", \"As expected, immunization with the antibody D did not reduce AT8-immunoreactivity in the CA1 ipsilateral to the fibril injection (Fig. 4C, P = 0.1009), as the epitope of the antibody is not present in the fibrils and it therefore cannot inhibit its uptake. However, as would be expected for an antibody having an effect on spread, it reduced AT8 immunoreactivity in the contralateral hippocampus (Fig. 4B and C, 2-fold, P = 0.00282).\", \"Figure 4\", \"Antibody D significantly reduced neurofibrillary tangles, quantified by AT100 antibody both by histochemical and biochemical approaches.\", \"As expected antibody D did not reduce pathology at the site of injection as it cannot block the uptake of K18 fibrils. In contrast, antibody D significantly reduced AT8-immunoreactivity in the contralateral hemisphere.\",",
    "Curator Statement": false
  },
  "AMGAB0599": {
    "Interaction ID": "AMGAB0599",
    "Antibody ID": "ABID0520",
    "Antibody name": "Antibody D",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1093/brain/awz100",
    "PMID": 31038156.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"As expected, immunization with the antibody D did not reduce AT8-immunoreactivity in the CA1 ipsilateral to the fibril injection (Fig. 4C, P = 0.1009), as the epitope of the antibody is not present in the fibrils and it therefore cannot inhibit its uptake. However, as would be expected for an antibody having an effect on spread, it reduced AT8 immunoreactivity in the contralateral hippocampus (Fig. 4B and C, 2-fold, P = 0.00282).\", \"Figure 4\", \"As expected antibody D did not reduce pathology at the site of injection as it cannot block the uptake of K18 fibrils. In contrast, antibody D significantly reduced AT8-immunoreactivity in the contralateral hemisphere.\",",
    "Curator Statement": "Authors state that the negligible effect in the CA1 ipsilateral, place of the fibril injection, was due to the P301L-K18 fibres lacking the epitope the Antibody D recognises."
  },
  "AMGAB0600": {
    "Interaction ID": "AMGAB0600",
    "Antibody ID": "ABID0521",
    "Antibody name": "Antibody A",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1093/brain/awz100",
    "PMID": 31038156.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot,",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In contrast, an amino-terminal tau antibody, which was less effective at blocking tau seeding in vitro showed less efficacy in reducing Alzheimer’s disease patient tau driven pathology in the transgenic mouse model.\", \"Figure 1\", \"Figure 2\", \"In contrast, antibody A immunization had no effect on AT8 immunoreactivity (Figs 1D and 2A); although a decrease in the number of AT8-positive cells was observed, this was, however, less than that seen with antibody D (Fig. 2C).\", \"(A) Percentage of AT8 immunopositive areas (A) in the ipsi- and contralateral CA1 layer. Statistical values: antibody D versus isotype, in the ipsilateral side: Z = −4.22, P < 0.0001 and in the contralateral side: Z = −3.55, P = 0.0004; antibody A versus isotype, in the ipsilateral side: Z = 0.7, P = 0.482 and in the contralateral side: Z = −0.62, P = 0.535).\", \"(B) Percentage of AT100 immunopositive areas in the ipsi- and contralateral CA1 layer. Statistical values: antibody D versus isotype, in the ipsilateral side: Z = −3.27, P = 0.0011 and in the contralateral side: Z = −2.7, P = 0.0068; antibody A versus isotype, in the ipsilateral side: Z = −1.76, P = 0.0784 and in the contralateral side: Z = −2.25, P = 0.0243).\", \"(C) Number of AT8-positive cells in the CA1 layer Statistical values: antibody D versus isotype, in the ipsilateral side: Z = −4.16, P < 0.0001 and in the contralateral side: Z = −4.02, P < 0.0001; antibody A versus isotype, in the ipsilateral side: Z = 2.84, P = 0.0045 and in the contralateral side: Z = 1.61, P = 0.105).\", \"Conversely, in hAD-injected groups, sarkosyl-insoluble materials characterized by high molecular weight species, pS396 and AT100-immunoreactivities, were higher in control isotype and antibody A-treated mice than in the antibody D-treated mice. High molecular weight species were mainly labelled by pSer396 and AT100 antibodies, which recognize epitopes mostly found in PHF-like structures (Buée-Scherrer et al., 1996; Allen et al., 2002; Augustinack et al., 2002). Antibody D strongly reduced the level of sarkosyl-insoluble material detected by M19G antibody (highly aggregated tau species) compared to the control isotype antibody (Fig. 3M; 1.6-fold, P = 0.0028) and compared to antibody A groups (Fig. 3M; 2-fold, P = 0.0011).\", \"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0601": {
    "Interaction ID": "AMGAB0601",
    "Antibody ID": "ABID0522",
    "Antibody name": "Anti-hTNFα",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1093/brain/awz100",
    "PMID": 31038156.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 1\", \"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0602": {
    "Interaction ID": "AMGAB0602",
    "Antibody ID": "ABID0177",
    "Antibody name": "TOMA",
    "Amyloid ID": "AGAMYID0023",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1093/eurheartj/ehad205",
    "PMID": 37122097.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Monoclonal anti-tau antibody therapy improved myocardial function and clearance of toxic aggregates in mice, supporting tau as a potential target for novel HF immunotherapy.\", \"Figure 7\", \"The functional improvement was accompanied by a reduction in the accumulation of tau oligomers (Figure 7H, I), and a more ordered distribution of Ca2+ handling proteins as exemplified by staining of the ryanodine receptors (RyRs) (Figure 7J), providing the first evidence of anti-proteotoxic mAb therapy for HF.\", \" Here we show that targeting tau oligomers with TOMA improves diastolic function 1 month after therapy (Figure 7B–G; see Supplementary material online, Tables S4 and S5) and reduces tau oligomer aggregates in a tauopathy mouse model (Figure 7H and I).\",",
    "Curator Statement": false
  },
  "AMGAB0603": {
    "Interaction ID": "AMGAB0603",
    "Antibody ID": "ABID0151",
    "Antibody name": "Ab-A",
    "Amyloid ID": "AGAMYID0010",
    "Amyloid name": "Transthyretin",
    "DOI": "10.1093/eurheartj/ehz695",
    "PMID": 31865366.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other: Technetium pyrophosphate (99mTc-PYP) imaging",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Using an experimental in vivo model the mAb was shown efficacious in removing aggregated TTR and has shown favourable effects on surrogates of functional cardiac performance.\", \"Figure 4A shows decrease in PYP cardiac uptake (% normalized TTR uptake ratio) in 10 mg/kg (P = 0.0016) and 5 mg/kg (P = 0.0047) Ab-AþTTR treatment groups (70.87% and 73.95%, respectively) relative to sham+TTR treatment group of animals (100%)\", \"This result demonstrates that Ab-A clears and degrades the aggregated TTR in the rat hearts.\", \"Figure 4\", \"In this experimental model, we observed that systemic delivery of Ab-A was capable of facilitating the clearance of TTR aggregates evident by a rapid reduction in the PyP signals as compared to IgG1 control mAb.\", \"Unlike stabilizers and silencers that are currently actively explored in ATTR amyloidosis, Ab-A has the dual capacity of promoting clearance and degradation of aggregated and already irreversibly destabilized TTR and in parallel, attenuating toxicity of preexisting plaques to cardiomyocytes thus offering a potential add-on therapy to the strategy of native TTR removal/stabilization.\", \"A surrogate test was developed to monitor its dosing and potential efficacy in reducing plaque burden.\"",
    "Curator Statement": false
  },
  "AMGAB0604": {
    "Interaction ID": "AMGAB0604",
    "Antibody ID": "ABID0152",
    "Antibody name": "1G4-2",
    "Amyloid ID": "AGAMYID0010",
    "Amyloid name": "Transthyretin",
    "DOI": "10.1093/eurheartj/ehz695",
    "PMID": 31865366.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other: Technetium pyrophosphate (99mTc-PYP) imaging",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"1G4-2 was used as mouse IgG sham control showing no unspecific binding\", Figure 4A shows decrease in PYP cardiac uptake (% normalized TTR uptake ratio) in 10 mg/kg (P = 0.0016) and 5 mg/kg (P = 0.0047) Ab-AþTTR treatment groups (70.87% and 73.95%, respectively) relative to sham+TTR treatment group of animals (100%)\", \"This result demonstrates that Ab-A clears and degrades the aggregated TTR in the rat hearts.\", \"Figure 4\", \"In this experimental model, we observed that systemic delivery of Ab-A was capable of facilitating the clearance of TTR aggregates evident by a rapid reduction in the PyP signals as compared to IgG1 control mAb.\"",
    "Curator Statement": false
  },
  "AMGAB0605": {
    "Interaction ID": "AMGAB0605",
    "Antibody ID": "ABID0419",
    "Antibody name": "BAM-10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/jb/mvm239",
    "PMID": 18174189.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,  TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"BAM-10 as an IgG form showed inhibition at 150 nM IC50 (Fig. 5C and D).\", \"Figure 6\", \"The IE of BAM-10 was evident from 0 to 3 h but no longer significant at the point of 6 h.\",",
    "Curator Statement": false
  },
  "AMGAB0606": {
    "Interaction ID": "AMGAB0606",
    "Antibody ID": "ABID0531",
    "Antibody name": "B6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/jb/mvm239",
    "PMID": 18174189.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo, In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,  TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"B6 inhibited the Aβ1–42 fibril formation with 600 nM IC50 in spite of being the monovalent scFv form.\",\"Inhibitory Activity of B6 scFvs on Aβ1–42 Fibrillation\", \"Figure 5\",\"On the other hand, the scFv clones selected from fibril Aβ1–42-coated plates markedly inhibited the Aβ1–42 fibrillation (Fig. 5B).\", \"Inhibitory activity of B6 scFv on Aβ1–42 fibrillation.\", \"Figure 6\", \"When B6 scFv was added at 3 h, Aβ1–42 appeared to form a large sphere and an immature fibril. When B6 scFv was added to Aβ1–42 at 6 h, the pre-existing fibril did not decrease with further incubation, and a mature fibril was observed.\", \"It is of note that soluble Aβ1–42-selected scFvs, except Fv1E4, hardly inhibited the Aβ1–42 fibrillation, whereas all fibrillar Aβ1–42-selected scFvs, including B6, significantly showed an inhibitory effect against the fibrillation of Aβ1–42 despite their monovalent nature (Fig. 5).\", \"The inhibitory effects (IE) of B6 or Fv1E4 scFv were detected at the early phase, fading away by around 3 h, although the IE of Fv1E4 were very weak (IC50 > 1,400 nM: Fig. 5E). \",",
    "Curator Statement": false
  },
  "AMGAB0607": {
    "Interaction ID": "AMGAB0607",
    "Antibody ID": "ABID0544",
    "Antibody name": "MY5R",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/jb/mvm239",
    "PMID": 18174189.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0608": {
    "Interaction ID": "AMGAB0608",
    "Antibody ID": "ABID0545",
    "Antibody name": "B7",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/jb/mvm239",
    "PMID": 18174189.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"On the other hand, the scFv clones selected from fibril Aβ1–42-coated plates markedly inhibited the Aβ1–42 fibrillation (Fig. 5B).\",\"It is of note that soluble Aβ1–42-selected scFvs, except Fv1E4, hardly inhibited the Aβ1–42 fibrillation, whereas all fibrillar Aβ1–42-selected scFvs, including B6, significantly showed an inhibitory effect against the fibrillation of Aβ1–42 despite their monovalent nature (Fig. 5).\",",
    "Curator Statement": false
  },
  "AMGAB0609": {
    "Interaction ID": "AMGAB0609",
    "Antibody ID": "ABID0546",
    "Antibody name": "D1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/jb/mvm239",
    "PMID": 18174189.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"On the other hand, the scFv clones selected from fibril Aβ1–42-coated plates markedly inhibited the Aβ1–42 fibrillation (Fig. 5B).\",\"It is of note that soluble Aβ1–42-selected scFvs, except Fv1E4, hardly inhibited the Aβ1–42 fibrillation, whereas all fibrillar Aβ1–42-selected scFvs, including B6, significantly showed an inhibitory effect against the fibrillation of Aβ1–42 despite their monovalent nature (Fig. 5).\",",
    "Curator Statement": false
  },
  "AMGAB0610": {
    "Interaction ID": "AMGAB0610",
    "Antibody ID": "ABID0547",
    "Antibody name": "F10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/jb/mvm239",
    "PMID": 18174189.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"On the other hand, the scFv clones selected from fibril Aβ1–42-coated plates markedly inhibited the Aβ1–42 fibrillation (Fig. 5B).\",\"It is of note that soluble Aβ1–42-selected scFvs, except Fv1E4, hardly inhibited the Aβ1–42 fibrillation, whereas all fibrillar Aβ1–42-selected scFvs, including B6, significantly showed an inhibitory effect against the fibrillation of Aβ1–42 despite their monovalent nature (Fig. 5).\",",
    "Curator Statement": false
  },
  "AMGAB0611": {
    "Interaction ID": "AMGAB0611",
    "Antibody ID": "ABID0548",
    "Antibody name": "FvE1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/jb/mvm239",
    "PMID": 18174189.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"The scFv clones selected from soluble Aβ1–42-coated plates hardly inhibited the Aβ1–42 fibrillation except that Fv1E4 scFv showed a weak inhibitory activity (Fig. 5A and E).\", \"It is of note that soluble Aβ1–42-selected scFvs, except Fv1E4, hardly inhibited the Aβ1–42 fibrillation, whereas all fibrillar Aβ1–42-selected scFvs, including B6, significantly showed an inhibitory effect against the fibrillation of Aβ1–42 despite their monovalent nature (Fig. 5).\",",
    "Curator Statement": false
  },
  "AMGAB0612": {
    "Interaction ID": "AMGAB0612",
    "Antibody ID": "ABID0549",
    "Antibody name": "FvE4",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/jb/mvm239",
    "PMID": 18174189.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"The scFv clones selected from soluble Aβ1–42-coated plates hardly inhibited the Aβ1–42 fibrillation except that Fv1E4 scFv showed a weak inhibitory activity (Fig. 5A and E).\", \"It is of note that soluble Aβ1–42-selected scFvs, except Fv1E4, hardly inhibited the Aβ1–42 fibrillation, whereas all fibrillar Aβ1–42-selected scFvs, including B6, significantly showed an inhibitory effect against the fibrillation of Aβ1–42 despite their monovalent nature (Fig. 5).\", \"The inhibitory effects (IE) of B6 or Fv1E4 scFv were detected at the early phase, fading away by around 3 h, although the IE of Fv1E4 were very weak (IC50 > 1,400 nM: Fig. 5E). \",",
    "Curator Statement": false
  },
  "AMGAB0613": {
    "Interaction ID": "AMGAB0613",
    "Antibody ID": "ABID0550",
    "Antibody name": "Fv2A7",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/jb/mvm239",
    "PMID": 18174189.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,  TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"The scFv clones selected from soluble Aβ1–42-coated plates hardly inhibited the Aβ1–42 fibrillation except that Fv1E4 scFv showed a weak inhibitory activity (Fig. 5A and E).\", \"Figure 6\", \"In the same experiments, Fv2A7 (anti-Aβ1–42 scFv as a negative control, see Fig. 2A) or unrelated scFv (data not shown) showed no influence on Aβ1–42 fibrillation.\", \"It is of note that soluble Aβ1–42-selected scFvs, except Fv1E4, hardly inhibited the Aβ1–42 fibrillation, whereas all fibrillar Aβ1–42-selected scFvs, including B6, significantly showed an inhibitory effect against the fibrillation of Aβ1–42 despite their monovalent nature (Fig. 5).\",",
    "Curator Statement": false
  },
  "AMGAB0614": {
    "Interaction ID": "AMGAB0614",
    "Antibody ID": "ABID0551",
    "Antibody name": "Fv2A8",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/jb/mvm239",
    "PMID": 18174189.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"The scFv clones selected from soluble Aβ1–42-coated plates hardly inhibited the Aβ1–42 fibrillation except that Fv1E4 scFv showed a weak inhibitory activity (Fig. 5A and E).\", \"It is of note that soluble Aβ1–42-selected scFvs, except Fv1E4, hardly inhibited the Aβ1–42 fibrillation, whereas all fibrillar Aβ1–42-selected scFvs, including B6, significantly showed an inhibitory effect against the fibrillation of Aβ1–42 despite their monovalent nature (Fig. 5).\",",
    "Curator Statement": false
  },
  "AMGAB0615": {
    "Interaction ID": "AMGAB0615",
    "Antibody ID": "ABID0552",
    "Antibody name": "Fv2B6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/jb/mvm239",
    "PMID": 18174189.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"The scFv clones selected from soluble Aβ1–42-coated plates hardly inhibited the Aβ1–42 fibrillation except that Fv1E4 scFv showed a weak inhibitory activity (Fig. 5A and E).\", \"It is of note that soluble Aβ1–42-selected scFvs, except Fv1E4, hardly inhibited the Aβ1–42 fibrillation, whereas all fibrillar Aβ1–42-selected scFvs, including B6, significantly showed an inhibitory effect against the fibrillation of Aβ1–42 despite their monovalent nature (Fig. 5).\",",
    "Curator Statement": false
  },
  "AMGAB0616": {
    "Interaction ID": "AMGAB0616",
    "Antibody ID": "ABID0446",
    "Antibody name": "1E8 scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/protein/gzt025",
    "PMID": 23766374.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro,",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point), ELISA,",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Here we show that the soluble 1E8 scFv binds to the central region of Aβ with an affinity of ∼55 nM and significantly reduces fibril formation of Aβ1–42. \", \"Here, we extend recombinant manipulation of 1E8 by engineering it to an scFv format, precisely determine its affinity for Aβ antigen and show its utility in inhibiting Aβ aggregation\", \"In contrast to the untreated Aβ1–42, incubation of Aβ1–42 with 1E8 scFv (20 μM) significantly (P < 0.001) reduced ThT fluorescence by ∼80% (Fig. 3A). This suggests that 1E8 scFv binds to Aβ1–42 and inhibits fibril formation. Furthermore, a concentration response curve for 1E8 scFv (2.5–20 μM) with Aβ1–42 showed that after 24 h 1E8 scFv reduced Aβ1–42 ThT fluorescence in a concentration-related manner (Fig. 3B), for example, at low concentration (2.5 μM) 1E8 scFv decreased Aβ1–42 ThT fluorescence by ∼20% (Fig. 3B).\", \"Figure 3\", \"After 72 h, the sample containing Aβ1–42 alone exhibited multiple fibril formation (Fig. 3C). However, when Aβ1–42 was incubated with 1E8 scFv (20 μM), only small aggregates (consistent with the ThT background) but no visible Aβ1–42 fibrils were observed (Fig. 3C).\",  \"The 1E8 scFv significantly reduced the ability of Aβ1–42 to aggregate and form fibrils in vitro; however, consistent with previous studies investigating antibodies that target the central region of Aβ, it did not disassociate pre-formed Aβ aggregates (Bard et al., 2003).\",",
    "Curator Statement": false
  },
  "AMGAB0617": {
    "Interaction ID": "AMGAB0617",
    "Antibody ID": "ABID0446",
    "Antibody name": "1E8 scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/protein/gzt025",
    "PMID": 23766374.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro,",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"The 1E8 scFv significantly reduced the ability of Aβ1–42 to aggregate and form fibrils in vitro; however, consistent with previous studies investigating antibodies that target the central region of Aβ, it did not disassociate pre-formed Aβ aggregates (Bard et al., 2003).\",",
    "Curator Statement": false
  },
  "AMGAB0618": {
    "Interaction ID": "AMGAB0618",
    "Antibody ID": "ABID0446",
    "Antibody name": "1E8 scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1093/protein/gzt025",
    "PMID": 23766374.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro,",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In a further series of experiments, 1E8 scFv was tested for its ability to disaggregate already preformed Aβ1–42 fibrils, with ThT fluorescence of Aβ1–42 fibrils measured in the presence and absence of 1E8 scFv at different time points (Fig. 4). Preformed Aβ1–42 fibrils alone did not exhibit a change in ThT fluorescence over the 24 h period suggesting that the maximum ThT fluorescence had been reached (Fig. 4). The addition of 1E8 scFv (20 μM) to preformed Aβ1–42 fibrils did not reduce ThT fluorescence (Fig. 4), leading to the conclusion that while effective in preventing fibril formation, the 1E8 scFv was unable to disaggregate existing fibrils.\", \"Figure 4\", \"The 1E8 scFv significantly reduced the ability of Aβ1–42 to aggregate and form fibrils in vitro; however, consistent with previous studies investigating antibodies that target the central region of Aβ, it did not disassociate pre-formed Aβ aggregates (Bard et al., 2003).\",",
    "Curator Statement": "No effect on dissagregating preformed fibrils."
  },
  "AMGAB0619": {
    "Interaction ID": "AMGAB0619",
    "Antibody ID": "ABID0126",
    "Antibody name": "Nbα-syn01",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1111/febs.16376",
    "PMID": 35090199.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro,",
    "Experimental method(s)": "TEM image in presence/absence of the antibody, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Novel engineered nanobodies specific for N‐terminal region of alpha‐synuclein recognize Lewy‐body pathology and inhibit in‐vitro seeded aggregation and toxicity\", \"Nbα‐syn01 and BivNbα‐syn01 were also able to inhibit α‐syn‐seeded aggregation in vitro and reduced α‐syn‐seeded aggregation and toxicity in cells showing their potential to reduce α‐syn pathology.\", \"Furthermore, the two nanobody formats were able to block α‐syn aggregation in vitro and α‐syn aggregates‐induced toxicity in cells.\", \"Nbα‐syn01 and BivNbα‐syn01 significantly inhibited α‐syn monomers seeded‐aggregation at concentrations of 8 and 2 μm respectively with P‐values = < 0.05 as denoted by the lower Th‐S counts (Fig. 5A).\", \"Figure 5\", \"Transmission electron microscopy images from the samples further confirmed the efficiency of the Nbs in inhibiting α‐syn seed‐induced aggregation (Fig. 5B).\", \"Nbα‐syn01 and BivNbα‐syn01 inhibit in‐vitro seeded aggregation and toxicity of α‐syn\",\"Nbα‐syn01 and its bivalent formats were not only able to inhibit α‐syn‐seeded aggregation in vitro but also reduced α‐syn‐ seeded aggregation and toxicity in cells.\", \"We report the generation of a nanobody, Nbα‐syn01, and its engineered bivalent form, BivNbα‐syn01, that targets an important N‐terminal region of α‐syn. They recognize ɑ‐syn fibrils with higher affinities and inhibit aggregation and rescue cellular toxicity in vitro.\",",
    "Curator Statement": false
  },
  "AMGAB0620": {
    "Interaction ID": "AMGAB0620",
    "Antibody ID": "ABID0442",
    "Antibody name": "BivNbα-syn01",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1111/febs.16376",
    "PMID": 35090199.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Novel engineered nanobodies specific for N‐terminal region of alpha‐synuclein recognize Lewy‐body pathology and inhibit in‐vitro seeded aggregation and toxicity\", \"Nbα‐syn01 and BivNbα‐syn01 were also able to inhibit α‐syn‐seeded aggregation in vitro and reduced α‐syn‐seeded aggregation and toxicity in cells showing their potential to reduce α‐syn pathology.\", \"Furthermore, the two nanobody formats were able to block α‐syn aggregation in vitro and α‐syn aggregates‐induced toxicity in cells.\", \"Nbα‐syn01 and BivNbα‐syn01 significantly inhibited α‐syn monomers seeded‐aggregation at concentrations of 8 and 2 μm respectively with P‐values = < 0.05 as denoted by the lower Th‐S counts (Fig. 5A).\", \"Figure 5\", \"Transmission electron microscopy images from the samples further confirmed the efficiency of the Nbs in inhibiting α‐syn seed‐induced aggregation (Fig. 5B).\",\"Nbα‐syn01 and BivNbα‐syn01 inhibit in‐vitro seeded aggregation and toxicity of α‐syn\",\"Nbα‐syn01 and its bivalent formats were not only able to inhibit α‐syn‐seeded aggregation in vitro but also reduced α‐syn‐ seeded aggregation and toxicity in cells.\", \"We report the generation of a nanobody, Nbα‐syn01, and its engineered bivalent form, BivNbα‐syn01, that targets an important N‐terminal region of α‐syn. They recognize ɑ‐syn fibrils with higher affinities and inhibit aggregation and rescue cellular toxicity in vitro.\",",
    "Curator Statement": false
  },
  "AMGAB0621": {
    "Interaction ID": "AMGAB0621",
    "Antibody ID": "ABID0255",
    "Antibody name": "VH1",
    "Amyloid ID": "AGAMYID0009",
    "Amyloid name": "Antibody light chain",
    "DOI": "10.1111/febs.17223",
    "PMID": 38982771.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody",
    "Amyloid species identified": "Protein monomers",
    "Antibody paratope, CDR, or Negative control": "Gln39, Lys43, Asp59, Tyr95, Tyr105, Lys106",
    "Quote of the interaction": "\"Using differential scanning fluorimetry and surface plasmon resonance, VH1 was characterised to bind and kinetically stabilise LCs. This improved stability corresponded to the inhibition of fibril formation of SMA, whereby even a 10 : 1 SMA : VH1 concentration reduced aggregation to baseline levels. Atomic resolution X-ray crystallographic data of the SMA : VH1 complex revealed binding in a 1 : 1 ratio, mimicking both the dimeric antigen binding site of the native Ig molecule and the native SMA homodimeric structure.\", \"VH1 inhibits SMA fibril formation\", \"SMA displayed a large increase in ThT fluorescence signal after day 12 which is accompanies by observation of fibrils by transmission electron microscopy (Fig. 4A–D and Fig. S1). However, in the presence of VH1 at 1 : 1, 2 : 1 and 10 : 1 SMA : VH1 ratios no increase in fluorescence was observed suggesting a reduction in fibril formation (Fig. 4A–C), confirmed by electron microscopy (Fig. 4E–G). \", \"Figure 4\", \"Inhibition of SMA amyloid formation by VH1 presence.\", \"The inhibition of amyloid formation by stabilisation of the LC monomer, as described for SMA here, exhibits promise as a potential therapeutic mechanism.\", \"We showed that sub-stoichiometric concentrations of VH1 were sufficient to reduce LC aggregation. This suggests that it may be sufficient to remove a subspecies of LCs that are prone to enhancing seeding or elongation of LC fibrils in order to prevent fibril formation. VH1 may also be able to bind to hydrophobic surfaces on LC oligomers and block their maturation into fibrils.\", \" Furthermore, VH1 presence prevented fibril formation of the amyloidogenic LC SMA even at 10 : 1 LC excess.\"",
    "Curator Statement": false
  },
  "AMGAB0622": {
    "Interaction ID": "AMGAB0622",
    "Antibody ID": "ABID0244",
    "Antibody name": "4A8.E11",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1111/jcmm.14119",
    "PMID": 30663210.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The results indicate a concentration‐dependent inhibitory effect of the 4A8.E11, 4B1.H9, 3F2.E10, and 5C9.A2 antibodies on the aggregation of hIAPP (Figure 3A‐D) or Aβ42 monomers (Figure 3E‐H), compared with the negative control IgG 1D4 antibody (Figure S5).\", \"Figure 3\", \"When the data were plotted together, it appeared that the antibodies have a comparable inhibitory effect on the two amyloid proteins (Figure 3I‐L), except for 3F2.E10 that acts more potently on Aβ42 aggregation (Figure 3K).\", \"mAbs inhibit hIAPP and Aβ42 aggregation. The mAbs‐mediated inhibition of hIAPP and Aβ42 aggregation was monitored by the ThT assay.\", \"I‐L) Data shown in A‐H are plotted together for direct comparison of the inhibition exerted by I) 4A8.E11; J) 4B1.H9; K) 3F2.E10 and L) 5C9.A2 on the aggregation of hIAPP (10 µmol/L, black) and Aβ42 (10 µmol/L, red). \", \"The ThT data indicate that these mAbs inhibit aggregation of hIAPP and Aβ42. \", \"These anti‐protofibril antibodies (a) detect specific structural elements from at least two different amyloid sources, (b) capture soluble protofibrils in solution, (c) disrupt normal aggregation kinetics, and (d) reveal valuable insight into to the localization of protofibrils in tissues of either models of disease or that of tissue from humans who were afflicted with disease.\",",
    "Curator Statement": false
  },
  "AMGAB0623": {
    "Interaction ID": "AMGAB0623",
    "Antibody ID": "ABID0244",
    "Antibody name": "4A8.E11",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1111/jcmm.14119",
    "PMID": 30663210.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The results indicate a concentration‐dependent inhibitory effect of the 4A8.E11, 4B1.H9, 3F2.E10, and 5C9.A2 antibodies on the aggregation of hIAPP (Figure 3A‐D) or Aβ42 monomers (Figure 3E‐H), compared with the negative control IgG 1D4 antibody (Figure S5).\", \"Figure 3\", \"When the data were plotted together, it appeared that the antibodies have a comparable inhibitory effect on the two amyloid proteins (Figure 3I‐L), except for 3F2.E10 that acts more potently on Aβ42 aggregation (Figure 3K).\", \"mAbs inhibit hIAPP and Aβ42 aggregation. The mAbs‐mediated inhibition of hIAPP and Aβ42 aggregation was monitored by the ThT assay.\", \"I‐L) Data shown in A‐H are plotted together for direct comparison of the inhibition exerted by I) 4A8.E11; J) 4B1.H9; K) 3F2.E10 and L) 5C9.A2 on the aggregation of hIAPP (10 µmol/L, black) and Aβ42 (10 µmol/L, red). \", \"The ThT data indicate that these mAbs inhibit aggregation of hIAPP and Aβ42. \", \"These anti‐protofibril antibodies (a) detect specific structural elements from at least two different amyloid sources, (b) capture soluble protofibrils in solution, (c) disrupt normal aggregation kinetics, and (d) reveal valuable insight into to the localization of protofibrils in tissues of either models of disease or that of tissue from humans who were afflicted with disease.\",",
    "Curator Statement": false
  },
  "AMGAB0624": {
    "Interaction ID": "AMGAB0624",
    "Antibody ID": "ABID0245",
    "Antibody name": "4B1.H9",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1111/jcmm.14119",
    "PMID": 30663210.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The results indicate a concentration‐dependent inhibitory effect of the 4A8.E11, 4B1.H9, 3F2.E10, and 5C9.A2 antibodies on the aggregation of hIAPP (Figure 3A‐D) or Aβ42 monomers (Figure 3E‐H), compared with the negative control IgG 1D4 antibody (Figure S5).\", \"Figure 3\", \"When the data were plotted together, it appeared that the antibodies have a comparable inhibitory effect on the two amyloid proteins (Figure 3I‐L), except for 3F2.E10 that acts more potently on Aβ42 aggregation (Figure 3K).\", \"mAbs inhibit hIAPP and Aβ42 aggregation. The mAbs‐mediated inhibition of hIAPP and Aβ42 aggregation was monitored by the ThT assay.\", \"I‐L) Data shown in A‐H are plotted together for direct comparison of the inhibition exerted by I) 4A8.E11; J) 4B1.H9; K) 3F2.E10 and L) 5C9.A2 on the aggregation of hIAPP (10 µmol/L, black) and Aβ42 (10 µmol/L, red). \", \"The ThT data indicate that these mAbs inhibit aggregation of hIAPP and Aβ42. \", \"These anti‐protofibril antibodies (a) detect specific structural elements from at least two different amyloid sources, (b) capture soluble protofibrils in solution, (c) disrupt normal aggregation kinetics, and (d) reveal valuable insight into to the localization of protofibrils in tissues of either models of disease or that of tissue from humans who were afflicted with disease.\",",
    "Curator Statement": false
  },
  "AMGAB0625": {
    "Interaction ID": "AMGAB0625",
    "Antibody ID": "ABID0245",
    "Antibody name": "4B1.H9",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1111/jcmm.14119",
    "PMID": 30663210.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The results indicate a concentration‐dependent inhibitory effect of the 4A8.E11, 4B1.H9, 3F2.E10, and 5C9.A2 antibodies on the aggregation of hIAPP (Figure 3A‐D) or Aβ42 monomers (Figure 3E‐H), compared with the negative control IgG 1D4 antibody (Figure S5).\", \"Figure 3\", \"When the data were plotted together, it appeared that the antibodies have a comparable inhibitory effect on the two amyloid proteins (Figure 3I‐L), except for 3F2.E10 that acts more potently on Aβ42 aggregation (Figure 3K).\", \"mAbs inhibit hIAPP and Aβ42 aggregation. The mAbs‐mediated inhibition of hIAPP and Aβ42 aggregation was monitored by the ThT assay.\", \"I‐L) Data shown in A‐H are plotted together for direct comparison of the inhibition exerted by I) 4A8.E11; J) 4B1.H9; K) 3F2.E10 and L) 5C9.A2 on the aggregation of hIAPP (10 µmol/L, black) and Aβ42 (10 µmol/L, red). \", \"The ThT data indicate that these mAbs inhibit aggregation of hIAPP and Aβ42. \", \"These anti‐protofibril antibodies (a) detect specific structural elements from at least two different amyloid sources, (b) capture soluble protofibrils in solution, (c) disrupt normal aggregation kinetics, and (d) reveal valuable insight into to the localization of protofibrils in tissues of either models of disease or that of tissue from humans who were afflicted with disease.\",",
    "Curator Statement": false
  },
  "AMGAB0626": {
    "Interaction ID": "AMGAB0626",
    "Antibody ID": "ABID0246",
    "Antibody name": "3F2.E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1111/jcmm.14119",
    "PMID": 30663210.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The results indicate a concentration‐dependent inhibitory effect of the 4A8.E11, 4B1.H9, 3F2.E10, and 5C9.A2 antibodies on the aggregation of hIAPP (Figure 3A‐D) or Aβ42 monomers (Figure 3E‐H), compared with the negative control IgG 1D4 antibody (Figure S5).\", \"Figure 3\", \"When the data were plotted together, it appeared that the antibodies have a comparable inhibitory effect on the two amyloid proteins (Figure 3I‐L), except for 3F2.E10 that acts more potently on Aβ42 aggregation (Figure 3K).\", \"mAbs inhibit hIAPP and Aβ42 aggregation. The mAbs‐mediated inhibition of hIAPP and Aβ42 aggregation was monitored by the ThT assay.\", \"I‐L) Data shown in A‐H are plotted together for direct comparison of the inhibition exerted by I) 4A8.E11; J) 4B1.H9; K) 3F2.E10 and L) 5C9.A2 on the aggregation of hIAPP (10 µmol/L, black) and Aβ42 (10 µmol/L, red). \", \"The ThT data indicate that these mAbs inhibit aggregation of hIAPP and Aβ42. \", \"These anti‐protofibril antibodies (a) detect specific structural elements from at least two different amyloid sources, (b) capture soluble protofibrils in solution, (c) disrupt normal aggregation kinetics, and (d) reveal valuable insight into to the localization of protofibrils in tissues of either models of disease or that of tissue from humans who were afflicted with disease.\",",
    "Curator Statement": false
  },
  "AMGAB0627": {
    "Interaction ID": "AMGAB0627",
    "Antibody ID": "ABID0246",
    "Antibody name": "3F2.E10",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1111/jcmm.14119",
    "PMID": 30663210.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The results indicate a concentration‐dependent inhibitory effect of the 4A8.E11, 4B1.H9, 3F2.E10, and 5C9.A2 antibodies on the aggregation of hIAPP (Figure 3A‐D) or Aβ42 monomers (Figure 3E‐H), compared with the negative control IgG 1D4 antibody (Figure S5).\", \"Figure 3\", \"When the data were plotted together, it appeared that the antibodies have a comparable inhibitory effect on the two amyloid proteins (Figure 3I‐L), except for 3F2.E10 that acts more potently on Aβ42 aggregation (Figure 3K).\", \"mAbs inhibit hIAPP and Aβ42 aggregation. The mAbs‐mediated inhibition of hIAPP and Aβ42 aggregation was monitored by the ThT assay.\", \"I‐L) Data shown in A‐H are plotted together for direct comparison of the inhibition exerted by I) 4A8.E11; J) 4B1.H9; K) 3F2.E10 and L) 5C9.A2 on the aggregation of hIAPP (10 µmol/L, black) and Aβ42 (10 µmol/L, red). \", \"The ThT data indicate that these mAbs inhibit aggregation of hIAPP and Aβ42. \", \"These anti‐protofibril antibodies (a) detect specific structural elements from at least two different amyloid sources, (b) capture soluble protofibrils in solution, (c) disrupt normal aggregation kinetics, and (d) reveal valuable insight into to the localization of protofibrils in tissues of either models of disease or that of tissue from humans who were afflicted with disease.\",",
    "Curator Statement": false
  },
  "AMGAB0628": {
    "Interaction ID": "AMGAB0628",
    "Antibody ID": "ABID0247",
    "Antibody name": "5C9.A2",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1111/jcmm.14119",
    "PMID": 30663210.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The results indicate a concentration‐dependent inhibitory effect of the 4A8.E11, 4B1.H9, 3F2.E10, and 5C9.A2 antibodies on the aggregation of hIAPP (Figure 3A‐D) or Aβ42 monomers (Figure 3E‐H), compared with the negative control IgG 1D4 antibody (Figure S5).\", \"Figure 3\", \"When the data were plotted together, it appeared that the antibodies have a comparable inhibitory effect on the two amyloid proteins (Figure 3I‐L), except for 3F2.E10 that acts more potently on Aβ42 aggregation (Figure 3K).\", \"mAbs inhibit hIAPP and Aβ42 aggregation. The mAbs‐mediated inhibition of hIAPP and Aβ42 aggregation was monitored by the ThT assay.\", \"I‐L) Data shown in A‐H are plotted together for direct comparison of the inhibition exerted by I) 4A8.E11; J) 4B1.H9; K) 3F2.E10 and L) 5C9.A2 on the aggregation of hIAPP (10 µmol/L, black) and Aβ42 (10 µmol/L, red). \", \"The ThT data indicate that these mAbs inhibit aggregation of hIAPP and Aβ42. \", \"These anti‐protofibril antibodies (a) detect specific structural elements from at least two different amyloid sources, (b) capture soluble protofibrils in solution, (c) disrupt normal aggregation kinetics, and (d) reveal valuable insight into to the localization of protofibrils in tissues of either models of disease or that of tissue from humans who were afflicted with disease.\",",
    "Curator Statement": false
  },
  "AMGAB0629": {
    "Interaction ID": "AMGAB0629",
    "Antibody ID": "ABID0247",
    "Antibody name": "5C9.A2",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1111/jcmm.14119",
    "PMID": 30663210.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The results indicate a concentration‐dependent inhibitory effect of the 4A8.E11, 4B1.H9, 3F2.E10, and 5C9.A2 antibodies on the aggregation of hIAPP (Figure 3A‐D) or Aβ42 monomers (Figure 3E‐H), compared with the negative control IgG 1D4 antibody (Figure S5).\", \"Figure 3\", \"When the data were plotted together, it appeared that the antibodies have a comparable inhibitory effect on the two amyloid proteins (Figure 3I‐L), except for 3F2.E10 that acts more potently on Aβ42 aggregation (Figure 3K).\", \"mAbs inhibit hIAPP and Aβ42 aggregation. The mAbs‐mediated inhibition of hIAPP and Aβ42 aggregation was monitored by the ThT assay.\", \"I‐L) Data shown in A‐H are plotted together for direct comparison of the inhibition exerted by I) 4A8.E11; J) 4B1.H9; K) 3F2.E10 and L) 5C9.A2 on the aggregation of hIAPP (10 µmol/L, black) and Aβ42 (10 µmol/L, red). \", \"The ThT data indicate that these mAbs inhibit aggregation of hIAPP and Aβ42. \", \"These anti‐protofibril antibodies (a) detect specific structural elements from at least two different amyloid sources, (b) capture soluble protofibrils in solution, (c) disrupt normal aggregation kinetics, and (d) reveal valuable insight into to the localization of protofibrils in tissues of either models of disease or that of tissue from humans who were afflicted with disease.\",",
    "Curator Statement": false
  },
  "AMGAB0630": {
    "Interaction ID": "AMGAB0630",
    "Antibody ID": "ABID0248",
    "Antibody name": "1D4",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1111/jcmm.14119",
    "PMID": 30663210.0,
    "Impact of the antibody on amyloid formation": "No effect, Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"The results indicate a concentration‐dependent inhibitory effect of the 4A8.E11, 4B1.H9, 3F2.E10, and 5C9.A2 antibodies on the aggregation of hIAPP (Figure 3A‐D) or Aβ42 monomers (Figure 3E‐H), compared with the negative control IgG 1D4 antibody (Figure S5).\", \"Figure S5\",",
    "Curator Statement": false
  },
  "AMGAB0631": {
    "Interaction ID": "AMGAB0631",
    "Antibody ID": "ABID0248",
    "Antibody name": "1D4",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.1111/jcmm.14119",
    "PMID": 30663210.0,
    "Impact of the antibody on amyloid formation": "No effect, Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"The results indicate a concentration‐dependent inhibitory effect of the 4A8.E11, 4B1.H9, 3F2.E10, and 5C9.A2 antibodies on the aggregation of hIAPP (Figure 3A‐D) or Aβ42 monomers (Figure 3E‐H), compared with the negative control IgG 1D4 antibody (Figure S5).\", \"Figure S5\",",
    "Curator Statement": false
  },
  "AMGAB0632": {
    "Interaction ID": "AMGAB0632",
    "Antibody ID": "ABID0324",
    "Antibody name": "cAb2789",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1111/jcmm.15511",
    "PMID": 32610368.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Total aggregation (final point)",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We also demonstrate the secreted anti‐β‐amyloid Fab protein functions in β‐amyloid aggregate solubilization.\", \"Figure 4\", \"A significant reduction in aggregates was observed after incubation with either an anti‐β‐amyloid Fab or concentrated medium from transfected cells.\", \"Function of the secreted anti‐β‐amyloid Fab was demonstrated using an aggregate solubilization assay.\", \"The purpose of the present study was the demonstration that early EPCs transfected ex vivo with an Fab‐encoding plasmid would express and secrete functional Fabs that could solubilize β‐amyloid aggregates. \",",
    "Curator Statement": false
  },
  "AMGAB0633": {
    "Interaction ID": "AMGAB0633",
    "Antibody ID": "ABID0185",
    "Antibody name": "204",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1111/jnc.12305",
    "PMID": 23672786.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other: ELISA",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Consistent with a decrease in amyloid plaques immunostaining, we observed a significant reduction in brain soluble and insoluble Aβ40 and Aβ42 levels (Fig. 3) in all three of the oligomer-specific antibody vaccinated groups.\", \"Figure 3\", \"\"Image analysis of sections from multiple animals demonstrated that Aβ deposits in A11, 204, and 205 vaccinated mice were decreased significantly as compared with control vaccinated mice. Fig. 2b, shows that all the immunized groups displayed a significant reduction in Aβ plaque load in hippocampus as compared to the respective controls (***p < 0.001, **p < 0.01). These results indicate that administration of oligomer specific antibodies lower the amount of plaque deposits, even in mice with extensive plaque and tangle neuropathology.\", \"Figure 2\", \"Consistent with a decrease in amyloid plaques immunostaining, we observed a significant reduction in brain soluble and insoluble Aβ40 and Aβ42 levels (Fig. 3) in all three of the oligomer-specific antibody vaccinated groups.\", \"Figure 3\", \" In contrast, our data indicate that the formation of amyloid deposits can be reversed with passive immunization using pre-fibrillar oligomer-specific antibodies. These antibodies are specific for oligomers that are immunologically distinct from fibrils and do not bind plaques (Kayed et al. 2010). We observed a significant reduction in both soluble and insoluble levels of Aβ40 and 42. This reduction may be affected by the opsonization of antibody-bound oligomeric Aβ42 or 40 by microglia or infiltrated macrophages.\", \"Our findings demonstrated that conformation-dependent antibodies efficiently clear amyloid plaque, tau pathology and improve cognition, which highlight that these oligomer specific antibodies have a therapeutic potential to prevent and treat Alzheimer’s disease.\",",
    "Curator Statement": false
  },
  "AMGAB0634": {
    "Interaction ID": "AMGAB0634",
    "Antibody ID": "ABID0185",
    "Antibody name": "204",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1111/jnc.12305",
    "PMID": 23672786.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other: ELISA",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Image analysis of sections from multiple animals demonstrated that Aβ deposits in A11, 204, and 205 vaccinated mice were decreased significantly as compared with control vaccinated mice. Fig. 2b, shows that all the immunized groups displayed a significant reduction in Aβ plaque load in hippocampus as compared to the respective controls (***p < 0.001, **p < 0.01). These results indicate that administration of oligomer specific antibodies lower the amount of plaque deposits, even in mice with extensive plaque and tangle neuropathology.\", \"Figure 2\", \"Consistent with a decrease in amyloid plaques immunostaining, we observed a significant reduction in brain soluble and insoluble Aβ40 and Aβ42 levels (Fig. 3) in all three of the oligomer-specific antibody vaccinated groups.\", \"Figure 3\", \" In contrast, our data indicate that the formation of amyloid deposits can be reversed with passive immunization using pre-fibrillar oligomer-specific antibodies. These antibodies are specific for oligomers that are immunologically distinct from fibrils and do not bind plaques (Kayed et al. 2010). We observed a significant reduction in both soluble and insoluble levels of Aβ40 and 42. This reduction may be affected by the opsonization of antibody-bound oligomeric Aβ42 or 40 by microglia or infiltrated macrophages.\", \"Our findings demonstrated that conformation-dependent antibodies efficiently clear amyloid plaque, tau pathology and improve cognition, which highlight that these oligomer specific antibodies have a therapeutic potential to prevent and treat Alzheimer’s disease.\"",
    "Curator Statement": false
  },
  "AMGAB0635": {
    "Interaction ID": "AMGAB0635",
    "Antibody ID": "ABID0185",
    "Antibody name": "204",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Tau",
    "DOI": "10.1111/jnc.12305",
    "PMID": 23672786.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"After 5 weeks of vaccination we observed statistically significant reduction in hyperphosphorylated tau aggregates as compared with control IgG vaccinated mice (Fig. 4b, **p < 0.01).\", \"Figure 4\", \"Passive vaccination with oligomer antibodies led to a reduction in total tau levels: (a) Representative photomicrographs of sections from brains (hippocampus) of 3xTg-Alzheimer’s disease mice after 5 weeks of vaccination (Control antibody, A11 antibody, 204 antibody, and 205 antibody vaccinated). Immunostaining was done with HT7 (which recognizes the total tau). Immunohistochemical analysis of oligomer antibody vaccinated mice showed a prominent reduction of total tau in the hippocampus (scale bar = 100 μm) as compared with control antibody vaccinated mice (b). The reduction was statistically significant **p < 0.01.\", \" These data are consistent with our results showing that passive immunization with anti-oligomer antibodies efficiently clears hyperphosphorylated tau. \", \"Our findings demonstrated that conformation-dependent antibodies efficiently clear amyloid plaque, tau pathology and improve cognition, which highlight that these oligomer specific antibodies have a therapeutic potential to prevent and treat Alzheimer’s disease.\",",
    "Curator Statement": "Authors speculate that Tau aggregates are diminished as a consequence of antibody-mediated Aβ-amyloid clearance."
  },
  "AMGAB0636": {
    "Interaction ID": "AMGAB0636",
    "Antibody ID": "ABID0186",
    "Antibody name": "205",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1111/jnc.12305",
    "PMID": 23672786.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other: ELISA",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Consistent with a decrease in amyloid plaques immunostaining, we observed a significant reduction in brain soluble and insoluble Aβ40 and Aβ42 levels (Fig. 3) in all three of the oligomer-specific antibody vaccinated groups.\", \"Figure 3\", \"\"Image analysis of sections from multiple animals demonstrated that Aβ deposits in A11, 204, and 205 vaccinated mice were decreased significantly as compared with control vaccinated mice. Fig. 2b, shows that all the immunized groups displayed a significant reduction in Aβ plaque load in hippocampus as compared to the respective controls (***p < 0.001, **p < 0.01). These results indicate that administration of oligomer specific antibodies lower the amount of plaque deposits, even in mice with extensive plaque and tangle neuropathology.\", \"Figure 2\", \"Consistent with a decrease in amyloid plaques immunostaining, we observed a significant reduction in brain soluble and insoluble Aβ40 and Aβ42 levels (Fig. 3) in all three of the oligomer-specific antibody vaccinated groups.\", \"Figure 3\", \" In contrast, our data indicate that the formation of amyloid deposits can be reversed with passive immunization using pre-fibrillar oligomer-specific antibodies. These antibodies are specific for oligomers that are immunologically distinct from fibrils and do not bind plaques (Kayed et al. 2010). We observed a significant reduction in both soluble and insoluble levels of Aβ40 and 42. This reduction may be affected by the opsonization of antibody-bound oligomeric Aβ42 or 40 by microglia or infiltrated macrophages.\", \"Our findings demonstrated that conformation-dependent antibodies efficiently clear amyloid plaque, tau pathology and improve cognition, which highlight that these oligomer specific antibodies have a therapeutic potential to prevent and treat Alzheimer’s disease.\",",
    "Curator Statement": false
  },
  "AMGAB0637": {
    "Interaction ID": "AMGAB0637",
    "Antibody ID": "ABID0186",
    "Antibody name": "205",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1111/jnc.12305",
    "PMID": 23672786.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other: ELISA",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Image analysis of sections from multiple animals demonstrated that Aβ deposits in A11, 204, and 205 vaccinated mice were decreased significantly as compared with control vaccinated mice. Fig. 2b, shows that all the immunized groups displayed a significant reduction in Aβ plaque load in hippocampus as compared to the respective controls (***p < 0.001, **p < 0.01). These results indicate that administration of oligomer specific antibodies lower the amount of plaque deposits, even in mice with extensive plaque and tangle neuropathology.\", \"Figure 2\", \"Consistent with a decrease in amyloid plaques immunostaining, we observed a significant reduction in brain soluble and insoluble Aβ40 and Aβ42 levels (Fig. 3) in all three of the oligomer-specific antibody vaccinated groups.\", \"Figure 3\", \" In contrast, our data indicate that the formation of amyloid deposits can be reversed with passive immunization using pre-fibrillar oligomer-specific antibodies. These antibodies are specific for oligomers that are immunologically distinct from fibrils and do not bind plaques (Kayed et al. 2010). We observed a significant reduction in both soluble and insoluble levels of Aβ40 and 42. This reduction may be affected by the opsonization of antibody-bound oligomeric Aβ42 or 40 by microglia or infiltrated macrophages.\", \"Our findings demonstrated that conformation-dependent antibodies efficiently clear amyloid plaque, tau pathology and improve cognition, which highlight that these oligomer specific antibodies have a therapeutic potential to prevent and treat Alzheimer’s disease.\"",
    "Curator Statement": false
  },
  "AMGAB0638": {
    "Interaction ID": "AMGAB0638",
    "Antibody ID": "ABID0186",
    "Antibody name": "205",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Tau",
    "DOI": "10.1111/jnc.12305",
    "PMID": 23672786.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"After 5 weeks of vaccination we observed statistically significant reduction in hyperphosphorylated tau aggregates as compared with control IgG vaccinated mice (Fig. 4b, **p < 0.01).\", \"Figure 4\", \"Passive vaccination with oligomer antibodies led to a reduction in total tau levels: (a) Representative photomicrographs of sections from brains (hippocampus) of 3xTg-Alzheimer’s disease mice after 5 weeks of vaccination (Control antibody, A11 antibody, 204 antibody, and 205 antibody vaccinated). Immunostaining was done with HT7 (which recognizes the total tau). Immunohistochemical analysis of oligomer antibody vaccinated mice showed a prominent reduction of total tau in the hippocampus (scale bar = 100 μm) as compared with control antibody vaccinated mice (b). The reduction was statistically significant **p < 0.01.\", \" These data are consistent with our results showing that passive immunization with anti-oligomer antibodies efficiently clears hyperphosphorylated tau. \", \"Our findings demonstrated that conformation-dependent antibodies efficiently clear amyloid plaque, tau pathology and improve cognition, which highlight that these oligomer specific antibodies have a therapeutic potential to prevent and treat Alzheimer’s disease.\",",
    "Curator Statement": "Authors speculate that Tau aggregates are diminished as a consequence of antibody-mediated Aβ-amyloid clearance."
  },
  "AMGAB0639": {
    "Interaction ID": "AMGAB0639",
    "Antibody ID": "ABID0289",
    "Antibody name": "mAbSL 113",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1111/jnc.15817",
    "PMID": 37002186.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, ELISA",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"mAbSL 113 significantly inhibited Aβ42 monomer aggregation by a unique mechanism compared with the inhibition displayed by Aβ mAb 513.\", \"Aβ42 protofibril dynamics were also markedly altered in the presence of mAbSL 113, whereby insoluble complex formation and protofibril deposition were stimulated by the antibody at low substoichiometric molar ratios.\", \"Figure 5\", \"Aβ42 monomer aggregation in the absence of antibody yielded a t1/2 value of 3.8 h and a lag time (tlag) of 2.9 h (Figure 5a). The inclusion of mAbSL 113 at a sub-stoichiometric concentration had a striking and unique effect on Aβ42 monomer aggregation. Although the data could not be fit with a conventional equation, a nucleation and growth phase was observed that correlated temporally with aggregation in the absence of antibody (Figure 5a). However, the aggregation progress was significantly and rapidly suppressed and failed to yield any detectable aggregates over time. The effect of mAbSL 113 on Aβ42 monomer aggregation kinetics suggested that the antibody was binding to aggregates soon after nucleation, thus preventing further growth.\", \"In the presence of mAbSL 113 or Aβ mAb 513 at a 1:10 antibody:Aβ molar ratio, the Aβ42 protofibrils immediately formed a complex in solution that did not appear to alter the protofibril structure, but could be removed from the solution by centrifugation. Nearly 93% and 78% of the Aβ42 protofibrils were found in an insoluble complex within 30 min of incubation with mAbSL 113 or Aβ mAb 513, respectively. After 2–3 days incubation with both antibodies, 100% of the Aβ42 protofibrils were removed from the solution by centrifugation (Figure 6a, post-spin). In an extended time course of incubation, SEC-isolated Aβ42 protofibrils became less soluble over time (Figure 6b). However, inclusion of mAbSL 113 and Aβ mAb 513 1:20 antibody: protofibril ratio hastened this process. The lower stoichiometric ratio allowed observation of differing effects between the conformational-selective mAbSL 113 and the nonconformational-selective Aβ mAb 513 antibodies (Figure 6b, left panel). At early time points (0–6 days), mAbSL 113 was much more effective than Aβ mAb 513 at altering protofibril stability and triggering conversion to an insoluble complex. Even at this low antibody: protofibril ratio, mAbSL 113 rapidly caused deposition of Aβ42 protofibrils just 30 min after inclusion in the solution (Figure 6b, left panel). Further lowering of the antibody: protofibril ratio to 1:50 yielded a similar difference between the effects of the two antibodies, with mAbSL 113 still exerting a significant impact on protofibril dynamics (Figure 6b, right panel). The deposition time course with the inclusion of Aβ mAb 513 was closer to that of Aβ42 protofibrils alone.\", \"Figure 6\", \"The mAbSL antibodies were potent inhibitors of Aβ42 monomer aggregation and rapidly triggered Aβ42 protofibril deposition at sub-stoichiometric molar ratios.\", \"This level of potent Aβ42 monomer aggregation inhibition was observed by the protofibril-selective mAbSL 113 antibody. However, the pattern of inhibition by mAbSL 113 in Figure 5a was suggestive of a mechanism in which soluble Aβ42 protofibrils were formed, rapidly bound by antibody, and their further assembly was suppressed. \", \" In the case of mAbSL 113, the interaction significantly hastened the deposition of soluble, diffusible Aβ42 protofibrils by forming an insoluble complex. This occurred at very low antibody–protofibril molar ratios (1:50).\", \"A new class of monoclonal Aβ antibodies selectively targets and triggers deposition of Aβ protofibrils\".",
    "Curator Statement": false
  },
  "AMGAB0640": {
    "Interaction ID": "AMGAB0640",
    "Antibody ID": "ABID0290",
    "Antibody name": "mAb 513",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1111/jnc.15817",
    "PMID": 37002186.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, ELISA",
    "Amyloid species identified": "Protein monomer, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"mAbSL 113 significantly inhibited Aβ42 monomer aggregation by a unique mechanism compared with the inhibition displayed by Aβ mAb 513.\", \"Figure 5\", \"The impact of Aβ mAb 513 (1:10 antibody-Aβ ratio) on Aβ42 monomer aggregation kinetics was very different, in that nucleation and elongation were both inhibited through a more conventional mechanism. t1/2 increased from 2.2 to 3.8 h in the presence of antibody, and the tlag was extended from 1.1 to 2.8 h (Figure 5b). The maximum ThT fluorescence was significantly reduced from 5400 to 1200 in the presence of the Aβ mAb 513. The inhibitory effect of the non-conformation-selective mAb suggested a mechanism whereby Aβ42 monomers are immediately bound upon incubation, effectively lowering the Aβ42 concentration and lengthened the lag phase and maximum aggregation.\", \"For Aβ42 alone, values for t1/2 and tlag were 2.2 and 1.1 h. In the presence of Aβ mAb 513, values for t1/2 and tlag were 3.8 and 2.8 h.\", \"In the presence of mAbSL 113 or Aβ mAb 513 at a 1:10 antibody:Aβ molar ratio, the Aβ42 protofibrils immediately formed a complex in solution that did not appear to alter the protofibril structure, but could be removed from the solution by centrifugation. Nearly 93% and 78% of the Aβ42 protofibrils were found in an insoluble complex within 30 min of incubation with mAbSL 113 or Aβ mAb 513, respectively. After 2–3 days incubation with both antibodies, 100% of the Aβ42 protofibrils were removed from the solution by centrifugation (Figure 6a, post-spin). In an extended time course of incubation, SEC-isolated Aβ42 protofibrils became less soluble over time (Figure 6b). However, inclusion of mAbSL 113 and Aβ mAb 513 1:20 antibody: protofibril ratio hastened this process. The lower stoichiometric ratio allowed observation of differing effects between the conformational-selective mAbSL 113 and the nonconformational-selective Aβ mAb 513 antibodies (Figure 6b, left panel). At early time points (0–6 days), mAbSL 113 was much more effective than Aβ mAb 513 at altering protofibril stability and triggering conversion to an insoluble complex. Even at this low antibody: protofibril ratio, mAbSL 113 rapidly caused deposition of Aβ42 protofibrils just 30 min after inclusion in the solution (Figure 6b, left panel). Further lowering of the antibody: protofibril ratio to 1:50 yielded a similar difference between the effects of the two antibodies, with mAbSL 113 still exerting a significant impact on protofibril dynamics (Figure 6b, right panel). The deposition time course with the inclusion of Aβ mAb 513 was closer to that of Aβ42 protofibrils alone.\", \"Figure 6\", \"The inhibition displayed by non-conformation-selective Aβ mAb 513 was also potent, but suggestive of a more conventional mechanism of inhibition.\", \"A new class of monoclonal Aβ antibodies selectively targets and triggers deposition of Aβ protofibrils\",",
    "Curator Statement": false
  },
  "AMGAB0641": {
    "Interaction ID": "AMGAB0641",
    "Antibody ID": "ABID0513",
    "Antibody name": "DesAb3–9",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1126/sciadv.1700488",
    "PMID": 28691099.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\",  \" (B) Solutions containing 2 μM Aβ42 were incubated in the presence of increasing (blue to green) Aβ42 monomer equivalents of the DesAbs (serial dilutions starting from 1 μM DesAb concentration; see fig. S5); each antibody targets a specific epitope within the sequence of Aβ42 (Fig. 1) and inhibits the aggregation of the peptide in a characteristic manner.\", \"We observed a progressive reduction in the overall rate of aggregation with increasing concentrations of the DesAbs (Fig. 3B), which shows that all DesAbs designed to bind Aβ42 are effective in inhibiting its aggregation, even at substoichiometric concentrations (as low as 1:32 antibody–to–Aβ42 monomer ratios).\", \"By contrast, the antibody DesAb-F (Table 1), which showed a strong inhibitory effect on α-synuclein aggregation (38), does not have any detectable effect on the aggregation of Aβ42 (fig. S5). Because DesAb-F differs from the antibodies designed to target Aβ42 discussed here only in the sequence of the complementary peptide grafted in the CDR3 loop, these results indicate that the inhibitory effects observed on the aggregation of Aβ42 specifically originate from the computationally designed peptides (Fig. 3B).\", \"We have illustrated the efficacy of this approach by generating a pool of antibodies designed to scan the sequence of Aβ42 and then by using kinetic methods to test the ability of these antibodies to inhibit specific microscopic steps in Aβ42 aggregation. This analysis has revealed that all DesAbs have significant effects on Aβ42 aggregation in vitro, and it has allowed us to identify two antibodies that target, respectively, the primary and secondary nucleation of the aggregation process with high selectivity. We have then confirmed that these in vitro results are fully consistent with the effects of the two antibodies in vivo using a C. elegans model of Aβ42-mediated toxicity.\",",
    "Curator Statement": false
  },
  "AMGAB0642": {
    "Interaction ID": "AMGAB0642",
    "Antibody ID": "ABID0514",
    "Antibody name": "DesAb13–19",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1126/sciadv.1700488",
    "PMID": 28691099.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\",  \" (B) Solutions containing 2 μM Aβ42 were incubated in the presence of increasing (blue to green) Aβ42 monomer equivalents of the DesAbs (serial dilutions starting from 1 μM DesAb concentration; see fig. S5); each antibody targets a specific epitope within the sequence of Aβ42 (Fig. 1) and inhibits the aggregation of the peptide in a characteristic manner.\", \"We observed a progressive reduction in the overall rate of aggregation with increasing concentrations of the DesAbs (Fig. 3B), which shows that all DesAbs designed to bind Aβ42 are effective in inhibiting its aggregation, even at substoichiometric concentrations (as low as 1:32 antibody–to–Aβ42 monomer ratios).\", \"By contrast, the antibody DesAb-F (Table 1), which showed a strong inhibitory effect on α-synuclein aggregation (38), does not have any detectable effect on the aggregation of Aβ42 (fig. S5). Because DesAb-F differs from the antibodies designed to target Aβ42 discussed here only in the sequence of the complementary peptide grafted in the CDR3 loop, these results indicate that the inhibitory effects observed on the aggregation of Aβ42 specifically originate from the computationally designed peptides (Fig. 3B).\", \"We found that the antibodies with a strong effect on secondary nucleation were the most effective in inhibiting the formation of these oligomers. In particular, DesAb29–36, which predominantly affects secondary nucleation, was the antibody with the strongest effect by decreasing the number of oligomers by 97%. Strikingly, this decrease is larger than that (90%) caused by DesAb13–19, which has a much more pronounced effect on the overall aggregation process reported by the ThT measurements. By contrast, the decrease (36%) caused by DesAb36–42 is much lower than that of DesAb29–36, despite the fact that the overall unseeded aggregation curves look very similar for these two antibodies.\", \"We have illustrated the efficacy of this approach by generating a pool of antibodies designed to scan the sequence of Aβ42 and then by using kinetic methods to test the ability of these antibodies to inhibit specific microscopic steps in Aβ42 aggregation. This analysis has revealed that all DesAbs have significant effects on Aβ42 aggregation in vitro, and it has allowed us to identify two antibodies that target, respectively, the primary and secondary nucleation of the aggregation process with high selectivity. We have then confirmed that these in vitro results are fully consistent with the effects of the two antibodies in vivo using a C. elegans model of Aβ42-mediated toxicity.\",",
    "Curator Statement": false
  },
  "AMGAB0643": {
    "Interaction ID": "AMGAB0643",
    "Antibody ID": "ABID0515",
    "Antibody name": "DesAb18–25",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1126/sciadv.1700488",
    "PMID": 28691099.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We find that DesAb18–25 and DesAb29–36 are able to selectively inhibit the primary and the surface-catalyzed secondary nucleation of Aβ42, respectively, and to consistently suppress the Aβ42-mediated toxicity in a Caenorhabditis elegans model.\", \"Figure 5\",  \" (B) Solutions containing 2 μM Aβ42 were incubated in the presence of increasing (blue to green) Aβ42 monomer equivalents of the DesAbs (serial dilutions starting from 1 μM DesAb concentration; see fig. S5); each antibody targets a specific epitope within the sequence of Aβ42 (Fig. 1) and inhibits the aggregation of the peptide in a characteristic manner.\", \"We observed a progressive reduction in the overall rate of aggregation with increasing concentrations of the DesAbs (Fig. 3B), which shows that all DesAbs designed to bind Aβ42 are effective in inhibiting its aggregation, even at substoichiometric concentrations (as low as 1:32 antibody–to–Aβ42 monomer ratios).\", \"By contrast, the antibody DesAb-F (Table 1), which showed a strong inhibitory effect on α-synuclein aggregation (38), does not have any detectable effect on the aggregation of Aβ42 (fig. S5). Because DesAb-F differs from the antibodies designed to target Aβ42 discussed here only in the sequence of the complementary peptide grafted in the CDR3 loop, these results indicate that the inhibitory effects observed on the aggregation of Aβ42 specifically originate from the computationally designed peptides (Fig. 3B).\", \"We have illustrated the efficacy of this approach by generating a pool of antibodies designed to scan the sequence of Aβ42 and then by using kinetic methods to test the ability of these antibodies to inhibit specific microscopic steps in Aβ42 aggregation. This analysis has revealed that all DesAbs have significant effects on Aβ42 aggregation in vitro, and it has allowed us to identify two antibodies that target, respectively, the primary and secondary nucleation of the aggregation process with high selectivity. We have then confirmed that these in vitro results are fully consistent with the effects of the two antibodies in vivo using a C. elegans model of Aβ42-mediated toxicity.\",",
    "Curator Statement": false
  },
  "AMGAB0644": {
    "Interaction ID": "AMGAB0644",
    "Antibody ID": "ABID0515",
    "Antibody name": "DesAb18–25",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1126/sciadv.1700488",
    "PMID": 28691099.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S12\", \"Finally, fluorescence imaging using the amyloid-specific probe NIAD-4 (see Materials and Methods) shows that the treatments using the DesAbs have a direct effect on the amount of Aβ42 aggregates in the worms (fig. S12).\",",
    "Curator Statement": false
  },
  "AMGAB0645": {
    "Interaction ID": "AMGAB0645",
    "Antibody ID": "ABID0516",
    "Antibody name": "DesAb29–36",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1126/sciadv.1700488",
    "PMID": 28691099.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro,",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We find that DesAb18–25 and DesAb29–36 are able to selectively inhibit the primary and the surface-catalyzed secondary nucleation of Aβ42, respectively, and to consistently suppress the Aβ42-mediated toxicity in a Caenorhabditis elegans model.\", \"Figure 5\",  \" (B) Solutions containing 2 μM Aβ42 were incubated in the presence of increasing (blue to green) Aβ42 monomer equivalents of the DesAbs (serial dilutions starting from 1 μM DesAb concentration; see fig. S5); each antibody targets a specific epitope within the sequence of Aβ42 (Fig. 1) and inhibits the aggregation of the peptide in a characteristic manner.\", \"We observed a progressive reduction in the overall rate of aggregation with increasing concentrations of the DesAbs (Fig. 3B), which shows that all DesAbs designed to bind Aβ42 are effective in inhibiting its aggregation, even at substoichiometric concentrations (as low as 1:32 antibody–to–Aβ42 monomer ratios).\", \"By contrast, the antibody DesAb-F (Table 1), which showed a strong inhibitory effect on α-synuclein aggregation (38), does not have any detectable effect on the aggregation of Aβ42 (fig. S5). Because DesAb-F differs from the antibodies designed to target Aβ42 discussed here only in the sequence of the complementary peptide grafted in the CDR3 loop, these results indicate that the inhibitory effects observed on the aggregation of Aβ42 specifically originate from the computationally designed peptides (Fig. 3B).\",\"We found that the antibodies with a strong effect on secondary nucleation were the most effective in inhibiting the formation of these oligomers. In particular, DesAb29–36, which predominantly affects secondary nucleation, was the antibody with the strongest effect by decreasing the number of oligomers by 97%. Strikingly, this decrease is larger than that (90%) caused by DesAb13–19, which has a much more pronounced effect on the overall aggregation process reported by the ThT measurements. By contrast, the decrease (36%) caused by DesAb36–42 is much lower than that of DesAb29–36, despite the fact that the overall unseeded aggregation curves look very similar for these two antibodies.\",  \"We have illustrated the efficacy of this approach by generating a pool of antibodies designed to scan the sequence of Aβ42 and then by using kinetic methods to test the ability of these antibodies to inhibit specific microscopic steps in Aβ42 aggregation. This analysis has revealed that all DesAbs have significant effects on Aβ42 aggregation in vitro, and it has allowed us to identify two antibodies that target, respectively, the primary and secondary nucleation of the aggregation process with high selectivity. We have then confirmed that these in vitro results are fully consistent with the effects of the two antibodies in vivo using a C. elegans model of Aβ42-mediated toxicity.\",",
    "Curator Statement": false
  },
  "AMGAB0646": {
    "Interaction ID": "AMGAB0646",
    "Antibody ID": "ABID0516",
    "Antibody name": "DesAb29–36",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1126/sciadv.1700488",
    "PMID": 28691099.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Supplementary Figure S12\", \"Finally, fluorescence imaging using the amyloid-specific probe NIAD-4 (see Materials and Methods) shows that the treatments using the DesAbs have a direct effect on the amount of Aβ42 aggregates in the worms (fig. S12).\",",
    "Curator Statement": false
  },
  "AMGAB0647": {
    "Interaction ID": "AMGAB0647",
    "Antibody ID": "ABID0517",
    "Antibody name": "DesAb36–42",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1126/sciadv.1700488",
    "PMID": 28691099.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\",  \" (B) Solutions containing 2 μM Aβ42 were incubated in the presence of increasing (blue to green) Aβ42 monomer equivalents of the DesAbs (serial dilutions starting from 1 μM DesAb concentration; see fig. S5); each antibody targets a specific epitope within the sequence of Aβ42 (Fig. 1) and inhibits the aggregation of the peptide in a characteristic manner.\", \"We observed a progressive reduction in the overall rate of aggregation with increasing concentrations of the DesAbs (Fig. 3B), which shows that all DesAbs designed to bind Aβ42 are effective in inhibiting its aggregation, even at substoichiometric concentrations (as low as 1:32 antibody–to–Aβ42 monomer ratios).\", \"By contrast, the antibody DesAb-F (Table 1), which showed a strong inhibitory effect on α-synuclein aggregation (38), does not have any detectable effect on the aggregation of Aβ42 (fig. S5). Because DesAb-F differs from the antibodies designed to target Aβ42 discussed here only in the sequence of the complementary peptide grafted in the CDR3 loop, these results indicate that the inhibitory effects observed on the aggregation of Aβ42 specifically originate from the computationally designed peptides (Fig. 3B).\",\"We found that the antibodies with a strong effect on secondary nucleation were the most effective in inhibiting the formation of these oligomers. In particular, DesAb29–36, which predominantly affects secondary nucleation, was the antibody with the strongest effect by decreasing the number of oligomers by 97%. Strikingly, this decrease is larger than that (90%) caused by DesAb13–19, which has a much more pronounced effect on the overall aggregation process reported by the ThT measurements. By contrast, the decrease (36%) caused by DesAb36–42 is much lower than that of DesAb29–36, despite the fact that the overall unseeded aggregation curves look very similar for these two antibodies.\", \"We have illustrated the efficacy of this approach by generating a pool of antibodies designed to scan the sequence of Aβ42 and then by using kinetic methods to test the ability of these antibodies to inhibit specific microscopic steps in Aβ42 aggregation. This analysis has revealed that all DesAbs have significant effects on Aβ42 aggregation in vitro, and it has allowed us to identify two antibodies that target, respectively, the primary and secondary nucleation of the aggregation process with high selectivity. We have then confirmed that these in vitro results are fully consistent with the effects of the two antibodies in vivo using a C. elegans model of Aβ42-mediated toxicity.\",",
    "Curator Statement": false
  },
  "AMGAB0648": {
    "Interaction ID": "AMGAB0648",
    "Antibody ID": "ABID0518",
    "Antibody name": "DesAb-F",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1126/sciadv.1700488",
    "PMID": 28691099.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Supplementary Figure S5\", \"A DesAb designed to target α-synuclein does not inhibit Aβ42 aggregation\", \"By contrast, the antibody DesAb-F (Table 1), which showed a strong inhibitory effect on α-synuclein aggregation (38), does not have any detectable effect on the aggregation of Aβ42 (fig. S5). Because DesAb-F differs from the antibodies designed to target Aβ42 discussed here only in the sequence of the complementary peptide grafted in the CDR3 loop, these results indicate that the inhibitory effects observed on the aggregation of Aβ42 specifically originate from the computationally designed peptides (Fig. 3B).\",",
    "Curator Statement": false
  },
  "AMGAB0649": {
    "Interaction ID": "AMGAB0649",
    "Antibody ID": "ABID0390",
    "Antibody name": "chα-miSOD1",
    "Amyloid ID": "AGAMYID0014",
    "Amyloid name": "Superoxide dismutase [Cu-Zn]",
    "DOI": "10.1126/scitranslmed.aah3924",
    "PMID": 30518612.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In transgenic mice overexpressing disease-causing human SOD1G37R or SOD1G93A mutations, treatment with the α-miSOD1 antibody delayed the onset of motor symptoms, extended survival by up to 2 months, and reduced aggregation of misfolded SOD1 and motor neuron degeneration.\", \"Histological analyses of spinal cord tissues at end stage revealed a significant reduction in SOD1 aggregate load by 51% in the ventral horn of the lumbar spinal cord of ch-miSOD1–treated animals compared to vehicle-treated control littermates (Fig. 3, E and F; P < 0.05).\", \"Figure 3\", \"(E and F) Misfolded SOD1 in the ventral horn of the lumbar spinal cord was reduced at the end stage of disease by treatment with chα-miSOD1 antibody (scale bar, 400 μm; n = 14 for the vehicle-treated group and n = 10 for the chα-miSOD1–treated group).\", \"α-miSOD1 antibody treatment ameliorated disease progression and the decline of motor function and increased survival in the three mouse models. Even when animals were euthanized at the same end stage of disease, that is, at an older median age in α-miSOD1–treated mice compared to controls, marked improvements in SOD1 aggregate load, muscle weight, and neuronal survival were observed after chronic α-miSOD1 treatment. The treatment effects were most prominent in the slower-progressing SOD1G37R mice when compared to the aggressively progressing SOD1G93A mice, in line with previous studies using active immunization to target SOD1 (13–16).\"",
    "Curator Statement": false
  },
  "AMGAB0650": {
    "Interaction ID": "AMGAB0650",
    "Antibody ID": "ABID0027.5",
    "Antibody name": "muMTAU",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1126/scitranslmed.abb2639",
    "PMID": 33980574.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo,",
    "Experimental method(s)": "Immunohistochemistry, Western blot",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"muMTAU reduces accumulation of tau pathology in a Tg mouse model of tauopathy\", \"After weekly intraperitoneal (ip) administration over a 13-week period, at doses of 3, 10, and 30 mg/kg, both muMTAU and muMTAU-DANG reduced the accumulation of pathological tau relative to mice administered with a control IgG2a antibody (30 mg/kg), as measured by IHC (Fig. 2, A to D) and Western blot (Fig. 2E and fig. S6), to detect phospho-tau epitopes.\", \"Figure 2\", \" On IHC, significant reductions in pTau212/214 were observed in mice dosed with muMTAU WT (10 or 30 mg/kg; P = 0.0366 and P < 0.0001, respectively) or muMTAU- DANG (30 mg/kg; P = 0.0009) compared to the control IgG2a antibody. No differences in pTau212/214 were observed when comparing between the groups administered the same doses of muMTAU (WT) and muMTAU-DANG [P = 0.9975 (3 mg/kg); P = 0.9926 (10 mg/kg); P = 8402 (30 mg/kg)]. Both the muMTAU (WT) and muMTAU-DANG treatment groups demonstrated a significant dose response in pTau212/214 reduction (P < 0.0001 and P < 0.0011, respectively) (Fig. 2, A to D). In addition, WB with cortical lysates demonstrated a significant dose response in pTau202/205 (AT8) reduction in both muMTAU (WT) and muMTAU-DANG treatment groups (P = 0.0331 and P = 0.0349, respectively) (Fig. 2E). Our results show that both muMTAU variants, which bind tau species in the extracellular space, can attenuate the brain accumulation of pathological tau and indicate that antibody effector function is not required for this activity.\", \"The ability of systemically administered muMTAU to reduce pathology in P301L-Tg mice is consistent with the hypothesis that an anti-tau antibody can reduce the spread of tau pathology by sequestering extracellular tau.\", \"Antibody semorinemab reduces tau pathology\", \"In addition, when administered intraperitoneally once weekly for 13 weeks, murine versions of semorinemab reduced the accumulation of tau pathology in a transgenic mouse model of tauopathy, independent of antibody effector function status.\",",
    "Curator Statement": false
  },
  "AMGAB0651": {
    "Interaction ID": "AMGAB0651",
    "Antibody ID": "ABID0027.6",
    "Antibody name": "muMTAU-DANG",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1126/scitranslmed.abb2639",
    "PMID": 33980574.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo,",
    "Experimental method(s)": "Immunohistochemistry, Western blot",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"After weekly intraperitoneal (ip) administration over a 13-week period, at doses of 3, 10, and 30 mg/kg, both muMTAU and muMTAU-DANG reduced the accumulation of pathological tau relative to mice administered with a control IgG2a antibody (30 mg/kg), as measured by IHC (Fig. 2, A to D) and Western blot (Fig. 2E and fig. S6), to detect phospho-tau epitopes.\", \"Figure 2\", \" On IHC, significant reductions in pTau212/214 were observed in mice dosed with muMTAU WT (10 or 30 mg/kg; P = 0.0366 and P < 0.0001, respectively) or muMTAU- DANG (30 mg/kg; P = 0.0009) compared to the control IgG2a antibody. No differences in pTau212/214 were observed when comparing between the groups administered the same doses of muMTAU (WT) and muMTAU-DANG [P = 0.9975 (3 mg/kg); P = 0.9926 (10 mg/kg); P = 8402 (30 mg/kg)]. Both the muMTAU (WT) and muMTAU-DANG treatment groups demonstrated a significant dose response in pTau212/214 reduction (P < 0.0001 and P < 0.0011, respectively) (Fig. 2, A to D). In addition, WB with cortical lysates demonstrated a significant dose response in pTau202/205 (AT8) reduction in both muMTAU (WT) and muMTAU-DANG treatment groups (P = 0.0331 and P = 0.0349, respectively) (Fig. 2E). Our results show that both muMTAU variants, which bind tau species in the extracellular space, can attenuate the brain accumulation of pathological tau and indicate that antibody effector function is not required for this activity.\", \"Antibody semorinemab reduces tau pathology\", \"In addition, when administered intraperitoneally once weekly for 13 weeks, murine versions of semorinemab reduced the accumulation of tau pathology in a transgenic mouse model of tauopathy, independent of antibody effector function status.\",",
    "Curator Statement": false
  },
  "AMGAB0652": {
    "Interaction ID": "AMGAB0652",
    "Antibody ID": "ABID0447",
    "Antibody name": "72D9",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1155/2013/984041",
    "PMID": 24063020.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody, ThT - Total aggregation (final point), Immunohistochemistry",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Here, we showed that the anti-AβO antibody (monoclonal 72D9) can modify the Aβ aggregation pathway.\", \"We found that the anti-AβO antibody (72D9) can modify the Aβ aggregation pathway and that it directly sequesters both extracellular and intraneuronal AβOs in a nontoxic state.\", \"To assess this issue, we incubated 12.5 μM seed-free Aβ42 alone or with antibodies at 37°C for 24 h. As shown in Figure 1(a), ThT fluorescence intensity decreased with the increasing 72D9 concentration, and nonspecific IgG2b showed no antifibrillogenic activity. \", \"Figure 1\", \"Using EM (Figure 1(b)), we find Aβ fibrils in the presence of IgG2b; however, a mixture of Aβ fibrils and nonfibrillar amorphous Aβ structures was observed in the presence of 72D9.\", \"Antifibrillogenic activities of 72D9. (a) Fibril formation of Aβ1-42 at 12.5 μM was assayed on the basis of ThT fluorescence intensity at 37°C for 24 h: dose-dependent inhibition of Aβ1-42 assembly was observed for 72D9; however, nonspecific IgG2b failed to inhibit seed-free Aβ1-42 (540,000 ×g ThT-negative supernatants) assembly. (b) Electron micrographs of incubation mixture containing 50 μM Aβ1-42 preincubated with IgG2b or 72D9. Aβ1-42 with control IgG2b shows mature fibrils (left panel). Aβ1-42 with 72D9 shows nonfibrillar amorphous structures (right panel).\",",
    "Curator Statement": false
  },
  "AMGAB0653": {
    "Interaction ID": "AMGAB0653",
    "Antibody ID": "ABID0124",
    "Antibody name": "mAb07/1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1159/000335913",
    "PMID": 22343072.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Passive Anti-pE3-Aβ Vaccination Lowered Total Aβ Deposition in a Prevention Trial\", \"In this study, mice were immunized weekly with the highly specific anti-pE3-Aβ mAb07/1 starting at 5.8 months of age, during the early stages of Aβ deposition. Following 32 weeks of vaccination, total Aβ deposition (including plaques and cerebral amyloid angiopathy) was reduced in the hippocampus and cerebellum in the approximately 14 month-old treated mice compared to age- and gender-matched PBS controls (table 1; fig. 2). In the hippocampus, pE3-Aβ and general Aβ (R1282) IR were reduced by 35% (p = 0.04) and 18% (p = 0.01), respectively, while Thioflavin-S-positive fibrillar amyloid was reduced by 50% (p = 0.02) in immunized mice when normalized to PBS controls. In the cerebellum, pE3-Aβ and general Aβ IR were lowered by 76% (p = 0.0004) and 52% (p = 0.005), respectively, while Thioflavin-S-positive fibrillar amyloid was 43% less (p = 0.13, n.s.) in immunized mice when normalized to the PBS control mice. The absolute values, listed in table 1, strongly suggest that passive immunization against pE3-Aβ reduced more than pE3-Aβ alone. For example, an absolute reduction of 2.4% in general Aβ (R1282) IR was observed in the hippocampus, whereas the absolute amount of pE3-Aβ in the PBS control group was much lower (0.61%; table 1). Similar reductions were observed in the cortex but were not quantified (data not shown). Semiquantitative analysis of vascular amyloid (scored 0–3) was similar in the hippocampus between PBS control and pE3-Aβ vaccinated mice (R1282: 0.89 ± 0.11 SEM vs. 0.59 ± 0.12, p = 0.11; pE3-Aβ: 0 vs. 0, p = n.s.). In the cerebellum, vascular amyloid was reduced by vaccination (R1282: 2.11 ± 0.26 vs. 1.47 ± 0.15, p = 0.03; pE3-Aβ: 0.33 ± 0.17 vs. 0.17 ± 0.09, p = 0.24).\", \"In a therapeutic study initiated well after the onset of cerebral Aβ deposition and gliosis, weekly passive immunization with anti-pE3-Aβ mAb07/1 in 23-monthold APPswe/PS1ΔE9 mice for 7 weeks resulted in the attenuation of pE3-Aβ and general Aβ (R1282 IR) deposition as well as fibrillar amyloid (Thioflavin S) in the hippocampus (a, b) and cerebellum (c, d) compared to PBS control mice. Immunohistochemical results (a, c) and Thioflavin S labeling were quantified by image analysis (b, d). \", \"Figure 3\", \"The percent of plaque reduction was similar between the prevention and the therapeutic trial, even though the absolute level of plaque deposition was higher in the older mice. However, even in the therapeutic study, the absolute amount of general Aβ and fibrillar amyloid deposits were reduced beyond the amount expected from clearance of pE3-Aβ deposits alone as shown in table 1, suggesting that pE3-Aβ removal may prevent new plaque formation. In both studies, Aβ deposit lowering by the pE3-Aβ mAb was greater in the cerebellum than the hippocampus (and the cortex, data not shown). This may be due, in part, to the lower abundance of Aβ deposition in the cerebellum relative to that in the hippocampus and cortex.\"",
    "Curator Statement": false
  },
  "AMGAB0654": {
    "Interaction ID": "AMGAB0654",
    "Antibody ID": "ABID0124",
    "Antibody name": "mAb07/1",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1159/000335913",
    "PMID": 22343072.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In this study, mice were immunized weekly with the highly specific anti-pE3-Aβ mAb07/1 starting at 5.8 months of age, during the early stages of Aβ deposition. Following 32 weeks of vaccination, total Aβ deposition (including plaques and cerebral amyloid angiopathy) was reduced in the hippocampus and cerebellum in the approximately 14 month-old treated mice compared to age- and gender-matched PBS controls (table 1; fig. 2). In the hippocampus, pE3-Aβ and general Aβ (R1282) IR were reduced by 35% (p = 0.04) and 18% (p = 0.01), respectively, while Thioflavin-S-positive fibrillar amyloid was reduced by 50% (p = 0.02) in immunized mice when normalized to PBS controls. In the cerebellum, pE3-Aβ and general Aβ IR were lowered by 76% (p = 0.0004) and 52% (p = 0.005), respectively, while Thioflavin-S-positive fibrillar amyloid was 43% less (p = 0.13, n.s.) in immunized mice when normalized to the PBS control mice. The absolute values, listed in table 1, strongly suggest that passive immunization against pE3-Aβ reduced more than pE3-Aβ alone. For example, an absolute reduction of 2.4% in general Aβ (R1282) IR was observed in the hippocampus, whereas the absolute amount of pE3-Aβ in the PBS control group was much lower (0.61%; table 1). Similar reductions were observed in the cortex but were not quantified (data not shown). Semiquantitative analysis of vascular amyloid (scored 0–3) was similar in the hippocampus between PBS control and pE3-Aβ vaccinated mice (R1282: 0.89 ± 0.11 SEM vs. 0.59 ± 0.12, p = 0.11; pE3-Aβ: 0 vs. 0, p = n.s.). In the cerebellum, vascular amyloid was reduced by vaccination (R1282: 2.11 ± 0.26 vs. 1.47 ± 0.15, p = 0.03; pE3-Aβ: 0.33 ± 0.17 vs. 0.17 ± 0.09, p = 0.24).\", \"In a therapeutic study initiated well after the onset of cerebral Aβ deposition and gliosis, weekly passive immunization with anti-pE3-Aβ mAb07/1 in 23-monthold APPswe/PS1ΔE9 mice for 7 weeks resulted in the attenuation of pE3-Aβ and general Aβ (R1282 IR) deposition as well as fibrillar amyloid (Thioflavin S) in the hippocampus (a, b) and cerebellum (c, d) compared to PBS control mice. Immunohistochemical results (a, c) and Thioflavin S labeling were quantified by image analysis (b, d). \", \"Figure 3\", \"Table 1\", \"The percent of plaque reduction was similar between the prevention and the therapeutic trial, even though the absolute level of plaque deposition was higher in the older mice. However, even in the therapeutic study, the absolute amount of general Aβ and fibrillar amyloid deposits were reduced beyond the amount expected from clearance of pE3-Aβ deposits alone as shown in table 1, suggesting that pE3-Aβ removal may prevent new plaque formation. In both studies, Aβ deposit lowering by the pE3-Aβ mAb was greater in the cerebellum than the hippocampus (and the cortex, data not shown). This may be due, in part, to the lower abundance of Aβ deposition in the cerebellum relative to that in the hippocampus and cortex.\"",
    "Curator Statement": false
  },
  "AMGAB0655": {
    "Interaction ID": "AMGAB0655",
    "Antibody ID": "ABID0032.9",
    "Antibody name": "Y01",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1172/JCI156537",
    "PMID": 36917188.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, in cellulo, in vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, FRET-based biosensor-cell assay, Western blot, immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Monoclonal antibody Y01 prevents tauopathy progression induced by lysine 280–acetylated tau in cell and mouse models\", \"Strikingly, upon interaction with acetylated tau aggregates, Y01 prevented tauopathy progression and increased neuronal viability in neuron cultures and in tau-Tg mice through antibody-mediated neutralization and phagocytosis, respectively.\", \"Y01 inhibits acetylation-induced tau aggregation and propagation, and promotes microglial tau phagocytosis.\", \"Figure 3\", \"Supplemental Figure S19\", \"Tau aggregation and seeding can be efficiently blocked by Y01.\", \"Strikingly, in a ThT assay, addition of Y01 dramatically decreased aggregation of p300-treated tau in a concentration-dependent manner, whereas IgG had no effect (Figure 3A and Supplemental Figure 19, A and B). In FRET experiments, Y01 prevented cellular tau from aggregation induced by acetylated tau aggregates (ac-tau-agg) (Figure 3B). Y01 also inhibited seeding of tau aggregation in the sarkosyl-insoluble fraction of human AD brain (Figure 3B, right; Supplemental Figure 19C; and Supplemental Table 2). These results indicate that the Y01 antibody may have the potential to reduce the progression of tauopathy aggregation and seeding induced by in vitro p300 acetylation, as well as by in vivo human AD tau aggregates.\",  \"Y01 antibody inhibits acetylation-induced tau aggregation and propagation but enhances microglial tau uptake by Y01.\", \"(A) Y01 antibody decreases aggregation of acetylated tau.\",  \"Semidenatured Western blotting revealed that the levels of smear bands corresponding to tau aggregates were substantially lower in primary neurons treated with Y01 than in neurons treated with IgG (Figure 3C).\", \"Semidenatured Western blots with cortex lysates from mice 17 months of age revealed that total tau (Tau5), tau-acK280 (Y01), and tau-pT231 (AT180) aggregate levels were decreased in antibody-injected brains (Figure 5F).\", \"Figure 5\", \"Y01 prevents in vivo seeding and propagation of human AD-derived tauopathy.\", \"In mice treated with IgG, the number of AT8-positive neurons containing accumulations of tau increased in both the ipsilateral and the contralateral hippocampus (Figure 6A), indicating neuronal damage via ipsilateral seeding and contralateral propagation by tauopathy. By contrast, administration of mY01 dramatically decreased the number of AT8-positive neurons containing tau accumulation in the dentate gyrus (Figure 6, B and C) of hippocampus and entorhinal cortex (Figure 6, B and D). Therefore, we conclude that treatment with the tau-acK280–targeting antibody mY01 in this mouse model exerts a beneficial inhibitory effect on proteopathic seeding induced by AD-derived insoluble tau aggregates and propagation both in vivo and in vitro.\", \"Figure 6\", \"Inhibitory effects of Y01 antibody on tau seeding and propagation in vivo.\", \"We assessed proteopathic tau seeding and propagation in tau-FRET assays and in vivo stereotaxic seeding and propagation experiments using AD brain–derived insoluble tau aggregates (Figures 3 and 6). These processes were effectively inhibited by Y01, an acK280-targeting antibody, suggesting that tau-acK280 is the core seeding-competent species in the AD brain.\", \"By targeting tau-acK280, the Y01 antibody inhibits tau aggregation and propagation, and promotes microglial tau clearance (Figure 3).\", \"Finally, the findings in this study indicate that tau-acK280 is a therapeutic target of the Y01 antibody, which inhibits tau aggregation, secretion, and propagation. Thus, Y01 represents a promising new therapeutic antibody for AD and other tauopathies.\",",
    "Curator Statement": false
  },
  "AMGAB0656": {
    "Interaction ID": "AMGAB0656",
    "Antibody ID": "ABID0464",
    "Antibody name": "Ab42.2",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1172/JCI25410",
    "PMID": 16341263.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"After 4 months of passive immunization with Ab9, Ab42.2, and Ab40.1, initiated when the mice were 7 months old, Aβ levels were significantly attenuated as assessed biochemically with Aβ ELISA following SDS extraction (>50% reduction in SDS Aβ; Figure 2A) or formic acid (FA) extraction of the SDS-insoluble material (>50% reduction in FA Aβ; Figure 2B). Figure 2C shows representative immunostained sections from immunized and control Tg2576 mice. Quantitative analysis of multiple immunostained sections also revealed a significant decrease in Aβ deposition. Both plaque numbers per field (Figure 2D) and total immunoreactive plaque load (data not shown) were significantly reduced.\", \"Mice were killed following treatment, and both SDS Aβ (A) and FA Aβ (B) were analyzed by capture ELISA. SDS Aβ40 and FA Aβ40 in control mice were 123 ± 27 and 3,613 ± 610 pmol/g, respectively; SDS Aβ42 and FA Aβ42 in control mice were 44 ± 4 and 840 ± 180 pmol/g, respectively.\",\"Figure 2\", \"Table 2\", \" In 7-month-old Tg2576 mice immunized with anti-Aβ mAbs, few blood vessels with trace amounts of Aβ amyloid staining were detected in control mice, but none were detected in the immunized mice with decreased levels of amyloid in the brain. Similarly, in the passively immunized CRND8 mice, the number and the intensity of CAA-positive vessels were slightly but not significantly reduced (Table 2).\",",
    "Curator Statement": "Prevented plaque deposition on young mice, but not on old mice with preexistent deposits."
  },
  "AMGAB0657": {
    "Interaction ID": "AMGAB0657",
    "Antibody ID": "ABID0464",
    "Antibody name": "Ab42.2",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1172/JCI25410",
    "PMID": 16341263.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\",\" In 7-month-old Tg2576 mice immunized with anti-Aβ mAbs, few blood vessels with trace amounts of Aβ amyloid staining were detected in control mice, but none were detected in the immunized mice with decreased levels of amyloid in the brain. Similarly, in the passively immunized CRND8 mice, the number and the intensity of CAA-positive vessels were slightly but not significantly reduced (Table 2).\",",
    "Curator Statement": "Prevented plaque deposition on young mice, but not on old mice with preexistent deposits."
  },
  "AMGAB0658": {
    "Interaction ID": "AMGAB0658",
    "Antibody ID": "ABID0464",
    "Antibody name": "Ab42.2",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1172/JCI25410",
    "PMID": 16341263.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-Aβ42, anti-Aβ40, and anti-Aβ1–16 mAbs attenuated plaque deposition in the prevention study.\", \"Passive immunotherapy with anti-Aβ42– and anti-Aβ40–specific mAbs attenuates amyloid deposition in young Tg2576 mice.\", \"After 4 months of passive immunization with Ab9, Ab42.2, and Ab40.1, initiated when the mice were 7 months old, Aβ levels were significantly attenuated as assessed biochemically with Aβ ELISA following SDS extraction (>50% reduction in SDS Aβ; Figure 2A) or formic acid (FA) extraction of the SDS-insoluble material (>50% reduction in FA Aβ; Figure 2B). Figure 2C shows representative immunostained sections from immunized and control Tg2576 mice. Quantitative analysis of multiple immunostained sections also revealed a significant decrease in Aβ deposition. Both plaque numbers per field (Figure 2D) and total immunoreactive plaque load (data not shown) were significantly reduced.\", \"Mice were killed following treatment, and both SDS Aβ (A) and FA Aβ (B) were analyzed by capture ELISA. SDS Aβ40 and FA Aβ40 in control mice were 123 ± 27 and 3,613 ± 610 pmol/g, respectively; SDS Aβ42 and FA Aβ42 in control mice were 44 ± 4 and 840 ± 180 pmol/g, respectively.\",\"Figure 2\", \"Weekly injections of 3-month-old CRND8 mice with 500 μg of Ab9 and Ab42.2 mAbs for 8 weeks resulted in significant reduction of SDS Aβ but not FA Aβ only in Ab9-treated mice (>40% reduction in SDS Aβ; Figure 3, A and B). Total Aβ42 levels (SDS Aβ plus FA Aβ) were also significantly reduced by Ab9 treatment. Quantitative analysis of the immunostained sections also revealed a significant decrease in Aβ deposition in Ab9-treated mice (Figure 3, C and D). Immunization with Ab42.2 did not lead to a significant decrease in Aβ load, although there was a trend toward reduction in Aβ42 levels (P = 0.13), suggesting that this mAb is less effective than Ab9 in clearing amyloid deposits in CRND8.\", \"Figure 3\",",
    "Curator Statement": "Prevented plaque deposition on young mice, but not on old mice with preexistent deposits."
  },
  "AMGAB0659": {
    "Interaction ID": "AMGAB0659",
    "Antibody ID": "ABID0464",
    "Antibody name": "Ab42.2",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1172/JCI25410",
    "PMID": 16341263.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In contrast, anti-Aβ42 and anti-Aβ40 mAbs were less effective in attenuating Aβ deposition in the therapeutic studies and were not effective in clearing diffuse plaques following direct injection into the cortex.\", \" However, when administered to older mice with higher Aβ loads, only anti-Aβ1–16 mAbs that recognize native Aβ amyloid were effective in attenuating Ab deposition.\", \"In contrast, 4 months of passive immunization with these same mAbs, initiated when the Tg2576 mice were 11 months old, had no significant effect on biochemical (Figure 2, E and F) or immunohistochemical Aβ loads (data not shown), although a slight but nonsignificant decrease in the SDS Aβ was seen in the Ab9-treated animals (35% reduction in SDS Aβ; Figure 2E).\", \"Figure 2\", \"Weekly injections of 3-month-old CRND8 mice with 500 μg of Ab9 and Ab42.2 mAbs for 8 weeks resulted in significant reduction of SDS Aβ but not FA Aβ only in Ab9-treated mice (>40% reduction in SDS Aβ; Figure 3, A and B). Total Aβ42 levels (SDS Aβ plus FA Aβ) were also significantly reduced by Ab9 treatment. Quantitative analysis of the immunostained sections also revealed a significant decrease in Aβ deposition in Ab9-treated mice (Figure 3, C and D). Immunization with Ab42.2 did not lead to a significant decrease in Aβ load, although there was a trend toward reduction in Aβ42 levels (P = 0.13), suggesting that this mAb is less effective than Ab9 in clearing amyloid deposits in CRND8.\", \"Figure 3\", \"Immunostained plaque load of Aβ was significantly decreased by Ab9, anti-Aβ1–16 mAb of IgG1 isotype (Ab3), and anti-Aβ1–16 mAb of IgG3 isotype (Ab2), whereas the anti-Aβ1–16 mAb of IgG2b isotype (Ab5) and both Ab40.1 and Ab42.2 had no measurable effect (Figure 4, A and C).\", \"Figure 4\",",
    "Curator Statement": "Prevented plaque deposition on young mice, but not on old mice with preexistent deposits."
  },
  "AMGAB0660": {
    "Interaction ID": "AMGAB0660",
    "Antibody ID": "ABID0465",
    "Antibody name": "Ab40.1",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1172/JCI25410",
    "PMID": 16341263.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Mice were killed following treatment, and both SDS Aβ (A) and FA Aβ (B) were analyzed by capture ELISA. SDS Aβ40 and FA Aβ40 in control mice were 123 ± 27 and 3,613 ± 610 pmol/g, respectively; SDS Aβ42 and FA Aβ42 in control mice were 44 ± 4 and 840 ± 180 pmol/g, respectively.\", \"Figure 2\", \"Table 2\", \" In 7-month-old Tg2576 mice immunized with anti-Aβ mAbs, few blood vessels with trace amounts of Aβ amyloid staining were detected in control mice, but none were detected in the immunized mice with decreased levels of amyloid in the brain. Similarly, in the passively immunized CRND8 mice, the number and the intensity of CAA-positive vessels were slightly but not significantly reduced (Table 2).\",",
    "Curator Statement": "Prevented plaque deposition on young mice, but not on old mice with preexistent deposits."
  },
  "AMGAB0661": {
    "Interaction ID": "AMGAB0661",
    "Antibody ID": "ABID0465",
    "Antibody name": "Ab40.1",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1172/JCI25410",
    "PMID": 16341263.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\",\" In 7-month-old Tg2576 mice immunized with anti-Aβ mAbs, few blood vessels with trace amounts of Aβ amyloid staining were detected in control mice, but none were detected in the immunized mice with decreased levels of amyloid in the brain. Similarly, in the passively immunized CRND8 mice, the number and the intensity of CAA-positive vessels were slightly but not significantly reduced (Table 2).\",",
    "Curator Statement": "Prevented plaque deposition on young mice, but not on old mice with preexistent deposits."
  },
  "AMGAB0662": {
    "Interaction ID": "AMGAB0662",
    "Antibody ID": "ABID0465",
    "Antibody name": "Ab40.1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1172/JCI25410",
    "PMID": 16341263.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-Aβ42, anti-Aβ40, and anti-Aβ1–16 mAbs attenuated plaque deposition in the prevention study.\", \"Passive immunotherapy with anti-Aβ42– and anti-Aβ40–specific mAbs attenuates amyloid deposition in young Tg2576 mice.\", \"After 4 months of passive immunization with Ab9, Ab42.2, and Ab40.1, initiated when the mice were 7 months old, Aβ levels were significantly attenuated as assessed biochemically with Aβ ELISA following SDS extraction (>50% reduction in SDS Aβ; Figure 2A) or formic acid (FA) extraction of the SDS-insoluble material (>50% reduction in FA Aβ; Figure 2B). Figure 2C shows representative immunostained sections from immunized and control Tg2576 mice. Quantitative analysis of multiple immunostained sections also revealed a significant decrease in Aβ deposition. Both plaque numbers per field (Figure 2D) and total immunoreactive plaque load (data not shown) were significantly reduced.\",\"Mice were killed following treatment, and both SDS Aβ (A) and FA Aβ (B) were analyzed by capture ELISA. SDS Aβ40 and FA Aβ40 in control mice were 123 ± 27 and 3,613 ± 610 pmol/g, respectively; SDS Aβ42 and FA Aβ42 in control mice were 44 ± 4 and 840 ± 180 pmol/g, respectively.\", \"Figure 2\",",
    "Curator Statement": "Prevented plaque deposition on young mice, but not on old mice with preexistent deposits."
  },
  "AMGAB0663": {
    "Interaction ID": "AMGAB0663",
    "Antibody ID": "ABID0465",
    "Antibody name": "Ab40.1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1172/JCI25410",
    "PMID": 16341263.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In contrast, anti-Aβ42 and anti-Aβ40 mAbs were less effective in attenuating Aβ deposition in the therapeutic studies and were not effective in clearing diffuse plaques following direct injection into the cortex.\", \" However, when administered to older mice with higher Aβ loads, only anti-Aβ1–16 mAbs that recognize native Aβ amyloid were effective in attenuating Ab deposition.\", \"In contrast, 4 months of passive immunization with these same mAbs, initiated when the Tg2576 mice were 11 months old, had no significant effect on biochemical (Figure 2, E and F) or immunohistochemical Aβ loads (data not shown), although a slight but nonsignificant decrease in the SDS Aβ was seen in the Ab9-treated animals (35% reduction in SDS Aβ; Figure 2E).\", \"Figure 2\", \"Immunostained plaque load of Aβ was significantly decreased by Ab9, anti-Aβ1–16 mAb of IgG1 isotype (Ab3), and anti-Aβ1–16 mAb of IgG3 isotype (Ab2), whereas the anti-Aβ1–16 mAb of IgG2b isotype (Ab5) and both Ab40.1 and Ab42.2 had no measurable effect (Figure 4, A and C).\", \"Figure 4\",",
    "Curator Statement": "Prevented plaque deposition on young mice, but not on old mice with preexistent deposits."
  },
  "AMGAB0664": {
    "Interaction ID": "AMGAB0664",
    "Antibody ID": "ABID0466",
    "Antibody name": "Ab9",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1172/JCI25410",
    "PMID": 16341263.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\", \"Table 2\", \" In 7-month-old Tg2576 mice immunized with anti-Aβ mAbs, few blood vessels with trace amounts of Aβ amyloid staining were detected in control mice, but none were detected in the immunized mice with decreased levels of amyloid in the brain. Similarly, in the passively immunized CRND8 mice, the number and the intensity of CAA-positive vessels were slightly but not significantly reduced (Table 2).\",",
    "Curator Statement": false
  },
  "AMGAB0665": {
    "Interaction ID": "AMGAB0665",
    "Antibody ID": "ABID0466",
    "Antibody name": "Ab9",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1172/JCI25410",
    "PMID": 16341263.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"However, when administered to older mice with higher Aβ loads, only anti-Aβ1–16 mAbs that recognize native Aβ amyloid were effective in attenuating Ab deposition.\", \"In contrast, 4 months of passive immunization with these same mAbs, initiated when the Tg2576 mice were 11 months old, had no significant effect on biochemical (Figure 2, E and F) or immunohistochemical Aβ loads (data not shown), although a slight but nonsignificant decrease in the SDS Aβ was seen in the Ab9-treated animals (35% reduction in SDS Aβ; Figure 2E).\", \"Figure 2\", \"Immunostained plaque load of Aβ was significantly decreased by Ab9, anti-Aβ1–16 mAb of IgG1 isotype (Ab3), and anti-Aβ1–16 mAb of IgG3 isotype (Ab2), whereas the anti-Aβ1–16 mAb of IgG2b isotype (Ab5) and both Ab40.1 and Ab42.2 had no measurable effect (Figure 4, A and C).\", \"Figure 4\",",
    "Curator Statement": false
  },
  "AMGAB0666": {
    "Interaction ID": "AMGAB0666",
    "Antibody ID": "ABID0467",
    "Antibody name": "Ab5",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1172/JCI25410",
    "PMID": 16341263.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Immunostained plaque load of Aβ was significantly decreased by Ab9, anti-Aβ1–16 mAb of IgG1 isotype (Ab3), and anti-Aβ1–16 mAb of IgG3 isotype (Ab2), whereas the anti-Aβ1–16 mAb of IgG2b isotype (Ab5) and both Ab40.1 and Ab42.2 had no measurable effect (Figure 4, A and C).\", \"Figure 4\",",
    "Curator Statement": false
  },
  "AMGAB0667": {
    "Interaction ID": "AMGAB0667",
    "Antibody ID": "ABID0468",
    "Antibody name": "Ab2",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1172/JCI25410",
    "PMID": 16341263.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Immunostained plaque load of Aβ was significantly decreased by Ab9, anti-Aβ1–16 mAb of IgG1 isotype (Ab3), and anti-Aβ1–16 mAb of IgG3 isotype (Ab2), whereas the anti-Aβ1–16 mAb of IgG2b isotype (Ab5) and both Ab40.1 and Ab42.2 had no measurable effect (Figure 4, A and C).\", \"Figure 4\",",
    "Curator Statement": false
  },
  "AMGAB0668": {
    "Interaction ID": "AMGAB0668",
    "Antibody ID": "ABID0469",
    "Antibody name": "Ab3",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1172/JCI25410",
    "PMID": 16341263.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Immunostained plaque load of Aβ was significantly decreased by Ab9, anti-Aβ1–16 mAb of IgG1 isotype (Ab3), and anti-Aβ1–16 mAb of IgG3 isotype (Ab2), whereas the anti-Aβ1–16 mAb of IgG2b isotype (Ab5) and both Ab40.1 and Ab42.2 had no measurable effect (Figure 4, A and C).\", \"Figure 4\",",
    "Curator Statement": false
  },
  "AMGAB0669": {
    "Interaction ID": "AMGAB0669",
    "Antibody ID": "ABID0023.9",
    "Antibody name": "Antibody 2286",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1186/1742-2094-1-24",
    "PMID": 15588287.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"However, cerebral amyloid angiopathy increased substantially with immunotherapy, and some deposits were associated with microhemorrhage.\",  \"Passive amyloid immunotherapy clears parenchymal Aβ deposits, but increases vascular amyloid\", \"Figure 2\", \"We then separately analyzed vascular and parenchymal deposits which revealed a near 90% reduction in parenchymal deposits (p < 0.001) but a 3–4 fold elevation of vascular Congo-red staining (p < 0.0001; Fig. 2A, center and right panels, respectively).\", \"There was a graded reduction in overall Congo-red staining nearing 75% as duration of antibody exposure increased (as reported previously; Fig. 2B). However, when separated into vascular Congo-red deposits and parenchymal deposits, there was an antibody-exposure-time-dependent increase in vascular deposition in both hippocampus and frontal cortex (Fig. 2C; p < 0.05 frontal cortex and hippocampus) and a corresponding nearly 90% decrease in parenchymal deposits (Fig. 2D; p < 0.001 in frontal cortex and hippocampus).\", \"Passive immunization with anti-Aβ antibodies decreases total and parenchymal amyloid loads while increasing vascular amyloid in frontal cortex and hippocampus of APP-transgenic mice. \", \"Mice treated with control antibodies revealed occasional cortical vascular amyloid deposits (22 months, Fig. 3A, 28 months, Fig. 3C), while mice administered anti-Aβ antibodies had increased amounts of vascular amyloid staining (3-month treatment, Fig 3B; 5-month treatment, Fig 3D).\", \"Figure 3\", \"Increased Congo red staining of blood vessels following anti-Aβ antibody administration is associated with activated microglia.\", \"When we analyzed the sections for only vascular amyloid (CAA) we found that this measure was significantly increased following 2, 3 and 5 months of anti-Aβ antibody treatment.\",",
    "Curator Statement": false
  },
  "AMGAB0670": {
    "Interaction ID": "AMGAB0670",
    "Antibody ID": "ABID0023.9",
    "Antibody name": "Antibody 2286",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/1742-2094-1-24",
    "PMID": 15588287.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Passive immunotherapy against Aβ in aged APP-transgenic mice reverses cognitive deficits and depletes parenchymal amyloid deposits in spite of increased vascular amyloid and microhemorrhage\", \"Dramatic reductions of diffuse Aβ immunostaining and parenchymal Congophilic amyloid deposits were observed after five months, indicating that even well-established amyloid deposits are susceptible to immunotherapy.\", \"Passive amyloid immunotherapy clears parenchymal Aβ deposits, but increases vascular amyloid\", \"In a prior experiment examining the effects of passive anti-Aβ immunotherapy for 1, 2 or 3 months in APP-transgenic mice killed at 21 months of age [14], we found a time-dependent reduction of both Aβ immunostaining of diffuse and fibrillar deposits and Congo-red staining of fibrillar amyloid deposits. In the current study we found a similar reduction in both Aβ immunostaining (Table 1) and total Congo-red staining (Fig. 2A, left panel; p < 0.001 frontal cortex and p < 0.01 hippocampus) after 5 months of immunotherapy. We noted that the bulk of what remained was vascular amyloid.\",  \"Table 1\", \"Figure 2\", \"We then separately analyzed vascular and parenchymal deposits which revealed a near 90% reduction in parenchymal deposits (p < 0.001) but a 3–4 fold elevation of vascular Congo-red staining (p < 0.0001; Fig. 2A, center and right panels, respectively).\", \"There was a graded reduction in overall Congo-red staining nearing 75% as duration of antibody exposure increased (as reported previously; Fig. 2B). However, when separated into vascular Congo-red deposits and parenchymal deposits, there was an antibody-exposure-time-dependent increase in vascular deposition in both hippocampus and frontal cortex (Fig. 2C; p < 0.05 frontal cortex and hippocampus) and a corresponding nearly 90% decrease in parenchymal deposits (Fig. 2D; p < 0.001 in frontal cortex and hippocampus).\", \"Total Aβ load is significantly reduced following 5 months of anti-Aβ antibody treatment. Percent area occupied by positive immunohistochemical stain for Aβ is shown ± standard error of the mean for both the frontal cortex and hippocampus. Also shown is the percent reduction of Aβ observed following anti-Aβ antibody treatment\", \"Passive immunization with anti-Aβ antibodies decreases total and parenchymal amyloid loads while increasing vascular amyloid in frontal cortex and hippocampus of APP-transgenic mice. \", \"A substantial reduction in total Congophilic amyloid deposits was observed in old APP-transgenic mice treated with anti-Aβ antibodies for 2 or more months. \", \"The remaining parenchymal amyloid load was almost completely eliminated with this antibody approach.\", \"Clearly, because total amyloid load was significantly reduced not all amyloid was shifted into the vessels; but, it appears that at least some of the Congophilic material was redistributed to the vasculature.\",",
    "Curator Statement": false
  },
  "AMGAB0671": {
    "Interaction ID": "AMGAB0671",
    "Antibody ID": "ABID0440",
    "Antibody name": "Antibody 2906",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1186/1742-2094-1-24",
    "PMID": 15588287.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 2\", \"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0672": {
    "Interaction ID": "AMGAB0672",
    "Antibody ID": "ABID0440",
    "Antibody name": "Antibody 2906",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/1742-2094-1-24",
    "PMID": 15588287.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0673": {
    "Interaction ID": "AMGAB0673",
    "Antibody ID": "ABID0471",
    "Antibody name": "KW1",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1186/2051-5960-2-43",
    "PMID": 24725347.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"KW1 results in an extended lag phase and the formation of non-fibrillar species at the expense of mature fibrils (Figure  5D,E), similar to previous observations with dimeric KW1 [29].\", \"The non-fibrillar aggregates formed by KW1 co-incubation with disaggregated Aβ(1–40) expose more surface hydrophobicity, as measured by increased binding of the dye 8-anilino-1-naphthalenesulfonic acid (ANS), than the more fibrillar aggregates formed in the absence of KW1 (Figure  5F). They also bind Thioflavin T (ThT), a dye that interacts with ordered β-sheet rich aggregates, more weakly than the more fibrillar species formed in the absence of KW1 (Figure  5G).\", \"Indeed, if we remodel such a situation in vitro by addition of KW1 to disaggregated Aβ(1-40) we find a significantly perturbed fibrillation pathway (Figure  5C). KW1 results in an extended lag phase and the formation of non-fibrillar species at the expense of mature fibrils (Figure  5D,E), similar to previous observations with dimeric KW1 [29].\", \"Indeed, the effects of KW1 are also associated with an altered structure of the Aβ peptide that is evident from TEM (Figure  5E) and ANS binding experiments (Figure  5F).\",",
    "Curator Statement": false
  },
  "AMGAB0674": {
    "Interaction ID": "AMGAB0674",
    "Antibody ID": "ABID0471",
    "Antibody name": "KW1",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1186/2051-5960-2-43",
    "PMID": 24725347.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 5\", \"Indeed, the effects of KW1 are also associated with an altered structure of the Aβ peptide that is evident from TEM (Figure  5E) and ANS binding experiments (Figure  5F).\",",
    "Curator Statement": false
  },
  "AMGAB0675": {
    "Interaction ID": "AMGAB0675",
    "Antibody ID": "ABID0391",
    "Antibody name": "DC8E8",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1186/alzrt277",
    "PMID": 25478018.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, Immunohistochemistry,",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Treatment with DC8E8 in a mouse AD model expressing mis-disordered human tau significantly reduced the amount of insoluble oligomerised tau and the number of early and mature neurofibrillary tangles in the transgenic mouse brains.\", \" DC8E8 prevents tau aggregation in vitro and reduces the amount of a wide range of tau oligomers and neurofibrillary pathologies in the brain in transgenic animals.\", \"Table 2\", \"The screening revealed that the mAb DC8E8 was most efficient in prevention of the pathological conformational change and fibrillisation of tau proteins compared with other tested tau-specific antibodies (Table 2). The antibody reduced the amount of oligomerised truncated tau by 84% when measured by thioflavin T fluorescence (Table 2).\", \"DC8E8 inhibitory activity on tau oligomerisation was examined at the various time points (1, 4 and 20 hours) (Figure 1A) and was highly statistically significant when analysed using an unpaired t-test (P < 0.0001). Furthermore, oligomerisation reactions from tested time points were analysed using immunoblotting as well. The analysis showed that DC8E8 inhibited the whole process of tau oligomerisation, that is, the formation of tau dimers, trimers and higher-order oligomers of mis-disordered tau (Figure 1B).\", \"Inhibitory activity of DC8E8 was statistically significant for the indicated time points when analysed using a nonparametric t-test (P < 0.0001).\", \"Figure 1\", \"DC8E8 immunotherapy significantly reduces levels of insoluble tau oligomers in transgenic mouse brain\", \"We found that DC8E8 therapy significantly reduced the levels of sarcosyl-insoluble tau oligomers (89%) (Figure 3C and D).\", \"Figure 3\", \"DC8E8 immunotherapy decreases load of neurofibrillary tangles in brains of transgenic mice expressing mis-disordered tau\",  \"Figure 4\", \" However, immunotherapy of transgenic mice with candidate therapeutic antibody DC8E8 significantly reduced early stages (Figure 4B and C) (P < 0.001) and late stages of tangle formation (P < 0.05) (Figure 4E and F) compared to those treated with mock antibody.\", \"DC8E8 significantly reduces the number of neurofibrillary tangles in transgenic mice. Transgenic mice were treated with mock antibody DC51 (A) and (D) and with DC8E8 (B) and (E). Neurofibrillary tangles (NFTs) were visualised with AT8 staining (A) and (B) and with pS214 antibody (D) and (E). Transgenic mice treated with therapeutic antibody DC8E8 showed significantly less tau pathology than mice treated with mock antibody DC51 (C) and (F). * - P < 0.05; *** - P < 0.001; boxes represent 75 percentiles, middle bars represent medians and outer horizontal bars represents data range.\",\"In line with this, DC8E8 inhibits the formation of dimers, trimers and oligomers by mis-disordered tau.\", \"The antibody was able to significantly reduce early and late tau pathology, showing that DC8E8 targets and disables disease-modified mis-disordered tau. Importantly, antibody DC8E8 recognises all forms of tau lesions, including pretangles and intracellular and extracellular NFTs, in both preclinical and fully developed human AD.\", \"(5) Binding of DC8E8 to a high-affinity epitope inhibits pathological tau–tau interaction and thus delineates a key regulatory domain for pathological tau assembly.\",",
    "Curator Statement": false
  },
  "AMGAB0676": {
    "Interaction ID": "AMGAB0676",
    "Antibody ID": "ABID0392",
    "Antibody name": "DC11",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1186/alzrt277",
    "PMID": 25478018.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"Surprisingly, within the panel of screened antibodies targeting mis-disordered tau, some antibodies displayed an opposite effect, that is, not inhibition but enhancement of tau oligomerisation (Table 2, mAb MN423 and DC11).\",",
    "Curator Statement": false
  },
  "AMGAB0677": {
    "Interaction ID": "AMGAB0677",
    "Antibody ID": "ABID0393",
    "Antibody name": "DC25",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1186/alzrt277",
    "PMID": 25478018.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\",",
    "Curator Statement": false
  },
  "AMGAB0678": {
    "Interaction ID": "AMGAB0678",
    "Antibody ID": "ABID0394",
    "Antibody name": "DC4R",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1186/alzrt277",
    "PMID": 25478018.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\",",
    "Curator Statement": false
  },
  "AMGAB0679": {
    "Interaction ID": "AMGAB0679",
    "Antibody ID": "ABID0395",
    "Antibody name": "dGAE56",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1186/alzrt277",
    "PMID": 25478018.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\",",
    "Curator Statement": false
  },
  "AMGAB0680": {
    "Interaction ID": "AMGAB0680",
    "Antibody ID": "ABID0396",
    "Antibody name": "DC144",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1186/alzrt277",
    "PMID": 25478018.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\",",
    "Curator Statement": false
  },
  "AMGAB0681": {
    "Interaction ID": "AMGAB0681",
    "Antibody ID": "ABID0397",
    "Antibody name": "MN423",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1186/alzrt277",
    "PMID": 25478018.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 2\", \"Surprisingly, within the panel of screened antibodies targeting mis-disordered tau, some antibodies displayed an opposite effect, that is, not inhibition but enhancement of tau oligomerisation (Table 2, mAb MN423 and DC11).\",",
    "Curator Statement": false
  },
  "AMGAB0682": {
    "Interaction ID": "AMGAB0682",
    "Antibody ID": "ABID0398",
    "Antibody name": "DC51",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1186/alzrt277",
    "PMID": 25478018.0,
    "Impact of the antibody on amyloid formation": "No effect,",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative Control",
    "Quote of the interaction": "\"Table 2\",\"A mock antibody, DC51[39], which does not bind to tau, did not influence the conformational change of tau, resulting in unaltered thioflavin T fluorescence.\", \"Figure 3\", \"Treatment of transgenic mice with mock antibody DC51 had no impact on the load of NFTs (Figure 4A and D).\", \"Figure 4\", \"DC8E8 significantly reduces the number of neurofibrillary tangles in transgenic mice. Transgenic mice were treated with mock antibody DC51 (A) and (D) and with DC8E8 (B) and (E). Neurofibrillary tangles (NFTs) were visualised with AT8 staining (A) and (B) and with pS214 antibody (D) and (E). Transgenic mice treated with therapeutic antibody DC8E8 showed significantly less tau pathology than mice treated with mock antibody DC51 (C) and (F). * - P < 0.05; *** - P < 0.001; boxes represent 75 percentiles, middle bars represent medians and outer horizontal bars represents data range.\",",
    "Curator Statement": false
  },
  "AMGAB0683": {
    "Interaction ID": "AMGAB0683",
    "Antibody ID": "ABID0144",
    "Antibody name": "PaD97-D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s12896-015-0146-8",
    "PMID": 26084577.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Bivalent scFv-Fc antibodies (Yumabs) were able to interfere with fibril formation at a substoichiometric level for PaD97-D6, PaD233-E5 and PaD236-H2 (Figure 6).\", \"Figure 6\", \"Addition of 4 μM scFv-Fc antibody to 5 μM Aβ42 monomers resulted in a reduction in ThT fluorescence of about 25% for PaD97-D6, nearly 50% for PaD236-H2 and even more elevated forPaD233-E5 after 96 h of incubation (Figure 6)\", \"PaD97-D6 and PaD236-H2 demonstrate a concentration dependent retardation of fibril formation resulting in shorter fibrils and an overall stronger appearance of unstructured aggregates. They do not prevent fibrillization entirely, which suggests a steric hindrance during monomer-monomer attachment [61].\"",
    "Curator Statement": false
  },
  "AMGAB0684": {
    "Interaction ID": "AMGAB0684",
    "Antibody ID": "ABID0145",
    "Antibody name": "PaD172-F12",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s12896-015-0146-8",
    "PMID": 26084577.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 6\", \" Interestingly, PaD172-F12, also directed against the N-terminal end of Aβ42 like PaD97-D6 and PaD236-H2, did not show an inhibitory effect.\"",
    "Curator Statement": false
  },
  "AMGAB0685": {
    "Interaction ID": "AMGAB0685",
    "Antibody ID": "ABID0146",
    "Antibody name": "PaD236-H2",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s12896-015-0146-8",
    "PMID": 26084577.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Bivalent scFv-Fc antibodies (Yumabs) were able to interfere with fibril formation at a substoichiometric level for PaD97-D6, PaD233-E5 and PaD236-H2 (Figure 6).\", \"Figure 6\", \"Addition of 4 μM scFv-Fc antibody to 5 μM Aβ42 monomers resulted in a reduction in ThT fluorescence of about 25% for PaD97-D6, nearly 50% for PaD236-H2 and even more elevated forPaD233-E5 after 96 h of incubation (Figure 6)\", \"PaD97-D6 and PaD236-H2 demonstrate a concentration dependent retardation of fibril formation resulting in shorter fibrils and an overall stronger appearance of unstructured aggregates. They do not prevent fibrillization entirely, which suggests a steric hindrance during monomer-monomer attachment [61].\", \"Albeit also binding to the amino-terminal region of Aβ42, PaD172-F12 exhibited no substantial effect on fibril formation.\", \"Interestingly, PaD233-E5 has a much more pronounced influence on amyloid-β fibrillogenesis than any other antibody as visualized by TEM. Yet the ThT absorbance after 96 h is similar to that of PaD236-H2 which might be an indication for the formation of smaller aggregates with a β-sheet rich content.\"",
    "Curator Statement": false
  },
  "AMGAB0686": {
    "Interaction ID": "AMGAB0686",
    "Antibody ID": "ABID0147",
    "Antibody name": "PaD213-A5",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s12896-015-0146-8",
    "PMID": 26084577.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 6\", \"Addition of 4 μM scFv-Fc antibody to 5 μM Aβ42 monomers resulted in a reduction in ThT fluorescence of about 25% for PaD97-D6, nearly 50% for PaD236-H2 and even more elevated forPaD233-E5 after 96 h of incubation (Figure 6). Comparison with PaD213-A5 or the negative control scFv-Fc antibody indicates that this effect is not contributed to antibody concentration or design.\" ,",
    "Curator Statement": false
  },
  "AMGAB0687": {
    "Interaction ID": "AMGAB0687",
    "Antibody ID": "ABID0148",
    "Antibody name": "PaD233-E5",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s12896-015-0146-8",
    "PMID": 26084577.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Bivalent scFv-Fc antibodies (Yumabs) were able to interfere with fibril formation at a substoichiometric level for PaD97-D6, PaD233-E5 and PaD236-H2 (Figure 6).\", \"The influence is most notable for PaD233-E5, the antibody targeting the central α-helical region of Aβ42.\", \"Figure 6\", \"Addition of 4 μM scFv-Fc antibody to 5 μM Aβ42 monomers resulted in a reduction in ThT fluorescence of about 25% for PaD97-D6, nearly 50% for PaD236-H2 and even more elevated forPaD233-E5 after 96 h of incubation (Figure 6)\", \"PaD233-E5 impacts fibril formation, which is not surprising as it targets the central region of Aβ42 with Aβ17–22 (LVFFAE), a part of the hydrophobic core element (LVFF) that is essential for β-sheet formation during fibrillization [65].\", \"Interestingly, PaD233-E5 has a much more pronounced influence on amyloid-β fibrillogenesis than any other antibody as visualized by TEM. Yet the ThT absorbance after 96 h is similar to that of PaD236-H2 which might be an indication for the formation of smaller aggregates with a β-sheet rich content.\", \"PaD233-E5, albeit binding also oligomers and fibrils, showed a 100fold increased affinity towards monomers. It is also one of the three antibodies exhibiting an inhibitory effect on the fibrillization of Aβ42 monomers.\",",
    "Curator Statement": false
  },
  "AMGAB0688": {
    "Interaction ID": "AMGAB0688",
    "Antibody ID": "ABID0139",
    "Antibody name": "NbSyn87",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1186/s12915-017-0390-6",
    "PMID": 28673288.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Atomic force microscopy (AFM), Other: Quartz crystal microbalance experiments, Other: single molecule FRET (sm-FRET), Digestion experiments by proteinase K",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "H1: GY--SGY-M,  H2: AIYRGDKITY,  H3: RRVVADSPLLSKTYAY",
    "Quote of the interaction": "\"We show that both nanobodies inhibit the formation of ɑS fibrils.\", \"We identified the ability of the nanobodies to inhibit the formation of ɑS fibrils and to destabilize toxic high-FRET oligomers of ɑS, and explored how the latter process affects oligomer-induced cytotoxicity.\", \"NbSyn2 and NbSyn87 inhibit the formation, maturation, and elongation of ɑS fibrils\", \"Figure 1\", \"In contrast, moderate inhibition of fibril formation was observed in the presence of NbSyn2, whereas solutions incubated in the presence of NbSyn87 gave rise to much lower ThT fluorescence signals over the entire duration of the experiment, indicating a stronger inhibition of ɑS fibril formation in the presence of this nanobody [13, 37]. In addition, we confirmed the inhibition of the formation of ThT-active aggregates in the presence of NbSyn2 and NbSyn87 by total internal reflection fluorescence microscopy imaging of the solutions extracted during the process of the aggregation reaction (Additional file 1: Figure S1).\", \"Figure S1\", \"In agreement with the findings from the ThT fluorescence assays, the images obtained in this way showed the presence of large numbers of amyloid fibrils in the solutions of ɑS that had been incubated in the absence of nanobodies or in the presence of NbHul5g or NbSyn2 (Fig. 1b). In the samples of ɑS incubated with NbSyn87, only small and apparently spherical aggregates along with monomeric species were observed, and no large fibrils could be detected (Fig. 1b). Comparison of average fibril heights from AFM maps revealed that fibrils formed in the presence of NbSyn2 were thinner than fibrils formed in the absence of nanobodies or in the presence of NbHul5g (Fig. 1c and Additional file 1: Figure S1), indicating that nanobodies impaired the maturation of ɑS fibrils. The differences in the fibril-forming capability of ɑS identified in the presence of the two ɑS-specific nanobodies might be due to the differences in the epitopes they bind.\", \"It was found that the elongation rate of ɑS fibrils markedly decreased in the presence of both ɑS-specific nanobodies, corresponding to 30–40% of the rate in their absence, as described in further detail in Additional file 2: Tables S3 and S4, and discussed in Additional file 2: Supplementary Results.\", \"Table S3\", \"Table S4\", \"Large amyloid fibrils and fibrillar fragments were observed in all samples at this time, except in the presence of NbSyn87, where short protofibrils were present along with oligomeric aggregates.\", \"Figure S2\", \"Figure S3\", \"Here, the histograms have been split into two populations of apparent sizes, small-mers (2–5 monomer units) and large-mers (6–150 monomer units). For large-mers, the differences in the FRET efficiency histograms are clearly observable, especially at times longer than 24 h. In the histograms of ɑS-only and ɑS with NbHul5g, the peak centered at the FRET efficiency value of 0.8 is dominant and corresponds to high-FRET oligomers. In the presence of both ɑS-specific nanobodies, the histograms are centered at the FRET efficiency value of 0.5, and the maximum at 0.8 is absent\", \"Figure 2\", \"The most rapid decrease in the monomer concentration, deduced from the monomer burst-rates [37], occurred in the samples containing 70 μM ɑS alone or in the presence of the control NbHul5g (Fig. 1d, e). However, samples containing NbSyn87 and NbSyn2 showed significantly slower monomer depletion. Based on the monomer depletion data derived from sm-FRET, after 30 h of aggregation, approximately 70% of the sample was aggregated in the ɑS-only reaction, 90% in the ɑS plus control nanobody, and approximately 40% in the samples containing both ɑS and NbSyn87 or NbSyn2. The oligomers were formed in all samples, and comprised less than 2% of the samples of ɑS (Fig. 1d–g).\", \"Transmission electron microscopy (TEM) images of the samples at incubation times longer than 100 h confirmed the presence of abundant quantities of amyloid fibrils in the solutions containing ɑS alone or in the presence of NbHul5g and of NbSyn2, while only oligomers and short protofibrils were detected in the presence of NbSyn87 (Additional file 3: Figure S2b). These results confirm that the nanobodies inhibit ɑS fibril formation, and are therefore in good agreement with the bulk ThT fluorescence data and AFM results obtained for wt unlabeled ɑS as detailed above (Fig. 1b).\", \"These showed clear differences between the control samples and the samples containing ɑS-specific NbSyn2 and NbSyn87 (Fig. 2).\", \"Instead of exhibiting two populations at times longer than 24 h, however, the FRET histograms of oligomers formed in the presence of ɑS-specific nanobodies showed a single broad peak. The appearance of these histograms resembles those that had been obtained previously for ɑS solutions at low concentrations, in which high-FRET oligomers were not formed at high levels, yet were not fully absent [37]. Therefore, the appearance of the FRET efficiency histograms suggests that, in the presence of ɑS-specific nanobodies, the formation of high-FRET oligomers is impeded.\", \"NbSyn2 and NbSyn87 enhance the conversion of high-FRET into low-FRET oligomeric species\", \"The addition of NbSyn2 or NbSyn87 resulted in a reproducible decrease of the mean FRET efficiency values (Fig. 3b).\", \"Figure 3\", \"In the absence of nanobodies and upon addition of the control NbHul5g, the majority of the large oligomeric species observed in the experiment had FRET efficiency values above 0.6, characteristic of high-FRET oligomers (first two panels). Upon addition of either NbSyn2 (third panel) or NbSyn87 (fourth panel), the average FRET efficiency distributions shifted to lower values, an effect that was particularly pronounced in the presence of NbSyn87\", \"To determine whether or not the populations of oligomers formed in the presence of the nanobodies were more susceptible to proteinase K digestion than these formed in their absence, we exposed ɑS samples after 29 h of incubation under aggregating conditions to varying concentrations of proteinase K. The resulting digestion profiles are shown in Fig. 4a, and representative contour plots of FRET efficiencies and size distributions derived for individual samples in this assay are given in Additional file 6: Figure S5. From Fig. 4a, the populations of oligomeric species formed in the presence of NbSyn2 or NbSyn87 were more susceptible to proteinase K digestion than those formed in the presence of NbHul5g. \", \"These findings are completely consistent with the conclusion that the population of the more toxic high-FRET oligomer type is reduced during the aggregation process of ɑS in the presence of NbSyn87 and NbSyn2.\", \"In this study, we have characterized the key molecular steps that are altered by the ɑS-specific nanobodies, NbSyn2 and NbSyn87, during the aggregation reaction of ɑS. We have observed a clear effect of NbSyn2 and NbSyn87 on the formation of ɑS fibrils and their resulting morphology. In addition, using single-molecule fluorescence measurements we have identified a selective action of the nanobodies at the earliest stages of the aggregation reaction associated with the formation of toxic oligomeric species. In particular, both nanobodies were found to slow down the conformational conversion from less stable low-FRET oligomers to more stable high-FRET oligomers. Moreover, we observed that both NbSyn2 and NbSyn87 are able rapidly to convert pre-formed high-FRET oligomers to low-FRET species, indicating that the high-FRET oligomers are destabilized upon the binding of these nanobodies. \", \"It shows that nanobodies targeting the C-terminal region inhibit the aggregation of ɑS not only by inhibiting its aggregation and elongation processes, but also by inhibiting the conformational conversion of oligomers formed prior to fibril formation. \"",
    "Curator Statement": false
  },
  "AMGAB0689": {
    "Interaction ID": "AMGAB0689",
    "Antibody ID": "ABID0140",
    "Antibody name": "NbSyn2",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1186/s12915-017-0390-6",
    "PMID": 28673288.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Atomic force microscopy (AFM), Other: Quartz crystal microbalance experiments, Other: single molecule FRET (sm-FRET), Digestion experiments by proteinase K",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "H1: GIDSSSYCM, H2: RINGLGGVK, H3: KFSPGYCGGSWSNFGY",
    "Quote of the interaction": "\"We show that both nanobodies inhibit the formation of ɑS fibrils.\", \"We identified the ability of the nanobodies to inhibit the formation of ɑS fibrils and to destabilize toxic high-FRET oligomers of ɑS, and explored how the latter process affects oligomer-induced cytotoxicity.\", \"NbSyn2 and NbSyn87 inhibit the formation, maturation, and elongation of ɑS fibrils\", \"Figure 1\", \"In contrast, moderate inhibition of fibril formation was observed in the presence of NbSyn2, whereas solutions incubated in the presence of NbSyn87 gave rise to much lower ThT fluorescence signals over the entire duration of the experiment, indicating a stronger inhibition of ɑS fibril formation in the presence of this nanobody [13, 37]. In addition, we confirmed the inhibition of the formation of ThT-active aggregates in the presence of NbSyn2 and NbSyn87 by total internal reflection fluorescence microscopy imaging of the solutions extracted during the process of the aggregation reaction (Additional file 1: Figure S1).\", \"Figure S1\", \"In agreement with the findings from the ThT fluorescence assays, the images obtained in this way showed the presence of large numbers of amyloid fibrils in the solutions of ɑS that had been incubated in the absence of nanobodies or in the presence of NbHul5g or NbSyn2 (Fig. 1b). In the samples of ɑS incubated with NbSyn87, only small and apparently spherical aggregates along with monomeric species were observed, and no large fibrils could be detected (Fig. 1b). Comparison of average fibril heights from AFM maps revealed that fibrils formed in the presence of NbSyn2 were thinner than fibrils formed in the absence of nanobodies or in the presence of NbHul5g (Fig. 1c and Additional file 1: Figure S1), indicating that nanobodies impaired the maturation of ɑS fibrils. The differences in the fibril-forming capability of ɑS identified in the presence of the two ɑS-specific nanobodies might be due to the differences in the epitopes they bind.\", \"It was found that the elongation rate of ɑS fibrils markedly decreased in the presence of both ɑS-specific nanobodies, corresponding to 30–40% of the rate in their absence, as described in further detail in Additional file 2: Tables S3 and S4, and discussed in Additional file 2: Supplementary Results.\", \"Table S3\", \"Table S4\", \"Figure S2\", \"Figure S3\", \"Here, the histograms have been split into two populations of apparent sizes, small-mers (2–5 monomer units) and large-mers (6–150 monomer units). For large-mers, the differences in the FRET efficiency histograms are clearly observable, especially at times longer than 24 h. In the histograms of ɑS-only and ɑS with NbHul5g, the peak centered at the FRET efficiency value of 0.8 is dominant and corresponds to high-FRET oligomers. In the presence of both ɑS-specific nanobodies, the histograms are centered at the FRET efficiency value of 0.5, and the maximum at 0.8 is absent\", \"Figure 2\", \"The most rapid decrease in the monomer concentration, deduced from the monomer burst-rates [37], occurred in the samples containing 70 μM ɑS alone or in the presence of the control NbHul5g (Fig. 1d, e). However, samples containing NbSyn87 and NbSyn2 showed significantly slower monomer depletion. Based on the monomer depletion data derived from sm-FRET, after 30 h of aggregation, approximately 70% of the sample was aggregated in the ɑS-only reaction, 90% in the ɑS plus control nanobody, and approximately 40% in the samples containing both ɑS and NbSyn87 or NbSyn2. The oligomers were formed in all samples, and comprised less than 2% of the samples of ɑS (Fig. 1d–g).\", \"Transmission electron microscopy (TEM) images of the samples at incubation times longer than 100 h confirmed the presence of abundant quantities of amyloid fibrils in the solutions containing ɑS alone or in the presence of NbHul5g and of NbSyn2, while only oligomers and short protofibrils were detected in the presence of NbSyn87 (Additional file 3: Figure S2b). These results confirm that the nanobodies inhibit ɑS fibril formation, and are therefore in good agreement with the bulk ThT fluorescence data and AFM results obtained for wt unlabeled ɑS as detailed above (Fig. 1b).\", \"These showed clear differences between the control samples and the samples containing ɑS-specific NbSyn2 and NbSyn87 (Fig. 2).\", \"Instead of exhibiting two populations at times longer than 24 h, however, the FRET histograms of oligomers formed in the presence of ɑS-specific nanobodies showed a single broad peak. The appearance of these histograms resembles those that had been obtained previously for ɑS solutions at low concentrations, in which high-FRET oligomers were not formed at high levels, yet were not fully absent [37]. Therefore, the appearance of the FRET efficiency histograms suggests that, in the presence of ɑS-specific nanobodies, the formation of high-FRET oligomers is impeded.\", \"NbSyn2 and NbSyn87 enhance the conversion of high-FRET into low-FRET oligomeric species\",  The addition of NbSyn2 or NbSyn87 resulted in a reproducible decrease of the mean FRET efficiency values (Fig. 3b).\", \"Figure 3\", \"In the absence of nanobodies and upon addition of the control NbHul5g, the majority of the large oligomeric species observed in the experiment had FRET efficiency values above 0.6, characteristic of high-FRET oligomers (first two panels). Upon addition of either NbSyn2 (third panel) or NbSyn87 (fourth panel), the average FRET efficiency distributions shifted to lower values, an effect that was particularly pronounced in the presence of NbSyn87\", \"To determine whether or not the populations of oligomers formed in the presence of the nanobodies were more susceptible to proteinase K digestion than these formed in their absence, we exposed ɑS samples after 29 h of incubation under aggregating conditions to varying concentrations of proteinase K. The resulting digestion profiles are shown in Fig. 4a, and representative contour plots of FRET efficiencies and size distributions derived for individual samples in this assay are given in Additional file 6: Figure S5. From Fig. 4a, the populations of oligomeric species formed in the presence of NbSyn2 or NbSyn87 were more susceptible to proteinase K digestion than those formed in the presence of NbHul5g. \", \"These findings are completely consistent with the conclusion that the population of the more toxic high-FRET oligomer type is reduced during the aggregation process of ɑS in the presence of NbSyn87 and NbSyn2.\", \"In this study, we have characterized the key molecular steps that are altered by the ɑS-specific nanobodies, NbSyn2 and NbSyn87, during the aggregation reaction of ɑS. We have observed a clear effect of NbSyn2 and NbSyn87 on the formation of ɑS fibrils and their resulting morphology. In addition, using single-molecule fluorescence measurements we have identified a selective action of the nanobodies at the earliest stages of the aggregation reaction associated with the formation of toxic oligomeric species. In particular, both nanobodies were found to slow down the conformational conversion from less stable low-FRET oligomers to more stable high-FRET oligomers. Moreover, we observed that both NbSyn2 and NbSyn87 are able rapidly to convert pre-formed high-FRET oligomers to low-FRET species, indicating that the high-FRET oligomers are destabilized upon the binding of these nanobodies. \", \"It shows that nanobodies targeting the C-terminal region inhibit the aggregation of ɑS not only by inhibiting its aggregation and elongation processes, but also by inhibiting the conformational conversion of oligomers formed prior to fibril formation. \"",
    "Curator Statement": false
  },
  "AMGAB0690": {
    "Interaction ID": "AMGAB0690",
    "Antibody ID": "ABID0141",
    "Antibody name": "cAbHuL5g (NbHul5g)",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1186/s12915-017-0390-6",
    "PMID": 28673288.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Atomic force microscopy (AFM), Other: Quartz crystal microbalance experiments, Other: single molecule FRET (sm-FRET), Digestion experiments by proteinase K",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 1\", \"We show that both nanobodies inhibit the formation of ɑS fibrils.\", \"We identified the ability of the nanobodies to inhibit the formation of ɑS fibrils and to destabilize toxic high-FRET oligomers of ɑS, and explored how the latter process affects oligomer-induced cytotoxicity.\", \"NbSyn2 and NbSyn87 inhibit the formation, maturation, and elongation of ɑS fibrils\", \"Figure 1\", \"In contrast, moderate inhibition of fibril formation was observed in the presence of NbSyn2, whereas solutions incubated in the presence of NbSyn87 gave rise to much lower ThT fluorescence signals over the entire duration of the experiment, indicating a stronger inhibition of ɑS fibril formation in the presence of this nanobody [13, 37]. In addition, we confirmed the inhibition of the formation of ThT-active aggregates in the presence of NbSyn2 and NbSyn87 by total internal reflection fluorescence microscopy imaging of the solutions extracted during the process of the aggregation reaction (Additional file 1: Figure S1).\", \"Figure S1\", \"In agreement with the findings from the ThT fluorescence assays, the images obtained in this way showed the presence of large numbers of amyloid fibrils in the solutions of ɑS that had been incubated in the absence of nanobodies or in the presence of NbHul5g or NbSyn2 (Fig. 1b). In the samples of ɑS incubated with NbSyn87, only small and apparently spherical aggregates along with monomeric species were observed, and no large fibrils could be detected (Fig. 1b). Comparison of average fibril heights from AFM maps revealed that fibrils formed in the presence of NbSyn2 were thinner than fibrils formed in the absence of nanobodies or in the presence of NbHul5g (Fig. 1c and Additional file 1: Figure S1), indicating that nanobodies impaired the maturation of ɑS fibrils. The differences in the fibril-forming capability of ɑS identified in the presence of the two ɑS-specific nanobodies might be due to the differences in the epitopes they bind.\", It was found that the elongation rate of ɑS fibrils markedly decreased in the presence of both ɑS-specific nanobodies, corresponding to 30–40% of the rate in their absence, as described in further detail in Additional file 2: Tables S3 and S4, and discussed in Additional file 2: Supplementary Results.\", \"Table S3\", \"Table S4\", \"Figure S2\", \"Large amyloid fibrils and fibrillar fragments were observed in all samples at this time, except in the presence of NbSyn87, where short protofibrils were present along with oligomeric aggregates.\", \"Figure S3\", \"Here, the histograms have been split into two populations of apparent sizes, small-mers (2–5 monomer units) and large-mers (6–150 monomer units). For large-mers, the differences in the FRET efficiency histograms are clearly observable, especially at times longer than 24 h. In the histograms of ɑS-only and ɑS with NbHul5g, the peak centered at the FRET efficiency value of 0.8 is dominant and corresponds to high-FRET oligomers. In the presence of both ɑS-specific nanobodies, the histograms are centered at the FRET efficiency value of 0.5, and the maximum at 0.8 is absent\", \"Figure 2\", \"The most rapid decrease in the monomer concentration, deduced from the monomer burst-rates [37], occurred in the samples containing 70 μM ɑS alone or in the presence of the control NbHul5g (Fig. 1d, e). However, samples containing NbSyn87 and NbSyn2 showed significantly slower monomer depletion. Based on the monomer depletion data derived from sm-FRET, after 30 h of aggregation, approximately 70% of the sample was aggregated in the ɑS-only reaction, 90% in the ɑS plus control nanobody, and approximately 40% in the samples containing both ɑS and NbSyn87 or NbSyn2. The oligomers were formed in all samples, and comprised less than 2% of the samples of ɑS (Fig. 1d–g).\", \"Transmission electron microscopy (TEM) images of the samples at incubation times longer than 100 h confirmed the presence of abundant quantities of amyloid fibrils in the solutions containing ɑS alone or in the presence of NbHul5g and of NbSyn2, while only oligomers and short protofibrils were detected in the presence of NbSyn87 (Additional file 3: Figure S2b). These results confirm that the nanobodies inhibit ɑS fibril formation, and are therefore in good agreement with the bulk ThT fluorescence data and AFM results obtained for wt unlabeled ɑS as detailed above (Fig. 1b).\", \"These showed clear differences between the control samples and the samples containing ɑS-specific NbSyn2 and NbSyn87 (Fig. 2).\", \"For the samples of ɑS alone, and ɑS in the presence of control NbHul5g, two peaks could be observed in the FRET efficiency histograms of the large-mers (Fig. 2), corresponding to the two previously identified oligomer populations [13, 37, 38]. Low-FRET oligomers are characterized by a population centered at an average FRET efficiency value (E) of 0.5, and high-FRET oligomers are indicated by the peak centered at E value of approximately 0.8 (Fig. 2). The high-FRET population was clearly distinguishable after 24 h of aggregation and was dominant by 30 h of incubation both in the absence of nanobodies and in the presence of the control nanobody (Fig. 2), in good agreement with our previously reported kinetics of high-FRET oligomer formation [13, 37]. The mild acceleration of the formation of high-FRET species in the presence of the control nanobody NbHul5g compared to the ɑS-only sample might be due to the crowding effect or transient interactions of NbHul5g with ɑS.\", \"Figure 3\", \"In the absence of nanobodies and upon addition of the control NbHul5g, the majority of the large oligomeric species observed in the experiment had FRET efficiency values above 0.6, characteristic of high-FRET oligomers (first two panels). Upon addition of either NbSyn2 (third panel) or NbSyn87 (fourth panel), the average FRET efficiency distributions shifted to lower values, an effect that was particularly pronounced in the presence of NbSyn87\",  \"To determine whether or not the populations of oligomers formed in the presence of the nanobodies were more susceptible to proteinase K digestion than these formed in their absence, we exposed ɑS samples after 29 h of incubation under aggregating conditions to varying concentrations of proteinase K. The resulting digestion profiles are shown in Fig. 4a, and representative contour plots of FRET efficiencies and size distributions derived for individual samples in this assay are given in Additional file 6: Figure S5. From Fig. 4a, the populations of oligomeric species formed in the presence of NbSyn2 or NbSyn87 were more susceptible to proteinase K digestion than those formed in the presence of NbHul5g. \",",
    "Curator Statement": false
  },
  "AMGAB0691": {
    "Interaction ID": "AMGAB0691",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s12974-015-0379-4",
    "PMID": 26311039.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"After the incubation of preformed Aβ fibrils with the N-terminal antibody 6E10, the fibrils were decreased, while the oligomers, mostly dimers and trimers, were significantly increased.\", \"Antibody targeting the N-terminus of Aβ promoted the disaggregation of preformed Aβ fibrils\", \"After the incubation of preformed Aβ fibrils with N-terminal antibody 6E10, which targets amino acids 1–16 of Aβ, truncated fibrils and small aggregates of a variable size were observed in the TEM assay (Fig. 1a).\", \"This variance in the disaggregation ability of the antibodies was indicated by significantly lower area fractions of Aβ fibrils in the 6E10 group (P = 0.001 vs PBS) (Fig. 1b).\", \"An N-terminal antibody promotes the disaggregation of preformed Aβ fibrils\", \"Figure 1\", \"The ThT assay was conducted to further investigate the time-dependent disaggregation of Aβ fibrils induced by antibodies. Aβ42 monomers were aggregated for 48 h and then co-incubated with antibodies for an additional 72 h for disaggregation. We found that the fluorescence intensity induced by Aβ fibrils was significantly lower in 6E10-treated samples compared to 4G8- and 8G7-treated samples and the PBS controls (Fig. 1c).\", \"These data suggest that an antibody against the N-terminus of Aβ was able to disaggregate Aβ fibrils.\", \"We found that more dimers and trimers (P < 0.001 vs PBS) and fewer fibrils (P = 0.001 vs PBS) and aggregates with a molecular weight more than 30 kDa (P = 0.016 vs PBS) were observed in the 6E10-treated samples compared with the 4G8- and 8G7-treated samples (Fig. 1d, e). There was no difference in the amount of Aβ oligomers among the 4G8/8G7-treated samples and PBS controls. These findings suggest that an antibody against the N-terminus of Aβ facilitated the transformation of Aβ fibrils into Aβ oligomers.\", \"In the present study, for the first time, we found that an antibody against the N-terminus of Aβ, but not antibodies against the middle domain or the C-terminus of Aβ, disaggregated preformed Aβ fibrils, leading to the formation of oligomers and enhancing the neurotoxicity of Aβ both in vitro and in vivo.\", \"In the present study, we found that an antibody against the N-terminus of Aβ (6E10) promoted the transformation of Aβ fibrils into toxic oligomers, primarily Aβ dimers and trimers, which are the major toxic forms of Aβ [22, 23] that cause significant neuronal death in the brain of mice. \", \"In our present study, we found that an antibody targeting the N-terminus of Aβ, but not antibodies to the middle domain and C-terminus of Aβ, was able to disaggregate Aβ fibrils, suggesting that the therapeutic function of anti-Aβ antibodies are closely related to their antigen epitopes.\", \"In conclusion, the present study indicated that solubilization of Aβ fibrils by an antibody against the N-terminus of Aβ leads to the formation of more toxic Aβ oligomeric species.\",",
    "Curator Statement": false
  },
  "AMGAB0692": {
    "Interaction ID": "AMGAB0692",
    "Antibody ID": "ABID0142",
    "Antibody name": "4G8",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s12974-015-0379-4",
    "PMID": 26311039.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"However, after the incubation with 4G8, which targets amino acids 17–24 of Aβ, and 8G7, which targets the C-terminus of Aβ and PBS-treated samples, highly aggregated fibrils were observed under TEM.\", \"Figure 1\", \"The ThT assay was conducted to further investigate the time-dependent disaggregation of Aβ fibrils induced by antibodies. Aβ42 monomers were aggregated for 48 h and then co-incubated with antibodies for an additional 72 h for disaggregation. We found that the fluorescence intensity induced by Aβ fibrils was significantly lower in 6E10-treated samples compared to 4G8- and 8G7-treated samples and the PBS controls (Fig. 1c).\", \"We found that more dimers and trimers (P < 0.001 vs PBS) and fewer fibrils (P = 0.001 vs PBS) and aggregates with a molecular weight more than 30 kDa (P = 0.016 vs PBS) were observed in the 6E10-treated samples compared with the 4G8- and 8G7-treated samples (Fig. 1d, e). There was no difference in the amount of Aβ oligomers among the 4G8/8G7-treated samples and PBS controls. These findings suggest that an antibody against the N-terminus of Aβ facilitated the transformation of Aβ fibrils into Aβ oligomers.\", \"In the present study, for the first time, we found that an antibody against the N-terminus of Aβ, but not antibodies against the middle domain or the C-terminus of Aβ, disaggregated preformed Aβ fibrils, leading to the formation of oligomers and enhancing the neurotoxicity of Aβ both in vitro and in vivo.\", \"In our present study, we found that an antibody targeting the N-terminus of Aβ, but not antibodies to the middle domain and C-terminus of Aβ, was able to disaggregate Aβ fibrils, suggesting that the therapeutic function of anti-Aβ antibodies are closely related to their antigen epitopes.\"",
    "Curator Statement": false
  },
  "AMGAB0693": {
    "Interaction ID": "AMGAB0693",
    "Antibody ID": "ABID0142",
    "Antibody name": "4G8",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s12974-015-0379-4",
    "PMID": 26311039.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\"",
    "Curator Statement": false
  },
  "AMGAB0694": {
    "Interaction ID": "AMGAB0694",
    "Antibody ID": "ABID0143",
    "Antibody name": "8G7",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s12974-015-0379-4",
    "PMID": 26311039.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"However, after the incubation with 4G8, which targets amino acids 17–24 of Aβ, and 8G7, which targets the C-terminus of Aβ and PBS-treated samples, highly aggregated fibrils were observed under TEM.\", \"Figure 1\", \"The ThT assay was conducted to further investigate the time-dependent disaggregation of Aβ fibrils induced by antibodies. Aβ42 monomers were aggregated for 48 h and then co-incubated with antibodies for an additional 72 h for disaggregation. We found that the fluorescence intensity induced by Aβ fibrils was significantly lower in 6E10-treated samples compared to 4G8- and 8G7-treated samples and the PBS controls (Fig. 1c).\", \"We found that more dimers and trimers (P < 0.001 vs PBS) and fewer fibrils (P = 0.001 vs PBS) and aggregates with a molecular weight more than 30 kDa (P = 0.016 vs PBS) were observed in the 6E10-treated samples compared with the 4G8- and 8G7-treated samples (Fig. 1d, e). There was no difference in the amount of Aβ oligomers among the 4G8/8G7-treated samples and PBS controls. These findings suggest that an antibody against the N-terminus of Aβ facilitated the transformation of Aβ fibrils into Aβ oligomers.\", \"In the present study, for the first time, we found that an antibody against the N-terminus of Aβ, but not antibodies against the middle domain or the C-terminus of Aβ, disaggregated preformed Aβ fibrils, leading to the formation of oligomers and enhancing the neurotoxicity of Aβ both in vitro and in vivo.\", \"In our present study, we found that an antibody targeting the N-terminus of Aβ, but not antibodies to the middle domain and C-terminus of Aβ, was able to disaggregate Aβ fibrils, suggesting that the therapeutic function of anti-Aβ antibodies are closely related to their antigen epitopes.\"",
    "Curator Statement": false
  },
  "AMGAB0695": {
    "Interaction ID": "AMGAB0695",
    "Antibody ID": "ABID0143",
    "Antibody name": "8G7",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s12974-015-0379-4",
    "PMID": 26311039.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\"",
    "Curator Statement": false
  },
  "AMGAB0696": {
    "Interaction ID": "AMGAB0696",
    "Antibody ID": "ABID0022",
    "Antibody name": "Dezamizumab",
    "Amyloid ID": "AGAMYID0017",
    "Amyloid name": "Serum amyloid P-component",
    "DOI": "10.1186/s13023-022-02405-7",
    "PMID": 35810311.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "SAP scintigraphy (123I-SAP)",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Miridesap depletes circulating serum amyloid P (SAP) and dezamizumab (anti-SAP monoclonal antibody) targets SAP on amyloid deposits, triggering amyloid removal.\", \"In a phase 1, first-in-human study (FIHS), progressive amyloid removal was observed in some patients after ≤ 3 cycles of miridesap/dezamizumab.\", \"Table 3\", \"Table 4\", \"Amyloid load reduced or remained stable in most responders whether the response was sustained or declining, which suggests that amyloid load reduction or stabilization does not always correlate with functional improvement or preservation.\", \"The most striking reductions in amyloid observed in the FIHS were in the liver. Nine of the ten patients with hepatic involvement had AL amyloidosis, and five showed a sustained response (two of whom achieved this response despite clonal relapse). In these sustained responders (patients 107, 108, 110, 113 and 116), who showed improved/stable liver function during follow-up based on GGT levels, the reduction or stabilization of amyloid load achieved in the FIHS was maintained during follow-up.\", \"Long-term follow-up data from this study show that the reduction in amyloid load seen in the FIHS was mostly maintained; however, all but one of the patients with AFib experienced a gradual decline in eGFR typical of this form of amyloidosis, and it is not apparent that the treatment had any impact on the rate of eGFR decline.\", \"In this study, the patient with ApoAI experienced improved amyloid load during the FIHS, which fluctuated between stable and worse over follow-up. All five patients with AFib had hepatic involvement, and reductions in amyloid load were seen during the FIHS. However, during follow-up four of these patients experienced declining renal function that resulted in end-stage renal disease in one patient and consideration of dialysis in another.\", \"Patients with AL showing a clear response (as evidenced by reduction in organ amyloid on SAP scans in the FIHS) generally demonstrated a sustained or continued improvement in response through the follow-up period, unless they entered clonal relapse. In patients with hereditary-type amyloidosis, in whom the precursor protein is produced continually, reductions in amyloid deposits in kidney/spleen were seen in the FIHS but renal function continued to decline in most patients.\",",
    "Curator Statement": false
  },
  "AMGAB0697": {
    "Interaction ID": "AMGAB0697",
    "Antibody ID": "ABID0022",
    "Antibody name": "Dezamizumab",
    "Amyloid ID": "AGAMYID0017",
    "Amyloid name": "Serum amyloid P-component",
    "DOI": "10.1186/s13023-022-02405-7",
    "PMID": 35810311.0,
    "Impact of the antibody on amyloid formation": "No effect,",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "SAP scintigraphy (123I-SAP)",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 3\", \"Table 4\"",
    "Curator Statement": false
  },
  "AMGAB0698": {
    "Interaction ID": "AMGAB0698",
    "Antibody ID": "ABID0434",
    "Antibody name": "10D5",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1186/s13024-017-0156-1",
    "PMID": 28143566.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-Aβ immunization significantly reduced VAβ burden but increased the number of hemosiderin deposits across all APOE genotypes with the strongest and the weakest effect in APP/ε2 and APP/ε3 mice, respectively.\", \"Figure 4\", \"Figure 5\", \"There is noticeable reduction in the density of Aβ immunoreactive capillaries following 10D5 mAb treatment shown on the right panel. \", \"10D5 mAb treatment reduced the CAA load in the brain cortex in APP/ε3 and APP/ε4 mice by 56% (p < 0.05) and 71% (p < 0.01) relative to the mean CAA load value in TY11-15 controls of corresponding genotypes. However, given significantly higher CAA load baseline in APP/ε4 mice the absolute CAA load reduction in APP/ε4 mice was 2.5 fold higher than that in APP/ε3 mice. Thus, the CAA load in APP/ε4 animals was reduced from 0.41 ± 0.03% in TY11-15 controls to 0.11 ± 0.02% in 10D5 mAb treated group (absolute CAA load reduction = 0.30%) while in APP/ε3 mice the absolute reduction in the CAA load was 0.12%.\", \"10D5 mAb treatment effected significant CCA reduction across all three APOE genotypes. In the brain cortex of APP/ε2 and APP/ε3 mice the density of Aβ immunopositive capillary profiles was reduced approximately two-fold (p < 0.001 and p < 0.05; respectively), while in the brain cortex of APP/ε4 mice it was reduced by 1.6 fold (p < 0.05). 10D5 mAb treatment reduced CCA in the thalamus of APP/ε2 mice 8.5 fold (p < 0.0001). Marked reduction also was observed in the thalamus of APP/ε3 and APP/ε4 mice, but it did not reach statistical significance as the data did not conform to normal distribution hence weaker non-parametric statistical analysis was used.\", \"Both CAA load and CCA incidence were reduced in 10D5 mAb treated mice with the strongest effect on CAA load reduction seen in APPε4 animals and the strongest effect on CCA incidence seen in APP/ε2 mice.\",",
    "Curator Statement": false
  },
  "AMGAB0699": {
    "Interaction ID": "AMGAB0699",
    "Antibody ID": "ABID0434",
    "Antibody name": "10D5",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13024-017-0156-1",
    "PMID": 28143566.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-Aβ immunization decreased both the load of fibrillar plaques and the load of Aβ immunopositive plaques in mice of all APOE backgrounds. Although the relative reduction in parenchymal Aβ plaque load was comparable across all APOE genotypes, APP/ε4 mice showed the greatest reduction in the absolute Aβ plaque load values, given their highest baseline.\", \"Figure 1\", \"Figure 2\", \"10D5 mAb immunization decreased both fibrillar and immmunopositive Aβ parenchymal plaque loads. The degree of reduction relative to TY11-15 controls was comparable across all three APOE genotypes. Thus, the fibrillar plaque load in the brain cortex in 10D5 mAb treated APP/ε2, APP/ε3, APP/ε4 mice was reduced by 27.7% (p < 0.01), 24.4% (p < 0.01), and 22.7% (p < 0.0001) of the TY11-15 control mean value for matching APOE genotype (Fig. 1a, b), respectively; while the load of Aβ immunopositive plaques was reduced by 43.7% (p < 0.0001), 36.0% (p < 0.01), and 44.3% (p < 0.0001) (Fig. 2a, b), respectively. Similarly, the load of fibrillar plaques in the hippocampus of 10D5 mAb treated APP/ε2, APP/ε3, APP/ε4 mice was decreased by 26.7% (p < 0.05), 34.0% (p < 0.01), and 42.5% (p < 0.0001) of the TY11-15 control mean value for matching APOE genotype (Fig. 1a, c), respectively; while the load of Aβ immunopositive plaques was lowered by 38.7% (p < 0.001), 30.1% (p < 0.05), and 38.3% (p < 0.0001) (Fig. 2c, d), respectively. However, given significantly higher plaque load baseline in APP/ε4 mice, the absolute plaque load reduction effected by same dose of 10D5 mAb was incomparably higher in APP/ε4 mice than in other genotypes. Thus, the fibrillar plaque load in the brain cortex was reduced from 1.93 ± 0.05% of the cortical cross-sectional area in TY11-15 APP/ε4 controls to 1.49 ± 0.06% in 10D5 mAb treated APP/ε4 mice (absolute reduction = 0.44%), while the load of immunopositive Aβ plaques was reduced from 2.67 ± 0.07% to 1.49 ± 0.09% between TY11-15 and 10D5 mAb groups, respectively (absolute reduction = 1.18%). For comparison in APP/ε2 and APP/ε3 mice the absolute reduction in the fibrillar plaque load in the brain cortex was 0.17% and 0.18%, respectively; while the absolute reduction in the load of Aβ immunopositive plaques was 0.89% and 0.61%, respectively. Analogously, the fibrillar plaque load in the hippocampus of APP/ε4 mice was reduced from 1.08 ± 0.10% of the hippocampal cross-sectional area in TY11-15 controls to 0.62 ± 0.05% in 10D5 mAb treated mice (absolute reduction = 0.46%), while the load of immunopositive Aβ plaques was reduced from 2.43 ± 0.15% to 1.50 ± 0.14% between TY11-15 and 10D5 mAb groups, respectively (absolute reduction = 0.93%). In APP/ε2 and APP/ε3 mice the absolute reduction in fibrillar plaque load in the hippocampus was 0.11% and 0.18%, respectively; while the absolute reduction in the load of Aβ immunopositive plaques was 0.62% and 0.42%, respectively. Despite greater treatment effect seen in APP/ε4 mice, post-treatment load of both fibrillar and immunopositive Aβ parenchymal plaques in APP/ε4 mice remained significantly higher than these in 10D5 mAb treated APP/ε2 and APP/ε3 mice (Fig. 1b, c and Fig. 2b, d).\",\"Average values of parenchymal Aβ plaque loads revealed by 4G8 mAb immunostaining were 2.57% ± 0.10% and 1.49% ± 0.09 in TY11-15 control and 10D5 mAb treated APP/ε4 groups; respectively; and they were not significantly different from values obtained with HJ3.4 mAb for the same animal groups (Additional file 1: Fig. S1 A, B).\", \"Supplementary Figure S1\", \"Both CAA load and CCA incidence were reduced in 10D5 mAb treated mice with the strongest effect on CAA load reduction seen in APPε4 animals and the strongest effect on CCA incidence seen in APP/ε2 mice.\",",
    "Curator Statement": false
  },
  "AMGAB0700": {
    "Interaction ID": "AMGAB0700",
    "Antibody ID": "ABID0460",
    "Antibody name": "TY11-15",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1186/s13024-017-0156-1",
    "PMID": 28143566.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 4\", \"Figure 5\", \"Differences between Age control and TY11-15 control for matching APOE genotypes in (b) and (c) were non-significant; not shown on the graph.\", \"There was no significant difference in the CAA load between untreated age-matched and TY11-15 control mice for each of APOE genotypes analyzed.\",",
    "Curator Statement": false
  },
  "AMGAB0701": {
    "Interaction ID": "AMGAB0701",
    "Antibody ID": "ABID0460",
    "Antibody name": "TY11-15",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13024-017-0156-1",
    "PMID": 28143566.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 1\", \"Figure 2\", \"10D5 mAb immunization decreased both fibrillar and immmunopositive Aβ parenchymal plaque loads. The degree of reduction relative to TY11-15 controls was comparable across all three APOE genotypes. Thus, the fibrillar plaque load in the brain cortex in 10D5 mAb treated APP/ε2, APP/ε3, APP/ε4 mice was reduced by 27.7% (p < 0.01), 24.4% (p < 0.01), and 22.7% (p < 0.0001) of the TY11-15 control mean value for matching APOE genotype (Fig. 1a, b), respectively; while the load of Aβ immunopositive plaques was reduced by 43.7% (p < 0.0001), 36.0% (p < 0.01), and 44.3% (p < 0.0001) (Fig. 2a, b), respectively. Similarly, the load of fibrillar plaques in the hippocampus of 10D5 mAb treated APP/ε2, APP/ε3, APP/ε4 mice was decreased by 26.7% (p < 0.05), 34.0% (p < 0.01), and 42.5% (p < 0.0001) of the TY11-15 control mean value for matching APOE genotype (Fig. 1a, c), respectively; while the load of Aβ immunopositive plaques was lowered by 38.7% (p < 0.001), 30.1% (p < 0.05), and 38.3% (p < 0.0001) (Fig. 2c, d), respectively. However, given significantly higher plaque load baseline in APP/ε4 mice, the absolute plaque load reduction effected by same dose of 10D5 mAb was incomparably higher in APP/ε4 mice than in other genotypes. Thus, the fibrillar plaque load in the brain cortex was reduced from 1.93 ± 0.05% of the cortical cross-sectional area in TY11-15 APP/ε4 controls to 1.49 ± 0.06% in 10D5 mAb treated APP/ε4 mice (absolute reduction = 0.44%), while the load of immunopositive Aβ plaques was reduced from 2.67 ± 0.07% to 1.49 ± 0.09% between TY11-15 and 10D5 mAb groups, respectively (absolute reduction = 1.18%). For comparison in APP/ε2 and APP/ε3 mice the absolute reduction in the fibrillar plaque load in the brain cortex was 0.17% and 0.18%, respectively; while the absolute reduction in the load of Aβ immunopositive plaques was 0.89% and 0.61%, respectively. Analogously, the fibrillar plaque load in the hippocampus of APP/ε4 mice was reduced from 1.08 ± 0.10% of the hippocampal cross-sectional area in TY11-15 controls to 0.62 ± 0.05% in 10D5 mAb treated mice (absolute reduction = 0.46%), while the load of immunopositive Aβ plaques was reduced from 2.43 ± 0.15% to 1.50 ± 0.14% between TY11-15 and 10D5 mAb groups, respectively (absolute reduction = 0.93%). In APP/ε2 and APP/ε3 mice the absolute reduction in fibrillar plaque load in the hippocampus was 0.11% and 0.18%, respectively; while the absolute reduction in the load of Aβ immunopositive plaques was 0.62% and 0.42%, respectively. Despite greater treatment effect seen in APP/ε4 mice, post-treatment load of both fibrillar and immunopositive Aβ parenchymal plaques in APP/ε4 mice remained significantly higher than these in 10D5 mAb treated APP/ε2 and APP/ε3 mice (Fig. 1b, c and Fig. 2b, d).\", \"We found no statistically significant differences between values of fibrillar plaque loads in the brain cortex and in the hippocampus between TY11-15 isotype control IgG2a antibody treated mice and untreated age-matched mice for corresponding APOE genotypes (Fig. 1a-c). Likewise the loads of immunopositive Aβ plaques in TY11-15 control and untreated age-matched mice for corresponding APOE genotypes were similar (Fig. 2a-e).\", \"Average values of parenchymal Aβ plaque loads revealed by 4G8 mAb immunostaining were 2.57% ± 0.10% and 1.49% ± 0.09 in TY11-15 control and 10D5 mAb treated APP/ε4 groups; respectively; and they were not significantly different from values obtained with HJ3.4 mAb for the same animal groups (Additional file 1: Fig. S1 A, B).\", \"Supplementary Figure S1\",",
    "Curator Statement": false
  },
  "AMGAB0702": {
    "Interaction ID": "AMGAB0702",
    "Antibody ID": "ABID0284",
    "Antibody name": "DMR7",
    "Amyloid ID": "AGAMYID0023",
    "Amyloid name": "Tau",
    "DOI": "10.1186/s13024-020-00404-5",
    "PMID": 33148293.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vivo, In cellulo",
    "Experimental method(s)": "Immunohistochemistry, Confocal microscopy, Immunofluorescence-based neuronal seeding assays,",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We found that both DMR7 and SKT82 immunoprecipitate pathological tau and significantly reduce the seeding of cellular tau aggregates induced by AD-tau in primary neurons by 60.5 + 13.8% and 82.2 + 8.3%, respectively, compared to IgG control.\", \"These findings demonstrate that conformation-selective tau mAbs, DMR7 and SKT82, inhibit tau pathology in primary neurons by preventing the uptake of tau seeds and reduce tau pathology in vivo, providing potential novel therapeutic candidates for the treatment of AD.\", \"Figure 4\", \"Tau mAbs inhibit seeded fibrillization of endogenous tau in primary neurons\", \"Both DMR7 and SKT82 significantly reduced the seeding of pathological tau aggregates in a dose-dependent manner (Fig. 4a and b), with mouse tau pathology inhibited by 60.5 + 13.8% with DMR7 treatment and 82.2 + 8.3% by SKT82 addition. Both conformation-selective tau mAbs provided greater inhibition of AD-tau seeding in primary neurons than the pan-tau control antibody, Tau5.\", \"Figure 6\", \"Tau mAbs inhibit seeded aggregation of tau pathology in slice cultures.\", \"These studies further confirm that the conformation-selective tau mAbs can inhibit AD-tau seeding of mouse tau pathology in neurons, here utilizing a more complex culture system.\", \"We observed a strong trend toward reduced tau pathology in the contralateral hippocampus of DMR7- and SKT82-treated mice compared to their respective IgG1 and IgG2b controls, although this did not quite reach statistical significance using two-tailed unpaired Student’s t-tests (p = 0.069 and 0.077, respectively). There was a significant decrease in ipsilateral tau pathology in mice that received SKT82 compared to those dosed with IgG2b control mAb (p = 0.044), although a reduction of AT8 tau pathology was not observed in this region upon DMR7 treatment (Fig. 7c), consistent with SKT82 exhibiting greater efficacy in the slice culture model.\", \"Figure 7\", \"SKT82 and DMR7 inhibit tau pathology in vivo.\", \" Binding of SKT82 and DMR7 to tau seeds prevents their uptake into primary neurons and inhibits the seeded aggregation of tau in WT mouse primary neurons and hippocampal slice cultures. Utilizing 5xFAD mice that harbor Aβ plaques, human brain-derived AD-tau injection induces robust endogenous mouse tau pathology that is inhibited by both SKT82 and DMR7, with SKT82 causing a reduction of both ipsilateral and contralateral tau pathology as assessed by IHC and biochemical extraction of insoluble tau from treated mice.\", \"Based on the comparable binding affinities, selectivity, and epitopes of DMR7 and SKT82, it was somewhat surprising that SKT82 was more effective than DMR7 at inhibiting tau pathology in slice cultures and the ipsilateral hippocampus in vivo.\", \"Although there was high intergroup variability that reduced statistical power, DMR7 and SKT82 treatment of AD-tau injected 5xFAD mice nonetheless demonstrated similar efficacy to other tau-based passive immunotherapy approaches which generally result in a maximum of 50% reduction of AT8 pathological tau detected by IHC.\",\"Here, we demonstrate that DMR7 and SKT82 inhibit seeded aggregation of tau pathology in primary neurons by blocking the uptake of fluorescently-labeled tau seeds, consistent with mechanisms reported by others [19, 27, 32] .\", \"We observed that binding of DMR7 and SKT82 to conformational epitopes containing the C-terminus and proline-rich domain provided greater inhibition of seeded tau aggregation in neurons than Tau5, which targets the proline-rich central domain of tau.\", \"SKT82 and DMR7 reduce tau pathology in vitro and in an in vivo AD model with multiple neuropathological hallmarks of AD.\",",
    "Curator Statement": "Human seeds drive aggregation of mice tau"
  },
  "AMGAB0703": {
    "Interaction ID": "AMGAB0703",
    "Antibody ID": "ABID0285",
    "Antibody name": "SKT82",
    "Amyloid ID": "AGAMYID0023",
    "Amyloid name": "Tau",
    "DOI": "10.1186/s13024-020-00404-5",
    "PMID": 33148293.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vivo, In cellulo",
    "Experimental method(s)": "Immunohistochemistry, Confocal microscopy, Immunofluorescence-based neuronal seeding assays,",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We found that both DMR7 and SKT82 immunoprecipitate pathological tau and significantly reduce the seeding of cellular tau aggregates induced by AD-tau in primary neurons by 60.5 + 13.8% and 82.2 + 8.3%, respectively, compared to IgG control.\", \"These findings demonstrate that conformation-selective tau mAbs, DMR7 and SKT82, inhibit tau pathology in primary neurons by preventing the uptake of tau seeds and reduce tau pathology in vivo, providing potential novel therapeutic candidates for the treatment of AD.\", \"Figure 4\", \"Tau mAbs inhibit seeded fibrillization of endogenous tau in primary neurons\", \"Both DMR7 and SKT82 significantly reduced the seeding of pathological tau aggregates in a dose-dependent manner (Fig. 4a and b), with mouse tau pathology inhibited by 60.5 + 13.8% with DMR7 treatment and 82.2 + 8.3% by SKT82 addition. Both conformation-selective tau mAbs provided greater inhibition of AD-tau seeding in primary neurons than the pan-tau control antibody, Tau5.\", \"The seeding of AT8-positive tau inclusions by AD-tau is significantly inhibited by SKT82 and there is a trend towards reduction of pathology by DMR7 that did not achieve statistical significance (Fig. 6a and b).\", \"Figure 6\", \"Tau mAbs inhibit seeded aggregation of tau pathology in slice cultures.\", \"SKT82 inhibits tau pathology in slice culture\", \"These studies further confirm that the conformation-selective tau mAbs can inhibit AD-tau seeding of mouse tau pathology in neurons, here utilizing a more complex culture system.\", \"We observed a strong trend toward reduced tau pathology in the contralateral hippocampus of DMR7- and SKT82-treated mice compared to their respective IgG1 and IgG2b controls, although this did not quite reach statistical significance using two-tailed unpaired Student’s t-tests (p = 0.069 and 0.077, respectively). There was a significant decrease in ipsilateral tau pathology in mice that received SKT82 compared to those dosed with IgG2b control mAb (p = 0.044), although a reduction of AT8 tau pathology was not observed in this region upon DMR7 treatment (Fig. 7c), consistent with SKT82 exhibiting greater efficacy in the slice culture model.\", \"Figure 7\", \"SKT82 and DMR7 inhibit tau pathology in vivo.\", \" Binding of SKT82 and DMR7 to tau seeds prevents their uptake into primary neurons and inhibits the seeded aggregation of tau in WT mouse primary neurons and hippocampal slice cultures. Utilizing 5xFAD mice that harbor Aβ plaques, human brain-derived AD-tau injection induces robust endogenous mouse tau pathology that is inhibited by both SKT82 and DMR7, with SKT82 causing a reduction of both ipsilateral and contralateral tau pathology as assessed by IHC and biochemical extraction of insoluble tau from treated mice.\",  \"Based on the comparable binding affinities, selectivity, and epitopes of DMR7 and SKT82, it was somewhat surprising that SKT82 was more effective than DMR7 at inhibiting tau pathology in slice cultures and the ipsilateral hippocampus in vivo.\", \"Although there was high intergroup variability that reduced statistical power, DMR7 and SKT82 treatment of AD-tau injected 5xFAD mice nonetheless demonstrated similar efficacy to other tau-based passive immunotherapy approaches which generally result in a maximum of 50% reduction of AT8 pathological tau detected by IHC.\", \"Here, we demonstrate that DMR7 and SKT82 inhibit seeded aggregation of tau pathology in primary neurons by blocking the uptake of fluorescently-labeled tau seeds, consistent with mechanisms reported by others [19, 27, 32] .\", \"We observed that binding of DMR7 and SKT82 to conformational epitopes containing the C-terminus and proline-rich domain provided greater inhibition of seeded tau aggregation in neurons than Tau5, which targets the proline-rich central domain of tau.\", \"SKT82 and DMR7 reduce tau pathology in vitro and in an in vivo AD model with multiple neuropathological hallmarks of AD.\",",
    "Curator Statement": "Human seeds drive aggregation of mice tau"
  },
  "AMGAB0704": {
    "Interaction ID": "AMGAB0704",
    "Antibody ID": "ABID0286",
    "Antibody name": "Tau5",
    "Amyloid ID": "AGAMYID0023",
    "Amyloid name": "Tau",
    "DOI": "10.1186/s13024-020-00404-5",
    "PMID": 33148293.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Both DMR7 and SKT82 significantly reduced the seeding of pathological tau aggregates in a dose-dependent manner (Fig. 4a and b), with mouse tau pathology inhibited by 60.5 + 13.8% with DMR7 treatment and 82.2 + 8.3% by SKT82 addition. Both conformation-selective tau mAbs provided greater inhibition of AD-tau seeding in primary neurons than the pan-tau control antibody, Tau5.\", \"We observed that binding of DMR7 and SKT82 to conformational epitopes containing the C-terminus and proline-rich domain provided greater inhibition of seeded tau aggregation in neurons than Tau5, which targets the proline-rich central domain of tau.\",",
    "Curator Statement": false
  },
  "AMGAB0705": {
    "Interaction ID": "AMGAB0705",
    "Antibody ID": "ABID0170",
    "Antibody name": "mAb5",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13024-021-00453-4",
    "PMID": 33957936.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"mAb5 passive immunotherapy alone and expression of rAAV-Il6 significantly attenuated Aβ accumulation, whereas expression of rAAV-Il10 significantly increased Aβ accumulation.\", \"rAAV-Il6 in combination with mAb5 resulted in a significant decrease in Thioflavin S positive plaque counts compared to either intervention alone, but the effect was only slightly additive.\", \"In contrast, rAAV-Il10 preconditioning completely abrogated the beneficial effect of mAb5 immunotherapy on amyloid deposition.\", \"Both mAb5 and Il6 reduce Aβ load, though the extent to which they alter Aβ accumulation depends on the methodology used to assess deposition.\", \"When immunohistochemical methods were used to assess overall Aβ deposition only the combination of mAb5 and Il6 showed a significant reduction (p < 0.01, One-way Anova with Turkey’s multiple comparison test) (Fig. 3a, b).\", \"Reduction in Aβ levels was achieved with both Il-6 overexpression and with immunotherapy, although a synergistic effect was not observed.\", \"Figure 3\", \"When Thioflavin S was used to assess compact amyloid plaque number per section, there was a clear and significant reduction by Il6 alone and mAb5 in combination  with Il6 (p < 0.001 and p < 0.0001, respectively) (Fig. 3c, d). \", \"Notably, the combination of mAb5 and Il6 reduced plaque number to a greater extent as compared to either treatment alone (p < 0.0001 for mIL6 / mAb5 versus mAb5 alone and p < 0.01 versus Il6 alone).\", \"mAb5 immunotherapy alone decreased Aβ deposition to some degree without appreciable effect on astrocytes or microglial cells.\",",
    "Curator Statement": false
  },
  "AMGAB0706": {
    "Interaction ID": "AMGAB0706",
    "Antibody ID": "ABID0569",
    "Antibody name": "Anti-ac-tauK174 (Clone 1)",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1186/s13024-024-00733-9",
    "PMID": 38915105.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo, in cellulo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), FRET-based biosensor-cell assay,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-ac-tauK174 treatment mitigates neurobehavioral impairment and reduces tau pathology in PS19 mice.\", \"Anti-ac-K174 antibody (Clone 1) treatment yielded a trend towards reduced neuronal atrophy (Fig. 3A, B, p = 0.09) and decreased accumulation of pathological p-tau (S202/T205, AT8) deposition in the hippocampus (Fig. 3D, E, p = 0.08).\", \"Figure 3\", \"Anti-ac-tauK174 treatment ameliorates behavioral impairments and reduces tau seeding in vitro\", \"Figure 6\", \"Specifically, we seeded Tau RD HEK293T cells with PS19 lysate and observed a significant increase in CFP/YFP FRET signal with TBI and a downward trend with antibody treatment (p = 0.0634) (Fig. 6F, G). These findings highlight the functional benefits of anti-ac-tauK174 immunotherapy, which both prevents TBI-induced memory deficits in PS19 mice and reduces tau seeding and spreading in human cells.\", \"Treatment with anti-ac-tauK174 antibodies yielded promising results in reducing tau pathology, improving cognitive function, and mitigating inflammatory responses.\",",
    "Curator Statement": false
  },
  "AMGAB0707": {
    "Interaction ID": "AMGAB0707",
    "Antibody ID": "ABID0570",
    "Antibody name": "Anti-ac-tauK174 (Clone 2)",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1186/s13024-024-00733-9",
    "PMID": 38915105.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Anti-ac-tauK174 treatment mitigates neurobehavioral impairment and reduces tau pathology in PS19 mice.\",\"Figure 3\", \"Anti-ac-tauK174 antibody reduces fibril-induced tau spreading in PS19 mice\", \"Clone 2 treatment significantly reduced the amount of aggregated tau in the contralateral side, providing evidence that anti-ac-tauK174 immunotherapy reduces tau spreading in vivo (Fig. 3G, H).\", \"Treatment with anti-ac-tauK174 antibodies yielded promising results in reducing tau pathology, improving cognitive function, and mitigating inflammatory responses.\",",
    "Curator Statement": false
  },
  "AMGAB0708": {
    "Interaction ID": "AMGAB0708",
    "Antibody ID": "ABID0006.9",
    "Antibody name": "RmAb158-scFv8D3",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-018-0377-8",
    "PMID": 29793530.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET), ELISA",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"When compared with unmodified antibody, the results not only indicated an increased therapeutic efficacy but also suggested alternative clearance mechanisms, because the modified antibody was uniformly distributed in the entire brain volume, allowing it to access and clear a larger pool of soluble Aβ.\", \"RmAb158-scFv8D3 clears soluble Aβ protofibrils with tenfold lower dose\", \"Total Aβ burden was also assessed with IHC and quantified as the total area covered by Aβ40 reactive deposits in brain sections (Fig. 3e and f). There was no significant difference between the groups, which all displayed substantial variation between mice.\", \"Figure 3\", \"Total Aβ1–40 (c) and Aβ1–42 (d) in FA soluble brain extract revealed no significant differences between the treatment groups. e Aβ burden, determined with Aβ40 IHC, showed no significant differences between the groups in either cortex or hippocampus, although the interindividual variation was high.\", \" Mice pretreated with RmAb158-scFv8D3 showed significantly lower SUVRs in all investigated regions (p < 0.01–0.001) in comparison with PBS injected mice.\", \"Figure 4\", \"However, using RmAb158-scFv8D3, a bispecific variant of the antibody engineered to enable receptor-mediated transcytosis across the BBB [16], we obtained a similar Aβ reduction with only 10% of the dose (Fig. 3).\", \"Hence, both the unmodified RmAb158 and the bispecific RmAb158-scFv8D3 have the ability to reduce brain levels of soluble Aβ aggregates, but RmAb158-scFv8D3 seems to have a tenfold higher efficiency in eliminating its target from the brain.\",",
    "Curator Statement": false
  },
  "AMGAB0709": {
    "Interaction ID": "AMGAB0709",
    "Antibody ID": "ABID0006.9.2",
    "Antibody name": "RmAb158",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-018-0377-8",
    "PMID": 29793530.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET), ELISA",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"ELISA analysis of Tris-buffered saline brain extracts demonstrated a 40% reduction of soluble Aβ protofibrils in both RmAb158-scFv8D3- and high-dose RmAb158-treated mice, whereas there was no Aβ protofibril reduction in mice treated with a low dose of RmAb158. Further, ex vivo autoradiography and PET imaging revealed different brain distribution patterns of RmAb158-scFv8D3 and RmAb158, suggesting that these antibodies may affect Aβ levels by different mechanisms.\", \"When compared with unmodified antibody, the results not only indicated an increased therapeutic efficacy but also suggested alternative clearance mechanisms, because the modified antibody was uniformly distributed in the entire brain volume, allowing it to access and clear a larger pool of soluble Aβ.\", \"Total Aβ burden was also assessed with IHC and quantified as the total area covered by Aβ40 reactive deposits in brain sections (Fig. 3e and f). There was no significant difference between the groups, which all displayed substantial variation between mice.\", \"Figure 3\", \"Total Aβ1–40 (c) and Aβ1–42 (d) in FA soluble brain extract revealed no significant differences between the treatment groups. e Aβ burden, determined with Aβ40 IHC, showed no significant differences between the groups in either cortex or hippocampus, although the interindividual variation was high.\", \"RmAb158-pretreated mice showed reduced SUVRs compared with PBS mice, but to a lesser extent, and the decrease was significant only in the hippocampus (p < 0.05) and the cortex (p < 0.05) (Fig. 4b).\", \"Figure 4\",\"In the present study, we have demonstrated that a single injection of RmAb158, given at a high dose (320 nmol/kg), can efficiently reduce brain levels of soluble Aβ protofibrils, whereas a tenfold lower dose had no such effect.\", \"Hence, both the unmodified RmAb158 and the bispecific RmAb158-scFv8D3 have the ability to reduce brain levels of soluble Aβ aggregates, but RmAb158-scFv8D3 seems to have a tenfold higher efficiency in eliminating its target from the brain.\",",
    "Curator Statement": false
  },
  "AMGAB0710": {
    "Interaction ID": "AMGAB0710",
    "Antibody ID": "ABID0004",
    "Antibody name": "Crenezumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-018-0424-5",
    "PMID": 30231896.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"There was no evidence of a treatment effect in either the low-dose SC or the high-dose IV cohort for the predefined primary endpoint: change in SUVRCB (florbetapir PET) from baseline to week 69 (Fig. 2a, d).\", \"Using the exploratory analyses with white matter reference regions (SUVRBAI-WM and SUVRMNI-WM), the longitudinal variability observed in the primary analysis was reduced, and fewer placebo patients showed evidence of amyloid reduction (Additional file 2: Figure S1B, C, E, F). There was a nonsignificant trend toward treatment difference observed in the high-dose IV cohort of 0.024 (95% CI –0.011 to 0.060; unadjusted p = 0.169) for SUVRBAI-WM, representing a 30% reduction in amyloid accumulation relative to placebo (Fig. 2e). Similarly, in the high-dose IV cohort, a nonsignificant trend toward treatment difference of 0.015 (95% CI –0.005 to 0.035; unadjusted p = 0.131) was observed for SUVRMNI-WM, representing a 60% reduction in amyloid accumulation relative to placebo (Fig. 2f). No treatment effect was observed in the low-dose SC cohort for SUVRMNI-WM and SUVRBAI-WM.\", \"No significant treatment effects were observed for any of the MRI-derived volumetric changes (hippocampus, ventricles, whole brain) from baseline to week 73 in either the low-dose SC or high-dose IV cohorts (Additional file 3: Figure S2). There was also no significant treatment effect observed in mean FDG PET SUVR changes from baseline to week 69 in either cohort (Additional file 4: Figure S3).\", \"Here we report the results of the phase II ABE4955g trial evaluating the impact of crenezumab on brain amyloid load and related biomarkers in mild-to-moderate AD with evidence of brain amyloid pathology based on amyloid PET. The primary endpoint was not met. Exploratory analyses evaluated two alternative methods of analyzing longitudinal amyloid PET data using different reference regions. These methods reduced longitudinal variability and suggested a possible reduction in amyloid accumulation in crenezumab-treated patients.\",",
    "Curator Statement": false
  },
  "AMGAB0711": {
    "Interaction ID": "AMGAB0711",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-018-0447-y",
    "PMID": 30486882.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Monomers, Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 3\", \"A 4-month chronic treatment with SAR255952 (10 mg/kg) significantly decreased guanidine-solubilized pan-Aβ levels (−41% at 10 mg/kg, p < 0.01) versus Ctl-IgG1-treated controls in the cortex while a nonsignificant trend was observed at 3 mg/kg (−25%) and no effect at 1 mg/kg (+6%) (Table 3). In comparison, the reference 3D6 (10 mg/kg) decreased cortical pan-Aβ levels (−43%, p < 0.05) while the dose of 3 mg/kg was inactive (Table 3).\", \"SAR255952 treatment did not significantly decrease guanidine-solubilized cortical Aβ42 levels (+16%, not significant at 1 mg/kg; −13%, not significant at 3 mg/kg; −31%, not significant at 10 mg/kg) versus Ctl-IgG1-treated controls (Table 3), nor did the reference 3D6 (+11%, not significant at 3 mg/kg; −35%, not significant at 10 mg/kg).\", \"Figure 3\", \"a Whole scanned Aβ-immunostained sagittal brain tissue section illustrating the decrease in the extracellular Aβ peptide deposition process in both cortical and hippocampal brain areas of representative mice chronically treated either with SAR255952 or 3D6, with respect to Ctrl-IgG1-treated mice.\", \"Statistical analysis of both histological and biochemical measurements denotes the significant effect of SAR255952 at 3 and 10 mg/kg injected doses in the cortex. The 3D6 effect is significant at 10 mg/kg.\", \" 3D6 treatment at the dose of 10 mg/kg also led to a marked decrease (−60%, p = 0.003) in extracellular Aβ peptide deposition in the cortex but was inactive at 3 mg/kg (+1%, not significant, Fig. 3a). In the hippocampus, the decreases were −41% (p = 0.012) at 10 mg/kg and −25% (not significant, p = 0.089) at 3 mg/kg (Table 2).\", \"Using murine versions, SAR255952 (aglycosylated mIgG1 with very low effector functions) was even moderately more potent than a 3D6 mIgG2a control (murine bapineuzumab) and only minimally less potent than the complete mIgG1 version of SAR255952 (data not shown), the latter two possessing significant high effector functions. Along with amyloid plaque lowering, microglial and astrocyte inflammation were decreased as well as plaque-associated dystrophic neurites, leading to improved synaptic function in the hippocampus.\",",
    "Curator Statement": "The different effect is due to the dose applied, while 10 mg/kg decreased amyloid deposition, 3 mg/kg did not."
  },
  "AMGAB0712": {
    "Interaction ID": "AMGAB0712",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-018-0447-y",
    "PMID": 30486882.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Monomers, Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 3\", \" In comparison, the reference 3D6 (10 mg/kg) decreased cortical pan-Aβ levels (−43%, p < 0.05) while the dose of 3 mg/kg was inactive (Table 3).\", \"SAR255952 treatment did not significantly decrease guanidine-solubilized cortical Aβ42 levels (+16%, not significant at 1 mg/kg; −13%, not significant at 3 mg/kg; −31%, not significant at 10 mg/kg) versus Ctl-IgG1-treated controls (Table 3), nor did the reference 3D6 (+11%, not significant at 3 mg/kg; −35%, not significant at 10 mg/kg).\", \"Figure 3\", \" 3D6 treatment at the dose of 10 mg/kg also led to a marked decrease (−60%, p = 0.003) in extracellular Aβ peptide deposition in the cortex but was inactive at 3 mg/kg (+1%, not significant, Fig. 3a). In the hippocampus, the decreases were −41% (p = 0.012) at 10 mg/kg and −25% (not significant, p = 0.089) at 3 mg/kg (Table 2).\",",
    "Curator Statement": "The different effect is due to the dose applied, while 10 mg/kg decreased amyloid deposition, 3 mg/kg did not."
  },
  "AMGAB0713": {
    "Interaction ID": "AMGAB0713",
    "Antibody ID": "ABID0012",
    "Antibody name": "SAR228810",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-018-0447-y",
    "PMID": 30486882.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 4\",\"Quantification of brain Aβ peptide deposition by immunohistochemistry confirmed that immunotolerization by itself had not affected Aβ peptide deposition in APPSL transgenic mice. When compared with Ctl-IgG1, treatments with SAR228810 and SAR255952 markedly reduced extracellular Aβ peptide deposition in the cortex (−63%, p = 0.0009, and −65%, p = 0.0015, respectively, Table 4), in the hippocampus (−67%, p = 0.0016, and −73%, p = 0.0005, respectively, Fig. 7), and in the thalamus (−83%, p = 0.0004, and −71%, p = 0.0074, respectively) (data not shown).\", \"Figure 7\", \"a Representative whole-scanned Aβ-immunostained sagittal brain tissue section illustrating the decrease in the extracellular Aβ peptide deposition process in cortical, hippocampal, and thalamic brain areas in representative immunotolerized mice chronically treated either with SAR255952 or SAR228810, in respect to immunotolerized or not Ctrl-igG1-treated mice.\", \"The humanized IgG4 antibody SAR228810 therefore had a similar activity at preventing amyloid plaque deposition than the mouse aglycosylated SAR255952, strongly suggesting that low to very low effector functions were sufficient to maintain in-vivo efficacy.\", \"To limit the risk of ARIA, SAR228810 was engineered with a double mutant human IgG4 Fc domain to endow drastically reduced effector functions which did not compromise its activity at preventing amyloid plaque development in vivo.\", \"Of note, the human antibody SAR228810 was also shown in vivo to have similar activity as murine SAR255952 using immunotolerized mice.\", \"Translating to human AD clinical studies where patients have a high cerebral amyloid deposition many years prior to the onset of symptoms, we are aware that the efficacy of SAR228810 was demonstrated only as a prevention of plaque accumulation and synaptic dysfunction but not for reduction of preexisting amyloid plaque load in the very aggressive APP transgenic line used.\", \"SAR228810 and its murine version can neutralize synthetic oAβ neurotoxicity and in animal models prevent amyloid plaque accumulation, related inflammation, and synaptic dysfunction.\"",
    "Curator Statement": false
  },
  "AMGAB0714": {
    "Interaction ID": "AMGAB0714",
    "Antibody ID": "ABID0012.5.2",
    "Antibody name": "SAR255952",
    "Amyloid ID": "AGAMYID0001",
    "Amyloid name": "Aβ-38",
    "DOI": "10.1186/s13195-018-0447-y",
    "PMID": 30486882.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA, Biochemical extraction",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Additional file 1 Table S2\", \"SAR255952 prevents accumulation the three Aβ subspecies, Aβ38, Aβ40 and Aβ42 in soluble and insoluble brain fractions in APPSL transgenic mice.\"",
    "Curator Statement": false
  },
  "AMGAB0715": {
    "Interaction ID": "AMGAB0715",
    "Antibody ID": "ABID0012.5.2",
    "Antibody name": "SAR255952",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1186/s13195-018-0447-y",
    "PMID": 30486882.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA, Biochemical extraction",
    "Amyloid species identified": "Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Additional file 1 Table S2\", \"SAR255952 prevents accumulation the three Aβ subspecies, Aβ38, Aβ40 and Aβ42 in soluble and insoluble brain fractions in APPSL transgenic mice.\"",
    "Curator Statement": false
  },
  "AMGAB0716": {
    "Interaction ID": "AMGAB0716",
    "Antibody ID": "ABID0012.5.2",
    "Antibody name": "SAR255952",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-018-0447-y",
    "PMID": 30486882.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In vivo, SAR255952, a mouse aglycosylated IgG1, dose-dependently prevented brain amyloid plaque formation and plaque-related inflammation with a minimal active dose of 3 mg/kg/week by the intraperitoneal route.\", \"Table 4\", \"Table 3\", \"A 4-month chronic treatment with SAR255952 (10 mg/kg) significantly decreased guanidine-solubilized pan-Aβ levels (−41% at 10 mg/kg, p < 0.01) versus Ctl-IgG1-treated controls in the cortex while a nonsignificant trend was observed at 3 mg/kg (−25%) and no effect at 1 mg/kg (+6%) (Table 3). In comparison, the reference 3D6 (10 mg/kg) decreased cortical pan-Aβ levels (−43%, p < 0.05) while the dose of 3 mg/kg was inactive (Table 3).\", \"SAR255952 treatment did not significantly decrease guanidine-solubilized cortical Aβ42 levels (+16%, not significant at 1 mg/kg; −13%, not significant at 3 mg/kg; −31%, not significant at 10 mg/kg) versus Ctl-IgG1-treated controls (Table 3), nor did the reference 3D6 (+11%, not significant at 3 mg/kg; −35%, not significant at 10 mg/kg).\", \"In an independent in-vivo study comparing Ctr-IgG1 and SAR255952 at the dose of 10 mg/kg in a similar 4-month treatment, differential extraction of soluble, membrane, and insoluble fractions demonstrated that SAR255952 led to a comparable decrease in soluble and insoluble fractions of all three Aβ subspecies (Aβ38, Aβ40, and Aβ42) (Additional file 1: Table S2).\", \"Additional file 1 Table S2\", \"SAR255952 prevents accumulation the three Aβ subspecies, Aβ38, Aβ40 and Aβ42 in soluble and insoluble brain fractions in APPSL transgenic mice.\", \"Figure 3\", \"Chronic treatment with SAR255952 prevents amyloid β (Aβ) peptide plaque deposition and brain microglial activation in APPSL transgenic Alzheimer’s mice. \", \"a Whole scanned Aβ-immunostained sagittal brain tissue section illustrating the decrease in the extracellular Aβ peptide deposition process in both cortical and hippocampal brain areas of representative mice chronically treated either with SAR255952 or 3D6, with respect to Ctrl-IgG1-treated mice.\", \"Statistical analysis of both histological and biochemical measurements denotes the significant effect of SAR255952 at 3 and 10 mg/kg injected doses in the cortex. The 3D6 effect is significant at 10 mg/kg.\", \"In SAR255952-treated mice, quantitative analysis evidenced a dose-dependent decrease in the total surface occupied by Aβ immunostaining in extracellular deposits in both cortical and hippocampal brain areas. The decrease in extracellular Aβ peptide deposition in the cortex was −78% (p < 0.0001) at 10 mg/kg, −51% (p = 0.013) at 3 mg/kg, and 11% (not significant) at 1 mg/kg compared with the Ctl-IgG1-treated control group (Table 3, Fig. 3a). In the hippocampus, the decrease was −80% (p < 0.0001) at 10 mg/kg, −59% (p = 0.012) at 3 mg/kg, and 35% (not significant) at 1 mg/kg (Table 3).\", \"These data indicated that a protofibrillar Aβ-specific antibody with much reduced effector functions was at least as effective as a pan-Aβ antibody with full effector function at preventing Aβ peptide deposition and related inflammation.\", \"Quantification of brain Aβ peptide deposition by immunohistochemistry confirmed that immunotolerization by itself had not affected Aβ peptide deposition in APPSL transgenic mice. When compared with Ctl-IgG1, treatments with SAR228810 and SAR255952 markedly reduced extracellular Aβ peptide deposition in the cortex (−63%, p = 0.0009, and −65%, p = 0.0015, respectively, Table 4), in the hippocampus (−67%, p = 0.0016, and −73%, p = 0.0005, respectively, Fig. 7), and in the thalamus (−83%, p = 0.0004, and −71%, p = 0.0074, respectively) (data not shown).\", \"Figure 7\", \"a Representative whole-scanned Aβ-immunostained sagittal brain tissue section illustrating the decrease in the extracellular Aβ peptide deposition process in cortical, hippocampal, and thalamic brain areas in representative immunotolerized mice chronically treated either with SAR255952 or SAR228810, in respect to immunotolerized or not Ctrl-igG1-treated mice.\", \"The humanized IgG4 antibody SAR228810 therefore had a similar activity at preventing amyloid plaque deposition than the mouse aglycosylated SAR255952, strongly suggesting that low to very low effector functions were sufficient to maintain in-vivo efficacy.\", \"Using murine versions, SAR255952 (aglycosylated mIgG1 with very low effector functions) was even moderately more potent than a 3D6 mIgG2a control (murine bapineuzumab) and only minimally less potent than the complete mIgG1 version of SAR255952 (data not shown), the latter two possessing significant high effector functions. Along with amyloid plaque lowering, microglial and astrocyte inflammation were decreased as well as plaque-associated dystrophic neurites, leading to improved synaptic function in the hippocampus.\", \"SAR228810 and its murine version can neutralize synthetic oAβ neurotoxicity and in animal models prevent amyloid plaque accumulation, related inflammation, and synaptic dysfunction.\",",
    "Curator Statement": "The different effect is due to the dose applied, while 10 mg/kg decreased amyloid deposition, 3 mg/kg did not."
  },
  "AMGAB0717": {
    "Interaction ID": "AMGAB0717",
    "Antibody ID": "ABID0012.5.2",
    "Antibody name": "SAR255952",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-018-0447-y",
    "PMID": 30486882.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 3\", \"A 4-month chronic treatment with SAR255952 (10 mg/kg) significantly decreased guanidine-solubilized pan-Aβ levels (−41% at 10 mg/kg, p < 0.01) versus Ctl-IgG1-treated controls in the cortex while a nonsignificant trend was observed at 3 mg/kg (−25%) and no effect at 1 mg/kg (+6%) (Table 3). In comparison, the reference 3D6 (10 mg/kg) decreased cortical pan-Aβ levels (−43%, p < 0.05) while the dose of 3 mg/kg was inactive (Table 3).\", \"SAR255952 treatment did not significantly decrease guanidine-solubilized cortical Aβ42 levels (+16%, not significant at 1 mg/kg; −13%, not significant at 3 mg/kg; −31%, not significant at 10 mg/kg) versus Ctl-IgG1-treated controls (Table 3), nor did the reference 3D6 (+11%, not significant at 3 mg/kg; −35%, not significant at 10 mg/kg).\",",
    "Curator Statement": "The different effect is due to the dose applied, while 10 mg/kg decreased amyloid deposition, 3 mg/kg did not."
  },
  "AMGAB0718": {
    "Interaction ID": "AMGAB0718",
    "Antibody ID": "ABID0002",
    "Antibody name": "Gantenerumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-019-0559-z",
    "PMID": 31831056.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Mean amyloid levels were reduced by 39 Centiloids by the first year and 59 Centiloids by year 2, a 3.5-times greater reduction than was seen after 2 years at 225 mg in SR. At years 1 and 2, 37% and 51% of patients, respectively, had amyloid-β plaque levels below the amyloid-β positivity threshold.\", \"Results from this exploratory interim analysis of the PET substudy suggest that gantenerumab doses up to 1200 mg resulted in robust amyloid-β plaque removal at 2 years. PET amyloid levels were consistent with sparse-to-no neuritic amyloid-β plaques in 51% of patients after 2 years of therapy.\", \"Gantenerumab markedly reduced brain amyloid-β plaque levels\", \"The reduction in amyloid PET was significant in all subgroups and at all time points. Mean (SE) PET Centiloid reductions from baseline were − 42 (7.1), − 48 (8.0), and − 21 (8.3) at week 52 and − 71 (7.7), − 61 (8.9), and − 34 (8.9) at week 104 in the MR-DBP, MR-DBA, and SR groups, respectively (Fig. 1); consistent results were observed for week 104 completers (Additional file 1: Table S1).\", \"Individually, all week 104 completers had reduced amyloid, with reductions ranging from 11 to 169 Centiloids, and 51% of patients had amyloid levels below the positivity threshold at week 104 (Fig. 1b). A strong correlation was seen between higher amyloid load at OLE baseline and greater amyloid reduction during the first year of gantenerumab treatment (Additional file 5: Figure S3). Large regional reductions were seen throughout the brain regions primarily involved in AD, with the greatest reductions observed in the anterior cingulate (Additional file 6: Figure S4).\", \"Figure 1\", \"Marked and consistent reduction of amyloid load in patients receiving high-dose gantenerumab. a Marked reduction of amyloid-β plaques in patients receiving high-dose gantenerumab, and consistent reduction of amyloid-β plaques in all patient groups. b Reduction of amyloid-β plaque burden to below positivity threshold following high-dose gantenerumab.\", \"Figure 2\", \"Amyloid-β plaque reduction with gantenerumab. Axial florbetapir brain PET images from five patients displaying reduction of amyloid-β plaques from OLE baseline to OLE week 52 and OLE week 104.\", \"Table 2\", \"This PET substudy of the MR and SR OLE studies investigated the effect of higher-dose gantenerumab on amyloid-β plaques over 104 weeks in patients with prodromal to moderate AD dementia. Reductions in PET values to below the amyloid-β positivity threshold were achieved in 37% of patients at week 52 and 51% at week 104, suggesting that amyloid-β plaques can be reduced to levels that would not support a neuropathological diagnosis of AD [34]. In addition, amyloid reductions were consistently observed across most patients, indicating that gantenerumab has the potential to reduce amyloid-β plaques as suggested by its proposed mechanism of action of preferential binding to amyloid-β aggregates and consequent plaque removal.\", \"Regional analyses indicate that amyloid reductions are fairly uniform throughout the regions of the brain known to have amyloid, indicating that sufficient blood-brain barrier penetration of gantenerumab has occurred to effect globally large amyloid reductions.\", \"We have shown that gantenerumab reduces amyloid-β plaques, one of the main pathological hallmarks of AD. \", \"Table S1\",  \"Reduction in Amyloid Load in Patients Receiving High-Dose Gantenerumab (Week 104 Completers). Findings in Week 104 completers show continued reduction in amyloid load across groups over 104 weeks, consistent with the overall group.\", \"Figure S3\", \"Correlation Between Amyloid Load at OLE Baseline and Amyloid Change Over Time. Rate of amyloid reduction during the first year of gantenerumab treatment appears to be linked to baseline amyloid burden. Higher rates of amyloid reduction are seen with greater baseline burden.\", \"Figure S4\", \"Regional Reductions in Amyloid Load. Amyloid reductions are seen in all regions known to be involved with amyloid pathology. Highest reductions are seen in the cingulate, frontal, and striatum areas. When adjusted for baseline amyloid burden, the caudate region shows the greatest regional reduction.\"",
    "Curator Statement": false
  },
  "AMGAB0719": {
    "Interaction ID": "AMGAB0719",
    "Antibody ID": "ABID0172",
    "Antibody name": "07/2a",
    "Amyloid ID": "AGAMYID0001",
    "Amyloid name": "Aβ-38",
    "DOI": "10.1186/s13195-019-0579-8",
    "PMID": 31931873.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"07/2a IgG2a and 3A1 IgG1 mAb’s lowered guanidine-HCl-extracted Aβ in aged APPSWE/PS1ΔE9 mice.\",\"Significant decreases in guanidine-HCl-extracted pGlu-3 Aβ (p < 0.05), Aβx-42 (p < 0.01), Aβx-40 (p < 0.05), and Aβx-38 (p < 0.05) were observed in Tg mice treated with 07/2a IgG2a mAb compared to PBS-treated Tg mice (a–d).\", \"07/2a treatment reduced guanidine-HCl-extracted Aβ levels in brain homogenates\", \"Biochemical analysis of guanidine-HCl-extracted Aβ from whole brain (excluding cerebellum) homogenates demonstrated a significantly reduced concentration of pGlu-3Aβ in the insoluble fraction from 07/2a-treated Tg mice compared to Tg PBS control mice (p < 0.05) (Fig. 3a). The levels of insoluble Aβx-42 were significantly lower in the 07/2a- and 3A1-treated mice compared with Tg PBS-injected mice (p < 0.05) (Fig. 3b). In addition, 07/2a-treated mice had significantly lower Aβx-40 (p < 0.05) and Aβx-38 (p < 0.05) in the insoluble Aβ fraction relative to Tg PBS control mice (Fig. 3c, d). A trend for reduction in Aβx-40 and Aβx-42 was observed by 3A1-treated mice compared to PBS-injected Tg mice and was significant when compared to PBS controls by Student’s t test (p < 0.05) (Fig. 3c, d). \",",
    "Curator Statement": false
  },
  "AMGAB0720": {
    "Interaction ID": "AMGAB0720",
    "Antibody ID": "ABID0172",
    "Antibody name": "07/2a",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1186/s13195-019-0579-8",
    "PMID": 31931873.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"07/2a IgG2a and 3A1 IgG1 mAb’s lowered guanidine-HCl-extracted Aβ in aged APPSWE/PS1ΔE9 mice.\",\"Significant decreases in guanidine-HCl-extracted pGlu-3 Aβ (p < 0.05), Aβx-42 (p < 0.01), Aβx-40 (p < 0.05), and Aβx-38 (p < 0.05) were observed in Tg mice treated with 07/2a IgG2a mAb compared to PBS-treated Tg mice (a–d).\", \"07/2a treatment reduced guanidine-HCl-extracted Aβ levels in brain homogenates\", \"Biochemical analysis of guanidine-HCl-extracted Aβ from whole brain (excluding cerebellum) homogenates demonstrated a significantly reduced concentration of pGlu-3Aβ in the insoluble fraction from 07/2a-treated Tg mice compared to Tg PBS control mice (p < 0.05) (Fig. 3a). The levels of insoluble Aβx-42 were significantly lower in the 07/2a- and 3A1-treated mice compared with Tg PBS-injected mice (p < 0.05) (Fig. 3b). In addition, 07/2a-treated mice had significantly lower Aβx-40 (p < 0.05) and Aβx-38 (p < 0.05) in the insoluble Aβ fraction relative to Tg PBS control mice (Fig. 3c, d). A trend for reduction in Aβx-40 and Aβx-42 was observed by 3A1-treated mice compared to PBS-injected Tg mice and was significant when compared to PBS controls by Student’s t test (p < 0.05) (Fig. 3c, d). \",",
    "Curator Statement": false
  },
  "AMGAB0721": {
    "Interaction ID": "AMGAB0721",
    "Antibody ID": "ABID0172",
    "Antibody name": "07/2a",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-019-0579-8",
    "PMID": 31931873.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo, in vitro",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Effector function of anti-pyroglutamate-3 Aβ antibodies affects cognitive benefit, glial activation and amyloid clearance in Alzheimer’s-like mice\", \"We demonstrated significant cognitive improvement, better plaque clearance, and more plaque-associated microglia in the absence of microhemorrhage in aged APPSWE/PS1ΔE9 Tg mice treated with 07/2a, but not 07/1 or 3A1, compared to PBS in our first in vivo study.\", \"All mAbs cleared plaques in an ex vivo assay, although 07/2a promoted the highest phagocytic activity. \", \" Treatment of APPSLxhQC mice with 07/2a and 07/2a-k mAbs in our second in vivo study showed significant plaque-lowering with both mAbs.\", \"Our results suggest that attenuation of behavioral deficits and clearance of amyloid is associated with strong effector function of the anti-pGlu-3 Aβ mAb in a therapeutic treatment paradigm.\", \"07/2a mAb immunotherapy reduced total Aβ plaque burden in aged APPSWE/PS1ΔE9 Tg mice\", \"Figure 2\", \"Quantitative image analysis on six stained sections at thee equidistant planes per marker demonstrated that there was a significant reduction of pGlu-3 Aβ (p < 0.001), general Aβ (p < 0.05), and fibrillar amyloid (p < 0.05) in the hippocampus of Tg mice immunized with 07/2a IgG2a mAb compared to Tg mice treated with PBS (q–t). Similarly, there was a significant reduction of pGlu-3 Aβ (p < 0.05), general Aβ, fibrillar amyloid, and Aβ1−x (p < 0.05) in the cortex of the Tg mice immunized with 07/2a IgG2a mAb compared to Tg mice treated with PBS (u–x).\", \"07/2a-specific significant reductions were also observed for general Aβ deposition in the HC (p < 0.05) and CTX (p < 0.001) where R1282 IR was reduced by 20% and 51%, respectively, compared to Tg PBS-injected mice (Fig. 2e–h, r, v).\", \"Thioflavin S-positive fibrillar amyloid plaques were reduced by 62% (p < 0.05) in HC and 23% (p < 0.05) in CTX in 07/2a-treated Tg mice compared to PBS controls (Fig. 2i–l, s, w).\",  \"Following 24 h incubation of the tissue with PMG, there was a significant reduction in R1282-positive staining present in the tissue pre-incubated with 07/2a mAb compared to incubation with IgG2a isotype control (p < 0.001) whereas exposure with the pGlu-3 Aβ IgG1 and 07/2a-k mAbs did not promote a significant reduction (Fig. 5a–h). Analysis of the guanidine-HCl insoluble Aβ homogenates by ELISA demonstrated that there was a significant decrease in pGlu-3 Aβ following incubation with the tissue with both 07/1 (p < 0.05) and 07/2a (p < 0.05) (Fig. 5i).\", \"Figure 5\", \"Additional file 1: Figure S5\", \"Ex vivo antibody-mediated phagocytosis assay demonstrates differences in plaque clearance based on antibody isotype. Unfixed, frozen plaque-rich tissue sections (20 μm) from 20-mo-old APPSWE/PS1ΔE9 Tg mice were pre-incubated with the following antibodies for 1 h: 07/1 IgG1, isotype control IgG1, 07/2a IgG2a, 07/2a-k IgG2a, or isotype control IgG2a. Following washing, the tissue was incubated with primary murine microglia (PMG) for 24 h and Aβ levels were determined. Representative photomicrographs of the hippocampus from each treatment group co-immunolabeled with a general Aβ marker, R1282, an activated microglial and macrophage marker, CD68 and a nucleic acid dye, DAPI (a-g) and showed decreased R1282 immunolabeling in the hippocampus of tissue pre-incubated with 07/2a IgG2a compared to isotype control (a–h). pGlu-3 Aβ, Aβx-40, and Aβx-42 levels were also determined by ELISA (i–k).\", \"We next compared two doses of the 07/2a antibody (150 and 500 μg) and one dose of 07/2a-k (500 μg) for their ability to clear Aβ in a plaque-rich AD model. Overall, Aβ clearance was similar between 07/2a-k, compared to that seen with 07/2a (Fig. 6). pGlu-3 Aβ (p < 0.05) and general Aβ (p < 0.01) immunoreactivity in the hippocampus showed significant reductions by 07/2a-k, similar to that of 07/2a-treated mice (Fig. 6a, b). The plaque-lowering potential of the CDC mutant antibody was further confirmed in the TBS soluble fraction isolated from the hemibrain of the treated mice and potentially containing toxic oligomers (Fig. 6c), although insoluble Aβ levels were not significantly altered.\", \"Figure 6\", \"In our present therapeutic study, pathological examination of chronic treatment effects of anti-pGlu3 Aβ IgG1 and IgG2a mAbs demonstrated reduced brain amyloid plaque burden and brain pGlu-3 Aβ, Aβx-42, Aβx-40, and Aβx-38 peptide levels.\", \"In our current study, 07/2a treatment not only demonstrated a decrease of cerebral pGlu-3 Aβ plaque deposition but also other forms of Aβ in the brain suggesting that by reducing pGlu-3 Aβ, it removed the seeds for further plaque deposition, a mechanism by which pGlu-3 Aβ has been reported to trigger AD pathogenesis [19].\",  \"Although none of the treatments showed an increased risk of microbleeds, we observed differences between the antibodies in the potential to reduce Aβ burden in the brain and increase plasma Aβ levels.\"",
    "Curator Statement": false
  },
  "AMGAB0722": {
    "Interaction ID": "AMGAB0722",
    "Antibody ID": "ABID0172",
    "Antibody name": "07/2a",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1186/s13195-019-0579-8",
    "PMID": 31931873.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"07/2a IgG2a and 3A1 IgG1 mAb’s lowered guanidine-HCl-extracted Aβ in aged APPSWE/PS1ΔE9 mice.\", \"Significant decreases in guanidine-HCl-extracted pGlu-3 Aβ (p < 0.05), Aβx-42 (p < 0.01), Aβx-40 (p < 0.05), and Aβx-38 (p < 0.05) were observed in Tg mice treated with 07/2a IgG2a mAb compared to PBS-treated Tg mice (a–d).\", \"07/2a treatment reduced guanidine-HCl-extracted Aβ levels in brain homogenates\", \"Biochemical analysis of guanidine-HCl-extracted Aβ from whole brain (excluding cerebellum) homogenates demonstrated a significantly reduced concentration of pGlu-3Aβ in the insoluble fraction from 07/2a-treated Tg mice compared to Tg PBS control mice (p < 0.05) (Fig. 3a). The levels of insoluble Aβx-42 were significantly lower in the 07/2a- and 3A1-treated mice compared with Tg PBS-injected mice (p < 0.05) (Fig. 3b). In addition, 07/2a-treated mice had significantly lower Aβx-40 (p < 0.05) and Aβx-38 (p < 0.05) in the insoluble Aβ fraction relative to Tg PBS control mice (Fig. 3c, d). A trend for reduction in Aβx-40 and Aβx-42 was observed by 3A1-treated mice compared to PBS-injected Tg mice and was significant when compared to PBS controls by Student’s t test (p < 0.05) (Fig. 3c, d). \",",
    "Curator Statement": false
  },
  "AMGAB0723": {
    "Interaction ID": "AMGAB0723",
    "Antibody ID": "ABID0173",
    "Antibody name": "07/2a-k",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-019-0579-8",
    "PMID": 31931873.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo, in vitro",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Effector function of anti-pyroglutamate-3 Aβ antibodies affects cognitive benefit, glial activation and amyloid clearance in Alzheimer’s-like mice\", \"We demonstrated significant cognitive improvement, better plaque clearance, and more plaque-associated microglia in the absence of microhemorrhage in aged APPSWE/PS1ΔE9 Tg mice treated with 07/2a, but not 07/1 or 3A1, compared to PBS in our first in vivo study.\", \"All mAbs cleared plaques in an ex vivo assay, although 07/2a promoted the highest phagocytic activity. \", \" Treatment of APPSLxhQC mice with 07/2a and 07/2a-k mAbs in our second in vivo study showed significant plaque-lowering with both mAbs.\", \"Our results suggest that attenuation of behavioral deficits and clearance of amyloid is associated with strong effector function of the anti-pGlu-3 Aβ mAb in a therapeutic treatment paradigm.\",\"Following 24 h incubation of the tissue with PMG, there was a significant reduction in R1282-positive staining present in the tissue pre-incubated with 07/2a mAb compared to incubation with IgG2a isotype control (p < 0.001) whereas exposure with the pGlu-3 Aβ IgG1 and 07/2a-k mAbs did not promote a significant reduction (Fig. 5a–h). Analysis of the guanidine-HCl insoluble Aβ homogenates by ELISA demonstrated that there was a significant decrease in pGlu-3 Aβ following incubation with the tissue with both 07/1 (p < 0.05) and 07/2a (p < 0.05) (Fig. 5i).\", \"Figure 5\",\"Additional file 1: Figure S5\", \"Ex vivo antibody-mediated phagocytosis assay demonstrates differences in plaque clearance based on antibody isotype. Unfixed, frozen plaque-rich tissue sections (20 μm) from 20-mo-old APPSWE/PS1ΔE9 Tg mice were pre-incubated with the following antibodies for 1 h: 07/1 IgG1, isotype control IgG1, 07/2a IgG2a, 07/2a-k IgG2a, or isotype control IgG2a. Following washing, the tissue was incubated with primary murine microglia (PMG) for 24 h and Aβ levels were determined. Representative photomicrographs of the hippocampus from each treatment group co-immunolabeled with a general Aβ marker, R1282, an activated microglial and macrophage marker, CD68 and a nucleic acid dye, DAPI (a-g) and showed decreased R1282 immunolabeling in the hippocampus of tissue pre-incubated with 07/2a IgG2a compared to isotype control (a–h). pGlu-3 Aβ, Aβx-40, and Aβx-42 levels were also determined by ELISA (i–k).\", \"We next compared two doses of the 07/2a antibody (150 and 500 μg) and one dose of 07/2a-k (500 μg) for their ability to clear Aβ in a plaque-rich AD model. Overall, Aβ clearance was similar between 07/2a-k, compared to that seen with 07/2a (Fig. 6). pGlu-3 Aβ (p < 0.05) and general Aβ (p < 0.01) immunoreactivity in the hippocampus showed significant reductions by 07/2a-k, similar to that of 07/2a-treated mice (Fig. 6a, b). The plaque-lowering potential of the CDC mutant antibody was further confirmed in the TBS soluble fraction isolated from the hemibrain of the treated mice and potentially containing toxic oligomers (Fig. 6c), although insoluble Aβ levels were not significantly altered.\", \"Figure 6\",\"In our present therapeutic study, pathological examination of chronic treatment effects of anti-pGlu3 Aβ IgG1 and IgG2a mAbs demonstrated reduced brain amyloid plaque burden and brain pGlu-3 Aβ, Aβx-42, Aβx-40, and Aβx-38 peptide levels.\", \"Although none of the treatments showed an increased risk of microbleeds, we observed differences between the antibodies in the potential to reduce Aβ burden in the brain and increase plasma Aβ levels.\", \"Antibody engineering to reduce CDC-mediated complement binding facilitated plaque clearance and led to the reduction of neuroinflammation in vivo.\",",
    "Curator Statement": false
  },
  "AMGAB0724": {
    "Interaction ID": "AMGAB0724",
    "Antibody ID": "ABID0174",
    "Antibody name": "3A1",
    "Amyloid ID": "AGAMYID0001",
    "Amyloid name": "Aβ-38",
    "DOI": "10.1186/s13195-019-0579-8",
    "PMID": 31931873.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"07/2a IgG2a and 3A1 IgG1 mAb’s lowered guanidine-HCl-extracted Aβ in aged APPSWE/PS1ΔE9 mice.\",\"Similarly, treatment with 3A1 mAb reduced guanidine-HCl-extracted Aβx-42 (p < 0.01), Aβx-40 (p < 0.05, t-test), and Aβx-38 (p < 0.05, t-test) in Tg mice compared to PBS controls (b–d)\",",
    "Curator Statement": false
  },
  "AMGAB0725": {
    "Interaction ID": "AMGAB0725",
    "Antibody ID": "ABID0174",
    "Antibody name": "3A1",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1186/s13195-019-0579-8",
    "PMID": 31931873.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"07/2a IgG2a and 3A1 IgG1 mAb’s lowered guanidine-HCl-extracted Aβ in aged APPSWE/PS1ΔE9 mice.\", \"Similarly, treatment with 3A1 mAb reduced guanidine-HCl-extracted Aβx-42 (p < 0.01), Aβx-40 (p < 0.05, t-test), and Aβx-38 (p < 0.05, t-test) in Tg mice compared to PBS controls (b–d)\",",
    "Curator Statement": false
  },
  "AMGAB0726": {
    "Interaction ID": "AMGAB0726",
    "Antibody ID": "ABID0174",
    "Antibody name": "3A1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-019-0579-8",
    "PMID": 31931873.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Effector function of anti-pyroglutamate-3 Aβ antibodies affects cognitive benefit, glial activation and amyloid clearance in Alzheimer’s-like mice\", \"We demonstrated significant cognitive improvement, better plaque clearance, and more plaque-associated microglia in the absence of microhemorrhage in aged APPSWE/PS1ΔE9 Tg mice treated with 07/2a, but not 07/1 or 3A1, compared to PBS in our first in vivo study.\", \"All mAbs cleared plaques in an ex vivo assay, although 07/2a promoted the highest phagocytic activity. \", \"Our results suggest that attenuation of behavioral deficits and clearance of amyloid is associated with strong effector function of the anti-pGlu-3 Aβ mAb in a therapeutic treatment paradigm.\", \"Additional file 1: Figure S5\", \"\"Although none of the treatments showed an increased risk of microbleeds, we observed differences between the antibodies in the potential to reduce Aβ burden in the brain and increase plasma Aβ levels.\"",
    "Curator Statement": false
  },
  "AMGAB0727": {
    "Interaction ID": "AMGAB0727",
    "Antibody ID": "ABID0174",
    "Antibody name": "3A1",
    "Amyloid ID": "AGAMYID0004",
    "Amyloid name": "pE3-Aβ",
    "DOI": "10.1186/s13195-019-0579-8",
    "PMID": 31931873.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"07/2a IgG2a and 3A1 IgG1 mAb’s lowered guanidine-HCl-extracted Aβ in aged APPSWE/PS1ΔE9 mice.\",\"Similarly, treatment with 3A1 mAb reduced guanidine-HCl-extracted Aβx-42 (p < 0.01), Aβx-40 (p < 0.05, t-test), and Aβx-38 (p < 0.05, t-test) in Tg mice compared to PBS controls (b–d)\",",
    "Curator Statement": false
  },
  "AMGAB0728": {
    "Interaction ID": "AMGAB0728",
    "Antibody ID": "ABID0175",
    "Antibody name": "07/1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-019-0579-8",
    "PMID": 31931873.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo, in vitro",
    "Experimental method(s)": "Immunohistochemistry,Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Effector function of anti-pyroglutamate-3 Aβ antibodies affects cognitive benefit, glial activation and amyloid clearance in Alzheimer’s-like mice\", \"We demonstrated significant cognitive improvement, better plaque clearance, and more plaque-associated microglia in the absence of microhemorrhage in aged APPSWE/PS1ΔE9 Tg mice treated with 07/2a, but not 07/1 or 3A1, compared to PBS in our first in vivo study.\", \"All mAbs cleared plaques in an ex vivo assay, although 07/2a promoted the highest phagocytic activity. \", \"Our results suggest that attenuation of behavioral deficits and clearance of amyloid is associated with strong effector function of the anti-pGlu-3 Aβ mAb in a therapeutic treatment paradigm.\", \"Following 24 h incubation of the tissue with PMG, there was a significant reduction in R1282-positive staining present in the tissue pre-incubated with 07/2a mAb compared to incubation with IgG2a isotype control (p < 0.001) whereas exposure with the pGlu-3 Aβ IgG1 and 07/2a-k mAbs did not promote a significant reduction (Fig. 5a–h). Analysis of the guanidine-HCl insoluble Aβ homogenates by ELISA demonstrated that there was a significant decrease in pGlu-3 Aβ following incubation with the tissue with both 07/1 (p < 0.05) and 07/2a (p < 0.05) (Fig. 5i).\", \"Figure 5\", \"Ex vivo antibody-mediated phagocytosis assay demonstrates differences in plaque clearance based on antibody isotype. Unfixed, frozen plaque-rich tissue sections (20 μm) from 20-mo-old APPSWE/PS1ΔE9 Tg mice were pre-incubated with the following antibodies for 1 h: 07/1 IgG1, isotype control IgG1, 07/2a IgG2a, 07/2a-k IgG2a, or isotype control IgG2a. Following washing, the tissue was incubated with primary murine microglia (PMG) for 24 h and Aβ levels were determined. Representative photomicrographs of the hippocampus from each treatment group co-immunolabeled with a general Aβ marker, R1282, an activated microglial and macrophage marker, CD68 and a nucleic acid dye, DAPI (a-g) and showed decreased R1282 immunolabeling in the hippocampus of tissue pre-incubated with 07/2a IgG2a compared to isotype control (a–h). pGlu-3 Aβ, Aβx-40, and Aβx-42 levels were also determined by ELISA (i–k).\", \"In our present therapeutic study, pathological examination of chronic treatment effects of anti-pGlu3 Aβ IgG1 and IgG2a mAbs demonstrated reduced brain amyloid plaque burden and brain pGlu-3 Aβ, Aβx-42, Aβx-40, and Aβx-38 peptide levels.\", \"Although none of the treatments showed an increased risk of microbleeds, we observed differences between the antibodies in the potential to reduce Aβ burden in the brain and increase plasma Aβ levels.\"",
    "Curator Statement": false
  },
  "AMGAB0729": {
    "Interaction ID": "AMGAB0729",
    "Antibody ID": "ABID0007.6",
    "Antibody name": "3D6_IgG2a",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-020-00719-x",
    "PMID": 33189132.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Interestingly, despite the lower abundance of the isoD7-Aβ epitope, the application of anti-isoD7-Aβ antibodies showed comparable treatment efficacy in terms of reduction of brain amyloid and spatial learning but did not result in an increase of plasma Aβ concentration as observed with 3D6 treatment.\", \"Treatment with the positive control antibody 3D6_IgG2a also resulted in lower Aβ contents in T-Per as well as 5 M GdmCl fractions, but no significant reduction was observed.\", \"Figure 5\", \"Figure 6\", \"Similar to the obtained ELISA data, immunohistochemical staining showed a significant reduction of Aβ plaque load in cortex and hippocampus after K11_IgG2a as well as 3D6_IgG2a treatment (Fig. 6b). The most prominent immunization effects were detected in the hippocampus which is also particularly affected in AD. Hippocampal staining with anti-isoD7-Aβ antibody revealed the highest reduction of isoD7-Aβ containing plaques from 3.6% surface area (isotype control group) to 1.6% surface area for the K11_IgG2a-treated group and to 1.8% surface area for the 3D6_IgG2a-treated animals (Fig. 6b). Interestingly, immunohistochemical staining using total Aβ-detecting antibody 3D6 demonstrated an even higher reduction of total Aβ in hippocampal and cortical ROI after 3D6_IgG2a treatment in comparison to K11_IgG2a treatment. Furthermore, the plaque morphology of 3D6_IgG2a-treated animals was different, with a more centralized and compact appearance, whereas the plaques in K11_IgG2a-treated mice were more diffuse and expanded (Fig. 6a).\", \"Together, ELISA and immunohistochemical analysis revealed a significant reduction of Aβ load by K11_IgG2a and 3D6_IgG2a antibody treatment.\",",
    "Curator Statement": false
  },
  "AMGAB0730": {
    "Interaction ID": "AMGAB0730",
    "Antibody ID": "ABID0323",
    "Antibody name": "K11",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-020-00719-x",
    "PMID": 33189132.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Interestingly, despite the lower abundance of the isoD7-Aβ epitope, the application of anti-isoD7-Aβ antibodies showed comparable treatment efficacy in terms of reduction of brain amyloid and spatial learning but did not result in an increase of plasma Aβ concentration as observed with 3D6 treatment.\", \"The present study demonstrates, for the first time, that the antibody-mediated targeting of isoD7-modified Aβ peptides leads to attenuation of AD-like amyloid pathology.\", \"Figure 4a shows immunohistochemical staining of brain slices from K11_IgG2a-treated 5xFAD mice by using 6E10. Despite the fact that 6E10 is not recognizing isoD7-Aβ, a clear reduction of Aβ plaque load was shown after K11_IgG2a treatment (Fig. 4a). This clearly demonstrates that targeting isoD7-Aβ results in a simultaneous reduction of non-modified total Aβ.\", \"Figure 4\", \"In 5 M GdmCl fractions, isoD7-Aβ content is reduced to 55.1% at the highest antibody concentration and to 69.8% at the lower dose (Fig. 4b). Total Aβ levels are also reduced to 65.6% and 76.1%, respectively (Fig. 4b). Same trends were seen in T-Per fractions, isoD7-Aβ is reduced to 62.1% at high dose and 70.8% at low dose; total Aβ is lowered to 71.0% and 74.0%, respectively (see Additional file 7).\", \"Additional file 7\", \"ELISA analysis of soluble T-Per fractions shows a significant reduction of isoD7-Aβ to 68.4% in K11_IgG2a-treated animals in comparison to the isotype control group. In T-Per fractions, total Aβ levels are also significantly reduced to 74.8% by K11_IgG2a treatment (Fig. 5a). ELISA analysis of 5 M GdmCl brain tissue fractions of 5xFAD mice treated with our anti-isoD7-Aβ antibody K11_IgG2a showed that total Aβ levels (lowered to 66.8%) as well as isoD7-Aβ levels (lowered to 68.6%) are significantly reduced in the left hemisphere in comparison to the isotype control group (Fig. 5b).\", \"Figure 5\", \"Figure 6\", \"Similar to the obtained ELISA data, immunohistochemical staining showed a significant reduction of Aβ plaque load in cortex and hippocampus after K11_IgG2a as well as 3D6_IgG2a treatment (Fig. 6b). The most prominent immunization effects were detected in the hippocampus which is also particularly affected in AD. Hippocampal staining with anti-isoD7-Aβ antibody revealed the highest reduction of isoD7-Aβ containing plaques from 3.6% surface area (isotype control group) to 1.6% surface area for the K11_IgG2a-treated group and to 1.8% surface area for the 3D6_IgG2a-treated animals (Fig. 6b). Interestingly, immunohistochemical staining using total Aβ-detecting antibody 3D6 demonstrated an even higher reduction of total Aβ in hippocampal and cortical ROI after 3D6_IgG2a treatment in comparison to K11_IgG2a treatment. Furthermore, the plaque morphology of 3D6_IgG2a-treated animals was different, with a more centralized and compact appearance, whereas the plaques in K11_IgG2a-treated mice were more diffuse and expanded (Fig. 6a).\", \"Together, ELISA and immunohistochemical analysis revealed a significant reduction of Aβ load by K11_IgG2a and 3D6_IgG2a antibody treatment.\",",
    "Curator Statement": false
  },
  "AMGAB0731": {
    "Interaction ID": "AMGAB0731",
    "Antibody ID": "ABID0001.6.2",
    "Antibody name": "Adu",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-021-00809-4",
    "PMID": 33836798.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We found that both Adu and SUS reduced the total plaque area in the hippocampus with no additive effect observed with the combination treatment (SUS + Adu). Whereas in the cortex where there was a trend towards reducing the total plaque area from either Adu or SUS, only the combination treatment yielded a statistically significant decrease in total plaque area compared to sham.\",  \"We calculated the percentage area occupied by plaque for two regions of interest, the cortex and the hippocampus, in 15–20 sections per mouse, assessing plaque burden in a one-in-eight series of sections along the rostral-caudal axis starting from the anterior commissure and ending at the ventral hippocampus. Analysis of cortical plaque burden in the different groups revealed an effect of treatment (F3,31 = 3.78, p = 0.02). A follow-up Holm-Sidak test found that combined SUS + Adu treatment resulted in a statistically significant 52% plaque reduction in the cortex of these mice compared to sham (p = 0.0066).\", \"At 22 months of age, APP23 mice have a severe plaque burden, with diffuse and compact plaques occupying 23% of the cortex in the sham-treated mice, compared to 16% of the cortex in mice administered Adu, 17% in mice administered SUS only, and 11% in mice which received SUS + Adu treatment (Fig. 2b). \". \"Figure 2\", \"Treatment strategies reduce plaques in APP23 mice.\", \"Plaque load in the hippocampus was reduced by Adu, SUS and SUS + Adu (f), with hippocampal black plaques (g) and amber plaques (h) analyzed separately.\", \"Aducanumab analog, SUS, and the combination therapy all effectively reduce amyloid plaques in the hippocampus of APP23 mice\", \" All three treatments (Adu, SUS and SUS + Adu) led to a significant reduction in total plaque area in the hippocampus compared to that in sham-treated APP23 mice (Fig. 2f). The sham-treated mice had a hippocampal plaque burden of 14.84% vs 8.68% for Adu-treated mice (p = 0.0432), 8.04% for SUS-treated mice (p = 0.043), and 6.92% for SUS + Adu-treated mice (p = 0.022). \", \"We further found that in our treatment paradigm (nine treatments from age 13 to 22 months of age), Adu delivered across the BBB with SUS produced a more marked reduction in the amyloid plaque burden in the cortex of 22 month-old APP23 mice compared to the effects of either the antibody or SUS alone, concomitant with improvements in memory.\", \"Our results show that administering a much lower cumulative dose of an Aducanumab analog than these authors used was ineffective at clearing plaques in the cortex of APP23 mice when treatment was commenced at 13 months of age; however, hippocampal plaques which develop at a more advanced age were reduced.\",  \"In contrast to peripheral injections alone, delivery of the Adu using SUS led to a reduction in both cortical and hippocampal plaques, concomitant with increased brain levels of the antibody.\", \" Here, we show that an Aducanumab analog, Adu or SUS alone have a comparable ability to reduce amyloid levels.\"",
    "Curator Statement": false
  },
  "AMGAB0732": {
    "Interaction ID": "AMGAB0732",
    "Antibody ID": "ABID0006",
    "Antibody name": "Lecanemab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-021-00813-8",
    "PMID": 33865446.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"At 18 months, 10-mg/kg biweekly lecanemab reduced brain amyloid (−0.306 SUVr units) while showing a drug-placebo difference in favor of active treatment by 27% and 30% on ADCOMS, 56% and 47% on ADAS-Cog14, and 33% and 26% on CDR-SB versus placebo according to Bayesian and frequentist analyses, respectively.\", \"Figure 3\", \"Results from prespecified key secondary endpoint analyses demonstrated that lecanemab reduced brain amyloid and showed early and sustained activity for 10 mg/kg biweekly lecanemab across the 18-month treatment period for several clinical measures of AD.\", \"Dose-dependent and robust reductions in amyloid PET SUVr values were observed using florbetapir as the imaging agent across all doses (nominal P < 0.0001 at 18 months of treatment for all doses). The baseline PET SUVr for the 10 mg/kg biweekly group was 1.37, with a mean change of −0.31 at 18 months, suggesting on average, that subjects treated with this dose fall below the SUVr threshold for amyloid-PET positivity for florbetapir. Consistent with PET SUVr results, a substantially larger proportion of subjects on lecanemab 10 mg/kg biweekly converted (by visual read) to amyloid negative (81%) compared to placebo (22%; placebo variability is generally attributed to variability associated with borderline amyloid PET positive cases).\",",
    "Curator Statement": false
  },
  "AMGAB0733": {
    "Interaction ID": "AMGAB0733",
    "Antibody ID": "ABID0283",
    "Antibody name": "ALZ-201",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-022-01141-1",
    "PMID": 36578089.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Inclusion of ALZ-201 at 0.13 times the concentration of rAβ42 dramatically reduced, but did not completely inhibit fibril formation\", \"Figure 2\", \"It proved to be specific for structured, oligomeric forms of the stabilised peptide Aβ42CC only (Fig. 1) and was able to prevent fibrillisation of Aβ42 (Fig. 2A).\",",
    "Curator Statement": false
  },
  "AMGAB0734": {
    "Interaction ID": "AMGAB0734",
    "Antibody ID": "ABID0006.1",
    "Antibody name": "RmAb158-scFv8D3",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-023-01236-3",
    "PMID": 37131196.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Neither RmAb158-scFv8D3 nor RmAb158 reduced soluble Aβ protofibrils or insoluble Aβ1-42 after a single injection treatment.\", \"Chronic treatment did not affect soluble Aβ aggregates, but a reduction in total Aβ42 was seen in the cortex of mice treated with both antibodies.\", \"Both RmAb158 and its bispecific variant RmAb158-scFv8D3 achieved positive effects of long-term treatment.\", \"Figure 2\", \"The effect of RmAb158-scFv8D3 and RmAb158 on soluble Aβ aggregates was studied in 5-month-old AppNL−G−F mice 3 days after a single dose of antibody (32 nmol/kg body weight) (Fig. 2A). Neither of the antibodies reduced Aβ aggregates in TBS 16 K extract of cortex and hippocampus (Fig. 2 B). However, in this acute therapeutic setting, where the antibody was administered only 3 days before assessment of Aβ pathology, a reduction would most likely be seen only in the most soluble pool of Aβ aggregates, i.e., in the TBS 100 K extract, that was subjected to centrifugation at 100,000 × g. Yet, unlike previous studies, no treatment effect was seen with either of the antibodies in AppNL−G−F mice (Fig. 2C).\", \"Figure 7\", \"Targeting the earliest formation of Aβ aggregates could inhibit seeding and further aggregation and deposition of Aβ in the brain. Thus, 3-month-old AppNL−G−F mice, where Aβ pathology is emerging, were administered three doses of RmAb158-scFv8D3 or RmAb158 during 1 week to clear the brain from these first Aβ aggregates (Fig. 2D). Ten weeks after antibody treatment, no significant effect was seen on levels of TBS soluble Aβ aggregates (Fig. 2E).\", \"Significant reduction of total Aβ1-42 was seen in the hippocampus of AppNL−G−F mice treated with RmAb158 and a similar trend was seen in the RmAb158-scFv8D3 high dose group. Although such trends were seen also in the cortex, no significant reduction was obtained. Interestingly, at the start of this therapeutic intervention, the total Aβ1-42 was already elevated in the cortex, while the hippocampus was still virtually devoid of Aβ pathology.\"",
    "Curator Statement": false
  },
  "AMGAB0735": {
    "Interaction ID": "AMGAB0735",
    "Antibody ID": "ABID0006.6",
    "Antibody name": "RmAb158",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s13195-023-01236-3",
    "PMID": 37131196.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Neither RmAb158-scFv8D3 nor RmAb158 reduced soluble Aβ protofibrils or insoluble Aβ1-42 after a single injection treatment.\", \"Chronic treatment did not affect soluble Aβ aggregates, but a reduction in total Aβ42 was seen in the cortex of mice treated with both antibodies.\", \"Both RmAb158 and its bispecific variant RmAb158-scFv8D3 achieved positive effects of long-term treatment.\", \"Figure 2\", \"The effect of RmAb158-scFv8D3 and RmAb158 on soluble Aβ aggregates was studied in 5-month-old AppNL−G−F mice 3 days after a single dose of antibody (32 nmol/kg body weight) (Fig. 2A). Neither of the antibodies reduced Aβ aggregates in TBS 16 K extract of cortex and hippocampus (Fig. 2 B). However, in this acute therapeutic setting, where the antibody was administered only 3 days before assessment of Aβ pathology, a reduction would most likely be seen only in the most soluble pool of Aβ aggregates, i.e., in the TBS 100 K extract, that was subjected to centrifugation at 100,000 × g. Yet, unlike previous studies, no treatment effect was seen with either of the antibodies in AppNL−G−F mice (Fig. 2C).\", \"Figure 7\",",
    "Curator Statement": false
  },
  "AMGAB0736": {
    "Interaction ID": "AMGAB0736",
    "Antibody ID": "ABID0101",
    "Antibody name": "S1G2",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Results show almost complete inhibition of aggregation for S1G2 (96.7 ± 0.37%, P < 0.001), E2E8 (97.6 ± 0.38%, P < 0.001), NS2A1 (94.4 ± 2.70%, P < 0.001) and S1D12 (92.3 ± 1.87%, P < 0.001).\"",
    "Curator Statement": false
  },
  "AMGAB0737": {
    "Interaction ID": "AMGAB0737",
    "Antibody ID": "ABID0101",
    "Antibody name": "S1G2",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the core or C-terminal binding mAbs showed statistically significant inhibition, with the exception of CA4 and S1D12 mAbs with both showing significant inhibition of FRET signal (29.7 ± 8.3%; P < 0.001 and 48.8 ± 13.6%; P < 0.001, respectively).\"",
    "Curator Statement": false
  },
  "AMGAB0738": {
    "Interaction ID": "AMGAB0738",
    "Antibody ID": "ABID0102",
    "Antibody name": "E2E8",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Results show almost complete inhibition of aggregation for S1G2 (96.7 ± 0.37%, P < 0.001), E2E8 (97.6 ± 0.38%, P < 0.001), NS2A1 (94.4 ± 2.70%, P < 0.001) and S1D12 (92.3 ± 1.87%, P < 0.001).\"",
    "Curator Statement": false
  },
  "AMGAB0739": {
    "Interaction ID": "AMGAB0739",
    "Antibody ID": "ABID0102",
    "Antibody name": "E2E8",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the core or C-terminal binding mAbs showed statistically significant inhibition, with the exception of CA4 and S1D12 mAbs with both showing significant inhibition of FRET signal (29.7 ± 8.3%; P < 0.001 and 48.8 ± 13.6%; P < 0.001, respectively).\"",
    "Curator Statement": false
  },
  "AMGAB0740": {
    "Interaction ID": "AMGAB0740",
    "Antibody ID": "ABID0103",
    "Antibody name": "NS2A1",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Results show almost complete inhibition of aggregation for S1G2 (96.7 ± 0.37%, P < 0.001), E2E8 (97.6 ± 0.38%, P < 0.001), NS2A1 (94.4 ± 2.70%, P < 0.001) and S1D12 (92.3 ± 1.87%, P < 0.001).\"",
    "Curator Statement": false
  },
  "AMGAB0741": {
    "Interaction ID": "AMGAB0741",
    "Antibody ID": "ABID0103",
    "Antibody name": "NS2A1",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the core or C-terminal binding mAbs showed statistically significant inhibition, with the exception of CA4 and S1D12 mAbs with both showing significant inhibition of FRET signal (29.7 ± 8.3%; P < 0.001 and 48.8 ± 13.6%; P < 0.001, respectively).\"",
    "Curator Statement": false
  },
  "AMGAB0742": {
    "Interaction ID": "AMGAB0742",
    "Antibody ID": "ABID0104",
    "Antibody name": "S1D12",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Results show almost complete inhibition of aggregation for S1G2 (96.7 ± 0.37%, P < 0.001), E2E8 (97.6 ± 0.38%, P < 0.001), NS2A1 (94.4 ± 2.70%, P < 0.001) and S1D12 (92.3 ± 1.87%, P < 0.001).\"",
    "Curator Statement": false
  },
  "AMGAB0743": {
    "Interaction ID": "AMGAB0743",
    "Antibody ID": "ABID0104",
    "Antibody name": "S1D12",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the core or C-terminal binding mAbs showed statistically significant inhibition, with the exception of CA4 and S1D12 mAbs with both showing significant inhibition of FRET signal (29.7 ± 8.3%; P < 0.001 and 48.8 ± 13.6%; P < 0.001, respectively).\"",
    "Curator Statement": false
  },
  "AMGAB0744": {
    "Interaction ID": "AMGAB0744",
    "Antibody ID": "ABID0105",
    "Antibody name": "CE2",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Strong aggregation inhibition properties were also seen with CE2 (82.8 ± 3.03%, P < 0.001), CE3 (84.4 ± 6.69%, P < 0.001) and less potent, but still statistically significant, with CA4 (46.9 ± 7.89% P < 0.05).\"",
    "Curator Statement": false
  },
  "AMGAB0745": {
    "Interaction ID": "AMGAB0745",
    "Antibody ID": "ABID0105",
    "Antibody name": "CE2",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the core or C-terminal binding mAbs showed statistically significant inhibition, with the exception of CA4 and S1D12 mAbs with both showing significant inhibition of FRET signal (29.7 ± 8.3%; P < 0.001 and 48.8 ± 13.6%; P < 0.001, respectively).\"",
    "Curator Statement": false
  },
  "AMGAB0746": {
    "Interaction ID": "AMGAB0746",
    "Antibody ID": "ABID0106",
    "Antibody name": "CE3",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Strong aggregation inhibition properties were also seen with CE2 (82.8 ± 3.03%, P < 0.001), CE3 (84.4 ± 6.69%, P < 0.001) and less potent, but still statistically significant, with CA4 (46.9 ± 7.89% P < 0.05).\"",
    "Curator Statement": false
  },
  "AMGAB0747": {
    "Interaction ID": "AMGAB0747",
    "Antibody ID": "ABID0106",
    "Antibody name": "CE3",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the core or C-terminal binding mAbs showed statistically significant inhibition, with the exception of CA4 and S1D12 mAbs with both showing significant inhibition of FRET signal (29.7 ± 8.3%; P < 0.001 and 48.8 ± 13.6%; P < 0.001, respectively).\"",
    "Curator Statement": false
  },
  "AMGAB0748": {
    "Interaction ID": "AMGAB0748",
    "Antibody ID": "ABID0107",
    "Antibody name": "CA4",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Strong aggregation inhibition properties were also seen with CE2 (82.8 ± 3.03%, P < 0.001), CE3 (84.4 ± 6.69%, P < 0.001) and less potent, but still statistically significant, with CA4 (46.9 ± 7.89% P < 0.05).\"",
    "Curator Statement": false
  },
  "AMGAB0749": {
    "Interaction ID": "AMGAB0749",
    "Antibody ID": "ABID0107",
    "Antibody name": "CA4",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the core or C-terminal binding mAbs showed statistically significant inhibition, with the exception of CA4 and S1D12 mAbs with both showing significant inhibition of FRET signal (29.7 ± 8.3%; P < 0.001 and 48.8 ± 13.6%; P < 0.001, respectively).\"",
    "Curator Statement": false
  },
  "AMGAB0750": {
    "Interaction ID": "AMGAB0750",
    "Antibody ID": "ABID0108",
    "Antibody name": "3aH6",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"All N-terminal binding mAbs tested showed statistically significant inhibition of L66 brain homogenate seeding ranging from 56.6 ± 6.2% (3aG3, P < 0.01) to 11.2 ± 4.6% (3bD11, P < 0.001) of FRET signal relative to the negative control.\"",
    "Curator Statement": false
  },
  "AMGAB0751": {
    "Interaction ID": "AMGAB0751",
    "Antibody ID": "ABID0109",
    "Antibody name": "3aG3",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"All N-terminal binding mAbs tested showed statistically significant inhibition of L66 brain homogenate seeding ranging from 56.6 ± 6.2% (3aG3, P < 0.01) to 11.2 ± 4.6% (3bD11, P < 0.001) of FRET signal relative to the negative control.\"",
    "Curator Statement": false
  },
  "AMGAB0752": {
    "Interaction ID": "AMGAB0752",
    "Antibody ID": "ABID0110",
    "Antibody name": "3aG4",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"All N-terminal binding mAbs tested showed statistically significant inhibition of L66 brain homogenate seeding ranging from 56.6 ± 6.2% (3aG3, P < 0.01) to 11.2 ± 4.6% (3bD11, P < 0.001) of FRET signal relative to the negative control.\"",
    "Curator Statement": false
  },
  "AMGAB0753": {
    "Interaction ID": "AMGAB0753",
    "Antibody ID": "ABID0111",
    "Antibody name": "CB7",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"All N-terminal binding mAbs tested showed statistically significant inhibition of L66 brain homogenate seeding ranging from 56.6 ± 6.2% (3aG3, P < 0.01) to 11.2 ± 4.6% (3bD11, P < 0.001) of FRET signal relative to the negative control.\"",
    "Curator Statement": false
  },
  "AMGAB0754": {
    "Interaction ID": "AMGAB0754",
    "Antibody ID": "ABID0112",
    "Antibody name": "3bD11",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"All N-terminal binding mAbs tested showed statistically significant inhibition of L66 brain homogenate seeding ranging from 56.6 ± 6.2% (3aG3, P < 0.01) to 11.2 ± 4.6% (3bD11, P < 0.001) of FRET signal relative to the negative control.\"",
    "Curator Statement": false
  },
  "AMGAB0755": {
    "Interaction ID": "AMGAB0755",
    "Antibody ID": "ABID0113",
    "Antibody name": "CC7",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The proline region mAb CC7 showed potent inhibition (11.5 ± 5.6% compared to control; P < 0.001). \"",
    "Curator Statement": false
  },
  "AMGAB0756": {
    "Interaction ID": "AMGAB0756",
    "Antibody ID": "ABID0114",
    "Antibody name": "E1B8",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the core or C-terminal binding mAbs showed statistically significant inhibition, with the exception of CA4 and S1D12 mAbs with both showing significant inhibition of FRET signal (29.7 ± 8.3%; P < 0.001 and 48.8 ± 13.6%; P < 0.001, respectively).\"",
    "Curator Statement": false
  },
  "AMGAB0757": {
    "Interaction ID": "AMGAB0757",
    "Antibody ID": "ABID0120",
    "Antibody name": "MoD9",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the core or C-terminal binding mAbs showed statistically significant inhibition, with the exception of CA4 and S1D12 mAbs with both showing significant inhibition of FRET signal (29.7 ± 8.3%; P < 0.001 and 48.8 ± 13.6%; P < 0.001, respectively).\"",
    "Curator Statement": false
  },
  "AMGAB0758": {
    "Interaction ID": "AMGAB0758",
    "Antibody ID": "ABID0123",
    "Antibody name": "412E10",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s13195-024-01561-1",
    "PMID": 39358820.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In cellulo",
    "Experimental method(s)": "FRET-based biosensor-cell assay.",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"None of the core or C-terminal binding mAbs showed statistically significant inhibition, with the exception of CA4 and S1D12 mAbs with both showing significant inhibition of FRET signal (29.7 ± 8.3%; P < 0.001 and 48.8 ± 13.6%; P < 0.001, respectively).\"",
    "Curator Statement": false
  },
  "AMGAB0759": {
    "Interaction ID": "AMGAB0759",
    "Antibody ID": "ABID0024.1.2",
    "Antibody name": "ScFv-MC1",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1186/s40478-018-0585-2",
    "PMID": 30134961.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Oligomeric/aggregated tau is significantly reduced in the hippocampus and hindbrain upon astrocytic expression of the scFv-MC1\", \"Tau aggregated forms in the hippocampus were significantly decreased when the scFv-MC1 was under neuronal or astrocytic expression (Fig. 7d), again with the astrocytic promoter being more efficient. In the cortex, a trend towards reduction is seen (Fig. 7e). Aggregated tau in the hindbrain was significantly reduced only when targeting the astrocytic population to release scFv-MC1 (Fig. 7f).\", \"Figure 7\", \"Insoluble tau is reduced in the HB and cortex\", \"As shown in Fig. 7h, a reduction of total insoluble tau in the hindbrain was seen in the astrocytic expression group. While no effect was detected on total insoluble tau in cortex (Fig. 7g), analysis of different phosphorylation residues showed a significant decrease of insoluble cortical tau phosphorylated at Thr231, together with a trend toward reduction of the other phospho-epitopes in both areas (Additional file 1: Figure S2a-f), again more pronounced with the GFAP promoter.\", \"Supplementary Figure S2\", \"Phosphorylated insoluble tau (INS) in cortex and HB. (a, b, c) Phosphorylation levels of insoluble tau in the cortex: the pThr231 residues showed a significant reduction (*P=0.0398 by non-parametric Kruskall-Wallis test) in the GFAP expressed group, while pSer202 (P=0.0685) and pSer396-404 (P=0.0649) showed a non-significant trend towards reduction in the same treatment cohort. (d, e, f) In the HB, no significant decrease in phosphorylated insoluble tau was detected, with a trend to reduction on pSer396-404 in the GFAP-scFv treated group (P=0.0768). \", \"Here we show that: 1) scFv-MC1 shares the same specificity of the parent MC1 antibody; 2) AAV5-vectored scFv-MC1 can be efficiently expressed by neurons or astrocytes; 3) scFv-MC1 can spread from the site of injection to adjacent brain structures; 4) scFv-MC1 is able to reduce/prevent tau pathology in JNPL3 adult mice, even in sites distant from injection, with efficacy on different tau species (soluble, oligomeric, insoluble), and more notably with astrocytic production.\",",
    "Curator Statement": false
  },
  "AMGAB0760": {
    "Interaction ID": "AMGAB0760",
    "Antibody ID": "ABID0125",
    "Antibody name": "mAb11",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1186/s40478-020-01069-3",
    "PMID": 33225991.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Passive immunization against Aβ reduces the number and enhances the size and compaction of amyloid plaques in the hippocampus\", \"We measured a significant decrease in the number of 4G8-positive Aβ plaques per mm2 in the hippocampus of mAb11-treated 5xFAD/AAV-tau mice compared with the sham-treated group (Fig. 5b). However, the total 4G8-positive area in the hippocampus remained similar in both groups (Fig. 5c). Indeed, the decreased number of Aβ plaques was compensated by a significant increase of plaque size in mAb11-treated 5xFAD/AAV-tau mice, from 303 μm2 in the sham-treated mice to an average of 495 μm2 in the mAb11-treated mice (Fig. 5d). In addition, Aβ plaques appeared more compact and lacked the fibrillary halo typically observed in non-treated 5xFAD mice (Fig. 5e).\", \"Although the late administration of anti-Aβ antibodies in 5xFAD/AAV-tau mice did not significantly reduce Aβ burden, it was found to modulate Aβ pathology by reducing the number of deposits, while enhancing their size and compaction.\", \"Figure 5\", \"Although passive immunization with mAb11 does not decrease the overall Aβ burden in 5xFAD/AAV-tau mice when administered after the onset of plaque deposition, the treated animals display a lower number of plaques with a larger size. Furthermore, plaques decorated with anti-Aβ antibodies appear more compact, with the loss of the Aβ fibrillary halo. \"",
    "Curator Statement": false
  },
  "AMGAB0761": {
    "Interaction ID": "AMGAB0761",
    "Antibody ID": "ABID0011",
    "Antibody name": "E2814",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s40478-020-0884-2",
    "PMID": 32019610.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro,",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, Western blot,",
    "Amyloid species identified": "Protein monomer, Oligomers, Protofibrils, Protofilaments, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Both 7G6 and E2814 showed a strong and significant inhibitory effect on tau aggregation (Fig. 5), suggesting that, if aggregation-competent tau is accessible to and bound by E2814, the antibody may have the ability to prevent further tau aggregation in a disease setting.\", \"Figure 5\", \"By binding to HVPGG, both antibodies effectively inhibit 4R-tau aggregation in vitro.\", \"Instead, by binding to the HVPGG epitope(s), E2814 could not only intervene in the misfolding of tau and formation of seeds but also facilitate their clearance.\", \"Both 7G6 and E2814 were equally effective in preventing in vitro heparin-induced aggregation of recombinant wild-type- and P301S tau (Fig. 5) despite loss of one epitope in the mutant protein. Furthermore, immunodepletion of seed-competent K18 peptide (repeat region only of wild-type 4R-tau) or recombinant 0N4R P301S monomer with E2814, resulted in effective removal of seeding activity in cells overexpressing 0N4R P301S tau. \", \"As with binding to 0N4R P301S tau, we have also demonstrated that 7G6 and E2814 effectively bind to 3R-tau isoforms and expect therefore that these antibodies will also prevent aggregation of 3R-tau.\",\"Given that E2814 could inhibit P301S tau aggregation in vitro it is plausible that binding to the R4 HVPGG is sufficient to sterically prevent formation and maturation of tau fibrils in AD brain.\",",
    "Curator Statement": false
  },
  "AMGAB0762": {
    "Interaction ID": "AMGAB0762",
    "Antibody ID": "ABID0011.5",
    "Antibody name": "7G6",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "P10636-8 or 2N4N isoform",
    "DOI": "10.1186/s40478-020-0884-2",
    "PMID": 32019610.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Quantification of sedimented particles (ultracentrifugation), Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, Western blot,",
    "Amyloid species identified": "Oligomers, Protofibrils, Protofilaments, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In an in vivo model of tau seeding and transmission, attenuation of deposition of sarkosyl-insoluble tau in brain could also be observed in response to antibody treatment. \", \"Both 7G6 and E2814 showed a strong and significant inhibitory effect on tau aggregation (Fig. 5), suggesting that, if aggregation-competent tau is accessible to and bound by E2814, the antibody may have the ability to prevent further tau aggregation in a disease setting.\", \"Figure 5\", \"Following peripheral 7G6 treatment, a modest, yet significant reduction in sarkosyl-insoluble tau levels was observed in the contralateral hippocampus compared to the IgG control group (Fig. 7 b; Additional file 1: Figure S10).\", \"Figure S10\", \"Figure 7\", \"By binding to HVPGG, both antibodies effectively inhibit 4R-tau aggregation in vitro.\", \"As with binding to 0N4R P301S tau, we have also demonstrated that 7G6 and E2814 effectively bind to 3R-tau isoforms and expect therefore that these antibodies will also prevent aggregation of 3R-tau.\", \"After 3 weeks, we observed attenuated levels of sarkosyl-insoluble tau in the contralateral hippocampus in 7G6-treated mice compared with control-treated mice but no differences were demonstrated in the injected half of the brain (Fig. 7). Despite the limitations of these data, e.g. reliance on the P301S mutation which may underestimate antibody efficacy due to weakening of binding at the R2 site, they do support the notion that the 7G6 antibody reduces seeded propagation of tau aggregation in the brain by being able to target conformational intermediates.\",",
    "Curator Statement": false
  },
  "AMGAB0763": {
    "Interaction ID": "AMGAB0763",
    "Antibody ID": "ABID0100",
    "Antibody name": "ACI-6677",
    "Amyloid ID": "AGAMYID0005",
    "Amyloid name": "TAR DNA-binding protein 43",
    "DOI": "10.1186/s40478-024-01867-z",
    "PMID": 39363348.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Turbidimetry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"ACI-6677 completely inhibited TDP-43 aggregation at an equimolar TDP-43-to-mAb ratio (Fig. 2A and B). The effect was indistinguishable from the result without aggregation induction (i.e., without TEV protease cleavage; Fig. 2A and B). The percentage of inhibition by ACI-6677 was 97% when normalized with an isotype control antibody (Fig. 2B).\"",
    "Curator Statement": false
  },
  "AMGAB0764": {
    "Interaction ID": "AMGAB0764",
    "Antibody ID": "ABID0007",
    "Antibody name": "Bapineuzumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1212/WNL.0000000000001877",
    "PMID": 26208959.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"A total of 115 carriers and 39 noncarriers were analyzed. The difference (δ) in mean baseline to 71 week change in 11C-PiB-PET GCA between bapineuzumab and placebo was significant in carriers (0.5 mg/kg vs placebo δ = −0.101; p = 0.004) and in pooled analyses of both carriers and noncarriers (0.5 mg/kg vs placebo δ = −0.068; p = 0.027; 1.0 mg/kg vs placebo δ = −0.133; p = 0.028) but not in the noncarrier trial separately.\", \"The 11C-PiB-PET imaging results demonstrated reduction of fibrillar Aβ accumulation in patients with Alzheimer disease treated with bapineuzumab; however, as no clinical benefit was observed, the findings are consistent with the hypotheses that bapineuzumab may not have been initiated early enough in the disease course, the doses were insufficient, or the most critical Aβ species were inadequately targeted.\", \" Among carriers (figure 2A), a baseline to 71 week increase in GCA was observed in the placebo group (mean ± SE 0.102 ± 0.026) but not in the bapineuzumab group (mean ± SE 0.001 ± 0.021), resulting in a significant treatment difference (δ) in the baseline to week 71 change in mean GCA between groups (δ = −0.101; p = 0.004). The baseline to week 71 increase (sample mean ± SE) in GCA among placebo carriers was similar among heterozygote (0.13 ± 0.034) and homozygote APOE ε4 carriers (0.08 ± 0.038). In noncarriers, a modest baseline to week 71 decrease in mean GCA was observed in the placebo group (−0.046 ± 0.0443), with no statistically significant treatment differences for either the 0.5-mg/kg (δ = 0.085, p = 0.193) or the 1.0-mg/kg groups (δ = −0.048, p = 0.466) compared with placebo (figure 2B). In the pooled study analysis that included participants from both studies (figure 2C), the baseline to week 71 11C-PiB-PET changes for placebo, 0.5 mg/kg, and 1.0 mg/kg, respectively, were 0.072 ± 0.023, 0.004 ± 0.019, and −0.061 ± 0.055, with treatment differences compared with placebo observed for both the 0.5-mg/kg (δ = −0.068; p = 0.027) and 1.0-mg/kg (δ = −0.133; p = 0.028) doses. The treatment differences observed in the carrier study and in the pooled analysis were most pronounced in the mild subgroup (figure 2, D and F).\", \"Figure 2\", \"Treatment differences were observed in the carrier study and in the pooled study results. Treatment differences appeared more prominent in participants with mild disease (carrier placebo/bapineuzumab [Bapi]: A, 40/75; D, 18/40; G, 22/35; noncarrier placebo/0.5 mg/kg/1.0 mg/kg: B, 15/12/12; E, 7/6/9; H, 8/6/3; pooled placebo/0.5 mg/kg/1.0 mg/kg: C, 55/87/12; F, 25/46/9; I, 30/41/3).\", \" Treatment-related differences in the change from baseline to week 71 regional SUVrs were observed in the anterior cingulate, posterior cingulate/precuneus, and lateral temporal cortices, with trends observed in the frontal and parietal cortices. Treatment-related differences in the change from baseline to week 71 SUVrs were also observed in the mesial temporal and occipital cortices and subcortical regions of the thalamus and striatum. The lack of treatment-related differences in GCA change over 71 weeks observed in the noncarrier study was also seen in the individual region analysis, except for the subcortical regions at the 1.0 mg/kg dose, in which treatment-related differences in the change from baseline to week 71 SUVrs were observed (table 2).\", \"A sensitivity analysis of the change in the mean GCA was also performed for each study using the pons as a reference region (figure 3). For carriers, there was a small increase in mean GCA for the placebo group (0.021 ± 0.0130), and a small decrease for the 0.5 mg/kg group (−0.023 ± 0.0102), resulting in a significant treatment-related difference in the baseline to week 71 change in GCA (δ = −0.044, p = 0.011). For noncarriers, there were no significant treatment-related differences in the baseline to week 71 change in 11C-PiB-PET GCA for the 0.5-mg/kg (δ = −0.041, p = 0.387) or 1.0-mg/kg groups (δ = −0.085, p = 0.083); however, in this analysis there was no change in mean GCA SUVr for the placebo group at week 71 (0.00 ± 0.0320), in contrast to the modest decrease observed using the cerebellar reference region. Additionally, a modest decrease was observed in the baseline to week 71 change in GCA in the 0.5 mg/kg group.\", \"Figure 3\", \"Similar to the results using the cerebellum as a reference region, a treatment difference in carriers was also observed when the pons was used as the reference region (carrier placebo/bapineuzumab [Bapi]: 40/75; noncarrier placebo/0.5 mg/kg/1.0 mg/kg: 15/12/12). SUVr = standardized uptake value ratio.\", \"Table 2\", \"The totality of the data from the 2 phase 3 PET bapineuzumab substudies suggests that IV treatment with bapineuzumab reduced fibrillar Aβ accumulation relative to placebo over 71 week in mild to moderate AD dementia. This reduction was most clearly evident in the carrier study and the pooled analyses (which included both carriers and noncarriers) for both the 0.5- and 1.0-mg/kg doses. The observation that the treatment differences seen in the carrier and pooled analyses seem to have been driven primarily by participants with mild disease raises the possibility that bapineuzumab immunotherapy could have a greater effect on amyloid accumulation in patients treated earlier in the disease course. \",",
    "Curator Statement": false
  },
  "AMGAB0765": {
    "Interaction ID": "AMGAB0765",
    "Antibody ID": "ABID0024",
    "Antibody name": "Zagotenemab",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1212/WNL.0000000000208061",
    "PMID": 38386949.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET), Plasma biomarker immunoassays",
    "Amyloid species identified": "Protein monomer, Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"No treatment effect was demonstrated by flortaucipir PET, volumetric MRI, or neurofilament light chain (NfL) analyses.\", \"There were no significant differences at week 104 on global or regional analyses with either zagotenemab dose group compared with placebo as measured by flortaucipir PET.\", \"Figure 4\", \" In addition, there was no evidence of disease-modifying effects seen on predefined biomarker outcome measures using tau PET, vMRI, or plasma NfL.\", \"Consistent with the absence of positive cognitive and functional benefit of zagotenemab intervention, no biomarker evidence was found to support the hypothesis that zagotenemab reduced cortical spread of AD-related tauopathy or pathologic disease progression.\", \"If the hypothesis of transneuronal spread-driving tau propagation is indeed true, zagotenemab, even at high doses, was not sufficient to curtail tau propagation to a degree detectable by flortaucipir PET imaging or translatable into an appreciable clinical or disease-modifying effect.\",",
    "Curator Statement": false
  },
  "AMGAB0766": {
    "Interaction ID": "AMGAB0766",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0008492",
    "PMID": 20041162.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Fluorescence microscopy",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Inhibition of coaggregation using an anti-Aβ antibody can be observed as 3D images on a microscopic scale.\", \"In contrast, when 0.6 µM anti-Aβ mouse monoclonal antibodies (6E10 and 4G8, specifically recognizing Aβ1-16 and Aβ18-22 epitopes, respectively) were incubated, fibril formation was significantly inhibited (Fig. 4c).\", \"Figure 4\", \"The effects of inhibition differed depending on antibodies: 6E10 blocked fibril elongation but not small aggregate formation, whereas 4G8 completely blocked Aβ aggregation. Since the 4G8 epitope corresponds to the region that forms a β-structure [31], the binding of 4G8 to the region may directly block the aggregation, whereas 6E10 may affect higher-order Aβ aggregation. 3D reconstruction of the Swept-field confocal microscope images demonstrated clear differences in the depth and size of Aβ aggregation in the presence of different antibodies (Fig. S6 and Movie S3–S5).\",",
    "Curator Statement": false
  },
  "AMGAB0767": {
    "Interaction ID": "AMGAB0767",
    "Antibody ID": "ABID0142",
    "Antibody name": "4G8",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0008492",
    "PMID": 20041162.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Fluorescence microscopy",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Inhibition of coaggregation using an anti-Aβ antibody can be observed as 3D images on a microscopic scale.\", \"In contrast, when 0.6 µM anti-Aβ mouse monoclonal antibodies (6E10 and 4G8, specifically recognizing Aβ1-16 and Aβ18-22 epitopes, respectively) were incubated, fibril formation was significantly inhibited (Fig. 4c).\", \"Figure 4\", \"The effects of inhibition differed depending on antibodies: 6E10 blocked fibril elongation but not small aggregate formation, whereas 4G8 completely blocked Aβ aggregation. Since the 4G8 epitope corresponds to the region that forms a β-structure [31], the binding of 4G8 to the region may directly block the aggregation, whereas 6E10 may affect higher-order Aβ aggregation. 3D reconstruction of the Swept-field confocal microscope images demonstrated clear differences in the depth and size of Aβ aggregation in the presence of different antibodies (Fig. S6 and Movie S3–S5).\",",
    "Curator Statement": false
  },
  "AMGAB0768": {
    "Interaction ID": "AMGAB0768",
    "Antibody ID": "ABID0574",
    "Antibody name": "anti-β~tubulin",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0008492",
    "PMID": 20041162.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "Fluorescence microscopy",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"When 0.6 µM (0.1 mg/ml) anti-β-tubulin (βTb) mouse monoclonal control antibody was mixed with 13 µM of 0.1% QDAβ(6) containing Aβ42, the fibril formation was unaffected.\", \"Figure 4\",",
    "Curator Statement": false
  },
  "AMGAB0769": {
    "Interaction ID": "AMGAB0769",
    "Antibody ID": "ABID0472",
    "Antibody name": "BAM-10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0010549",
    "PMID": 20485502.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Antibodies Targeted to the Brain with Image-Guided Focused Ultrasound Reduces Amyloid-β Plaque Load in the TgCRND8 Mouse Model of Alzheimer's Disease\", \"Four days post-treatment, Aβ pathology was significantly reduced in TgCRND8 mice.\", \"Figure 3\", \"Focused ultrasound delivery of BAM-10 to the brain reduces Aβ plaque pathology in TgCRND8 mice.\", \" In 4 days, the mean (F) count, (G) size and (H) surface area of Aβ plaques on the right, MRIgFUS-targeted side of the brain was consistently reduced in comparison to the left side of the brain only for the BAM-10/FUS-treated mice (F–H; n = 6, paired t-tests, p = 0.008, p = 0.048 and p = 0.003, respectively). This difference is unique to BAM-10/FUS treatment as there was no significant difference between right and left side of the brain in mice from other treatment groups (F′–H′: BAM-10 treated group, n = 6, paired t-tests, p = 0.294, p = 0.941 and p = 0.402; F″–H″: Untreated group, n = 6, paired t-tests, p = 0.502, p = 0.690, p = 0.610). Scale bars: A–C = 100 µm (inset = 20 µm); D = 1 mm; E = 50 µm.\", \"Among all groups (untreated, FUS-, BAM-10-, BAM-10/FUS-treated; n = 6 for all groups), statistically significant differences in plaque pathology were found only in BAM-10/FUS-treated mice, comparing the left (untreated) and right (treated) sides of the brain for each mouse (paired t-tests, Fig. 3F,G,H ). In all mice treated with BAM-10/FUS there were fewer plaques on the right, MRIgFUS-targeted hemisphere (12% reduction), in comparison to their respective contralateral sides (p = 0.008, n = 6, paired t-test, Fig. 3F ). The mean plaque size was lower on the right hemisphere, in comparison to the left, in 5 out of 6 BAM-10/FUS-treated mice, representing a significant reduction in plaque size (12% mean reduction, Fig. 3G ). Further, the estimated surface area covered by Aβ plaques was significantly smaller on the right compared to the left hemisphere (p = 0.003, n = 6, paired t-test, Fig. 3H ) for all mice in the BAM-10/FUS group, with a mean reduction of 23%.\", \" Importantly, we report for the first time that a single MRIgFUS treatment in conjunction with one low dose (40 µg) of intravenous BAM-10 anti-Aβ antibodies reduces the pathology of compact plaques in TgCRND8 mice in terms of the number, mean size and surface area occupied by Aβ.\", \"Significant reduction of plaque burden was evident based on the number or size of plaques alone (12% reduction in both cases), and the total surface area of Aβ plaques (23% reduction).\", \"The reduction of plaque load in TgCRND8 mice, on the BAM-10/FUS treated hemisphere compared to the untreated side of the brain, was achieved rapidly – within 4 days – and with a single low dose of 40 µg of anti-Aβ antibody.\", \"Here, the delivery of anti-Aβ antibodies to the brain using non-surgical MRIgFUS yielded a significant reduction in Aβ plaque pathology 4 days after a single treatment.\", \"Lastly, we demonstrated MRIgFUS immunotherapy can quickly decrease compact plaque burden after a single treatment in a model of AD with aggressive Aβ pathology.\", \"In conclusion, this is the first report to demonstrate that MRIgFUS delivery of anti-Aβ antibodies rapidly reduces plaque pathology.\",",
    "Curator Statement": "The authors refer to Transcranial focused ultrasound as FUS. BAM-10 with FUS diminished the amyloid deposition, while without FUS it did not."
  },
  "AMGAB0770": {
    "Interaction ID": "AMGAB0770",
    "Antibody ID": "ABID0472",
    "Antibody name": "BAM-10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0010549",
    "PMID": 20485502.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \" In 4 days, the mean (F) count, (G) size and (H) surface area of Aβ plaques on the right, MRIgFUS-targeted side of the brain was consistently reduced in comparison to the left side of the brain only for the BAM-10/FUS-treated mice (F–H; n = 6, paired t-tests, p = 0.008, p = 0.048 and p = 0.003, respectively). This difference is unique to BAM-10/FUS treatment as there was no significant difference between right and left side of the brain in mice from other treatment groups (F′–H′: BAM-10 treated group, n = 6, paired t-tests, p = 0.294, p = 0.941 and p = 0.402; F″–H″: Untreated group, n = 6, paired t-tests, p = 0.502, p = 0.690, p = 0.610). Scale bars: A–C = 100 µm (inset = 20 µm); D = 1 mm; E = 50 µm.\", \"Among all groups (untreated, FUS-, BAM-10-, BAM-10/FUS-treated; n = 6 for all groups), statistically significant differences in plaque pathology were found only in BAM-10/FUS-treated mice, comparing the left (untreated) and right (treated) sides of the brain for each mouse (paired t-tests, Fig. 3F,G,H ).\", \"Other groups (Fig. 3F′–H′, 3F″–G″), including FUS alone (not shown), had no significant difference in the number of plaques, mean plaque size and surface area covered by Aβ plaques between hemispheres (p>0.05).\",",
    "Curator Statement": "The authors refer to Transcranial focused ultrasound as FUS. BAM-10 with FUS diminished the amyloid deposition, while without FUS it did not."
  },
  "AMGAB0771": {
    "Interaction ID": "AMGAB0771",
    "Antibody ID": "ABID0542",
    "Antibody name": "22C4 scFv",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1371/journal.pone.0018296",
    "PMID": 21483675.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),ELISA",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Moreover, the scFv inhibited Aβ fibril formation and Aβ-mediated neurotoxicity in vitro. In a preventative therapeutic approach chronic intranasal treatment with scFv reduced congophilic amyloid angiopathy (CAA) and beta-amyloid plaque numbers in the cortex of APPswe/PS1dE9 mice. This reduction of CAA and plaque pathology was associated with a redistribution of brain Aβ from the insoluble fraction to the soluble peptide pool.\",\"This analysis showed a significantly decreased number of CAA-positive vessels in 22C4 scFv (*** p<0.005) and 22C4 IgG (* p<0.05) treated animals when compared to PBS treated controls (Fig. 4 F).\", \"Figure 4\", \"Determination of CAA-positive vessels by Thioflavin S staining. The number of vessels with CAA was significantly decreased in mice treated with 22C4 IgG (* p<0.05) and 22C4 scFv (*** p<0.005) when compared to animals that had received PBS as a control.\", \"Both, the insoluble Aβ1-40 and Aβ1-42 in the GuHCl-fraction (I and L) were decreased.\", \"Neither Aβ1-40 nor Aβ1-42 levels were significantly different among the treatment groups in the membrane-bound TBS Triton fraction; in the “insoluble” GuHCl-fraction, however, levels of both Aβ1-40 and Aβ1-42 were significantly decreased. \", \"In this study we report the novel finding that chronic intranasal treatment of APPswe/PS1dE9 mice with 22C4 scFv and 22C4 IgG resulted in decreased Aβ accumulation in the parenchyma and vessels of the brain and accordingly also showed decreased Aβ levels in the insoluble fraction but increased levels in the soluble fraction of brain extracts. Animals treated with 22C4 scFv exhibited significantly less plaques in brain parenchyma, but there was no statistical difference in plaque size among the treatment groups.\", \"Our results also demonstrated that the 22C4 scFv reduced CAA in transgenic mice without increasing microhemorrhages, which might be attributable to the route of delivery.\", \"In this study we report for the first time that chronic intranasal treatment of transgenic mice before the onset of Aβ deposition with 22C4 scFv resulted in decreased Aβ accumulation in the parenchyma and vessels of the brain and accordingly also showed decreased Aβ levels in the insoluble fraction but increased levels in the soluble fraction.\",",
    "Curator Statement": false
  },
  "AMGAB0772": {
    "Interaction ID": "AMGAB0772",
    "Antibody ID": "ABID0542",
    "Antibody name": "22C4 scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0018296",
    "PMID": 21483675.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo, in vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), ELISA",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Chronic Intranasal Treatment with an Anti-Aβ30-42 scFv Antibody Ameliorates Amyloid Pathology in a Transgenic Mouse Model of Alzheimer's Disease\", \"Moreover, the scFv inhibited Aβ fibril formation and Aβ-mediated neurotoxicity in vitro. In a preventative therapeutic approach chronic intranasal treatment with scFv reduced congophilic amyloid angiopathy (CAA) and beta-amyloid plaque numbers in the cortex of APPswe/PS1dE9 mice. This reduction of CAA and plaque pathology was associated with a redistribution of brain Aβ from the insoluble fraction to the soluble peptide pool.\", \"22C4 scFv inhibits both Aβ1-42 aggregation and neurotoxicity in vitro but does not bind to full-length APP\",  \"Figure 3\", \"The addition of 22C4 scFv to the aggregation assay showed a dose-dependent effect on Aβ1-42 aggregation. Aggregation was delayed when using Aβ1-42-scFv ratios of 10∶1 and could almost be completely prevented when using equimolar concentrations.\", \" When the scFv was added to the assay at substoichiometric concentrations it reduced fibril formation rather than completely inhibiting Aβ1-42 aggregation.\", \"22C4 scFv lowers plaque number and reduces insoluble Aβ levels in the brains of intranasally treated APP transgenic mice\", \"The quantitative analysis of the plaque number revealed that animals treated with 22C4 scFv had a significantly lower plaque number when compared to PBS treated animals (Fig 4 D; * p<0.05).\", \"Figure 4\", \"22C4 scFv reduced amyloid plaque number and influenced the amount of Aβ1-40 and Aβ1-42 in brains of treated animals.\", \"The plaque number (D) was significantly reduced in 22C4 scFv and 22C4 IgG treated animals as compared to PBS treated animals, however, there was no difference in plaque size (E) between the treatment groups (* p<0.05).\", \"Both, the insoluble Aβ1-40 and Aβ1-42 in the GuHCl-fraction (I and L) were decreased.\", \"Neither Aβ1-40 nor Aβ1-42 levels were significantly different among the treatment groups in the membrane-bound TBS Triton fraction; in the “insoluble” GuHCl-fraction, however, levels of both Aβ1-40 and Aβ1-42 were significantly decreased. \", \"22C4 scFv potently inhibited Aβ aggregation and Aβ-mediated neurotoxicity in vitro, presumably by binding to Aβ monomers thereby blocking their assembly to larger and potentially neurotoxic oligomeric aggregates. \", \"In this study we report the novel finding that chronic intranasal treatment of APPswe/PS1dE9 mice with 22C4 scFv and 22C4 IgG resulted in decreased Aβ accumulation in the parenchyma and vessels of the brain and accordingly also showed decreased Aβ levels in the insoluble fraction but increased levels in the soluble fraction of brain extracts. Animals treated with 22C4 scFv exhibited significantly less plaques in brain parenchyma, but there was no statistical difference in plaque size among the treatment groups.\", \"In this study we report for the first time that chronic intranasal treatment of transgenic mice before the onset of Aβ deposition with 22C4 scFv resulted in decreased Aβ accumulation in the parenchyma and vessels of the brain and accordingly also showed decreased Aβ levels in the insoluble fraction but increased levels in the soluble fraction.\",",
    "Curator Statement": "The authors describe a dose-dependent effect on Aβ1-42 aggregation, with complete inhibition on equimolar concentrations."
  },
  "AMGAB0773": {
    "Interaction ID": "AMGAB0773",
    "Antibody ID": "ABID0542",
    "Antibody name": "22C4 scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0018296",
    "PMID": 21483675.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The addition of 22C4 scFv to the aggregation assay showed a dose-dependent effect on Aβ1-42 aggregation. Aggregation was delayed when using Aβ1-42-scFv ratios of 10∶1 and could almost be completely prevented when using equimolar concentrations.\", \"Figure 3\", \"The fluorescence did not increase when Aβ1-42 was co-incubated with equimolar concentrations of 22C4 scFv when compared to the peptide alone, indicating that the scFv inhibited Aβ1-42 aggregation.\", \"Complete inhibition of Aβ42 aggregation by 22C4 scFv was only achieved when 22C4 scFv was added to Aβ42 at the beginning of the assay. \", Supplementary Figure S3\", \"22C4 scFv potently inhibited Aβ aggregation and Aβ-mediated neurotoxicity in vitro, presumably by binding to Aβ monomers thereby blocking their assembly to larger and potentially neurotoxic oligomeric aggregates. \",",
    "Curator Statement": "The authors describe a dose-dependent effect on Aβ1-42 aggregation, with complete inhibition on equimolar concentrations."
  },
  "AMGAB0774": {
    "Interaction ID": "AMGAB0774",
    "Antibody ID": "ABID0542",
    "Antibody name": "22C4 scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0018296",
    "PMID": 21483675.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Notably, 22C4 scFv only inhibited aggregation completely when added to Aβ1-42 at the beginning of the assay. When added after the onset of aggregation, 22C4 scFv did not inhibit aggregation but rather delayed progression (Figure S3A).\", \"Supplementary Figure S3\", \"When added after onset of aggregation, 22C4 scFv did not effectively inhibit Aβ42 aggregation but rather delayed the progression of the aggregation process. \", \"When added after the onset of aggregation, 22C4 scFv could not inhibit aggregation but rather delayed aggregation progression.\",",
    "Curator Statement": "The authors describe a reduction in Aβ1-42 aggregation when the 22C4 scFv antibody is added at the moment the ThT fluorescence reaches the half-maximal emission."
  },
  "AMGAB0775": {
    "Interaction ID": "AMGAB0775",
    "Antibody ID": "ABID0542",
    "Antibody name": "22C4 scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0018296",
    "PMID": 21483675.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"The quantitative analysis of the plaque number revealed that animals treated with 22C4 scFv had a significantly lower plaque number when compared to PBS treated animals (Fig 4 D; * p<0.05). However, there was no difference in plaque size between the treatment groups (Fig. 4 E). \", \"The plaque number (D) was significantly reduced in 22C4 scFv and 22C4 IgG treated animals as compared to PBS treated animals, however, there was no difference in plaque size (E) between the treatment groups (* p<0.05).\", \"In this study we report the novel finding that chronic intranasal treatment of APPswe/PS1dE9 mice with 22C4 scFv and 22C4 IgG resulted in decreased Aβ accumulation in the parenchyma and vessels of the brain and accordingly also showed decreased Aβ levels in the insoluble fraction but increased levels in the soluble fraction of brain extracts. Animals treated with 22C4 scFv exhibited significantly less plaques in brain parenchyma, but there was no statistical difference in plaque size among the treatment groups.\",",
    "Curator Statement": "The authors find a reduction in plaques number but not in plaque size after 22C4 scFv treatment."
  },
  "AMGAB0776": {
    "Interaction ID": "AMGAB0776",
    "Antibody ID": "ABID0543",
    "Antibody name": "22C4 IgG",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1371/journal.pone.0018296",
    "PMID": 21483675.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),ELISA",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"This analysis showed a significantly decreased number of CAA-positive vessels in 22C4 scFv (*** p<0.005) and 22C4 IgG (* p<0.05) treated animals when compared to PBS treated controls (Fig. 4 F).\", \"Figure 4\", \"Determination of CAA-positive vessels by Thioflavin S staining. The number of vessels with CAA was significantly decreased in mice treated with 22C4 IgG (* p<0.05) and 22C4 scFv (*** p<0.005) when compared to animals that had received PBS as a control.\", \"Both, the insoluble Aβ1-40 and Aβ1-42 in the GuHCl-fraction (I and L) were decreased.\", \"Neither Aβ1-40 nor Aβ1-42 levels were significantly different among the treatment groups in the membrane-bound TBS Triton fraction; in the “insoluble” GuHCl-fraction, however, levels of both Aβ1-40 and Aβ1-42 were significantly decreased. \", \"In this study we report the novel finding that chronic intranasal treatment of APPswe/PS1dE9 mice with 22C4 scFv and 22C4 IgG resulted in decreased Aβ accumulation in the parenchyma and vessels of the brain and accordingly also showed decreased Aβ levels in the insoluble fraction but increased levels in the soluble fraction of brain extracts. Animals treated with 22C4 scFv exhibited significantly less plaques in brain parenchyma, but there was no statistical difference in plaque size among the treatment groups.\",",
    "Curator Statement": false
  },
  "AMGAB0777": {
    "Interaction ID": "AMGAB0777",
    "Antibody ID": "ABID0543",
    "Antibody name": "22C4 IgG",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0018296",
    "PMID": 21483675.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),ELISA",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"The plaque number (D) was significantly reduced in 22C4 scFv and 22C4 IgG treated animals as compared to PBS treated animals, however, there was no difference in plaque size (E) between the treatment groups (* p<0.05).\", \"Both, the insoluble Aβ1-40 and Aβ1-42 in the GuHCl-fraction (I and L) were decreased.\", \"Neither Aβ1-40 nor Aβ1-42 levels were significantly different among the treatment groups in the membrane-bound TBS Triton fraction; in the “insoluble” GuHCl-fraction, however, levels of both Aβ1-40 and Aβ1-42 were significantly decreased. \",\"In this study we report the novel finding that chronic intranasal treatment of APPswe/PS1dE9 mice with 22C4 scFv and 22C4 IgG resulted in decreased Aβ accumulation in the parenchyma and vessels of the brain and accordingly also showed decreased Aβ levels in the insoluble fraction but increased levels in the soluble fraction of brain extracts. Animals treated with 22C4 scFv exhibited significantly less plaques in brain parenchyma, but there was no statistical difference in plaque size among the treatment groups.\",",
    "Curator Statement": "The authors find a reduction in plaques number but not in plaque size after 22C4 IgG treatment."
  },
  "AMGAB0778": {
    "Interaction ID": "AMGAB0778",
    "Antibody ID": "ABID0543",
    "Antibody name": "22C4 IgG",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0018296",
    "PMID": 21483675.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Protein monomer, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"The plaque number (D) was significantly reduced in 22C4 scFv and 22C4 IgG treated animals as compared to PBS treated animals, however, there was no difference in plaque size (E) between the treatment groups (* p<0.05).\",\"In this study we report the novel finding that chronic intranasal treatment of APPswe/PS1dE9 mice with 22C4 scFv and 22C4 IgG resulted in decreased Aβ accumulation in the parenchyma and vessels of the brain and accordingly also showed decreased Aβ levels in the insoluble fraction but increased levels in the soluble fraction of brain extracts. Animals treated with 22C4 scFv exhibited significantly less plaques in brain parenchyma, but there was no statistical difference in plaque size among the treatment groups.\",",
    "Curator Statement": "The authors find a reduction in plaques number but not in plaque size after 22C4 IgG treatment."
  },
  "AMGAB0779": {
    "Interaction ID": "AMGAB0779",
    "Antibody ID": "ABID0010.5",
    "Antibody name": "2A4",
    "Amyloid ID": "AGAMYID0009",
    "Amyloid name": "Antibody Light chain κ1",
    "DOI": "10.1371/journal.pone.0052686",
    "PMID": 23300743.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "in vivo",
    "Experimental method(s)": "Other: Gravimetric Analysis",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Treatment with 2A4 expedited regression of ALκ amyloidomas in mice, likely mediated by the action of macrophages and neutrophils, relative to animals that received a control antibody.\", \"Cohorts of mice bearing 50 mg human ALκ (Hig, L) amyloidomas were prepared by injecting precisely equivalent volumes of the stock amyloid slurry subcutaneously on the back. The mice were treated at a site away from the amyloidoma by sc injection of 100 µg 2A4 mAb for 4 wk (2 injections per week). For these experiments, the mAb JH70 served as a control. The amyloidomas, excised post-mortem, were photographed and weighed. The 2A4-treated mice had, on average, significantly smaller masses with a mean weight of 146±150 mg, as compared to the JH70 control mAb-treated animals with amyloid masses averaging 420±260 mg (p = 0.03) (Fig. 7A). Gross anatomy confirmed that the size of the amyloid masses excised from 2A4-treated mice were much smaller relative to those from the JH70-treated animals (Fig. 7B)\", \"Figure 7\", \"In the studies present here, mAb 2A4 was shown to bind the amyloid mass in vivo and to accelerate the resolution of the amyloidoma as compared to a control reagent (Fig. 7). Furthermore, immune cell recruitment at the amyloidoma site was characterized by a much different pattern than was seen in control Ab-treated mice.\"",
    "Curator Statement": false
  },
  "AMGAB0780": {
    "Interaction ID": "AMGAB0780",
    "Antibody ID": "ABID0137",
    "Antibody name": "JH70",
    "Amyloid ID": "AGAMYID0009",
    "Amyloid name": "Antibody Light chain κ1",
    "DOI": "10.1371/journal.pone.0052686",
    "PMID": 23300743.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "in vivo",
    "Experimental method(s)": "Other: Gravimetric Analysis",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Cohorts of mice bearing 50 mg human ALκ (Hig, L) amyloidomas were prepared by injecting precisely equivalent volumes of the stock amyloid slurry subcutaneously on the back. The mice were treated at a site away from the amyloidoma by sc injection of 100 µg 2A4 mAb for 4 wk (2 injections per week). For these experiments, the mAb JH70 served as a control. The amyloidomas, excised post-mortem, were photographed and weighed. The 2A4-treated mice had, on average, significantly smaller masses with a mean weight of 146±150 mg, as compared to the JH70 control mAb-treated animals with amyloid masses averaging 420±260 mg (p = 0.03) (Fig. 7A). Gross anatomy confirmed that the size of the amyloid masses excised from 2A4-treated mice were much smaller relative to those from the JH70-treated animals (Fig. 7B)\", \"Figure 7\", \"In the studies present here, mAb 2A4 was shown to bind the amyloid mass in vivo and to accelerate the resolution of the amyloidoma as compared to a control reagent (Fig. 7). Furthermore, immune cell recruitment at the amyloidoma site was characterized by a much different pattern than was seen in control Ab-treated mice.\"",
    "Curator Statement": false
  },
  "AMGAB0781": {
    "Interaction ID": "AMGAB0781",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0063162",
    "PMID": 23696796.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, ThT - Total aggregation (final point),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"Aβ aggregation was significantly decreased by incubation with Privigen and Privigen F(ab)2 at 100 µM and pAbs-Aβ and 6E10 at 1 µM but not with Privigen Fc at 100 µM (* p<0.05; ** p<0.005).\", \"Kinetic analysis of 5 µM Aβ42 incubated with Privigen, pAbs-Aβ and 6E10 (all 1 µM) revealed that pAbs-Aβ delayed Aβ aggregation, Privigen (data not shown) had no effect whereas 6E10 completely inhibited Aβ aggregation (Fig. 3B). When the Thioflavin T fluorescence was measured after 12 h of aggregation, statistical analysis revealed that both pAbs-Aβ and 6E10 significantly reduced Aβ aggregation (Fig. 3D; * p<0.05; ** p<0.005).\",",
    "Curator Statement": false
  },
  "AMGAB0782": {
    "Interaction ID": "AMGAB0782",
    "Antibody ID": "ABID0164",
    "Antibody name": "6F6",
    "Amyloid ID": "AGAMYID0022",
    "Amyloid name": "mice Aβ-42",
    "DOI": "10.1371/journal.pone.0065518",
    "PMID": 23799019.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Prophylactic treatment with 6F6 demonstrated a dose dependent reduction in the accumulation of both Aβ and activated C3 deposition. \", \"Aβ deposition around the RPE/Bruch’s membrane, (red label), was present in the control group at 6 months (Figure 3A) but was clearly impacted by anti Aβ mAb treatment in the prophylactic regime (Figures 3B, 3C and 3D). The scoring of Aβ load and differences compared to the vehicle control group are shown in Figure 3D and in Table S1. Aβ was also, dependent upon fixation time, detected in some sections in outer segments and photoreceptors of cfh−/− mice at three and six months of age, without prophylactic treatment, (data not shown). \", \"The data demonstrated that: dosing with 6F6 significantly lowered the amount of Aβ deposited in the retinae of cfh−/− mice by scores of 1.2 (p<0.0001), 0.9 (p<0.0001) and 0.4 (p = 0.0378), at the 600 µg, 300 µg and 60 µg doses, respectively.\", \"Figure 3\", \"Table S1\", \"Mice dosed with 6F6 show a dose dependent significant reduction, (asterisks, see text for levels of significance), in Aβ deposition at 60 µg, 300 µg and 600 µg and in activated C3 deposition at 300 µg and 600 µg compared to those treated with vehicle, (D) and (E) respectively.\", \"Aβ (red) and activated complement C3 deposition (green, detected using clone 2/11, HM1065, Hycult Biotech., see Table 3), around the RPE/Bruch’s membrane was strongly evident in the negative control group at nine months (Figure 4A) and was clearly impacted by 6F6 treatment in the therapeutic regime (Figures 4B, 4C and 4D).\", \"Figure 4\", \"Mice dosed with 6F6 show a dose dependent significant reduction, (asterisks, see text for levels of significance), in Aβ deposition at 60 µg and 600 µg and in activated C3 deposition at 600 µg compared compared to those treated with vehicle, (D) at 9 months of age (9MO), 3 months (+12w) after treatment.\", \"Dosing with 6F6 at 600 µg significantly lowered Aβ deposited in the retinae of cfh−/− mice by a score of 1.25 (p = 0.0028) at week 4, and by 1.06 points at week 12 (p<0.0001). Dosing with 6F6 at 60 µg showed a significant lowering of the amount of Aβ deposited in the retinae of cfh−/− mice by a score of 1 (p = 0.0069) at week 4 and significantly lowered score by 0.72 (p = 0.0008) at week 12.\", \"Table S3\", \"Figure 7\", \"Differences of **p = 0.0232, for Amyloid β deposition and of *p = 0.0414 for C3 deposition were noted comparing 6F6 treated with IgG2A control. \", \"Figure S6\", \"Prophylactic treatment of cfh−/− mice with 6F6 led to a dose dependent, (3–30 mg/kg), reduction in the retinal deposition of Aβ and activated complement C3. Therapeutic treatment of cfh−/− mice with 6F6 at a 30mg/kg dose led to a significant reduction in the retinal deposition of Aβ and activated complement C3 after both 4 and 12 weeks.\",",
    "Curator Statement": false
  },
  "AMGAB0783": {
    "Interaction ID": "AMGAB0783",
    "Antibody ID": "ABID0165",
    "Antibody name": "IgG2A",
    "Amyloid ID": "AGAMYID0022",
    "Amyloid name": "mice Aβ-42",
    "DOI": "10.1371/journal.pone.0065518",
    "PMID": 23799019.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 7\", \"Differences of **p = 0.0232, for Amyloid β deposition and of *p = 0.0414 for C3 deposition were noted comparing 6F6 treated with IgG2A control. \", \"Figure S6\",",
    "Curator Statement": false
  },
  "AMGAB0784": {
    "Interaction ID": "AMGAB0784",
    "Antibody ID": "ABID0420",
    "Antibody name": "A8 scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0124736",
    "PMID": 25919299.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, TEM image in presence/absence of the antibody, ThT - Total aggregation (final point), Dot Blot, ELISA",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Single chain variable fragment against aβ expressed in baculovirus inhibits abeta fibril elongation and promotes its disaggregation\", \"Our data demonstrated that the Ni-NTA agarose affinity-purified A8 scFv inhibited the forward reaction of “on-pathway” aggregation and Aβ fibril maturation. The effect of A8 scFv on Aβ fibrillogenesis was markedly more significant when administered at the start of the Aβ folding reaction. Furthermore, the results also showed that pre-formed Aβ fibrils could be disaggregated via incubation with purified A8 scFv, which suggested that A8 scFv is involved in the reverse reaction of Aβ aggregation. Therefore, A8 scFv was capable of both inhibiting fibrillogenesis and disaggregating matured fibrils.\", \"Furthermore, anti-Aβ scFvs were used to regulate the kinetics of Aβ aggregation and disassembly at different stages.\", \"Inhibition of on-pathway Aβ aggregation in the early stage by anti-Aβ scFv from baculovirus in a dose-dependent manner\", \"While long and branched fibrils were found in the control group incubated with boric acid buffer (Fig 2A a), the branched fibrils disappeared and the length of the fibrils decreased significantly in the scFv-treated group (Fig 2A b, c, and d) at 48 h (data not shown) and 96 h (Fig 2A and Fig 2B).\", \"Figure 2\", \"Inhibition of Aβ aggregation via the addition of an anti-Aβ scFv to the assembly reaction.\", \"To confirm the effects of scFv inhibition on Aβ fibril elongation, the Aβ peptides were treated with scFv in a dose-dependent manner starting at 0 h. Forty-eight hours later, the length of the fibrils was not significantly reduced (p > 0.05, Fig 3A b) in the 1× molar scFv-treated group compared with the buffer-treated control fibers (Fig 3A a); however, in the 5× molar scFv-treated group, the length of the fibrils was significantly decreased (p < 0.05, Fig 3A c and Fig 3B). As expected, if the concentration of scFv increased to 10× molar concentration, the length was highly significantly reduced (p < 0.01, Fig 3A d and Fig 3B), and only short and less-branched fibrils and aggregates were observed compared with the control group (Fig 3A a).\", \"Figure 3\", \" We found that the scFv affected the kinetics of Aβ fibril formation, slowed the aggregation reaction and disaggregated the pre-formed fibrils (Fig 4A and 4B) into shorter and less branched fibrils. Our results suggested that anti-Aβ scFv treatment can result in both the inhibition of the aggregation and the enhancement of the disaggregation pathways of Aβ in vitro.\", \"Figure 4\", \" Disaggregation of mature Aβ fibrils (48 h incubation) by anti-Aβ scFv.\", \"(A) TEM images of the disaggregation of Aβ fibrils in the absence (a, c and d) or presence (b) of anti-Aβ scFv.\", \"We also treated Aβ fibrils with the anti-Aβ scFv expressed in E. coli BL21 and obtained similar results. The number of Aβ fibrils decreased in both of the anti-Aβ scFv ([VH-(G4S)3-VL (S4C Fig and S4E Fig) and VL-(G4S)3-VH (S4D Fig and S4E Fig)])-treated groups (S4 Fig).\", \"Figure S3\", \"Figure S4\", \"The elongation of Aβ fibrils was inhibited by the anti-Aβ scFv expressed in E. coli BL21.\", \"(A) TEM images of Aβ aggregation at 0 h; (B) Aβ fibrils formed and elongated during 48 h of incubation in boric acid saline buffer; (C) and (D) The increase in the number of fibrils was inhibited by anti-Aβ scFv (VH-(G4S)3-VL or VL-(G4S)3-VH from E. coli) treatment for 48 h; (E) The diagram shows the number of fibrils longer than 200 nm in each group in (A), (B), (C) and (D). VL-VH indicates VL-(G4S)3-VH, and VH-VL indicates VH-(G4S)3-VL. ns: not significant.\", \"The versions expressed in baculovirus have more pronounced effects on Aβ degradation, and the His-Tag does not interfere with the effects of scFvs.\", \"Figure 5\", \"Our data showed that a scFv without the Fc fragment was capable of inhibiting Aβ aggregation and fibril elongation. Notably, the effect of this scFv was substantially significant when administered beginning at the initiation of the assembly reaction. Additionally, mature Aβ fibrils can be disaggregated by an anti-Aβ scFv targeting N-terminal amino acids 1–6.\", \"These data indicate that baculovirus-expressed A8 scFv inhibited fibril formation and disaggregated the pre-formed fibrils, suggesting that baculovirus-expressed A8 scFvs participates in both the forward and reverse reactions of Aβ fibril formation.\", \"Taken together, in this study, a scFv derived from an anti-Aβ MAb was successfully expressed in baculovirus and was shown to recognize Aβ42 and affect the regulation of the ultrastructural dynamics of on-pathway Aβ aggregation and disaggregation. The baculovirus-expressed A8 scFv exerted effect on both the aggregation of Aβ monomers into fibrils and the disassembly of fibrils into smaller molecules.\",",
    "Curator Statement": "scFv from A8 mAb. Tested expressing the linker after the VL (before the VH), after the VH (before the VL) and in different expression systems (Baculovirus and E. coli.) and all had similar outcomes."
  },
  "AMGAB0785": {
    "Interaction ID": "AMGAB0785",
    "Antibody ID": "ABID0540",
    "Antibody name": "PHF13",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1371/journal.pone.0125614",
    "PMID": 25933020.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Robust increases in hippocampal AT8 tau pathology were evident in both the IgG2b- and PHF13-treated mice, with ipsilateral pathology being 3–5 fold higher than that in the contralateral side (Fig 6A). No significant differences were observed between the PHF13 and IgG2b treatment groups in the area occupied in the ipsilateral or contralateral hippocampal area occupied by AT8 (Fig 6A) immunostaining. Total AT8- and MC1-positive cell counts were derived from both ipsi and contralateral EC, since these represent sites of spread of tau pathology following injection of the PFFs.\", \"Figure 6\", \"Figure 7\", \" There was no difference in MC1 immunostaining between the two groups in the ipsilateral hippocampus. The lack of an antibody-mediated decrease in AT8 (Fig 6A) or MC1 (Fig 7B) immunostaining in the ipsilateral hippocampus is likely due to the rapid and robust induction of pathology in this region that results from the internalization of K18PL PFFs, which as noted are not recognized by the PHF13 antibody. When the results of the studies with K18PL PFF-injected young PS19 from both laboratories are considered in total, there is evidence that PHF13 treatment can reduce tau pathology in the EC and the contralateral hippocampus in a model in which there is rapid spreading of tau pathology from the initial sites of PFF injection, with a resulting improvement of performance in the NOR test.\",",
    "Curator Statement": false
  },
  "AMGAB0786": {
    "Interaction ID": "AMGAB0786",
    "Antibody ID": "ABID0540",
    "Antibody name": "PHF13",
    "Amyloid ID": "AGAMYID0006",
    "Amyloid name": "Microtubule-associated protein tau",
    "DOI": "10.1371/journal.pone.0125614",
    "PMID": 25933020.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" A significant decline in AT8 (p<0.05) and MC1 positive counts (p<0.01) was evident within the EC after PHF13 treatment relative to the IgG2b group (Fig 6B and 6C). These results demonstrate a reduction in the spread of tau pathology from the hippocampus to the EC following treatment with PHF13.\", \"Figure 6\", \"PHF13 reduces EC tau pathology and rescues NOR performance in PS19 mice injected with K18PL PFFs.\", \" When the results of the two large, but similarly designed studies, were combined (resulting in 22–26 mice/treatment), a significant reduction of MC1-positive tau pathology was observed in the contralateral hippocampus of the PHF13-treated PS19 mice relative to the IgG2b-treated control group (p<0.01), despite the relatively large variation in the extent of hippocampal tau pathology (Fig 7B).\", \"Figure 7\", \"PHF13 reduces contralateral hippocampal tau pathology in PS19 mice injected with K18PL PFFs.\", \"Administration of PHF13 to PFF-injected PS19 mice resulted in a significant reduction in tau pathology in the EC and improvement in a NOR cognitive assay. Moreover, there was evidence of reduced tau pathology in the contralateral hippocampus in a second large study utilizing this model.\",",
    "Curator Statement": false
  },
  "AMGAB0787": {
    "Interaction ID": "AMGAB0787",
    "Antibody ID": "ABID0389",
    "Antibody name": "3F5",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0180076",
    "PMID": 28662102.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, Immunohistochemistry, ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"A novel monoclonal antibody against the N-terminus of Aβ1-42 reduces plaques and improves cognition in a mouse model of Alzheimer’s disease\", \"The mAb (3F5) showed the ability to disrupt Aβ1–42 aggregation and prevent Aβ-mediated neurotoxicity in vitro.\", \"In a mouse model of AD, administration with 3F5 for 3 months in 6 months-old mice demonstrated that the mAb specifically bound with Aβ1–42 to promote the depolymerization of Aβ fibrils, facilitated endocytosis of Aβ1–42 by microglia, and attenuated the death and apoptosis of neuronal cells, accompanied by neurite outgrowth.\", \"APP/PS1 double-transgenic mice treated with 3F5 mAb showed reduced memory loss, cognitive decline, and decreased levels of amyloid deposits in the brain.\", \"As a consequence, the antibody reduces plaques in the AD mouse brain, in association with reduction in the pathology of AD.\", \"This mAb demonstrates the capacity to disrupt Aβ1–42 aggregation in vitro and reduce Aβ-mediated neurotoxicity.\",  \"3F5 promotes the clearance of Aβ1–42 from the mouse brain\",\"Moreover, 3F5 dose-dependently reduced Aβ fibril fluorescence intensity when co-incubated with preformed Aβ fibrils for 48 and 72 h (Fig 5D). \", \"Figure 5\", \"Thus, Aβ burden in the cerebral tissues was reduced by 3F5 presumably by promoting the efflux of Aβ1–42 from the brain, deaggregation of Aβ fibrils and phagocytosis of Aβ1–42 by microglia.\", \"3F5 promotes the clearance of Aβ1–42 from the brain.\", \"3F5 decreases the number of plaques in the hippocampus and cerebral cortex of Tg-mice\", \"Immunohistochemistry of hippocampus and cerebral cortex from Tg-mice after 3 months of antibody treatment showed (Fig 6A and 6C) Aβ plaque area in 3F5-treated mice decreased by 43% compared with the tissues from control mice which contained senior plaques mostly in the hippocampus.\", \"Figure 6\", \"In agreement with Fig 6A and 6C, 3F5-treated Tg-mice exhibited 60% decrease in Aβ deposits in the cerebral cortex (Fig 6B and 6D).\", \"These data demonstrate that 3F5 antibody is able to promote the clearance of senior plaques in the hippocampus and cerebral cortex of Tg-mice in association with improved cognition and memory.\", \"In this study, we successfully developed an Aβ1–42 N-terminus targeting antibody 3F5, and confirmed that the mAb specifically bound Aβ1–42 to promote depolymerization of Aβ fibrils, facilitate endocytosis of Aβ1–42 by microglia, and attenuate the death and apoptosis of neuronal cells, accompanied by neurite outgrowth.\", \"Further, 3F5 reduced Aβ burden and initiated Aβ efflux from the brain in Tg-mice.\",",
    "Curator Statement": false
  },
  "AMGAB0788": {
    "Interaction ID": "AMGAB0788",
    "Antibody ID": "ABID0007.1",
    "Antibody name": "scFv-h3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0181480",
    "PMID": 28771492.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 7\", \"(C) Aβ Immunohistochemistry of coronal sections. Aβ-immunoreactivity decreased to similar levels as those in non-transgenic animals when 3xTg-AD were treated with scFv-h3D6-Ec or scFv-h3D6-Pp.\", \"Finally, immunohistological analysis of brain slices with the anti-Aβ antibody 6E10 (Fig 7C) also corroborated these results. Aβ-immunoreactivity decreased to similar levels as those in non-transgenic animals when 3xTg-AD were treated with scFv-h3D6-Ec or scFv-h3D6-Pp.\", \" It is capable of withdrawing Aβ oligomers from the amyloid pathway and, this way, prevent their cytotoxicity.\",",
    "Curator Statement": false
  },
  "AMGAB0789": {
    "Interaction ID": "AMGAB0789",
    "Antibody ID": "ABID0007.1.2",
    "Antibody name": "scFv-h3D6-Pp",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0181480",
    "PMID": 28771492.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 7\", \"(C) Aβ Immunohistochemistry of coronal sections. Aβ-immunoreactivity decreased to similar levels as those in non-transgenic animals when 3xTg-AD were treated with scFv-h3D6-Ec or scFv-h3D6-Pp.\", \"Finally, immunohistological analysis of brain slices with the anti-Aβ antibody 6E10 (Fig 7C) also corroborated these results. Aβ-immunoreactivity decreased to similar levels as those in non-transgenic animals when 3xTg-AD were treated with scFv-h3D6-Ec or scFv-h3D6-Pp.\", \" It is capable of withdrawing Aβ oligomers from the amyloid pathway and, this way, prevent their cytotoxicity.\",",
    "Curator Statement": false
  },
  "AMGAB0790": {
    "Interaction ID": "AMGAB0790",
    "Antibody ID": "ABID0007.1",
    "Antibody name": "ScFv-h3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0188191",
    "PMID": 29155887.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "TEM image in presence/absence of the antibody, Secondary structure composition by Circular dichroism (CD)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Arithmetic sum of the spectra of each molecule alone (black) vs experimental spectra of different mixtures (orange). (a) scFv-h3D6+apoE-MP; (b) scFv-h3D6+apoJ-MP; (c) scFv-h3D6+Aβ; (d) apoE-MP+Aβ; (e) apoJ-MP+Aβ; the conformational change is evident for apoE-MP+Aβ (d); clear for scFv-h3D6+Aβ (c), and faint for apoJ-MP+Aβ (e).\", \"As mentioned above, the scFv-h3D6/Aβ complex aggregates as WL fibrils and this is the molecular basis of its protective effect[28]. It is interesting to notice that the formation of WL fibrils is an intrinsic property of the scFv-h3D6, and that such an aggregation pathway is thermodynamically and kinetically favoured when the scFv-h3D6 and Aβ form a complex, explaining how the scFv-h3D6 withdraws Aβ oligomers from the amyloid pathway and, consequently, how cytotoxicity is avoided. \", \"When scFv-h3D6 and Aβ were co-incubated, WL fibrils were formed, also in the presence of apoJ-MP, but not when apoE-MP was involved, as was seen with oligomers. \", \"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0791": {
    "Interaction ID": "AMGAB0791",
    "Antibody ID": "ABID0327",
    "Antibody name": "AAV-scFc-IgG",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1371/journal.pone.0226245",
    "PMID": 31887144.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"AAV-mediated expression of this scFv-IgG reduced cortical and hippocampal plaque load in a transgenic mouse model of progressive β-amyloid plaque accumulation.\", \"Figure 5\", \"Both control groups showed clear plaque accumulation in cortex and hippocampus, whereas animals treated with the AAV-scFv-Fc targeting Aβ, or the positive control Aβ IgG had significantly fewer plaques.\", \"Aβ plaque load in cortex and hippocampus was quantified by IHC in coronal brain sections (Fig 5C, left). Compared to their respective controls, a single injection of the AAV-scFv-IgG caused the same magnitude of plaque reduction in the hippocampus as the αAβ IgG benchmark, despite the differences in plaque load between the control groups (Fig 5C, graph). Plaque reduction was also significantly reduced in cortex (Fig 5C graph), consistent with evidence that the scFv-IgG diffuses from the site of expression to bind to distal plaques.\", \"The typical passive immunotherapy regimen of 10mg/kg weekly anti-Aβ IgG for 16 weeks caused significant reductions in amyloid plaque formation in APP animals. In contrast, a single intracranial injection of the AAV-scFc-IgG resulted in comparable efficacy after 4 months of expression.\", \"Long term expression of this vector in APP mice caused plaque reduction both in the cortex (52% reduction) and hippocampus (87% reduction).\", \"The observed magnitude of plaque reduction in animals treated with a single intracranial injection of AAV-scFv-IgG was similar to animals treated with weekly IV injections of 10mg/kg anti-Aβ antibody for 4 months, highlighting the value of gene delivery for long term treatment paradigms.\",",
    "Curator Statement": false
  },
  "AMGAB0792": {
    "Interaction ID": "AMGAB0792",
    "Antibody ID": "ABID0002",
    "Antibody name": "Gantenerumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.14283/jpad.2020.68",
    "PMID": 33336218.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In this 36-month update, we demonstrate continued reduction, with mean (standard error) centiloid values at 36 months of −4.3 (7.5), 0.8 (6.7), and 4.7 (8.0) in the SCarlet RoAD (double-blind pooled placebo and active groups), Marguerite RoAD double-blind placebo, and Marguerite RoAD double-blind active groups respectively representing a change of −57.0 (10.3), −90.3 (9.0), and −74.9 (10.5) centiloids respectively. These results demonstrate that prolonged gantenerumab treatment, at doses up to 1200 mg, reduces amyloid plaque levels below the amyloid positivity threshold. \",  \"Consistent with our previous report, reductions in mean amyloid burden were observed across cohorts after 12 and 24 months of open-label therapy, with 37% and 52% of participants, respectively, reaching levels below the amyloid positivity threshold (Figure 1) (7). Continued reductions beyond 24 months were observed after 36 months, with mean amyloid levels approaching zero centiloids across all cohorts. The absolute mean (SE) amyloid burden after 36 months were −4.3 (7.5), 0.8 (6.7), and 4.7 (8.0) centiloids for the SR, MR-DBP and MR-DBA cohorts, respectively, representing a change of −57.0 (10.3), −90.3 (9.0), −74.9 (10.5) centiloids respectively. Furthermore, the proportion of participants below the amyloid positivity threshold was 24 of 30 participants (80%) at 36 months (Figure 1).\", \"Figure 1\", \"The consistent reduction in Aβ suggests that gantenerumab is able to remove Aβ species successfully.\",",
    "Curator Statement": false
  },
  "AMGAB0793": {
    "Interaction ID": "AMGAB0793",
    "Antibody ID": "ABID0003",
    "Antibody name": "Donanemab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.14283/jpad.2021.56",
    "PMID": 34585215.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Treatment with donanemab resulted in rapid reduction of amyloid, even after a single dose. By 24 weeks, amyloid positron emission tomography mean changes from baseline for single donanemab doses in Centiloids were: −16.5 (standard error 11.22) 10-mg/kg intravenous; 40.0 (standard error 11.23) 20 mg/kg intravenous; and −49.6 (standard error 15.10) 40-mg/kg intravenous. Mean reduction of amyloid plaque in multiple dose cohorts by 24 weeks in Centiloids were: 55.8 (standard error 9.51) 10-mg/kg every 2 weeks; −50.2 (standard error 10.54) 10-mg/kg every 4 weeks; and −58.4 (standard error 9.66) 20-mg/kg every 4 weeks. Amyloid on average remained below baseline levels up to 72 weeks after a single dose of donanemab. Repeated dosing resulted in continued florbetapir positron emission tomography reductions over time compared to single dosing with 6 out of 28 patients attaining complete amyloid clearance within 24 weeks. Within these, 5 out of 10 patients in the 20 mg/kg every 4 weeks cohort attained complete amyloid clearance within 36 weeks. When dosing with donanemab was stopped after 24 weeks of repeat dosing in the 10 mg every 2 weeks cohort, florbetapir positron emission tomography reductions were sustained up to 72 weeks. For the single dose cohorts on day 1, dose proportional increases in donanemab pharmacokinetics were observed from 10 to 40 mg/kg. Dose proportional increases in pharmacokinetics were also observed at steady state with the multiple dose cohorts.\", \"Single and multiple doses of donanemab demonstrated a rapid, robust, and sustained reduction up to 72 weeks in brain amyloid plaque despite treatment-emergent antidrug antibodies detected in most patients. \", \"Figure 1\", \" At Week 24, amyloid PET least squares mean Centiloid changes from baseline for single donanemab doses were: −16.5 (standard error [SE] = 11.22) 10-mg/kg IV; −40.0 (SE = 11.23) 20-mg/kg IV; and −49.6 (SE = 15.10) 40-mg/kg IV. In contrast, in the placebo group there was no significant reduction in florbetapir PET at 72 weeks (90.9 Centiloids at 72 weeks compared to 104.4 Centiloids at baseline). Corresponding Centiloid changes for multiple doses at Week 24 included: −55.8 (SE = 9.51) 10-mg/kg Q2W; −50.2 (SE = 10.54) 10-mg/kg Q4W; and −58.4 (SE = 9.66) 20-mg/kg Q4W. Patients in the 20 mg/kg Q4W cohort tended to achieve greater plaque reduction earlier in the study than patients in either of the 10 mg/kg multiple dose cohorts (Figures 1 and 2). After dosing, a sustained reduction of brain amyloid level without significant reaccumulation for up to 72 weeks was observed across all single- and multiple-dose cohorts.\", \"Overall, 2 participants in single-dose cohorts (1 in 20-mg /kg and 1 in 40-mg /kg) and 9 participants in the multiple-dose cohorts (2 in 10mg/kg Q2W; 2 in 10-mg /kg Q4W; and 5 in 20-mg /kg Q4W) achieved complete amyloid clearance status based on a threshold 24.1 Centiloid value. Most participants achieving amyloid clearance starting at 12 or 24 weeks remained amyloid negative for the duration of their florbetapir PET measurements.\", \"Reduction in cerebral amyloid (Centiloid units) and SUVr changes from baseline were visually comparable between non-Japanese and Japanese patients (Supplemental Figure 3).\", \"Supplementary Figure 3\", \"The main findings in this study were that:\\n\\n1)single and multiple doses of donanemab up to 40 mg and 20-mg/kg Q4W, respectively, reduced amyloid plaque deposits in patients with AD; 5 out of 10 patients in the 20 mg/kg Q4W cohort attained complete amyloid clearance within 36 weeks\\n2)the observed amyloid plaque lowering by donanemab was rapid, robust, and sustained\\n3)nearly all donanemab-treated patients developed anti-drug antibodies, however, there was no overall significant effect of the antibodies on the PK of donanemab for the duration of the study, given the observed linear PK \\n4)donanemab was generally well tolerated with manageable ARIA-E events that resolved completely upon treatment discontinuation.\",\" A novel finding in this study is that a significant reduction in cerebral amyloid plaque was observed, even after single doses of donanemab, and the reduction was sustained up to 72 weeks after the single dose. Importantly, the rate of the observed amyloid plaque lowering was rapid, with a greater than 50 Centiloid reduction observed after 24-weeks of multiple-dose donanemab treatment. Furthermore, complete amyloid clearance, as measured by florbetapir PET, was observed for 5 of 10 patients (50.0%) treated with 20-mg/ kg Q4W donanemab. This result was sustained through 18 months.\", \"Single and multiple doses of donanemab demonstrated a rapid and robust reduction in brain amyloid plaque. Single and multiple doses of donanemab yielded sustained amyloid plaque reduction without evidence of significant reaccumulation when measured at 72 weeks.\",",
    "Curator Statement": false
  },
  "AMGAB0794": {
    "Interaction ID": "AMGAB0794",
    "Antibody ID": "ABID0001",
    "Antibody name": "Aducanumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.14283/jpad.2022.30",
    "PMID": 35542991.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Amyloid PET substudies assessed n=488 and n=585 patients in EMERGE and ENGAGE, respectively. These substudies showed a dose- and time-dependent reduction in amyloid PET SUVR in both EMERGE and ENGAGE. At week 78, the difference in adjusted mean change from baseline between high-dose aducanumab and placebo was -0.278 (95% CI, -0.306 to -0.250; P<.0001) for EMERGE (Fig. 2a) and -0.232 (95% CI, -0.256 to -0.208; P<.0001) for ENGAGE (Fig. 2b). For the high-dose aducanumab arm, the reduction in adjusted mean change from baseline in amyloid PET SUVR in ENGAGE was 16.5% less than that in EMERGE at week 78.\", \"Figure 2\", \"After 78 weeks, 48% of patients from EMERGE and 31% of patients from ENGAGE treated with high-dose aducanumab had a PET composite SUVR score of .1.10, a proposed threshold that distinguishes between Aβ-negative and -positive patients (Supplemental Data Table 4) (25).\", \"In Aβ PET substudies, significant dose- and time-dependent reductions in amyloid PET SUVR were associated with aducanumab treatment in both EMERGE and ENGAGE. However, the magnitude of these changes differed in the high-dose arms: reductions in brain amyloid levels were 16.5% lower at week 78 in ENGAGE (.0.232) compared with EMERGE (-0.278).\", \"These findings from EMERGE and ENGAGE demonstrate that treatment with aducanumab, an anti-Aβ monoclonal antibody, directly affects both an upstream biomarker of AD (Aβ plaque) as well as an intermediate biomarker of AD (soluble p-tau). In both studies, reductions in amyloid PET SUVR were correlated with a reduction in plasma p-tau181 levels.\",",
    "Curator Statement": false
  },
  "AMGAB0795": {
    "Interaction ID": "AMGAB0795",
    "Antibody ID": "ABID0001",
    "Antibody name": "Aducanumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.14283/jpad.2024.106",
    "PMID": 39350371.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Consistent with the overall data set, a robust dose-dependent decrease in amyloid beta levels as assessed with amyloid-PET and plasma p-tau181 was observed. \", \"Consistent with the overall population (20), a dose- and time-dependent reduction in brain Aβ plaque levels was observed in each study compared with placebo (Fig. 3A, B). At Week 78, high-dose aducanumab decreased brain Aβ plaque levels (centiloid units) by −48.2 (95% CI, −63.1 to −33.2) in EMERGE (n=9) and −59.9 (95% CI, −75.0 to −44.7) in ENGAGE (n=6). In the low-dose arm, the difference from placebo in mean centiloid units at Week 78 was −35.1 (95% CI, −51.6 to −18.5) in EMERGE (n=7) and −25.8 (95% CI, −38.9 to −12.7) in ENGAGE (n=9).\", Figure 3\"",
    "Curator Statement": false
  },
  "AMGAB0796": {
    "Interaction ID": "AMGAB0796",
    "Antibody ID": "ABID0023.5",
    "Antibody name": "2H6",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1523/JNEUROSCI.0695-06.2006",
    "PMID": 16707786.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Significantly fewer vascular amyloid deposits and microhemorrhages were observed in mice administered the de-2H6 antibody compared with those receiving unmodified 2H6 antibody.\", \"Compact Congophilic amyloid deposits are reduced by intact or deglycosylated anti-Aβ 2H6 antibody administration, whereas vascular amyloid is increased\", \"Figure 5\",\"Mice treated with the 2H6 antibody showed significant reductions in compact amyloid deposits in both the frontal cortex and hippocampus, but there was an obvious increase in amyloid deposits in the vasculature of both regions (Fig. 5, frontal cortex, C; hippocampus, D).\", \"Total and parenchymal Congo red staining of APP transgenic mice is reduced, whereas vascular Congo red is increased after treatment with intact or deglycosylated anti-Aβ 2H6 (D-2H6).\",",
    "Curator Statement": false
  },
  "AMGAB0797": {
    "Interaction ID": "AMGAB0797",
    "Antibody ID": "ABID0023.5",
    "Antibody name": "2H6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.0695-06.2006",
    "PMID": 16707786.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Deglycosylated Anti-Amyloid-β Antibodies Eliminate Cognitive Deficits and Reduce Parenchymal Amyloid with Minimal Vascular Consequences in Aged Amyloid Precursor Protein Transgenic Mice\", \"Both groups receiving anti-Aβ antibodies showed significant reductions in total Aβ immunochemistry and Congo red.\", \"Figure 3\", \"APP transgenic mice treated with anti-Aβ antibodies 2H6 (Fig. 3, frontal cortex, C; hippocampus, D) or deglycosylated 2H6 (Fig. 3, frontal cortex, E; hippocampus, F) showed significant reductions in total Aβ immunohistochemistry of similar magnitude in both the frontal cortex and hippocampus with both antibodies. Quantification of the percentage area occupied by positive staining showed a 50% reduction in total Aβ in the frontal cortex (Fig. 4A) and a 55% reduction in the hippocampus (Fig. 4B).\", \"Figure 4\", \"Total Aβ immunohistochemistry is significantly reduced in both the frontal cortex and hippocampus by systemic treatment with either intact or deglycosylated anti-Aβ (D-2H6) antibodies.\", \"Compact Congophilic amyloid deposits are reduced by intact or deglycosylated anti-Aβ 2H6 antibody administration, whereas vascular amyloid is increased\", \"Figure 5\", \"Mice treated with the 2H6 antibody showed significant reductions in compact amyloid deposits in both the frontal cortex and hippocampus, but there was an obvious increase in amyloid deposits in the vasculature of both regions (Fig. 5, frontal cortex, C; hippocampus, D).\", \"Quantification of total Congo red area stained shows significant reductions after 14 weeks of treatment of APP transgenic mice with either intact 2H6 [80% in frontal cortex and hippocampus (Fig. 6A)] or deglycosylated 2H6 [70% in frontal cortex and 55% in hippocampus (Fig. 6A)].\", \"Figure 6\", \"These show that dramatic reductions in Congophilic compact plaque loads in the group treated with 2H6 was dramatically reduced [95% in both frontal cortex and in hippocampus (Fig. 6B)].\", \"Total and parenchymal Congo red staining of APP transgenic mice is reduced, whereas vascular Congo red is increased after treatment with intact or deglycosylated anti-Aβ 2H6 (D-2H6).\", \"In the current study, we have shown that systemic administration of de-2H6 reduces diffuse amyloid deposits as effectively as its intact counterpart and also produces significant reductions in compact amyloid deposits.\",",
    "Curator Statement": false
  },
  "AMGAB0798": {
    "Interaction ID": "AMGAB0798",
    "Antibody ID": "ABID0023.6",
    "Antibody name": "de-2H6",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1523/JNEUROSCI.0695-06.2006",
    "PMID": 16707786.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Significantly fewer vascular amyloid deposits and microhemorrhages were observed in mice administered the de-2H6 antibody compared with those receiving unmodified 2H6 antibody.\", \"We also show that this deglycosylated antibody significantly reduces microhemorrhage incidence compared with the unmodified antibody and is associated with lower levels of cerebral amyloid angiopathy (CAA).\", \"Compact Congophilic amyloid deposits are reduced by intact or deglycosylated anti-Aβ 2H6 antibody administration, whereas vascular amyloid is increased\", \"Figure 5\", \"Mice treated with de-2H6 antibody also showed significant reductions in compact amyloid deposits in the frontal cortex and hippocampus, but more staining in the vasculature could also be observed in both regions (Fig. 5, frontal cortex, E; hippocampus, F).\", \"When we quantified vascular Congophilic staining by manually deselecting the parenchymal deposits, we observed significant increases in APP transgenic mice treated with the intact 2H6 antibody.\",  \"These increases were 3.5-fold in the frontal cortex and threefold in the hippocampus (Fig. 6C). In comparison, mice treated with the de-2H6 antibody showed significantly less vascular amyloid than the mice treated with the unmodified 2H6 antibody (Fig. 6C). Nonetheless, the vascular deposits in the mice treated with de-2H6 were increased twofold in the frontal cortex and 1.5-fold in the hippocampus (Fig. 6C) when compared with the mice administered the control antibodies.\", \"Total and parenchymal Congo red staining of APP transgenic mice is reduced, whereas vascular Congo red is increased after treatment with intact or deglycosylated anti-Aβ 2H6 (D-2H6).\", \"In the current study, we have shown that deglycosylation of an anti-Aβ antibody retains the ability of the antibody to reduce amyloid deposition and eliminate cognitive deficits with considerable reduction in the potentially adverse vascular changes, such as CAA and microhemorrhage.\",",
    "Curator Statement": false
  },
  "AMGAB0799": {
    "Interaction ID": "AMGAB0799",
    "Antibody ID": "ABID0023.6",
    "Antibody name": "de-2H6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.0695-06.2006",
    "PMID": 16707786.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Deglycosylated Anti-Amyloid-β Antibodies Eliminate Cognitive Deficits and Reduce Parenchymal Amyloid with Minimal Vascular Consequences in Aged Amyloid Precursor Protein Transgenic Mice\", \"Both groups receiving anti-Aβ antibodies showed significant reductions in total Aβ immunochemistry and Congo red.\", \" Here we show that long-term systemic administration of deglycosylated anti-Aβ effectively removes amyloid deposits in old APP transgenic mice despite impaired effector cell interaction.\", \"Figure 3\", \"Figure 4\", \"APP transgenic mice treated with anti-Aβ antibodies 2H6 (Fig. 3, frontal cortex, C; hippocampus, D) or deglycosylated 2H6 (Fig. 3, frontal cortex, E; hippocampus, F) showed significant reductions in total Aβ immunohistochemistry of similar magnitude in both the frontal cortex and hippocampus with both antibodies. Quantification of the percentage area occupied by positive staining showed a 50% reduction in total Aβ in the frontal cortex (Fig. 4A) and a 55% reduction in the hippocampus (Fig. 4B).\", \"Total Aβ immunohistochemistry is significantly reduced in both the frontal cortex and hippocampus by systemic treatment with either intact or deglycosylated anti-Aβ (D-2H6) antibodies.\", \"Compact Congophilic amyloid deposits are reduced by intact or deglycosylated anti-Aβ 2H6 antibody administration, whereas vascular amyloid is increased\", \"Figure 5\", \"Mice treated with de-2H6 antibody also showed significant reductions in compact amyloid deposits in the frontal cortex and hippocampus, but more staining in the vasculature could also be observed in both regions (Fig. 5, frontal cortex, E; hippocampus, F).\", \"Quantification of total Congo red area stained shows significant reductions after 14 weeks of treatment of APP transgenic mice with either intact 2H6 [80% in frontal cortex and hippocampus (Fig. 6A)] or deglycosylated 2H6 [70% in frontal cortex and 55% in hippocampus (Fig. 6A)].\", \"Figure 6\", \"The reduction of parenchymal deposits after de-2H6 treatment was less robust than that observed with the intact 2H6 but was still highly significant [75% in frontal cortex and 65% in hippocampus Fig. 6B)].\", \"Total and parenchymal Congo red staining of APP transgenic mice is reduced, whereas vascular Congo red is increased after treatment with intact or deglycosylated anti-Aβ 2H6 (D-2H6).\", \"In the current study, we have shown that deglycosylation of an anti-Aβ antibody retains the ability of the antibody to reduce amyloid deposition and eliminate cognitive deficits with considerable reduction in the potentially adverse vascular changes, such as CAA and microhemorrhage.\", \"In the current study, we have shown that systemic administration of de-2H6 reduces diffuse amyloid deposits as effectively as its intact counterpart and also produces significant reductions in compact amyloid deposits.\", \"In the current study, we show that a deglycosylated C-terminal anti-Aβ antibody improves cognition and removes amyloid almost as efficiently as the intact version of this antibody.\",",
    "Curator Statement": false
  },
  "AMGAB0800": {
    "Interaction ID": "AMGAB0800",
    "Antibody ID": "ABID0509",
    "Antibody name": "anti-AMN (2908)",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1523/JNEUROSCI.0695-06.2006",
    "PMID": 16707786.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 5\", \"Nonetheless, the vascular deposits in the mice treated with de-2H6 were increased twofold in the frontal cortex and 1.5-fold in the hippocampus (Fig. 6C) when compared with the mice administered the control antibodies.",
    "Curator Statement": false
  },
  "AMGAB0801": {
    "Interaction ID": "AMGAB0801",
    "Antibody ID": "ABID0509",
    "Antibody name": "anti-AMN (2908)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.0695-06.2006",
    "PMID": 16707786.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 3\", \"Figure 4\", \"Total Aβ immunohistochemistry is significantly reduced in both the frontal cortex and hippocampus by systemic treatment with either intact or deglycosylated anti-Aβ (D-2H6) antibodies. A shows quantification of total Aβ immunohistochemistry in the frontal cortex. B shows quantification in the hippocampus. **p < 0.01 when compared with mice treated with control antibody anti-AMN (2908).\", \"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0802": {
    "Interaction ID": "AMGAB0802",
    "Antibody ID": "ABID0002",
    "Antibody name": "Gantenerumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.1405-14.2014",
    "PMID": 25164658.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "We performed a chronic study in APPLondon transgenic mice that received treatment with anti-Aβ antibody gantenerumab and BACE inhibitor RO5508887, either as mono- or combination treatment. Treatment aimed to evaluate efficacy on amyloid progression, similar to preexisting amyloidosis as present in Alzheimer's disease patients. Mono-treatments with either compound caused a dose-dependent reduction of total brain Aβ and amyloid burden.\", \"There are revealing differences between treatment effects on total brain Aβ40/Aβ42 as measured by quantitative immunotype assays and amyloidosis determined by immunohistochemistry and quantitative microscopy (Fig. 4). The extent of plaque reduction can be appreciated in representative brain sections by comparing the substantial plaque deposition present in vehicle-treated animals (Fig. 4A) and the considerable plaque reduction after mono-treatments of BACE inhibitor at high-dose, gantenerumab, and combination treatment with gantenerumab and BACE inhibitor at high-dose (Fig. 4B–D).\", \"Figure 4\", \" In the combination arms, the decrease in plaque number appears dependent on gantenerumab. This is evident by similar levels of plaque numbers measured with gantenerumab alone or in combination with BACE-inhibitor. In contrast, the number of plaques with high dose BACE inhibitor was significantly larger than for antibody mono-treatment. When both high- and low-doses of BACE inhibitor are compared with combination with gantenerumab, a statistically significant (p < 0.001) decrease of plaque numbers are seen in cortex and hippocampus. Notably, the total plaque number in both combination doses with BACE inhibitor and gantenerumab are slightly reduced below levels measured at baseline, which suggests that new plaque formation was efficiently inhibited.\", \"Notably, plaque reduction is most substantial in the animals that received both drugs. E, The quantification and statistical evaluation of the area surface occupied by plaques across all treatment groups for cortex and hippocampus. Decrease of plaque surface is significant while variable in treatment groups compared with vehicle-treated mice. The combination treatment significantly enhances the amyloid-plaque lowering for both the low- and the high-dose of RO5508887 in the cortex. F, Effect of mono- and combination treatments on total plaque number. Significantly enhanced efficacy by combination treatment is seen in both brain regions examined.\", \"Figure 5\", \"The reduction in number of plaques compared with vehicle is most evident in the treatment arms with gantenerumab (monotherapy or in combination with BACE inhibitor). Reduction of plaque number was significant (p < 0.001) in all treatment groups. Nearly complete prevention of de novo plaque formation was observed with gantenerumab alone and in combination with BACE inhibitor.\", \"A morphometrical analysis of the treatment effect in relationship to plaque sizes is shown for cortex and hippocampus. Decrease of plaque numbers is significant in all treatment groups compared with vehicle treated mice. Reduction of plaque number is dose dependent for BACE inhibitor (BI) monotherapy and most pronounced for gantenerumab (Gant) treatment groups.\", \"The decrease of plaque numbers was most apparent and statistical significant for all plaque sizes in the cortical region when baseline levels are compared with combination groups (Fig. 5A), although less pronounced in the hippocampus (Fig. 5B). In the neocortices, which carry highest levels of plaque burden, the number of smaller, 4–64 μm2 plaques was found to be significantly reduced compared with baseline. Plaque numbers were also significantly (p < 0.001 to p < 0.05) reduced for larger plaques of diameters ranging from 64–256 μm2 and also for very large plaques >256 μm2 when compared with the baseline group of APPLondon mice.\", \"The decrease of plaque numbers was most apparent and statistical significant for all plaque sizes in the cortical region when baseline levels are compared with combination groups (Fig. 5A), although less pronounced in the hippocampus (Fig. 5B). In the neocortices, which carry highest levels of plaque burden, the number of smaller, 4–64 μm2 plaques was found to be significantly reduced compared with baseline. Plaque numbers were also significantly (p < 0.001 to p < 0.05) reduced for larger plaques of diameters ranging from 64–256 μm2 and also for very large plaques >256 μm2 when compared with the baseline group of APPLondon mice.\",",
    "Curator Statement": false
  },
  "AMGAB0803": {
    "Interaction ID": "AMGAB0803",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.1762-16.2016",
    "PMID": 27656027.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" We show here that vascular cognitive impairment and dementia (VCID) comorbidity eliminates cognitive efficacy of anti-Aβ immunotherapy, despite amyloid clearance.\", \"We found that there was no cognitive benefit of immunotherapy in our comorbidity model despite comparable reductions in total amyloid burden.\", \"Figure 3\", \"Congo red analysis showed that amyloid levels were reduced in the parenchyma following 3D6 treatment in APP/PS1 mice on both the control diet and the HHcy diet when they were compared with APP/PS1 mice on control diet with control antibody (Fig. 4E). This effect was more pronounced in the hippocampus than the frontal cortex.\", \"Total Aβ deposition, which is mostly diffuse deposition, was reduced in the 3D6-treated animals, both APP/PS1 and APP/PS1/HHcy compared with APP/PS1 controls. Total Aβ deposition in the APP/PS1 mice on HHcy diet with 3D6 were not significantly different compared with APP/PS1 mice on HHcy diet with IgG2a, although they did show trends for reduction.\",",
    "Curator Statement": false
  },
  "AMGAB0804": {
    "Interaction ID": "AMGAB0804",
    "Antibody ID": "ABID0573",
    "Antibody name": "α-Aβ",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1523/JNEUROSCI.2055-09.2009",
    "PMID": 19906959.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Protofibrils, Mature fibrils, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"To exclude that the α-Aβ antibody treatment used here decreased parenchymal Aβ plaques but increased vascular Aβ deposits, we quantified CAA visualized by ThioS staining. However, no differences were detected between treatment and control groups (APP/PS1+ct ab: 0.21 ± 0.09 vs APP/PS1+α-Aβ: 0.17 ± 0.09% area).\",",
    "Curator Statement": false
  },
  "AMGAB0805": {
    "Interaction ID": "AMGAB0805",
    "Antibody ID": "ABID0573",
    "Antibody name": "α-Aβ",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.2055-09.2009",
    "PMID": 19906959.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Protofibrils, Mature fibrils, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" Abeta immunotherapy of 8-9-month-old mice expressing familial AD-causing mutations in the amyloid precursor protein and presenilin-1 genes with an antibody against Abeta decreased compact beta-amyloid plaque burden and promoted survival of newly born neurons in the hippocampal dentate gyrus.\", \"Passive Aβ immunotherapy attenuated β-amyloid pathology in APP/PS1-transgenic mice\", \"Figure 1\", \"There was a significantly lower area fraction of ThioS-positive β-amyloid plaques in APP/PS1 mice treated with Aβ immunotherapy (1.14 ± 0.14% area) compared with control antibody-treated mice (1.75 ± 0.16% area; p < 0.05; unpaired t test).\", \" Although the antibody treatment did not change the 6E10-immunopositive Aβ burden (data not shown), the amount of β-amyloid plaques detected by ThioS staining in the whole brain was significantly reduced by 37.8% in α-Aβ compared with ct ab-treated mice (APP/PS1+ct ab: 1.75 ± 0.16 vs APP/PS1+α-Aβ: 1.14 ± 0.14% area; p < 0.05) (Fig. 1C,D).\", \"In the hippocampus, the area fraction covered with ThioS+ β-amyloid plaques in antibody-treated APP/PS1 mice was >60% lower, from 1.32 ± 0.29% in vehicle-treated APP/PS1 animals to 0.48 ± 0.21% (p = 0.05) in α-Aβ-treated mice.\",",
    "Curator Statement": "Although there is no reduction in immunohistochemical signal, the presented figures in Figure 1 did show less plaques in the treated mice."
  },
  "AMGAB0806": {
    "Interaction ID": "AMGAB0806",
    "Antibody ID": "ABID0573",
    "Antibody name": "α-Aβ",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.2055-09.2009",
    "PMID": 19906959.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "Protofibrils, Mature fibrils, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 1\", \" Although the antibody treatment did not change the 6E10-immunopositive Aβ burden (data not shown), the amount of β-amyloid plaques detected by ThioS staining in the whole brain was significantly reduced by 37.8% in α-Aβ compared with ct ab-treated mice (APP/PS1+ct ab: 1.75 ± 0.16 vs APP/PS1+α-Aβ: 1.14 ± 0.14% area; p < 0.05) (Fig. 1C,D).\",",
    "Curator Statement": "Although there is no reduction in immunohistochemical signal, the presented figures in Figure 1 did show less plaques in the treated mice."
  },
  "AMGAB0807": {
    "Interaction ID": "AMGAB0807",
    "Antibody ID": "ABID0001.6.4",
    "Antibody name": "chaducanumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.2080-16.2016",
    "PMID": 27810931.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In vivo, In vitro",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Multiphoton microscopy (Kastanenka et al., 2015) showed clearance of existing amyloid plaques 3 weeks after chaducanumab treatment. Even though a 6-month-long systemic treatment with chaducanumab did not lead to amyloid plaque clearance, calcium overload in neurons in Tg2576 mice was ameliorated.\", \"Topical application of chaducanumab clears plaques\", \"Acute topical application of chaducanumab led to plaque clearance, determined as a decrease in the amyloid plaque number (Fig. 1B–E,L). A total of 48 ± 4% of plaques disappeared after chaducanumab treatment compared with only 14 ± 3% of plaques disappearing after treatment with a control antibody, P1.17 (Fig. 1J, Mann–Whitney test, p < 0.0001, n = 31 z-stacks in 3 mice treated with chaducanumab, n = 39 z-stacks in 4 mice treated with the control antibody). Furthermore, a decrease in size of 13 ± 2% of the remaining individual plaques was observed after chaducanumab treatment (Fig. 1M). Acute application of chaducanumab did not prevent deposition of new plaques significantly (Fig. 1B,D,K; chaducanumab: 34 ± 5% of new plaques appeared vs control: 44 ± 9%; Mann–Whitney test, p = 0.98; n = 31 z-stacks in 3 mice treated with chaducanumab, n = 39 z-stacks in 4 mice treated with the control antibody). Overall amyloid plaque burden was reduced within the imaged volumes (Fig. 1B–E,O).\", \"Figure 1\", \"Aducanumab treatment resulted in 27 ± 8% reduction in amyloid plaque burden, whereas treatment with the control antibody resulted in a 33 ± 15% increase in amyloid burden (Fig. 1N; Mann–Whitney test, p < 0.0001; n = 31 z-stacks in 3 mice treated with aducanumab, n = 39 z-stacks in 4 mice treated with the control antibody). Therefore, a single topical application of chaducanumab led to a rapid decrease in amyloid burden as measured with longitudinal imaging.\", \"Topical application of chaducanumab leads to plaque clearance in old Tg2576 mice.\", \"Chronic treatment with chaducanumab does not affect existing plaques in very old Tg2576 mice\", \"There was no substantial plaque clearance after the 6 month treatment period in either the chaducanumab- or the control-treated animals (chaducanumab: 4 ± 1% of amyloid plaques were cleared; control: 5 ± 2% of plaques cleared; Mann–Whitney test, p = 0.35; n = 42 z-stacks in 5 mice treated with chaducanumab, n = 22 z-stacks in 3 mice treated with the control antibody), nor was there any evidence of substantial new plaque appearance (chaducanumab: 8.5 ± 2% of new plaques appeared, control: 6 ± 3% of new plaques appeared; Mann–Whitney test, p = 0.06; n = 42 z-stacks in 5 mice treated with chaducanumab, n = 22 z-stacks in 3 mice treated with the control antibody) after control antibody (Fig. 3E–K) or chaducanumab (Fig. 3L–R) treatment. Therefore, the net change in plaque number (Fig. 3B) or amyloid plaque burden (Fig. 3C) was not significant for either condition. The size of plaques was not altered as a result of chaducanumab or control antibody treatment over the 6 month period (46 ± 4% of amyloid plaques increased in size after chaducanumab treatment vs 35 ± 6% of plaques increased in size after control antibody treatment; Mann–Whitney test, p = 0.12; n = 42 z-stacks in 5 mice treated with chaducanumab, n = 22 z-stacks in 3 mice treated with the control antibody).\", \"Figure 3\", \" Cortical amyloid plaque burden from in vivo imaging on the last imaging session was comparable to total cortical amyloid plaque burden analyzed postmortem and similar to that in hippocampus (Fig. 3D).\", \"We demonstrated that acute topical application of chaducanumab, the murine analog of aducanumab, to the brain of Tg2576 mice resulted in clearance of existing amyloid plaques.\", \"Chronic systemic administration over 6 months with chaducanumab failed to clear existing amyloid plaques in these mice (18–24 months of age), consistent with the notion that immunotherapy is more effective for the prevention or treatment of amyloidosis at earlier stages and not as effective in advanced stages with substantial parenchymal plaque deposits.\", \"In conclusion, treatment with chaducanumab led to the improvement of a functional outcome measure without reducing the amyloid load significantly after chronic treatment in very old mice.\",",
    "Curator Statement": false
  },
  "AMGAB0808": {
    "Interaction ID": "AMGAB0808",
    "Antibody ID": "ABID0321",
    "Antibody name": "P1.17",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.2080-16.2016",
    "PMID": 27810931.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...),",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Acute topical application of chaducanumab led to plaque clearance, determined as a decrease in the amyloid plaque number (Fig. 1B–E,L). A total of 48 ± 4% of plaques disappeared after chaducanumab treatment compared with only 14 ± 3% of plaques disappearing after treatment with a control antibody, P1.17 (Fig. 1J, Mann–Whitney test, p < 0.0001, n = 31 z-stacks in 3 mice treated with chaducanumab, n = 39 z-stacks in 4 mice treated with the control antibody). \", \"Treatment with an isotype-matched monoclonal antibody with no known epitope in mouse brain, P1.17, did not result in amyloid plaque clearance (Fig. 1F–J), and there was a modest increase in amyloid burden in these mice over the 3 week period (Fig. 1O).\", \"Figure 1\", \"There was no substantial plaque clearance after the 6 month treatment period in either the chaducanumab- or the control-treated animals (chaducanumab: 4 ± 1% of amyloid plaques were cleared; control: 5 ± 2% of plaques cleared; Mann–Whitney test, p = 0.35; n = 42 z-stacks in 5 mice treated with chaducanumab, n = 22 z-stacks in 3 mice treated with the control antibody), nor was there any evidence of substantial new plaque appearance (chaducanumab: 8.5 ± 2% of new plaques appeared, control: 6 ± 3% of new plaques appeared; Mann–Whitney test, p = 0.06; n = 42 z-stacks in 5 mice treated with chaducanumab, n = 22 z-stacks in 3 mice treated with the control antibody) after control antibody (Fig. 3E–K) or chaducanumab (Fig. 3L–R) treatment. Therefore, the net change in plaque number (Fig. 3B) or amyloid plaque burden (Fig. 3C) was not significant for either condition. The size of plaques was not altered as a result of chaducanumab or control antibody treatment over the 6 month period (46 ± 4% of amyloid plaques increased in size after chaducanumab treatment vs 35 ± 6% of plaques increased in size after control antibody treatment; Mann–Whitney test, p = 0.12; n = 42 z-stacks in 5 mice treated with chaducanumab, n = 22 z-stacks in 3 mice treated with the control antibody).\", \"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0809": {
    "Interaction ID": "AMGAB0809",
    "Antibody ID": "ABID0399",
    "Antibody name": "scFv9",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1523/JNEUROSCI.2795-06.2006",
    "PMID": 17108166.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot, ELISA",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Both anti-Aβ scFvs significantly attenuated Aβ40 and Aβ42 levels in SDS-soluble and SDS-insoluble, formic acid (FA)-soluble extracts (Fig. 3). ScFv9 and scFv42.2 reduced SDS and FA Aβ40 and Aβ42, respectively, and appeared to decrease immunoreactive Aβ loads as well (Fig. 3).\", \"Figure 3\", \"Anti-Aβ scFvs attenuate Aβ deposition in 5-month-old CRND8 mice.\", \"In all scFv-treated mice, plaque loads were decreased significantly (Fig. 4A,B). Aβ40 and Aβ42 levels in the SDS-soluble fraction were also reduced significantly by all scFvs (Fig. 4C) as follows: scFv9 (25 and 20% reduction in Aβ40 and Aβ42, respectively); scFv40.1 (40% reduction in both Aβ40 and Aβ42); and scFV42.2 (30 and 20% reduction in Aβ40 and Aβ42, respectively).\", \"Figure 4\", \"Intracranial Adeno-Associated Virus-Mediated Delivery of Anti-Pan Amyloid β, Amyloid β40, and Amyloid β42 Single-Chain Variable Fragments Attenuates Plaque Pathology in Amyloid Precursor Protein Mice\", \"In situ expression of each of the anti-Aβ scFvs after intracerebroventricular AAV serotype 1 delivery to P0 pups decreased Aβ deposition by 25–50%.\", \"Anti-Aβ scFv reduces Aβ deposition in CRND8 mice\",",
    "Curator Statement": false
  },
  "AMGAB0810": {
    "Interaction ID": "AMGAB0810",
    "Antibody ID": "ABID0399",
    "Antibody name": "scFv9",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.2795-06.2006",
    "PMID": 17108166.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot, ELISA",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Both anti-Aβ scFvs significantly attenuated Aβ40 and Aβ42 levels in SDS-soluble and SDS-insoluble, formic acid (FA)-soluble extracts (Fig. 3). ScFv9 and scFv42.2 reduced SDS and FA Aβ40 and Aβ42, respectively, and appeared to decrease immunoreactive Aβ loads as well (Fig. 3).\", \"Figure 3\", \"Anti-Aβ scFvs attenuate Aβ deposition in 5-month-old CRND8 mice.\", \"In all scFv-treated mice, plaque loads were decreased significantly (Fig. 4A,B). Aβ40 and Aβ42 levels in the SDS-soluble fraction were also reduced significantly by all scFvs (Fig. 4C) as follows: scFv9 (25 and 20% reduction in Aβ40 and Aβ42, respectively); scFv40.1 (40% reduction in both Aβ40 and Aβ42); and scFV42.2 (30 and 20% reduction in Aβ40 and Aβ42, respectively).\", \"Figure 4\", \"Intracranial Adeno-Associated Virus-Mediated Delivery of Anti-Pan Amyloid β, Amyloid β40, and Amyloid β42 Single-Chain Variable Fragments Attenuates Plaque Pathology in Amyloid Precursor Protein Mice\", \"In situ expression of each of the anti-Aβ scFvs after intracerebroventricular AAV serotype 1 delivery to P0 pups decreased Aβ deposition by 25–50%.\", \"Anti-Aβ scFv reduces Aβ deposition in CRND8 mice\", \"Intracranial Adeno-Associated Virus-Mediated Delivery of Anti-Pan Amyloid β, Amyloid β40, and Amyloid β42 Single-Chain Variable Fragments Attenuates Plaque Pathology in Amyloid Precursor Protein Mice\", \"In situ expression of each of the anti-Aβ scFvs after intracerebroventricular AAV serotype 1 delivery to P0 pups decreased Aβ deposition by 25–50%.\", \"Anti-Aβ scFv reduces Aβ deposition in CRND8 mice\",",
    "Curator Statement": false
  },
  "AMGAB0811": {
    "Interaction ID": "AMGAB0811",
    "Antibody ID": "ABID0400",
    "Antibody name": "scFv40.1",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1523/JNEUROSCI.2795-06.2006",
    "PMID": 17108166.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot, ELISA",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In all scFv-treated mice, plaque loads were decreased significantly (Fig. 4A,B). Aβ40 and Aβ42 levels in the SDS-soluble fraction were also reduced significantly by all scFvs (Fig. 4C) as follows: scFv9 (25 and 20% reduction in Aβ40 and Aβ42, respectively); scFv40.1 (40% reduction in both Aβ40 and Aβ42); and scFV42.2 (30 and 20% reduction in Aβ40 and Aβ42, respectively).\", \"Figure 4\", \"The largest effect was demonstrated by scFv40.1, which was possibly attributable to a higher expression level in the mouse brain.\",  \"Intracranial Adeno-Associated Virus-Mediated Delivery of Anti-Pan Amyloid β, Amyloid β40, and Amyloid β42 Single-Chain Variable Fragments Attenuates Plaque Pathology in Amyloid Precursor Protein Mice\", \"In situ expression of each of the anti-Aβ scFvs after intracerebroventricular AAV serotype 1 delivery to P0 pups decreased Aβ deposition by 25–50%.\", \"Anti-Aβ scFv reduces Aβ deposition in CRND8 mice\",",
    "Curator Statement": false
  },
  "AMGAB0812": {
    "Interaction ID": "AMGAB0812",
    "Antibody ID": "ABID0400",
    "Antibody name": "scFv40.1",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.2795-06.2006",
    "PMID": 17108166.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In all scFv-treated mice, plaque loads were decreased significantly (Fig. 4A,B). Aβ40 and Aβ42 levels in the SDS-soluble fraction were also reduced significantly by all scFvs (Fig. 4C) as follows: scFv9 (25 and 20% reduction in Aβ40 and Aβ42, respectively); scFv40.1 (40% reduction in both Aβ40 and Aβ42); and scFV42.2 (30 and 20% reduction in Aβ40 and Aβ42, respectively).\", \"Figure 4\", \"The largest effect was demonstrated by scFv40.1, which was possibly attributable to a higher expression level in the mouse brain.\",  \"Intracranial Adeno-Associated Virus-Mediated Delivery of Anti-Pan Amyloid β, Amyloid β40, and Amyloid β42 Single-Chain Variable Fragments Attenuates Plaque Pathology in Amyloid Precursor Protein Mice\", \"In situ expression of each of the anti-Aβ scFvs after intracerebroventricular AAV serotype 1 delivery to P0 pups decreased Aβ deposition by 25–50%.\", \"Anti-Aβ scFv reduces Aβ deposition in CRND8 mice\",",
    "Curator Statement": false
  },
  "AMGAB0813": {
    "Interaction ID": "AMGAB0813",
    "Antibody ID": "ABID0401",
    "Antibody name": "scFv42.2",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1523/JNEUROSCI.2795-06.2006",
    "PMID": 17108166.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Both anti-Aβ scFvs significantly attenuated Aβ40 and Aβ42 levels in SDS-soluble and SDS-insoluble, formic acid (FA)-soluble extracts (Fig. 3). ScFv9 and scFv42.2 reduced SDS and FA Aβ40 and Aβ42, respectively, and appeared to decrease immunoreactive Aβ loads as well (Fig. 3).\", \"Figure 3\", \"Anti-Aβ scFvs attenuate Aβ deposition in 5-month-old CRND8 mice.\", \"In all scFv-treated mice, plaque loads were decreased significantly (Fig. 4A,B). Aβ40 and Aβ42 levels in the SDS-soluble fraction were also reduced significantly by all scFvs (Fig. 4C) as follows: scFv9 (25 and 20% reduction in Aβ40 and Aβ42, respectively); scFv40.1 (40% reduction in both Aβ40 and Aβ42); and scFV42.2 (30 and 20% reduction in Aβ40 and Aβ42, respectively).\", \"Figure 4\", \"Intracranial Adeno-Associated Virus-Mediated Delivery of Anti-Pan Amyloid β, Amyloid β40, and Amyloid β42 Single-Chain Variable Fragments Attenuates Plaque Pathology in Amyloid Precursor Protein Mice\", \"In situ expression of each of the anti-Aβ scFvs after intracerebroventricular AAV serotype 1 delivery to P0 pups decreased Aβ deposition by 25–50%.\", \"Anti-Aβ scFv reduces Aβ deposition in CRND8 mice\", \"Intracranial Adeno-Associated Virus-Mediated Delivery of Anti-Pan Amyloid β, Amyloid β40, and Amyloid β42 Single-Chain Variable Fragments Attenuates Plaque Pathology in Amyloid Precursor Protein Mice\", \"In situ expression of each of the anti-Aβ scFvs after intracerebroventricular AAV serotype 1 delivery to P0 pups decreased Aβ deposition by 25–50%.\", \"Anti-Aβ scFv reduces Aβ deposition in CRND8 mice\",",
    "Curator Statement": false
  },
  "AMGAB0814": {
    "Interaction ID": "AMGAB0814",
    "Antibody ID": "ABID0401",
    "Antibody name": "scFv42.2",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.2795-06.2006",
    "PMID": 17108166.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot, ELISA",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Both anti-Aβ scFvs significantly attenuated Aβ40 and Aβ42 levels in SDS-soluble and SDS-insoluble, formic acid (FA)-soluble extracts (Fig. 3). ScFv9 and scFv42.2 reduced SDS and FA Aβ40 and Aβ42, respectively, and appeared to decrease immunoreactive Aβ loads as well (Fig. 3).\", \"Figure 3\", \"Anti-Aβ scFvs attenuate Aβ deposition in 5-month-old CRND8 mice.\", \"In all scFv-treated mice, plaque loads were decreased significantly (Fig. 4A,B). Aβ40 and Aβ42 levels in the SDS-soluble fraction were also reduced significantly by all scFvs (Fig. 4C) as follows: scFv9 (25 and 20% reduction in Aβ40 and Aβ42, respectively); scFv40.1 (40% reduction in both Aβ40 and Aβ42); and scFV42.2 (30 and 20% reduction in Aβ40 and Aβ42, respectively).\", \"Figure 4\", \"Intracranial Adeno-Associated Virus-Mediated Delivery of Anti-Pan Amyloid β, Amyloid β40, and Amyloid β42 Single-Chain Variable Fragments Attenuates Plaque Pathology in Amyloid Precursor Protein Mice\", \"In situ expression of each of the anti-Aβ scFvs after intracerebroventricular AAV serotype 1 delivery to P0 pups decreased Aβ deposition by 25–50%.\", \"Anti-Aβ scFv reduces Aβ deposition in CRND8 mice\", \"Intracranial Adeno-Associated Virus-Mediated Delivery of Anti-Pan Amyloid β, Amyloid β40, and Amyloid β42 Single-Chain Variable Fragments Attenuates Plaque Pathology in Amyloid Precursor Protein Mice\", \"In situ expression of each of the anti-Aβ scFvs after intracerebroventricular AAV serotype 1 delivery to P0 pups decreased Aβ deposition by 25–50%.\", \"Anti-Aβ scFv reduces Aβ deposition in CRND8 mice\",",
    "Curator Statement": false
  },
  "AMGAB0817": {
    "Interaction ID": "AMGAB0817",
    "Antibody ID": "ABID0004",
    "Antibody name": "Crenezumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.4742-11.2012",
    "PMID": 22787053.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo,",
    "Experimental method(s)": "ThT - Total aggregation (final point), Other: not specified, Other: Laser-scanning microscope,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Furthermore, MABT-mediated amyloid plaque removal was demonstrated using in vivo live imaging in hAPP(V717I)/PS1 transgenic mice.\", \"Figure 1\", \"F, In vitro functionality was shown by the ability of MABT to impede Aβ1–42 aggregation (left panel), and to disassemble preformed Aβ1–42 aggregates (right panel) in a ThT-based assay, with an Aβ1–42 to MABT molar ratio of 10:1. \", \"Inhibition of Aβ assembly and disaggregation of preformed protofibrillar Aβ peptides by MABT\", \"When we compared MABT to a control anti-Aβ mAb directed against the N terminus of Aβ1–42, and thus not overlapping with the core amino acids that form the self-assembly domain, MABT demonstrated 83% greater inhibitory effect on Aβ1–42 aggregation in a ThT assay (Fig. 1F, left panel). Similarly, an 80% greater dissociation of preaggregated Aβ1–42 peptide was observed, when compared with the control N terminus anti-Aβ mAb (Fig. 1F, right panel). \", \"We obtained comparable results in this assay, namely that MABT prevented the self-assembly of Aβ1–42 in a dose-dependent manner (Fig. 1G).\", \"Following a single peripheral MABT administration (60 mg/kg, i.p.), plaque volume decreased over the 3 week period after dosing (average week-to-week normalized change in volume; −0.036, −0.034, and −0.034). A second dose of MABT was administered to a single animal and seven plaques were followed by imaging, three of which were completely removed by week 9. These observations are consistent with our in vitro data suggesting that MABT can induce Aβ removal, presumably via microglia uptake.\", \"Figure 5\", \"On average, the individual plaque size decreased in volume after systemic dosing with MABT (14 plaques, 2 animals).\", \"Furthermore, targeting a unique epitope on Aβ has allowed us to identify an antibody that binds multiple forms of Aβ, including oligomeric forms, while inhibiting aggregation and promoting disaggregation of Aβ.\", \"MABT (also known as crenezumab), a humanized anti-Aβ IgG4 effector-reduced antibody, was selected for its in vitro and in vivo efficacy, including ability to protect neurons from Aβ oligomer-induced toxicity. MABT was also selected for its ability to promote microglial engulfment of Aβ without aberrantly activating microglia. Based on these preclinical data, we hypothesize that MABT would have a reduced risk of vascular-related findings, which are likely a consequence of an anti-Aβ antibody binding aggregated Aβ and maintaining full effector function to elicit a proinflammatory reaction around vascular amyloid.\"",
    "Curator Statement": false
  },
  "AMGAB0818": {
    "Interaction ID": "AMGAB0818",
    "Antibody ID": "ABID0004.6",
    "Antibody name": "mMABT",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.4742-11.2012",
    "PMID": 22787053.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ThT - Total aggregation (final point)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"When compared with vehicle control, treatment with mMABT reduced plaque load in mMABT-treated mice by 31%, and improved memory performance with a 32% increase in recognition index as observed in a novel object recognition test (Fig. 1A). \", \"Figure 1\", \"An in vivo efficacy study administering mMABT to hAPP(V717I) mice showed a reduction in Aβ plaque load (left panel) and improved memory performance (right panel). \"",
    "Curator Statement": false
  },
  "AMGAB0819": {
    "Interaction ID": "AMGAB0819",
    "Antibody ID": "ABID0177",
    "Antibody name": "TOMA",
    "Amyloid ID": "AGAMYID0023",
    "Amyloid name": "Mouse Tau",
    "DOI": "10.1523/JNEUROSCI.4989-14.2015",
    "PMID": 25810517.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Removal of tau oligomers in mice immunized with TOMA rescued cognitive deficits.\", \" Mice receiving TOMA showed an obvious reduction in the appearance of oligomeric tau staining (Fig. 2B).\", \"Figure 2\", \"Quantification by ELISA confirms the reduction of tau oligomer levels in brains of mice receiving TOMA (T22, gray bar, *p < 0.02, two-tailed Student's t test), whereas there was no difference between groups regarding the concentration of total Tau, measured with Tau 5 antibody (two-tailed Student's t test; Fig. 3A).\", \"Reduction of tau oligomers in mice immunized with TOMA.\", \" A remarkable reduction of tau oligomer (showed in red; B) was observed in mice immunized with TOMA.\", \"We next analyzed the status of tau aggregates in brain homogenates from mice immunized with TOMA or control antibody by Western blot using the pan anti-tau antibody Tau 5. A marked and specific reduction of tau oligomers (∼64–150 kDa) was found in only the TOMA group (Fig. 5D).\", \"Here, we extended our studies to examine the mechanistic effects of removal of tau oligomers via immunotherapy in an AD mouse model.\", \"Significantly, we showed that a single intravenous dose of TOMA reduces tau oligomers from the brains of Tg2576 mice and ameliorated memory deficits in a cortex- and hippocampus-dependent manner, implying a role of tau in mediating cognitive decline. \", \"To our surprise, dot blot analysis of the coimmunoprecipitation revealed that mice treated with TOMA exhibited low levels of both tau oligomers and Aβ peptide, confirming our previous results shown early here by ELISA.\",",
    "Curator Statement": false
  },
  "AMGAB0820": {
    "Interaction ID": "AMGAB0820",
    "Antibody ID": "ABID0426",
    "Antibody name": "Anti-Rhodamine antibody",
    "Amyloid ID": "AGAMYID0023",
    "Amyloid name": "Mouse Tau",
    "DOI": "10.1523/JNEUROSCI.4989-14.2015",
    "PMID": 25810517.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, Western blot,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 2\", \"Mice treated with the control antibody (IgG group) showed abundant tau oligomers (stained with T22 and shown in red) in the cortex area (Fig. 2A) and a characteristic staining pattern with 4G8 (anti-β-amyloid antibody; Fig. 2C, green).\", \"Merge is shown in E and F. Mice receiving the control antibody (IgG group) showed abundant tau oligomers (showed in red; A) and a characteristic 4G8 immunoreaction pattern (showed in green; C).\", \"Figure 5\", \"We next analyzed the status of tau aggregates in brain homogenates from mice immunized with TOMA or control antibody by Western blot using the pan anti-tau antibody Tau 5. A marked and specific reduction of tau oligomers (∼64–150 kDa) was found in only the TOMA group (Fig. 5D).\"",
    "Curator Statement": false
  },
  "AMGAB0821": {
    "Interaction ID": "AMGAB0821",
    "Antibody ID": "ABID0421",
    "Antibody name": "3H3",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1523/JNEUROSCI.5109-14.2015",
    "PMID": 25904780.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"A human monoclonal IgG that binds aβ assemblies and diverse amyloids exhibits anti-amyloid activities in vitro and in vivo\", \"Functional studies showed that 3H3 inhibits both Aβ and LC amyloid formation in vitro and abrogates disruption of hippocampal synaptic plasticity by AD-patient-derived soluble Aβ in vivo. \", \"This IgG mAb, 3H3, recognized diverse amyloids, inhibited elongation of Aβ and LC amyloids, and reduced the disruption of synaptic plasticity in the rat hippocampus by AD brain extract.\", \"At the higher mAb concentrations tested, 0.25–1.0 μm, the 3H3 inhibited Aβ40 fibril elongation, whereas the 30B mAb did not. \", \" At the lower concentrations, 0.06 and 0.13 μm, the time course for fibril formation was delayed, although there was an increase in the total amount of ThT fluorescence relative to the control. Similar results were seen with JTO fibrils (Fig. 3c,d), with inhibition of fibril growth at 0.5 and 1.0 μm and elongation delay at 0.25 μm, which also gave a greater final level of ThT fluorescence than the control.\", \"Figure 3\", \"Dose-dependent inhibition of de novo Aβ and LC amyloid fibril formation by subequimolar 3H3. Aβ and LC monomers were incubated in the presence of dilution series of the 3H3 and 30B mAbs. The progress curves for Aβ (A, B) and LC (C, D) amyloid fibril formation show that 3H3 dose-dependently inhibited the formation of ThT positive amyloidogenic aggregates, whereas the control 30B did not.\", \"At low concentrations, 3H3 delayed fibril formation but increased the total amount of amyloid formed, whereas at higher concentrations, amyloid formation was inhibited.\",\"In conclusion, we have isolated an affinity matured human mAb that binds a pan-amyloid epitope and has binding specificity for aggregated amyloid forms. The mAb has anti-amyloid activities in vitro and in vivo, suggesting that naturally occurring anti-amyloid antibodies such as 3H3 may be protective and have potential as anti-amyloid therapeutics.\"",
    "Curator Statement": false
  },
  "AMGAB0822": {
    "Interaction ID": "AMGAB0822",
    "Antibody ID": "ABID0421",
    "Antibody name": "3H3",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1523/JNEUROSCI.5109-14.2015",
    "PMID": 25904780.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"At the lower concentrations, 0.06 and 0.13 μm, the time course for fibril formation was delayed, although there was an increase in the total amount of ThT fluorescence relative to the control.\", \"Figure 3\", \"At low concentrations, 3H3 delayed fibril formation but increased the total amount of amyloid formed, whereas at higher concentrations, amyloid formation was inhibited.\",",
    "Curator Statement": "At low concentrations the final ThT signal is higher than the control."
  },
  "AMGAB0823": {
    "Interaction ID": "AMGAB0823",
    "Antibody ID": "ABID0421",
    "Antibody name": "3H3",
    "Amyloid ID": "AGAMYID0009",
    "Amyloid name": "Antibody Light chain",
    "DOI": "10.1523/JNEUROSCI.5109-14.2015",
    "PMID": 25904780.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition),",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Functional studies showed that 3H3 inhibits both Aβ and LC amyloid formation in vitro and abrogates disruption of hippocampal synaptic plasticity by AD-patient-derived soluble Aβ in vivo. \", \"This IgG mAb, 3H3, recognized diverse amyloids, inhibited elongation of Aβ and LC amyloids, and reduced the disruption of synaptic plasticity in the rat hippocampus by AD brain extract.\", \" 3H3 concentrations of 0.06 and 0.13 μm did not alter the rate of ThT uptake by JTO.\", \"Figure 3\", \"Dose-dependent inhibition of de novo Aβ and LC amyloid fibril formation by subequimolar 3H3. Aβ and LC monomers were incubated in the presence of dilution series of the 3H3 and 30B mAbs. The progress curves for Aβ (A, B) and LC (C, D) amyloid fibril formation show that 3H3 dose-dependently inhibited the formation of ThT positive amyloidogenic aggregates, whereas the control 30B did not.\", \"At low concentrations, 3H3 delayed fibril formation but increased the total amount of amyloid formed, whereas at higher concentrations, amyloid formation was inhibited.\", \"In conclusion, we have isolated an affinity matured human mAb that binds a pan-amyloid epitope and has binding specificity for aggregated amyloid forms. The mAb has anti-amyloid activities in vitro and in vivo, suggesting that naturally occurring anti-amyloid antibodies such as 3H3 may be protective and have potential as anti-amyloid therapeutics.\"",
    "Curator Statement": "The authors use JTO to refer to a recombinant amyloidogenic λ6 LC variable region cloned from a multiple myeloma patient."
  },
  "AMGAB0824": {
    "Interaction ID": "AMGAB0824",
    "Antibody ID": "ABID0421",
    "Antibody name": "3H3",
    "Amyloid ID": "AGAMYID0009",
    "Amyloid name": "Antibody Light chain",
    "DOI": "10.1523/JNEUROSCI.5109-14.2015",
    "PMID": 25904780.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"At low concentrations, 3H3 delayed fibril formation but increased the total amount of amyloid formed, whereas at higher concentrations, amyloid formation was inhibited.\", \"Figure 3\",",
    "Curator Statement": "The authors use JTO to refer to a recombinant amyloidogenic λ6 LC variable region cloned from a multiple myeloma patient. At low concentrations the amyloid sigal was increased."
  },
  "AMGAB0825": {
    "Interaction ID": "AMGAB0825",
    "Antibody ID": "ABID0422",
    "Antibody name": "3H3 scFv",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1523/JNEUROSCI.5109-14.2015",
    "PMID": 25904780.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"This IgG mAb, 3H3, recognized diverse amyloids, inhibited elongation of Aβ and LC amyloids, and reduced the disruption of synaptic plasticity in the rat hippocampus by AD brain extract.\", \"Expression of a single-chain variable fragment (scFv) derived from 3H3, attenuated Aβ amyloid deposition in the brains of TgCRND8-transgenic mice and cerebral amyloid angiopathy (CAA) from ADan deposition in a mouse model of FDD.\", \"Figure 5\", \"We assessed the effects of 3H3 scFv expression on Aβ plaque deposition. We stained brain sections from PBS-injected (Fig. 5d,f) or pAAV-3H3 scFv-injected mice (Fig. 5e,g) with either a pan-Aβ mAb (Fig. 5d,e) or an Aβ40-specific mAb (Fig. 5f,g). We did not observe clear differences in the number of plaques present. However, the plaque morphology in the pAAV-3H3 scFv-injected mice was more diffuse (Fig. 5f,g). In the injected mouse brains, the plaques were decorated by the 3H3 scFv, as visualized by anti-c-Myc staining around the plaques (Fig. 5h).\", \"3H3 scFvs attenuates Aβ deposition in 5 month-old CRND8 mice.\", \" Aβ40 levels were significantly lower in the SDS and FA extracts from the AAV-3H3 scFv-injected mice, compared with the control mice, but a statistically significant change was not observed in Aβ42 levels in the SDS and FA extracts or in the Aβ40 or Aβ42 levels in the RIPA-extracted fractions. Quantification of the total Aβ40 plaque burden on brain sections of control and scFv-expressing mice also did not show a significant difference (Fig. 5j).\", \"In the TgCRND8-transgenic mouse model of CNS Aβ deposition, expression of the 3H3 scFv significantly reduced the levels of SDS- and FA-extractable Aβ40, but had no statistically significant change in Aβ42 levels. This selective effect on Aβ40 is consistent with selective targeting of Aβ amyloid because Aβ40 is more selectively deposited in cored amyloid plaques, whereas Aβ42 deposits in both cored amyloid plaques and more diffuse immunoreactive deposits that are not congophilic. Indeed, a change in plaque morphology was noted in the mice expressing the 3H3 scFV because the plaques appeared less compact and more diffuse. The 3H3 scFV was observed to surround Aβ plaques in the brain, suggesting that it may inhibit amyloid formation by plaque binding.\", \" In any case, our data with the 3H3 scFv indicates that pan-amyloid scFv antibodies can attenuate deposition of different amyloids in vivo.\", \"In conclusion, we have isolated an affinity matured human mAb that binds a pan-amyloid epitope and has binding specificity for aggregated amyloid forms. The mAb has anti-amyloid activities in vitro and in vivo, suggesting that naturally occurring anti-amyloid antibodies such as 3H3 may be protective and have potential as anti-amyloid therapeutics.\"",
    "Curator Statement": false
  },
  "AMGAB0826": {
    "Interaction ID": "AMGAB0826",
    "Antibody ID": "ABID0422",
    "Antibody name": "3H3 scFv",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.1523/JNEUROSCI.5109-14.2015",
    "PMID": 25904780.0,
    "Impact of the antibody on amyloid formation": "No effect, Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"A 3H3 single-chain variable fragment (scFv) retained the binding specificity of the 3H3 IgG and, when expressed in the brains of transgenic mice using an adeno-associated virus (AAV) vector, decreased parenchymal Aβ amyloid deposition in TgCRND8 mice and ADan (Danish Amyloid) cerebral amyloid angiopathy in the mouse model of FDD.\", \"Functional studies showed that 3H3 inhibits both Aβ and LC amyloid formation in vitro and abrogates disruption of hippocampal synaptic plasticity by AD-patient-derived soluble Aβ in vivo.\", \"Expression of a single-chain variable fragment (scFv) derived from 3H3, attenuated Aβ amyloid deposition in the brains of TgCRND8-transgenic mice and cerebral amyloid angiopathy (CAA) from ADan deposition in a mouse model of FDD.\", \"We assessed the effects of 3H3 scFv expression on Aβ plaque deposition. We stained brain sections from PBS-injected (Fig. 5d,f) or pAAV-3H3 scFv-injected mice (Fig. 5e,g) with either a pan-Aβ mAb (Fig. 5d,e) or an Aβ40-specific mAb (Fig. 5f,g). We did not observe clear differences in the number of plaques present. However, the plaque morphology in the pAAV-3H3 scFv-injected mice was more diffuse (Fig. 5f,g). In the injected mouse brains, the plaques were decorated by the 3H3 scFv, as visualized by anti-c-Myc staining around the plaques (Fig. 5h).\", \"Figure 5\", \"3H3 scFvs attenuates Aβ deposition in 5 month-old CRND8 mice.\", \" Aβ40 levels were significantly lower in the SDS and FA extracts from the AAV-3H3 scFv-injected mice, compared with the control mice, but a statistically significant change was not observed in Aβ42 levels in the SDS and FA extracts or in the Aβ40 or Aβ42 levels in the RIPA-extracted fractions. Quantification of the total Aβ40 plaque burden on brain sections of control and scFv-expressing mice also did not show a significant difference (Fig. 5j).\", \"In the TgCRND8-transgenic mouse model of CNS Aβ deposition, expression of the 3H3 scFv significantly reduced the levels of SDS- and FA-extractable Aβ40, but had no statistically significant change in Aβ42 levels. This selective effect on Aβ40 is consistent with selective targeting of Aβ amyloid because Aβ40 is more selectively deposited in cored amyloid plaques, whereas Aβ42 deposits in both cored amyloid plaques and more diffuse immunoreactive deposits that are not congophilic. Indeed, a change in plaque morphology was noted in the mice expressing the 3H3 scFV because the plaques appeared less compact and more diffuse. The 3H3 scFV was observed to surround Aβ plaques in the brain, suggesting that it may inhibit amyloid formation by plaque binding.\", \" In any case, our data with the 3H3 scFv indicates that pan-amyloid scFv antibodies can attenuate deposition of different amyloids in vivo.\", \"In conclusion, we have isolated an affinity matured human mAb that binds a pan-amyloid epitope and has binding specificity for aggregated amyloid forms. The mAb has anti-amyloid activities in vitro and in vivo, suggesting that naturally occurring anti-amyloid antibodies such as 3H3 may be protective and have potential as anti-amyloid therapeutics.\"",
    "Curator Statement": false
  },
  "AMGAB0827": {
    "Interaction ID": "AMGAB0827",
    "Antibody ID": "ABID0422",
    "Antibody name": "3H3 scFv",
    "Amyloid ID": "AGAMYID0016",
    "Amyloid name": "ADanPP",
    "DOI": "10.1523/JNEUROSCI.5109-14.2015",
    "PMID": 25904780.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Control mice developed significant Thio-S-positive CAA in the meninges, thalamus, and cerebellum, whereas 3H3 scFv-expressing mice had less CAA pathology in these tissues (Fig. 6a). Quantification of reduction in Thio-S-positive total positive signal as well as the number of Thio-S-labeled blood vessels revealed statistically significant reductions in the 3H3 scFv-expressing mouse brains (Fig. 6b).\", \"Figure 6\", \" In the control mice, typical staining was observed in the hippocampus as well as in the blood vessels in the cerebellum, whereas mice expressing 3H3 scFv had virtually no amyloid-like deposits in the hippocampus and less ADan-positive CAA in the cerebellum (Fig. 6c).\", \"In the FDD model of CAA deposition in ADan mice, 3H3 scFv expression reduced amyloid deposition and CAA while reducing inflammation-associated expression of GFAP.\", \" In any case, our data with the 3H3 scFv indicates that pan-amyloid scFv antibodies can attenuate deposition of different amyloids in vivo.\", \"In conclusion, we have isolated an affinity matured human mAb that binds a pan-amyloid epitope and has binding specificity for aggregated amyloid forms. The mAb has anti-amyloid activities in vitro and in vivo, suggesting that naturally occurring anti-amyloid antibodies such as 3H3 may be protective and have potential as anti-amyloid therapeutics.\"",
    "Curator Statement": false
  },
  "AMGAB0828": {
    "Interaction ID": "AMGAB0828",
    "Antibody ID": "ABID0423",
    "Antibody name": "30B",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.1523/JNEUROSCI.5109-14.2015",
    "PMID": 25904780.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"At the higher mAb concentrations tested, 0.25–1.0 μm, the 3H3 inhibited Aβ40 fibril elongation, whereas the 30B mAb did not. \", \"At the lower concentrations, 0.06 and 0.13 μm, the time course for fibril formation was delayed, although there was an increase in the total amount of ThT fluorescence relative to the control. Similar results were seen with JTO fibrils (Fig. 3c,d), with inhibition of fibril growth at 0.5 and 1.0 μm and elongation delay at 0.25 μm, which also gave a greater final level of ThT fluorescence than the control.\", \"Figure 3\", \"Dose-dependent inhibition of de novo Aβ and LC amyloid fibril formation by subequimolar 3H3. Aβ and LC monomers were incubated in the presence of dilution series of the 3H3 and 30B mAbs. The progress curves for Aβ (A, B) and LC (C, D) amyloid fibril formation show that 3H3 dose-dependently inhibited the formation of ThT positive amyloidogenic aggregates, whereas the control 30B did not.\",",
    "Curator Statement": false
  },
  "AMGAB0829": {
    "Interaction ID": "AMGAB0829",
    "Antibody ID": "ABID0013.5",
    "Antibody name": "9E4",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1523/JNEUROSCI.5314-13.2014",
    "PMID": 25009275.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo, In cellulo",
    "Experimental method(s)": "Immunohistochemistry, Immunobloting,",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"CT α-syn antibodies attenuated synaptic and axonal pathology, reduced the accumulation of CT-truncated α-syn (CT-α-syn) in axons, rescued the loss of tyrosine hydroxylase fibers in striatum, and improved motor and memory deficits. Among them, 1H7 and 5C1 were most effective at decreasing levels of CT-α-syn and higher-molecular-weight aggregates.\", \"Immunotherapy reduced the accumulation of CT-truncated α-syn and improved axonal and motor deficits by protecting α-syn from CT cleavage.\", \"Passive immunotherapy reduces the accumulation of CT-α-syn in the cortex and striatum of mThy1-α-syn tg mice\", \" We observed a trend toward a reduction in number of cells with intraneuronal accumulation of α-syn in the temporal cortex of animals treated with 9E4 and 1H7, although those differences were not significant compared with IgG1 (27-1)-treated α-syn tg mice (Fig. 3B).\", \"Figure 3\", \"However, measurements of α-syn immunoreactivity in the neuropil showed a significant reduction in animals treated with the antibodies 9E4, 1H7, and 5C1, but not with 5D12, compared with 27-1-treated α-syn tg mice (Fig. 3C). \", \"Immunohistochemical analysis with the antibody SYN105 against CT-α-syn, which recognizes abnormal α-syn aggregates in the neuropil (Games et al., 2013), showed a significant reduction of these aggregates in both temporal cortex and striatum in the α-syn tg mice treated with the 9E4, 1H7, and 5C1 antibodies compared with α-syn tg mice treated with the IgG1 control 27-1 (Fig. 3E,F).\", \"This analysis showed that, compared with α-syn tg animals treated with 27-1 (control IgG1), mice immunized with 9E4, 1H7, and 5C1, but not 5D12, displayed reduced levels of FL-α-syn (14 kDa) and CT-α-syn (12 kDa) in brain homogenates (Fig. 5).\", \"Figure 5\", \"Together, these results show that 1H7 and 5C1 show activity similar to 9E4 at reducing the accumulation of CT-α-syn in the tg mice.\", \"Treatment with 9E4, 1H7, and to a lesser extent 5C1, reduced the percentage of axons in the striatum displaying accumulation of CT-α-syn, whereas 5D12 had no significant effect (Fig. 6B).\", \"Figure 6\", \"CT α-syn antibodies block the propagation of full-length α-syn in vitro\", \" We found that, comparable to 9E4, immunotherapy with the 1H7 and 5C1, and to a lesser extent 5D12, reduced the accumulation and propagation of CT-truncated α-syn and improved the axonal and motor deficits via a mechanism that might involve protecting α-syn from CT cleavage.\", \"Immunotherapy with the 5C1 analog of 9E4, but not with the 5D12 analog, reduced α-syn accumulation and related deficits in vivo.\", \"B, In tg animals immunized with CT α-syn antibodies, propagation of extracellular α-syn oligomers is inhibited and α-syn is protected from CT truncation. The rate of α-syn aggregation is thus diminished and α-syn oligomers can be effectively directed toward clearance pathways.\",",
    "Curator Statement": false
  },
  "AMGAB0830": {
    "Interaction ID": "AMGAB0830",
    "Antibody ID": "ABID0013.9",
    "Antibody name": "5C1",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1523/JNEUROSCI.5314-13.2014",
    "PMID": 25009275.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo, In cellulo",
    "Experimental method(s)": "Immunohistochemistry, Immunobloting,",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"CT α-syn antibodies attenuated synaptic and axonal pathology, reduced the accumulation of CT-truncated α-syn (CT-α-syn) in axons, rescued the loss of tyrosine hydroxylase fibers in striatum, and improved motor and memory deficits. Among them, 1H7 and 5C1 were most effective at decreasing levels of CT-α-syn and higher-molecular-weight aggregates.\", \"Immunotherapy reduced the accumulation of CT-truncated α-syn and improved axonal and motor deficits by protecting α-syn from CT cleavage.\", \"Passive immunotherapy reduces the accumulation of CT-α-syn in the cortex and striatum of mThy1-α-syn tg mice\", \"Figure 3\", \"However, measurements of α-syn immunoreactivity in the neuropil showed a significant reduction in animals treated with the antibodies 9E4, 1H7, and 5C1, but not with 5D12, compared with 27-1-treated α-syn tg mice (Fig. 3C).\", \"Immunohistochemical analysis with the antibody SYN105 against CT-α-syn, which recognizes abnormal α-syn aggregates in the neuropil (Games et al., 2013), showed a significant reduction of these aggregates in both temporal cortex and striatum in the α-syn tg mice treated with the 9E4, 1H7, and 5C1 antibodies compared with α-syn tg mice treated with the IgG1 control 27-1 (Fig. 3E,F).\", \"This analysis showed that, compared with α-syn tg animals treated with 27-1 (control IgG1), mice immunized with 9E4, 1H7, and 5C1, but not 5D12, displayed reduced levels of FL-α-syn (14 kDa) and CT-α-syn (12 kDa) in brain homogenates (Fig. 5).\", \"Figure 5\", \"Together, these results show that 1H7 and 5C1 show activity similar to 9E4 at reducing the accumulation of CT-α-syn in the tg mice.\", \"Treatment with 9E4, 1H7, and to a lesser extent 5C1, reduced the percentage of axons in the striatum displaying accumulation of CT-α-syn, whereas 5D12 had no significant effect (Fig. 6B).\", \"Figure 6\", \"CT α-syn antibodies block the propagation of full-length α-syn in vitro\", \" We found that, comparable to 9E4, immunotherapy with the 1H7 and 5C1, and to a lesser extent 5D12, reduced the accumulation and propagation of CT-truncated α-syn and improved the axonal and motor deficits via a mechanism that might involve protecting α-syn from CT cleavage.\", \"Immunotherapy with the 5C1 analog of 9E4, but not with the 5D12 analog, reduced α-syn accumulation and related deficits in vivo.\", \"B, In tg animals immunized with CT α-syn antibodies, propagation of extracellular α-syn oligomers is inhibited and α-syn is protected from CT truncation. The rate of α-syn aggregation is thus diminished and α-syn oligomers can be effectively directed toward clearance pathways.\",",
    "Curator Statement": false
  },
  "AMGAB0831": {
    "Interaction ID": "AMGAB0831",
    "Antibody ID": "ABID0287",
    "Antibody name": "1H7",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1523/JNEUROSCI.5314-13.2014",
    "PMID": 25009275.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo, In cellulo",
    "Experimental method(s)": "Immunohistochemistry, Immunobloting,",
    "Amyloid species identified": "Protein monomer, Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"CT α-syn antibodies attenuated synaptic and axonal pathology, reduced the accumulation of CT-truncated α-syn (CT-α-syn) in axons, rescued the loss of tyrosine hydroxylase fibers in striatum, and improved motor and memory deficits. Among them, 1H7 and 5C1 were most effective at decreasing levels of CT-α-syn and higher-molecular-weight aggregates.\", \"Immunotherapy reduced the accumulation of CT-truncated α-syn and improved axonal and motor deficits by protecting α-syn from CT cleavage.\", \"Passive immunotherapy reduces the accumulation of CT-α-syn in the cortex and striatum of mThy1-α-syn tg mice\", \" We observed a trend toward a reduction in number of cells with intraneuronal accumulation of α-syn in the temporal cortex of animals treated with 9E4 and 1H7, although those differences were not significant compared with IgG1 (27-1)-treated α-syn tg mice (Fig. 3B).\", \"Figure 3\", \"However, measurements of α-syn immunoreactivity in the neuropil showed a significant reduction in animals treated with the antibodies 9E4, 1H7, and 5C1, but not with 5D12, compared with 27-1-treated α-syn tg mice (Fig. 3C).\", \"Immunohistochemical analysis with the antibody SYN105 against CT-α-syn, which recognizes abnormal α-syn aggregates in the neuropil (Games et al., 2013), showed a significant reduction of these aggregates in both temporal cortex and striatum in the α-syn tg mice treated with the 9E4, 1H7, and 5C1 antibodies compared with α-syn tg mice treated with the IgG1 control 27-1 (Fig. 3E,F).\", \"This analysis showed that, compared with α-syn tg animals treated with 27-1 (control IgG1), mice immunized with 9E4, 1H7, and 5C1, but not 5D12, displayed reduced levels of FL-α-syn (14 kDa) and CT-α-syn (12 kDa) in brain homogenates (Fig. 5).\", \"Figure 5\", \"Together, these results show that 1H7 and 5C1 show activity similar to 9E4 at reducing the accumulation of CT-α-syn in the tg mice.\", \"Treatment with 9E4, 1H7, and to a lesser extent 5C1, reduced the percentage of axons in the striatum displaying accumulation of CT-α-syn, whereas 5D12 had no significant effect (Fig. 6B).\", \"Figure 6\", \"CT α-syn antibodies block the propagation of full-length α-syn in vitro\", \" We found that, comparable to 9E4, immunotherapy with the 1H7 and 5C1, and to a lesser extent 5D12, reduced the accumulation and propagation of CT-truncated α-syn and improved the axonal and motor deficits via a mechanism that might involve protecting α-syn from CT cleavage.\",\"B, In tg animals immunized with CT α-syn antibodies, propagation of extracellular α-syn oligomers is inhibited and α-syn is protected from CT truncation. The rate of α-syn aggregation is thus diminished and α-syn oligomers can be effectively directed toward clearance pathways.\",",
    "Curator Statement": false
  },
  "AMGAB0832": {
    "Interaction ID": "AMGAB0832",
    "Antibody ID": "ABID0288",
    "Antibody name": "5D12",
    "Amyloid ID": "AGAMYID0007",
    "Amyloid name": "Alpha-synuclein",
    "DOI": "10.1523/JNEUROSCI.5314-13.2014",
    "PMID": 25009275.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In vivo, In cellulo",
    "Experimental method(s)": "Immunohistochemistry, Immunobloting,",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"CT α-syn antibodies attenuated synaptic and axonal pathology, reduced the accumulation of CT-truncated α-syn (CT-α-syn) in axons, rescued the loss of tyrosine hydroxylase fibers in striatum, and improved motor and memory deficits.\", \"Immunotherapy reduced the accumulation of CT-truncated α-syn and improved axonal and motor deficits by protecting α-syn from CT cleavage. \", \"Passive immunotherapy reduces the accumulation of CT-α-syn in the cortex and striatum of mThy1-α-syn tg mice\", \"Figure 3\", \"However, measurements of α-syn immunoreactivity in the neuropil showed a significant reduction in animals treated with the antibodies 9E4, 1H7, and 5C1, but not with 5D12, compared with 27-1-treated α-syn tg mice (Fig. 3C).\", \"Immunohistochemical analysis with the antibody SYN105 against CT-α-syn, which recognizes abnormal α-syn aggregates in the neuropil (Games et al., 2013), showed a significant reduction of these aggregates in both temporal cortex and striatum in the α-syn tg mice treated with the 9E4, 1H7, and 5C1 antibodies compared with α-syn tg mice treated with the IgG1 control 27-1 (Fig. 3E,F).\", \"Treatment with the antibody 5D12 resulted in a significant reduction of CT-α-syn in neocortex, but not in striatum (Fig. 3E,F).\", \"This analysis showed that, compared with α-syn tg animals treated with 27-1 (control IgG1), mice immunized with 9E4, 1H7, and 5C1, but not 5D12, displayed reduced levels of FL-α-syn (14 kDa) and CT-α-syn (12 kDa) in brain homogenates (Fig. 5).\", \"Figure 5\",\"Treatment with 9E4, 1H7, and to a lesser extent 5C1, reduced the percentage of axons in the striatum displaying accumulation of CT-α-syn, whereas 5D12 had no significant effect (Fig. 6B).\", \"Figure 6\", \"CT α-syn antibodies block the propagation of full-length α-syn in vitro\",\" We found that, comparable to 9E4, immunotherapy with the 1H7 and 5C1, and to a lesser extent 5D12, reduced the accumulation and propagation of CT-truncated α-syn and improved the axonal and motor deficits via a mechanism that might involve protecting α-syn from CT cleavage.\", \"Immunotherapy with the 5C1 analog of 9E4, but not with the 5D12 analog, reduced α-syn accumulation and related deficits in vivo. Consistent with this finding, 5D12 blocked the CT cleavage of α-syn and the propagation of α-syn to a lesser extent.\",  \"B, In tg animals immunized with CT α-syn antibodies, propagation of extracellular α-syn oligomers is inhibited and α-syn is protected from CT truncation. The rate of α-syn aggregation is thus diminished and α-syn oligomers can be effectively directed toward clearance pathways.\",",
    "Curator Statement": false
  },
  "AMGAB0833": {
    "Interaction ID": "AMGAB0833",
    "Antibody ID": "ABID0462",
    "Antibody name": "mAb11",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.15252/emmm.201606370",
    "PMID": 27402340.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro, In cellulo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Western blot",
    "Amyloid species identified": "Oligomers, Mature fibrils,",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 4\", \"Upon pre‐incubation of cryosections with mAb11 (1 μg/ml), amyloid plaque clearance by wt BMDM was significantly stimulated (Fig 4A and B). In line with the results in Fig 1, TREM2‐deficient BMDM were significantly less efficient in clearing amyloid plaques than wt BMDM under the same experimental conditions (Fig 4A and B).\", \"Reduced amyloid plaque clearance by BMDM derived from the Trem2 ko animals upon antibody stimulation was confirmed by Western blotting of total protein lysates generated from cryosections after termination of the experiment. In line with the experiments in Fig 4A and B, mAb11 caused a stronger reduction in Aβ signals on Western blots in the presence than in the absence of TREM2. However, even in the absence of TREM2, a reduction in Aβ was observed with mAb11 pre‐incubation as compared to the no‐antibody control (Fig 4E).\", \"Figure 5\", \" In line with the fAβ42 uptake assays described in Fig 1, this revealed a concentration‐dependent clearance of amyloid plaques (Fig 5A and B). Comparison of the extend of methoxy‐X04‐positive amyloid labeling after clearance by BMDM derived from wt or Trem2 ko mice demonstrates that antibody‐mediated clearance can occur in the absence of TREM2 (Fig 5A and B), similar to the uptake of fAβ42 shown in Fig 1. However, the total capacity to engulf amyloid plaques is reduced in Trem2 ko BMDM (Fig 5A and B). Of note, a statistically significant effect on amyloid plaque clearance is observed in Trem2 ko BMDM at 0.1 μg/ml, a concentration which is therapeutically reachable in brain by appropriate dose adjustment (Bohrmann et al, 2012; Lathuiliere et al, 2016).\", \"After antibody binding to Aβ, uptake and amyloid plaque clearance increase in a concentration‐dependent manner in the presence or absence of functional TREM2, although the total uptake capacity of cells lacking TREM2 is reduced.\", \"We now demonstrate that mAb11, a murine IgG2a antibody, which has similar amyloid binding properties like Gantenerumab (Lathuiliere et al, 2016) which is currently explored in clinical trials (Bohrmann et al, 2012), significantly stimulates Aβ engulfment even in the absence of TREM2.\", \"Anti‐Aβ antibodies stimulate Aβ uptake and amyloid plaque clearance in a dose‐dependent manner in the presence or absence of TREM2.\", \"Albeit compensatory increases of Fc receptor‐mediated phagocytosis, TREM2‐deficient phagocytic cells, showed significantly reduced uptake of antibody‐bound Aβ and as a consequence reduced clearance of amyloid plaques. Titration experiments revealed that reduced efficacy of amyloid plaque clearance by Trem2 knockout cells can be improved by elevating the concentration of therapeutic antibodies.\",",
    "Curator Statement": false
  },
  "AMGAB0834": {
    "Interaction ID": "AMGAB0834",
    "Antibody ID": "ABID0377",
    "Antibody name": "W20",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.2174/15672050113106660176",
    "PMID": 24156260.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"However, the levels of insoluble Aβ40 and Aβ42 (GuHCl fraction) did not decrease (Fig. 7C), which was consistent with the plaque measurements in the mouse brains.\", \"Figure 7\",",
    "Curator Statement": false
  },
  "AMGAB0835": {
    "Interaction ID": "AMGAB0835",
    "Antibody ID": "ABID0377",
    "Antibody name": "W20",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.2174/15672050113106660176",
    "PMID": 24156260.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo, In cellulo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), ELISA",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 7\", \". In the current study, we showed that W20 blocked the binding of A oligomers to SH-SY5Y cells, did not bind to heat shock protein, rescued cognitive impairments in APP/PS1 transgenic mice, and interfered with A levels and deposits in mouse brain.\", \"The neuritic plaque formation was noticeably reduced in the hippocampus with the W20 treatment (Fig. 4E).\", \"Figure 4\", \"Compared with the vehicle-treated AD mice, the W20-treated mice showed significantly lower area fraction and plaque numbers in the hippocampus than in the neocortex (Figs. 5A and 5C). Plaque size in both hippocampus and cortex of the scFv treated mice was not significantly lower than that of vehicle treated AD mice (Fig. 5B). These results suggest that 5 g of W20 can effectively prevent A accumulation and deposition in the hippocampus, but not in the neocortex.\", \"Figure 5\", \"Although Aβ deposits were reduced in the hippocampus (Fig. 4E), the abundance of insoluble Aβ in the whole brain homogenate was not affected, which may have been caused by the much smaller size of the hippocampus compared with that of the whole brain\", \"A significant reduction was observed in the W20-treated group compared with the controls (vehicle) in the number of plaques and plaque area fraction in the hippocampus rather than in the cortex (*P < 0.05). \", \"W20 can also reduce the levels of soluble Aβ40, Aβ42, and hippocampal amyloid burden in AD transgenic mice although it does not contain Fc fragment, which is consistent with previous investigations that addressed that non-Fc mediated mechanisms are also involved in Aβ clearance [43]. \", \"W20 may initially diffuse to the adjacent hippocampus from lateral ventricles after injection, reducing hippocampal plaque burden\", \"Our present results showed that the conformation dependent oligomer-specific scFv antibody, W20, blocked the binding of Aβ oligomers to SH-SY5Y cells, did not bind to heat shock protein, rescued cognitive impairments in APP/PS1 transgenic mice, and decreased A levels and deposits in mouse brain.\"",
    "Curator Statement": "W20 decreased plaque in the hippocampus, while not in the neocortex."
  },
  "AMGAB0836": {
    "Interaction ID": "AMGAB0836",
    "Antibody ID": "ABID0377",
    "Antibody name": "W20",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.2174/15672050113106660176",
    "PMID": 24156260.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), ELISA",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"However, the levels of insoluble Aβ40 and Aβ42 (GuHCl fraction) did not decrease (Fig. 7C), which was consistent with the plaque measurements in the mouse brains.\", \"Figure 7\", \"The neuritic plaque formation was noticeably reduced in the hippocampus with the W20 treatment (Fig. 4E). However, the plaques in the neocortex of W20-treated APP/PS1 mice did not decrease (Fig. 4B).\", \"Figure 4\", \" Plaque size in both hippocampus and cortex of the scFv treated mice was not significantly lower than that of vehicletreated AD mice (Fig. 5B). These results suggest that 5 g of W20 can effectively prevent A accumulation and deposition in the hippocampus, but not in the neocortex.\", \"Figure 5\",",
    "Curator Statement": "W20 decreased plaque in the hippocampus, while not in the neocortex, nor reduced insoluble Aβ-42."
  },
  "AMGAB0837": {
    "Interaction ID": "AMGAB0837",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.2174/1567205011666140812114341",
    "PMID": 25115543.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"APP mice infused with an anti-Aβ monoclonal antibody did show some reduction in  amyloid deposits.\", \" In the posterior cortex,  there  was  a  significant  reduction  of  Congo  red stained  deposits  in  APP  mice  infused  with  6E10  (Fig.  6B) compared with the saline- infused mice. A trend in the same direction  was  observed  in  the  hippocampus. \", \"Figure 6\", \"Treatment with anti-Aβ antibody but not IVIG significantly lowered congophilic compact plaques in posterior cortex in APP transgenic mice. \", \"APP mice treated with  anti-Aβ  antibody showed a significantly decreased Congo red positive staining in posterior cortex and a trend towards a decrease in hippocampus compared to APP mice infused with saline.\", \"There was a slight reduction  in  compacted  amyloid  with  the  mouse  anti-Aβ monoclonal antibody used here, confirming prior work.\"",
    "Curator Statement": false
  },
  "AMGAB0838": {
    "Interaction ID": "AMGAB0838",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.2174/1567205011666140812114341",
    "PMID": 25115543.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Congo Red (CR) staining, Immunohistochemistry",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"No effect of anti-Aβ antibody was observed in anterior cortex.\", \"Treatment with IVIG or anti-Aβ antibody had no effect on Aβ content in APP transgenic mice.\", \"Neither anti-Aβ antibody nor IVIG treatment in APP mice showed significant difference in the percentage of positive  area ratio compared to saline control APP mice in the structures analyzed.\",",
    "Curator Statement": false
  },
  "AMGAB0839": {
    "Interaction ID": "AMGAB0839",
    "Antibody ID": "ABID0441",
    "Antibody name": "5C8H5",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.2174/1567205012666150325183708",
    "PMID": 25817256.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"In conclusion, the novel monoclonal antibody induces more Aβ clearance and less microglial cell activation in the absence of inflamma-tion, accompanied by an increased Th2-polarized immune response, which makes it a more promising therapeutic strat-egy.\",  \"Detergent-soluble (Fig. 3C, E) and 5 M guanidine extraction-prepared insoluble (Fig. 3D, F) Aβ40/Aβ42 peptides in the hippocampus and the cortex were measured using ELISA. The Aβ40/Aβ42 levels of the immunized group declined significantly compared to the IgG group, and they changed to various degrees.\", \"Figure 3\", \"The finding that Aβ40/42 decreased in the brain while increasing in the serum as anti-Aβ antibodies or antigen were administered, was consistent with the previous hypothesis that antibodies entering the CNS to reduce pathology by Aβ deposition were transported from the brain to the periphery. \",",
    "Curator Statement": false
  },
  "AMGAB0840": {
    "Interaction ID": "AMGAB0840",
    "Antibody ID": "ABID0441",
    "Antibody name": "5C8H5",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.2174/1567205012666150325183708",
    "PMID": 25817256.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Compared with 4Aβ1-15-treated mice, the mice in the 5C8H5 group induced more Aβ clearance with less microglial cell activation in a niche of Th2-polarized immune response.\", \"In conclusion, the novel monoclonal antibody induces more Aβ clearance and less microglial cell activation in the absence of inflamma-tion, accompanied by an increased Th2-polarized immune response, which makes it a more promising therapeutic strat-egy.\", \"Detergent-soluble (Fig. 3C, E) and 5 M guanidine extraction-prepared insoluble (Fig. 3D, F) Aβ40/Aβ42 peptides in the hippocampus and the cortex were measured using ELISA. The Aβ40/Aβ42 levels of the immunized group declined significantly compared to the IgG group, and they changed to various degrees.\", \"Figure 3\", \"5C8H5 Induces More Cerebral Plaque Clearance than 4Aβ1-15 in APP/PS1 Mice\", \"Figure 4\", \"The effect of treatment on plaque burden is demonstrated in confocal micrographs of brain sections obtained from the mouse with the median level of Aβ plaque burden within each group (Fig. 4A-C for hippocampus, 4E-G for cortex). The majority of the larger compacted plaques and most of the diffuse deposits were absent in the 5C8H5 group compared to the other two APP/PS1 groups [29]. Quantitative image analysis showed that 5C8H5 and 4Aβ115 reduced Aβ plaque burden by 66% and 41% in the hippocampus and by 61% and 39% in the cortex compared with IgG-treated mice (Fig. 4D, 4H). Notably, the Aβ plaque burden in the 5C8H5-treated mice was statistically lower than in the 4Aβ1-15 group in both the hippocampus and the cortex.\", \"Passive Immunity-Induced Aβ Plaque Clearance with Less Microglial Activation while Microglia Associated with Aβ Plaques Increased \", \"Aβ plaque burdens in 5C8H5-treated mice were statistically less than 4Aβ1-15-treated mice (*P <0.05). \", \"The aforementioned experiments demonstrated that the  MAb 5C8H5 could induce Aβ plaque clearance. \", \"Vaccinating APP/PS1 mice with 5C8H5 significantly reduced Aβ plaques and microglial cell activation with a Th2-polarized immune response, and the inflammation was markedly reduced compared to the homogenous antigen vaccine and controls.\", \"The finding that Aβ40/42 decreased in the brain while increasing in the serum as anti-Aβ antibodies or antigen were administered, was consistent with the previous hypothesis that antibodies entering the CNS to reduce pathology by Aβ deposition were transported from the brain to the periphery. \", \"The immunohistochemistry and quantitative image analyses of brain sections showed that 5C8H5 and 4Aβ1-15 reduced the plaque burden significantly, while the 5C8H5 group showed a markedly lower Aβ burden than the 4Aβ115 group [41]. Thus passive immunization against Aβ peptide is sufficient to reduce amyloid deposition in APP/PS1 mice.\", \" 5C8H5 induces Aβ clearance without exacerbating microhemorrhages.\", \"The novel MAb 5C8H5 produced in our lab reduced Aβ plaques and induced less microglial activation and neuroinflammation; thus, it represents an effective and safe therapy.\",",
    "Curator Statement": false
  },
  "AMGAB0841": {
    "Interaction ID": "AMGAB0841",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.2174/1567205013666161108110031",
    "PMID": 27829339.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, ELISA",
    "Amyloid species identified": "Monomers, oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Whereas fibrillary morphology was maintained after incubation with PBS or a control scFv, 3D6 and B7 scFv were able to disaggregate pre-formed fibrils. In contrast, B6 failed to  disaggregate fibrils probably because of its lower affinity  towards Aβ fibrils over soluble oligomers (52 nM vs 24 nM).\", \"Figure 1\", \"Figure 4\", \"Whereas  the injection of DNA encoding scFv did not result in a decrease of Aβ levels except for 3D6, injection of mRNA resulted in 40 % decrease in an acute amyloidosis model (Fig. 4).\", \"In this more stringent AD model, no decrease  in formic acid-soluble A was measured after injection of B7-IL2ss mRNA polyplexes with similar Aβ burden in mice treated with either PBS, polyplexes prepared with an irrelevant scFv and, polyplexes formed with an anti-Aβ scFv. \", \"In accordance with previous studies, B7 scFv had  affinity towards A fibers and was able to disaggregate pre formed aggregates in vitro [43, 51-53]. \", \"Notably, B7-IL2ss mRNA encoding scFv delivery was able to decrease Aβ burden in an acute amyloidosis model. The finding that only the construct with a secretion sequence was able to decrease Aβ burden suggests that a threshold concentration of extracellular anti-Aβ is required to engage Aβ deposits and promote their disaggregation, a pattern similar to other anti-A 1-42 scFvs [54, 55].\", \"Although a detectable decrease in A burden could be measured in the early AD model, no reduction in A 1-42 levels could be achieved after intracranial injection of the polyplexes in the AD transgenic mouse model.\", \"Our approach challenges these limitations and we demonstrate that introduction of mRNA encoding Aβ-specific scFv can result in detectable antibody levels in the brain with successful transfection of neurons in vivo resulting in decreased Aβ burden in an acute AD mouse model but not a model reflecting later AD stages.\", \"Figure 5\", \"The selected anti-amyloid beta scFv showed affinity towards Aβ and disaggregated Aβ fibers in  vitro.\"",
    "Curator Statement": false
  },
  "AMGAB0842": {
    "Interaction ID": "AMGAB0842",
    "Antibody ID": "ABID0193",
    "Antibody name": "B6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.2174/1567205013666161108110031",
    "PMID": 27829339.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, ELISA",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Whereas fibrillary morphology was maintained after incubation with PBS or a control scFv, 3D6 and B7 scFv were able to disaggregate pre-formed fibrils. In contrast, B6 failed to  disaggregate fibrils probably because of its lower affinity  towards Aβ fibrils over soluble oligomers (52 nM vs 24 nM).\", \"Figure 1\", \"Figure 4\", \"Whereas  the injection of DNA encoding scFv did not result in a decrease of Aβ levels except for 3D6, injection of mRNA resulted in 40 % decrease in an acute amyloidosis model (Fig. 4).\", \"In this more stringent AD model, no decrease  in formic acid-soluble A was measured after injection of B7-IL2ss mRNA polyplexes with similar Aβ burden in mice treated with either PBS, polyplexes prepared with an irrelevant scFv and, polyplexes formed with an anti-Aβ scFv. \", \"In accordance with previous studies, B7 scFv had  affinity towards A fibers and was able to disaggregate pre formed aggregates in vitro [43, 51-53]. \", \"Notably, B7-IL2ss mRNA encoding scFv delivery was able to decrease Aβ burden in an acute amyloidosis model. The finding that only the construct with a secretion sequence was able to decrease Aβ burden suggests that a threshold concentration of extracellular anti-Aβ is required to engage Aβ deposits and promote their disaggregation, a pattern similar to other anti-A 1-42 scFvs [54, 55].\", \"Although a detectable decrease in A burden could be measured in the early AD model, no reduction in A 1-42 levels could be achieved after intracranial injection of the polyplexes in the AD transgenic mouse model.\", \"Our approach challenges these limitations and we demonstrate that introduction of mRNA encoding Aβ-specific scFv can result in detectable antibody levels in the brain with successful transfection of neurons in vivo resulting in decreased Aβ burden in an acute AD mouse model but not a model reflecting later AD stages.\", \"Figure 5\", \"The selected anti-amyloid beta scFv showed affinity towards Aβ and disaggregated Aβ fibers in  vitro.\"",
    "Curator Statement": false
  },
  "AMGAB0843": {
    "Interaction ID": "AMGAB0843",
    "Antibody ID": "ABID0194",
    "Antibody name": "B7",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.2174/1567205013666161108110031",
    "PMID": 27829339.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In vitro, In vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics, ELISA",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Whereas fibrillary morphology was maintained after incubation with PBS or a control scFv, 3D6 and B7 scFv were able to disaggregate pre-formed fibrils. In contrast, B6 failed to  disaggregate fibrils probably because of its lower affinity  towards Aβ fibrils over soluble oligomers (52 nM vs 24 nM).\", \"Figure 1\", \"Figure 4\", \"Whereas  the injection of DNA encoding scFv did not result in a decrease of Aβ levels except for 3D6, injection of mRNA resulted in 40 % decrease in an acute amyloidosis model (Fig. 4).\", \"In this more stringent AD model, no decrease  in formic acid-soluble A was measured after injection of B7-IL2ss mRNA polyplexes with similar Aβ burden in mice treated with either PBS, polyplexes prepared with an irrelevant scFv and, polyplexes formed with an anti-Aβ scFv. \", \"In accordance with previous studies, B7 scFv had  affinity towards A fibers and was able to disaggregate pre formed aggregates in vitro [43, 51-53]. \", \"Notably, B7-IL2ss mRNA encoding scFv delivery was able to decrease Aβ burden in an acute amyloidosis model. The finding that only the construct with a secretion sequence was able to decrease Aβ burden suggests that a threshold concentration of extracellular anti-Aβ is required to engage Aβ deposits and promote their disaggregation, a pattern similar to other anti-A 1-42 scFvs [54, 55].\", \"Although a detectable decrease in A burden could be measured in the early AD model, no reduction in A 1-42 levels could be achieved after intracranial injection of the polyplexes in the AD transgenic mouse model.\", \"Our approach challenges these limitations and we demonstrate that introduction of mRNA encoding Aβ-specific scFv can result in detectable antibody levels in the brain with successful transfection of neurons in vivo resulting in decreased Aβ burden in an acute AD mouse model but not a model reflecting later AD stages.\", \"Figure 5\", \"The selected anti-amyloid beta scFv showed affinity towards Aβ and disaggregated Aβ fibers in  vitro.\"",
    "Curator Statement": false
  },
  "AMGAB0844": {
    "Interaction ID": "AMGAB0844",
    "Antibody ID": "ABID0382",
    "Antibody name": "9D5",
    "Amyloid ID": "AGAMYID0010",
    "Amyloid name": "Transthyretin",
    "DOI": "10.3109/13506129.2016.1148025",
    "PMID": 26981744.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, ELISA",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 3\", \"In contrast, 9D5 unexpectedly failed to inhibit TTR-V122I fibril formation, despite showing similar specificity and affinity for non-native TTR. It remains to be explored whether 9D5 is more sensitive to the assay conditions used (e.g. low pH).\", \"That 9D5 failed to inhibit in vitro fibrillogenesis was unexpected since this antibody showed binding affinities and selectivity for non-native conformations of TTR similar to the other three mis-TTR mAbs. \",",
    "Curator Statement": false
  },
  "AMGAB0845": {
    "Interaction ID": "AMGAB0845",
    "Antibody ID": "ABID0383",
    "Antibody name": "14G8",
    "Amyloid ID": "AGAMYID0010",
    "Amyloid name": "Transthyretin",
    "DOI": "10.3109/13506129.2016.1148025",
    "PMID": 26981744.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, ELISA",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"(B) In contrast to 14G8, the isotype control antibody, EG27/1, did not inhibit TTR fibril formation as demonstrated by no reduction in ThT fluorescence intensity.\",\"Increasing 14G8 mAb concentrations caused a monotonic decrease in ThT fluorescence indicating a substoichiometric inhibition of TTR fibrillation (IC50 = 0.028 ± 0.009 mg/mL; n = 3; Figure 3A and Table 3). The isotype control mAb did not cause inhibition of TTR fibrillation (Figure 3B), thus demonstrating the specificity of 14G8 mediated inhibition.\", \"Table 3\", \"Four identified monoclonal antibodies were characterized. These antibodies selectively bound the target epitope on monomeric and non-native misfolded forms of TTR and strongly suppressed TTR fibril formation in vitro.\"., \"Inhibition of TTR-V122I fibril formation by mis-TTR antibodies (n=3 assays/antibody).\", \"The ability of mis-TTR antibodies to suppress fibrillogenesis in vitro at substoichiometric levels suggests that the TTR amyloidogenic species targeted by mis-TTR mAbs, although very impactful, may be at low abundance in relation to the total TTR in solution.\", \"Thus, it is likely that our mis-TTR mAbs inhibit TTR aggregation and fibril formation by impeding the self-association of the protein as proposed for small non-native peptides specific for this site [38]. \", \"These antibodies inhibit TTR fibrillogenesis and induce antibody-dependent phagocytic uptake of TTR aggregates in vitro.\",",
    "Curator Statement": false
  },
  "AMGAB0846": {
    "Interaction ID": "AMGAB0846",
    "Antibody ID": "ABID0384",
    "Antibody name": "6C1",
    "Amyloid ID": "AGAMYID0010",
    "Amyloid name": "Transthyretin",
    "DOI": "10.3109/13506129.2016.1148025",
    "PMID": 26981744.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 3\", \"Comparable substoichiometric IC50 values determined for 5A1 and 6C1 (Table 3) suggested analogous mechanisms of fibril inhibition for each of these mis-TTR mAbs.\", \"Four identified monoclonal antibodies were characterized. These antibodies selectively bound the target epitope on monomeric and non-native misfolded forms of TTR and strongly suppressed TTR fibril formation in vitro.\"., \"Inhibition of TTR-V122I fibril formation by mis-TTR antibodies (n=3 assays/antibody).\", \"The ability of mis-TTR antibodies to suppress fibrillogenesis in vitro at substoichiometric levels suggests that the TTR amyloidogenic species targeted by mis-TTR mAbs, although very impactful, may be at low abundance in relation to the total TTR in solution.\", \"Thus, it is likely that our mis-TTR mAbs inhibit TTR aggregation and fibril formation by impeding the self-association of the protein as proposed for small non-native peptides specific for this site [38]. \", \"These antibodies inhibit TTR fibrillogenesis and induce antibody-dependent phagocytic uptake of TTR aggregates in vitro.\",",
    "Curator Statement": false
  },
  "AMGAB0847": {
    "Interaction ID": "AMGAB0847",
    "Antibody ID": "ABID0385",
    "Antibody name": "5A1",
    "Amyloid ID": "AGAMYID0010",
    "Amyloid name": "Transthyretin",
    "DOI": "10.3109/13506129.2016.1148025",
    "PMID": 26981744.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Table 3\", \"Comparable substoichiometric IC50 values determined for 5A1 and 6C1 (Table 3) suggested analogous mechanisms of fibril inhibition for each of these mis-TTR mAbs.\", \"Four identified monoclonal antibodies were characterized. These antibodies selectively bound the target epitope on monomeric and non-native misfolded forms of TTR and strongly suppressed TTR fibril formation in vitro.\"., \"Inhibition of TTR-V122I fibril formation by mis-TTR antibodies (n=3 assays/antibody).\", \"The ability of mis-TTR antibodies to suppress fibrillogenesis in vitro at substoichiometric levels suggests that the TTR amyloidogenic species targeted by mis-TTR mAbs, although very impactful, may be at low abundance in relation to the total TTR in solution.\", \"Thus, it is likely that our mis-TTR mAbs inhibit TTR aggregation and fibril formation by impeding the self-association of the protein as proposed for small non-native peptides specific for this site [38]. \", \"These antibodies inhibit TTR fibrillogenesis and induce antibody-dependent phagocytic uptake of TTR aggregates in vitro.\",",
    "Curator Statement": false
  },
  "AMGAB0848": {
    "Interaction ID": "AMGAB0848",
    "Antibody ID": "ABID0386",
    "Antibody name": "EG27/1",
    "Amyloid ID": "AGAMYID0010",
    "Amyloid name": "Transthyretin",
    "DOI": "10.3109/13506129.2016.1148025",
    "PMID": 26981744.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative Control",
    "Quote of the interaction": "\"Figure 3\", \"(B) In contrast to 14G8, the isotype control antibody, EG27/1, did not inhibit TTR fibril formation as demonstrated by no reduction in ThT fluorescence intensity.\", \"Increasing 14G8 mAb concentrations caused a monotonic decrease in ThT fluorescence indicating a substoichiometric inhibition of TTR fibrillation (IC50 = 0.028 ± 0.009 mg/mL; n = 3; Figure 3A and Table 3). The isotype control mAb did not cause inhibition of TTR fibrillation (Figure 3B), thus demonstrating the specificity of 14G8 mediated inhibition.\", \"Table 3\",",
    "Curator Statement": false
  },
  "AMGAB0849": {
    "Interaction ID": "AMGAB0849",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-120850",
    "PMID": 23160008.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0850": {
    "Interaction ID": "AMGAB0850",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-120850",
    "PMID": 23160008.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 2\",",
    "Curator Statement": false
  },
  "AMGAB0851": {
    "Interaction ID": "AMGAB0851",
    "Antibody ID": "ABID0454",
    "Antibody name": "HJ3.4",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.3233/JAD-132789",
    "PMID": 24643138.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Soluble Aβ was extracted from cortexes and hippocampi by TBS followed by extraction of insoluble using formic acid, and Aβ was evaluated by ELISA. On panel A is shown insoluble Aβ40 and Aβ42 and on panel B, soluble Aβ40 and Aβ42. C, The level of Aβ oligomers was measured in soluble fraction using dimer-specific ELISA as described in the methods. For all panels, difference between the means were analyzed by one-way ANOVA and showed no significant change and two-way ANOVA demonstrated no interaction and no significant main effects of LXR or anti- Aβ treatments.\",",
    "Curator Statement": false
  },
  "AMGAB0852": {
    "Interaction ID": "AMGAB0852",
    "Antibody ID": "ABID0454",
    "Antibody name": "HJ3.4",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-132789",
    "PMID": 24643138.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Histological quantification, Immunohistochemistry, ELISA",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Amyloid plaques are unaffected by Aβ immunization or LXR agonist\", \" Fig. 2 demonstrates that neither treatment affected % area (Fig. 2A and B) or number of the compact amyloid plaques (Fig. 2C and D) in hippocampus and cortex. \", \"Figure 2\", \"Aβ immunization and LXR agonist treatment did not affect amyloid plaque level and insoluble amyloid in depositing APP23 mice.\", \"Aβ immunization and LXR agonist treatment did not affect amyloid plaque level and insoluble amyloid in depositing APP23 mice.\", \"Figure 3\", \"Soluble and insoluble Aβ is not affected by Aβ immunization and LXR agonist treatment.\", \"Furthermore, our data demonstrate that even though there was no effect on amyloid plaques, anti-Aβ antibody and LXR ligand treatments improved significantly the performance in two behavior tests (see Fig. 1). \",",
    "Curator Statement": false
  },
  "AMGAB0853": {
    "Interaction ID": "AMGAB0853",
    "Antibody ID": "ABID0006.5",
    "Antibody name": "mAb158",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-140741",
    "PMID": 25096615.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Sandwich ELISA, Immunoprecipitation",
    "Amyloid species identified": "Protein monomer, Oligomers, Protofibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"mAb158 reached the brain and reduced the brain protofibril levels by 42% in an exposure-dependent manner both after long-term and short-term treatment in tg-ArcSwe mice. Notably, a 53% reduction of protofibrils/oligomers in cerebrospinal fluid (CSF) that correlated with reduced brain protofibril levels was observed after long-term treatment, suggesting that CSF protofibrils/oligomers could be used as a potential biomarker. \", \"Further, we find that the mAb158-mediated selective reduction of brain Aβ protofibrils was mirrored by a similar lowering of protofibrils in cerebrospinal fluid (CSF) from tg-ArcSwe mice, indicating a possible use of CSF Aβ protofibrils as a clinical biomarker.\", \"Long-term administration of mAb158 in tg-ArcSwe mice reduces Aβ protofibril levels in brain and CSF\", \"A significant 42% reduction of brain protofibrils was detected in mAb158-treated mice compared to placebo-treated mice (Fig. 4A).\", \"Figure 4\", \" Long-term treatment with mAb158 reduces Aβ protofibril levels in brain and CSF of tg-ArcSwe mice. \", \"A significant 42% reduction in brain protofibril levels was detected in mice receiving long-term treatment with mAb158, compared to placebo-treated mice (t-test, p < 0.0001).\", \"B) Aβ protofibril/oligomer levels in CSF were measured with the 82E1 sandwich ELISA. A significant 53% reduction in protofibril/oligomer levels was detected in mAb158-treated mice, compared to placebo-treated mice (t-test, p < 0.0001). C) A highly significant correlation was observed between protofibrils in brain and protofibrils/oligomers in CSF (Pearson’s rank correlation, p < 0.0001, R2 = 0.291). \", \"A 53% reduction of protofibrils/oligomers was detected in CSF from mAb158-treated mice compared to placebo (Fig. 4B).\", \"The treatment effect was also evaluated in 100000× g brain TBS extracts and was similar to the effect observed in the 16000× g TBS extracts (46% reduction in protofibril levels after longterm treatment with mAb158 compared to placebo, data not shown).\", \" To ensure that these results were not limited to a transgenic model carrying the Arctic mutation, long-term treatment with mAb158 was performed in Tg2576 mice, resulting in a 27% reduction in brain protofibril levels after treatment with 12 mg/kg mAb158, and a 40% reduction after treatment with 24 mg/kg mAb158 (see Supplementary Fig. 6).\", \"Supplementary Figure 5.\", \"Short-term treatment with mAb158 reduces Aβ protofibril levels in brain and of tg-ArcSwe mice.\", \"Significant reductions in protofibrils were detected in mAb158-treated mice sacrificed both 24 h (42%) and 7 days (48%) after the last injection, compared to PBS-treated mice (also sacrificed 7 days after the last injection, one-way ANOVA p=0.003, followed by Tukey’s multiple comparison test).\", \"Supplementary Figure 6\", \"Long-term treatment with mAb158 reduces Aβ protofibril levels in brain of Tg2576 mice.\", \"Significant reductions reduction in brain protofibril levels were detected both in Tg2576 mice receiving 12 mg/kg (27%), and in mice receiving 24 mg/kg mAb158 (40%, one-way ANOVA p<0.0001, followed by Tukey’s multiple comparison test), compared to placebo-treated mice. \", \"Short-term administration of mAb158 in tg-ArcSwe mice reduces Aβ protofibril levels in brain and CSF\", \"Short-term treatment with mAb158 resulted in a significant 42% reduction of Aβ protofibrils in brain TBS extracts from mAb158-treated mice sacrificed 7 days after the last injection, compared to placebo-treated mice (Fig. 5A).\", \"A trend toward protofibril reduction was observed in brain of mAb158treated mice sacrificed 24 h after the last injection and in CSF protofibrils/oligomers of mice sacrificed at 7 days and 24 h, although these reductions did not reach significance (Fig. 5B).\", \" The protofibril reductions observed in TBS extracts after short-term treatment with mAb158 were verified with the 82E1 sandwich ELISA. A 42% reduction in brain protofibrils/oligomers was observed in mice sacrificed 24 h after the last injection, and a 48% reduction in mice sacrificed 7 days after the last injection.\", \"mAb158 reaches the brain and correlates with reduced brain protofibril levels in tg-ArcSwe mice\", \"Figure 5\", \"Short-term treatment with mAb158 reduces Aβ protofibril levels in brain and CSF of tg-ArcSwe mice. \", \"A significant 42% reduction in protofibrils was detected in mAb158-treated mice sacrificed 7 days after the last injection, compared to PBS-treated mice (also sacrificed 7 days after the last injection, one-way ANOVA p = 0.0076, followed by Tukey’s multiple comparison test). A trend towards reduction in brain protofibrils was observed 24 h after the last mAb158 injection, but this reduction was non-significant.\", \"A trend towards reduction in protofibril/oligomer levels was detected in mAb158-treated mice, compared to untreated mice, but this reduction did not reach significance (one-way ANOVA p = 0.054).\", \"mAb158 reaches the brain and correlates with reduced protofibril levels in tg-ArcSwe mice.\", \"Long-term treatment with mAb158 reduces soluble aggregated Aβ levels in brain\", \"Long-term treatment with mAb158 reduces SDS-denatured Aβ1-42 levels in brain from tg-ArcSwe mice.\", \"Figure 7\", \"A significant 29% reduction in SDS-denatured Aβ1-42 was detected in the mice that received mAb158, compared to placebo-treated mice (t-test, p < 0.001).\", \"A significant 29% reduction of total Aβ42 in SDS-denatured TBS extracts was observed in mice that had received longterm treatment with mAb158 compared to placebo (Fig. 7).\", \"Taken together, these results indicate the specific ability of mAb158 to selectively bind and reduce soluble Aβ protofibrils in vitro and in vivo, with minimal binding to native Aβ monomers.\", \"We have also used mAb158 for long- and short-term treatment of tg-ArcSwe mice, and found that mAb158 reaches the brain from the plasma compartment and that the treatment leads to reduced levels of soluble Aβ protofibrils in brain extracts in an exposure-dependent manner. Importantly, we demonstrate that the reduction of brain protofibrils in tg-ArcSwe mice was mirrored by a reduction of protofibrils/oligomers in CSF, indicating the use of CSF protofibrils/oligomers as a biomarker for treatment effect.\", \"In both the long-term and the short-term mAb158 treatment studies in tg-ArcSwe mice, a significant treatment effect on brain protofibrils was found, and this effect correlated to brain mAb158 concentration suggesting an exposure-dependent treatment effect.\", \"A strong treatment effect on brain protofibril levels could be observed after long- and short-term treatment in the subgroup sacrificed 7 days after the last injection.\", \"In addition to the brain protofibril clearance, a reduction in CSF protofibrils that correlated to brain protofibrils was observed in the long-term study. However, a trend toward brain and CSF protofibril reductions could be shown in the subgroup of mice that had received short-term treatment and was sacrificed 24 h after the last injection.\",",
    "Curator Statement": false
  },
  "AMGAB0854": {
    "Interaction ID": "AMGAB0854",
    "Antibody ID": "ABID0007",
    "Antibody name": "Bapineuzumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-160369",
    "PMID": 27589523.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Positron emission tomography (PET)",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Florbetapir PET SUVR decreased significantly (p = 0.038) from baseline to month 12 for the bapineuzumab 7 mg/month group only; reductions versus placebo were not significant for any dosage. \", \"Table 3\",  \" In this study, no statistically significant difference was observed between any dose of bapineuzumab and placebo with respect to the reduction in florbetapir PET GCA SUVR at month 12 from baseline in the planned analyses. The florbetapir PET GCA SUVR at month 12 showed a statistically significant reduction from baseline for only the 7 mg/month dose, with no evidence of a dose-related trend.\", \"The results of this truncated study did not demonstrate any clinically significant differences between placebo and once-monthly SC bapineuzumab 2, 7, or 20 mg for 12 months on change in cerebral amyloid signal from baseline.\"",
    "Curator Statement": false
  },
  "AMGAB0855": {
    "Interaction ID": "AMGAB0855",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.3233/JAD-170056",
    "PMID": 28800329.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 7\",",
    "Curator Statement": "While treatment with 3D6 did not alter the total anti-Aβ40 reactive deposits, the non-vessels were increased thile the vessel-associated decreased."
  },
  "AMGAB0856": {
    "Interaction ID": "AMGAB0856",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.3233/JAD-170056",
    "PMID": 28800329.0,
    "Impact of the antibody on amyloid formation": "No effect,",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 7\", \"Treatment with 3D6 did not significantly alter the levels of Aβ40 deposits whether quantified as total or after separation into non-vessel and vessel-associated pools (c.f. Fig. 7B-D).\",",
    "Curator Statement": "While treatment with 3D6 did not alter the total anti-Aβ40 reactive deposits, the non-vessels were increased thile the vessel-associated decreased."
  },
  "AMGAB0857": {
    "Interaction ID": "AMGAB0857",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.3233/JAD-170056",
    "PMID": 28800329.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 7\",",
    "Curator Statement": "While treatment with 3D6 did not alter the total anti-Aβ40 reactive deposits, the non-vessels were increased thile the vessel-associated decreased."
  },
  "AMGAB0858": {
    "Interaction ID": "AMGAB0858",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-170056",
    "PMID": 28800329.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition),",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The finding that 3D6-treated mice show little difference in plaque load versus theisotype control antibody mice is consistent with results shown in Figs. 7 and 8.\", \"Figure 6\", \"Figure 7\", \"Figure 8\", \"Total Aβ42 area was not significantly different between the verubecestat or 3D6 treatment groups and their respective controls (Fig. 8B).\", \"The 3D6 treated group showed no change in total Aβ42 deposits versus isotype control-treated mice (Fig. 8B) and a significant increase in non-vessel associated Aβ42 (+38%; p < 0.05, t-test) and a small decrease in vessel Aβ42 deposits (–7%, p < 0.05, t-test; c.f. Fig. 8C, D). \"The increase in ARIA-H occurred despite minimal effects of 3D6 on brain Aβ load.\"",
    "Curator Statement": "The treatment resulted in a small decrease of deposits of Aβ-42."
  },
  "AMGAB0859": {
    "Interaction ID": "AMGAB0859",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-170056",
    "PMID": 28800329.0,
    "Impact of the antibody on amyloid formation": "No effect,",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"Mice treated with the 3D6 antibody did not show a significant change in Thioflavin S positive area compared to control antibody-treated mice (–12%, p = 0.36, t-test; Fig. 3C).\", \"Cortical and hippocampal Aβ-reactive deposits were not impacted by 3D6 treatment (Fig. 6A-D). The finding that 3D6-treated mice show little difference in plaque load versus theisotype control antibody mice is consistent with results shown in Figs. 7 and 8.\", \"Figure 6\", \"Figure 7\", \"Figure 8\", \"Total Aβ42 area was not significantly different between the verubecestat or 3D6 treatment groups and their respective controls (Fig. 8B).\", \"The 3D6 treated group showed no change in total Aβ42 deposits versus isotype control-treated mice (Fig. 8B) and a significant increase in non-vessel associated Aβ42 (+38%; p < 0.05, t-test) and a small decrease in vessel Aβ42 deposits (–7%, p < 0.05, t-test; c.f. Fig. 8C, D). The cause of the small shift in Aβ42 localization is not known but could be related to a change in the availability of the Aβ42 C-terminal epitope to bind antibody. Also, the pathophysiological relevance of the low absolute level of Aβ42 deposition makes it difficult to assign pathophysiological relevance to observations on Aβ42 deposition.\", \"The anti-Aβ antibody, 3D6, which has previously been reported to recognize native plaques and reduce plaque load under similar study conditions as used here did not reduce amyloid burden in this study despite causing the anticipated increase in ARIA-H.\", \"Mice treated with the bapineuzimab analog, 3D6, for 12 weeks showed the expected increase in plasma Aβ levels indicative of target engagement and a significant elevation in ARIA-H as measured by Prussian blue staining or qualitative review of Prussian blue profiles by a board-certified toxicologist. The increase in ARIA-H occurred despite minimal effects of 3D6 on brain Aβ load. This contrasts with published findings showing significant 3D6 mediated clearance of existing plaques [14]. A longer treatment period may have elicited a greater impact of 3D6 on brain Aβ load but nonetheless the 3D6 treated animals demonstrated elevated ARIA-H which supports that this approach was sensitive enough to detect elevation of ARIA-H.\",",
    "Curator Statement": false
  },
  "AMGAB0860": {
    "Interaction ID": "AMGAB0860",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-170056",
    "PMID": 28800329.0,
    "Impact of the antibody on amyloid formation": "Faster aggregation",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry,",
    "Amyloid species identified": "Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The 3D6 treated group showed no change in total Aβ42 deposits versus isotype control-treated mice (Fig. 8B) and a significant increase in non-vessel associated Aβ42 (+38%; p < 0.05, t-test) and a small decrease in vessel Aβ42 deposits (–7%, p < 0.05, t-test; c.f. Fig. 8C, D). The cause of the small shift in Aβ42 localization is not known but could be related to a change in the availability of the Aβ42 C-terminal epitope to bind antibody. Also, the pathophysiological relevance of the low absolute level of Aβ42 deposition makes it difficult to assign pathophysiological relevance to observations on Aβ42 deposition.\", \"Figure 8\",",
    "Curator Statement": "The treatment resulted in a small increase in vessel-associated deposits of Aβ-42."
  },
  "AMGAB0861": {
    "Interaction ID": "AMGAB0861",
    "Antibody ID": "ABID0184",
    "Antibody name": "A8",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.3233/JAD-190874",
    "PMID": 31839610.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" The western blot results showed that the expression levels of Aβ42 oligomers (about 30 kD) but not Aβ40 aggregate (about 10 kD) in the brains of the A8-treated group were lower (p < 0.01) than those of the IgG-treated APP/PS1 mouse group or APP/PS1 control mice (Fig. 2A, B), while there was no significant difference in the level of either form between the APP/PS1 and IgG groups.\", \"Figure 2\", \"The western blot results in the present study showed that Aβ42 but not Aβ40 levels in the brains of APP/PS1 mice decreased (p < 0.05) after eight-week treatment with mAb A8 compared with the levels in the IgG-treated group (Fig. 2A, B). \",",
    "Curator Statement": false
  },
  "AMGAB0862": {
    "Interaction ID": "AMGAB0862",
    "Antibody ID": "ABID0184",
    "Antibody name": "A8",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-190874",
    "PMID": 31839610.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition), Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"To confirm the efficacy of mAb A8 in the double-transgenic APPswe/PS1ΔE9 (APP/PS1) mice, here we reported the related findings. The Morris water maze (MWM) data showed that the A8 treatment group had a shorter escape latency than the control groups in the place navigation test and the probe trial (p < 0.05). Moreover, immunohistochemistry showed decreased levels of both Aβ and p-tau in the brains of APP/PS1 mice. Regarding Aβ levels, western blot results showed that Aβ42 oligomer (p < 0.01) but not Aβ40 levels were diminished in brains of A8-treated APP/PS1 mice.\", \"Aβ42 oligomer and plaque but not Aβ40 levels were diminished in the brains of A8-treated APP/PS1 mice\", \" The western blot results showed that the expression levels of Aβ42 oligomers (about 30 kD) but not Aβ40 aggregate (about 10 kD) in the brains of the A8-treated group were lower (p < 0.01) than those of the IgG-treated APP/PS1 mouse group or APP/PS1 control mice (Fig. 2A, B), while there was no significant difference in the level of either form between the APP/PS1 and IgG groups.\", \"Fig.2 Aβ42 oligomers and Aβ plaques were reduced significantly in the brain of APP/PS1 mice by A8 treatment.\", \"Figure 2\", \" A, B) The decrease in Aβ42 oligomers can be detected by a western blot assay; line 1, APP/PS1 control group; line 2, IgG-treated group; line 3, A8-treated group; line 4, wild-type mice. In the quantitative graph of the western blot data, the ratio of Aβ42 to β-actin was decreased in the A8-treated group (n = 3 mice) compared with the IgG control group or APP/PS1 control mice (n = 3 mice).\", \" D) In the A8 treated group, the Aβ plaques in the hippocampal region (arrow) were decreased than in the control group (scale bar = 100 μm).\", \"The abundance of Aβ plaques in the cortex and hippocampus decreased significantly (One-way analysis of variance and Student’s t-test, n = 3 per group. \", \"However, compared with the IgG group or APP/PS1 control mice (Fig. 2C), the A8-treated group (Fig. 2D) had a significantly decreased number of Aβ plaques in the hippocampal region (p < 0.01, Fig. 2E).\", \"The western blot results in the present study showed that Aβ42 but not Aβ40 levels in the brains of APP/PS1 mice decreased (p < 0.05) after eight-week treatment with mAb A8 compared with the levels in the IgG-treated group (Fig. 2A, B). \",",
    "Curator Statement": false
  },
  "AMGAB0863": {
    "Interaction ID": "AMGAB0863",
    "Antibody ID": "ABID0184",
    "Antibody name": "A8",
    "Amyloid ID": "AGAMYID0022",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-2010-091195",
    "PMID": 21297277.0,
    "Impact of the antibody on amyloid formation": "No effect, Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, TEM image in presence/absence of the antibody,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We used a strain of monoclonal antibody against Aβ42 oligomers, designated A8, as an Aβ inhibitor to suppress Aβ aggregation and Aβ-derived cell toxicity in vitro, and as a passive immunotherapy approach to treat SAMP8 (senescence accelerated mouse sub-line P8) mice, an animal model of AD, in vivo. First, our results showed that pre-incubation of A8 with Aβ oligomers inhibited both the maturation of Aβ fiber and Aβ oligomer toxicity on SH-SY5Y cells.\", \"A8 inhibited Aβ42 fibrillation\", \"After continuous incubation for 5 days at 25◦C,Aβ42 was aggregated into characteristic fibrils with filamentous structure, which were evident under EM. Three arrows were used to point out a single fiberin Fig. 1A. However, this aggregation was prevented when equimolar concentration of Aβ42 was pre-incubated with A8\", \"Instead of the long fiber, there were lots of short rod-shaped, granular or bead-like amorphous structures in the visual field (Fig. 1B). In contrast, the preformed Aβ fiber was not degraded by A8 incubation (data not shown).\", \"Figure 1\", \"Aβ oligomers were diminished in SAMP8 mice brain\",  \"No sig-nificant differences of Aβ oligomer levels in brainsections were found among IgG-treated, buffer-treatedand SAMP8 mouse control groups (P > 0.05) (data notshown). However, compared with these groups, theAβ oligomer levels of brain sections in cortex and hippocampus region were reduced significantly in A8 treated group (P < 0.05) (Fig. 4A–F).\", \"Figure 4\", \"Fig. 4. Aβ oligomer levels reduced significantly in SAMP8 mice brain by A8 treatment.\", \" B) In A8 treated group, the Aβ oligomer levels in cortex (arrow head) and hippocampus region (arrow )were reduced compared with control group; C–F) Photos with higher magnification of the arrowhead or arrow indicated areas from A and B, respectively, were shown here (scale bar = 100 \u0002m).\", \" G, H) The positive staining rates of Aβ oligomer (the ratios of positive staining cell tototal cell) decreased significantly (P < 0.05) both in cortex (G) and hippocampus (H) via A8 treatment.\", \"I, J) The reduction of Aβ oligomer can also be confirmed by Western blot assay (I), line 1, control group; line 2, A8 treated group; line 3, buffer treated group; line 4, IgG treated group. \", \"As expected, we found that A8 candisturb Aβ fibrillation, suppress Aβ oligomer cytotoxicity, and improve learning and memory in SAMP8 mice.\", \"Ultimately, our data shows that A8 can prevent Aβ42 fibrillation as well as neutralizethe toxicity of Aβ42 oligomers, which is partially consistent with previously reported NU antibodies [14].\", \"Therefore,it was the specific recognition of A8 for Aβ oligomers that suppressed Aβ fiber maturation and prevented Aβ oligomer toxicity.\", \"From our results, the improved learning and memory performance was associated with alleviation of pathological assemblies of Aβ, which is partially consistent with previous works [4, 7]. The pathological assemblies of Aβ included soluble oligomers and plaques. Evidence suggested that not only plaque clearance, but pathological oligomer neutralization would influence the efficacy of immunotherapy.\", \"The underlying mechanism of this effect involved the reduced Aβ pathology, including inhibition ofAβ oligomer derived cytotoxicity, and amyloid protein aggregation, and amelioration of phospho-tau pathology.\"",
    "Curator Statement": false
  },
  "AMGAB0864": {
    "Interaction ID": "AMGAB0864",
    "Antibody ID": "ABID0450",
    "Antibody name": "scFv59",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.3233/JAD-2011-110230",
    "PMID": 21709371.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Figure 3\", \"rAAV-CAscFv59 injection tended to reduce Aβ40 loads in the hippocampus (0.18 ± 0.025%) compared to PBS injection (0.23 ± 0.034%) but the difference was not significant.\", \"rAAV5-mediated scFv59 delivery significantly reduced Aβ42 load in the hippocampus but a decrease in Aβ40 load was not significant (Figure 3e–g).\",",
    "Curator Statement": "scFv encoded in adeno-associated virus (rAAV)."
  },
  "AMGAB0865": {
    "Interaction ID": "AMGAB0865",
    "Antibody ID": "ABID0450",
    "Antibody name": "scFv59",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-2011-110230",
    "PMID": 21709371.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Immunoreactive Aβ deposits reduced in the hippocampus.\", \"rAAV5-mediated scFv59 brain delivery reduces Aβ load in the hippocampus in TgAPPswe/PS1dE9 mice\", \"Figure 3\", \"The average Aβ loads in hippocampus were 0.39 ± 0.09, 0.65 ± 0.15 and 0.70 ± 0.06% for mice subjected to rAAV5-CAscFv59, rAAV5-CAscFv-Gag and PBS injection, respectively (Figure 3d). Thus, rAAV5-CAscFv59 injection reduced the Aβ load in the hippocampus by approximately 45% as compared with PBS injection (P = 0.01, n = 8 for each group). In the neocortex, the average amyloid load in rAAV-CAscFv59-injected mice (1.14 ± 0.15%) was less than those in rAAV-CAscFv-Gag-injected (1.32 ± 0.18%) and PBS-injected (1.30 ± 0.15%) mice but the difference was not significant (scFv59 vs. PBS, P = 0.1).\", \"rAAV5-mediated scFv59 expression reduces immunoreactive Aβ deposits in the hippocampus but not in the neocortex.\", \"Because rAAV-CAscFv59 injection reduced the average Aβ load in the hippocampus but not in the neocortex by 6E10 immunoreactivity, we further investigated hippocampal Aβ loads by Aβ40 and Aβ42 C-terminal-specific antibodies.\", \"Because rAAV-CAscFv59 injection reduced the average Aβ load in the hippocampus but not in the neocortex by 6E10 immunoreactivity, we further investigated hippocampal Aβ loads by Aβ40 and Aβ42 C-terminal-specific antibodies. rAAV-CAscFv59 injection also reduced the average Aβ42 load in the hippocampus (0.20 ± 0.028% for rAAV-CAscFv59 and 0.30 ± 0.034% for PBS, P < 0.05) (Figure 3e–g).\", \"rAAV5-mediated scFv59 delivery significantly reduced Aβ42 load in the hippocampus but a decrease in Aβ40 load was not significant (Figure 3e–g).\",",
    "Curator Statement": "scFv encoded in adeno-associated virus (rAAV)."
  },
  "AMGAB0866": {
    "Interaction ID": "AMGAB0866",
    "Antibody ID": "ABID0451",
    "Antibody name": "scFv-Gag",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.3233/JAD-2011-110230",
    "PMID": 21709371.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": false,
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 3\",",
    "Curator Statement": "scFv encoded in adeno-associated virus (rAAV)."
  },
  "AMGAB0867": {
    "Interaction ID": "AMGAB0867",
    "Antibody ID": "ABID0451",
    "Antibody name": "scFv-Gag",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-2011-110230",
    "PMID": 21709371.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": false,
    "Experimental method(s)": "Immunohistochemistry,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative control",
    "Quote of the interaction": "\"Figure 3\", \"The average Aβ loads in hippocampus were 0.39 ± 0.09, 0.65 ± 0.15 and 0.70 ± 0.06% for mice subjected to rAAV5-CAscFv59, rAAV5-CAscFv-Gag and PBS injection, respectively (Figure 3d). Thus, rAAV5-CAscFv59 injection reduced the Aβ load in the hippocampus by approximately 45% as compared with PBS injection (P = 0.01, n = 8 for each group). In the neocortex, the average amyloid load in rAAV-CAscFv59-injected mice (1.14 ± 0.15%) was less than those in rAAV-CAscFv-Gag-injected (1.32 ± 0.18%) and PBS-injected (1.30 ± 0.15%) mice but the difference was not significant (scFv59 vs. PBS, P = 0.1).\", \"Our studies indicate that rAAV5-mediated therapeutic delivery of anti-Aβ scFv reduced Aβ load in the hippocampus but was associated with a lower Aβ40:42 ratio in CSF, a focal increase in blood vessel Aβ deposits, and cerebral hemorrhages. \",",
    "Curator Statement": "scFv encoded in adeno-associated virus (rAAV)."
  },
  "AMGAB0868": {
    "Interaction ID": "AMGAB0868",
    "Antibody ID": "ABID0002",
    "Antibody name": "Gantenerumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-2011-110977",
    "PMID": 21955818.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo, in cellulo",
    "Experimental method(s)": "Immunohistochemistry, confocal microscopy, ELISA",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Gantenerumab: A Novel Human Anti-Aβ Antibody Demonstrates Sustained Cerebral Amyloid-Binding and Elicits Cell-Mediated Removal of Human Amyloid-β\", \". In functional assays gantenerumab induced cellular phagocytosis of human amyloid-β deposits in AD brain slices when co-cultured with primary human macrophages and neutralized oligomeric Aβ 42-mediated inhibitory effects on long-term potentiation in rat brain. In APP751swedishxPS2N141I transgenic mice, gantenerumab showed sustained binding to cerebral amyloid-β and, upon chronic treatment, significantly reduced small amyloid-β plaques by recruiting microglia and prevented new plaque formation. Unlike other A antibodies, gantenerumab did not alter plasma Aβ suggesting undisturbed systemic clearance of soluble Aβ. These studies demonstrated that gantenerumab preferentially interacts with aggregated Aβ in the brain and lowers amyloid by eliciting effector cell-mediated clearance\", \"The amyloid lowering capacity was confirmed in an ex vivo phagocytosis assay using human effector cells and in vivo in PS2APP double transgenic mice.\", \"Gantenerumab elicits clearance of human Aβ plaques ex vivo\", \" Aconcentration-dependent decrease of Aβ plaque load was seen (Fig. 3a–c). Notably, gantenerumab preincubated at 0.07 nM(10ng/mL)was the minimal effective concentration (p≤0.05) able to lower Aβ amyloid in this assay (Fig. 3b and e) with amyloid removal highly significant (p≤0.01 to p≤0.001) and almost complete after preincubation with gantenerumab at ≥7nM (Fig. 3c and e)\", \"Figure 3\", \"Another control experiment with unspecific human IgG1 in the presence of macrophages showed unchanged Aβ load confirming that induction of phagocytic activity required gantenerumab (Fig. 3e)\", \"Sustained binding of gantenerumab to Aβ plaques in vivo leads to reduction of small Aβ plaques\", \" Brain section without gantenerumab shows the distribution of numerous amyloid-β plaques in the grey matter of the frontal cortical lobe after culturing with human macrophages (a) and a concentration-dependent decrease of amyloid-β plaques when gantenerumab was added (b and c). Plaques were slightly reduced after preincubation with gantenerumab at 0.07nM (10ng/mL) (b) and substantially at 7nM (1,000ng/mL) (c). Control section preincubated with gantenerumab 35nM (5,000ng/mL) in the absence of cells indicated ability of BAP2 to label amyloid-β plaques (d). Quantitative analysis of the experiment shown in (a–c) revealed a significant concentration dependent reduction of amyloid-β plaques, while control with unrelated human IgG1 antibody is inactive (e). Determination of EC50 showed a consistent plaque clearance by macrophages from two different human donors in additional independent experiments (f).\", \" A significant reduction of Aβ amyloid plaques was evident in gantenerumab-treated PS2APP mice compared with vehicle controls (Fig. 5a and b). A detailed morphometric analysis revealed a significant (p≤0.001) reduction of Aβ plaque numbers in hippocampus (36%), neocortex (40%), and thalamus (70%),respectively(Fig.5c–e).Notably, the activity of gantenerumab correlated with plaque dimensions. The number of smaller, less than 400 m2,Aβ plaques was most efficiently reduced when compared with vehicle treated animals (Fig. 5f). This reduction reflected not only a significant (p≤0.001) prevention of de novo plaque formation as revealed by comparison to the vehicle treated group, but also a significant (p≤0.05 to p≤0.01) clearance of pre-existing small plaques up to a size range of ≤300 m2 when compared to the baseline group of PS2APP mice.\", \"Figure 5\", \"By measuring the surface fraction of stained plaques, a significant decrease (p≤0.001) was seen in thalamus and a trend in cortex (p=0.07) andhippocampus(p=0.23) compared to vehicle treated animals (data not shown).\", \" Reduction of A plaques was seen after treatment with gantenerumab (a) compared with vehicle (b).\", \"A significant reduction in plaque number is evident after treatment with gantenerumab (n=12), compared to the progressive plaque formation seen in vehicle treated animals (n=14). A significant clearance activity of gantenerumab was seen specifically for smaller amyloid deposits up to a size of 400 m2 as shown for the hippocampal region (f).\", \"Gantenerumab neutralizes Aβ42 oligomers in vivo\", \" However, gantenerumab clearly elicited clearance of small-sized Aβ plaques and inhibited formation of new plaques after chronic treatment of PS2APP mice.\", \"In summary, our findings provide evidence that the specificity and avidity of gantenerumab facilitates sustained binding to cerebral Aβ in vivo leading to reduction of the amyloid plaque burden by triggering effector cell-mediated clearance mechanisms.\",",
    "Curator Statement": "While the effect is visible on small plaques, there's no effect of ganterumab on large plaques."
  },
  "AMGAB0869": {
    "Interaction ID": "AMGAB0869",
    "Antibody ID": "ABID0002",
    "Antibody name": "Gantenerumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3233/JAD-2011-110977",
    "PMID": 21955818.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Confocal microscopy",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The build-up of larger plaques with surfaces of ≥400 m2 was similar for both the vehicle- and gantenerumab-treated groups after the 5 month treatment period (Fig. 5f) suggesting that larger plaques were more resistant to clearance in the PS2APP mouse model used in our study.\", \"Figure 5\", \" It is interesting to note that despite this significant “decoration” of A plaques by gantenerumab large plaques (>400 m2) were relatively resistant to clearance as evident from the 5-months treatment study.\"",
    "Curator Statement": "While the effect is visible on small plaques, there's no effect of ganterumab on large plaques."
  },
  "AMGAB0870": {
    "Interaction ID": "AMGAB0870",
    "Antibody ID": "ABID0012.5.2",
    "Antibody name": "SAR255952",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3389/fnagi.2016.00055",
    "PMID": 27047372.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition), No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, MRI",
    "Amyloid species identified": "Protofibrils, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"SAR255952 reduced amyloid load in 8.5-months-old animals, but not in 5.5-months animals compared to mice treated with a control antibody (DM4).\", \"Histological evaluation confirmed the reduction of amyloid load and revealed a lower density of amyloid plaques in 8.5-months SAR255952-treated animals\", \"The longitudinal follow-up of individual amyloid plaques by MRI revealed that plaques that were visible at 5.5 months were still visible at 8.5 months in both SAR255952 and DM4-treated mice. This suggests that the amyloid load reduction induced by SAR255952 is related to a slowing down in the formation of new plaques rather than to the clearance of already formed plaques.\", \"(E) Measures from MR sections revealed an increased amyloid load between 5.5 and 8.5 months in SAR255952 and DM4-treated animals (repeated measure ANOVA and post hoc analysis within each group F[1,11] = 23 and 29, respectively, ∗∗∗p < 0.001). At 8.5 months, the amyloid load was lower in SAR255952-treated animals (n = 9) compared to control DM4-treated mice (n = 4; repeated measure ANOVA and post hoc analysis F[1,11] = 7, ∗p = 0.02). Histological measures confirmed the lower amyloid load [F, Student’s t-test, t(10) = 2.3, ∗p = 0.04] and reduced density of amyloid plaques [G, t(10) = 2.7, ∗p = 0.02] in SAR255952-treated animals at 8.5 months. The average size of the amyloid plaques was not modulated by therapy [H, t(10) = 0.6, ns]. \", \"Figure 1\", \"In both DM4 (A,B) and SAR255952-treated (C,D) APP/PS1 mice the plaques detected at 5.5 months were still visible at 8.5 months (yellow arrows).\", \"Figure 2\", \"The visual observation of these images revealed an age-related increased in amyloid load in both DM4 (Figures 2A,B) and SAR255952-treated animals (Figures 2C,D).\", \"Quantitative studies of MRI sections revealed a similar amyloid load in the 5.5-months-old animals treated with DM4 or SAR255952 antibodies (n.s., Figure 1E). Amyloid load increased in both DM4 and SAR255952-treated animals between the ages of 5.5–8.5 months (from 3.4 ± 0.6% to 7.5 ± 0.2% and from 3.3 ± 0.3% to 5.7 ± 0.4% in DM4 and SAR255952-treated mice, respectively, p < 0.001, Figure 1E). At 8.5 months, the amyloid load detected by MRI was 24% lower in the SAR255952-treated mice compared to the DM4-treated mice (p = 0.02, Figure 1E).\", \"Histological evaluations confirmed the lower amyloid load in 8.5-months-old APP/PS1 animals treated with SAR255952 compared to animals treated with the control antibody (15.8 ± 2.0% versus 10.6 ± 1.1%, respectively, p = 0.04, Figure 1F). In addition, histological quantifications revealed that the number of amyloid plaques (plaque density) was reduced by 33% in the SAR255952-treated animals compared to the DM4-treated animals (p = 0.02, Figure 1G), whereas the size of the plaques was not significantly different in the two groups (Figure 1H).\", \"There was also a strong positive correlation between the IgG load and the amyloid load (r = 0.90, p = 0.002, Figure 3D) or amyloid density (r = 0.85, p = 0.007, Figure 3E) detected by histology.\", \"Figure 3\",",
    "Curator Statement": false
  },
  "AMGAB0871": {
    "Interaction ID": "AMGAB0871",
    "Antibody ID": "ABID0381",
    "Antibody name": "DM4",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3389/fnagi.2016.00055",
    "PMID": 27047372.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry, MRI",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "Negative Control",
    "Quote of the interaction": "\"SAR255952 reduced amyloid load in 8.5-months-old animals, but not in 5.5-months animals compared to mice treated with a control antibody (DM4).\", \"The longitudinal follow-up of individual amyloid plaques by MRI revealed that plaques that were visible at 5.5 months were still visible at 8.5 months in both SAR255952 and DM4-treated mice. \", \"(E) Measures from MR sections revealed an increased amyloid load between 5.5 and 8.5 months in SAR255952 and DM4-treated animals (repeated measure ANOVA and post hoc analysis within each group F[1,11] = 23 and 29, respectively, ∗∗∗p < 0.001). At 8.5 months, the amyloid load was lower in SAR255952-treated animals (n = 9) compared to control DM4-treated mice (n = 4; repeated measure ANOVA and post hoc analysis F[1,11] = 7, ∗p = 0.02). Histological measures confirmed the lower amyloid load [F, Student’s t-test, t(10) = 2.3, ∗p = 0.04] and reduced density of amyloid plaques [G, t(10) = 2.7, ∗p = 0.02] in SAR255952-treated animals at 8.5 months. The average size of the amyloid plaques was not modulated by therapy [H, t(10) = 0.6, ns]. \", \"Figure 1\", \"In both DM4 (A,B) and SAR255952-treated (C,D) APP/PS1 mice the plaques detected at 5.5 months were still visible at 8.5 months (yellow arrows).\", \"Figure 2\", \"The visual observation of these images revealed an age-related increased in amyloid load in both DM4 (Figures 2A,B) and SAR255952-treated animals (Figures 2C,D).\", \"Quantitative studies of MRI sections revealed a similar amyloid load in the 5.5-months-old animals treated with DM4 or SAR255952 antibodies (n.s., Figure 1E). Amyloid load increased in both DM4 and SAR255952-treated animals between the ages of 5.5–8.5 months (from 3.4 ± 0.6% to 7.5 ± 0.2% and from 3.3 ± 0.3% to 5.7 ± 0.4% in DM4 and SAR255952-treated mice, respectively, p < 0.001, Figure 1E). At 8.5 months, the amyloid load detected by MRI was 24% lower in the SAR255952-treated mice compared to the DM4-treated mice (p = 0.02, Figure 1E).\", \"Histological evaluations confirmed the lower amyloid load in 8.5-months-old APP/PS1 animals treated with SAR255952 compared to animals treated with the control antibody (15.8 ± 2.0% versus 10.6 ± 1.1%, respectively, p = 0.04, Figure 1F). In addition, histological quantifications revealed that the number of amyloid plaques (plaque density) was reduced by 33% in the SAR255952-treated animals compared to the DM4-treated animals (p = 0.02, Figure 1G), whereas the size of the plaques was not significantly different in the two groups (Figure 1H).\", \"Figure 3\", \"We also found a positive relationship between the amyloid and IgG loads in the SAR255952-treated APP/PS1 mice which is consistent with the targeting of fibrillar amyloid forms of Aβ by SAR255952. By using Gd-stained MRI, we were able to demonstrate the efficacy of this anti-Aβ antibody to slow down the evolution of amyloid load. We could also monitor individual plaques during two imaging sessions separated by 3 months and showed that, even in the SAR255952-treated animals, plaques that were present at the first time point were still detected 3 months later. This suggests that the targeting of fibrillar forms of Aβ by SAR255952 does not lead to the clearance of the plaques. The lower amyloid load in the SAR255952-treated animals was thus due to a decrease in the formation of new plaques, probably related to the targeting of protofibrillar forms of Aβ.\", \"On the basis of our histological study, we also reported that the lower amyloid load in the SAR255952-treated animals was linked to a reduction of amyloid plaque density and not to a diminution of the size of the plaques.\",",
    "Curator Statement": false
  },
  "AMGAB0872": {
    "Interaction ID": "AMGAB0872",
    "Antibody ID": "ABID0007.1",
    "Antibody name": "scFv-h3D6",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.3390/biom15111602",
    "PMID": 41301520.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Apart from being effective in reducing Aβ to the same extent as the complete antibody, scFv-h3D6 prevented induced hemorrhagic events.\", \"Concerning treatments, mAb-m3D6 and scFv-h3D6 reduced Aβ40 levels in TBS-soluble (U = 0, p = 0.0022, r = 1 and U = 2; p = 0.0087, r = 0.88, respectively) and FA-soluble (U = 3, p = 0.0152, r = 0.83 and U = 0, p = 0.0022, r = 1, respectively) fractions in the hippocampus (Figure 5A–C). However, treatments were not effective against Aβ42.\", \"Figure 5\", \"Both mAb-m3D6 and scFv-h3D6 reduced Aβ levels by the same extent.\", \"Both mAb-m3D6 and scFv-h3D6 Reduce Aβ Levels\", \"Although both treatments reduced Aβ levels, the difficulty of crossing the BBB and the advanced stage of AD in the aged APP23 mice supports the accepted idea of Aβ-immunotherapy being more effective at the early stages of the disease.\", \"Aβ40 reduction in this work was not enough to restore neurodegeneration featuring in very-late stages of the disease\",",
    "Curator Statement": false
  },
  "AMGAB0873": {
    "Interaction ID": "AMGAB0873",
    "Antibody ID": "ABID0007.1",
    "Antibody name": "scFv-h3D6",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.3390/biom15111602",
    "PMID": 41301520.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"As already observed in 22-month-old 3xTg-AD mice [22], no differences in either Aβ40 or Aβ42 levels among the non-treated, mAb-m3D6-treated and scFv-h3D6-treated APP23 mice were found in the cortex (Figure 5G–F).\", \"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0874": {
    "Interaction ID": "AMGAB0874",
    "Antibody ID": "ABID0007.1",
    "Antibody name": "scFv-h3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3390/biom15111602",
    "PMID": 41301520.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Apart from being effective in reducing Aβ to the same extent as the complete antibody, scFv-h3D6 prevented induced hemorrhagic events.\", \"Concerning treatments, mAb-m3D6 and scFv-h3D6 reduced Aβ40 levels in TBS-soluble (U = 0, p = 0.0022, r = 1 and U = 2; p = 0.0087, r = 0.88, respectively) and FA-soluble (U = 3, p = 0.0152, r = 0.83 and U = 0, p = 0.0022, r = 1, respectively) fractions in the hippocampus (Figure 5A–C). However, treatments were not effective against Aβ42.\", \"Figure 5\", \"As already observed in 22-month-old 3xTg-AD mice [22], no differences in either Aβ40 or Aβ42 levels among the non-treated, mAb-m3D6-treated and scFv-h3D6-treated APP23 mice were found in the cortex (Figure 5G–F).\",",
    "Curator Statement": false
  },
  "AMGAB0875": {
    "Interaction ID": "AMGAB0875",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.3390/biom15111602",
    "PMID": 41301520.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Concerning treatments, mAb-m3D6 and scFv-h3D6 reduced Aβ40 levels in TBS-soluble (U = 0, p = 0.0022, r = 1 and U = 2; p = 0.0087, r = 0.88, respectively) and FA-soluble (U = 3, p = 0.0152, r = 0.83 and U = 0, p = 0.0022, r = 1, respectively) fractions in the hippocampus (Figure 5A–C). However, treatments were not effective against Aβ42.\", \"Figure 5\", \"Both mAb-m3D6 and scFv-h3D6 reduced Aβ levels by the same extent.\", \"Both mAb-m3D6 and scFv-h3D6 Reduce Aβ Levels\", \"Although both treatments reduced Aβ levels, the difficulty of crossing the BBB and the advanced stage of AD in the aged APP23 mice supports the accepted idea of Aβ-immunotherapy being more effective at the early stages of the disease.\", \"Aβ40 reduction in this work was not enough to restore neurodegeneration featuring in very-late stages of the disease\",",
    "Curator Statement": false
  },
  "AMGAB0876": {
    "Interaction ID": "AMGAB0876",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.3390/biom15111602",
    "PMID": 41301520.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"As already observed in 22-month-old 3xTg-AD mice [22], no differences in either Aβ40 or Aβ42 levels among the non-treated, mAb-m3D6-treated and scFv-h3D6-treated APP23 mice were found in the cortex (Figure 5G–F).\", \"Figure 5\",",
    "Curator Statement": false
  },
  "AMGAB0877": {
    "Interaction ID": "AMGAB0877",
    "Antibody ID": "ABID0007.5",
    "Antibody name": "3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3390/biom15111602",
    "PMID": 41301520.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "ELISA",
    "Amyloid species identified": "Not specified",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Concerning treatments, mAb-m3D6 and scFv-h3D6 reduced Aβ40 levels in TBS-soluble (U = 0, p = 0.0022, r = 1 and U = 2; p = 0.0087, r = 0.88, respectively) and FA-soluble (U = 3, p = 0.0152, r = 0.83 and U = 0, p = 0.0022, r = 1, respectively) fractions in the hippocampus (Figure 5A–C). However, treatments were not effective against Aβ42.\",\"Figure 5\", \"As already observed in 22-month-old 3xTg-AD mice [22], no differences in either Aβ40 or Aβ42 levels among the non-treated, mAb-m3D6-treated and scFv-h3D6-treated APP23 mice were found in the cortex (Figure 5G–F).\",",
    "Curator Statement": false
  },
  "AMGAB0878": {
    "Interaction ID": "AMGAB0878",
    "Antibody ID": "ABID0149",
    "Antibody name": "DesAb18-24",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.3390/ijms21124542",
    "PMID": 32630615.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"2.1. The DesAbs Inhibit Aβ40 Aggregation\", \"We observed that DesAb18-24 strongly inhibits Aβ40 aggregation, causing a significant delay in the half-time of aggregation (t1/2) (Figure 1a), which is in agreement with previous findings for Aβ42 [18]. Indeed, at the highest concentration of DesAb18-24 (2 µM), Aβ40 did not aggregate beyond t1/2 in this experiment on the time course of 25 h. \", \"Figure 1\", \"Interestingly, both DesAbs inhibited the aggregation kinetics in a concentration-dependent manner, as illustrated by the relative changes in t1/2 (Figure 1c). Experiments were carried out in triplicate, and indicated that both designed antibodies can significantly delay Aβ40 aggregation.\", \"DesAb18-24 and DesAb34-40 inhibit Aβ40 aggregation.\", \"(c) Relative change in half-time (t1/2) calculated from dividing t1/2 for each experimental condition by the average t1/2 determined for Aβ40 in the absence of DesAbs to show the relative delay in aggregation induced by the antibodies.\",",
    "Curator Statement": false
  },
  "AMGAB0879": {
    "Interaction ID": "AMGAB0879",
    "Antibody ID": "ABID0150",
    "Antibody name": "DesAb34-40",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "10.3390/ijms21124542",
    "PMID": 32630615.0,
    "Impact of the antibody on amyloid formation": "Slower aggregation (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics,",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"2.1. The DesAbs Inhibit Aβ40 Aggregation\", \"Further experiments on DesAb34-40 revealed that this designed antibody was also able to interfere with the reaction, as observed by an overall delay in the aggregation kinetics (Figure 1b).\", \"Figure 1\", \"Interestingly, both DesAbs inhibited the aggregation kinetics in a concentration-dependent manner, as illustrated by the relative changes in t1/2 (Figure 1c). Experiments were carried out in triplicate, and indicated that both designed antibodies can significantly delay Aβ40 aggregation.\", \"DesAb18-24 and DesAb34-40 inhibit Aβ40 aggregation. \", \"(c) Relative change in half-time (t1/2) calculated from dividing t1/2 for each experimental condition by the average t1/2 determined for Aβ40 in the absence of DesAbs to show the relative delay in aggregation induced by the antibodies. \",",
    "Curator Statement": false
  },
  "AMGAB0881": {
    "Interaction ID": "AMGAB0881",
    "Antibody ID": "ABID0004.1",
    "Antibody name": "Crenezumab-like scFv (scFv-C)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3390/ijms24098371",
    "PMID": 37176076.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics, Other: Molecuar Dynamics Simulations",
    "Amyloid species identified": "Protein monomer, Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "CDR-L1 (SSQSLVYSN), CDR-L2 (QLLIYVS), CDR-L3 (THVP), CDR-H1 (GFTFSSYGMSWV), CDR-H2 (GGST), CDR-H3 (YCASGDYW).",
    "Quote of the interaction": "\"As the results indicated that scFv-C could recognize Aβ42 monomer/oligomer and promote the disaggregation of Aβ42 fiber as determined by the Thioflavin-T assay, the potential mechanism of its interaction with Aβ42 was investigated using molecular dynamics analysis. Interactions involving hydrogen bonds and salt bonds were predicted between scFv-C and Aβ42 pentamer, suggesting the possibility of inhibiting further aggregation of Aβ42.\", \"ScFvs can depolymerize aggregated Aβ42. After incubation for 23 h, the percentage of fluorescence intensity of the mixture treated with scFvs decreased. The results indicated that the amount of aggregated Aβ42 treated with scFv-C, scFv-S, and scFv-S dropped to 39%, 45%, and 42%, respectively (Figure 4), while the fluorescence intensity of aggregated Aβ42 dropped to 91%. The above results suggested that scFvs could depolymerize aggregated Aβ42.\", \"Figure 4\", \", \"Depolymerization of aggregated Aβ42 by scFvs.\", \"The RMSD of the Ala21 to Gly29 region of five Aβ monomers, bound and unbound to scFv-C, were obtained and compared. The results showed that the RMSD value of the Ala21 to Gly29 region of mono1, mono3, and mono4 of Aβ5 was significantly increased by antibody binding, indicating that scFv-C may have the potential to disrupt the structure of Aβ5 (Figure 8).\", \"Figure 8\", \"After comparing mono1 to mono5 between the bound and unbound systems, the conclusion is that the binding of scFv-C tends to deaggregate Aβ42 fiber.\", \"Figure 9\",  \" The RMSD values of the Ala21 to Gly29 region of mono1, mono3, and mono4 of Aβ5 were significantly increased by antibody binding, indicating that scFv-C may have the potential to disrupt the structure of Aβ5. In addition, it can be observed in Figure 4 that after incubation for 23 h, the fluorescence intensity of the Aβ fiber mixture treated with scFv-C decreases to 39%, which can also imply the deaggregation effect of scFv-C on the formed Aβ42 fiber.\", \"ScFv-C can bind to monomers, oligomers, and fibrous Aβ42. After binding, there is a tendency for it to depolymerize aggregated Aβ42. In addition, ScFv-C forms hydrogen bonds and salt bonds to prevent Aβ42 from further aggregation.\"",
    "Curator Statement": false
  },
  "AMGAB0882": {
    "Interaction ID": "AMGAB0882",
    "Antibody ID": "ABID0005.1",
    "Antibody name": "Solanezumab-like scFv (scFv-S)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3390/ijms24098371",
    "PMID": 37176076.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"ScFvs can depolymerize aggregated Aβ42. After incubation for 23 h, the percentage of fluorescence intensity of the mixture treated with scFvs decreased. The results indicated that the amount of aggregated Aβ42 treated with scFv-C, scFv-S, and scFv-S dropped to 39%, 45%, and 42%, respectively (Figure 4), while the fluorescence intensity of aggregated Aβ42 dropped to 91%. The above results suggested that scFvs could depolymerize aggregated Aβ42.\", \"Figure 4\", \", \"Depolymerization of aggregated Aβ42 by scFvs.\"",
    "Curator Statement": false
  },
  "AMGAB0883": {
    "Interaction ID": "AMGAB0883",
    "Antibody ID": "ABID0270",
    "Antibody name": "12B4-like scFv (scFv-12B4)",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3390/ijms24098371",
    "PMID": 37176076.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vitro",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Protein monomer",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"ScFvs can depolymerize aggregated Aβ42. After incubation for 23 h, the percentage of fluorescence intensity of the mixture treated with scFvs decreased. The results indicated that the amount of aggregated Aβ42 treated with scFv-C, scFv-S, and scFv-S dropped to 39%, 45%, and 42%, respectively (Figure 4), while the fluorescence intensity of aggregated Aβ42 dropped to 91%. The above results suggested that scFvs could depolymerize aggregated Aβ42.\", \"Figure 4\", \", \"Depolymerization of aggregated Aβ42 by scFvs.\"",
    "Curator Statement": false
  },
  "AMGAB0884": {
    "Interaction ID": "AMGAB0884",
    "Antibody ID": "ABID0470",
    "Antibody name": "m81",
    "Amyloid ID": "AGAMYID0012",
    "Amyloid name": "IAPP",
    "DOI": "10.3390/vaccines9111316",
    "PMID": 34835247.0,
    "Impact of the antibody on amyloid formation": "No aggregation (complete inhibition)",
    "Experimental Model(s)": "In vitro, in vivo",
    "Experimental method(s)": "ThT - Aggregation kinetics",
    "Amyloid species identified": "Oligomers, Mature fibrils",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The here described monoclonal antibody (mAb) m81, specific for oligomeric and fibrils, but not for soluble free IAPP, is able to prevent oligomer growth and aggregate formation in vitro, and blocks islet inflammation and disease progression in vivo.\", \"Moreover, during in vitro fibril formation experiments, the mAb was able to prevent aggregation and block progression of aggregate formation when added during oligomerization. In addition, when injected in a transgenic mouse model mimicking T2DM in humans, the mAb was able to reduce hyperglycemia, fibril formation in the islets, and decreased inflammation, while insulin-production remained largely normal.\", \"m81 mAb Prevents Fibril Formation and Stops the Aggregation Progress When Added at an Oligomeric State\", \"When m81 mAb was added to soluble hIAPP before aggregation (Figure 3, hIAPP + M81(t = 0)), followed by incubation at 37 °C, hIAPP did not aggregate, in contrast to the control hIAPP (Figure 3, hIAPP). Interestingly, when m81 mAb was added after the synthetic fibrils had already reached an oligomeric state (at ca. 100 min, Figure 2, hIAPP + M81(t = 100)), the mAb stopped aggregate formation, and prevented further assembly into larger fibrils; under these conditions, Thioflavin T signal remained constant, indicating that previously formed aggregates cannot be reversed into the state of monomeric hIAPP. Thus, m81 mAb, by binding to oligomers, can prevent in vitro amyloid aggregate formation and block the progression of oligomers into larger fibrils, but cannot reverse oligomerization.\", \"Figure 3\", \"m81 mAb can prevent fibrils formation in vitro and block aggregation process up to an oligomeric stage.\", \"m81 mAb Is Able to Prevent Hyperglycemia, Fibril Formation in Pancreatic Islets, Decrease Inflammation and Maintain Insulin-Production in a Mouse Model of T2DM in Human\", \"Figure 4\",  \" Pancreatic slides of mice treated with m81 mAb showed significantly decreased levels of amyloidogenic aggregates detected with Thioflavin S (Figure 4H–J), along with higher insulin (Figure 4H–J) and lower IL-1β levels (Figure 4H,I,K).\", \"This indicates that treatment with m81 mAb can reduce endogenous hIAPP aggregates in vivo, and ameliorate symptoms of T2DM.\", \"m81 mAb prevents hyperglycemia increase and human IAPP aggregate formation in pancreatic islets, and decreases IL-1β level.\", \"urthermore, this mAb was able to block IAPP aggregate formation in vitro, and reduce aggregate loads in vivo in a murine model of T2DM.\", \"We demonstrate here that m81 mAb is able to block IAPP oligomerization and fibril formation in vitro.\", \"This antibody is shown to prevent IAPP aggregation in vitro and aggregate deposition in vivo, delaying the onset of T2DM.\",",
    "Curator Statement": false
  },
  "AMGAB0885": {
    "Interaction ID": "AMGAB0885",
    "Antibody ID": "ABID0131",
    "Antibody name": "6E10",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.3791/54215",
    "PMID": 27585306.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Immunohistochemistry",
    "Amyloid species identified": "Oligomers",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"We found that the level Aβo was substantially decreased by 6E10 antibody treatment (Figure 1B). Marked neurodegeneration was observed near the injecting site of Aβo, and was attenuated by 6E10 antibody treatment (Figure 1B). These results are consistent with Aβo accumulation that we observed in the DG following repeated Aβo infusions in mice.28 Clearance of amyloid deposition by immunotherapy with 6E10 antibody shown here is in line with another report done in a transgenic AD mouse model.31\", \"Figure 2\", \"Video\",",
    "Curator Statement": false
  },
  "AMGAB0886": {
    "Interaction ID": "AMGAB0886",
    "Antibody ID": "ABID0434",
    "Antibody name": "10D5",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.4161/intv.25693",
    "PMID": 28944103.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Longitudinal multiphoton fluorescence microscopy",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" While microglia were observed to surround senile plaques, topical anti-Aβ antibody administration, which led to a reduction in plaque size, directed microglia toward senile plaques, and the overall size of microglia and number of processes were increased.\", \"We observed a significant reduction of plaque size that reached ~40% of the original size by day 7 after 10D5 application, as previously described under similar conditions.\", \"Individual, identified plaques were monitored with longitudinal multiphoton imaging immediately after the surgery (day 1) as well as on days 2, 3, 4 and 7. Anti-Aβ antibody treatment showed a tendency to reduce senile plaque size as soon as 24 h after the application of the treatment. This effect reached statistical significance 3 d after the application of 10D5 and was still present on day 7, reaching ~40% reduction when compared with day 1, as previously described (Fig. 1).6,8 We detected a significant treatment×day effect using two-way ANOVA [F(4,650) = 2.724; *p = 0.029] when 10D5 treated and untreated mice were compared. Further analysis showed a significant reduction of senile plaque size using two-way ANOVA for repeated samples followed by Tamhane test [F(15,491) = 3.906; *p < 0.001, vs. day 1]. No significant differences were observed in untreated mice along the imaging sessions (two-way ANOVA treatment×day effect: [F(7,137) = 0.593; p = 867]) as previously described,19,26,27 supporting the fact that senile plaques do not change in size at these time intervals once deposited (Fig. 1).\", \"Figure 1\", \"We detected a significant treatmentXday effect using two-way ANOVA [F(4,650) = 2.724; *p = 0.029] when 10D5 and control treated mice were compared. We further observed a significant animalXtreatment effect in 10D5 treated mice using two-way ANOVA for repeated samples followed by Tamhane test [F(15,491) = 3.906; *p < 0.001, vs. day 1]\",",
    "Curator Statement": false
  },
  "AMGAB0887": {
    "Interaction ID": "AMGAB0887",
    "Antibody ID": "ABID0434",
    "Antibody name": "10D5",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.4161/intv.25693",
    "PMID": 28944103.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "In vivo Multiphoton Fluorescence Microscopy",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\" Acute studies (1 h before treatment and up to 2 h after antibody application) revealed no significant effect of cranial window implantation or antibody treatment on senile plaque size, microglia burden, microglia size and number of processes either in the close proximity or far from senile plaques (Table S1). Along with this no appreciable early changes were observed in microglia process extension and retraction (Fig. S1).\", \" No significant effects were detected on senile plaque size, expressed as percentage of plaque size in session 1 (120 min) using two-way ANOVA without replication [F(9,55)=0.371; P=0.944] (4-16 senile plaques).\",",
    "Curator Statement": "Acute, \"immediate\", studies did not appreciate effect of the immunotherapy."
  },
  "AMGAB0888": {
    "Interaction ID": "AMGAB0888",
    "Antibody ID": "ABID0007.1",
    "Antibody name": "ScFv-h3D6",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "10.4161/mabs.25424",
    "PMID": 23884018.0,
    "Impact of the antibody on amyloid formation": "Diminished amyloid quantity at the final point (partial inhibition)",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other: Immunoblot",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Brain tissues of these animals revealed a global decrease of Aβ oligomers in the cortex and olfactory bulb after treatment, but this was not seen in the hippocampus and cerebellum.\",  \"Figure 5\", \"Figure 5. Immunoblotting analysis of the soluble Aβ-amyloid oligomers from extracellular extracts of 5 mo-old NTg and 3xTg-AD mice. (A) Extracellular extracts from several brain subregions (HC, hippocampus; CX, cortex; OB, olfactory bulb and CR, cerebellum), from non-transgenic (NTg) and triple transgenic (3xTg-AD) mice i.p. treated with 85 μg of scFv-h3D6 (+) and i.p. treated with PBS (-), were analyzed. Profiles for NTg mice did not change upon scFv-h3D6 treatment. The profiles for 3xTg-AD mice of extracellular soluble Aβ oligomers in CX and OB showed a clear decrease of the dodecameric, nonameric, hexameric and trimeric Aβ-species upon treatment (squared), while in HC and CR remained the same.\", \"In contrast, the treatment changed the aggregation profile of the Aβ-peptide in the cortex and in the olfactory bulb. Both cortex and olfactory bulb showed a dramatic decrease in dodecamers, nonamers and hexamers levels (Fig. 5). It was also likely that the trimer detected in the untreated cortex disappeared upon scFv-h3D6 treatment.\", \"ScFv-h3D6 treatment eliminated Aβ-oligomers\", \"To compare the aggregation extent of the Aβ peptide in different brain areas of treated and non-treated animals, protein extracts from hippocampus, cortex, olfactory bulb and cerebellum were analyzed by western-blot analysis with the 6E10 antibody. Twelve, nine and six-mer oligomers of the Aβ peptide were globally decreased in cortex and olfactory bulb upon treatment, but this effect was observed neither in the hippocampus nor in the cerebellum.\", \"Therefore, scFv-h3D6 is effective in eliminating the most toxic species of Aβ-oligomers and constitutes a promising therapy.\"",
    "Curator Statement": false
  },
  "AMGAB0889": {
    "Interaction ID": "AMGAB0889",
    "Antibody ID": "ABID0005",
    "Antibody name": "Solanezumab",
    "Amyloid ID": "AGAMYID0002",
    "Amyloid name": "Aβ-40",
    "DOI": "None assigned",
    "PMID": 27725918.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA, Western blot",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"The SOLA-AD case had copious numbers of amyloid laden blood vessels in all areas of the cerebral cortex, from leptomeningeal perforating arteries to arteriolar deposits which attained the cerebral amyloid angiopathy (CAA) maximum score of 12.\", \"The SOLA-AD subject had 4.4-fold more soluble Aβ40 and 5.6-fold more insoluble Aβ40 in the frontal lobe compared to NI-AD cases.\", \"Solanezumab immunotherapy provided no apparent relief in the clinical evolution of dementia in this particular AD patient, since there was a continuous cognitive deterioration and full expression of amyloid deposition and neuropathology.\", \"The SOLA-AD case had copious numbers of blood vessels loaded with amyloid in all areas of the cerebral cortex (Figures 1D, 1E and 2) from leptomeningeal perforating arteries to arteriolar/capillary deposits which attained the CAA maximum score of 12. Figure 2 shows that the walls of the brain microvessels in the cerebral cortex of the frontal, temporal and occipital lobes were heavily loaded with amyloid deposits as demonstrated by Thioflavine-S. In contrast, the corresponding CAA scores for the 5 NI-AD cases averaged a total of 3.6 while the NDC cases only reached 0.75 (Table 1).\", \"Table 1\", \"Figure 2\", \"In this respect, the difference between our SOLA-AD case and the NI-AD cases (n = 5), in terms of the soluble and insoluble fractions, are large. In the frontal lobe, the Tris-soluble Aβ40 fraction amounted to 13,634 pg/mg total protein vs. 3,067 pg/mg total protein, respectively, and for the GDFA/GHCl-soluble Aβ40 1,711 ng/mg total protein vs. 304 ng/mg total protein, respectively. In the temporal lobe, the Tris-soluble Aβ40 fraction in the SOLA-AD case and the NI-AD group were 13,128 pg/mg total protein vs. 165 pg/mg total protein, respectively. In this regard, the SOLA-AD had 4.4-fold more soluble Aβ40 and 5.6-fold more insoluble Aβ40 in the frontal lobe compared to NI-AD cases. In the temporal lobe of the SOLA-AD case, the soluble Aβ40 was 80-fold increased, and the insoluble Aβ40 13-fold more abundant than in the NI-AD cases.\", \"Table 3\",",
    "Curator Statement": "The authors refer to solanezumab-treated AD case as SOLA-AD, to non-demented controls as NDC and non-immunized AD as NI-AD."
  },
  "AMGAB0890": {
    "Interaction ID": "AMGAB0890",
    "Antibody ID": "ABID0005",
    "Antibody name": "Solanezumab",
    "Amyloid ID": "AGAMYID0003",
    "Amyloid name": "Aβ-42",
    "DOI": "None assigned",
    "PMID": 27725918.0,
    "Impact of the antibody on amyloid formation": "No effect",
    "Experimental Model(s)": "In vivo",
    "Experimental method(s)": "Other amyloid-staining dyes (Proteostat, Th-S, hFTAA, Bis-ANS, ...), Immunohistochemistry, ELISA, Western blot",
    "Amyloid species identified": "No information provided",
    "Antibody paratope, CDR, or Negative control": "No information provided",
    "Quote of the interaction": "\"Solanezumab immunotherapy provided no apparent relief in the clinical evolution of dementia in this particular AD patient, since there was a continuous cognitive deterioration and full expression of amyloid deposition and neuropathology.\", \"Table 1\", \"Figure 1\",  \"In addition, the SOLA-AD patient demonstrated an abundant number of cortical amyloid plaques, most of them showing compact deposits of Aβ, which were similar to the number of plaque deposits observed in the NI-AD cases (total plaque scores: 13.5 and 14.7, respectively), as shown in Table 1 and Figure 1.\", \" Another interesting feature was the presence of foci of fibrillar amyloid bundles in the cerebellum of the SOLA-AD subject (Figure 1C), which are consistent with advanced amyloid dissemination observed in the final stages of AD.\", \"Table 3\",",
    "Curator Statement": "The authors refer to solanezumab-treated AD case as SOLA-AD, to non-demented controls as NDC and non-immunized AD as NI-AD."
  }
}