interactor_name,interactee_name,interactor_sequence,interactee_sequence,aggregation_speed,elongates_by_attaching,heterogenous_fibers,aggregation_speed_details,elongates_by_attaching_details,heterogenous_fibers_details,general_remarks_field,doi,AGID
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGG,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,20 µM of (B) Abeta(1–42) was co-incubated with either 0.5 or 1 µM of Abeta(1–38) and monitored for ThT fluorescence over time.,NA,Interactor: AB38 Interactee: AB42,10.1038/s41598-020-80164-w,AG00001
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGG,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,20 µM of (C) Abeta(1–40) was co-incubated with either 0.5 or 1 µM of Abeta(1–38) and monitored for ThT fluorescence over time.,NA,AB38 Interactee: AB40,10.1038/s41598-020-80164-w,AG00002
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,"Interactor: AB42, interactee: AB42",10.1038/s41598-020-80164-w,AG00003
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,"Interactor: AB40, interactee: AB40",10.1038/s41598-020-80164-w,AG00004
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGG,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGG,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,"Interactor: AB38, interactee: AB38",10.1038/s41598-020-80164-w,AG00005
Alpha-synuclein,IAPP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,"Yes, direct evidence.",Yes,"The maximum ThT emission observed at the end of the reaction for co-incubated hIAPP and halphaSyn was ~ fivefold higher than that observed for hIAPP alone (Fig. 2A), suggesting that hIAPP and halphaSyn cross-seed fibril formation. • Moreover, the end stage ThT emission when cross-seeding IAPP monomers with 35 and 70 µM of halphaSyn monomers was not only distinctly higher than that observed when co-incubating 2 µM hIAPP and 7 µM halphaSyn monomers (Fig. 3a–c) but resulted in maximal measurable ThT emission levels that exceeded the setting of the plate reader (Fig. 3b,c). • Similarly, when using a higher hIAPP monomer concentration of 4 µM, co-incubation with 7, 35, and 70 µM halphaSyn monomers potently and dose dependently cross-seeded fibril formation as evident from the increase in both ThT emission (Supplementary Fig. 8a) and fibrillar density (Supplementary Fig. 8b–e)","Te maximum TT emission observed at the end of the reaction for co-incubated hIAPP and halphaSyn was~fvefold higher than that observed for hIAPP alone (Fig. 2a), suggesting that hIAPP and halphaSyn cross-seed fbril formation. Consistently, halphaSyn and IAPP TEM double immunogold labelling of the end-stage formed fbrils revealed prominent, dense fbrillar structures that was composed of both alphaSyn and hIAPP, suggesting that under these conditions halphaSyn and hIAPP form heterofbrils (Fig. 2b,b’).","Consistently, halphaSyn and IAPP TEM double immunogold labelling of the end-stage formed fibrils revealed prominent, dense fibrillar structures that was composed of both alphaSyn and hIAPP, suggesting that under these conditions halphaSyn and hIAPP form heterofibrils","interactor: halphaSyn monomers (7 μM, 35 μM, 70 μM)  interactee: hIAPP monomers (2 μM, 4 μM)",10.1038/s41598-020-77409-z,AG00006
Alpha-synuclein,IAPP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Formation of fibrils by the interactee is inhibited,No,"Compared with that of 2 μM hIAPP monomers alone, 7 μM halphaSyn seeds negatively influenced amyloid fibril formation (Fig. 2f)","Compared with that of 2 μM hIAPP monomers alone, 7 μM halphaSyn seeds negatively influenced amyloid fibril formation (Fig. 2f)","Together, these data suggest that at equimolar concentrations to that of monomers, i.e. 7 µM, pre-formed seeds and fibrils do not promote fibrillar growth of hIAPP monomers nor hIAPP hetero-amyloid fibril formation.","interactor: halphaSyn seeds, i.e. sonicated pre-formed halphaSyn fibrils (7 μM)  interactee: hIAPP monomers (2 μM) Together, these data provide evidence that halphaSyn and hIAPP monomers dose-dependently and bi-directionally cross-seed and co-aggregate into hybrid amyloid fibrils at concentrations of alphaSyn monomer of 7 μM or higher, whereas seeds and fibrils are less potent at crossseeding IAPP monomer fibril formation and growth at equimolar concentrations.",10.1038/s41598-020-77409-z,AG00007
Alpha-synuclein,IAPP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,No,No,and halphaSyn pre-formed fibrils resulted in ThT emission curves that were superimposed over that of 2 μM hIAPP monomers alone (Fig. 2h),and halphaSyn pre-formed fibrils resulted in ThT emission curves that were superimposed over that of 2 μM hIAPP monomers alone (Fig. 2h),"Together, these data suggest that at equimolar concentrations to that of monomers, i.e. 7 µM, pre-formed seeds and fibrils do not promote fibrillar growth of hIAPP monomers nor hIAPP hetero-amyloid fibril formation.","interactor: halphaSyn pre-formed fibrils (7 μM)  interactee: hIAPP monomers (2 μM) Together, these data provide evidence that halphaSyn and hIAPP monomers dose-dependently and bi-directionally cross-seed and co-aggregate into hybrid amyloid fibrils at concentrations of alphaSyn monomer of 7 μM or higher, whereas seeds and fibrils are less potent at crossseeding IAPP monomer fibril formation and growth at equimolar concentrations.",10.1038/s41598-020-77409-z,AG00008
Alpha-synuclein,IAPP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,"Although 7 μM halphaSyn seeds and fbrils did not stimulate fbril growth when combined with 2 μM hIAPP monomers (Fig. 2f,h), higher concentrations, i.e. 35 and 70 μM, of halphaSyn seeds and fbrils enhanced TT emission levels as compared with that of hIAPP monomers or halphaSyn seeds and fbrils alone (Supplementary Fig. 10a–f).","higher concentrations, i.e. 35 and 70 µM, of halphaSyn seeds and fibrils enhanced ThT emission levels as compared with that of hIAPP monomers or halphaSyn seeds and fibrils alone",NA,"interactor: halphaSyn seeds (i.e. sonicated pre-formed) and fibrils (35 and 70 µM)  interactee: hIAPP monomers (2 μM) Together, these data provide evidence that halphaSyn and hIAPP monomers dose-dependently and bi-directionally cross-seed and co-aggregate into hybrid amyloid fibrils at concentrations of alphaSyn monomer of 7 μM or higher, whereas seeds and fibrils are less potent at crossseeding IAPP monomer fibril formation and growth at equimolar concentrations.",10.1038/s41598-020-77409-z,AG00009
Alpha-synuclein,IAPP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No,No information,"Cross-seeding 2 µM hIAPP monomers with lower, 0.2 µM, concentrations of halphaSyn monomers, seeds, and fibrils resulted in none to very limited increase in ThT emission as compared to that of hIAPP monomers alone (Supplementary Fig. 11a–c).","Together, these data provide evidence that halphaSyn and hIAPP monomers dose-dependently and bi-directionally cross-seed and co-aggregate into hybrid amyloid fibrils at concentrations of .Syn monomer of 7 µM or higher, whereas seeds and fibrils are less potent at crossseeding IAPP monomer fibril formation and growth at equimolar concentrations",NA,"interactor: halphaSyn 0,2 μM monomers/seeds/fibrils  interactee: hIAPP monomers (2 μM) Together, these data provide evidence that halphaSyn and hIAPP monomers dose-dependently and bi-directionally cross-seed and co-aggregate into hybrid amyloid fibrils at concentrations of alphaSyn monomer of 7 μM or higher, whereas seeds and fibrils are less potent at crossseeding IAPP monomer fibril formation and growth at equimolar concentrations.",10.1038/s41598-020-77409-z,AG00010
IAPP,Alpha-synuclein,KCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTY,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No,"In contrast, co-incubation of non-amyloidogenic rat IAPP monomers with halphaSyn monomers did not result in fibrillar growth (Supplementary Fig. 5).",co-incubation of non-amyloidogenic rat IAPP monomers with halphaSyn monomers did not result in fibrillar growth (Supplementary Fig. 5).,co-incubation of non-amyloidogenic rat IAPP monomers with halphaSyn monomers did not result in fibrillar growth (Supplementary Fig. 5).,interactor: rat IAPP monomers (2 μM) inteactee: halphaSyn monomers (7 μM) – co-incubation non-aggregating homologues of known amyloid protein,10.1038/s41598-020-77409-z,AG00011
Alpha-synuclein,IAPP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,KCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No,"In contrast, co-incubation of non-amyloidogenic rat IAPP monomers with halphaSyn monomers did not result in fibrillar growth (Supplementary Fig. 5).",co-incubation of non-amyloidogenic rat IAPP monomers with halphaSyn monomers did not result in fibrillar growth (Supplementary Fig. 5).,co-incubation of non-amyloidogenic rat IAPP monomers with halphaSyn monomers did not result in fibrillar growth (Supplementary Fig. 5).,interacotr: halphaSyn monomers (7 μM)  interactee: rat IAPP monomers (2 μM) – co-incubation non-aggregating homologues of known amyloid protein,10.1038/s41598-020-77409-z,AG00012
Alpha-synuclein,IAPP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,whereas preformed aS amyloid seeds inhibit IAPP amyloid formation (Fig. 2 C and G),whereas preformed aS amyloid seeds inhibit IAPP amyloid formation (Fig. 2 C and G),NA,Interactor: alpha-synuclein amyloid seeds Interactee: IAPP,10.1073/pnas.1610371113,AG00013
IAPP,Alpha-synuclein,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,We found that preformed IAPP amyloid seeds speed up aS amyloid formation (Fig. 2A),"Cross-seeding of amyloid fiber formation of aS by IAPP amyloid seeds: 70 µM aS alone (black), with 3.5 µM (red) and 7 µM (blue) IAPP amyloid seeds added",The resulting amyloid fibers (from reactions in Fig. 2 A and B) have the dimensions matching that of the aggregating protein when aggregating alone,Interactor: IAPP amyloid fiber seeds Interactee: alpha-synuclein,10.1073/pnas.1610371113,AG00014
Alpha-synuclein,IAPP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,TPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYGLRNAVEVLKREPLNYLPL,Faster aggregation,Yes; implied by kinetics.,No,preformed aS amyloid seeds speed up pro-IAPP amyloid formation (Fig. 2B),Cross-seeding of amyloid fiber formation of pro-IAPP by aS amyloid seeds: 140 µM pro-IAPP alone (black) and with 7 µM (red) aS amyloid seeds added.,The resulting amyloid fibers (from reactions in Fig. 2 A and B) have the dimensions matching that of the aggregating protein when aggregating alone,Interactor: alpha-synuclein amyloid fiber seeds Interactee: pro-IAPP,10.1073/pnas.1610371113,AG00015
IAPP,Alpha-synuclein,TPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYGLRNAVEVLKREPLNYLPL,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No,and preformed pro-IAPP amyloid seeds inhibit aS amyloid formation (Fig. 2 D and H),"Inhibition of amyloid fiber formation of aS by pro-IAPP amyloid seeds: 70 µM aS alone (black), with 7 µM (red) and 14 µM (blue) pro-IAPP fibrils.",and preformed pro-IAPP amyloid seeds inhibit aS amyloid formation (Fig. 2 D and H),Interactor: pro-IAPP amyloid fiber seeds Interctee: alpha-synuclein,10.1073/pnas.1610371113,AG00016
IAPP,Alpha-synuclein,TPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYGLRNAVEVLKREPLNYLPL,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No information,"the pro-IAPP monomers inhibit aS aggregation in a concentration-dependent manner (Fig. 3A). Notably, under these conditions, pro-IAPP itself does not form amyloid fibers. Thus, like the pro-IAPP seeds (Fig. 2D), pro-IAPP monomers block aS from aggregation and the atomic force microscopy (AFM) images lack amyloids or oligomers (Fig. 3D)","the pro-IAPP monomers inhibit aS aggregation in a concentration-dependent manner (Fig. 3A). Notably, under these conditions, pro-IAPP itself does not form amyloid fibers. Thus, like the pro-IAPP seeds (Fig. 2D), pro-IAPP monomers block aS from aggregation and the atomic force microscopy (AFM) images lack amyloids or oligomers (Fig. 3D)","the pro-IAPP monomers inhibit aS aggregation in a concentration-dependent manner (Fig. 3A). Notably, under these conditions, pro-IAPP itself does not form amyloid fibers. Thus, like the pro-IAPP seeds (Fig. 2D), pro-IAPP monomers block aS from aggregation and the atomic force microscopy (AFM) images lack amyloids or oligomers (Fig. 3D)",Interactor: pro-IAPP amyloid monomers Interactee: alpha-synuclein,10.1073/pnas.1610371113,AG00017
Alpha-synuclein,IAPP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,TPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYGLRNAVEVLKREPLNYLPL,No effect,"Yes, direct evidence.",Yes,"In contrast, if aS monomers are added to high concentrations of pro-IAPP (concentration that aggregates with lag time of 30 h), the resulting thioflavin T (ThT) emission becomes significantly increased but the lag time remains the same (Fig. 3B). This finding implies that aS monomers become incorporated into the pro-IAPP amyloids without effect on formation speed but allowing for increased ThT emission","Effects on pro-IAPP amyloid formation upon the addition of aS monomers [140 µM proIAPP alone (black) and with 35 µM (red) or 70 µM (blue) aS]. This finding implies that aS monomers become incorporated into the pro-IAPP amyloids without effect on formation speed but allowing for increased ThT emission. The increased ThT emission may be due to better ThT binding to resulting mixed amyloid fibers or simply more amyloids are made.In essence, therefore, aS amyloid formation becomes slowed down when monomers are added to high concentrations of pro-IAPP and instead pro-IAPP is capable of recruiting the aS monomers into its amyloid fibers. AFM images of these mixtures imply that thicker fibrils are formed (8–10 nm) compared with the fibrils of pro-IAPP alone (Fig. 3E and Table 1).","Effects on pro-IAPP amyloid formation upon the addition of aS monomers [140 µM proIAPP alone (black) and with 35 µM (red) or 70 µM (blue) aS]. This finding implies that aS monomers become incorporated into the pro-IAPP amyloids without effect on formation speed but allowing for increased ThT emission. The increased ThT emission may be due to better ThT binding to resulting mixed amyloid fibers or simply more amyloids are made.In essence, therefore, aS amyloid formation becomes slowed down when monomers are added to high concentrations of pro-IAPP and instead pro-IAPP is capable of recruiting the aS monomers into its amyloid fibers. AFM images of these mixtures imply that thicker fibrils are formed (8–10 nm) compared with the fibrils of pro-IAPP alone (Fig. 3E and Table 1).",Interactor: alpha-synuclein monomers Interactee: pro-IAPP,10.1073/pnas.1610371113,AG00018
Alpha-synuclein,IAPP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,"Yes, direct evidence.",Yes,"In contrast, mixing of IAPP and aS monomers results in coaggregation that is faster than either protein alone","AFM images of these mixtures suggest that the resulting amyloid fibers have a thickness of only ∼2 nm, which is thinner than what we observe for the two homoprotein amyloids (Table 1). The resulting amyloid fibers in the aS–IAPP mixture appear needle-like with rough, but sharp, edges according to thorough AFM image inspection (Fig. 3F; we note that AFM quantification, apart from the Z height, is uncertain). In contrast to the typical amyloids formed by IAPP and aS individually, the amyloid fibers formed in mixtures of the two monomers are very fragile: the AFM tip easily destroys these fibers. Therefore, the tapping mode imaging was possible only at instrument settings that corresponded to the exposure to weak forces. The differences in amyloid fiber morphology, together with the altered reaction kinetics, strongly argue for the formation of coassembled amyloids of aS and IAPP.","AFM images of these mixtures suggest that the resulting amyloid fibers have a thickness of only ∼2 nm, which is thinner than what we observe for the two homoprotein amyloids (Table 1). The resulting amyloid fibers in the aS–IAPP mixture appear needle-like with rough, but sharp, edges according to thorough AFM image inspection (Fig. 3F; we note that AFM quantification, apart from the Z height, is uncertain). In contrast to the typical amyloids formed by IAPP and aS individually, the amyloid fibers formed in mixtures of the two monomers are very fragile: the AFM tip easily destroys these fibers. Therefore, the tapping mode imaging was possible only at instrument settings that corresponded to the exposure to weak forces. The differences in amyloid fiber morphology, together with the altered reaction kinetics, strongly argue for the formation of coassembled amyloids of aS and IAPP.",Interactor: alpha-synuclein monomers Interactee: IAPP monomers,10.1073/pnas.1610371113,AG00019
IAPP,Alpha-synuclein,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",Yes,"In contrast, mixing of IAPP and aS monomers results in coaggregation that is faster than either protein alone","""AFM images of these mixtures suggest that the resulting amyloid fibers have a thickness of only ∼2 nm, which is thinner than what we observe for the two homoprotein amyloids (Table 1). The resulting amyloid fibers in the aS–IAPP mixture appear needle-like with rough, but sharp, edges according to thorough AFM image inspection (Fig. 3F; we note that AFM quantification, apart from the Z height, is uncertain). In contrast to the typical amyloids formed by IAPP and aS individually, the amyloid fibers formed in mixtures of the two monomers are very fragile: the AFM tip easily destroys these fibers. Therefore, the tapping mode imaging was possible only at instrument settings that corresponded to the exposure to weak forces. The differences in amyloid fiber morphology, together with the altered reaction kinetics, strongly argue for the formation of coassembled amyloids of aS and IAPP.""","""AFM images of these mixtures suggest that the resulting amyloid fibers have a thickness of only ∼2 nm, which is thinner than what we observe for the two homoprotein amyloids (Table 1). The resulting amyloid fibers in the aS–IAPP mixture appear needle-like with rough, but sharp, edges according to thorough AFM image inspection (Fig. 3F; we note that AFM quantification, apart from the Z height, is uncertain). In contrast to the typical amyloids formed by IAPP and aS individually, the amyloid fibers formed in mixtures of the two monomers are very fragile: the AFM tip easily destroys these fibers. Therefore, the tapping mode imaging was possible only at instrument settings that corresponded to the exposure to weak forces. The differences in amyloid fiber morphology, together with the altered reaction kinetics, strongly argue for the formation of coassembled amyloids of aS and IAPP.""",Interactor: IAPP monomers Interactee: alpha-synuclein monomers,10.1073/pnas.1610371113,AG00020
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",Yes,"We found that in all three cases (aS, IAPP, and pro-IAPP), preformed amyloid fiber seeds, speed up aggregation of monomers of the same protein (Fig. 1 B and C; not shown for IAPP as the seeded reaction is too fast to capture by manual mixing).","The resulting amyloid fibers have cross-sections of about 3–4 nm for IAPP and pro-IAPP, but 7–9 nm for aS (Fig. 1 D–F and Table 1). Reported amyloid fiber dimensions for IAPP are ∼5 nm for single fibers (42–44). For aS, the just-released solid-state NMR structure of full-length aS amyloid has a core dimension of ∼4.5 nm, surprisingly, with its beta-strands arranged in a Greek Key motif (45). This information implies that our larger aS amyloids may be assemblies of more than one aS proto-fibril.","The resulting amyloid fibers have cross-sections of about 3–4 nm for IAPP and pro-IAPP, but 7–9 nm for aS (Fig. 1 D–F and Table 1). Reported amyloid fiber dimensions for IAPP are ∼5 nm for single fibers (42–44). For aS, the just-released solid-state NMR structure of full-length aS amyloid has a core dimension of ∼4.5 nm, surprisingly, with its beta-strands arranged in a Greek Key motif (45). This information implies that our larger aS amyloids may be assemblies of more than one aS proto-fibril.",interactor:  alpha-synuclein amyloid fiber seeds interactee:  alpha-synuclein monomers,10.1073/pnas.1610371113,AG00021
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,"Yes, direct evidence.",Yes,"We found that in all three cases (aS, IAPP, and pro-IAPP), preformed amyloid fiber seeds, speed up aggregation of monomers of the same protein (Fig. 1 B and C; not shown for IAPP as the seeded reaction is too fast to capture by manual mixing).","The resulting amyloid fibers have cross-sections of about 3–4 nm for IAPP and pro-IAPP, but 7–9 nm for aS (Fig. 1 D–F and Table 1). Reported amyloid fiber dimensions for IAPP are ∼5 nm for single fibers (42–44). For aS, the just-released solid-state NMR structure of full-length aS amyloid has a core dimension of ∼4.5 nm, surprisingly, with its beta-strands arranged in a Greek Key motif (45). This information implies that our larger aS amyloids may be assemblies of more than one aS proto-fibril.","The resulting amyloid fibers have cross-sections of about 3–4 nm for IAPP and pro-IAPP, but 7–9 nm for aS (Fig. 1 D–F and Table 1). Reported amyloid fiber dimensions for IAPP are ∼5 nm for single fibers (42–44). For aS, the just-released solid-state NMR structure of full-length aS amyloid has a core dimension of ∼4.5 nm, surprisingly, with its beta-strands arranged in a Greek Key motif (45). This information implies that our larger aS amyloids may be assemblies of more than one aS proto-fibril.",Interactor: IAPP amyloid fiber seeds Interactee: IAPP monomers,10.1073/pnas.1610371113,AG00022
IAPP,IAPP,TPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYGLRNAVEVLKREPLNYLPL,TPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYGLRNAVEVLKREPLNYLPL,Faster aggregation,No information,No information,"We found that in all three cases (aS, IAPP, and pro-IAPP), preformed amyloid fiber seeds, speed up aggregation of monomers of the same protein (Fig. 1 B and C; not shown for IAPP as the seeded reaction is too fast to capture by manual mixing).",NA,NA,Interactor: pro-IAPP amyloid fiber seeds Interactee: pro-IAPP monomers,10.1073/pnas.1610371113,AG00023
Amyloid beta,Tau,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,Faster aggregation,"Yes, direct evidence.",No,Quantitative analysis at the different time points post-seeding revealed that Abeta-seeds induced significant Tau-aggregation at 3 days post-seeding (Fig. 3).,NA,"Abeta is scarcely detected per fibril compared to the abundant detection of Tau, suggesting that Abeta-seeds provide a nucleus, which is subsequently preferably extended by TauMono",Interactor: Amyloid beta (1-42) seeds Interactee: Tau monomers,10.1007/s00401-015-1525-x,AG00024
Tau,Tau,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,Faster aggregation,"Yes, direct evidence.",No information,Quantitative analysis revealed significant induction of Tau-aggregation by Abeta-seeds and Tau-seeds,NA,NA,Interactor: Tau seeds Interactee: Tau monomers,10.1007/s00401-015-1525-x,AG00025
Amyloid beta,Tau,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,Faster aggregation,"Yes, direct evidence.",No information,Pre-aggregated Abeta-seeds strongly accelerate incipient or preexisting Tau-aggregation,NA,NA,Interactor: Amyloid beta (1-42) seeds Interactee: Tau seeds,10.1007/s00401-015-1525-x,AG00026
Amyloid beta,Tau,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,No aggregation,Formation of fibrils by the interactee is inhibited,No,their monomeric forms (monomeric Tau and monomeric Abeta) did not induce significant Tauaggregation in this assay (Fig. S2).,their monomeric forms (monomeric Tau and monomeric Abeta) did not induce significant Tauaggregation in this assay (Fig. S2).,NA,Interactor: Amyloid beta (1-42) monomers Interactee: Tau monomers,10.1007/s00401-015-1525-x,AG00027
IAPP,Tau,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Pre-aggregated Abeta, but not pre-aggregated amylin, nor albumin, induce aggregation of monomeric Tau, following direct co-incubation","Pre-aggregated Abeta, but not pre-aggregated amylin, nor albumin, induce aggregation of monomeric Tau, following direct co-incubation","Pre-aggregated Abeta, but not pre-aggregated amylin, nor albumin, induce aggregation of monomeric Tau, following direct co-incubation",Interactor: Amylin seeds  Interactee: Tau monomers,10.1007/s00401-015-1525-x,AG00028
Albumin,Tau,MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPF EDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEP ERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLF FAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAV ARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLK ECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYAR RHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFE QLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVV LNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTL SEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLV AASQAALGL,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Pre-aggregated Abeta, but not pre-aggregated amylin, nor albumin, induce aggregation of monomeric Tau, following direct co-incubation","Pre-aggregated Abeta, but not pre-aggregated amylin, nor albumin, induce aggregation of monomeric Tau, following direct co-incubation","Pre-aggregated Abeta, but not pre-aggregated amylin, nor albumin, induce aggregation of monomeric Tau, following direct co-incubation",Interactor: Albumin  Interactee: Tau monomers There is no information about Albumin sequence so I've chosen uniprot sequence.,10.1007/s00401-015-1525-x,AG00029
CsgA,CsgA,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Faster aggregation,Yes; implied by kinetics.,No information,"Addition of preformed CsgAEC fiber seeds completely eliminated the lag phase (Fig. 1A), which was consistent with previous observations (55)","Taken together, these results suggest that CsgA homologs from different bacteria efficiently cross-seed in vitro.",NA,"The article explored the csgA / csgB interactions of different species. Here, both interactee and interactor came from Escherichia coli.",10.1074/jbc.M112.383737,AG00030
CsgA,CsgA,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGNHNGGGNSSGPDSTLSIYQYGSANAALALQSDARKSETTITQSGYGNGADVGQGADNSTIELTQNGFRNNATIDQWNAKNSDITVGQYGGNNAALVNQTASDSSVMVRQVGFGNNATANQY,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Faster aggregation,Yes; implied by kinetics.,No information,"In the presence of 5% (w/w) preformed CsgAST or CsgACK seeds, CsgAEC fibrillated with no lag phase, indicating fibers of CsgAST or CsgACK efficiently cross-seeded CsgAEC polymerization (Fig. 1A)","In the presence of 5% (w/w) preformed CsgAST or CsgACK seeds, CsgAEC fibrillated with no lag phase, indicating fibers of CsgAST or CsgACK efficiently cross-seeded CsgAEC polymerization (Fig. 1A)",NA,"The article explored the csgA / csgB interactions of different species. Here, interactor came from Salmonella typhimurium and interactee came from Escherichia coli.",10.1074/jbc.M112.383737,AG00031
CsgA,CsgA,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGGHNNGGNNSGPESTLSIFQYGSANSALALQSDARKSDLSIKQYGHGNGADVGQGADNSGIDLTQNGYRNSATIDQWNAKNSDIVVSQFGGRNGALVNQTASDSQVSVTQVGFGNNATANQY,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Faster aggregation,Yes; implied by kinetics.,No information,"In the presence of 5% (w/w) preformed CsgAST or CsgACK seeds, CsgAEC fibrillated with no lag phase, indicating fibers of CsgAST or CsgACK efficiently cross-seeded CsgAEC polymerization (Fig. 1A)","In the presence of 5% (w/w) preformed CsgAST or CsgACK seeds, CsgAEC fibrillated with no lag phase, indicating fibers of CsgAST or CsgACK efficiently cross-seeded CsgAEC polymerization (Fig. 1A)",NA,"The article explored the csgA / csgB interactions of different species. Here, interactor came from Citrobacter koseri and interactee came from Escherichia coli.",10.1074/jbc.M112.383737,AG00032
CsgA,CsgA,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGNHNGGGNSSGPDSTLSIYQYGSANAALALQSDARKSETTITQSGYGNGADVGQGADNSTIELTQNGFRNNATIDQWNAKNSDITVGQYGGNNAALVNQTASDSSVMVRQVGFGNNATANQY,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGNHNGGGNSSGPDSTLSIYQYGSANAALALQSDARKSETTITQSGYGNGADVGQGADNSTIELTQNGFRNNATIDQWNAKNSDITVGQYGGNNAALVNQTASDSSVMVRQVGFGNNATANQY,Faster aggregation,Yes; implied by kinetics.,No information,"Like CsgAEC, monomeric CsgAST assembled into fibers with an approximately 4 h lag phase. The polymerization was accelerated by 5% (w/w) of its own fibers, CsgAEC fibers, or CsgACK fibers (Fig. 1B).","Taken together, these results suggest that CsgA homologs from different bacteria efficiently cross-seed in vitro.",NA,"The article explored the csgA / csgB interactions of different species. Here, both interactee and interactor came from Salmonella typhimurium.",10.1074/jbc.M112.383737,AG00033
CsgA,CsgA,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGNHNGGGNSSGPDSTLSIYQYGSANAALALQSDARKSETTITQSGYGNGADVGQGADNSTIELTQNGFRNNATIDQWNAKNSDITVGQYGGNNAALVNQTASDSSVMVRQVGFGNNATANQY,Faster aggregation,Yes; implied by kinetics.,No information,"Like CsgAEC, monomeric CsgAST assembled into fibers with an approximately 4 h lag phase. The polymerization was accelerated by 5% (w/w) of its own fibers, CsgAEC fibers, or CsgACK fibers (Fig. 1B).","Taken together, these results suggest that CsgA homologs from different bacteria efficiently cross-seed in vitro.",NA,"The article explored the csgA / csgB interactions of different species. Here, interactor came from Escherichia coli and interactee came from Salmonella typhimurium.",10.1074/jbc.M112.383737,AG00034
CsgA,CsgA,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGGHNNGGNNSGPESTLSIFQYGSANSALALQSDARKSDLSIKQYGHGNGADVGQGADNSGIDLTQNGYRNSATIDQWNAKNSDIVVSQFGGRNGALVNQTASDSQVSVTQVGFGNNATANQY,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGNHNGGGNSSGPDSTLSIYQYGSANAALALQSDARKSETTITQSGYGNGADVGQGADNSTIELTQNGFRNNATIDQWNAKNSDITVGQYGGNNAALVNQTASDSSVMVRQVGFGNNATANQY,Faster aggregation,Yes; implied by kinetics.,No information,"Like CsgAEC, monomeric CsgAST assembled into fibers with an approximately 4 h lag phase. The polymerization was accelerated by 5% (w/w) of its own fibers, CsgAEC fibers, or CsgACK fibers (Fig. 1B).","Taken together, these results suggest that CsgA homologs from different bacteria efficiently cross-seed in vitro.",NA,"The article explored the csgA / csgB interactions of different species. Here, interactor came from Citrobacter koseri and interactee came from Salmonella typhimurium.",10.1074/jbc.M112.383737,AG00035
CsgA,CsgA,MKSQAKMSLIALAITAGLSGHALAASTINEISVKQTGEGQDTLVAQTGVINAAAVTQTGNAQVATVVQDGVWHEAQVNSTGDANEVTVSQQTDWHVAAVDVTGNNNEAEVTQDGFFNQSSNDVVGNDNLVSVNQLGELNESYVEITGNENSAFVEQEGDENLAVFRVEGDNNDGDIKQYGNNNQAGLIALDLSANVGNNNDVSVEQIGNNNFGAAKGIAGNDNSVDIYQKGDNHTGFVYALAGSENDISMEQEGSNNTAYLSMTTGDDNTVDITQDGDSNTVGDSLIADIQGDDNDITIKQKGDSNGAEFQVWGDSNDVDLKQRGDANFATFGAYGTDNDFDLSSKGDNNELVAFATGEDNSIEISQEGDANFAYVDATGNDNEVNVEQDGDQNETIITVEGNNNADVTALQHRGDLNLIDLIIEGDENAAEITQAGSGNWVGGDSSSSFAASSFGVSGDNNSLMITQTGNDNLVLGSQAGNNNSISVTQSGDMNVATVVQY,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Faster aggregation,Yes; implied by kinetics.,No information,The addition of preformed CsgASO fibers effectively eliminated the lag phase of CsgAEC polymerization (Fig. 1C).,"Taken together, these results suggest that CsgA homologs from different bacteria efficiently cross-seed in vitro.",NA,"The article explored the csgA / csgB interactions of different species. Here, interactor came from Shewanella oneidensis and interactee came from Escherichia coli.",10.1074/jbc.M112.383737,AG00036
CsgB,CsgA,MKNKLLFMMLTILGAPGIAAAAGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Faster aggregation,Yes; implied by kinetics.,No information,CsgAEC polymerization can also be seeded by E. coli CsgB (CsgBEC) fibers in vitro (Fig. 1D).,CsgAEC polymerization can also be seeded by E. coli CsgB (CsgBEC) fibers in vitro (Fig. 1D).,NA,"The article explored the csgA / csgB interactions of different species. Here, both interactee and interactor came from Escherichia coli.",10.1074/jbc.M112.383737,AG00037
CsgB,CsgA,MKNKLLFMMLTILGAPGIATATNYDLARSEYNFAVNELSKSSFNQAAIIGQVGTDNSARVRQEGSKLLSVISQEGGNNRAKVDQAGNYNFAYIEQTGNANDASISQSAYGNSAAIIQKGSGNKANITQYGTQKTAVVVQKQSHMAIRVTQR,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Faster aggregation,Yes; implied by kinetics.,No information,"To determine the seeding specificity of CsgB, CsgBE and CsgB homologs from S. typhimurium (CsgBST) were expressed and purified. 5% (w/w) CsgBST fibers efficiently promoted the polymerization of CsgAEC (Fig. 1D).","We have shown both in vitro and in vivo that CsgBEC can cross-seed CsgAST and CsgACK, and in turn CsgBST can cross-seed CsgAEC (Figs. 1, 2, and 4, and supplemental Fig. S5).",NA,"The article explored the csgA / csgB interactions of different species. Here, interactor came from Salmonella typhimurium and interactee came from Escherichia coli.",10.1074/jbc.M112.383737,AG00038
CsgB,CsgA,MKNKLLFMMLTILGAPGIAAAAGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGNHNGGGNSSGPDSTLSIYQYGSANAALALQSDARKSETTITQSGYGNGADVGQGADNSTIELTQNGFRNNATIDQWNAKNSDITVGQYGGNNAALVNQTASDSSVMVRQVGFGNNATANQY,Faster aggregation,Yes; implied by kinetics.,No information,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGNHNGGGNSSGPDSTLSIYQYGSANAALALQSDARKSETTITQSGYGNGADVGQGADNSTIELTQNGFRNNATIDQWNAKNSDITVGQYGGNNAALVNQTASDSSVMVRQVGFGNNATANQY,"Similarly, 5% (w/w) CsgBEC seeds cross-seeded the polymerization of CsgAST and CsgACK (Fig. 1E and data not shown), suggesting that CsgB can cross-seed CsgA of a different bacteria.",NA,"The article explored the csgA / csgB interactions of different species. Here, interactor came from Escherichia coli and interactee came from  Salmonella typhimurium.",10.1074/jbc.M112.383737,AG00039
CsgB,CsgA,MKNKLLFMMLTILGAPGIATATNYDLARSEYNFAVNELSKSSFNQAAIIGQVGTDNSARVRQEGSKLLSVISQEGGNNRAKVDQAGNYNFAYIEQTGNANDASISQSAYGNSAAIIQKGSGNKANITQYGTQKTAVVVQKQSHMAIRVTQR,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGNHNGGGNSSGPDSTLSIYQYGSANAALALQSDARKSETTITQSGYGNGADVGQGADNSTIELTQNGFRNNATIDQWNAKNSDITVGQYGGNNAALVNQTASDSSVMVRQVGFGNNATANQY,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"The article explored the csgA / csgB interactions of different species. Here, both interactee and interactor came from Salmonella typhimurium.",10.1074/jbc.M112.383737,AG00040
CsgA,CsgA,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYAYGGGASALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTAVGFGANATAHQY,Faster aggregation,Yes; implied by kinetics.,No information,"Consistent with previous results, 5% E. coli CsgA fibers completely eliminated the lag phase and promoted the polymerization of CsgAslowgo (Fig. 3)","CsgAslowgo (CsgAQ49A,N54A,Q139A,N144A), which can be seeded by E. coli CsgA fibers",NA,"Both interactee and interactor came from Escherichia coli. As interactee CsgAslowgo =  (CsgAQ49A,N54A,Q139A,N144A) was considered.",10.1074/jbc.M112.383737,AG00041
CsgA,CsgA,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGNHNGGGNSSGPDSTLSIYQYGSANAALALQSDARKSETTITQSGYGNGADVGQGADNSTIELTQNGFRNNATIDQWNAKNSDITVGQYGGNNAALVNQTASDSSVMVRQVGFGNNATANQY,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYAYGGGASALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTAVGFGANATAHQY,No effect,No,No information,"The polymerization of freshly purified CsgAslowgo was not efficiently seeded by fibers of CsgAST, CsgACK, or CsgASO (Fig. 3 and data not shown).","The polymerization of freshly purified CsgAslowgo was not efficiently seeded by fibers of CsgAST, CsgACK, or CsgASO (Fig. 3 and data not shown).",NA,"Here, interactor came from Salmonella typhimurium and interactee came from Escherichia coli. As interactee CsgAslowgo = (CsgAQ49A,N54A,Q139A,N144A) was considered.",10.1074/jbc.M112.383737,AG00042
CsgA,CsgA,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGGHNNGGNNSGPESTLSIFQYGSANSALALQSDARKSDLSIKQYGHGNGADVGQGADNSGIDLTQNGYRNSATIDQWNAKNSDIVVSQFGGRNGALVNQTASDSQVSVTQVGFGNNATANQY,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYAYGGGASALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTAVGFGANATAHQY,No effect,No,No information,"The polymerization of freshly purified CsgAslowgo was not efficiently seeded by fibers of CsgAST, CsgACK, or CsgASO (Fig. 3 and data not shown).","The polymerization of freshly purified CsgAslowgo was not efficiently seeded by fibers of CsgAST, CsgACK, or CsgASO (Fig. 3 and data not shown).",NA,"Here, interactor came from Citrobacter koseri and interactee came from Escherichia coli. As interactee CsgAslowgo = (CsgAQ49A,N54A,Q139A,N144A) was considered.",10.1074/jbc.M112.383737,AG00043
CsgA,CsgA,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGGHNNGGNNSGPESTLSIFQYGSANSALALQSDARKSDLSIKQYGHGNGADVGQGADNSGIDLTQNGYRNSATIDQWNAKNSDIVVSQFGGRNGALVNQTASDSQVSVTQVGFGNNATANQY,Faster aggregation,Yes; implied by kinetics.,No information,CsgACK also self-polymerized and could be cross-seeded by seeds of CsgAEC or CsgAST (data not shown).,CsgACK also self-polymerized and could be cross-seeded by seeds of CsgAEC or CsgAST (data not shown).,NA,"The article explored the csgA / csgB interactions of different species. Here, interactor came from Escherichia coli and interactee came from Citrobacter koseri.",10.1074/jbc.M112.383737,AG00044
CsgA,CsgA,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGNHNGGGNSSGPDSTLSIYQYGSANAALALQSDARKSETTITQSGYGNGADVGQGADNSTIELTQNGFRNNATIDQWNAKNSDITVGQYGGNNAALVNQTASDSSVMVRQVGFGNNATANQY,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGGHNNGGNNSGPESTLSIFQYGSANSALALQSDARKSDLSIKQYGHGNGADVGQGADNSGIDLTQNGYRNSATIDQWNAKNSDIVVSQFGGRNGALVNQTASDSQVSVTQVGFGNNATANQY,Faster aggregation,Yes; implied by kinetics.,No information,CsgACK also self-polymerized and could be cross-seeded by seeds of CsgAEC or CsgAST (data not shown).,CsgACK also self-polymerized and could be cross-seeded by seeds of CsgAEC or CsgAST (data not shown).,NA,"The article explored the csgA / csgB interactions of different species. Here, interactor came from Salmonella typhimurium and interactee came from Citrobacter koseri.",10.1074/jbc.M112.383737,AG00045
CsgB,CsgA,MKNKLLFMMLTILGAPGIAAAAGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR,MKLLKVAAFAAIVVSGSALAGVVPQWGGGGGHNNGGNNSGPESTLSIFQYGSANSALALQSDARKSDLSIKQYGHGNGADVGQGADNSGIDLTQNGYRNSATIDQWNAKNSDIVVSQFGGRNGALVNQTASDSQVSVTQVGFGNNATANQY,Faster aggregation,Yes; implied by kinetics.,No information,"Similarly, 5% (w/w) CsgBEC seeds cross-seeded the polymerization of CsgAST and CsgACK (Fig. 1E and data not shown), suggesting that CsgB can cross-seed CsgA of a different bacteria.","Similarly, 5% (w/w) CsgBEC seeds cross-seeded the polymerization of CsgAST and CsgACK (Fig. 1E and data not shown), suggesting that CsgB can cross-seed CsgA of a different bacteria.",NA,"The article explored the csgA / csgB interactions of different species. Here, interactor came from Escherichia coli and interactee came from Citrobacter koseri.",10.1074/jbc.M112.383737,AG00046
Amyloid beta,CsgA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,No effect,No,No information,Curli subunits didn’t cross-seed with Abeta1-42 or Sup35-NM.,Neither Abeta1–42 nor Sup35 NM was able to seed CsgAEC,NA,"Here, interactee came from Escherichia coli and interactor is  Abeta1–42",10.1074/jbc.M112.383737,AG00047
Sup35,CsgA,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"Moreover, circular dichroism spectra revealed that the secondary structures of CsgA fibers and Sup35-NM fibers are different, NM fibers have more random coil structure (7, 79) (data not shown), indicating that CsgA and Sup35 fibers may adopt incompatible conformations that limit the cross-seeding efficiency.","Moreover, circular dichroism spectra revealed that the secondary structures of CsgA fibers and Sup35-NM fibers are different, NM fibers have more random coil structure (7, 79) (data not shown), indicating that CsgA and Sup35 fibers may adopt incompatible conformations that limit the cross-seeding efficiency.",NA,"as interactor Sup35 NM (N-terminal and middle domain) was used, interactee is CsgA Escherichia coli",10.1074/jbc.M112.383737,AG00048
CsgB,Sup35,MKNKLLFMMLTILGAPGIAAAAGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,No effect,No,No information,NA,"Neither Abeta1–42 nor Sup35 NM was able to seed CsgAEC, nor could the fibrillization of Abeta1–42 or Sup35 NM be seeded by CsgBEC fibers (supplemental Fig. S3).",NA,as interactee Sup35 NM (N-terminal and middle domain) was used and interactor came from Escherichia coli,10.1074/jbc.M112.383737,AG00049
CsgA,Amyloid beta,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No,No information,NA,"Therefore, although cross-seeding occurs between curli homologs, curli cannot cross-seed with unrelated amyloidogenic proteins.",NA,as interactee Abeta1–42 and as interactor CsgA Escherichia coli,10.1074/jbc.M112.383737,AG00050
CsgA,Sup35,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,Faster aggregation,Yes; implied by kinetics.,No information,"The addition of CsgAEC seeds slightly increased the fibrillization of Sup35 NM, although to much lower levels than Sup35 NM seeded by its own fibers (supplemental Fig. S3).",NA,NA,interactee came from Escherichia coli,10.1074/jbc.M112.383737,AG00051
CsgA,CsgA,MKSQAKMSLIALAITAGLSGHALAASTINEISVKQTGEGQDTLVAQTGVINAAAVTQTGNAQVATVVQDGVWHEAQVNSTGDANEVTVSQQTDWHVAAVDVTGNNNEAEVTQDGFFNQSSNDVVGNDNLVSVNQLGELNESYVEITGNENSAFVEQEGDENLAVFRVEGDNNDGDIKQYGNNNQAGLIALDLSANVGNNNDVSVEQIGNNNFGAAKGIAGNDNSVDIYQKGDNHTGFVYALAGSENDISMEQEGSNNTAYLSMTTGDDNTVDITQDGDSNTVGDSLIADIQGDDNDITIKQKGDSNGAEFQVWGDSNDVDLKQRGDANFATFGAYGTDNDFDLSSKGDNNELVAFATGEDNSIEISQEGDANFAYVDATGNDNEVNVEQDGDQNETIITVEGNNNADVTALQHRGDLNLIDLIIEGDENAAEITQAGSGNWVGGDSSSSFAASSFGVSGDNNSLMITQTGNDNLVLGSQAGNNNSISVTQSGDMNVATVVQY,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYAYGGGASALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTAVGFGANATAHQY,No effect,No,No information,"The polymerization of freshly purified CsgAslowgo was not efficiently seeded by fibers of CsgAST, CsgACK, or CsgASO (Fig. 3 and data not shown).","The polymerization of freshly purified CsgAslowgo was not efficiently seeded by fibers of CsgAST, CsgACK, or CsgASO (Fig. 3 and data not shown).",NA,"Here, interactor came from  Shewanella oneidensis and interactee came from Escherichia coli. As interactee CsgAslowgo = (CsgAQ49A,N54A,Q139A,N144A) was considered.",10.1074/jbc.M112.383737,AG00052
CsgA,Alpha-synuclein,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTK EQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDP DNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,Purified monomeric CsgA accelerated production of alphaSyn aggregates during in vitro biochemical amyloid assays,NA,"Surprisingly, we could not detect a direct interaction between purified CsgA and aSyn monomers by surface plas- mon resonance (Figure 3—figure supplement 1D), perhaps indicating transient interactions or requirements for prior oligomerization of either or both proteins.",NA,10.7554/eLife.53111,AG00053
CsgA,Tau,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,No effect,No,No,"Unlike alphaSyn, Tau aggregation was not accelerated by CsgA",NA,NA,NA,10.7554/eLife.53111,AG00054
CsgA,Alpha-synuclein,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYAYGGGASALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTAVGFGANATAHQY,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No effect,No,No,"as a non-amyloidogenic form of CsgA (CsgA:Q49A/N54A/Q139A/N144A; ‘SlowGo’ Wang and Chapman, 2008) did not augment alphaSyn aggregation in vitro",NA,NA,NA,10.7554/eLife.53111,AG00055
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1021/acsomega.6b00559,AG00056
IAPP,IAPP,KCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,his result indicates that the introduction of rIAPP to the hIAPP solution at the nucleation stage slows down the seed formation and early aggregation of hIAPP,NA,NA,NA,10.1021/acsomega.6b00559,AG00057
IAPP,IAPP,KCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,"In Figure 1c, 15 min after the addition of rIAPP to the 6- h-seeded hIAPP solutions, the aggregation rate was accelerated, as indicated by immediate ThT signal enhancement followed by a deeper slope at the growth phase.",NA,"because rIAPP alone does not aggregate and form amyloid fibrils, during the cross-seeding process, any increase in the final ThT intensity does not result from hIAPP fibrils alone but instead results from new hybrid hIAPP/rIAPP fibrils.",NA,10.1021/acsomega.6b00559,AG00058
IAPP,IAPP,KCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,"Finally, when adding rIAPP to the preformed hIAPP fibrils at a final plateau stage of 14 h, the cross-seeding between rIAPP and hIAPP still occurred, but the acceleration of aggregation was much less than those found for preformed hIAPP aggregates at the nucleation and growth phase",NA,"because rIAPP alone does not aggregate and form amyloid fibrils, during the cross-seeding process, any increase in the final ThT intensity does not result from hIAPP fibrils alone but instead results from new hybrid hIAPP/rIAPP fibrils.",NA,10.1021/acsomega.6b00559,AG00059
Alpha-lactalbumin,Amyloid beta,EQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIMCVKKILDKVGINYWLAHKALCSEKLDQWLCEKL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"Alpha-lactalbumin, albumin, and beta-lactoglobulin delayed the fibrillation of Abeta at low concentrations, their inhibition efficiencies were weaker compared with catalase and pyruvate kinase.",NA,NA,"results depends on interactor concentration. Here: 100nM, 500nM, while interactee concentration: 10µm",10.1074/jbc.M114.574947,AG00062
Albumin,Amyloid beta,MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"Alpha-lactalbumin, albumin, and beta-lactoglobulin delayed the fibrillation of Abeta at low concentrations, their inhibition efficiencies were weaker compared with catalase and pyruvate kinase.",NA,NA,"results depend on interactor concentration. Here: 500nM, while interactee concentration: 10µm",10.1074/jbc.M114.574947,AG00063
Beta-lactoglobulin,Amyloid beta,LIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"Alpha-lactalbumin, albumin, and beta-lactoglobulin delayed the fibrillation of Abeta at low concentrations, their inhibition efficiencies were weaker compared with catalase and pyruvate kinase.",NA,NA,"results depend on interactor concentration. Here: 10µm, 1µm, while interactee concentration: 10µm",10.1074/jbc.M114.574947,AG00064
Alpha-lactalbumin,Amyloid beta,EQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIMCVKKILDKVGINYWLAHKALCSEKLDQWLCEKL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Albumin and alpha-lactalbumin completely prevented Abeta fibrillation >24 h at 1 and 10 µm, respectively.","Albumin and alpha-lactalbumin completely prevented Abeta fibrillation >24 h at 1 and 10 µm, respectively.","Albumin and alpha-lactalbumin completely prevented Abeta fibrillation >24 h at 1 and 10 µm, respectively.","results depend on interactor concentration. Here: 1µm, 10µm, while interactee concentration: 10µm",10.1074/jbc.M114.574947,AG00065
Albumin,Amyloid beta,MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Albumin and alpha-lactalbumin completely prevented Abeta fibrillation >24 h at 1 and 10 µm, respectively.","Albumin and alpha-lactalbumin completely prevented Abeta fibrillation >24 h at 1 and 10 µm, respectively.","Albumin and alpha-lactalbumin completely prevented Abeta fibrillation >24 h at 1 and 10 µm, respectively.","results depend on interactor concentration. Here: 1µm, 10µm, while interactee concentration: 10µm",10.1074/jbc.M114.574947,AG00066
Lysozyme,Amyloid beta,MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1074/jbc.M114.574947,AG00067
Beta-lactoglobulin,Amyloid beta,LIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No information,No information,NA,NA,NA,"results depend on interactor concentration. Here: 500µm,100µm, while interactee concentration: 10µm",10.1074/jbc.M114.574947,AG00068
Albumin,Amyloid beta,MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No information,No information,NA,NA,NA,"results depend on interactor concentration. Here: 100µm, while interactee concentration: 10µm",10.1074/jbc.M114.574947,AG00069
Rnq1,Sup35,MDTDKLISEAESHFSQGNHAEAVAKLTSAAQSNPNDEQMSTIESLIQKIAGYVMDNRSGGSDASQDRAAGGGSSFMNTLMADSKGSSQTQLGKLALLATVMTHSSNKGSSNRGFDVGTVMSMLSGSGGGSQSMGASGLAALASQFFKSGNNSQGQGQGQGQGQGQGQGQGQGSFTALASLASSFMNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQ YQQQGQNYQHQQQGQQQQQGHSSSFSALASMASSYLGNNSNSNSSYGGQQQANEYGRPQQNGQQQSNEYGRPQYGGNQNSNGQHESFNFSGNFSQQNNNGNQNRY,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,Faster aggregation,"Yes, direct evidence.",No information,The addition of Rnq1 fibers (orange line) reduces the lag time for Sup35 polymerization to approximately 12.5hours,"However, there was a strong interaction between Rnq1 and Sup35 when the Sup35NM-7xHis protein was used as bait, as a large proportion of Rnq1 appeared in the bound fractions. Rnq1 was still present in the unbound fraction, yet not all Rnq1 is expected to be aggregated or Sup35-binding-competent in [RNQ+] cells. Importantly, when no Sup35NM-7xHis was present on the beads, all Rnq1 protein was present in the unbound fraction, indicating the lack of non-specific binding of Rnq1 to the column. Thus, the strong binding between ex vivo Rnq1 to the Sup35 prion-forming domain appears to be specific and stable.",NA,Interactor: Rnq1 fibers,10.1038/s41598-017-05829-5,AG00070
Rnq1,Sup35,MDTDKLISEAESHFSQGNHAEAVAKLTSAAQSNPNDEQMSTIESLIQKIAGYVMDNRSGGSDASQDRAAGGGSSFMNTLMADSKGSSQTQLGKLALLATVMTHSSNKGSSNRGFDVGTVMSMLSGSGGGSQSMGASGLAALASQFFKSGNNSQGQGQGQGQGQGQGQGQGQGSFTALASLASSFMNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQYQQQGQNYQHQQQGQQQQQGHSSSFSALASMASSYLGNNSNSNSSYGGQQQANEYGRPQQNGQQQSNEYGRPQYGGNQNSNGQHESFNFSGNFSQQNNNGNQNRY,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,No effect,No information,No information,We found that the addition of monomeric Rnq1 did not have an effect on the lag phase of Sup35 polymerization relative to the unseeded reaction.,NA,NA,Interactor: Rnq1 monomers,10.1038/s41598-017-05829-5,AG00071
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,EVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,"Yes, direct evidence.",Yes,NA,"To further support the assertion Abeta(11-40) and Abeta(1-40) fibres co-assemble we used 1H-NMR to monitor fibre growth. Spectra of Abeta(11-40) and Abeta(1-40) in D2O at pH 7.4 reveal well resolved and characteristic deltaH resonances for His13 and His14, these peaks are shifted downfield for the Abeta(11-40) peptide at pH 7.4, as shown in figure 3A. [...] The NMR experiment enables monitoring fibre growth of Abeta(11-40) and Abeta(1-40) independently from within an equimolar mixture. The lag-times are almost identical for both peptides at 7.5 hours whilst the apparent elongation rates kapp are also very similar; 0.15 and 0.17 (± 0.02) hrs-1 for Abeta(1-40) and Abeta(11-40) respectively. This strongly suggests that, in the case of Abeta(1-40) and Abeta(11-40), the fibres largely co-fibrillise.","In mixtures of Abeta(11-40)/(1-40), only short rod-like fibres are observed, similar in length to Abeta(11-40) in isolation, figure 2a. If Abeta(11-40) and Abeta(1-40) form fibres independently one would expect very long fibres to also be present, as is observed for Abeta(1-40) in isolation. Quantification of fibre length distribution, (figure 2a) indicates only very short fibres (<400 nm) are consistently present. Incorporation of Abeta(11-40) into Abeta(1-40) fibres imparts these fibres with a similar susceptibility to sheer forces as isolated Abeta(11-40)",Interactor: Abeta (1-40) Interactee: Abeta (11-40),10.1002/anie.201704618,AG00072
Amyloid beta,Amyloid beta,EVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,Interactor: Abeta (11-40) Interactee: Abeta (1-40),10.1002/anie.201704618,AG00073
Amyloid beta,Amyloid beta,EVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,"This behaviour is in marked contrast to the binary mixture of Abeta(11-40)/(1-42) this mixture does not co-fibrillise and these fibres form independently. For this mixture, there is an equal proportion of long fibres, very similar in length distribution to Abeta(1-42), together with very short fibre-rods very similar in length distribution to Abeta(11-40), shown in figure 2b",Interactor: Abeta (11-40) Interactee: Abeta (1-42),10.1002/anie.201704618,AG00074
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,EVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,Yes,NA,NA,"This behaviour is in marked contrast to the binary mixture of Abeta(11-40)/(1-42) this mixture does not co-fibrillise and these fibres form independently. For this mixture, there is an equal proportion of long fibres, very similar in length distribution to Abeta(1-42), together with very short fibre-rods very similar in length distribution to Abeta(11-40), shown in figure 2b",Interactor: Abeta (1-42) Interactee: Abeta (11-40),10.1002/anie.201704618,AG00075
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,EVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No,No,NA,"Abeta(1-40) is nucleated by Abeta(11-40) (pale blue) and Abeta(1-40) (dark blue), but not by Abeta(1- 42) (red) or Abeta(11-42) seeds (pink) at pH 7.4, Abeta(1-40) 10 µM, n = 3 traces.","Abeta(1-40) is nucleated by Abeta(11-40) (pale blue) and Abeta(1-40) (dark blue), but not by Abeta(1- 42) (red) or Abeta(11-42) seeds (pink) at pH 7.4, Abeta(1-40) 10 µM, n = 3 traces.",Interactor: Abeta (11-42) Interactee: Abeta (1-40),10.1002/anie.201704618,AG00076
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,Yes; implied by kinetics.,No,Abeta(11-42) and Abeta(1-42) do not accelerate Abeta(1-40) fibre formation.,"Studies on the assembly of Abeta(1-40) with Abeta(1-42) show that for the C-terminal truncations the two isoforms interact during early oligomerization, but go on to form fibres independently traces.","Studies on the assembly of Abeta(1-40) with Abeta(1-42) show that for the C-terminal truncations the two isoforms interact during early oligomerization, but go on to form fibres independently traces.",Interactor: Abeta (1-42) Interactee: Abeta (1-40),10.1002/anie.201704618,AG00077
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,"HEWL2 seed / monomeric HEWL pH 2, 45°C hen egg-white lysozyme (HEWL) Seed = sonicated fibrils 200 nm lenght Number means pH, pH 2 with heating",10.3389/fmolb.2020.00206,AG00078
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,"HEWL6.3 seed / monomeric HEWL pH 2, 45°C hen egg-white lysozyme (HEWL), number means pH, pH 6,3 with 3 M GdnHCl Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00079
Lysozyme,Lysozyme,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"HLZ2 seed / monomeric HEWL pH 2, 45°C Human lysozyme (HLZ), Number means pH - pH 2 with heating hen egg-white lysozyme (HEWL) Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00080
Lysozyme,Lysozyme,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"HLZ6.3 seed / monomeric HEWL pH 2, 45°C Human lysozyme (HLZ), number means pH, pH 6,3 with 3 M GdnHCl hen egg-white lysozyme (HEWL) Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00081
Lysozyme,Lysozyme,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,"HLZ2 seed / monomeric HLZ pH 2, 45°C Human lysozyme (HLZ), Number means pH, pH 2 with heating Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00082
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,"Monomeric HLZ, at pH 2, seeded with HLZ2S or cross-seeded with HEWL2S produced long, flexible fibrils (Figures 4 A, B) that looked identical to those produced during the unseeded reactions (Figures 1 A, C)","HEWL2 seed / monomeric HLZ pH 2, 45°C Human lysozyme (HLZ), hen egg-white lysozyme (HEWL), Number means pH, pH 2 with heating Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00083
Lysozyme,Lysozyme,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,"HLZ6.3 seed / monomeric HLZ pH 2, 45°C Human lysozyme (HLZ), number means pH, pH 6,3 with 3 M GdnHCl Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00084
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,"HLZ, at pH 2, cross-polymorph seeded with HLZ6.3S or cross-species-cross-polymorph seeded with HEWL6.3S, produced fibrils that were shorter and straighter (more rigid) (Figures 4C, D), being more similar to the unseeded fibrils produced at pH 6.3 (Figures 1B, D).","HEWL6.3 seed / monomeric HLZ pH 2, 45°C Human lysozyme (HLZ), hen egg-white lysozyme (HEWL), number means pH, pH 6,3 with 3 M GdnHCl Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00085
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,"HEWL6.3 seed / monomeric HEWL pH 6.3, 45°C hen egg-white lysozyme (HEWL), number means pH, pH 6,3 with 3 M GdnHCl Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00086
Lysozyme,Lysozyme,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"HLZ6.3 seed / monomeric HEWL pH 6.3, 45°C Human lysozyme (HLZ), number means pH, pH 6,3 with 3 M GdnHCl hen egg-white lysozyme (HEWL) Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00087
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,"HEWL2 seed / monomeric HEWL pH 6.3, 45°C hen egg-white lysozyme (HEWL), Number means pH, pH 2 with heating Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00088
Lysozyme,Lysozyme,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"HLZ2 seed / monomeric HEWL pH 6.3, 45°C Human lysozyme (HLZ), Number means pH, pH 2 with heating hen egg-white lysozyme (HEWL) Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00089
Lysozyme,Lysozyme,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,"HLZ6.3 seed / monomeric HLZ pH 6.3, 45°C Human lysozyme (HLZ), number means pH, pH 6,3 with 3 M GdnHCl Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00090
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,Faster aggregation,"Yes, direct evidence.",No information,NA,NA,NA,"HEWL6.3 seed / monomeric HLZ pH 6.3, 45°C Human lysozyme (HLZ), hen egg-white lysozyme (HEWL), number means pH, pH 6,3 with 3 M GdnHCl Seed = sonicated fibrils 200nm lenght",10.3389/fmolb.2020.00206,AG00091
Lysozyme,Lysozyme,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,"HLZ2 seed / monomeric HLZ pH 6.3, 45°C Human lysozyme (HLZ), Number means pH, pH 2 with heating Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00092
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,"Treating monomeric HLZ, at pH 6.3, with HLZ2S or HEWL2S, also produced short, rigid fibrils (Figures 4E, F) similar to the unseeded fibril at pH 6.3 (Figures 1B, D).","HEWL2 seed / monomeric HLZ pH 6.3, 45°C Human lysozyme (HLZ), hen egg-white lysozyme (HEWL), Number means pH, pH 2 with heating Seed = sonicated fibrils 200 nm lenght",10.3389/fmolb.2020.00206,AG00093
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Here, we looked for HEWL6.3S cross-seeding of HLZ under simulated gastric conditions (pepsin, pH 1.2, 34 mM NaCl, 37°C) and found that only one out of 36 samples showed signs of amyloid formation after 4 days (Figure 5E).","such a low propensity for amyloid fibril formation, even in the presence of fibril seeds, might be expected when the solution conditions are well below the equilibrium denaturation mid-point (conditions?)","Here, we looked for HEWL6.3S cross-seeding of HLZ under simulated gastric conditions (pepsin, pH 1.2, 34 mM NaCl, 37°C) and found that only one out of 36 samples showed signs of amyloid formation after 4 days.","HEWL6.3 pre-treated fibrils with 0,5 mg/ml pepsin / HLZ monomers in simulated gastric fluid (pH 1,2, 37°C, pepsin, 34 mM NaCl, 4 days) Human lysozyme (HLZ), hen egg-white lysozyme (HEWL), number means pH, pH 6,3 with 3 M GdnHCl",10.3389/fmolb.2020.00206,AG00094
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Here, we looked for HEWL6.3S cross-seeding of HLZ under simulated gastric conditions (pepsin, pH 1.2, 34 mM NaCl, 37°C) and found that only one out of 36 samples showed signs of amyloid formation after 4 days (Figure 5E).","such a low propensity for amyloid fibril formation, even in the presence of fibril seeds, might be expected when the solution conditions are well below the equilibrium denaturation mid-point (conditions?)","Here, we looked for HEWL6.3S cross-seeding of HLZ under simulated gastric conditions (pepsin, pH 1.2, 34 mM NaCl, 37°C) and found that only one out of 36 samples showed signs of amyloid formation after 4 days.","HEWL6.3 fibrils / HLZ monomers in simulated gastric fluid (pH 1,2, 37°C, pepsin, 34 mM NaCl, 4 days) Human lysozyme (HLZ), hen egg-white lysozyme (HEWL), number means pH, pH 6,3 with 3 M GdnHCl",10.3389/fmolb.2020.00206,AG00095
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Here, we looked for HEWL6.3S cross-seeding of HLZ under simulated gastric conditions (pepsin, pH 1.2, 34 mM NaCl, 37°C) and found that only one out of 36 samples showed signs of amyloid formation after 4 days (Figure 5E).","such a low propensity for amyloid fibril formation, even in the presence of fibril seeds, might be expected when the solution conditions are well below the equilibrium denaturation mid-point (conditions?)","Here, we looked for HEWL6.3S cross-seeding of HLZ under simulated gastric conditions (pepsin, pH 1.2, 34 mM NaCl, 37°C) and found that only one out of 36 samples showed signs of amyloid formation after 4 days.","HEWL2 sonicated fibrils / HLZ monomers in simulated gastric fluid (pH 1,2, 37°C, pepsin, 34 mM NaCl, 4 days) Human lysozyme (HLZ), hen egg-white lysozyme (HEWL), Number means pH, pH 2 with heating",10.3389/fmolb.2020.00206,AG00096
proSP-C,Amyloid beta,LVTTATFSIGSTGLVVYDYQQLLIAYKPAPGTCCYIMKIAPESIPSLEALNRKVHNFQMECSLQAKPAVPTSKLGQAEGRDAGSAPSGGDPAFLGMAVNTLCGEVPLYYI,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"Clearly, the lag time for A40 aggregation has increased exten- sively in the presence of pro-SP-C or Bri2 BRICHOS, whereas the elongation rate is largely unaffected.","Clearly, the lag time for A40 aggregation has increased exten- sively in the presence of pro-SP-C or Bri2 BRICHOS, whereas the elongation rate is largely unaffected.",NA,interactee: Aß-40,10.1074/jbc.M112.393157,AG00097
Bri2,Amyloid beta,SVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPRNLLELLINIKAGTYLPQSYLIHEHMVITDRIENIDHLGFFIYRLCHDKETYKL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"Clearly, the lag time for A40 aggregation has increased exten- sively in the presence of pro-SP-C or Bri2 BRICHOS, whereas the elongation rate is largely unaffected. Validator's answer","Clearly, the lag time for A40 aggregation has increased exten- sively in the presence of pro-SP-C or Bri2 BRICHOS, whereas the elongation rate is largely unaffected.",NA,interactee: Aß-40,10.1074/jbc.M112.393157,AG00098
proSP-C,Amyloid beta,LVTTATFSIGSTGLVVYDYQQLLIAYKPAPGTCCYIMKIAPESIPSLEALNRKVHNFQMECSLQAKPAVPTSKLGQAEGRDAGSAPSGGDPAFLGMAVNTLCGEVPLYYI,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"Both pro-SP-C and Bri2 BRICHOS retard also the aggrega- tion of A42, and only substoichiometric amounts of the BRICHOS proteins are required","Both pro-SP-C and Bri2 BRICHOS retard also the aggrega- tion of A42, and only substoichiometric amounts of the BRICHOS proteins are require",NA,interactee: Aß-42,10.1074/jbc.M112.393157,AG00099
Bri2,Amyloid beta,SVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPRNLLELLINIKAGTYLPQSYLIHEHMVITDRIENIDHLGFFIYRLCHDKETYKL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"Both pro-SP-C and Bri2 BRICHOS retard also the aggrega- tion of A42, and only substoichiometric amounts of the BRICHOS proteins are required","Both pro-SP-C and Bri2 BRICHOS retard also the aggrega- tion of A42, and only substoichiometric amounts of the BRICHOS proteins are require",NA,interactee: Aß-42,10.1074/jbc.M112.393157,AG00100
S100A9,Amyloid beta,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,"In contrast to the Ab1–40 (0.2 mM) control samples, a sharp increase in ThT intensity was observed with the addition of S100A9 (0.02 mM",NA,They were dimensionally similar to those observed in the Ab control samples after 3 d of incubation under the same condition (Fig. S1).,NA,10.1371/journal.pone.0032953,AG00101
IAPP,IAPP,QRLANFLVHSSNNFGAILSS,QRLANFLVHSSNNFGAILSS,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interactor & interactee: WT,10.1016/j.jmb.2010.09.052,AG00102
IAPP,IAPP,SSLIAGFNNSSHVLFNALRQ,QRLANFLVHSSNNFGAILSS,No effect,No,No,NA,NA,NA,Interactor: retro version of IAPP (RETRO) Interactee: WT,10.1016/j.jmb.2010.09.052,AG00103
IAPP,IAPP,LIQSAFGNNVHLSRFNSSAL,QRLANFLVHSSNNFGAILSS,No effect,No,No,NA,NA,NA,Interactor: DESIGN (based on TANGO peptide) that is devoid of any aggregation-prone regions despite sharing the same amino acid composition as WT and RETRO Interactee: WT,10.1016/j.jmb.2010.09.052,AG00104
IAPP,IAPP,SSLIAGFNNSSHVLFNALRQ,SSLIAGFNNSSHVLFNALRQ,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interactor & interactee: retro version of IAPP,10.1016/j.jmb.2010.09.052,AG00105
IAPP,IAPP,QRLANFLVHSSNNFGAILSS,SSLIAGFNNSSHVLFNALRQ,No effect,No,No,NA,NA,NA,Interactee: retro version of IAPP (RETRO) Interactor: WT,10.1016/j.jmb.2010.09.052,AG00106
IAPP,IAPP,LIQSAFGNNVHLSRFNSSAL,SSLIAGFNNSSHVLFNALRQ,No effect,No,No,NA,NA,NA,Interactor: DESIGN (based on TANGO peptide) that is devoid of any aggregation-prone regions despite sharing the same amino acid composition as WT and RETRO Interactee: retro version of IAPP,10.1016/j.jmb.2010.09.052,AG00107
IAPP,IAPP,SSLIAGFNNSSHVLFNALRQ,LIQSAFGNNVHLSRFNSSAL,No effect,No,No,NA,NA,NA,Interactee: DESIGN (based on TANGO peptide) that is devoid of any aggregation-prone regions despite sharing the same amino acid composition as WT and RETRO Interactor: retro version of IAPP,10.1016/j.jmb.2010.09.052,AG00108
IAPP,IAPP,LIQSAFGNNVHLSRFNSSAL,LIQSAFGNNVHLSRFNSSAL,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interactee & interactor: DESIGN (based on TANGO peptide) that is devoid of any aggregation-prone regions despite sharing the same amino acid composition as WT and RETRO,10.1016/j.jmb.2010.09.052,AG00109
IAPP,IAPP,QRLANFLVHSSNNFGAILSS,LIQSAFGNNVHLSRFNSSAL,No effect,No,No,NA,NA,NA,Interactee: DESIGN (based on TANGO peptide) that is devoid of any aggregation-prone regions despite sharing the same amino acid composition as WT and RETRO Interactor: WT,10.1016/j.jmb.2010.09.052,AG00110
IAPP,IAPP,KCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"The lag time matches previous experiments, as does the increase in the lag time and the decrease in intensity for inhibition experiments",NA,NA,rat IAPP / human IAPP,10.1038/nchem.1293,AG00111
proSP-C,Amyloid beta,HMSQKHTEMVLEMSIGAPEAQQRLALSEHLVTTATFSIGSTGLVVYDYQQLLIAYKPAPGTCCYIMKIAPESIPSLEALNRKVHNFQMECSLQAKPAVPTSKLGQAEGRDAGSAPSGGDPAFLGMAVNTLCGEVPLYYI,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,"Yes, direct evidence.",No information,"Monomeric S95R proSP-C BRICHOS was, however, more efficient in reducing Abeta42 fibril formation than trimeric wild-type protein (Fig. 6).; Limited trypsinization of proSP-C BRICHOS enhances the ability to delay Abeta42 aggregation, as observed by ThT fluorescence (Fig. 3E and SI Fig. S2).; Abeta42 fibrils formed with 1 μM trypsinated BRICHOS; The addition of bis-ANS shifts the oligomeric state of proSP-C BRICHOS from trimeric to monomeric (Fig. 5A) and potentiates its capacity to delay Abeta42 fibril formation (Fig. 5B and C).","To investigate if trypsinization has an effect on proSP-C BRICHOS binding to Abeta42 fibrils, we used immunoTEM, which showed that trypsinated proSP-C BRICHOS associates with the surface of Abeta42 fibrils, similar as intact proSP-C BRICHOS does (Fig. 4).",NA,"wt proSP-C BRICHOS as interactor. The authors used also proSP-C BRICHOS modifications such as trypsinization or addition of bis-ANS, what also resulted in slower aggregation.",10.1016/j.bbapap.2015.04.005,AG00112
proSP-C,Amyloid beta,HMSQKHTEMVLEMSIGAPEAQQRLALSEHLVTTATFRIGSTGLVVYDYQQLLIAYKPAPGTCCYIMKIAPESIPSLEALNRKVHNFQMECSLQAKPAVPTSKLGQAEGRDAGSAPSGGDPAFLGMAVNTLCGEVPLYYI,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"Monomeric S95R proSP-C BRICHOS was, however, more efficient in reducing Abeta42 fibril formation than trimeric wild-type protein (Fig. 6).",NA,NA,S95R proSP-C BRICHOS as interactor,10.1016/j.bbapap.2015.04.005,AG00113
PrP,IAPP,KTNMKHMAGAAAAGAVVGGLG,KCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Since the CD results indicate a relatively rapid transformation fromalpha-helix tobeta-sheetin these mixtures, it appears that PrP106−126is very effective inconverting rIAPP to the extendedbeta-hairpin conformer, butthese conformers do not subsequently go on to form proto-fibrils, unlike the hIAPP beta-hairpins.","Since the CD resultsindicate a relatively rapid transformation fromalpha-helix tobeta-sheetin these mixtures, it appears that PrP106−126is very effective inconverting rIAPP to the extendedbeta-hairpin conformer, but these conformers do not subsequently go on to form proto-fibrils, unlike the hIAPPbeta-hairpins.",NA,interactee: full length rIAPP,10.1021/jacs.8b05925,AG00115
PrP,IAPP,KTNMKHMAGAAAAGAVVGGLG,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,"Yes, direct evidence.",Yes,NA,"hat we observe,however, is that both human and rat IAPP form similar quantities of coaggregates, as seen in their respective massspectra (Figure 1)","hat we observe,however, is that both human and rat IAPP form similar quantities of coaggregates, as seen in their respective massspectra (Figure 1)",interactee: full  length hIAPP,10.1021/jacs.8b05925,AG00116
PrP,IAPP,KTNMKHMAGAAAAGAVVGGLG,KCNTATCA,No effect,"Yes, direct evidence.",Yes,NA,"The 1−8, 8−20, 20−29, and 29−37 regions of hIAPP have all been shown to be capable of self-assembly.59−62We have therefore individually combined each of these fragments with PrP106−126to as certain their aggregation propensity with the prion fragment (Figure S3). Of these, only 8−20 hIAPP formed new peaks corresponding to a 1:1 adduction of hIAPP 8−20 with PrP106−126(Figure 7A), forming aggregates up to (2 + 2) PrP106−126:hIAPP 8−20","The 1−8, 8−20, 20−29, and 29−37 regions of hIAPP have all been shown to be capable of self-assembly.59−62We have therefore individually combined each of these fragments with PrP106−126to as certain their aggregation propensity with the prion fragment (Figure S3). Of these, only 8−20 hIAPP formed new peaks corresponding to a 1:1 adduction of hIAPP 8−20 with PrP106−126(Figure 7A), forming aggregates up to (2 + 2) PrP106−126:hIAPP 8−20",interactee: 1-8hIAPP,10.1021/jacs.8b05925,AG00117
PrP,IAPP,KTNMKHMAGAAAAGAVVGGLG,ATQRLANFLVHSS,No information,"Yes, direct evidence.",Yes,NA,"The 1−8, 8−20, 20−29, and 29−37 regions of hIAPP have all been shown to be capable of self-assembly.59−62We have therefore individually combined each of these fragments with PrP106−126to as certain their aggregation propensity with the prion fragment (Figure S3). Of these, only 8−20 hIAPP formed new peaks corresponding to a 1:1 adduction of hIAPP 8−20 with PrP106−126(Figure 7A), forming aggregates up to (2 + 2) PrP106−126:hIAPP 8−20","The 1−8, 8−20, 20−29, and 29−37 regions of hIAPP have all been shown to be capable of self-assembly.59−62We have therefore individually combined each of these fragments with PrP106−126to as certain their aggregation propensity with the prion fragment (Figure S3). Of these, only 8−20 hIAPP formed new peaks corresponding to a 1:1 adduction of hIAPP 8−20 with PrP106−126(Figure 7A), forming aggregates up to (2 + 2) PrP106−126:hIAPP 8−20",interactee: 8-20 hIAPP,10.1021/jacs.8b05925,AG00118
PrP,IAPP,KTNMKHMAGAAAAGAVVGGLG,SNNFGAILSS,No information,"Yes, direct evidence.",Yes,NA,"The 1−8, 8−20, 20−29, and 29−37 regions of hIAPP have all been shown to be capable of self-assembly.59−62We have therefore individually combined each of these fragments with PrP106−126to as certain their aggregation propensity with the prion fragment (Figure S3). Of these, only 8−20 hIAPP formed new peaks corresponding to a 1:1 adduction of hIAPP 8−20 with PrP106−126(Figure 7A), forming aggregates up to (2 + 2) PrP106−126:hIAPP 8−20","The 1−8, 8−20, 20−29, and 29−37 regions of hIAPP have all been shown to be capable of self-assembly.59−62We have therefore individually combined each of these fragments with PrP106−126to as certain their aggregation propensity with the prion fragment (Figure S3). Of these, only 8−20 hIAPP formed new peaks corresponding to a 1:1 adduction of hIAPP 8−20 with PrP106−126(Figure 7A), forming aggregates up to (2 + 2) PrP106−126:hIAPP 8−20",interactee: 20-29hIAPP,10.1021/jacs.8b05925,AG00119
PrP,IAPP,KTNMKHMAGAAAAGAVVGGLG,STNVGSNTY,Faster aggregation,"Yes, direct evidence.",Yes,NA,"The 1−8, 8−20, 20−29, and 29−37 regions of hIAPP have all been shown to be capable of self-assembly.59−62We have therefore individually combined each of these fragments with PrP106−126to as certain their aggregation propensity with the prion fragment (Figure S3). Of these, only 8−20 hIAPP formed new peaks corresponding to a 1:1 adduction of hIAPP 8−20 with PrP106−126(Figure 7A), forming aggregates up to (2 + 2) PrP106−126:hIAPP 8−20","The 1−8, 8−20, 20−29, and 29−37 regions of hIAPP have all been shown to be capable of self-assembly.59−62We have therefore individually combined each of these fragments with PrP106−126to as certain their aggregation propensity with the prion fragment (Figure S3). Of these, only 8−20 hIAPP formed new peaks corresponding to a 1:1 adduction of hIAPP 8−20 with PrP106−126(Figure 7A), forming aggregates up to (2 + 2) PrP106−126:hIAPP 8−20",interactee: 29-37hIAPP,10.1021/jacs.8b05925,AG00120
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,"When fresh Ab40 was incubated with fAb40 at37C, the fluorescence increased hyperbolically without a lag phase, and a plateau occurred after ~4 h","fresh Ab40 was incubated at 37 degrees,which was characterized by a 1 day lag time, a 5 days period of increasing ThT binding, and a plateau after 6 days. When fresh Ab40 was incubated with fAb40, the fluorescence increased hyperbolically without a lag phase, and a plateau occurred after 4 h","As shown in Fig. 2b, fAb40 produced with a fresh Ab40 solution assumed a non-branched, helical filament structure of 7 nm with a helical periodicity of approximately 220 nm, as described previously (Ono et al. 2003, 2008). A typical fibrillar structure was also observed when Ab40 was incubated with fAb40, fAb42, faS, oligo Ab40, oligo Ab42, or oligo aS (Figs. 2c–h).",Interaction between fresh Ab40 and fAb40,10.1111/j.1471-4159.2012.07847.x,AG00121
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,"When fresh Ab40 was incubated with fAb40 at 37C, the fluorescence increased hyperbolically without a lag phase, and a plateau occurred after 4 h (Fig. 2a). This curve is consistent with a first-order kinetic model (Ono et al. 2003). Similar effects were observed after the addition of fAb42 or faS.",NA,"A typical fibrillar structure was also observed when Ab40 was incubated with fAb40, fAb42, faS, oligo Ab40, oligo Ab42, or oligo aS (Figs. 2c–h)","Interactor: fAbeta42, Interactee: Abeta40",10.1111/j.1471-4159.2012.07847.x,AG00122
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,"When fresh Ab40 was incubated with fAb40 at 37C, the fluorescence increased hyperbolically without a lag phase, and a plateau occurred after 4 h (Fig. 2a). This curve is consistent with a first-order kinetic model (Ono et al. 2003). Similar effects were observed after the addition of fAb42 or faS.",NA,"A typical fibrillar structure was also observed when Ab40 was incubated with fAb40, fAb42, faS, oligo Ab40, oligo Ab42, or oligo aS (Figs. 2c–h).",Interactor: falphaS Interactee: Abeta40,10.1111/j.1471-4159.2012.07847.x,AG00123
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,Yes,The fluorescence increased hyperbolically without a lag phase when fresh Ab42 was incubated with fAb42 at 37C and a binding plateau occurred after 2 h (Fig. 3a).,NA,"Typical fibrillar structures were also observed when Ab42 was incubated with fAb42, fAb40, faS, oligo Ab42, oligo Ab40, or oligo aS (Figs. 3c–h).",Interactor: fAbeta42 Interactee: Abeta42,10.1111/j.1471-4159.2012.07847.x,AG00124
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,The fluorescence increased hyperbolically without a lag phase when fresh Ab42 was incubated with fAb42 at 37C and a binding plateau occurred after 2 h (Fig. 3a). A similar effect was observed after the addition of fAb40 or faS.,NA,"""Typical fibrillar structures were also observed when Ab42 was incubated with fAb42, fAb40, faS, oligo Ab42, oligo Ab40, or oligo aS (Figs. 3c–h).""",Interactor: fAbeta40 Interactee: Abeta42,10.1111/j.1471-4159.2012.07847.x,AG00125
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,The fluorescence increased hyperbolically without a lag phase when fresh Ab42 was incubated with fAb42 at 37C and a binding plateau occurred after 2 h (Fig. 3a). A similar effect was observed after the addition of fAb40 or faS.,NA,"""Typical fibrillar structures were also observed when Ab42 was incubated with fAb42, fAb40, faS, oligo Ab42, oligo Ab40, or oligo aS (Figs. 3c–h).""",Interactor: falphaS Interactee: Abeta42,10.1111/j.1471-4159.2012.07847.x,AG00126
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,"The fluorescence also increased hyperbolically without a lag phase when fresh Ab42 was incubated with oligo Ab42 at 37C and a plateau occurred after 4 h (Fig. 3a). Similar effects were observed after the addition of oligo Ab40 or oligo aS, although their growth rates (oligo Ab40, 24.7 FU/ h; oligo aS, 21.5 FU/h) were lower than that of oligo Ab42",NA,"""Typical fibrillar structures were also observed when Ab42 was incubated with fAb42, fAb40, faS, oligo Ab42, oligo Ab40, or oligo aS (Figs. 3c–h).""",Interactor: oligo Abeta42 Interactee: Abeta42,10.1111/j.1471-4159.2012.07847.x,AG00127
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,"The fluorescence also increased hyperbolically without a lag phase when fresh Ab42 was incubated with oligo Ab42 at 37C and a plateau occurred after 4 h (Fig. 3a). Similar effects were observed after the addition of oligo Ab40 or oligo aS, although their growth rates (oligo Ab40, 24.7 FU/ h; oligo aS, 21.5 FU/h) were lower than that of oligo Ab42",NA,"""Typical fibrillar structures were also observed when Ab42 was incubated with fAb42, fAb40, faS, oligo Ab42, oligo Ab40, or oligo aS (Figs. 3c–h).""",Interactor: oligo alphaS  Interactee: Abeta42,10.1111/j.1471-4159.2012.07847.x,AG00128
Amyloid beta,Alpha-synuclein,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,"The binding curves increased hyperbolically without a lag phase when aS was incubated with faS and a plateau occurred after 6 h (Fig. 4a). A similar effect was observed after the addition of fAb40 or fAb42, although their growth rates were different.",NA,"Typical fibrillar structures were also observed when aS wasincubated with faS, fAb40, fAb42, oligo aS, oligo Ab40, or oligo Ab42",Interactor: fAbeta40 Interactee: alphaS,10.1111/j.1471-4159.2012.07847.x,AG00129
Amyloid beta,Alpha-synuclein,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,"The binding curves increased hyperbolically without a lag phase when aS was incubated with faS and a plateau occurred after 6 h (Fig. 4a). A similar effect was observed after the addition of fAb40 or fAb42, although their growth rates were different.",NA,"We observed non-branched, helical filaments with diameters of 10 nm after the incubation of fresh aS (Fig. 4b). Typical fibrillar structures were also observed when aS was incubated with faS, fAb40, fAb42, oligo aS, oligo Ab40, or oligo Ab42 (Figs. 4c–h).",Interactor: fAbeta42 Interactee: alphaS,10.1111/j.1471-4159.2012.07847.x,AG00130
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,"The aS produced a sigmoidal curve in the absence of any fibrils or oligomers, which was characterized by a lag time of 12 h, a period of increasing ThS binding for 4.5 days, and a plateau after 5 days. The binding curves increased hyperbolically without a lag phase when aS was incubated with faS and a plateau occurred after 6 h",NA,NA,Interactor: falphaS Interactee: alphaS,10.1111/j.1471-4159.2012.07847.x,AG00131
Amyloid beta,Alpha-synuclein,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,"The fluorescence also increased hyperbolically without a lag phase when fresh aS was incubated with oligo aS at 37C and a plateau occurred after 3 days (Fig. 4a). Similar effects were observed after the addition of oligo Ab40 or oligo Ab42, although their growth rates (oligo Ab40, 3.7 FU/h; oligo Ab42, 4.7 FU/h) were significantly lower than oligo aS",NA,"We observed non-branched, helical filaments with diameters of 10 nm after the incubation of fresh aS (Fig. 4b). Typical fibrillar structures were also observed when aS was incubated with faS, fAb40, fAb42, oligo aS, oligo Ab40, or oligo Ab42 (Figs. 4c–h).",Interactor: oligo Abeta40 Interactee: alphaS,10.1111/j.1471-4159.2012.07847.x,AG00132
Amyloid beta,Alpha-synuclein,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,"The fluorescence also increased hyperbolically without a lag phase when fresh aS was incubated with oligo aS at 37C and a plateau occurred after 3 days (Fig. 4a). Similar effects were observed after the addition of oligo Ab40 or oligo Ab42, although their growth rates (oligo Ab40, 3.7 FU/h; oligo Ab42, 4.7 FU/h) were significantly lower than oligo aS",NA,"We observed non-branched, helical filaments with diameters of 10 nm after the incubation of fresh aS (Fig. 4b). Typical fibrillar structures were also observed when aS was incubated with faS, fAb40, fAb42, oligo aS, oligo Ab40, or oligo Ab42 (Figs. 4c–h).",Interactor: oligo Abeta42 Interactee: alphaS,10.1111/j.1471-4159.2012.07847.x,AG00133
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,"The fluorescence also increased hyperbolically without a lag phase when fresh aS was incubated with oligo aS at 37C and a plateau occurred after 3 days (Fig. 4a). Similar effects were observed after the addition of oligo Ab40 or oligo Ab42, although their growth rates (oligo Ab40, 3.7 FU/h; oligo Ab42, 4.7 FU/h) were significantly lower than oligo aS",NA,"We observed non-branched, helical filaments with diameters of 10 nm after the incubation of fresh aS (Fig. 4b). Typical fibrillar structures were also observed when aS was incubated with faS, fAb40, fAb42, oligo aS, oligo Ab40, or oligo Ab42 (Figs. 4c–h).",Interactor:  oligo alphaS  Interactee: alphaS,10.1111/j.1471-4159.2012.07847.x,AG00134
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,Fluorescence also increased hyperbolically without a lag phase when fresh Ab40 was incubated with oligo Ab40 at 37C and a plateau occurred after 48 h (Fig. 2a).,NA,"A typical fibrillar structure was also observed when Ab40 was incubated with fAb40, fAb42, faS, oligo Ab40, oligo Ab42, or oligo aS (Figs. 2c–h).",Interactor: oligo Abeta40 Interactee: Abeta40,10.1111/j.1471-4159.2012.07847.x,AG00135
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,"Fluorescence also increased hyperbolically without a lag phase when fresh Ab40 was incubated with oligo Ab40 at 37C and a plateau occurred after 48 h (Fig. 2a). Similar effects were observed after the addition of oligo Ab42 or oligo aS, although their growth rates (oligo Ab42, 8.1 FU/h; oligo aS, 6.4 FU/h) were significantly lower",NA,"A typical fibrillar structure was also observed when Ab40 was incubated with fAb40, fAb42, faS, oligo Ab40, oligo Ab42, or oligo aS (Figs. 2c–h).",Interactor: oligo Abeta42 Interactee: Abeta40,10.1111/j.1471-4159.2012.07847.x,AG00136
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,"Fluorescence also increased hyperbolically without a lag phase when fresh Ab40 was incubated with oligo Ab40 at 37C and a plateau occurred after 48 h (Fig. 2a). Similar effects were observed after the addition of oligo Ab42 or oligo aS, although their growth rates (oligo Ab42, 8.1 FU/h; oligo aS, 6.4 FU/h) were significantly lower",NA,"A typical fibrillar structure was also observed when Ab40 was incubated with fAb40, fAb42, faS, oligo Ab40, oligo Ab42, or oligo aS (Figs. 2c–h).",Interactor: oligo alphaS  Interactee: Abeta40,10.1111/j.1471-4159.2012.07847.x,AG00137
Transthyretin,Amyloid beta,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,GSNKGAIIGLM,No aggregation,Formation of fibrils by the interactee is inhibited,No,"The tube with Abeta25–35 preincubated with purified TTR showed no visible macroaggregates, although, upon centrifugation, some microaggregates were visible at the bottom of the tube, resulting in a slight decrease of Congo Red absorbance of the tube supernatant (Fig. 8, curve 3) when compared to the OD of the Congo Red control tube not containing Abeta25–35 (Fig. 8, curve 1). However, this concentration of TTR (12.5 μg/mL) prevented the formation of Abeta25–35 large fibrillary macroaggregates (and protected against Abeta25–35 -induced RBCs lysis). In the tube containing Congo Red plus Abeta25–35, the presence of large fibrillar macroaggregates was also detected by the clear-cut decrease of OD in the tube supernatant after centrifugation and detection of residual Congo Red absorbance (Fig. 8, curve 2).","In the absence of TTR, Congo Red stainable aggregates were visible after 4 h. A solution containing 20 μM Abeta25–35 plus Congo Red at a final concentration of 25 μM demonstrated red fibrillar aggregates, visible also by the naked eye from 4- h incubation at room temperature onward. Preincubation of Abeta25–35 with 12.5 μg/mL TTR blocked the formation of visible macroaggregates. These phenomena are clearly demonstrated in macrotiter wells (Fig. 6).",NA,Transthyretin inhibits Aß25-35,10.1016/j.clinbiochem.2005.08.007,AG00138
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Consistent with the previous report,(20) addition of PrP (in the present study at the PrP:Abeta1–42 molar ratio of 1:20) strongly inhibited the reaction, with no increase of ThT fluorescence observed up to at least 24 h of incubation.",NA,NA,Interactee: Aß1-42,10.1021/cn500019c,AG00140
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,"As expected, addition of preformed Abeta1–42 fibrils (fragmented by sonication) as a seed completely eliminated the lag phase observed in the nonseeded reaction, resulting in a rapid increase in ThT fluorescence.",NA,NA,Abeta1-42 fibrils as interactor,10.1021/cn500019c,AG00141
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"However, when seeds were first preincubated in the presence of PrP (at the PrP to fibrillar Abeta molar ratio of 1:2), their ability to initiate fibrillization of Abeta1–42 was greatly diminished, as indicated by much slower increase in ThT fluorescence (Figure 1).; Indeed, AFM analysis of the products of seeded reactions both in the absence and presence of PrP indicates the presence of fibrillar aggregates, even though fibrils formed in the presence of PrP appear to be less abundant, shorter and often bundled into larger aggregates",NA,NA,Abeta1-42 fibrils were first preincubated in the presence of PrP and then Abeta1-42 was added,10.1021/cn500019c,AG00142
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,Abeta40 inhibits Abeta42 aggregation in vitro,"When Aß40 was mixed with Aß42 (Aß40:Aß42 ratio; 0.5:1 and 1:1), Aß40 inhibited the formation of HMW Aß42 aggregates, and the vast majority of Aß42 remained as LMWspecies (indicated by4at the bottom of the blot).",NA,Interactor: Abeta40. Interactee: Abeta42,10.1523/JNEUROSCI.4849-06.2007,AG00143
Beta-parvalbumin,Alpha-synuclein,MAFAGILNDADITAALAACKAEGSFDHKAFFTKVGLAAKSPADIKKVFEIIDQDKSDFVEEDELKLFLQNFSAGARALSDAETKVFLKAGDSDGDGKIGVDEFGAMIKA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No effect,No information,No information,the presence of holo-PV had no effect on alphaS amyloid formation (Fig. 2a),NA,NA,The results depend on the presence of calcium ions (Ca). Here beta-parvalbumin (PV) in the presence of Ca - holo-PV.,10.1038/s41598-018-23850-0,AG00144
Beta-parvalbumin,Alpha-synuclein,MAFAGILNDADITAALAACKAEGSFDHKAFFTKVGLAAKSPADIKKVFEIIDQDKSDFVEEDELKLFLQNFSAGARALSDAETKVFLKAGDSDGDGKIGVDEFGAMIKA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No,"We found that whereas the presence of holo-PV had no effect on alphaS amyloid formation (Fig. 2a), mixing of apo-PV and alphaS resulted in a ThT fluorescence curve exactly like the apo-PV alone one. Thus, the increased ThT emission expected upon alphaS amyloid formation was lacking, implying that alphaS amyloid formation was blocked (Fig. 2b).","We found that whereas the presence of holo-PV had no effect on alphaS amyloid formation (Fig. 2a), mixing of apo-PV and alphaS resulted in a ThT fluorescence curve exactly like the apo-PV alone one. Thus, the increased ThT emission expected upon alphaS amyloid formation was lacking, implying that alphaS amyloid formation was blocked (Fig. 2b).","AFM analysis of the resulting amyloid fibers in apo-PV/alphaS mixtures demonstrated that amyloid fiber dimensions are homogeneous and match those of apo-PV (Fig. 2c,d; Figure S2B).","The results depend on the presence of calcium ions (Ca). Here beta-parvalbumin (PV) in the absence of Ca - apo-PV.; Due to ThT plots, we could say that the kinetic of aggregation after interaction is faster. However, based on the expected signal for the alphaS and apo-PV mixture, the authors claimed that , alphaS amyloid formation was blocked.",10.1038/s41598-018-23850-0,AG00145
TDP-43,Alpha-synuclein,MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRTSQAHRVITKTKATCRGSQTRPSVLEITLIVALILVQQLVGDQHPMQGRAVVLMEALAQAWILSLLAGECRQWGCGWLV,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",Yes,NA,"As expected, the dot blot analysis of the sample using aS and TDP-43 antibodies showed presence of bothaS and TDP-43 PrLD confirming that aS co-aggregates with TDP-43 PrLD during fibrils formation (Figure S2(a)).","As expected, the dot blot analysis of the sample using aS and TDP-43 antibodies showed presence of bothaS and TDP-43 PrLD confirming that aS co-aggregates with TDP-43 PrLD during fibrils formation (Figure S2(a)).",NA,10.1016/j.jmb.2021.166953,AG00146
Alpha-synuclein,TDP-43,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRTSQAHRVITKTKATCRGSQTRPSVLEITLIVALILVQQLVGDQHPMQGRAVVLMEALAQAWILSLLAGECRQWGCGWLV,Faster aggregation,"Yes, direct evidence.",Yes,NA,"As expected, the dot blot analysis of the sample using aS and TDP-43 antibodies showed presence of both aS and TDP-43 PrLD confirming that aS co-aggregates with TDP-43 PrLD during fibrils formation (Figure S2(a)).","As expected, the dot blot analysis of the sample using aS and TDP-43 antibodies showed presence of both aS and TDP-43 PrLD confirming that aS co-aggregates with TDP-43 PrLD during fibrils formation (Figure S2(a)).",NA,10.1016/j.jmb.2021.166953,AG00147
Tau,Alpha-synuclein,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No information,"Our combined analysis of alpha-synuclein aggregation in the presence and absence of tau revealed that monomeric forms of tau accelerate the formation of alpha-synuclein filaments. alpha-Synuclein monomers were also able to induce tau aggregation (Figure 4b and Figure S6) at the same experimental conditions. Interestingly, filamentous aggregates of alpha-synuclein seeded tau aggregation more effectively than alpha- synuclein monomers (Figure 4b,c). These results indicate that the composition of protein aggregates formed from the protein mixture depends on the molar ratio of the two proteins","Two-dimensional 1 H/15N heteronuclear single-quantum coherence (HSQC) NMR spectra were acquired for 15N-labeled alpha-synuclein in the absence and presence of unlabeled tau (Figure 7a and Figure S11). In the overlaid HSQC NMR spectra, notable changes in the chemical shift were observed for numerous residues upon additions of tau monomers. The chemical shift perturbations are more pronounced in the C-terminal region of alpha-synuclein (Figure 7b). The Nterminal regions (15−63) are also slightly affected, while the nonamyloid-beta component (NAC) region (65−95) remains nearly unchanged. The titration NMR experiments indicate that tau affects both N-terminal as well as C-terminal regions of alpha-synuclein. The addition of tau also causes the NMR signal to decrease in intensity for the residues undergoing chemical shift changes (Figure S12). However, the decreases in the NMR signal intensity is observed only for the C-terminal region (110−140) of alpha-synuclein (Figure S12). These NMR results suggest that tau may selectively interact with the Cterminal region on intermediate time scales (millisecond to microsecond), while the N-terminal region is not directly involved in the interaction with tau",NA,"Alpha-Synuclein monomers as well as fibrillar forms of alpha-synuclein can also induce tau aggregation. Finally, our combined analyses of synergistic aggregation of the two proteins can be extended to understand synergistic interactions between other pathological proteins including TAR-DNA-binding protein 43 (TDP-43) and alpha-synuclein.",10.1021/acs.biochem.9b00215,AG00148
PSMalpha3,PSMalpha1,MEFVAKLFKFFKDLLGKFLGNN,MGIIAGIIKVIKSLIEQFTGK,Faster aggregation,Yes; implied by kinetics.,No information,It can be seen that compared to the non-seeded aggregation seeds of all the other aggregating PSM peptides PSMa3 and PSMb1–2 accelerated the aggregation process (Figure 4 and Figure 4—figure supplement 1).,NA,NA,PSMalpha3 as interactor and PSMalpha1 as interactee were used,10.7554/elife.59776,AG00149
PSMbeta1,PSMalpha1,MEGLFNAIKDTVTAAINNDGAKLGTSIVSIVENGVGLLGKLFGF,MGIIAGIIKVIKSLIEQFTGK,Faster aggregation,Yes; implied by kinetics.,No information,It can be seen that compared to the non-seeded aggregation seeds of all the other aggregating PSM peptides PSMa3 and PSMb1–2 accelerated the aggregation process (Figure 4 and Figure 4—figure supplement 1).,NA,NA,PSMbeta1 as interactor and PSMalpha1 as interactee were used,10.7554/elife.59776,AG00150
PSMbeta2,PSMalpha1,MTGLAEAIANTVQAAQQHDSVKLGTSIVDIVANGVGLLGKLFGF,MGIIAGIIKVIKSLIEQFTGK,Faster aggregation,Yes; implied by kinetics.,No information,It can be seen that compared to the non-seeded aggregation seeds of all the other aggregating PSM peptides PSMa3 and PSMb1–2 accelerated the aggregation process (Figure 4 and Figure 4—figure supplement 1).,NA,NA,PSMbeta2 as interactor and PSMalpha1 as interactee were used,10.7554/elife.59776,AG00151
PSMalpha1,PSMbeta1,MGIIAGIIKVIKSLIEQFTGK,MEGLFNAIKDTVTAAINNDGAKLGTSIVSIVENGVGLLGKLFGF,Faster aggregation,Yes; implied by kinetics.,No information,"Similar to PSMalpha1, PSMbeta1 aggregation is also accelerated by the presence of all the other types of preformed fibril seeds, namely PSMalpha1, PSMalpha3, and PSMbeta2 seeds (Figure 4e).",NA,NA,PSMalpha1 as interactor and PSMbeta1 as interactee were used,10.7554/elife.59776,AG00152
PSMalpha3,PSMbeta1,MEFVAKLFKFFKDLLGKFLGNN,MEGLFNAIKDTVTAAINNDGAKLGTSIVSIVENGVGLLGKLFGF,Faster aggregation,Yes; implied by kinetics.,No information,"Similar to PSMalpha1, PSMbeta1 aggregation is also accelerated by the presence of all the other types of preformed fibril seeds, namely PSMalpha1, PSMalpha3, and PSMbeta2 seeds (Figure 4e).",NA,NA,PSMalpha3 as interactor and PSMbeta1 as interactee were used,10.7554/elife.59776,AG00153
PSMbeta2,PSMbeta1,MTGLAEAIANTVQAAQQHDSVKLGTSIVDIVANGVGLLGKLFGF,MEGLFNAIKDTVTAAINNDGAKLGTSIVSIVENGVGLLGKLFGF,Faster aggregation,Yes; implied by kinetics.,No information,"Similar to PSMalpha1, PSMbeta1 aggregation is also accelerated by the presence of all the other types of preformed fibril seeds, namely PSMalpha1, PSMalpha3, and PSMbeta2 seeds (Figure 4e).",NA,NA,PSMbeta2 as interactor and PSMbeta1 as interactee were used,10.7554/elife.59776,AG00154
PSMalpha1,PSMalpha3,MGIIAGIIKVIKSLIEQFTGK,MEFVAKLFKFFKDLLGKFLGNN,Faster aggregation,Yes; implied by kinetics.,No information,NA,Unlike PSMalpha1 and PSMbeta1 the fast aggregating PSMalpha3 is cross-seeded by PSMalpha1 and PSMbeta2 but not PSMbeta1 (Figure 4c).,NA,PSMalpha1 as interactor and PSMalpha3 as interactee were used,10.7554/elife.59776,AG00155
PSMbeta2,PSMalpha3,MTGLAEAIANTVQAAQQHDSVKLGTSIVDIVANGVGLLGKLFGF,MEFVAKLFKFFKDLLGKFLGNN,Faster aggregation,Yes; implied by kinetics.,No information,NA,Unlike PSMalpha1 and PSMbeta1 the fast aggregating PSMalpha3 is cross-seeded by PSMalpha1 and PSMbeta2 but not PSMbeta1 (Figure 4c).,NA,PSMbeta2 as interactor and PSMalpha3 as interactee were used,10.7554/elife.59776,AG00156
PSMbeta1,PSMalpha3,MEGLFNAIKDTVTAAINNDGAKLGTSIVSIVENGVGLLGKLFGF,MEFVAKLFKFFKDLLGKFLGNN,No aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Unlike PSMalpha1 and PSMbeta1 the fast aggregating PSMalpha3 is cross-seeded by PSMalpha1 and PSMbeta2 but not PSMbeta1 (Figure 4c).,NA,PSMbeta1 as interactor and PSMalpha3 as interactee were used,10.7554/elife.59776,AG00157
PSMalpha1,PSMbeta2,MGIIAGIIKVIKSLIEQFTGK,MTGLAEAIANTVQAAQQHDSVKLGTSIVDIVANGVGLLGKLFGF,Faster aggregation,Yes; implied by kinetics.,No information,Similar to PSMalpha3 the aggregation of PSMbeta2 is accelerated by only PSMalpha1 and PSMbeta1 whereas PSMalpha3 seeded interestingly enhanced the lag phase of PSMbeta2 dramatically (Figure 4f).,PSMbeta2 that aggregate through a nucleation-elongation dominated aggregation mechanism can be seeded with some (PSMalpha1 and PSMbeta1) but not all of the peptides (PSMalpha3) which aggregate through a mechanism dominated by secondary nucleation.,NA,PSMalpha1 as interactor and PSMbeta2 as interactee were used,10.7554/elife.59776,AG00158
PSMbeta1,PSMbeta2,MEGLFNAIKDTVTAAINNDGAKLGTSIVSIVENGVGLLGKLFGF,MTGLAEAIANTVQAAQQHDSVKLGTSIVDIVANGVGLLGKLFGF,Faster aggregation,Yes; implied by kinetics.,No information,Similar to PSMalpha3 the aggregation of PSMbeta2 is accelerated by only PSMalpha1 and PSMbeta1 whereas PSMalpha3 seeded interestingly enhanced the lag phase of PSMbeta2 dramatically (Figure 4f).,PSMbeta2 that aggregate through a nucleation-elongation dominated aggregation mechanism can be seeded with some (PSMalpha1 and PSMbeta1) but not all of the peptides (PSMalpha3) which aggregate through a mechanism dominated by secondary nucleation.,NA,PSMbeta1 as interactor and PSMbeta2 as interactee were used,10.7554/elife.59776,AG00159
PSMalpha3,PSMbeta2,MEFVAKLFKFFKDLLGKFLGNN,MTGLAEAIANTVQAAQQHDSVKLGTSIVDIVANGVGLLGKLFGF,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,Similar to PSMalpha3 the aggregation of PSMbeta2 is accelerated by only PSMalpha1 and PSMbeta1 whereas PSMalpha3 seeded interestingly enhanced the lag phase of PSMbeta2 dramatically (Figure 4f).,PSMbeta2 that aggregate through a nucleation-elongation dominated aggregation mechanism can be seeded with some (PSMalpha1 and PSMbeta1) but not all of the peptides (PSMalpha3) which aggregate through a mechanism dominated by secondary nucleation.,NA,PSMalpha3 as interactor and PSMbeta2 as interactee were used,10.7554/elife.59776,AG00160
PSMalpha1,PSMalpha2,MGIIAGIIKVIKSLIEQFTGK,MGIIAGIIKFIKGLIEKFTGK,Faster aggregation,Yes; implied by kinetics.,No information,Both PSMalpha2 and PSMalpha4 aggregation could be induced in the presence of PSMalpha1 and PSMbeta1 seeds but not by PSMalpha3 and PSMbeta2 seeds (Figure 4b and d).,NA,NA,PSMalpha1 as interactor and PSMalpha2 as interactee were used,10.7554/elife.59776,AG00161
PSMbeta1,PSMalpha2,MEGLFNAIKDTVTAAINNDGAKLGTSIVSIVENGVGLLGKLFGF,MGIIAGIIKFIKGLIEKFTGK,Faster aggregation,Yes; implied by kinetics.,No information,Both PSMalpha2 and PSMalpha4 aggregation could be induced in the presence of PSMalpha1 and PSMbeta1 seeds but not by PSMalpha3 and PSMbeta2 seeds (Figure 4b and d).,NA,NA,PSMbeta1 as interactor and PSMalpha2 as interactee were used,10.7554/elife.59776,AG00162
PSMalpha3,PSMalpha2,MEFVAKLFKFFKDLLGKFLGNN,MGIIAGIIKFIKGLIEKFTGK,No aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,PSMalpha3 as interactor and PSMalpha2 as interactee were used,10.7554/elife.59776,AG00163
PSMalpha1,PSMalpha4,MGIIAGIIKVIKSLIEQFTGK,MAIVGTIIKIIKAIIDIFAK,Faster aggregation,Yes; implied by kinetics.,No information,Both PSMalpha2 and PSMalpha4 aggregation could be induced in the presence of PSMalpha1 and PSMbeta1 seeds but not by PSMalpha3 and PSMbeta2 seeds (Figure 4b and d).,NA,NA,PSMalpha1 as interactor and PSMalpha4 as interactee were used,10.7554/elife.59776,AG00164
PSMbeta1,PSMalpha4,MEGLFNAIKDTVTAAINNDGAKLGTSIVSIVENGVGLLGKLFGF,MAIVGTIIKIIKAIIDIFAK,Faster aggregation,Yes; implied by kinetics.,No information,Both PSMalpha2 and PSMalpha4 aggregation could be induced in the presence of PSMalpha1 and PSMbeta1 seeds but not by PSMalpha3 and PSMbeta2 seeds (Figure 4b and d).,NA,NA,PSMbeta1 as interactor and PSMalpha4 as interactee were used,10.7554/elife.59776,AG00165
PSMalpha3,PSMalpha4,MEFVAKLFKFFKDLLGKFLGNN,MAIVGTIIKIIKAIIDIFAK,No aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,PSMalpha3 as interactor and PSMalpha4 as interactee were used,10.7554/elife.59776,AG00166
PSMalpha1,Delta-toxin,MGIIAGIIKVIKSLIEQFTGK,MAQDIISTIGDLVKWIIDTVNKFTKK,Faster aggregation,Yes; implied by kinetics.,No information,For delta-toxin aggregation could be induced by the presence of PSMalpha1 and PSMbeta2 seeds but not PSMalpha3 seeds (Figure 4g).,NA,NA,NA,10.7554/elife.59776,AG00167
PSMbeta2,Delta-toxin,MTGLAEAIANTVQAAQQHDSVKLGTSIVDIVANGVGLLGKLFGF,MAQDIISTIGDLVKWIIDTVNKFTKK,Faster aggregation,Yes; implied by kinetics.,No information,For delta-toxin aggregation could be induced by the presence of PSMalpha1 and PSMbeta2 seeds but not PSMalpha3 seeds (Figure 4g).,NA,NA,NA,10.7554/elife.59776,AG00168
PSMalpha3,Delta-toxin,MEFVAKLFKFFKDLLGKFLGNN,MAQDIISTIGDLVKWIIDTVNKFTKK,No aggregation,Formation of fibrils by the interactee is inhibited,No,For delta-toxin aggregation could be induced by the presence of PSMalpha1 and PSMbeta2 seeds but not PSMalpha3 seeds (Figure 4g).,NA,NA,NA,10.7554/elife.59776,AG00169
PSMalpha1,PSMalpha1,MGIIAGIIKVIKSLIEQFTGK,MGIIAGIIKVIKSLIEQFTGK,Faster aggregation,Yes; implied by kinetics.,No,"Aggregation of PSMalpha1 in the presence and absence of low concentrations of preformed seeds (monomers: 0.5 mg/mL, seeds: 0–250 nM). Significant effects on the rate of aggregation were observed. Indeed a decrease in the lag phase was observed with increasing seed concentration for PSMalpha1, PSMalpha3, and PSMbeta1 (Figure 1d–f and h),","Aggregation of PSMalpha1 in the presence and absence of low concentrations of preformed seeds (monomers: 0.5 mg/mL, seeds: 0–250 nM). Significant effects on the rate of aggregation were observed. Indeed a decrease in the lag phase was observed with increasing seed concentration for PSMalpha1, PSMalpha3, and PSMbeta1 (Figure 1d–f and h),",NA,NA,10.7554/elife.59776,AG00170
PSMalpha3,PSMalpha3,MEFVAKLFKFFKDLLGKFLGNN,MEFVAKLFKFFKDLLGKFLGNN,Faster aggregation,Yes; implied by kinetics.,No,"Aggregation of PSMalpha3 in the presence and absence of low concentrations of preformed seeds (monomers: 0.4 mg/mL, seeds: 0–250 nM). Significant effects on the rate of aggregation were observed. Indeed a decrease in the lag phase was observed with increasing seed concentration for PSMalpha1, PSMalpha3, and PSMbeta1 (Figure 1d–f and h),","Aggregation of PSMalpha3 in the presence and absence of low concentrations of preformed seeds (monomers: 0.4 mg/mL, seeds: 0–250 nM). Significant effects on the rate of aggregation were observed. Indeed a decrease in the lag phase was observed with increasing seed concentration for PSMalpha1, PSMalpha3, and PSMbeta1 (Figure 1d–f and h),",NA,NA,10.7554/elife.59776,AG00171
PSMbeta1,PSMbeta1,MEGLFNAIKDTVTAAINNDGAKLGTSIVSIVENGVGLLGKLFGF,MEGLFNAIKDTVTAAINNDGAKLGTSIVSIVENGVGLLGKLFGF,Faster aggregation,Yes; implied by kinetics.,No,"Aggregation of PSMbeta1 in the presence and absence of low concentration of preformed seeds (monomers: 0.025 mg/mL, seeds: 0–100 nM). Significant effects on the rate of aggregation were observed. Indeed a decrease in the lag phase was observed with increasing seed concentration for PSMalpha1, PSMalpha3, and PSMbeta1 (Figure 1d–f and h),","Aggregation of PSMbeta1 in the presence and absence of low concentration of preformed seeds (monomers: 0.025 mg/mL, seeds: 0–100 nM). Significant effects on the rate of aggregation were observed. Indeed a decrease in the lag phase was observed with increasing seed concentration for PSMalpha1, PSMalpha3, and PSMbeta1 (Figure 1d–f and h),",NA,NA,10.7554/elife.59776,AG00172
PSMbeta2,PSMbeta2,MTGLAEAIANTVQAAQQHDSVKLGTSIVDIVANGVGLLGKLFGF,MTGLAEAIANTVQAAQQHDSVKLGTSIVDIVANGVGLLGKLFGF,No effect,No,No,"Aggregation of PSMbeta2 in the presence and absence of low concentration of preformed seeds (monomers: 0.05 mg/mL, seeds: 0–100 nM). No significant effects on the rate of aggregation are evident. The aggregation kinetics of PSMbeta2 was not affected by the presence of low amounts of seeds confirming the lack of self-replication processes in the form of surface catalyzed secondary nucleation (Figure 1h).","Aggregation of PSMbeta2 in the presence and absence of low concentration of preformed seeds (monomers: 0.05 mg/mL, seeds: 0–100 nM). No significant effects on the rate of aggregation are evident. The aggregation kinetics of PSMbeta2 was not affected by the presence of low amounts of seeds confirming the lack of self-replication processes in the form of surface catalyzed secondary nucleation (Figure 1h).",NA,NA,10.7554/elife.59776,AG00173
Delta-toxin,PSMalpha2,MAQDIISTIGDLVKWIIDTVNKFTKK,MGIIAGIIKFIKGLIEKFTGK,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Far UV-CD spectra of PSMalpha2 and delta-toxin after 7 days of incubation at 37°C display alpha-helical character consistent with the lack of aggregation. However, we observe only one minimum at around 208 nm of delta-toxin in comparison to monomeric delta-toxin, which possess two minima at around 208 and 224 nm (Figure 2—figure supplement 1a and b). This is consistent with the lack of aggregation seen for these peptides by ThT fluorescence.","Far UV-CD spectra of PSMalpha2 and delta-toxin after 7 days of incubation at 37°C display alpha-helical character consistent with the lack of aggregation. However, we observe only one minimum at around 208 nm of delta-toxin in comparison to monomeric delta-toxin, which possess two minima at around 208 and 224 nm (Figure 2—figure supplement 1a and b). This is consistent with the lack of aggregation seen for these peptides by ThT fluorescence.",NA,NA,10.7554/elife.59776,AG00174
PSMbeta2,PSMalpha2,MTGLAEAIANTVQAAQQHDSVKLGTSIVDIVANGVGLLGKLFGF,MGIIAGIIKFIKGLIEKFTGK,No aggregation,No,No,Both PSMalpha2 and PSMalpha4 aggregation could be induced in the presence of PSMalpha1 and PSMbeta1 seeds but not by PSMalpha3 and PSMbeta2 seeds (Figure 4b and d).,Both PSMalpha2 and PSMalpha4 aggregation could be induced in the presence of PSMalpha1 and PSMbeta1 seeds but not by PSMalpha3 and PSMbeta2 seeds (Figure 4b and d).,NA,NA,10.7554/elife.59776,AG00175
PSMbeta2,PSMalpha4,MTGLAEAIANTVQAAQQHDSVKLGTSIVDIVANGVGLLGKLFGF,MAIVGTIIKIIKAIIDIFAK,No aggregation,No,No,Both PSMalpha2 and PSMalpha4 aggregation could be induced in the presence of PSMalpha1 and PSMbeta1 seeds but not by PSMalpha3 and PSMbeta2 seeds (Figure 4b and d).,Both PSMalpha2 and PSMalpha4 aggregation could be induced in the presence of PSMalpha1 and PSMbeta1 seeds but not by PSMalpha3 and PSMbeta2 seeds (Figure 4b and d).,NA,NA,10.7554/elife.59776,AG00176
PSMbeta1,Delta-toxin,MEGLFNAIKDTVTAAINNDGAKLGTSIVSIVENGVGLLGKLFGF,MAQDIISTIGDLVKWIIDTVNKFTKK,Faster aggregation,Yes; implied by kinetics.,No information,A slight increase in ThT fluorescence is also observed in the presence of PSMbeta1 seeds but this is both very slow and a very small increase as compared to the increase seen in the presence of PSMalpha1 and PSMbeta2 seeds.,A slight increase in ThT fluorescence is also observed in the presence of PSMbeta1 seeds but this is both very slow and a very small increase as compared to the increase seen in the presence of PSMalpha1 and PSMbeta2 seeds.,NA,NA,10.7554/elife.59776,AG00177
Alpha-synuclein,IAPP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1007/978-1-4939-7816-8_6,AG00178
IAPP,Alpha-synuclein,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1007/978-1-4939-7816-8_6,AG00179
Alpha-synuclein,Pmel17,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,PTAEAPNTTAGQVPTTEVVGTTPGQAPTAEPSGTTSVQVPTTEVISTAPVQMPTAESTGMTPEKVPVSEVMGTTLAEMSTPEATGMTPAEVSIVVLSGTTAAQVTTTEWVETTARELPIPEPEGPDASSI,Faster aggregation,"Yes, direct evidence.",Yes,RPT aggregation was stimulated by the presence of alpha-syn seeds (green),"Further analysis found a similar half-pitch fibril length, with averages ranging from 150 nm to 160 nm (Fig. 2E). It is evident that alpha-syn fibrils can nucleate RPT aggregation, altering the ultrastructural features of the subsequent fibrils which can be faithfully propagated over multiple generations.","Raman microspectroscopy revealed subtle changes in the amideIII band shape akin to alpha-syn (Fig. 2 F, Left), while the overall beta-sheet content remained comparable, as indicated by the amideI band (Fig. 2 F, Right). Additionally, limited protease digestion with cathepsin L showed enhanced protection of RPT regions in cross-seeded vs. self-seeded fibrils, with reduced relative protease accessibility observed between residues 329 and 338 and between residues 369 and 382 (Fig. 2G). Together, the spectroscopic and biochemical data support that cross-seeded fibrils exhibit altered structure from those of unseeded/self-seeded RPT fibrils.",NA,10.1073/pnas.2009702117,AG00181
Pmel17,Alpha-synuclein,PTAEAPNTTAGQVPTTEVVGTTPGQAPTAEPSGTTSVQVPTTEVISTAPVQMPTAESTGMTPEKVPVSEVMGTTLAEMSTPEATGMTPAEVSIVVLSGTTAAQVTTTEWVETTARELPIPEPEGPDASSI,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No effect,No,No,"The cross-seeding effect was unidirectional, as RPT fibrils did not influence alpha-syn aggregation (Fig. 2C teal blue)",NA,NA,NA,10.1073/pnas.2009702117,AG00182
Pmel17,Pmel17,PTAEAPNTTAGQVPTTEVVGTTPGQAPTAEPSGTTSVQVPTTEVISTAPVQMPTAESTGMTPEKVPVSEVMGTTLAEMSTPEATGMTPAEVSIVVLSGTTAAQVTTTEWVETTARELPIPEPEGPDASSI,PTAEAPNTTAGQVPTTEVVGTTPGQAPTAEPSGTTSVQVPTTEVISTAPVQMPTAESTGMTPEKVPVSEVMGTTLAEMSTPEATGMTPAEVSIVVLSGTTAAQVTTTEWVETTARELPIPEPEGPDASSI,Faster aggregation,Yes; implied by kinetics.,No,"RPT aggregation was stimulated by the presence of alpha-syn seeds, although not as efficiently as self-seeded RPT (blue curve)",NA,NA,NA,10.1073/pnas.2009702117,AG00183
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,"Aggregation of 30 μM RPT (black in B) and alpha-syn (black in C) alone, or with 3 μM preformed alpha-syn (green in B; purple in C)","Aggregation of 30 μM RPT (black in B) and alpha-syn (black in C) alone, or with 3 μM preformed alpha-syn (green in B; purple in C)",NA,NA,10.1073/pnas.2009702117,AG00184
Cystatin C,Amyloid beta,MAGPLRAPLLLLAILAVALAVSPAAGSSPGKPPRLVGGPMDASVEEEGVRRALDFAVGEYNKASNDMYHSRALQVVRARKQIVAGVNYFLDVELGRTTCTKTQPNLDNCPFHDQPHLKRKAFCSFQIYAVPWQGTMTLSKSTCQDA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,"Interactor: mCys - monomers, dCys - dimers",10.1074/jbc.M117.786558,AG00185
Cystatin C,Amyloid beta,MAGPLRAPLLLLAILAVALAVSPAAGSSPGKPPRLVGGPMDASVEEEGVRRALDFAVGEYNKASNDMYHSRALQVVRARKQIVAGVNYFLDVELGRTTCTKTQPNLDNCPFHDQPHLKRKAFCSFQIYAVPWQGTMTLSKSTCQDA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,Interactor: oCys - oligomers,10.1074/jbc.M117.786558,AG00186
S100A9,Amyloid beta,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,VHHQKLVFFAEDV,Faster aggregation,"Yes, direct evidence.",No,NA,"We believe that the strong hydrophobic interaction between the CHC of Ab12–24 peptides towards S100A9, as well as the hydrogen bonds formed between the two ends of Ab12–24 with the residues exposed to the solvent from S100A9, play an important role in the induction of amyloid oligomerization. I",NA,"Interactor: S100A9 (MRP14), Interactee:Aß12–24",10.1039/c3ra43665a,AG00187
IAPP,Amyloid beta,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,Yes,"The lag time of the mixture was comparable to the IAPP alone and significantly reduced compared to Abeta42 alone, consistent with previous experimental reports that mixing of Abeta and IAPP retarded the rate of IAPP assembly while accelerated the fibril formation by Abeta. 32,33","In vitro studies of Abeta-IAPP cross- and self-association. Seven different concentrations from 1 to 5 μM were studied with each kinetic measurement performed at least in triplicate. The concentration dependence of (A) the aggregation lag time for Abeta-IAPP co-aggregation (blue), and the self-aggregation of Abeta (black) and IAPP (red).",NA,NA,10.1021/acschemneuro.7b00396,AG00188
Amyloid beta,IAPP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,Yes,"The lag time of the mixture was comparable to the IAPP alone and significantly reduced compared to Abeta42 alone, consistent with previous experimental reports that mixing of Abeta and IAPP retarded the rate of IAPP assembly while accelerated the fibril formation by Abeta. 32,33","In vitro studies of Abeta-IAPP cross- and self-association. Seven different concentrations from 1 to 5 μM were studied with each kinetic measurement performed at least in triplicate. The concentration dependence of (A) the aggregation lag time for Abeta-IAPP co-aggregation (blue), and the self-aggregation of Abeta (black) and IAPP (red).",NA,NA,10.1021/acschemneuro.7b00396,AG00189
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,Yes,NA,NA,NA,NA,10.1074/jbc.M803159200,AG00190
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1074/jbc.M803159200,AG00191
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,Yes,NA,NA,NA,NA,10.1074/jbc.M803159200,AG00192
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,Yes; implied by kinetics.,Yes,"We found that even the lowest concentration of A
42PF (1 M) was sufficient to accelerate the fibrillogenesis of monomeric A
42 (Fig. 6A), whereas no such effect was observed (for any molar ratio) when A
42PF were added to monomeric A
40 under identical conditions (Fig. 6B).",NA,NA,NA,10.1074/jbc.M803159200,AG00193
Amyloid beta,S100A9,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,Faster aggregation,Yes; implied by kinetics.,No,The highest ThT fluorescence signal was observed in the S100A9-Abeta(1–40) solution reflecting the development of large quantities of mature fibrils (Fig. 4k).,NA,"Similarly, S100A9 and Abeta(1–40) can also promote each other’s amyloid assembly into joint large supercomplexes. It is important to note, that Abeta(1–40) alone, incubated even at 100 μM concentration for 24 h and up to 7 days, formed mature fibrils but they were still less thick, with ca. 6 nm height in AFM cross-sections (supplemental files 5j, k), and remained smooth compared to the coated fibrillar bundles of S100A9-Abeta(1–40) discussed above",Amyloid beta(1-40),10.1007/s00401-013-1208-4,AG00197
S100A9,Amyloid beta,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,The highest ThT fluorescence signal was observed in the S100A9-Abeta(1–40) solution reflecting the development of large quantities of mature fibrils (Fig. 4k).,NA,"Similarly, S100A9 and Abeta(1–40) can also promote each other’s amyloid assembly into joint large supercomplexes. It is important to note, that Abeta(1–40) alone, incubated even at 100 μM concentration for 24 h and up to 7 days, formed mature fibrils but they were still less thick, with ca. 6 nm height in AFM cross-sections (supplemental files 5j, k), and remained smooth compared to the coated fibrillar bundles of S100A9-Abeta(1–40) discussed above",Amyloid beta(1-40),10.1007/s00401-013-1208-4,AG00198
Amyloid beta,IAPP,GSNKGAIIGLM,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,"Yes, direct evidence.",No,"When Abeta25–35 monomers were mixed with hIAPP fibrils, there was no obvious increase in fluorescence intensity","When hIAPP incubated with Abeta25–35 at a ratio of 1:1, a series of new peaks of hetero-oligomers formed by hIAPP and Abeta25–35 appeared","there was no significant difference in the fiber morphology between hIAPP alone and the mixtures, but more fibrils could be observed in the mixtures","Interactor: Aß25-35 monomers, Interactee: hIAPP fibrils",10.1002/jms.4643,AG00199
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No,hIAPP fibrils significantly shortened the lag phase and accelerated the aggregation of hIAPP monomers,NA,"there was no significant difference in the fiber morphology between hIAPP alone and the mixtures, but more fibrils could be observed in the mixtures","Interactor: hIAPP fibrils. Interactee: hIAPP monomers, hIAPP seeds also accelerate hIAPP monomers",10.1002/jms.4643,AG00200
IAPP,Amyloid beta,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,GSNKGAIIGLM,No effect,No,No,"the influence of hIAPP seeds on the fibrillation of Abeta25–35 was studied. Similar to the kinetic data of hIAPP fibrils, hIAPP seeds only accelerated the aggregation of hIAPP monomers rather than Abeta25–35 monomers.",NA,"there was no significant difference in the fiber morphology between hIAPP alone and the mixtures, but more fibrils could be observed in the mixtures",Interactor: hIAPP seeds. Interactee: Aß25-35 monomers,10.1002/jms.4643,AG00201
Amyloid beta,IAPP,GSNKGAIIGLM,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No,NA,"For the mixtures, all the fibrillation processes of the first stage were very similar to that observed of hIAPP alone at the same concentration.","For the mixtures, all the fibrillation processes of the first stage were very similar to that observed of hIAPP alone at the same concentration.","Interactor: Aß25-35, Interactee: hIAPP",10.1002/jms.4643,AG00202
Amyloid beta,Alpha-synuclein,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTK EQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDP DNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No information,"Ab1–42 strongly promoted the formation of presumed hSYN oligomers and high molecular weight hSYN polymers (Fig. 6d), consistent with previous observations (36). This effect was observed with both aged (putatively aggregated) and freshly solubilized Ab1–42. However, because Ab1–42 aggregates rapidly in aqueous solutions, we cannot be certain that the effect was independent of the aggregation state of Ab1–42.",NA,NA,Interactor: Amyloid beta1-42,10.1073/pnas.211412398,AG00203
Amyloid beta,Alpha-synuclein,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No effect,No,No information,". Interestingly, the less fibrillogenic Ab1–40 did not affect hSYN aggregation in vitro (Fig. 6d).",NA,NA,Interactor: Amyloid beta 1-42,10.1073/pnas.211412398,AG00204
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No information,"In contrast to the prominent effects of Ab on SYN accumulation, hSYN expression did not significantly alter the extracellular deposition of Ab into plaques or the development of plaque-associated neuritic dystrophy",NA,NA,Interactee: Amyloid beta 1-42,10.1073/pnas.211412398,AG00205
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No information,No information,"In contrast to the prominent effects of Ab on SYN accumulation, hSYN expression did not significantly alter the extracellular deposition of Ab into plaques or the development of plaque-associated neuritic dystrophy",NA,NA,Interactee: Amyloid beta 1-40,10.1073/pnas.211412398,AG00206
Rnq1,Sup35,MDTDKLISEAESHFSQGNHAEAVAKLTSAAQSNPNDEQMSTIESLIQKIAGYVMDNRSGGSDASQDRAAGGGSSFMNTLMADSKGSSQTQLGKLALLATVMTHSSNKGSSNRGFDVGTVMSMLSGSGGGSQSMGASGLAALASQFFKSGNNSQGQGQGQGQGQGQGQGQGQGSFTALASLASSFMNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQYQQQGQNYQHQQQGQQQQQGHSSSFSALASMASSYLGNNSNSNSSYGGQQQANEYGRPQQNGQQQSNEYGRPQYGGNQNSNGQHESFNFSGNFSQQNNNGNQNRY,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,Faster aggregation,"Yes, direct evidence.",No,"RnqPD aggregates cross-seed polymerization of Sup35NM in vitro. A, kinetics of polymerization of 8 μm Sup35NM in the presence of 1% of preformed Sup35NM fibers (bold black curve) or the indicated amount of RnqPD aggregates (thin black curves). Seed was sonicated for 20 s in all the reactions. Gray curve, unseeded reaction",NA,NA,Interactor: RNQ-PD (395–1215 bp) Interactee: SUP35-NM,10.1074/jbc.M609269200,AG00207
Sup35,Rnq1,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,MDTDKLISEAESHFSQGNHAEAVAKLTSAAQSNPNDEQMSTIESLIQKIAGYVMDNRSGGSDASQDRAAGGGSSFMNTLMADSKGSSQTQLGKLALLATVMTHSSNKGSSNRGFDVGTVMSMLSGSGGGSQSMGASGLAALASQFFKSGNNSQGQGQGQGQGQGQGQGQGQGSFTALASLASSFMNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQYQQQGQNYQHQQQGQQQQQGHSSSFSALASMASSYLGNNSNSNSSYGGQQQANEYGRPQQNGQQQSNEYGRPQYGGNQNSNGQHESFNFSGNFSQQNNNGNQNRY,Faster aggregation,"Yes, direct evidence.",No,NA,NA,NA,Interactor: SUP35-NM Interactee: RNQ-PD,10.1074/jbc.M609269200,AG00208
Rnq1,Rnq1,MDTDKLISEAESHFSQGNHAEAVAKLTSAAQSNPNDEQMSTIESLIQKIAGYVMDNRSGGSDASQDRAAGGGSSFMNTLMADSKGSSQTQLGKLALLATVMTHSSNKGSSNRGFDVGTVMSMLSGSGGGSQSMGASGLAALASQFFKSGNNSQGQGQGQGQGQGQGQGQGQGSFTALASLASSFMNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQYQQQGQNYQHQQQGQQQQQGHSSSFSALASMASSYLGNNSNSNSSYGGQQQANEYGRPQQNGQQQSNEYGRPQYGGNQNSNGQHESFNFSGNFSQQNNNGNQNRY,MDTDKLISEAESHFSQGNHAEAVAKLTSAAQSNPNDEQMSTIESLIQKIAGYVMDNRSGGSDASQDRAAGGGSSFMNTLMADSKGSSQTQLGKLALLATVMTHSSNKGSSNRGFDVGTVMSMLSGSGGGSQSMGASGLAALASQFFKSGNNSQGQGQGQGQGQGQGQGQGQGSFTALASLASSFMNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQYQQQGQNYQHQQQGQQQQQGHSSSFSALASMASSYLGNNSNSNSSYGGQQQANEYGRPQQNGQQQSNEYGRPQYGGNQNSNGQHESFNFSGNFSQQNNNGNQNRY,Faster aggregation,Yes; implied by kinetics.,No,"A–D, kinetics of RnqPD polymerization monitored by ThT fluorescence. A, 10 and 20 M RnqPD, unseeded and seeded with 5% pre-formed RnqPD aggregates",". In contrast, freshly dissolved RnqPD treated with 2% SDS migrated as a monomer and some low oligomeric forms (Fig. 1E). SDS-resistant subparticles were also observed when in vitro made aggregates of full-length Rnq1 were examined (supplemental Fig. S1B). Morphology of RnqPD Aggregates—To analyze the morphology of aggregated RnqPD, we used TEM. RnqPD aggregates were made in bulk in a vigorously agitated reaction mixture (see “Experimental Procedures”).",NA,"Interactor: RNQ-PD (395–1215 bp), Interactee: RNQ-PD (395–1215 bp)",10.1074/jbc.M609269200,AG00209
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,These results indicated that monomeric alpha-synuclein delayed substantially the overall rates of formation of Abeta42 fibrils in a concentration-dependent manner (Fig. 1 A–C and Fig. S1A).,These results indicated that monomeric alpha-synuclein delayed substantially the overall rates of formation of Abeta42 fibrils in a concentration-dependent manner (Fig. 1 A–C and Fig. S1A).,NA,Kinetic results depend on the form of interactor. Here: molecular.,10.1073/pnas.1700239114,AG00210
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Kinetic results depend on the form of interactor. Here: fibrilar.,10.1073/pnas.1700239114,AG00211
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"When Abeta42 aggregation was performed under seeding conditions, in the presence of preformed alpha-synuclein fibrils, the aggregation process was found to be accelerated.",NA,NA,Kinetic results depend on the form of interactor. Here: fibrilar.,10.1073/pnas.1700239114,AG00212
Amyloid beta,Amyloid beta,VGSNKGAIIGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interactor: Aß24-34 WT. Interactee:Aß1-42,10.1074/jbc.M117.806109,AG00213
IAPP,Amyloid beta,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interactor: hIAPP. Interactee:Aß1-42,10.1074/jbc.M117.806109,AG00214
IAPP,Amyloid beta,SGNNFGAILSS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interactor: hIAPP 19-29 S20G. Interactee: Aß1-42,10.1074/jbc.M117.806109,AG00215
Amyloid beta,IAPP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interactor: Aß1-42 Interactee:hIAPP,10.1074/jbc.M117.806109,AG00216
IAPP,IAPP,SGNNFGAILSS,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interactor: hIAPP 1-29 S20G. Interactee: hIAPP,10.1074/jbc.M117.806109,AG00217
Amyloid beta,IAPP,VGSNKGAIIGL,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interactor: Aß24-34. Interactee: hIAPP,10.1074/jbc.M117.806109,AG00218
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interactor: Aß1-42. Interactee: Aß1-42,10.1074/jbc.M117.806109,AG00219
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interactor:hIAPP Interactee: hIAPP,10.1074/jbc.M117.806109,AG00220
Alpha-synuclein,Tau,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,Faster aggregation,"Yes, direct evidence.",No information,Alpha-syn induces fibrillization of tau and that coincubation of tau and alpha-syn synergistically promotes fibrillization of both proteins,"To assess the composition of the fibrils formed from mixing alpha-syn and tau, we performed immuno-EM with antibodies to alpha-syn and tau and secondary antibodies conjugated to either 5-nm or 10-nm colloidal gold particles (Fig. 3). Whereas many fibrils were labeled solely with antibodies to alpha-syn (Fig. 3A), bundled fibrils labeled with both alpha-syn and tau antibodies were also demonstrated (Fig. 3, B and C).",NA,"Immunolabeling confirmed , that fibrils consist of two different amyloids, however there is no information about the structure of resulting fibrils. Therefore, the answer for 3rd question was ""no information"".",10.1126/science.1082324,AG00221
Tau,Alpha-synuclein,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No information,The coincubation of tau T40 and alpha-syn resulted in greater K114 fluorescence compared to samples that contained only alpha-syn (Fig. 1A).,"To assess the composition of the fibrils formed from mixing alpha-syn and tau, we performed immuno-EM with antibodies to alpha-syn and tau and secondary antibodies conjugated to either 5-nm or 10-nm colloidal gold particles (Fig. 3). Whereas many fibrils were labeled solely with antibodies to alpha-syn (Fig. 3A), bundled fibrils labeled with both alpha-syn and tau antibodies were also demonstrated (Fig. 3, B and C).",NA,"Immunolabeling confirmed, that fibrils consist of two different amyloids, however there is no information about the structure of resulting fibrils. Therefore, the answer for 3rd question was ""no information"".",10.1126/science.1082324,AG00222
Alpha-synuclein,Tau,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Coincubation of beta-syn or Δ71-82 alpha-syn with tau T40 did not result in detectable K114 fluorescence (Fig. 1A) or the accumulation of pelletable syn or tau T40 polymers (Figs. 1, B and C, and 2A).",NA,NA,"Δ71-82 alpha-syn, an artificial alpha-syn mutant (residues 71–82 in human alpha-syn were deleted) as interactor",10.1126/science.1082324,AG00223
Tau,Amyloid beta,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Incubation of Abeta (1-40) with tau T40 did not promote fibrillogenesis. On the contrary, there was a reduction in amyloidogenic polymers asindicated by lower K114 fluorescence.","Incubation of Abeta (1-40) with tau T40 did not promote fibrillogenesis. On the contrary, there was a reduction in amyloidogenic polymers asindicated by lower K114 fluorescence.","Incubation of Abeta (1-40) with tau T40 did not promote fibrillogenesis. On the contrary, there was a reduction in amyloidogenic polymers asindicated by lower K114 fluorescence.",NA,10.1126/science.1082324,AG00224
Amyloid beta,Amyloid beta,EFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,Yes,"In addition, amyloid fibril formation is also observed in mixtures of both species at concentrations of Abeta(1-42) (2 μM) and pEAbeta(3-42) (0.5 μM) where each of the species individually does not show any aggregation under the same conditions (Fig. 2C).",NA,"Heteromolecular mixtures of monomeric pEAbeta(3-42) and Abeta(1-42) displayed a single sigmoidal aggregation kinetic curve, indicating that both species undergo co-aggregation.","Pyroglutamate-modified Abeta(3-42) monomers as interactor, Abeta(1–42) monomers as interactee",10.1039/C6SC04797A,AG00225
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,EFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,Yes,"In addition, amyloid fibril formation is also observed in mixtures of both species at concentrations of Abeta(1-42) (2 μM) and pEAbeta(3-42) (0.5 μM) where each of the species individually does not show any aggregation under the same conditions (Fig. 2C).",NA,"Heteromolecular mixtures of monomeric pEAbeta(3-42) and Abeta(1-42) displayed a single sigmoidal aggregation kinetic curve, indicating that both species undergo co-aggregation.","Abeta(1–42) monomers as interactor, Pyroglutamate-modified Abeta(3-42) monomers as interactee",10.1039/C6SC04797A,AG00226
Amyloid beta,Amyloid beta,EFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"Compared to the seeding effect of Abeta(1-42) fibrils, only small amounts of pEAbeta(3-42) fibrils are needed to accelerate Abeta(1-42) aggregation drastically",NA,NA,"Pyroglutamate-modified Abeta(3-42) fibrils as interactor, Abeta(1–42) monomers as interactee",10.1039/C6SC04797A,AG00227
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,EFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"By adding 5% Abeta(1-42) fibrils the fibrillation of pEAbeta(3-42) was almost completely inhibited, as judged by ThT fluorescence. (...) We have acquired AFM images of a mixture of pEAbeta(3-42) and 5% Abeta(1-42) fibrils (Fig. S7†) that show clusters of fibrils that appear to be coated in monomer.","By adding 5% Abeta(1-42) fibrils the fibrillation of pEAbeta(3-42) was almost completely inhibited, as judged by ThT fluorescence. (...) We have acquired AFM images of a mixture of pEAbeta(3-42) and 5% Abeta(1-42) fibrils (Fig. S7†) that show clusters of fibrils that appear to be coated in monomer.","By adding 5% Abeta(1-42) fibrils the fibrillation of pEAbeta(3-42) was almost completely inhibited, as judged by ThT fluorescence. (...) We have acquired AFM images of a mixture of pEAbeta(3-42) and 5% Abeta(1-42) fibrils (Fig. S7†) that show clusters of fibrils that appear to be coated in monomer.","Abeta(1–42) fibrils as interactor, Pyroglutamate-modified Abeta(3-42) monomers as interactee",10.1039/C6SC04797A,AG00228
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,EFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"Abeta(1–42) fibrils as interactor, Pyroglutamate-modified Abeta(3-42) monomers seeded with 20% Pyroglutamate-modified Abeta(3-42) fibrils as interactee",10.1039/C6SC04797A,AG00229
Alpha-synuclein,PrP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.bbrc.2019.10.120,AG00230
Alpha-synuclein,PrP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,No effect,No,No,NA,NA,NA,NA,10.1016/j.bbrc.2019.10.120,AG00231
IAPP,IAPP,NFGAILSS,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1021/acs.biochem.7b00739,AG00232
IAPP,IAPP,NFGAIL,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1021/acs.biochem.7b00739,AG00233
IAPP,IAPP,NFGAILS,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1021/acs.biochem.7b00739,AG00234
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,The second and most important aspect of the mixed oligomer ATD in Figure 2c is that no species larger than tetramers are observed.,"""The second and most important aspect of the mixed oligomer ATD in Figure 2c is that no species larger than tetramers are observed.""","""The second and most important aspect of the mixed oligomer ATD in Figure 2c is that no species larger than tetramers are observed.""",Interactor: Abeta40  Interactee: Abeta42,10.1021/ja8092604,AG00235
Sup35,Sup35,GNNQQNY,GNNQQNY,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1016/j.colsurfb.2016.10.011,AG00236
Sup35,Albumin,GNNQQNY,MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL,No effect,No information,No information,No remarkable difference in the turbidity changebetween the INS solutions with and without the GNNQQNY aggre-gates was observed (Fig. 4a). The CD spectra of the two INS solutionsat day 3 were nearly identical to that of a fresh INS solution(Fig. 4b). Similar trends in the turbidity and CD spectral changeswere observed for the HSA and LYS solutions,NA,NA,NA,10.1016/j.colsurfb.2016.10.011,AG00238
Sup35,Lysozyme,GNNQQNY,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,No effect,No information,No information,No remarkable difference in the turbidity changebetween the INS solutions with and without the GNNQQNY aggre-gates was observed (Fig. 4a). The CD spectra of the two INS solutionsat day 3 were nearly identical to that of a fresh INS solution(Fig. 4b). Similar trends in the turbidity and CD spectral changeswere observed for the HSA and LYS solutions,NA,NA,NA,10.1016/j.colsurfb.2016.10.011,AG00240
Kappa-casein,Beta-lactoglobulin,MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYG LNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHP HPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEI NTVQVTSTAV,MKCLLLALALTCGAQALIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI,Slower aggregation,Formation of fibrils by the interactee is inhibited,Yes,The heated  beta -Lg and  kappa -CN  mixture exhibited a slower increase in fluorescence than the  individual proteins and a fluorescence plateau (maximum)  that is intermediate between the two individual proteins.,NA,"After heating, well-defined, long,  curly amyloid fibrillar structures were present that had a  uniquely different morphology compared to the heated sam- ples of each individual protein (Figure 9F), implying that  beta -Lg and  kappa -CN interact upon heating and copolymerize to  form heteropolymeric amyloid fibrils that are distinctly dif- ferent to the amyloid fibrils formed by each protein on its  own.",NA,10.1002/smll.201603591,AG00241
Beta-lactoglobulin,Kappa-casein,MKCLLLALALTCGAQALIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI,MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYG LNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHP HPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEI NTVQVTSTAV,Slower aggregation,Formation of fibrils by the interactee is inhibited,Yes,The heated  beta -Lg and  kappa -CN  mixture exhibited a slower increase in fluorescence than the  individual proteins and a fluorescence plateau (maximum)  that is intermediate between the two individual proteins.,NA,"After heating, well-defined, long,  curly amyloid fibrillar structures were present that had a  uniquely different morphology compared to the heated sam- ples of each individual protein (Figure 9F), implying that  beta -Lg and  kappa -CN interact upon heating and copolymerize to  form heteropolymeric amyloid fibrils that are distinctly dif- ferent to the amyloid fibrils formed by each protein on its  own.",NA,10.1002/smll.201603591,AG00242
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"In all cases of self-seeding, we observe shortening of the lag phase in the presence of preformed seeds as would be expected in the presence of a surface-catalyzed secondary nucleation process of monomer on fibril surface",NA,NA,Interactor: Abeta42 seeds Interactee: Abeta42 monomers,10.1021/jacs.5b07849,AG00243
Amyloid beta,Amyloid beta,SGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,SGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"In all cases of self-seeding, we observe shortening of the lag phase in the presence of preformed seeds as would be expected in the presence of a surface-catalyzed secondary nucleation process of monomer on fibril surface",NA,NA,Interactor: -15Abeta42 seeds Interactee: -15Abeta42 monomers,10.1021/jacs.5b07849,AG00244
Amyloid beta,Amyloid beta,DARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"In all cases of self-seeding, we observe shortening of the lag phase in the presence of preformed seeds as would be expected in the presence of a surface-catalyzed secondary nucleation process of monomer on fibril surface",NA,NA,Interactor: −30Abeta42 preformed fibrils Interactee: −30Abeta42 monomers,10.1021/jacs.5b07849,AG00245
Amyloid beta,Amyloid beta,SGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,Yes,"In all cases of self-seeding, we observe shortening of the lag phase in the presence of preformed seeds as would be expected in the presence of a surface-catalyzed secondary nucleation process of monomer on fibril surface",NA,"Still, Abeta42 and NTE-Abeta42 co-aggregate to form mixed fibrils and fibrils of either Abeta42 or NTE-Abeta42 catalyze aggregation of all monomers.",Interactor: −15Abeta42 fibrils Interactee: Abeta42 monomers,10.1021/jacs.5b07849,AG00246
Amyloid beta,Amyloid beta,DARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,"Yes, direct evidence.",Yes,NA,NA,"Still, Abeta42 and NTE-Abeta42 co-aggregate to form mixed fibrils and fibrils of either Abeta42 or NTE-Abeta42 catalyze aggregation of all monomers.",Interactor: −30Abeta42 fibrils Interactee: Abeta42 monomers,10.1021/jacs.5b07849,AG00247
Amyloid beta,Amyloid beta,ANTSNEVQPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,Yes,"In all cases of self-seeding, we observe shortening of the lag phase in the presence of preformed seeds as would be expected in the presence of a surface-catalyzed secondary nucleation process of monomer on fibril surface",NA,"Still, Abeta42 and NTE-Abeta42 co-aggregate to form mixed fibrils and fibrils of either Abeta42 or NTE-Abeta42 catalyze aggregation of all monomers.",Intercator: −40Abeta42 fibrils Interactee: Abeta42 monomers,10.1021/jacs.5b07849,AG00248
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,SGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,Yes,"In all cases of self-seeding, we observe shortening of the lag phase in the presence of preformed seeds as would be expected in the presence of a surface-catalyzed secondary nucleation process of monomer on fibril surface",NA,"Still, Abeta42 and NTE-Abeta42 co-aggregate to form mixed fibrils and fibrils of either Abeta42 or NTE-Abeta42 catalyze aggregation of all monomers.",Interactor: Abeta42 fibrils Interactee: −15Abeta42 monomers,10.1021/jacs.5b07849,AG00249
Amyloid beta,Amyloid beta,DARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,SGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"In all cases of self-seeding, we observe shortening of the lag phase in the presence of preformed seeds as would be expected in the presence of a surface-catalyzed secondary nucleation process of monomer on fibril surface",NA,NA,Interactor: −30Abeta42 fibrils Interactee: −15Abeta42 monomers,10.1021/jacs.5b07849,AG00250
Amyloid beta,Amyloid beta,DARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,SGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"In all cases of self-seeding, we observe shortening of the lag phase in the presence of preformed seeds as would be expected in the presence of a surface-catalyzed secondary nucleation process of monomer on fibril surface",NA,NA,Interactor: −30Abeta42 fibrils Interactee: −15Abeta42 monomers,10.1021/jacs.5b07849,AG00251
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,Yes,"In all cases of self-seeding, we observe shortening of the lag phase in the presence of preformed seeds as would be expected in the presence of a surface-catalyzed secondary nucleation process of monomer on fibril surface",NA,"Still, Abeta42 and NTE-Abeta42 co-aggregate to form mixed fibrils and fibrils of either Abeta42 or NTE-Abeta42 catalyze aggregation of all monomers.",Interactor: Abeta42 fibrils Interactee: −30Abeta42 monomers,10.1021/jacs.5b07849,AG00252
Amyloid beta,Amyloid beta,SGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"In all cases of self-seeding, we observe shortening of the lag phase in the presence of preformed seeds as would be expected in the presence of a surface-catalyzed secondary nucleation process of monomer on fibril surface",NA,NA,Interactor: −15Abeta42 fibrils Interactee: −30Abeta42 monomers,10.1021/jacs.5b07849,AG00253
Amyloid beta,Amyloid beta,ANTSNEVQPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"In all cases of self-seeding, we observe shortening of the lag phase in the presence of preformed seeds as would be expected in the presence of a surface-catalyzed secondary nucleation process of monomer on fibril surface",NA,NA,Interactor: −40Abeta42 fibrils Interactee: −30Abeta42 monomers,10.1021/jacs.5b07849,AG00254
PrP,PrP,NLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGND,GQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRS,No effect,Yes; implied by kinetics.,No,the addition of high amounts (10%) of PrP(107-143) fibrils into PrP(89-230) monomer solution had no effect on aggregation kinetics within the experimental time,NA,"As suggested by AFM images (Figure 2e), it seems that the PrP(107-143) fibrils are incapable of elongatingthrough recruitment of PrP(89-230) monomers (or the elongation rate is extremely slow). Moreover, FTIR results suggest that the presence of PrP(107-143) fibrils has no effect on the structural profiles of the resulting PrP(89-230) fibrils.",Interactor: PrP(107-143) fibrils 10% added at the beggining of the reaction (small concentration of interactee) Interactee: PrP(89-230),10.3390/ijms21197410,AG00255
PrP,PrP,NLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGND,GQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRS,No effect,Yes; implied by kinetics.,No,The presence of monomeric PrP(107-143) has no effect on the aggregation kinetics of PrP(89-230)-seed-induced aggregation reaction,NA,"As suggested by AFM images (Figure 2e), it seems that the PrP(107-143) fibrils are incapable of elongatingthrough recruitment of PrP(89-230) monomers (or the elongation rate is extremely slow). Moreover, FTIR results suggest that the presence of PrP(107-143) fibrils has no effect on the structural profiles of the resulting PrP(89-230) fibrils.",Interactor: PrP(107-143) monomers Interactee: PrP(89-230)  seed,10.3390/ijms21197410,AG00256
PrP,PrP,GQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRS,NLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGND,Faster aggregation,No information,No information,NA,NA,NA,Interactor: PrP(89-230) seed introduced at different time point and the result is the same for every time point Interactee: PrP(107-143) fibrils 10%,10.3390/ijms21197410,AG00257
PrP,PrP,NLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGND,GQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRS,Faster aggregation,Yes; implied by kinetics.,No,"This suggests that the nucleation enhancing effect of PrP(107-143) fibrils is much stronger at later stages (i.e., at 435 min) of the aggregation reaction and this could be explained by the fact that the concentration of nuclei/fibril ends is much higher at this stage of the reaction. These results are in agreement with the data presented in Figure 1, where the synergistic effect of different PrP fibrils was most evident at the highest concentrations of PrP(89-230) fibrils",NA,"As suggested by AFM images (Figure 2e), it seems that the PrP(107-143) fibrils are incapable of elongatingthrough recruitment of PrP(89-230) monomers (or the elongation rate is extremely slow). Moreover, FTIR results suggest that the presence of PrP(107-143) fibrils has no effect on the structural profiles of the resulting PrP(89-230) fibrils.",Interactor: PrP(107-143) fibrils 10% added at the later stages of the reaction (high concentration of interactee) Interactee: PrP(89-230),10.3390/ijms21197410,AG00258
Rnq1,Sup35,MDTDKLISEAESHFSQGNHAEAVAKLTSAAQSNPNDEQMSTIESLIQKIAGYVMDNRSGGSDASQDRAAGGGSSFMNTLMADSKGSSQTQLGKLALLATVMTHSSNKGSSNRGFDVGTVMSMLSGSGGGSQSMGASGLAALASQFFKSGNNSQGQGQGQGQGQGQGQGQGQGSFTALASLASSFMNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQYQQQGQNYQHQQQGQQQQQGHSSSFSALASMASSYLGNNSNSNSSYGGQQQANEYGRPQQNGQQQSNEYGRPQYGGNQNSNGQHESFNFSGNFSQQNNNGNQNRY,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,Faster aggregation,"Yes, direct evidence.",No information,"""Conversion of soluble NM into amyloid occurred when Rnq1 preformed sonicated fibers were added at a value equal to 10% mol/mol, and the rate of NM conversion increased as the ratio of Rnq1 to NM increased (Fig. 3A)""",NA,NA,Interactee: Sup35 (NM prion domain),10.1073/pnas.0404968101,AG00259
Transthyretin,Sup35,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,No effect,No,No,"On the contrary, TTR-WT and alphaSyn amyloids did not seed NM conversion even when added at 50% mol/mol ratio (Fig. 3C).","On the contrary, TTR-WT and alphaSyn amyloids did not seed NM conversion even when added at 50% mol/mol ratio (Fig. 3C).",NA,Interactee: Sup35 (NM prion domain),10.1073/pnas.0404968101,AG00260
Alpha-synuclein,Sup35,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,No effect,No,No,"On the contrary, TTR-WT and alphaSyn amyloids did not seed NM conversion even when added at 50% mol/mol ratio (Fig. 3C).",NA,NA,Interactee: Sup35 (NM prion domain),10.1073/pnas.0404968101,AG00261
Lysozyme,Sup35,MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,No effect,No,No,NA,NA,NA,Interactee: Sup35 (NM prion domain),10.1073/pnas.0404968101,AG00264
Albumin,Amyloid beta,MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Our TEM images clearly show that monomeric Abeta(1-40) and Abeta(1-42) incubated in the presence of 50 µM HSA, are only capable of assembling into a large quantity of small circular oligomers while fibre formation is inhibited,",NA,NA,Interactee: Abeta(1-40) monomers,10.1016/j.jmb.2018.01.008,AG00265
Albumin,Amyloid beta,MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,"""Our TEM images clearly show that monomeric Abeta(1-40) and Abeta(1-42) incubated in the presence of 50 µM HSA, are only capable of assembling into a large quantity of small circular oligomers while fibre formation is inhibited,""",NA,NA,Interactee: Abeta(1-42) monomers,10.1016/j.jmb.2018.01.008,AG00266
Albumin,Amyloid beta,MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,Yes; implied by kinetics.,No information,"In agreement with the ThT studies, Figure 2h shows that the addition of 50 µM albumin to preformed fibres does not impact the quantity of preformed Abeta fibres.",NA,NA,Interactee: Abeta(1-40) preformed fibers,10.1016/j.jmb.2018.01.008,AG00267
Albumin,Amyloid beta,MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,Yes; implied by kinetics.,No information,"TEM images of Abeta(1-40) incubated with cholesterol bound albumin confirms Abeta is able to form amyloid fibres similar in appearance to those formed in the absence of albumin, Figure 6d.  When the HSA (10 µM) was loaded with palmitic acid, the A fibre growth was no longer inhibited by the fatty acid loaded albumin, and returned to its maximum ThT fluorescence, Figure 7c.",NA,NA,Interactor: fatty acid/ cholesterol loaded albumin  Interactee: Abeta(1-40),10.1016/j.jmb.2018.01.008,AG00268
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No,No,"By adding 10%  Abeta40 to  Abeta42 (i.e. 9/1 ratio), no significant change in the lag and elongation phases was observed compared with Abeta42 alone.",NA,NA,"Interactor: 10% Abeta 1-40, Interactee: Abeta 1-42",10.1111/febs.12813,AG00269
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,No,No,"However, with addition of 10% Abeta42 to Abeta40 (i.e. 1/9 ratio), the Abeta40 lag time was significantly extended from ~ 17 to ~ 80 h.",NA,NA,"Interactor: 10% Abeta 1-42, Interactee: Abeta 1-40",10.1111/febs.12813,AG00270
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,"Yes, direct evidence.",Yes,NA,NA,"At 6 h incubation, the Abeta42- dominant species have some aggregated short protofi- brils with length ranging from ~ 20 to ~ 90 nm in the supernatants, whereas few of these protofibrils can be observed in the Abeta40-dominant species. The equally mixed samples generally have round-shaped oligomers with a diameter ranging from ~ 6 to 20 nm and some short protofibrils were also present. Longer fibrils were found in the insoluble portions, especially in the Abeta42- dominant species.","Interactor: Abeta 1-42, Interactee: Abeta 1-40 - interactor and interactee are equally mixed",10.1111/febs.12813,AG00271
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,"Yes, direct evidence.",Yes,NA,NA,"At 6 h incubation, the Abeta42- dominant species have some aggregated short protofi- brils with length ranging from ~ 20 to ~ 90 nm in the supernatants, whereas few of these protofibrils can be observed in the Abeta40-dominant species. The equally mixed samples generally have round-shaped oligomers with a diameter ranging from ~ 6 to 20 nm and some short protofibrils were also present. Longer fibrils were found in the insoluble portions, especially in the Abeta42- dominant species.","Interactor: Abeta 1-40, Interactee: Abeta 1-42 - interactor and interactee are equally mixed",10.1111/febs.12813,AG00272
IAPP,IAPP,CMLCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,These data suggested that AGE-IAPP can interact with IAPP and boost the aggregation of IAPP,NA,NA,"Interactor: AGE-IAPP Interactee: IAPP IAPP:AGE-IAPP ratios: 1:3, 1:1, 3:1",10.1016/j.bpj.2019.05.013,AG00273
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,"Consistent with previous studies, 10% IAPP fibrils (in its monomeric unit) can successfully seed amyloid formation by IAPP monomers, resulting in a quick increase of ThT intensity without an obvious lag time.",NA,NA,Interactor: IAPP fibrils Interactee: IAPP monomers,10.1016/j.bpj.2019.05.013,AG00274
IAPP,IAPP,CMLCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,CMLCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,"Compared with unseeded reactions, IAPP and AGE-IAPP both formed amyloid fibrils much faster in the presence of AGE-IAPP fibrils, suggesting that both peptides can be seeded by AGE-IAPP fibrils.",NA,NA,Interactor: AGE-IAPP fibrils Interactee: AGE-IAPP monomers,10.1016/j.bpj.2019.05.013,AG00275
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,CMLCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No,No,"Interestingly, no matter what percentage of AGE-IAPP in the mixture, the kinetic profiles of amyloid formation for conditions containing AGE-IAPP are almost identical to the one of AGE-IAPP alone",NA,NA,"Interactor: IAPP Interactee: AGE-IAPP AGE-IAPP:IAPP ratios: 1:3, 1:1, 3:1",10.1016/j.bpj.2019.05.013,AG00276
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,CMLCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interactor: IAPP seeds Interactee: AGE-IAPP,10.1016/j.bpj.2019.05.013,AG00277
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,"Yes, direct evidence.",No,"wt TTR had very little effect on the Abeta aggregation rate,",NA,EM images of Abeta alone or with wt TTR were very similar to each other,Interactee: Abeta(1-40)  Interactor: wt TTR,10.1021/bi101280t,AG00278
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,"Yes, direct evidence.",Yes,T119M moderately increased the rate of Abeta aggregation over the time course of measurement,NA,"With the T119MþAbeta mixture (Figure 9C), there appeared to be relatively more long fibrils.",Interactee: Abeta(1-40)  Interactor: T119M,10.1021/bi101280t,AG00279
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,"Yes, direct evidence.",Yes,"The strongest effect was detected with M-TTR, which significantly suppressed Abeta aggregation, lowering both the total intensity and the rate of increase over ∼20 h.",NA,"The most striking difference was with the M-TTRþ Abeta mixture (Figure 9D), where very few long fibrils were observed.",Interactee: Abeta(1-40)  Interactor: M-TTR,10.1021/bi101280t,AG00280
IAPP,Amyloid beta,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Abeta40 fibrillogenesis exhibited a lag time of approximately 48 h and reached completion at 72–96 h (Figure 2 d,e). In the presence of an equimolar amount of IAPP-GI,however, Abeta40 fibrillogenesis was completely blocked (Figure 2 d,e).",NA,NA,"Interactor: [(NMe)G24,(N-Me)I26]-IAPP (IAPP-GI) Interactee: Abeta40  In hIAPP (N-Me)IG26 and (N-Me)I26 are N-methylation of two amide bonds on the same “side” of the b-strand in the amyloid core sequence IAPP(22–27), so this sequence is mutated",10.1002/anie.200604056,AG00281
IAPP,Amyloid beta,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,"Yes, direct evidence.",Yes,"IAPP delays Abeta40 fibrillogenesis, and IAPP fibrillogenesis is delayed by Abeta40.","Direct evidence for Abeta40/IAPP heterocomplex formation was obtained by CD spectroscopy (data not shown), Abeta pull-down assays,and fluorescence spectroscopy (Figure 5 c–e).","Western blotting with anti-Abeta40 showed twice as many trimers in the mixtures than in the Abeta40 incubation alone and significant amounts of low-molecular-weight oligomers,including tetra-,penta-, and hexamers which were completely absent from the Abeta40 incubations (Figure 5 f; see also Figure S3 in the Supporting Information). Western blotting with anti- IAPP also revealed increased amounts and downward shifts of the trimers to hexamers in the mixtures (Figure 5 f). These results suggest that trimers to hexamers were the main heterooligomeric species in the mixtures.","Interactor: IAPP 16,5 um Interactee: Abeta40 16,5 um",10.1002/anie.200604056,AG00282
Amyloid beta,IAPP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,"Yes, direct evidence.",Yes,"IAPP delays Abeta40 fibrillogenesis, and IAPP fibrillogenesis is delayed by Abeta40.","Direct evidence for Abeta40/IAPP heterocomplex formation was obtained by CD spectroscopy (data not shown), Abeta pull-down assays,and fluorescence spectroscopy (Figure 5 c–e).","Western blotting with anti-Abeta40 showed twice as many trimers in the mixtures than in the Abeta40 incubation alone and significant amounts of low-molecular-weight oligomers,including tetra-,penta-, and hexamers which were completely absent from the Abeta40 incubations (Figure 5 f; see also Figure S3 in the Supporting Information). Western blotting with anti- IAPP also revealed increased amounts and downward shifts of the trimers to hexamers in the mixtures (Figure 5 f). These results suggest that trimers to hexamers were the main heterooligomeric species in the mixtures.",Interactor: Abeta40 Interactee: IAPP,10.1002/anie.200604056,AG00283
Amyloid beta,IAPP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,"Yes, direct evidence.",No,"Interestingly, when incubating equimolar Abeta (25 µM) and hIAPP (25 µM) together, the ThT curve displayed a ~6 h lag phase more slowly than that of Abeta and hIAPP alone.",NA,"Overall, it is confirmed that all homo-seeding and cross-seeding samples formed fibrils at 24 h, and the morphologies of mature fibrils were similar in all cases.","Interactor: Abeta1-42 12.5µM, 25µM, Interactee: hIAPP1-37  12.5µM, 25µM",10.1021/acschemneuro.5b00192,AG00284
IAPP,Amyloid beta,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,"Yes, direct evidence.",No,"Interestingly, when incubating equimolar Abeta (25 µM) and hIAPP (25 µM) together, the ThT curve displayed a ~6 h lag phase more slowly than that of Abeta and hIAPP alone.",NA,"Overall, it is confirmed that all homo-seeding and cross-seeding samples formed fibrils at 24 h, and the morphologies of mature fibrils were similar in all cases.","Interactor: hIAPP1-37 12.5µM, 25µM, Interactee: Abeta1-42 12.5µM, 25µM",10.1021/acschemneuro.5b00192,AG00285
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVSFAEDVGSNKGAIIGPMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Yes; implied by kinetics.,No,"Our results show that Abeta42 exhibits a typical aggregation pattern with a ~ 2 h lag phase (Figure S5A) and that low concentrations of purified Abeta42DM (15 nM) were sufficient to significantly suppress Abeta42 aggregation (at 4 μM) (Figure 3A). ThT fluorescence was monitored upon coincubation of Abeta42 (4 μM) with Abeta42DM at different concentrations (black, red, blue, pink and green represent 0, 7.8, 15.5, 31 and 62 nM, respectively)","To confirm direct binding between Abeta42 and Abeta42DM in vitro and to further illuminate the effect of Abeta42DM on Abeta42 aggregation kinetics, we used Abeta42DM and Abeta42 peptides and monitored their direct binding by surface plasmon resonance (SPR) spectroscopy. The parameters of binding were computed by fitting the SPR sensograms using a Langmuir 1:1 binding model (Figure 2B and C). Our results showed that when immobilized to the chip, Abeta42DM binds Abeta42 with kon and koff rates of 300 M-1s-1 and 1.6×10-4 s-1, respectively, with the KD for the interaction being 520 nm (Figure 2B).",NA,aB42 F19S L34P inhibits aB42,10.1042/BCJ20180247,AG00286
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,No,No,NA,NA,NA,NA,10.1021/jacs.7b13660,AG00287
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAGDVGSNKGAIIGLMVGGVV,Faster aggregation,"Yes, direct evidence.",Yes,NA,NA,We have also presented the effectiveness of a SSNMR approach to elucidate site-specific structural features for cross-seeded amyloid fibrils for the first time. This approach is likely applicable to examine structural cross talk of various amyloid proteins,NA,10.1021/jacs.7b13660,AG00288
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1110/ps.04707004,AG00289
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGTLQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1110/ps.04707004,AG00290
Lysozyme,Lysozyme,KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCNIPCSALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1110/ps.04707004,AG00291
Lysozyme,Lysozyme,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1110/ps.04707004,AG00292
Alpha-lactalbumin,Lysozyme,KQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAIVENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEKL,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,"Yes, direct evidence.",Yes,NA,NA,NA,NA,10.1110/ps.04707004,AG00293
Lysozyme,Lysozyme,KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCNIPCSALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL,KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCNIPCSALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1110/ps.04707004,AG00295
Alpha-lactalbumin,Alpha-lactalbumin,KQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAIVENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEKL,KQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAIVENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEKL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1110/ps.04707004,AG00296
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCNIPCSALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1110/ps.04707004,AG00297
Lysozyme,Alpha-lactalbumin,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAIVENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEKL,No effect,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1110/ps.04707004,AG00298
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQD,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,No,No,"For the 1–135/FL alphasyn mixture, little if any aggregation occurred, as the 1–135 alphasyn truncation appears to be highly similar to the FL protein, which does not appreciably aggregate at this concentration.","For the 1–135/FL alphasyn mixture, little if any aggregation occurred, as the 1–135 alphasyn truncation appears to be highly similar to the FL protein, which does not appreciably aggregate at this concentration.","For the 1–135/FL alphasyn mixture, little if any aggregation occurred, as the 1–135 alphasyn truncation appears to be highly similar to the FL protein, which does not appreciably aggregate at this concentration.",NA,10.1074/jbc.RA118.005603,AG00299
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPS,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,Yes,"Comparatively, with increasing extent of C-truncation from 1–129 and shorter, the FL protein is induced to aggregate at earlier time points",NA,the resulting mixed fibrils composed of both C-truncated and FL alphasyn,NA,10.1074/jbc.RA118.005603,AG00300
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAY,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,Yes,These results demonstrate that physiologically C-truncated forms of alphasyn can directly accelerate formation of FL alphasyn fibrils through their robust tendency to aggregate.,NA,the resulting mixed fibrils composed of both C-truncated and FL alphasyn,NA,10.1074/jbc.RA118.005603,AG00301
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILED,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,Yes,"Most striking was the mixture of 1–115 with FL alphasyn, where within 12 h, FL alphasyn had aggregated to a greater extent than FL alphasyn alone at 150 μm and 96 h",NA,the resulting mixed fibrils composed of both C-truncated and FL alphasyn,NA,10.1074/jbc.RA118.005603,AG00302
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILED,KTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No information,"Yes, direct evidence.",Yes,NA,"21–140 and C-truncated alphasyn were co-aggregated to form mixed fibrils, which were immunolabeled with antibodies 4110 and 94-3A10 and then detected by secondary antibodies conjugated to 10- or 6-nm gold nanoparticles, respectively. Fibrils composed of either 21–140 + 1–115 alphasyn or 21–140 + 1–129 alphasyn are reactive to both antibodies 4110 (arrowheads) and 94-3A10 (arrows), demonstrating the presence of both the 21–140 alphasyn and C-truncated alphasyn within the same fibrils.",21–140 and C-truncated alphasyn were co-aggregated to form mixed fibrils,NA,10.1074/jbc.RA118.005603,AG00303
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPS,KTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No information,"Yes, direct evidence.",Yes,NA,"21–140 and C-truncated alphasyn were co-aggregated to form mixed fibrils, which were immunolabeled with antibodies 4110 and 94-3A10 and then detected by secondary antibodies conjugated to 10- or 6-nm gold nanoparticles, respectively. Fibrils composed of either 21–140 + 1–115 alphasyn or 21–140 + 1–129 alphasyn are reactive to both antibodies 4110 (arrowheads) and 94-3A10 (arrows), demonstrating the presence of both the 21–140 alphasyn and C-truncated alphasyn within the same fibrils.",21–140 and C-truncated alphasyn were co-aggregated to form mixed fibrils,NA,10.1074/jbc.RA118.005603,AG00304
New1,New1,MPPKKFKDLNSFLDDQPKDPNLVASPFGGYFKNPAADAGSNNASKKSSYQQQRNWKQGGNYQQGGYQSYNSNYNNYNNYNNYNNYNNYNNYNKYNGQGYQKSTYKQSAVTPNQSGTPTPSASTTSLTSLNEKLSNLELTPISQFLSKIPECQSITDCKNQIKLIIEEFGKEGNSTGEKIEEWKIVDVLSKFIKPKNPSLVRESAMLIISNIAQFFSGKPPQEAYLLPFFNVALDCISDKENTVKRAAQHAIDSLLNCFPMEALTCFVLPTILDYLSSGAKWQAKMAALSVVDRIREDSANDLLELTFKDAVPVLTDVATDFKPELAKQGYKTLLDYVSILDNLDLSPRYKLIVDTLQDPSKVPESVKSLSSVTFVAEVTEPSLSLLVPILNRSLNLSSSSQEQLRQTVIVVENLTRLVNNRNEIESFIPLLLPGIQKVVDTASLPEVRELAEKALNVLKEDDEADKENKFSGRLTLEEGRDFLLDHLKDIKADDSCFVKPYMNDETVIKYMSKILTVDSNVNDWKRLEDFLTAVFGGSDSQREFVKQDFIHNLRALFYQEKERADEDEGIEIVNTDFSLAYGSRMLLNKTNLRLLKGHRYGLCGRNGAGKSTLMRAIANGQLDGFPDKDTLRTCFVEHKLQGEEGDLDLVSFIALDEELQSTSREEIAAALESVGFDEERRAQTVGSLSGGWKMKLELARAMLQKADILLLDEPTNHLDVSNVKWLEEYLLEHTDITSLIVSHDSGFLDTVCTDIIHYENKKLAYYKGNLAAFVEQKPEAKSYYTLTDSNAQMRFPPPGILTGVKSNTRAVAKMTDVTFSYPGAQKPSLSHVSCSLSLSSRVACLGPNGAGKSTLIKLLTGELVPNEGKVEKHPNLRIGYIAQHALQHVNEHKEKTANQYLQWRYQFGDDREVLLKESRKISEDEKEMMTKEIDIDDGRGKRAIEAIVGRQKLKKSFQYEVKWKYWKPKYNSWVPKDVLVEHGFEKLVQKFDDHEASREGLGYRELIPSVITKHFEDVGLDSEIANHTPLGSLSGGQLVKVVIAGAMWNNPHLLVLDEPTNYLDRDSLGALAVAIRDWSGGVVMISHNNEFVGALCPEQWIVENGKMVQKGSAQVDQSKFEDGGNADAVGLKASNLAKPSVDDDDSPANIKVKQRKKRLTRNEKKLQAERRRLRYIEWLSSPKGTPKPVDTDDEED,MPPKKFKDLNSFLDDQPKDPNLVASPFGGYFKNPAADAGSNNASKKSSYQQQRNWKQGGNYQQGGYQSYNSNYNNYNNYNNYNNYNNYNNYNKYNGQGYQKSTYKQSAVTPNQSGTPTPSASTTSLTSLNEKLSNLELTPISQFLSKIPECQSITDCKNQIKLIIEEFGKEGNSTGEKIEEWKIVDVLSKFIKPKNPSLVRESAMLIISNIAQFFSGKPPQEAYLLPFFNVALDCISDKENTVKRAAQHAIDSLLNCFPMEALTCFVLPTILDYLSSGAKWQAKMAALSVVDRIREDSANDLLELTFKDAVPVLTDVATDFKPELAKQGYKTLLDYVSILDNLDLSPRYKLIVDTLQDPSKVPESVKSLSSVTFVAEVTEPSLSLLVPILNRSLNLSSSSQEQLRQTVIVVENLTRLVNNRNEIESFIPLLLPGIQKVVDTASLPEVRELAEKALNVLKEDDEADKENKFSGRLTLEEGRDFLLDHLKDIKADDSCFVKPYMNDETVIKYMSKILTVDSNVNDWKRLEDFLTAVFGGSDSQREFVKQDFIHNLRALFYQEKERADEDEGIEIVNTDFSLAYGSRMLLNKTNLRLLKGHRYGLCGRNGAGKSTLMRAIANGQLDGFPDKDTLRTCFVEHKLQGEEGDLDLVSFIALDEELQSTSREEIAAALESVGFDEERRAQTVGSLSGGWKMKLELARAMLQKADILLLDEPTNHLDVSNVKWLEEYLLEHTDITSLIVSHDSGFLDTVCTDIIHYENKKLAYYKGNLAAFVEQKPEAKSYYTLTDSNAQMRFPPPGILTGVKSNTRAVAKMTDVTFSYPGAQKPSLSHVSCSLSLSSRVACLGPNGAGKSTLIKLLTGELVPNEGKVEKHPNLRIGYIAQHALQHVNEHKEKTANQYLQWRYQFGDDREVLLKESRKISEDEKEMMTKEIDIDDGRGKRAIEAIVGRQKLKKSFQYEVKWKYWKPKYNSWVPKDVLVEHGFEKLVQKFDDHEASREGLGYRELIPSVITKHFEDVGLDSEIANHTPLGSLSGGQLVKVVIAGAMWNNPHLLVLDEPTNYLDRDSLGALAVAIRDWSGGVVMISHNNEFVGALCPEQWIVENGKMVQKGSAQVDQSKFEDGGNADAVGLKASNLAKPSVDDDDSPANIKVKQRKKRLTRNEKKLQAERRRLRYIEWLSSPKGTPKPVDTDDEED,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1111/j.1365-2443.2011.01510.x,AG00308
Sup35,New1,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,MPPKKFKDLNSFLDDQPKDPNLVASPFGGYFKNPAADAGSNNASKKSSYQQQRNWKQGGNYQQGGYQSYNSNYNNYNNYNNYNNYNNYNNYNKYNGQGYQKSTYKQSAVTPNQSGTPTPSASTTSLTSLNEKLSNLELTPISQFLSKIPECQSITDCKNQIKLIIEEFGKEGNSTGEKIEEWKIVDVLSKFIKPKNPSLVRESAMLIISNIAQFFSGKPPQEAYLLPFFNVALDCISDKENTVKRAAQHAIDSLLNCFPMEALTCFVLPTILDYLSSGAKWQAKMAALSVVDRIREDSANDLLELTFKDAVPVLTDVATDFKPELAKQGYKTLLDYVSILDNLDLSPRYKLIVDTLQDPSKVPESVKSLSSVTFVAEVTEPSLSLLVPILNRSLNLSSSSQEQLRQTVIVVENLTRLVNNRNEIESFIPLLLPGIQKVVDTASLPEVRELAEKALNVLKEDDEADKENKFSGRLTLEEGRDFLLDHLKDIKADDSCFVKPYMNDETVIKYMSKILTVDSNVNDWKRLEDFLTAVFGGSDSQREFVKQDFIHNLRALFYQEKERADEDEGIEIVNTDFSLAYGSRMLLNKTNLRLLKGHRYGLCGRNGAGKSTLMRAIANGQLDGFPDKDTLRTCFVEHKLQGEEGDLDLVSFIALDEELQSTSREEIAAALESVGFDEERRAQTVGSLSGGWKMKLELARAMLQKADILLLDEPTNHLDVSNVKWLEEYLLEHTDITSLIVSHDSGFLDTVCTDIIHYENKKLAYYKGNLAAFVEQKPEAKSYYTLTDSNAQMRFPPPGILTGVKSNTRAVAKMTDVTFSYPGAQKPSLSHVSCSLSLSSRVACLGPNGAGKSTLIKLLTGELVPNEGKVEKHPNLRIGYIAQHALQHVNEHKEKTANQYLQWRYQFGDDREVLLKESRKISEDEKEMMTKEIDIDDGRGKRAIEAIVGRQKLKKSFQYEVKWKYWKPKYNSWVPKDVLVEHGFEKLVQKFDDHEASREGLGYRELIPSVITKHFEDVGLDSEIANHTPLGSLSGGQLVKVVIAGAMWNNPHLLVLDEPTNYLDRDSLGALAVAIRDWSGGVVMISHNNEFVGALCPEQWIVENGKMVQKGSAQVDQSKFEDGGNADAVGLKASNLAKPSVDDDDSPANIKVKQRKKRLTRNEKKLQAERRRLRYIEWLSSPKGTPKPVDTDDEED,No effect,No,No,NA,"(B) The effect of seeds on New1N amyloid formation. Closed circles and open triangles indicate New1N amyloid formation under the New1N-seeds and Sup35NM-seeds, respectively.",NA,NA,10.1111/j.1365-2443.2011.01510.x,AG00309
New1,Sup35,MPPKKFKDLNSFLDDQPKDPNLVASPFGGYFKNPAADAGSNNASKKSSYQQQRNWKQGGNYQQGGYQSYNSNYNNYNNYNNYNNYNNYNNYNKYNGQGYQKSTYKQSAVTPNQSGTPTPSASTTSLTSLNEKLSNLELTPISQFLSKIPECQSITDCKNQIKLIIEEFGKEGNSTGEKIEEWKIVDVLSKFIKPKNPSLVRESAMLIISNIAQFFSGKPPQEAYLLPFFNVALDCISDKENTVKRAAQHAIDSLLNCFPMEALTCFVLPTILDYLSSGAKWQAKMAALSVVDRIREDSANDLLELTFKDAVPVLTDVATDFKPELAKQGYKTLLDYVSILDNLDLSPRYKLIVDTLQDPSKVPESVKSLSSVTFVAEVTEPSLSLLVPILNRSLNLSSSSQEQLRQTVIVVENLTRLVNNRNEIESFIPLLLPGIQKVVDTASLPEVRELAEKALNVLKEDDEADKENKFSGRLTLEEGRDFLLDHLKDIKADDSCFVKPYMNDETVIKYMSKILTVDSNVNDWKRLEDFLTAVFGGSDSQREFVKQDFIHNLRALFYQEKERADEDEGIEIVNTDFSLAYGSRMLLNKTNLRLLKGHRYGLCGRNGAGKSTLMRAIANGQLDGFPDKDTLRTCFVEHKLQGEEGDLDLVSFIALDEELQSTSREEIAAALESVGFDEERRAQTVGSLSGGWKMKLELARAMLQKADILLLDEPTNHLDVSNVKWLEEYLLEHTDITSLIVSHDSGFLDTVCTDIIHYENKKLAYYKGNLAAFVEQKPEAKSYYTLTDSNAQMRFPPPGILTGVKSNTRAVAKMTDVTFSYPGAQKPSLSHVSCSLSLSSRVACLGPNGAGKSTLIKLLTGELVPNEGKVEKHPNLRIGYIAQHALQHVNEHKEKTANQYLQWRYQFGDDREVLLKESRKISEDEKEMMTKEIDIDDGRGKRAIEAIVGRQKLKKSFQYEVKWKYWKPKYNSWVPKDVLVEHGFEKLVQKFDDHEASREGLGYRELIPSVITKHFEDVGLDSEIANHTPLGSLSGGQLVKVVIAGAMWNNPHLLVLDEPTNYLDRDSLGALAVAIRDWSGGVVMISHNNEFVGALCPEQWIVENGKMVQKGSAQVDQSKFEDGGNADAVGLKASNLAKPSVDDDDSPANIKVKQRKKRLTRNEKKLQAERRRLRYIEWLSSPKGTPKPVDTDDEED,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,Faster aggregation,Yes; implied by kinetics.,Yes,"The seeds must be the sonicated fragments of New1N amyloid, as the addition of the same amount of New1N in nonamyloid state had no effect (results not shown).","(C) The effect of seeding on Sup35NM amyloid formation. Closed circles and open triangles indicate Sup35NM amyloid formation under the Sup35NM-seeds and New1N-seeds, respectively.","p35NM-seeds except by Sup35NM[New1N]-seeds. It appears that the Sup35NM[New1N] amyloid retains some conformational memory of the original New1N amyloid, which is recognized during subsequent New1N amyloid formation.",NA,10.1111/j.1365-2443.2011.01510.x,AG00310
IAPP,Tau,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,VQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQ,Faster aggregation,"Yes, direct evidence.",Yes,NA,"For the mixtures, in addition to all the peaks that correspond to R3 and IAPP, we observedtwo new peaks at n/z = (1 + 1)/+5, (1 + 1)/+7 that could beassigned to 1:1 hetero-oligomers of R3 and IAPP (Figure1A(iii)).We observed the formation of hetero-oligomers even with lower concentration of peptides (Figure S1). In-order to confirm/verify the composition of these hetero-oligomers, we carried out injection energy studies.34At higher injection energy, the hetero-oligomers are expected to dissociate back to their parent species.34Upon increasing the injection energy, we observed a drop in the signal for hetero-oligomers that was accompanied by an increase in the signal for monomeric R3(n/z = 1/+2, n/z = 1/+3) and IAPP (n/z = 1/+2) (Figure 1B,Figure S2).This set of data confirms that the peaks that we assigned to hetero-oligomers are indeed due to the hetero-oligomerization of R3 and IAPP.","For the mixtures, in addition to all the peaks that correspond to R3 and IAPP, we observedtwo new peaks at n/z = (1 + 1)/+5, (1 + 1)/+7 that could beassigned to 1:1 hetero-oligomers of R3 and IAPP (Figure1A(iii)).We observed the formation of hetero-oligomers even with lower concentration of peptides (Figure S1). In-order to confirm/verify the composition of these hetero-oligomers, we carried out injection energy studies.34At higher injection energy, the hetero-oligomers are expected to dissociate back to their parent species.34Upon increasing the injection energy, we observed a drop in the signal for hetero-oligomers that was accompanied by an increase in the signal for monomeric R3(n/z = 1/+2, n/z = 1/+3) and IAPP (n/z = 1/+2) (Figure 1B,Figure S2).This set of data confirms that the peaks that we assigned to hetero-oligomers are indeed due to the hetero-oligomerization of R3 and IAPP.",NA,10.1021/acschemneuro.9b00516,AG00311
Alpha-synuclein,S100A9,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,Faster aggregation,Yes; implied by kinetics.,Yes,"Indeed, co-aggregation of alpha-syn and S100A9 occurs significantly faster than amyloid formation of the individual proteins","Amyloid co-aggregation and cytotoxicity of S100A9 and alpha-syn. a Normalized kinetic curves of amyloid formation monitored by ThT fluorescence and fitted by sigmoidal function for 70 μM alpha-syn (in black), 70 μM S100A9 (blue), and both proteins taken at equimolar ratio (red). Experimental data points are shown in gray. b Lag phase (dark bars) and midpoint of growth phase (light bars) of the amyloid formation kinetics derived from fitting. Protein samples are indicated under the x-axis and in the same color coding as in a.","The co-aggregates of mixed S100A9 and alpha-syn, sampled at the oligomer and fibrillar stages, are significantly larger in size than the corresponding amyloid structures of the individual proteins (Fig. 5d–i), and this correlates with a reduction of S100A9 amyloid oligomer cytotoxicity (Fig. 5l).",NA,10.1186/s12974-018-1210-9,AG00312
S100A9,Alpha-synuclein,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,"Amyloid co-aggregation and cytotoxicity of S100A9 and alpha-syn. a Normalized kinetic curves of amyloid formation monitored by ThT fluorescence and fitted by sigmoidal function for 70 μM alpha-syn (in black), 70 μM S100A9 (blue), and both proteins taken at equimolar ratio (red). Experimental data points are shown in gray. b Lag phase (dark bars) and midpoint of growth phase (light bars) of the amyloid formation kinetics derived from fitting. Protein samples are indicated under the x-axis and in the same color coding as in a.","The co-aggregates of mixed S100A9 and alpha-syn, sampled at the oligomer and fibrillar stages, are significantly larger in size than the corresponding amyloid structures of the individual proteins (Fig. 5d–i), and this correlates with a reduction of S100A9 amyloid oligomer cytotoxicity (Fig. 5l).",NA,10.1186/s12974-018-1210-9,AG00313
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No,"As shown in Fig. 2a, when seeds of preformed alpha-synuclein amyloid fibril were present, fibrillation of alpha-synuclein was accelerated greatly; the 370-h lag time observed in the absence of seeds was abolished in the presence of 0.3, 0.5, 0.8, 1% (v/v) seeds, reflecting a typical seed (nucleus)-dependent fibril formation mechanism.","FITC-labeled alpha-synuclein, GroES, and lysozyme were prepared, and then amyloid fibrils were formed from these proteins. Each amyloid fibril was then sonicated to prepare seeds. The FITC-labeled seed proteins were then added to Cy5-labeled alpha-synuclein solution to form seeded alpha-synuclein fibrils. The seeded fibril formation was performer in sealed glass plates. As shown in Fig. 3, FITC-labeled seed proteins were observed as green fluorescent particles using a FITC long pass filter (Fig. 3, a, b, and c). When the same view was observed with a Cy5 filter, Cy5-labeled alpha-synuclein was observed as amyloid fibrils extending from these FITC-labeled seeds with a clear red color. Soluble Cy5-labeled alpha-synuclein was also seen in pale red as a background (Fig. 3, d, e, and f). With this filter, the FITC-labeled seed fibril was also illuminated slightly. This result suggests that alpha-synuclein could elongate in a bidirectional manner from the seeded nucleus.",NA,NA,10.1074/jbc.M508623200,AG00314
GroES,Alpha-synuclein,MNIRPLHDRVIVKRKEVETKSAGGIVLTGSAAAKSTRGEVLAVGNGRILENGEVKPLDVKVGDIVIFNDGYGVKSEKIDNEEVLIMSESDILAIVEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",Yes,"The lag time before fibril extension became shorter with increasing amounts of preformed seeds (1, 5, 10% v/v) for all three proteins.","FITC-labeled alpha-synuclein, GroES, and lysozyme were prepared, and then amyloid fibrils were formed from these proteins. Each amyloid fibril was then sonicated to prepare seeds. The FITC-labeled seed proteins were then added to Cy5-labeled alpha-synuclein solution to form seeded alpha-synuclein fibrils. The seeded fibril formation was performer in sealed glass plates. As shown in Fig. 3, FITC-labeled seed proteins were observed as green fluorescent particles using a FITC long pass filter (Fig. 3, a, b, and c). When the same view was observed with a Cy5 filter, Cy5-labeled alpha-synuclein was observed as amyloid fibrils extending from these FITC-labeled seeds with a clear red color. Soluble Cy5-labeled alpha-synuclein was also seen in pale red as a background (Fig. 3, d, e, and f). With this filter, the FITC-labeled seed fibril was also illuminated slightly. This result suggests that alpha-synuclein could elongate in a bidirectional manner from the seeded nucleus.","the structural characteristics of amyloid fibrils formed in the presence of various seed types were very similar to that of fibrils formed from alpha-synuclein-preformed seeds as observed by TEM, with the notable exception of fibril diameter. The diameter values of amyloid samples prepared from GroES fibril seeds (Fig. 2f) were 190 (+/-15). These values were significantly different from the value of 170 (+/-10) Å of fibril samples prepared from alpha-synuclein fibril seeds (Fig. 2e) and spontaneous fibrillation (Fig. 1d). Interestingly, each value was almost the same as that of the protein fibril seed (diameters: GroES fibrils, 200 (+/-20) Å). ; As shown in Fig. 4, TEM measurements indicated that both 10- and 40-nm gold particles were observed attached to a single amyloid fibril (Fig. 4b). (…) These results, taken together with the results from the fluorescence microscopy experiments in Fig. 3, clearly indicated that different proteins (seed) could be incorporated into a single amyloid fibril of alpha -synuclein.",NA,10.1074/jbc.M508623200,AG00315
Lysozyme,Alpha-synuclein,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No,"The lag time before fibril extension became shorter with increasing amounts of preformed seeds (1, 5, 10% v/v) for all three proteins.","FITC-labeled alpha-synuclein, GroES, and lysozyme were prepared, and then amyloid fibrils were formed from these proteins. Each amyloid fibril was then sonicated to prepare seeds. The FITC-labeled seed proteins were then added to Cy5-labeled alpha-synuclein solution to form seeded alpha-synuclein fibrils. The seeded fibril formation was performer in sealed glass plates. As shown in Fig. 3, FITC-labeled seed proteins were observed as green fluorescent particles using a FITC long pass filter (Fig. 3, a, b, and c). When the same view was observed with a Cy5 filter, Cy5-labeled alpha-synuclein was observed as amyloid fibrils extending from these FITC-labeled seeds with a clear red color. Soluble Cy5-labeled alpha-synuclein was also seen in pale red as a background (Fig. 3, d, e, and f). With this filter, the FITC-labeled seed fibril was also illuminated slightly. This result suggests that alpha-synuclein could elongate in a bidirectional manner from the seeded nucleus.",NA,NA,10.1074/jbc.M508623200,AG00317
Tau,Tubulin,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),Faster aggregation,Yes; implied by kinetics.,No information,"When 2.3 μm recombinant Tau (a microtubule-associated protein known to promote microtubule assembly) was incubated with 10 μm tubulin, microtubule assembly was detected as an increase in turbidity (Fig. 1A).",NA,NA,NA,10.1074/jbc.M116.736355,AG00318
Alpha-synuclein,Tubulin,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),No effect,No information,No information,sequence unavailable (protein complex),NA,NA,NA,10.1074/jbc.M116.736355,AG00319
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"For the Abeta42 aggregation reaction at a starting concentration of 10 μM, the monomer concentration drops over 50% within the first several hours, then continues to decline more slowly over the next three days, finally reaching apparent equilibrium at about 100 hrs (Fig. 1a, ●). The weight-normalized ThT signal produced by aliquots of this reaction correspondingly rise rapidly in the initial 24 hours, reaching a plateau within 60 hrs to a relatively high yield of ThT fluorescence of ~ 2.2 x 105 fluorescence units per µg (Fig. 1a, ○). The steady increase in weightnormalized ThT signal over the first 24 hrs suggests a transition through one or more intermediates with steadily increasing levels of ThT-sensitive beta-structure. Further detail is provided by EM (Fig. 2) and DLS (Fig. 3) analyses of reaction time points. After 1 hr, when 10% of the Abeta42 molecules have already been converted to sedimentable aggregates (Fig. 1a, ●), DLS reveals a broad distribution of particles centered at ~ 10 nm in hydrodynamic radius (Fig. 3b), and this is consistent with EM images showing lightly staining particles in the same size range (Fig. 2a). After 2 hrs, when about 30% of the Abeta42 molecules have been converted to aggregates (Fig. 1a, ●), most particles take up slightly more stain (Fig. 2b) and many have more clearly defined boundaries (Fig. 2c). By 8 hrs, when about of 60% of Abeta42 molecules are aggregated, EM analysis shows two types of oligomeric intermediate: narrow, positively stained filaments (Fig. 2d) and globular and wormlike negatively stained aggregates (Fig. 2e",NA,NA,NA,10.1016/j.jmb.2015.06.008,AG00320
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAPGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,"Many tiny or short fibrils were observed in A30Pseeds, whereas relatively long fibrils were predominantly detected in WT, E46K, and A53T seeds(Fig. 2A,v,vi,vii, and viii). This observation was confirmed by measuring the fibril length in these seeds. Short fibrils of less than 100 nm were predominant in the A30P seeds, whereas longer fibrils were detected in the WT and A53T seeds",NA,10.1074/jbc.M807482200,AG00321
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKKGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1074/jbc.M807482200,AG00322
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1074/jbc.M807482200,AG00323
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1074/jbc.M807482200,AG00324
Amyloid beta,Amyloid beta,EFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1016/j.peptides.2009.01.027,AG00325
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,EFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1016/j.peptides.2009.01.027,AG00326
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Conversion of IAPP (6.25 μM, pH 7.4) into fibrils was accomplished within 2–4 h. In the presence of IAPP-GI (1∕1), however, fibril formation was completely suppressed (14 days) ( Fig. 6A).; IAPP-GI completely interrupted IAPP fibrillization (at 1∕1) regardless of the stage of the process, i.e., when added both before and after nucleation.","Conversion of IAPP (6.25 μM, pH 7.4) into fibrils was accomplished within 2–4 h. In the presence of IAPP-GI (1∕1), however, fibril formation was completely suppressed (14 days) ( Fig. 6A).","Conversion of IAPP (6.25 μM, pH 7.4) into fibrils was accomplished within 2–4 h. In the presence of IAPP-GI (1∕1), however, fibril formation was completely suppressed (14 days) ( Fig. 6A).",NA,10.1073/pnas.0507471103,AG00327
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,"However, when Abeta42 is incubated with M-TTR, the aggregates formed are non-fibrillar",NA,10.1002/pro.3396,AG00328
IAPP,Amyloid beta,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"In this context, we have shown using both TEM and the ThT assay that Ab40 fibrillogenesis is completely blocked by full-length IAPP-GI.",NA,NA,NA,10.1002/cbic.201100192,AG00329
IAPP,Amyloid beta,KCNTATC,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,IAPP(1–7) and IAPP(30–37) also did not significantly interfere with Ab40 fibrillogenesis,NA,NA,NA,10.1002/cbic.201100192,AG00330
IAPP,Amyloid beta,NVGSNTY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1002/cbic.201100192,AG00331
IAPP,Amyloid beta,ATQRLANFLVHSSNNFGAILS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1002/cbic.201100192,AG00332
Bri2,IAPP,QTIEENIKIFEEEEVEFISVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPRNLLELLINIKAGTYLPQSYLIHEHMVITDRIENIDHLGFFIYRLCHDKETYKL,SEQUENCEUNAVAILABLE,No aggregation,Formation of fibrils by the interactee is inhibited,No,IAPP alone formed fibrils after ∼1.5-h-long lag phase whereas fibril formation was completely abolished in the presence of Bri2 BRICHOS; Addition of Bri2 BRICHOS at a 1:1 ratio to IAPP from the start or during the lag phase revealed complete inhibition of fibril formation (Fig. 5A). Addition during the elongation phase resulted in an abrupt flattening of the ThT curve. At higher IAPP concentrations (10:1 ratio) only addition of Bri2 BRICHOS from the start could completely prevent fibril formation during the analyzed time period.,NA,NA,NA,10.1073/pnas.1715951115,AG00334
Bri2,IAPP,QTIEENIKIFEEEEVEFISVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPRNLLELLINIKAGTYLPQSYLIHEHMVITDRIENIDHLGFFIYRLCHDKETYKL,SEQUENCEUNAVAILABLE,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,Addition during lag phase at a 10:1 ratio resulted in delayed fibril formation from ∼1 h to >15 h,NA,NA,NA,10.1073/pnas.1715951115,AG00335
Bri2,IAPP,QTIEENIKIFEEEEVEFISVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPRNLLELLINIKAGTYLPQSYLIHEHMVITDRIENIDHLGFFIYRLCHDKETYKL,SEQUENCEUNAVAILABLE,No effect,No information,No information,"At higher IAPP concentrations (10:1 ratio) only addition of Bri2 BRICHOS from the start could completely prevent fibril formation during the analyzed time period. Addition during lag phase at a 10:1 ratio resulted in delayed fibril formation from ∼1 h to >15 h, and addition during elongation phase had no inhibiting effect (Fig. 5B).",NA,NA,NA,10.1073/pnas.1715951115,AG00336
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No information,"Yes, direct evidence.",No,NA,"As the three-line component is a result of interlacing between unlabeled and labeled Ab in the fibrils, the ratio of the three-line component populations in Ab40- versus Ab42-diluted samples can be used as an estimate for the relative efficiency of incorporating Ab40 into Ab42 fibrils. Using the data from Fig. 3b, the efficiency of incorporating Ab40 into Ab42 fibrils, relative to incorporating Ab42 into Ab42 fibrils, is 58% (= 31%/53%). In other words, when mixing Ab40 and Ab42 at 1 : 1 ratio, approximately 58% Ab40 proteins are forming interlaced fibrils with Ab42, and the remaining 42% forms Ab40-only fibrils.",NA,NA,10.1111/jnc.12202,AG00337
Tau,Alpha-synuclein,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,"The lag phase became shorter, when tau K18 and alpha-syn were mixed (Fig. 1c).",NA,NA,NA,10.1016/j.jmb.2018.04.020,AG00338
Alpha-synuclein,Tau,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1016/j.jmb.2018.04.020,AG00339
Tau,Alpha-synuclein,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAPGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,"Our results show that the aggregation kinetics of the PD mutant, A30P, is significantly accelerated by the addition of tau K18.",NA,NA,NA,10.1016/j.jmb.2018.04.020,AG00340
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,The aggregation of Abeta(1–42) was reduced in the presence of TTR,NA,NA,NA,10.1021/acs.jmedchem.9b01970,AG00341
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,VHHQKLVFFAEDVGSNK,No aggregation,Formation of fibrils by the interactee is inhibited,No,"This ultrastructural analysis showed that the presence of TTR clearly prevented Abeta(12–28) fibrillization, resulting in the presence of fewer, less complex fibrils and small aggregates (Figure 6D), compared to the control, the Abeta(12–28) alone (Figure 6A–C), which presented long and complex fibrils.","This ultrastructural analysis showed that the presence of TTR clearly prevented Abeta(12–28) fibrillization, resulting in the presence of fewer, less complex fibrils and small aggregates (Figure 6D), compared to the control, the Abeta(12–28) alone (Figure 6A–C), which presented long and complex fibrils.",NA,NA,10.1021/acs.jmedchem.9b01970,AG00342
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,TEM confirmed that no fibrils were formed when AB1–40 was coincubated with any of the TTRs at high concentrations (25 M TTR/25 M A1–40; Fig. 1B),NA,NA,NA,10.1523/JNEUROSCI.2561-13.2013,AG00343
Transthyretin,Amyloid beta,MASLRLFLLCLAGLVFVSEAGPAGAGESKCPLMVKVLDAVRGSPAVDVAVKVFKKTSEGSWEPFASGKTAESGELHGLTTDEKFVEGVYRVELDTKSYWKTLGISPFHEFADVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPQN,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,TEM confirmed that no fibrils were formed when A1–40 was coincubated with any of the TTRs at high concentrations (25 M TTR/25 M A1–40; Fig. 1B).,NA,NA,NA,10.1523/JNEUROSCI.2561-13.2013,AG00344
Transthyretin,Amyloid beta,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTMAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,TEM confirmed that no fibrils were formed when A1–40 was coincubated with any of the TTRs at high concentrations (25 M TTR/25 M A1–40; Fig. 1B),NA,NA,NA,10.1523/JNEUROSCI.2561-13.2013,AG00345
Transthyretin,Amyloid beta,GPTGTGESKCPLMVAVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,TEM confirmed that no fibrils were formed when A1–40 was coincubated with any of the TTRs at high concentrations (25 M TTR/25 M A1–40; Fig. 1B).,NA,NA,NA,10.1523/JNEUROSCI.2561-13.2013,AG00346
Transthyretin,Amyloid beta,GPTGTGESKCPLMVKVLDAVRGSPAINVAMHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,TEM confirmed that no fibrils were formed when A1–40 was coincubated with any of the TTRs at high concentrations (25 M TTR/25 M A1–40; Fig. 1B).,NA,NA,NA,10.1523/JNEUROSCI.2561-13.2013,AG00347
Transthyretin,Amyloid beta,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,TEM confirmed that no fibrils were formed when A1–40 was coincubated with any of the TTRs at high concentrations (25 M TTR/25 M A1–40; Fig. 1B).,NA,NA,NA,10.1523/JNEUROSCI.2561-13.2013,AG00348
Transthyretin,Amyloid beta,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPMHEHAEVVFTANDSGPRRYTIAAMLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,TEM confirmed that no fibrils were formed when A1–40 was coincubated with any of the TTRs at high concentrations (25 M TTR/25 M A1–40; Fig. 1B).,NA,NA,NA,10.1523/JNEUROSCI.2561-13.2013,AG00349
S100A9,Amyloid beta,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"In the presence of 3 µM non-aggregating S100A9, Abeta42 amyloid formation is delayed, as reflected in an increased lag-phase and decreased both growth phase slope and ThT plateau level (Fig. 4A). 30 µM seeds lead to some delay in amyloid formation and decrease in ThT fluorescence plateau (Fig. 4D).",NA,NA,NA,10.1039/C9SC05905A,AG00350
S100A9,Amyloid beta,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1039/C9SC05905A,AG00351
S100A9,Amyloid beta,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No,No,"The effects of the same concentrations of S100A9 fibrillar species on Abeta42 fibrillation is less pronounced, i.e. 3 µM S100A9 fibrillar seeds do not significantly perturb the Abeta42 fibrillation",NA,NA,NA,10.1039/C9SC05905A,AG00352
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,No information,No,"Co-incubation of Abeta42 with 3% Abeta42 fibrils produces pronounced seeding effect on Abeta42 fibrillation, effectively abolishing the lagphase and inducing mature fibril formation",NA,NA,NA,10.1039/C9SC05905A,AG00353
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1039/C9SC05905A,AG00354
Amyloid beta,S100A9,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,No effect,No,No,NA,NA,NA,NA,10.1039/C9SC05905A,AG00355
S100A9,S100A9,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,No effect,No,No,NA,NA,NA,NA,10.1039/C9SC05905A,AG00356
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,RHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,3 μM Abeta (1–42) monomers / 3 μM Abeta (5–42) monomers,10.1021/acschemneuro.8b00676,AG00357
Amyloid beta,Amyloid beta,RHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,3 μM Abeta (5–42) monomers / 3 μM Abeta (1–42) monomers,10.1021/acschemneuro.8b00676,AG00358
Amyloid beta,Amyloid beta,RHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,"1,5 μM Abeta (5–42) monomers / 1,5 μM Abeta (1–42) monomers",10.1021/acschemneuro.8b00676,AG00359
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,RHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,https://drive.google.com/open?id=1CX1TreA34X0V6SSffmP0ocNAMrsaZY8T,NA,NA,"1,5 μM Abeta (1–42) monomers / 1,5 μM Abeta (5–42) monomers",10.1021/acschemneuro.8b00676,AG00360
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Abeta (1–42) seeds / 2 μM Abeta (1–42) monomer Seeds = preformed fibrils,10.1021/acschemneuro.8b00676,AG00361
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,RHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Abeta (1–42) seeds / 2 μM Abeta (5–42) monomer Seeds = preformed fibrils,10.1021/acschemneuro.8b00676,AG00362
Amyloid beta,Amyloid beta,RHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,"Abeta (5–42) seeds 0,01% & 0,1%-10% / 2 μM Abeta (1–42) monomer (no effect for 0,03% seeds) Seeds = preformed fibrils",10.1021/acschemneuro.8b00676,AG00363
Amyloid beta,Amyloid beta,RHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,RHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,No,No,NA,"By contrast, the effect of Abeta42 seeds on Abeta5−42 aggregation cannot be explained with this simple model (Figure 4B). Most notably, the slope of the aggregation curves, determined by the elongation and secondary nucleation rates of the growing fibrils, increases with increasing Abeta42 seed amount. This observation indicates that the fibrils formed from Abeta5−42 monomers, in the presence of 0.1% or more of Abeta42 seeds, differ significantly from those formed from pure Abeta5−42 monomer. Fits using different models trying to describe this behavior are shown in Supporting Information Figures S7 and S8. The fact that the slope of the aggregation curves increases continuously as the seed concentration is increased, as reflected by the increase in k2 when fitted to the curves individually (Figure S8), implies that the Abeta42 seeds induce the formation of a new type of Abeta5−42 fibrils, which are not formed directly from Abeta5−42 monomers and have a higher propensity to self-replicate.",NA,"Abeta (5–42) seeds 0,3%-10% / 2 μM Abeta (5–42) monomer Seeds = preformed fibrils",10.1021/acschemneuro.8b00676,AG00364
Amyloid beta,Amyloid beta,RHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,RHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No,NA,NA,NA,"Abeta (5–42) seeds 0,01%-0,1% / 2 μM Abeta (5–42) monomer Seeds = preformed fibrils",10.1021/acschemneuro.8b00676,AG00365
Alpha-crystallin,Kappa-casein,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYG LNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHP HPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEI NTVQVTSTAV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,"bovine alpha-crystallin / bovine kappa-casein; reducing conditions, 37°C & 50°C",10.1111/j.1742-4658.2007.06144.x,AG00366
Alpha-crystallin,Kappa-casein,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYG LNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHP HPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEI NTVQVTSTAV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,"bovine alpha-crystallin / bovine kappa-casein; nonreducing conditions, 55°C",10.1111/j.1742-4658.2007.06144.x,AG00367
Alpha-crystallin,Kappa-casein,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYG LNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHP HPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEI NTVQVTSTAV,No effect,No information,No information,NA,NA,NA,"bovine alpha-crystallin / bovine kappa-casein; nonreducing conditions, 37°C, +0.25x & +0.5x alpha-crystallin",10.1111/j.1742-4658.2007.06144.x,AG00368
Alpha-crystallin,Kappa-casein,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYG LNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHP HPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEI NTVQVTSTAV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,"bovine alpha-crystallin / bovine kappa-casein; nonreducing conditions, 37°C, +1x alpha-crystallin",10.1111/j.1742-4658.2007.06144.x,AG00369
Alpha-crystallin,Alpha-synuclein,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,"human alphaB-crystallin / human alphaSyn; 37°C & 45°C & 60°C, + +0.5x & +1x alphaB-crystallin",10.1111/j.1742-4658.2007.06144.x,AG00370
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,WT and all truncated alphaS fibrils induced the aggregation of FL alphaS protein,NA,NA,NA,10.1074/jbc.RA118.001862,AG00371
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSE,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,WT and all truncated alphaS fibrils induced the aggregation of FL alphaS protein,NA,NA,Interactions between Human FL (full length) and truncated alphaS fibril seeds. Here C-terminally truncated alphaS (ΔC10: residues 1–130) as interactor,10.1074/jbc.RA118.001862,AG00372
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,WT and all truncated alphaS fibrils induced the aggregation of FL alphaS protein,NA,NA,Interactions between Human FL (full length) and truncated alphaS fibril seeds. Here C-terminally truncated alphaS (ΔC20: residues 1–120) as interactor,10.1074/jbc.RA118.001862,AG00373
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQE,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,WT and all truncated alphaS fibrils induced the aggregation of FL alphaS protein,NA,NA,Interactions between Human FL (full length) and truncated alphaS fibril seeds. Here C-terminally truncated alphaS (ΔC30: residues 1–110) as interactor,10.1074/jbc.RA118.001862,AG00374
Alpha-synuclein,Alpha-synuclein,AKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,WT and all truncated alphaS fibrils induced the aggregation of FL alphaS protein,NA,NA,"Interactions between Human FL (full length) and truncated alphaS fibril seeds. Here, N-terminally truncated alphaS (ΔN10: residues 11–140) as interactor",10.1074/jbc.RA118.001862,AG00375
Alpha-synuclein,Alpha-synuclein,KTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,WT and all truncated alphaS fibrils induced the aggregation of FL alphaS protein,NA,NA,Interactions between Human FL (full length) and truncated alphaS fibril seeds. Here N-terminally truncated alphaS (ΔN20: residues 21–140) as interactor,10.1074/jbc.RA118.001862,AG00376
Alpha-synuclein,Alpha-synuclein,GKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,WT and all truncated alphaS fibrils induced the aggregation of FL alphaS protein,NA,NA,Interactions between Human FL (full length) and truncated alphaS fibril seeds. Here N-terminally truncated alphaS (ΔN30: residues 31–140) as interactor,10.1074/jbc.RA118.001862,AG00377
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDIKIMERVVEQMCTTQYQKESQAYYDGRRS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,"When 2.5µM of full-length PrP(23–231) was added at the start of the reaction, theThT signal was completely suppressed for Abeta42 and greatly reduced for Abeta42Arc (Fig. 4, A and B, red traces). Under these conditions, TEM revealed largely the presence of spherical oligomeric Abeta assemblies typically 10–20 nm in diameter (Fig. 4, E and F).",NA,NA,2.5µM of full-length PrP (23-231) / Abeta42 monomers,10.1074/jbc.RA118.003319,AG00387
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDIKIMERVVEQMCTTQYQKESQAYYDGRRS,DAEFRHDSGYEVHHQKLVFFAGDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"When 2.5µM of full-length PrP(23–231) was added at the start of the reaction, theThT signal was completely suppressed for Abeta42 and greatly reduced for Abeta42Arc (Fig. 4, A and B, red traces). Under these conditions, TEM revealed largely the presence of spherical oligomeric Abeta assemblies typically 10–20 nm in diameter (Fig. 4, E and F).","Under these conditions, TEM revealed largely the presence of spherical oligomeric Abeta assemblies typically 10–20 nm in diameter (Fig. 4, E and F).",NA,2.5µM of full-length PrP (23-231) / Abeta42Arc monomers,10.1074/jbc.RA118.003319,AG00388
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDIKIMERVVEQMCTTQYQKESQAYYDGRRS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"Furthermore, the addition of 5 µM PrP(23–231) to a preparation of Abeta-amyloid fibers resulted in a 40–50% reduction in the ThT fluorescence signal, suggesting disruption of the preformed fibrils.","Furthermore, the addition of 5 µM PrP(23–231) to a preparation of Abeta-amyloid fibers resulted in a 40–50% reduction in the ThT fluorescence signal, suggesting disruption of the preformed fibrils.",NA,"5 µM PrP(23–231) / Abeta42 mature fibers; PrP(23–231) was added to a preparation of Abeta-amyloid fibers in some point, highlighted with an arrow in Figure 4 A and B",10.1074/jbc.RA118.003319,AG00389
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDIKIMERVVEQMCTTQYQKESQAYYDGRRS,DAEFRHDSGYEVHHQKLVFFAGDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"Furthermore, the addition of 5 µM PrP(23–231) to a preparation of Abeta-amyloid fibers resulted in a 40–50% reduction in the ThT fluorescence signal, suggesting disruption of the preformed fibrils.",NA,NA,"5 µM PrP(23–231) / Abeta42Arc mature fibers; PrP(23–231) was added to a preparation of Abeta-amyloid fibers in some point, highlighted with an arrow in Figure 4 A and B",10.1074/jbc.RA118.003319,AG00390
Tau,Amyloid beta,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,GSNKGAIIGLM,Slower aggregation,Formation of fibrils by the interactee is inhibited,Yes,The co-incubation of tau with the Abpeptide under non-reducing condition resulted in the decreased aggregated forms of Ab25–3,NA,"ore interestingly, for the co-incu- bated samples, the morphology and size of the fragments were different with the individual fragments and the new formed annular protofibrils with the average diameter and height of 48 and 1.6 nm, respect- ively, were detected",NA,10.1093/jb/mvaa101,AG00391
Transthyretin,Transthyretin,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,No effect,No,No,TTR fibrils did not induce any increase in fluorescence signal when incubated with newly dissolved TTR or solubilized IAPP,NA,NA,NA,10.1155/2008/429274,AG00392
IAPP,Transthyretin,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1155/2008/429274,AG00393
Transthyretin,IAPP,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No,No,TTR fibrils did not induce any increase in fluorescence signal when incubated with newly dissolved TTR or solubilized IAPP,NA,NA,NA,10.1155/2008/429274,AG00394
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1155/2008/429274,AG00395
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,"Yes, direct evidence.",No information,NA,"By using SPR, we evaluated the ability of immobilized fibrils of Abeta1–40 and 1–42 to template free monomers of either the same or the other primary sequence (...) In our cross-templating studies, we found that Abeta1–42 monomers were readily incorporated into Abeta1–40 fibrils with kinetics and affinities that were similar to their homo-paired counterparts (Fig. 1c and d).",NA,NA,10.1016/j.jmb.2018.05.001,AG00396
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No information,No,No information,NA,"We show here that monomeric Abeta1–42 can be cross-templated and incorporated into the ends of Abeta1–40 fibrils, while incorporation of Abeta1–40 monomers into Abeta1–42 fibrils is very poor.",NA,NA,10.1016/j.jmb.2018.05.001,AG00397
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,Fig. 3a shows the progress of the reactions when Abeta1–40 monomers are mixed in solution with different concentrations of Abeta1–40 fibrils,NA,NA,NA,10.1016/j.jmb.2018.05.001,AG00398
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,No,No information,NA,NA,NA,NA,10.1016/j.jmb.2018.05.001,AG00399
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1016/j.jmb.2018.05.001,AG00400
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"However, Fig. 3d illustrates how monomers of Abeta1–42 where readily seeded in solution by fibrils of Abeta1–40 and expose a significant and seed-dependent reduction of the lag-phase.",NA,NA,NA,10.1016/j.jmb.2018.05.001,AG00401
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,The formation of new fibrils is thus strongly enhanced by the presence of seed fibrils,NA,NA,NA,10.1017/S0033583516000172,AG00402
Amyloid beta,Tau,KLVFFAENVGS,RPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVS,Faster aggregation,Yes; implied by kinetics.,No information,"We tested seeding of the microtubule binding domain of tau, K18 + (244-380) in a ThT assay at 37˚C under shaking conditions and found that fibrils of Ab1-42 and Ab16- 26 D23N seeded aggregation, though not as efficiently as fibrils of K18",NA,NA,NA,10.7554/eLife.46924,AG00403
Tau,Tau,RPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVS,RPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVS,Faster aggregation,Yes; implied by kinetics.,No,"We tested seeding of the microtubule binding domain of tau, K18 + (244-380) in a ThT assay at 37˚C under shaking conditions and found that fibrils of Ab1-42 and Ab16- 26 D23N seeded aggregation, though not as efficiently as fibrils of K18",NA,NA,NA,10.7554/eLife.46924,AG00404
Amyloid beta,Tau,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,RPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVS,Faster aggregation,Yes; implied by kinetics.,No information,"We tested seeding of the microtubule binding domain of tau, K18 + (244-380) in a ThT assay at 37˚C under shaking conditions and found that fibrils of Ab1-42 and Ab16- 26 D23N seeded aggregation, though not as efficiently as fibrils of K18",NA,NA,NA,10.7554/eLife.46924,AG00405
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.7554/eLife.46924,AG00406
Tau,Amyloid beta,RPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.7554/eLife.46924,AG00407
Serum amyloid A,Serum amyloid A,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.3109/13506129.2011.630761 ,AG00408
Medin,Serum amyloid A,RLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQFVA,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),Faster aggregation,Yes; implied by kinetics.,No information,"Interestingly, also aggregated medin had this ability to seed AA fibrillogenesis",NA,NA,NA,10.3109/13506129.2011.630761,AG00409
Serum amyloid A,Medin,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),RLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQFVA,No effect,No information,No information,AA amyloid-like fibrils did not accelerate AMed amyloid formation (data not shown),NA,NA,NA,10.3109/13506129.2011.630761,AG00410
Medin,Medin,RLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQFVA,RLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQFVA,Faster aggregation,No information,No,NA,NA,NA,NA,10.3109/13506129.2011.630761,AG00411
Transthyretin,IAPP,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKV EIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,The results show that TTR can prolong the lag-phase as well as impair elongation in the course of IAPP-amyloid formation.,NA,NA,"interactor: TTR 500nM, 250nM, 125nM, 62nM interactee: IAPP µM",10.3390/biom11030411,AG00412
FapC,Amyloid beta,MKPTMALKPLVFALAALMAVAAQAGPAEKWKPTPAPTGTVAAAVTDTQVSKDNKFDDTKT LNNAGANGSLSNSKGNLGANIAAGSGNQQDNAAAITSSAGDAATVFAVADIYQESKDNKF TNKGTQNNALLNNSANNSSGNVGVNVAAGQGNQQKNNLAIVTADGKNVAAASNTEQVSLD NHFLNEASSKHSYKPQYVVNNAGLLNSANNASGNIGVNVAAGAGNQQSNTLTLGSGCTVC AAGTGSKLAF,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,"Yes, direct evidence.",Yes,"addition to that, the physical presence of FapC monomers and fibrils could reduce mutual A𝛽–A𝛽 interactions to slow down the peptide fibrillization. Specifically, the fibrillization rate constant (k) of A𝛽 was markedly increased from 0.7 to 1.6 h−1 in the presence of FapCS (Figure 1B), while the lag time of A𝛽 was essentially abolished and the fibrillization half-life was decreased by 86% (Figure 1C,D). Static light scattering (SLS) also reflected a significantly more rapid A𝛽 fibrillar growth when incubated with FapCS (Figure 1E).","Our simulations demonstrated that FapC had several A𝛽- binding hotspots scattered along the protein sequence, among which only FapC41-50 was amyloidogenic to allow incorporation of A𝛽 into the corresponding nanofibril, i.e., seeding the fibrillization of A𝛽. These results were consistent with the experimental observation that a fraction of FapCS was incorporated into A𝛽 fibrils while other FapCS adsorbed to the sides of A𝛽 fibrils. Together, our computational and experimental results suggested that the exposed surfaces of FapCS upon sonication were likely heterogeneous and only a subset of FapCS with the “seedingcompetent” hotspots exposed could nucleate the formation of A𝛽 fibrils, while the rest bound to A𝛽 via other hotspot sequences.","Our simulations demonstrated that FapC had several A𝛽- binding hotspots scattered along the protein sequence, among which only FapC41-50 was amyloidogenic to allow incorporation of A𝛽 into the corresponding nanofibril, i.e., seeding the fibrillization of A𝛽. These results were consistent with the experimental observation that a fraction of FapCS was incorporated into A𝛽 fibrils while other FapCS adsorbed to the sides of A𝛽 fibrils. Together, our computational and experimental results suggested that the exposed surfaces of FapCS upon sonication were likely heterogeneous and only a subset of FapCS with the “seedingcompetent” hotspots exposed could nucleate the formation of A𝛽 fibrils, while the rest bound to A𝛽 via other hotspot sequences.Only in one out of the ten independent simulations A𝛽 stayed on the lateral surface of the FapC nanofibril. As a result, the probability distribution of center-of-mass (COM) distances between the A𝛽 monomers and the FapC41-50 nanofibril featured three peaks (Figure 2D), where the highest peak corresponded to binding of the peptide at the two nanofibril ends.","FapC seeds (FapCS) propagated their structural characteristics and acted as a catalyst for promoting A𝛽 amyloidogenesis in vitro, in silico and in a zebrafish AD model.",10.1002/advs.202001299,AG00415
Sup35,Amyloid beta,GNNQQNY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,"Yes, direct evidence.",Yes,"When incubating non-amylogenic GNNQQNY (15 μM) with Abeta at 1 : 1 and 1 : 2 molar ratios, GNNQQNY clearly promoted Abeta fibrillization as judged by the increase of Imax from 207 to 295 at a 1 : 1 ratio and from 344 to 522 at a 1 : 2 ratio (Abeta at 2-fold excess).",GNNQQNY cross-seeds with Abeta to promote amyloid fibrillization,"Higher concentration of Abeta, due to its fast aggregation nature, tends to form homogenous seeds with non-detectable influence by GNNQQNY, and then the dominant Abeta seeds serve as structural templates to recruit GNNQQNY monomers to form hybrid GNNQQNY-Abeta fibrils at the later aggregation stage.","GNNQQNY – a short fragment from yeast prion protein Sup35 – can cross-seed with both amyloid-b (Ab, associated with Alzheimer’s disease) and human islet amyloid polypeptide (hIAPP, associated with type II diabetes) to form b-structure-rich assemblies and to accelerate amyloid fibrillization.",10.1039/D0TB02958K,AG00416
Sup35,IAPP,GNNQQNY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,"Yes, direct evidence.",Yes,"The ThT kinetic curves in Fig. 2a show the typical sigmoidal increase of amyloid aggregation for both pure hIAPP and GNNQQNY-hIAPP cases, consistent with the amyloid nucleation-polymerization model.",GNNQQNY cross-seeds with hIAPP to promote amyloid fibrillization,"AFM images of pure hIAPP (15 μM) and hybrid GNNQQNY-hIAPP (15 μM : 15 μM) aggregates at different aggregation times of 6, 12, and 24 h",NA,10.1039/D0TB02958K,AG00417
Sup35,Amyloid beta,GNNAQNY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,"Yes, direct evidence.",No,"Furthermore, co-incubation of non-amyloidogenic Q4A (15 μM) with either Abeta (15 μM) or hIAPP (15 μM) did not enable cross-seeding, instead it resulted in similar aggregation kinetics to pure Abeta (Fig. 6d) or pure hIAPP (Fig. 6e).","Furthermore, co-incubation of non-amyloidogenic Q4A (15 μM) with either Abeta (15 μM) or hIAPP (15 μM) did not enable cross-seeding, instead it resulted in similar aggregation kinetics to pure Abeta (Fig. 6d) or pure hIAPP (Fig. 6e).","Furthermore, co-incubation of non-amyloidogenic Q4A (15 μM) with either Abeta (15 μM) or hIAPP (15 μM) did not enable cross-seeding, instead it resulted in similar aggregation kinetics to pure Abeta (Fig. 6d) or pure hIAPP (Fig. 6e).",NA,10.1039/D0TB02958K,AG00418
Sup35,IAPP,GNNAQNY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,No,No information,"Furthermore, co-incubation of non-amyloidogenic Q4A (15 μM) with either Abeta (15 μM) or hIAPP (15 μM) did not enable cross-seeding, instead it resulted in similar aggregation kinetics to pure Abeta (Fig. 6d) or pure hIAPP (Fig. 6e",NA,NA,NA,10.1039/D0TB02958K,AG00419
Sup35,Amyloid beta,GNNQQNY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"addition of GNNQQNY to 1 h Abeta seeds promoted ThT intensity significantly and immediately, indicating that Abeta seeds can efficiently cross-seed GNNQQNY and promote their aggregation",NA,NA,"Adding GNNQQNY (15 μM) to preformed Abeta (15 μM) seeds formed at different aggregation stage. Here, addition of GNNQQNY to 1 h (lag phase) Abeta seeds",10.1039/D0TB02958K,AG00420
Sup35,Amyloid beta,GNNQQNY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"cross-seeding of GNNQQNY with 5 h Abeta seeds at the growth phase also promoted fibril formation, but in a much less efficient way",NA,NA,"Adding GNNQQNY (15 μM) to preformed Abeta (15 μM) seeds formed at different aggregation stage. Here, addition of GNNQQNY to 5 h (growth phase) Abeta seeds.",10.1039/D0TB02958K,AG00421
Sup35,Amyloid beta,GNNQQNY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No,No information,"This less cross-seeding efficiency became more pronounced when adding GNNQQNY to preformed Abeta fibrils (14 h), leading to almost no change in the ThT curve.",NA,NA,"Adding GNNQQNY (15 μM) to preformed Abeta (15 μM) seeds formed at different aggregation stage. Here, addition of GNNQQNY to 14 h (early equilibrium phase) Abeta seeds.",10.1039/D0TB02958K,AG00422
Sup35,IAPP,GNNQQNY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,"It can be seen in Fig. 3b that after adding GNNQQNY to the 5 h seeded hIAPP solution at the lag-phase, the cross-seeding aggregation remained in the lag phase for ∼1 h, followed by a rapid increase of aggregation at the growth phase between 6–10 h, and finally promoted fibril formation with a 96% increase in Imax.",NA,NA,"Adding GNNQQNY (15 μM) to preformed hIAPP (15 μM) seeds formed at different aggregation stage. Here, addition of GNNQQNY to 5 h (lag phase) hIAPP seeds",10.1039/D0TB02958K,AG00423
Sup35,IAPP,GNNQQNY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"Adding GNNQQNY (15 μM) to preformed hIAPP (15 μM) seeds formed at different aggregation stage. Here, addition of GNNQQNY to 12 h (growth phase) hIAPP seeds.",10.1039/D0TB02958K,AG00424
Sup35,IAPP,GNNQQNY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No,No information,"However, hIAPP mature fibrils lost their ability to cross-seed GNNQQNY, as judged by the almost same ThT kinetic curves of cross-seeding of GNNQQNY with 18 h hIAPP fibrils as that of pure hIAPP aggregation.","However, hIAPP mature fibrils lost their ability to cross-seed GNNQQNY, as judged by the almost same ThT kinetic curves of cross-seeding of GNNQQNY with 18 h hIAPP fibrils as that of pure hIAPP aggregation.",NA,"Adding GNNQQNY (15 μM) to preformed hIAPP (15 μM) seeds formed at different aggregation stage. Here, addition of GNNQQNY to 18 h (early equilibrium phase) hIAPP seeds.",10.1039/D0TB02958K,AG00425
Alpha-synuclein,Tau,KTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,Faster aggregation,Yes; implied by kinetics.,No information,"After three days, alpha-syn significantly increased the sedimentation and K114 fluorometry of P301L tau over that of WT tau (Fig. 10A–C), whereas in the absence of alpha-syn neither WT nor P301L tau aggregated after 7 d (Fig. 10A, right)",NA,NA,interactor: prefibrilized alphaSyn (21-140) interactee: tau,10.1523/JNEUROSCI.0297-11.2011,AG00426
Albumin,Lysozyme,DTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPENLPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAKEYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEYGFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTEDYLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKAFDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENFVAFVDKCCAADDKEACFAVEGPKLVVSTQTALA,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1021/bi501333q,AG00431
Lysozyme,Albumin,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,DTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPENLPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAKEYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEYGFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTEDYLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKAFDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENFVAFVDKCCAADDKEACFAVEGPKLVVSTQTALA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1021/bi501333q,AG00432
Albumin,Cytochrome C,DTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPENLPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAKEYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEYGFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTEDYLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKAFDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENFVAFVDKCCAADDKEACFAVEGPKLVVSTQTALA,MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1021/bi501333q,AG00433
Albumin,Albumin,DTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPENLPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAKEYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEYGFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTEDYLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKAFDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENFVAFVDKCCAADDKEACFAVEGPKLVVSTQTALA,DTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPENLPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAKEYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEYGFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTEDYLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKAFDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENFVAFVDKCCAADDKEACFAVEGPKLVVSTQTALA,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1021/bi501333q,AG00434
Lysozyme,Lysozyme,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1021/bi501333q,AG00435
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1016/j.febslet.2013.02.008,AG00437
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,Yes,NA,NA,NA,NA,10.1016/j.febslet.2013.02.008,AG00438
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,Interactor:AB40 Interactee:AB42,10.1016/j.ijms.2018.02.002,AG00439
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1016/j.ijms.2018.02.002,AG00440
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Abeta42,10.1016/j.ijms.2018.02.002,AG00441
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,AB40,10.1016/j.ijms.2018.02.002,AG00442
IAPP,Amyloid beta,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,"Yes, direct evidence.",Yes,NA,NA,NA,NA,10.1039/C7CP08552D,AG00443
Lysozyme,Amyloid beta,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQIN SRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRD VRQYVQGCGV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1039/C3CC42325E,AG00444
Albumin,Amyloid beta,MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No,No,NA,NA,NA,NA,10.1016/J.BPJ.2009.08.028,AG00445
Albumin,Amyloid beta,MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL,VHHQKLVFFAEDVGSRK,No effect,No,No,NA,NA,NA,NA,10.1016/J.BPJ.2009.08.028,AG00446
Albumin,Amyloid beta,MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No,No,NA,NA,NA,NA,10.1016/J.BPJ.2009.08.028,AG00447
Albumin,Amyloid beta,MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,Yes,NA,NA,NA,NA,10.1016/J.BPJ.2009.08.028,AG00448
PrP,Amyloid beta,GQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"The presence of prion protein lengthens the lag phase of both Abeta42 and AbetapE3-42 peptides, leaving the fibril growth rate substantially unaffected NMR and ThT data indicated that, for both peptides, PrP competed with nucleation and elongation processes, delaying further growth of the NMR-invisible Abeta species and/or fibril. The morphological analysis confirmed that PrP induces a profound change in the structure of both Abeta peptides, decreasing the amount and the interconnections of the fibers",NA,NA,human PrP (90-231) / Abeta (1–42),10.1007/s12035-018-1202-x,AG00449
PrP,Amyloid beta,GQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"The presence of prion protein lengthens the lag phase of both Abeta42 and AbetapE3-42 peptides, leaving the fibril growth rate substantially unaffected NMR and ThT data indicated that, for both peptides, PrP competed with nucleation and elongation processes, delaying further growth of the NMR-invisible Abeta species and/or fibril. The morphological analysis confirmed that PrP induces a profound change in the structure of both Abeta peptides, decreasing the amount and the interconnections of the fibers.",NA,NA,human PrP (90-231) / Abeta-(pE3-42),10.1007/s12035-018-1202-x,AG00450
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,NA,"Experimental results indicate a contrasting role of rIAPP in hIAPP aggregation, in which rIAPP initially inhibits the early aggregation and nuclei formation of hIAPP, but hIAPP seeds can also recruit both hIAPP and rIAPP to form more hybrid fibrils, thus promoting amyloid fibrillation ultimately. The coincubation of hIAPP and rIAPP also decreases cell viability, presumably due to the formation of more toxic hybrid oligomers at the prolonged lag phase. Comparative MD simulations confirm that the crosssequence interactions between hIAPP and rIAPP stabilize beta-sheet structure and thus likely promote their fibrillization. This work provides valuable insights into a critical role of cross-amyloid interactions in protein aggregation.",NA,NA,10.1021/la500632d,AG00451
Apolipoprotein A-I,Amyloid beta,MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,No information,No information,"Consistent with this small effect on amyloid structure and with the formation of limited amounts of non-fibrillar aggregates, ThT binding was somewhat reduced (∼35%) under those conditions (Fig. 3D, trace 2)",NA,NA,Apo:Aß 20:1,10.1016/j.biocel.2008.12.003,AG00452
Apolipoprotein A-I,Amyloid beta,MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,"By contrast, when higher concentrations of apoA-I were present during A aggregation (A:apoA-I molar ratio of 2:1) abundant smaller aggregates were detected (Fig. 3C), with shorter, curvilinear and thinner structures resembling protofibrils predominating in the samples instead of the long amyloid fibrils composed of A alone. Intriguingly, the structures formed in the presence of apoA-I bound ∼60% more ThT (Fig. 3D, trace 3)",NA,NA,Apo:Aß 2:1,10.1016/j.biocel.2008.12.003,AG00453
Transthyretin,Amyloid beta,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"The fibril formation kinetics of a 5.0 μM sample of Abeta40 were found to be significantly slowed down in the presence of either TTR variant, but the comparison of kinetic traces at similar m.e. shows that WT-TTR has a more effective inhibitory effect",NA,NA,tetrameric transthyretin with Aß40,10.1021/acs.biomac.9b01475,AG00454
Transthyretin,Amyloid beta,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPMHEHAEVVFTANDSGPRRYTIAAMLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"The fibril formation kinetics of a 5.0 μM sample of Abeta40 were found to be significantly slowed down in the presence of either TTR variant, but the comparison of kinetic traces at similar m.e. shows that WT-TTR has a more effective inhibitory effect",NA,NA,monomeric transthyretin with Aß40,10.1021/acs.biomac.9b01475,AG00455
Lysozyme,Amyloid beta,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQIN SRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRD VRQYVQGCGV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,The Abeta aggregation kinetics were substantially slowed down at a 1:1 ratio between Abeta1-42 and lysozyme;,NA,NA,NA,10.1016/j.nbd.2015.08.024,AG00456
Lysozyme,Amyloid beta,KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQIN SRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRD VRQYVQGCGV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.nbd.2015.08.024,AG00457
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1021/acs.biochem.9b00655,AG00458
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,"When Abeta monomers were mixed with alphaS fibrils, ThT fluorescence and morphology were similar to those of the alphaS fibril only samples (Figure 1A and Figure 1D; compare to Figure S7B).",NA,10.1021/acs.biochem.9b00655,AG00459
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1021/acs.biochem.9b00655,AG00460
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1021/acs.biochem.9b00655,AG00461
Tau,Amyloid beta,VQIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,"At 25 μM, AcPHF6 was able to dramatically increase the fibrillogenesis of both Abeta40 and Abeta42.",NA,NA,NA,10.1021/acschemneuro.7b00433,AG00462
Tau,Amyloid beta,VQIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"In contrast, at 1 μM, AcPHF6 was able to prevent Abeta40 aggregation (48% inhibition at 24 h)",NA,NA,NA,10.1021/acschemneuro.7b00433,AG00463
Tau,Amyloid beta,VQIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No information,No information,"At 5 μM, it exhibited almost no activity toward Abeta40",NA,NA,NA,10.1021/acschemneuro.7b00433,AG00464
Tau,Amyloid beta,VQIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00465
Tau,Amyloid beta,VQIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"AcPHF6 was able to dramatically increase the fibrillogenesis of both Abeta40 and Abeta42.; In contrast, at 1 μM, AcPHF6 (...) was a weak promoter of Abeta42 aggregation.; At 5 μM, it (...) was able to promote Abeta42 aggregation.",NA,NA,NA,10.1021/acschemneuro.7b00433,AG00466
Tau,Amyloid beta,VQIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00467
Tau,Amyloid beta,VQIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,The native peptide PHF6 was able to prevent Abeta40 aggregation at 5 and 25 μM respectively at pH 7.4.,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00468
Tau,Amyloid beta,VQIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,"However, at 1 μM, it was able to promote Abeta fibrillogenesis (Figure 4A) although this effect was not comparable to the significant and dramatic acceleration in fibril assembly seen with AcPHF6.",NA,NA,NA,10.1021/acschemneuro.7b00433,AG00469
Tau,Amyloid beta,VQIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00470
Tau,Amyloid beta,AQIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No information,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00471
Tau,Amyloid beta,AQIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00472
Tau,Amyloid beta,AQIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00473
Tau,Amyloid beta,VAIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00474
Tau,Amyloid beta,VAIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00475
Tau,Amyloid beta,VAIVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00476
Tau,Amyloid beta,VQAVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No information,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00477
Tau,Amyloid beta,VQAVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00478
Tau,Amyloid beta,VQAVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00479
Tau,Amyloid beta,VQAVYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00480
Tau,Amyloid beta,VQIAYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00481
Tau,Amyloid beta,VQIAYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00482
Tau,Amyloid beta,VQIAYK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00483
Tau,Amyloid beta,VQIVAK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00484
Tau,Amyloid beta,VQIVYA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00485
Tau,Amyloid beta,VQIVYA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00486
Tau,Amyloid beta,VQIVYA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00487
Tau,Amyloid beta,VQIVYA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00488
Tau,Amyloid beta,VQIVYA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1021/acschemneuro.7b00433,AG00489
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,"Abeta40 and Abeta11−40 seeds not only effectively promoted their own aggregation and shortened the lag phase time of Abeta40 and Abeta11−40 significantly (Figure 1A, Table 1, Figure S2)",NA,NA,NA,10.1021/acs.langmuir.8b03599,AG00490
Amyloid beta,Amyloid beta,EVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1021/acs.langmuir.8b03599,AG00491
Amyloid beta,Amyloid beta,EVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,EVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1021/acs.langmuir.8b03599,AG00492
Amyloid beta,Amyloid beta,EVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,"Yes, direct evidence.",No information,NA,NA,NA,NA,10.1021/acs.langmuir.8b03599,AG00493
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,"Self and cross-seeding of Ab42 and Ab40, respectively, in 20 mM sodium phosphate, 200 mM EDTA, 0.02% NaN3, pH 7.4 with 5 mM ThT. With increasing self-seed concentration the lag-phase decreases until the sigmoidal shape disappears. The self-seeding is much more efficient than the cross-seeding. At high seed concentrations (10–50%) the ThT fluorescence increases earlier with cross seed compared to no seed, but without affecting the half-time. Half-time as a function of the logarithm of the seed concentration. The self-seeding data displays clear concentration dependence while the cross-seeding data lack this property",NA,fibril elongation and surface-catalyzed secondary nucleation are highly specific events resulting in the formation of distinct fibrils composed of Ab42 or Ab40,Ab42 monomers with different concetration of Ab42 fibrils,10.1039/C4SC02517B,AG00494
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,Yes; implied by kinetics.,No,"Self and cross-seeding of Ab42, in 20 mM sodium phosphate, 200 mM EDTA, 0.02% NaN3, pH 7.4 with 5 mM ThT. With increasing self-seed concentration the lag-phase decreases until the sigmoidal shape disappears. The self-seeding is much more efficient than the cross-seeding. At high seed concentrations (10–50%) the ThT fluorescence increases earlier with cross seed compared to no seed, but without affecting the half-time. Half-time as a function of the logarithm of the seed concentration. The self-seeding data displays clear concentration dependence while the cross-seeding data lack this property",NA,fibril elongation and surface-catalyzed secondary nucleation are highly specific events resulting in the formation of distinct fibrils composed of Ab42 or Ab40,Ab42 monomers with differents concetrations of Ab40 fibrils,10.1039/C4SC02517B,AG00495
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,"Self and cross-seeding of Ab42, in 20 mM sodium phosphate, 200 mM EDTA, 0.02% NaN3, pH 7.4 with 5 mM ThT. With increasing self-seed concentration the lag-phase decreases until the sigmoidal shape disappears. The self-seeding is much more efficient than the cross-seeding. At high seed concentrations (10–50%) the ThT fluorescence increases earlier with cross seed compared to no seed, but without affecting the half-time. Half-time as a function of the logarithm of the seed concentration. The self-seeding data displays clear concentration dependence while the cross-seeding data lack this property",NA,fibril elongation and surface-catalyzed secondary nucleation are highly specific events resulting in the formation of distinct fibrils composed of Ab42 or Ab40,Ab40 monomers with differents concetrations of Ab42 fibrils,10.1039/C4SC02517B,AG00496
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,"Self and cross-seeding of Ab42, in 20 mM sodium phosphate, 200 mM EDTA, 0.02% NaN3, pH 7.4 with 5 mM ThT. With increasing self-seed concentration the lag-phase decreases until the sigmoidal shape disappears. The self-seeding is much more efficient than the cross-seeding. At high seed concentrations (10–50%) the ThT fluorescence increases earlier with cross seed compared to no seed, but without affecting the half-time. Half-time as a function of the logarithm of the seed concentration. The self-seeding data displays clear concentration dependence while the cross-seeding data lack this property",NA,fibril elongation and surface-catalyzed secondary nucleation are highly specific events resulting in the formation of distinct fibrils composed of Ab42 or Ab40,Ab40 monomers with differents concetrations of Ab40 fibrils,10.1039/C4SC02517B,AG00497
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"In presence of N1, but not C1, Abeta polymerization was delayed in a dose-dependent manner, with a significantly extended lag phase (6–16 h) (Fig. 4B).","In presence of N1, but not C1, Abeta polymerization was delayed in a dose-dependent manner, with a significantly extended lag phase (6–16 h) (Fig. 4B).","In presence of N1, but not C1, Abeta polymerization was delayed in a dose-dependent manner, with a significantly extended lag phase (6–16 h) (Fig. 4B).","0,5 µM, 1 µM, 2,5 µM N1 / 20 µM Abeta (1–42), redissolved N1 - residues 23–111 of murine PrPC",10.1074/jbc.M112.423954,AG00498
PrP,Amyloid beta,AGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No,No,"N1 inhibited Abeta polymerization in a dose-dependent fashion, whereas C1 had no effect.","N1 inhibited Abeta polymerization in a dose-dependent fashion, whereas C1 had no effect.","N1 inhibited Abeta polymerization in a dose-dependent fashion, whereas C1 had no effect.","0,1 µM, 0,5 µM, 2 µM C1 / 20 µM Abeta (1–42), redissolved C1 - residues 112–230 of murine PrP no effect because: no fibrillization there? (they did not check), almost no effect on ThT compare to N1, and so they write ""no effect"", also there was no binding, no coprecipitation",10.1074/jbc.M112.423954,AG00499
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVCSKTKEGCVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,Interactee: WT alpha-synuclein Interactor: alpha-synuclein CC,10.1002/anie.201503018,AG00500
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVCSKTKEGCVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,Interactee: Amyloid beta 40 Interactor: alpha-synuclein CC,10.1002/anie.201503018,AG00501
Alpha-synuclein,Amyloid beta,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,Interactee: Amyloid beta 40  Interactor: WT alpha-synuclein,10.1002/anie.201503018,AG00502
Alpha-synuclein,IAPP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,Interactee: IAPP  Interactor: WT alpha-synuclein,10.1002/anie.201503018,AG00503
Alpha-synuclein,IAPP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVCSKTKEGCVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,Interactee: IAPP Interactor: alpha-synuclein CC,10.1002/anie.201503018,AG00504
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQ PHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGN DWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDV KMMERVVEQMCVTQYQKESQAYYDGRRS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"In the absence of PrPC, Ab40 (10 uM) readily forms fibers, exhibiting a characteristic sigmoidal growth curve with a lag-phase (47 h) followed by rapid elongation of fibers (Fig. 1A). In the presence of equimolar concentration of PrPC (10 uM) no amyloid fibers are detected even after 450 h (Fig. 1B).",NA,NA,NA,10.1096/fj.12-222588,AG00505
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQ,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,PrPC inhibits Ab42 fiber formation. Kinetics of Ab42 (5 uM) fiber formation was monitored by fluorescence upon ThT binding to amyloid.,NA,NA,NA,10.1096/fj.12-222588,AG00506
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQ PHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGG,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1096/fj.12-222588,AG00507
S100A9,Amyloid beta,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIE HIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,KKLVFF,Faster aggregation,Yes; implied by kinetics.,No information,S100A9 fibrillated much faster in the presence of both NCAM1-PrP (Figure 1A) and NCAM1-Abeta (Figure 1B) compared to S100A9 alone,NA,NA,"interactee: S100A9, interactor: NCAM1-Abeta (aa 16-20)",10.1021/acschembio.9b00394,AG00508
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQ PHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGN DWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDV KMMERVVEQMCVTQYQKESQAYYDGRRS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"We found that recombinant PrP pro- foundly delays Apolymerization, even when present in amounts that are highly substoichiometric to A(Fig. 2a). The half-time for polymerization was nearly doubled at a PrP/A ratio of 1:160 and tripled at a ratio of 1:20 (Fig. 2b).",NA,NA,full PrP - Abeta42,10.1074/jbc.M117.789990,AG00509
PrP,Amyloid beta,HVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGN DWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDV KMMERVVEQMCVTQYQKESQAYYDGRRS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No information,"As expected, removing the entire N-terminal domain (yield- ing construct 110–230) completely abolished the inhibitory effect of PrP on Afibrillation (Fig. 6, compare b and c).",NA,NA,PrP(110-231) - Abeta42,10.1074/jbc.M117.789990,AG00510
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQ PHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No information,"To our surprise, however, we found that the isolated N-terminal domain (residues 23–119), which includes both of the putative ADDL-binding sites, had no effect on polymerization (Fig. 6d).",NA,NA,PrP(23-119) - Abeta42,10.1074/jbc.M117.789990,AG00511
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQ PHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGN DW,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"A more C-terminally extended construct, 23–144, which ends just before the first -helix, had a weak inhibitory effect at the highest concentrations, but much less than full-length PrP(23– 230) (Fig. 6e).",NA,NA,PrP(23-144) - Abeta42,10.1074/jbc.M117.789990,AG00512
PrP,Amyloid beta,KTNLKHVAGAAAAGAVVGGLG,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"We also tested a construct ( 105–125), which is missing only a short hinge region connecting the N- and C-terminal domains, and found that it inhibited polymerization less effectively than the wild- type protein, implying that this region is also important for  inhibitoryactivity(Fig.6f).",NA,NA,PrP(105-125) - Abeta42,10.1074/jbc.M117.789990,AG00513
p53,p53,MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRHCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD,MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1073/pnas.1500262112,AG00514
p53,p53,MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPCEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD,MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1073/pnas.1500262112,AG00515
CsgB,CsgA,MKNKLLFMMLTILGAPGIAAAAGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1073/pnas.0703310104,AG00516
IAPP,CsgA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,No effect,No information,No information,NA,NA,NA,NA,10.1073/pnas.0703310104,AG00517
Alpha-crystallin,Alpha-synuclein,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.jmb.2004.05.054,AG00518
Alpha-crystallin,Alpha-synuclein,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Yes; implied by kinetics.,No,"In the case of the A53T mutant, the formation of fibrils started slightly earlier (after ca 15 hours) in comparison to wild-type alpha-synuclein (Figure 1B). (...) Near-complete inhibition of fibril formation was achieved by sub-stoichiometric amounts of alphaB-crystallin (0.25 : 1.0 and 0.5 : 1.0 molar ratios of alphaB-crystallin/alpha-synuclein). However, at a 1 : 1 ratio, the ability of alphaB-crystallin to prevent fibril formation was reversed with significant fibril formation observed.",NA,NA,A53T mutant of alpha-synuclein as interactee,10.1016/j.jmb.2004.05.054,AG00519
Alpha-crystallin,Alpha-synuclein,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAPGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Yes; implied by kinetics.,No information,"AlphaB-crystallin was very effective in suppressing fibrillization of A30P alpha-synuclein at all concentrations.; Electron micrographs of samples containing alphaB-crystallin and alpha-synuclein (wild-type or mutants) at a 0.25 : 1.0 molar ratio, showed a significant reduction in the number of fibrils, but not their length.",NA,NA,A30P mutant of alpha-synuclein as interactee,10.1016/j.jmb.2004.05.054,AG00520
Beta-crystallin,Alpha-synuclein,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTK EQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDP DNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,For oligomeric betaH-crystallin the inhibitory effect was shown to be similar to that of alpha-crystallin (Figs 1B vs 2A). (...) Addition of alpha-crystallin progressively retards and even inhibits fibril formation within the time frame of the experiment.,NA,NA,NA,10.1371/journal.pone.0235198,AG00521
Beta-crystallin,Alpha-synuclein,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1371/journal.pone.0235198,AG00522
Gamma-crystallin,Alpha-synuclein,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,For monomeric gammaB-crystallins the inhibition of fibril formation was slightly less efficient (Fig 2B).,NA,NA,NA,10.1371/journal.pone.0235198,AG00523
Gamma-crystallin,Alpha-synuclein,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1371/journal.pone.0235198,AG00524
Alpha-crystallin,Alpha-synuclein,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No effect,No information,No information,https://drive.google.com/open?id=1agj07Ah2agzs6V3hkbnsZLoYLOT7iMqQ,NA,NA,NA,10.1371/journal.pone.0235198,AG00525
Alpha-crystallin,Alpha-synuclein,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1371/journal.pone.0235198,AG00526
Alpha-crystallin,Alpha-synuclein,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1371/journal.pone.0235198,AG00527
Sup35,Sup35,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,Faster aggregation,"Yes, direct evidence.",No,NA,NA,NA,"Interactor: yeast prion-forming protein Sup35NM seeds  Interactee: yeast prion-forming protein Sup35NM monomers seeds = sonicated fibrils, from 0.1 to 5%",10.1073/pnas.2104148118,AG00528
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No,"Similarly to Sup35NM, assembly of Abeta42 monomers (Abeta42m) was significantly accelerated by the addition of as little as 0.1% pre-formed Abeta42 fibril-seeds (Abeta42s). The lag-phase was eliminated in the presence of as low as ∼1% monomer molar equivalents or more of seeds",NA,NA,"Interactor: human Aß42 peptide seeds Interactee: human Aß42 peptide monomers;  seeds = sonicated fibrils, from 0.1 to 5%",10.1073/pnas.2104148118,AG00529
Amyloid beta,Sup35,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,Faster aggregation,"Yes, direct evidence.",No information,"For Sup35NM amyloid formation, Abeta42s was also able to significantly shorten, but not eliminate, the length of the lag phase",NA,NA,"Interactor: human Aß42 peptide seeds Interactee: yeast prion-forming protein Sup35NM monomers;  seeds = sonicated fibrils, from 0.1 to 5%",10.1073/pnas.2104148118,AG00530
Sup35,Amyloid beta,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,the addition of heterologous seeds (in this case the unrelated Sup35NMs) in low concentrations (~5% or less monomer molar equivalents) to monomer solutions of Abeta42 was able to statistically significantly reduce the lag time of the Abeta42 amyloid formation,NA,NA,"Interactor: yeast prion-forming protein Sup35NM seeds Interactee:  human Aß42 peptide monomers;  seeds = sonicated fibrils, from 0.1 to 5%",10.1073/pnas.2104148118,AG00531
Lysozyme,IAPP,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Conversely, complete inhibition of IAPP was observed in the presence of Lys over the 14 h sampling period for ThT",NA,NA,NA,10.1038/s41598-017-02597-0,AG00532
Alpha-lactalbumin,IAPP,EQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIMCVKKILDKVGINYWLAHKALCSEKLDQWLCEKL,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No,"In comparison, the IAPP-aLac mixture was mainly present as large amorphous aggregates after 24 h, which was also observed as off-white precipitates in solution (Fig. 1B upper panel, inset). Based on the ThT assay (Fig. 1A), the amorphous aggregates contained significant beta-sheet structures. Considering the opposing charges of IAPP and aLac, it is likely that electrostatic attraction with aLac strongly perturbed IAPP self-assembly into fibrils, while favoured formation of amorphous structures.","In comparison, the IAPP-aLac mixture was mainly present as large amorphous aggregates after 24 h, which was also observed as off-white precipitates in solution (Fig. 1B upper panel, inset). Based on the ThT assay (Fig. 1A), the amorphous aggregates contained significant beta-sheet structures. Considering the opposing charges of IAPP and aLac, it is likely that electrostatic attraction with aLac strongly perturbed IAPP self-assembly into fibrils, while favoured formation of amorphous structures.",NA,NA,10.1038/s41598-017-02597-0,AG00533
Amyloid beta,Amyloid beta,FRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"for the 3:1 and 5:1 [Abeta (1–40): Abeta (4–40)] ratios, a different trend was observed, with CuII additions leading to a gradual increase in tlag and decrease in Fmax. (Figure S10)",NA,NA,NA,10.1002/chem.202004484,AG00534
Amyloid beta,Amyloid beta,FRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1002/chem.202004484,AG00535
Amyloid beta,Amyloid beta,FRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,"Values significantly higher than those of each peptide were observed for the 5:1 and 3:1 mixtures of Ab1–40/Ab4–40, indicative of a fast growth phase. Thus, the tlag and k’ parameters follow the same trend, namely an acceleration of Ab1–40 aggregation by the co-presence of a substoichiometric amount of Ab4–40.",NA,NA,NA,10.1002/chem.202004484,AG00536
Amyloid beta,Amyloid beta,VVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No information,No,"Addition of 1- or 5-fold excess Abeta(39−42) had no apparent effect on beta-sheet formation by either Abeta40 or Abeta42, suggesting that despite changing the oligomer size distribution of Abeta42, Abeta(39−42) did not inhibit its later aggregation.",NA,NA,Interactor: Abeta (39-42) Interactee: Abeta (1–40),10.1021/bi201520b,AG00539
Amyloid beta,Amyloid beta,VVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No,"Addition of 1- or 5-fold excess Abeta(39−42) had no apparent effect on beta-sheet formation by either Abeta40 or Abeta42, suggesting that despite changing the oligomer size distribution of Abeta42, Abeta(39−42) did not inhibit its later aggregation.",NA,NA,Interactor: Abeta (39-42) Interactee: Abeta (1–42),10.1021/bi201520b,AG00540
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKKGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No,"However, the WT-pH 7.4 fibrils did not elongate in the presence of E46K monomers","However, the WT-pH 7.4fibrils did not elongate in the presence of E46K monomers",NA,"Ineractee: WT-pH 7.4 fibrils Interactor: E46K-pH 7.4, pH 5.8 monomers",10.1021/acsnano.0c03074,AG00548
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKKGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKKGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No,The E46K-pH 7.4 elongation rate was accelerated to 2.3±2.3 nm/min in the presence of E46K-pH 5.8 monomers,NA,NA,Interactee: E46K-pH 7.4 Interactor: E46K-pH 5.8 monomers,10.1021/acsnano.0c03074,AG00549
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKKGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No,The E46K-pH 7.4fibrils showed slow or no growth in the presence of WT monomers,The E46K-pH 7.4fibrils showed slow or no growth in the presence of WT monomers,NA,Interactee: E46K-pH 7.4 fibrils Interactor: WT monomers,10.1021/acsnano.0c03074,AG00550
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No,"In the presence of WT-pH 7.4 monomers, the WT-pH 7.4 fibrils grew unidirectionally at a rate of 4.1 ± 3.5 nm/min and displayed the same structure as the fibril seeds",NA,NA,Ineractee: WT-pH 7.4 fibrils Interactor: WT-pH 7.4,10.1021/acsnano.0c03074,AG00551
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No effect,"Yes, direct evidence.",No,"The WT-pH 7.4 fibrils still incorporated WT-pH 5.8 monomers while maintaining their polarity, structure, and elongation rate (3.5 ± 3.1 nm/min)",NA,NA,Interactee: WT-pH 7.4 Interactor: WT-pH 5.8 monomers,10.1021/acsnano.0c03074,AG00552
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,"Yes, direct evidence.",No,The WT-pH 5.8 elongation rate was lower (1.3 ± 1.0 nm/min) in the presence of WT-pH 7.4 monomers,NA,NA,Interactee: WT-pH 5.8  Interactor: WT-pH 7.4 monomers,10.1021/acsnano.0c03074,AG00553
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKKGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No,"WT-pH 5.8 fibrils grew little or not at all in the presence of E46K monomers, but occasionally unidirectional growth of thin filaments with the thickness distinct from the parent fibrils was observed","WT-pH 5.8 fibrils grew little or not at all in the presence of E46K monomers, but occasionally unidirectional growth of thin filaments with the thickness distinct from the parent fibrils was observed",NA,"Interactee: WT-pH 5.8  Interactor: E46K-pH 7.4, pH 5.8 monomers",10.1021/acsnano.0c03074,AG00554
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKKGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,"Yes, direct evidence.",No,"""Unlike the other fibrils in this study, the E46K-pH 5.8 fibrils incorporated the WT-pH 5.8 monomers and grew unidirectionally while producing the same spiral structure as the seeds, although its elongation rate was reduced to 3.9 ± 1.8 nm/min (Figure 4e−h) compared to self-seeding growth (17.1 ± 8.7 nm/min) """,NA,NA,Interactee: E46K-pH 5.8 fibrils Interactor: WT-pH 5.8 monomers,10.1021/acsnano.0c03074,AG00555
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKKGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No,"However, the E46K-pH 5.8 fibrils did not elongate in the presence of the WT-pH 7.4 monomers, suggesting they did not incorporate the WT monomers at pH 7.4","However, the E46K-pH 5.8 fibrils did",NA,Interactee: E46K-pH 5.8 fibrils Interactor: WT-pH 7.4 monomers,10.1021/acsnano.0c03074,AG00556
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKKGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKKGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,"Yes, direct evidence.",Yes,The E46K-pH 5.8 elongation rate was slower (1.7 ± 0.9 nm/min) in the presence of E46K-pH 7.4 monomers (Figures 4i−l and S5d) and occasionally showed extrusion of the thinner striated structures different than those of the seed fibrils,NA,The E46K-pH 5.8 elongation rate was slower (1.7 ± 0.9 nm/min) in the presence of E46K-pH 7.4 monomers (Figures 4i−l and S5d) and occasionally showed extrusion of the thinner striated structures different than those of the seed fibrils,Interactee: E46K-pH 5.8 fibrils Interactor: E46K-pH 7.4 monomers,10.1021/acsnano.0c03074,AG00557
IAPP,IAPP,KCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"Thioflavin-T fluorescence-monitored kinetic experiments, transmission electron microscopy, and circular dichroism showed that rat IAPP lengthened the lag phase for amyloid formation by human IAPP, slowed the growth rate, reduced the amount of amyloid fibrils produced in a dosedependent manner, and altered the morphology of the fibrils.",NA,NA,NA,10.1021/bi901751b,AG00558
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No,"In contrast, addition of the human IAPP seeds to the human IAPP reaction abolished the lag phase as expected (Figure 5).",NA,NA,NA,10.1021/bi901751b,AG00559
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Kinetic curves presented in Figure 5 demonstrate that mature human IAPP fibrils are not capable of seeding fibril formation by rat IAPP under these conditions. The fluorescence intensity of the mixture of rat IAPP with the human IAPP seeds is slightly higher than that of the rat IAPP reaction alone, but this is due to the fact that human amyloid fibril seeds bind to thioflavin-T. The critical observation is that no significant change in thioflavin-T fluorescence is observed over the time course of the reaction.",NA,NA,NA,10.1021/bi901751b,AG00560
IAPP,IAPP,KCNTATCATQRLPNFLVRSSNNLGPVLPPTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"The time to reach 50% of the final fluorescence intensity, T50, is 5.3 times longer for the 10:1mixture of A13P-rat IAPP and human IAPP than for a sample of pure human IAPP. (Figure 6)",NA,NA,NA,10.1021/bi901751b,AG00561
IAPP,IAPP,KCNTATCATQRLANDLVRSSNNLGPVLPPTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1021/bi901751b,AG00562
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAPLSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"A 1:1 molar mixture of wild- type IAPP with either inhibitor behaves very differently than does the wild-type peptide in the absence of inhibitor. Like the I26P peptide, the G24P mutant is an inhibitor of amyloid formation. It lengthens the lag phase and decreases the value of final thioflavin-T fluorescence intensity, but it does not completely abolish amyloid formation by IAPP.",NA,NA,NA,10.1021/ja1046186,AG00563
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFPAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"A 1:1 molar mixture of wild- type IAPP with either inhibitor behaves very differently than does the wild-type peptide in the absence of inhibitor. Like the I26P peptide, the G24P mutant is an inhibitor of amyloid formation. It lengthens the lag phase and decreases the value of final thioflavin-T fluorescence intensity, but it does not completely abolish amyloid formation by IAPP.",NA,NA,NA,10.1021/ja1046186,AG00564
IAPP,Amyloid beta,KCNTATCATQRLANFLVHSSNNFGAPLSSTNVGSNTY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"Thioflavin-T-monitored kinetic assays reveal that each peptide is a moderate inhibitor of amyloid formation by A1-40, and show that the two IAPP point mutants exert different relative effects on the lag phase and the final thioflavin-T fluorescence intensity (Figure 3A).",NA,NA,NA,10.1021/ja1046186,AG00565
IAPP,Amyloid beta,KCNTATCATQRLANFLVHSSNNFPAILSSTNVGSNTY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"Thioflavin-T-monitored kinetic assays reveal that each peptide is a moderate inhibitor of amyloid formation by A1-40, and show that the two IAPP point mutants exert different relative effects on the lag phase and the final thioflavin-T fluorescence intensity (Figure 3A).",NA,NA,NA,10.1021/ja1046186,AG00566
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,No information,No information,"We first performed a self seeding experiment for Abeta40. As shown in Fig. 1A, in the absence of seeds, spontaneous Abeta40 fibrillization at 50 μm has a lag time of 17.7 h, and a half time of 18.7 h. The lag time was shortened by the presence of Abeta40 fibril seeds in a concentration-dependent manner (Fig. 1A). Remarkably, the presence of just 0.25% Abeta40 fibril seeds shortened the lag time by more than half.",NA,NA,NA,10.1002/1873-3468.12526,AG00567
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,No information,No information,The self seeding effect for Abeta42 is much less prominent than Abeta40 self seeding. Even 8% fibril seeds did not reduce the lag time by half.,NA,NA,NA,10.1002/1873-3468.12526,AG00568
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,No information,No information,"We have also performed the cross-seeding of Abeta40 fibrillization using a different batch of Abeta40. The lag time was shortened by addition of Abeta42 seeds in a seed concentration-dependent fashion (Fig. S1A). The exact lag time is different between batches, but the effect of cross-seeding remains true.",NA,NA,NA,10.1002/1873-3468.12526,AG00569
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,No information,No information,"Abeta40 fibril seeds also accelerated Abeta42 aggregation in a concentration-dependent manner (Fig. 2B). The lag time and half time of cross-seeding are shown in Fig. 2C,D. At seed concentrations of 8% or lower, the seeding effect is similar for Abeta40 and Abeta42 seeds. Only at 16% seed concentration, we observed a dramatic difference between Abeta40 and Abeta42 seeds.",NA,NA,NA,10.1002/1873-3468.12526,AG00570
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No,"based on the ThT fluorescence intensity, in heterologous reactions, wt monomers fibrillized with both A30P and A53T seeds","In heterologous aggregations, wt monomers appeared to grow well on both A30P and A53T seeds, with close to 50% of the total fibril lengths linked with growth on the seeds.",NA,NA,10.1021/acschemneuro.5b00322,AG00571
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAPGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No,"based on the ThT fluorescence intensity, in heterologous reactions, wt monomers fibrillized with both A30P and A53T seeds","In heterologous aggregations, wt monomers appeared to grow well on both A30P and A53T seeds, with close to 50% of the total fibril lengths linked with growth on the seeds.",NA,NA,10.1021/acschemneuro.5b00322,AG00572
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No,"In homologous aggregations, all of the reactions lacked the lag phase, which is characteristic of a seeded aggregation","In homologous aggregations, 40−50% of the total (new) fibril length was linked to the seeds, whereas about 30% of the fibril length did not show the presence of any seed. The fibrils that are not associated with seeds are most likely fragments of the extensions grown on seeds because none of the alphaSyn sequences studied shows de novo fibrillization in 24 h under quiescent aggregation conditions.",NA,NA,10.1021/acschemneuro.5b00322,AG00573
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAPGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAPGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No,"In homologous aggregations, all of the reactions lacked the lag phase, which is characteristic of a seeded aggregation","In homologous aggregations, 40−50% of the total (new) fibril length was linked to the seeds, whereas about 30% of the fibril length did not show the presence of any seed. The fibrils that are not associated with seeds are most likely fragments of the extensions grown on seeds because none of the alphaSyn sequences studied shows de novo fibrillization in 24 h under quiescent aggregation conditions.",NA,NA,10.1021/acschemneuro.5b00322,AG00574
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAPGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No,NA,The A30P monomers fibrillized on wt seeds account for ∼50% of the total fibril lengths.,NA,NA,10.1021/acschemneuro.5b00322,AG00575
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAPGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No,"A30P monomers aggregated on wt seeds with a t1/2 of 5.7 ± 0.2 h, whereas they did not appear to grow at all on A53T seeds (based on the ThT assay up to the experimental time of 65 h).",NA,NA,NA,10.1021/acschemneuro.5b00322,AG00576
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No,"In homologous aggregations, all of the reactions lacked the lag phase, which is characteristic of a seeded aggregation","In homologous aggregations, 40−50% of the total (new) fibril length was linked to the seeds, whereas about 30% of the fibril length did not show the presence of any seed. The fibrils that are not associated with seeds are most likely fragments of the extensions grown on seeds because none of the alphaSyn sequences studied shows de novo fibrillization in 24 h under quiescent aggregation conditions.",NA,NA,10.1021/acschemneuro.5b00322,AG00577
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",No,NA,NA,NA,NA,10.1021/acschemneuro.5b00322,AG00578
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAPGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No,Figure 4b,NA,NA,NA,10.1021/acschemneuro.5b00322,AG00579
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,Self-seeding with MsWT PFFs at 1% (w/w) of the monomer concentration dramatically accelerated the assembly of MsWT alpha-Syn compared to unseeded reactions (Figures 1C and S2).,Self-seeding with MsWT PFFs at 1% (w/w) of the monomer concentration dramatically accelerated the assembly of MsWT alpha-Syn compared to unseeded reactions (Figures 1C and S2).,NA,NA,10.1016/j.celrep.2016.08.053,AG00580
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,No effect,No information,No information,"In contrast, initiation rates of cross-seeding reactions containing HuWTPFFs were similar to unseeded reactions.","Taken together,although both WT and chimerica-Syn PFFs are capable of seeding fibril formation in vitro, the initiation rates of templating are strongly determined by sequence homology between seeds and substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00581
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,"Taken together,although both WT and chimerica-Syn PFFs are capable of seeding fibril formation in vitro, the initiation rates of templating are strongly determined by sequence homology between seeds and substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00582
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,"Taken together,although both WT and chimerica-Syn PFFs are capable of seeding fibril formation in vitro, the initiation rates of templating are strongly determined by sequence homology between seeds and substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00583
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,"Taken together,although both WT and chimerica-Syn PFFs are capable of seeding fibril formation in vitro, the initiation rates of templating are strongly determined by sequence homology between seeds and substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00584
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKGEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,"Taken together,although both WT and chimerica-Syn PFFs are capable of seeding fibril formation in vitro, the initiation rates of templating are strongly determined by sequence homology between seeds and substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00585
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,"Taken together,although both WT and chimerica-Syn PFFs are capable of seeding fibril formation in vitro, the initiation rates of templating are strongly determined by sequence homology between seeds and substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00586
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,"Taken together,although both WT and chimerica-Syn PFFs are capable of seed-ing fibril formation in vitro, the initiation rates of templating arestrongly determined by sequence homology between seedsand substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00587
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,No effect,No information,No information,NA,Fibrils combining these two substitutions (MsAS PFFs) seeded with ∼80% lower efficiency than MsWT alpha-Syn PFFs.,NA,NA,10.1016/j.celrep.2016.08.053,AG00588
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,NA,"Taken together,although both WT and chimerica-Syn PFFs are capable of seed-ing fibril formation in vitro, the initiation rates of templating arestrongly determined by sequence homology between seedsand substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00589
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,"Taken together,although both WT and chimerica-Syn PFFs are capable of seed-ing fibril formation in vitro, the initiation rates of templating arestrongly determined by sequence homology between seedsand substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00590
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,"Taken together,although both WT and chimerica-Syn PFFs are capable of seed-ing fibril formation in vitro, the initiation rates of templating arestrongly determined by sequence homology between seedsand substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00591
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No effect,No information,No information,"Trans-templating of HuWT monomers by MsWT, HuTN, and HuTNG PFFs proceeded inefficiently, with initiation rates similar to unseeded reactions.","Trans-templating of HuWT monomers by MsWT, HuTN, and HuTNG PFFs proceeded inefficiently, with initiation rates similar to unseeded reactions.",NA,NA,10.1016/j.celrep.2016.08.053,AG00592
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKGEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No effect,No information,No information,"Trans-templating of HuWT monomers by MsWT, HuTN, and HuTNG PFFs proceeded inefficiently, with initiation rates similar to unseeded reactions.","Taken together,although both WT and chimerica-Syn PFFs are capable of seed-ing fibril formation in vitro, the initiation rates of templating arestrongly determined by sequence homology between seedsand substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00593
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,"Taken together,although both WT and chimerica-Syn PFFs are capable of seed-ing fibril formation in vitro, the initiation rates of templating arestrongly determined by sequence homology between seedsand substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00594
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,"Taken together, although both WT and chimerica-Syn PFFs are capable of seeding fibril formation in vitro, the initiation rates of templating are strongly determined by sequence homology between seeds and substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00595
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,"Taken together, although both WT and chimerica-Syn PFFs are capable of seeding fibril formation in vitro, the initiation rates of templating are strongly determined by sequence homology between seeds and substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00596
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No effect,No information,No information,"Trans-templating of HuWT monomers by MsWT, HuTN, and HuTNG PFFs proceeded inefficiently, with initiation rates similar to unseeded reactions.","Taken together, although both WT and chimerica-Syn PFFs are capable of seeding fibril formation in vitro, the initiation rates of templating are strongly determined by sequence homology between seeds and substrate.",NA,NA,10.1016/j.celrep.2016.08.053,AG00597
Transthyretin,CsgA,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"Addition of WT-TTR to freshly purified CsgA at a molar ratio 1:1 increased the lag phase to 4 h (Fig. 1A), suggesting that WT-TTR interferes with the early nucleation and elongation stages of amyloidogenesis",NA,NA,human WT-TTR / 15 μM CsgA from E. coli 1:1,10.1073/pnas.1708805114,AG00598
Transthyretin,CsgA,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,No effect,No information,No information,NA,NA,NA,"human WT-TTR / 15 μM CsgA from E. coli1:2, 1:5",10.1073/pnas.1708805114,AG00599
Lysozyme,CsgA,MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,No effect,No information,No information,"No change in the extent or kinetics of CsgA aggregation was observed in the presence of either BSA or lysozyme (Fig. 1C),",NA,NA,"human lysozyme / 7 μM CsgA from E. coli, 1:1",10.1073/pnas.1708805114,AG00600
Transthyretin,CsgA,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPMHEHAEVVFTANDSGPRRYTIAAMLSPYSYSTTAVVTNPKE,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,No aggregation,Formation of fibrils by the interactee is inhibited,No,"When added to soluble CsgA at the same ratio (1:1), M-TTR abolished CsgA fibril formation",NA,NA,"Human M-TTR, nontetramer-forming F87M/L110M / 15 μM CsgA from E. coli 1:1",10.1073/pnas.1708805114,AG00601
Transthyretin,CsgA,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPMHEHAEVVFTANDSGPRRYTIAAMLSPYSYSTTAVVTNPKE,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,"Human M-TTR nontetramer-forming, F87M/L110M / 15 μM CsgA from E. coli 1:2, 1:5",10.1073/pnas.1708805114,AG00602
CsgA,CsgA,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Faster aggregation,Yes; implied by kinetics.,No,CsgA amyloid assembly is accelerated by the addition of CsgA seeds (Fig. 4A).,NA,NA,CsgA seeds 2% (weight) / 15 μM CsgA; CsgA from E. coli Seeds = preformed and sonicated CsgA fibrils,10.1073/pnas.1708805114,AG00603
Transthyretin,CsgA,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTMAVVTNPKE,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"Its inhibitory capacity was comparable to that of tetrameric WT-TTR, Figure 5A",NA,NA,Human TTR mutant T119M (highly stable human TTR tetramer mutant) / CsgA from E. coli,10.1073/pnas.1708805114,AG00604
Transthyretin,CsgA,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPMHEHAEVVFTANDSGPRRYTIAAMLSPYSYSTTAVVTNPKE,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,No aggregation,Formation of fibrils by the interactee is inhibited,No,M-TTR completely inhibited amyloid assembly by each variant (Fig. S5 A).,NA,NA,"Human M-TTR nontetramer-forming, F87M/L110M / CsgA ΔR1 from E. coli, with deletion of segment R1 (but sequence of WT CsgA)",10.1073/pnas.1708805114,AG00605
Transthyretin,CsgA,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPMHEHAEVVFTANDSGPRRYTIAAMLSPYSYSTTAVVTNPKE,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,No aggregation,Formation of fibrils by the interactee is inhibited,No,M-TTR completely inhibited amyloid assembly by each variant (Fig. S5 B).,NA,NA,"Human M-TTR nontetramer-forming, F87M/L110M / CsgA ΔR3 from E. coli, with deletion of segment R3 (but sequence of WT CsgA)",10.1073/pnas.1708805114,AG00606
Transthyretin,CsgA,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPMHEHAEVVFTANDSGPRRYTIAAMLSPYSYSTTAVVTNPKE,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,No aggregation,Formation of fibrils by the interactee is inhibited,No,M-TTR completely inhibited amyloid assembly by each variant (Fig. S5 C).,NA,NA,"Human M-TTR nontetramer-forming, F87M/L110M / CsgA ΔR5 from E. coli, with deletion of segment R5 (but sequence of WT CsgA)",10.1073/pnas.1708805114,AG00607
Transthyretin,CsgA,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"WT-TTR only delayed the appearance of fibers by the CsgA ΔR1, CsgA ΔR3, and CsgA ΔR5 (Fig. S5 A)",NA,NA,"Human WT-TTR tetramer-forming / CsgA ΔR1 from E. coli, with deletion of segment R1 (but sequence of WT CsgA)",10.1073/pnas.1708805114,AG00608
Transthyretin,CsgA,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"WT-TTR only delayed the appearance of fibers by the CsgA ΔR1, CsgA ΔR3, and CsgA ΔR5 (Fig. S5 B)",NA,NA,"Human WT-TTR tetramer-forming / CsgA ΔR3 from E. coli, with deletion of segment R3 (but sequence of WT CsgA)",10.1073/pnas.1708805114,AG00609
Transthyretin,CsgA,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"WT-TTR only delayed the appearance of fibers by the CsgA ΔR1, CsgA ΔR3, and CsgA ΔR5 (Fig. S5 C)",NA,NA,"Human WT-TTR tetramer-forming / CsgA ΔR5 from E. coli, with deletion of segment R5 (but sequence of WT CsgA)",10.1073/pnas.1708805114,AG00610
Transthyretin,CsgB,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPMHEHAEVVFTANDSGPRRYTIAAMLSPYSYSTTAVVTNPKE,AGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR,No aggregation,Formation of fibrils by the interactee is inhibited,No,M-TTR inhibited CsgBtrunc from assembling into amyloid; Fig. S5D,NA,NA,"Human M-TTR nontetramer-forming, F87M/L110M / CsgBtrunc from E.coli, -> not truncated sequence, authors did not mention where the truncation is 1:1",10.1073/pnas.1708805114,AG00611
Transthyretin,CsgB,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,AGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"WT-TTR did not significantly alter CsgBtrunc fibril formation, Fig. S5D",NA,NA,"Human WT-TTR tetramer-forming / CsgBtrunc from E.coli, -> not truncated sequence, authors did not mention where the truncation is 1:1",10.1073/pnas.1708805114,AG00612
Transthyretin,CsgA,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,No effect,No information,No information,The addition of WT-TTR to CsgA in a molar ratio of 1:1 failed to influence the kinetics of seeded CsgA aggregation,NA,NA,human WT-TTR / CsgA seeds 2% (weight) & 15 μM CsgA (1:1 CsgA:WT-TTR) Seeds = preformed and sonicated CsgA fibrils,10.1073/pnas.1708805114,AG00613
Transthyretin,CsgA,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPMHEHAEVVFTANDSGPRRYTIAAMLSPYSYSTTAVVTNPKE,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,the addition of M-TTR at the same ratio substantially inhibited the accelerating effect of CsgA seeding (Fig. 4C),NA,NA,Human M-TTR / CsgA seeds 2% (weight) & 15 μM CsgA (1:1 CsgA:M-TTR) Seeds = preformed and sonicated CsgA fibrils,10.1073/pnas.1708805114,AG00614
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTPDGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Inhibition of alphaS wt fibril elongation by turn variants. Elongation of wt fibril seeds by wt monomers (initial concentration 25 µM) in the absence and presence of different concentrations of all seven turn variants that did not elongate alphaS wt fibrils by themselves.,NA,NA,10.1016/j.bpc.2020.106519,AG00615
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKNPDGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Inhibition of alphaS wt fibril elongation by turn variants. Elongation of wt fibril seeds by wt monomers (initial concentration 25 µM) in the absence and presence of different concentrations of all seven turn variants that did not elongate alphaS wt fibrils by themselves.,NA,NA,10.1016/j.bpc.2020.106519,AG00616
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKSPNGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Inhibition of alphaS wt fibril elongation by turn variants. Elongation of wt fibril seeds by wt monomers (initial concentration 25 µM) in the absence and presence of different concentrations of all seven turn variants that did not elongate alphaS wt fibrils by themselves.,NA,NA,10.1016/j.bpc.2020.106519,AG00617
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKVNGKVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Inhibition of alphaS wt fibril elongation by turn variants. Elongation of wt fibril seeds by wt monomers (initial concentration 25 µM) in the absence and presence of different concentrations of all seven turn variants that did not elongate alphaS wt fibrils by themselves.,NA,NA,10.1016/j.bpc.2020.106519,AG00618
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTNGGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Inhibition of alphaS wt fibril elongation by turn variants. Elongation of wt fibril seeds by wt monomers (initial concentration 25 µM) in the absence and presence of different concentrations of all seven turn variants that did not elongate alphaS wt fibrils by themselves.,NA,NA,10.1016/j.bpc.2020.106519,AG00619
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKYNGKVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Inhibition of alphaS wt fibril elongation by turn variants. Elongation of wt fibril seeds by wt monomers (initial concentration 25 µM) in the absence and presence of different concentrations of all seven turn variants that did not elongate alphaS wt fibrils by themselves.,NA,NA,10.1016/j.bpc.2020.106519,AG00620
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTGNGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Inhibition of alphaS wt fibril elongation by turn variants. Elongation of wt fibril seeds by wt monomers (initial concentration 25 µM) in the absence and presence of different concentrations of all seven turn variants that did not elongate alphaS wt fibrils by themselves.,NA,NA,10.1016/j.bpc.2020.106519,AG00621
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTYNGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S4 Cross-elongation of alphaS wt and beta2’-turn variants. Time courses of elongation of wt fibril seeds by beta2’-turn variant monomers (left) and elongation of beta2’-turn variant fibril seeds by wt monomers (middle and right). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00622
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTYNGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S4 Cross-elongation of alphaS wt and beta2’-turn variants. Time courses of elongation of wt fibril seeds by beta2’-turn variant monomers (left) and elongation of beta2’-turn variant fibril seeds by wt monomers (middle and right). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00623
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKSGNTVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,Fig. S4 Cross-elongation of alphaS wt and beta2’-turn variants. Time courses of elongation of wt fibril seeds by beta2’-turn variant monomers (left) and elongation of beta2’-turn variant fibril seeds by wt monomers (middle and right). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00624
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKSGNTVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,Fig. S4 Cross-elongation of alphaS wt and beta2’-turn variants. Time courses of elongation of wt fibril seeds by beta2’-turn variant monomers (left) and elongation of beta2’-turn variant fibril seeds by wt monomers (middle and right). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00625
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTGNGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S4 Cross-elongation of alphaS wt and beta2’-turn variants. Time courses of elongation of wt fibril seeds by beta2’-turn variant monomers (left) and elongation of beta2’-turn variant fibril seeds by wt monomers (middle and right). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00626
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKSGDSVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S4 Cross-elongation of alphaS wt and beta2’-turn variants. Time courses of elongation of wt fibril seeds by beta2’-turn variant monomers (left) and elongation of beta2’-turn variant fibril seeds by wt monomers (middle and right). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00627
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKSGDSVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S4 Cross-elongation of alphaS wt and beta2’-turn variants. Time courses of elongation of wt fibril seeds by beta2’-turn variant monomers (left) and elongation of beta2’-turn variant fibril seeds by wt monomers (middle and right). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00628
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKVNGKVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S3 Cross-elongation of alphaS wt and beta1’-turn variants. Time courses of elongation of wt fibril seeds by beta1’-turn variant monomers (top left) and elongation of beta1’-turn variant fibril seeds by wt monomers (other panels). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00629
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKYNGQVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S3 Cross-elongation of alphaS wt and beta1’-turn variants. Time courses of elongation of wt fibril seeds by beta1’-turn variant monomers (top left) and elongation of beta1’-turn variant fibril seeds by wt monomers (other panels). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00630
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKYNGQVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S3 Cross-elongation of alphaS wt and beta1’-turn variants. Time courses of elongation of wt fibril seeds by beta1’-turn variant monomers (top left) and elongation of beta1’-turn variant fibril seeds by wt monomers (other panels). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00631
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTNGGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S3 Cross-elongation of alphaS wt and beta1’-turn variants. Time courses of elongation of wt fibril seeds by beta1’-turn variant monomers (top left) and elongation of beta1’-turn variant fibril seeds by wt monomers (other panels). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00632
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTYGNVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S3 Cross-elongation of alphaS wt and beta1’-turn variants. Time courses of elongation of wt fibril seeds by beta1’-turn variant monomers (top left) and elongation of beta1’-turn variant fibril seeds by wt monomers (other panels). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00633
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTYGNVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S3 Cross-elongation of alphaS wt and beta1’-turn variants. Time courses of elongation of wt fibril seeds by beta1’-turn variant monomers (top left) and elongation of beta1’-turn variant fibril seeds by wt monomers (other panels). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00634
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKYNGKVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S3 Cross-elongation of alphaS wt and beta1’-turn variants. Time courses of elongation of wt fibril seeds by beta1’-turn variant monomers (top left) and elongation of beta1’-turn variant fibril seeds by wt monomers (other panels). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00635
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKNPDGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S2 Cross-elongation of alphaS wt and beta1-turn variants. Time courses of elongation of wt fibril seeds by beta1-turn variant monomers (left) and elongation of beta1-turn variant fibril seeds by wt monomers (middle and right). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00636
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKSPDTVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S2 Cross-elongation of alphaS wt and beta1-turn variants. Time courses of elongation of wt fibril seeds by beta1-turn variant monomers (left) and elongation of beta1-turn variant fibril seeds by wt monomers (middle and right). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00637
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKSPDTVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S2 Cross-elongation of alphaS wt and beta1-turn variants. Time courses of elongation of wt fibril seeds by beta1-turn variant monomers (left) and elongation of beta1-turn variant fibril seeds by wt monomers (middle and right). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00638
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKSPNGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,Fig. S2 Cross-elongation of alphaS wt and beta1-turn variants. Time courses of elongation of wt fibril seeds by beta1-turn variant monomers (left) and elongation of beta1-turn variant fibril seeds by wt monomers (middle and right). The time courses of homo-elongation are shown for comparison.,NA,NA,10.1016/j.bpc.2020.106519,AG00639
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTPDGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1016/j.bpc.2020.106519,AG00640
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00665
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAPLSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00666
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAPLSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00667
IAPP,IAPP,KCNTATCATQRLANFLVRSSNNLGVPLPPTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00668
IAPP,IAPP,KCNTATCATQRLANFLVHSGNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00669
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVRSSNNLGVPLPPTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00670
IAPP,IAPP,KCNTATCATQRLANFLVLSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVRSSNNLGVPLPPTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00671
IAPP,IAPP,KCNTATCATQRLANFLVLSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVRSSNNLGVPLPPTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00672
IAPP,IAPP,KCNTATCATQRLANFLVHSGNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVRSSNNLGVPLPPTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00673
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVRSSNNLGVPLPPTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00674
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00675
IAPP,IAPP,KCNTATCATQRLANFLVRSSNNLGVPLPPTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00676
IAPP,IAPP,KCNTATCATQRLANFLVLSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00677
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAPLSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00678
IAPP,IAPP,KCNTATCATQRLANFLVHSGNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAPLSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00679
IAPP,IAPP,KCNTATCATQRLANFLVHSGNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00680
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVLSSNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00681
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVLSSNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00682
IAPP,IAPP,KCNTATCATQRLANFLVRSSNNLGVPLPPTNVGSNTY,KCNTATCATQRLANFLVLSSNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00683
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAPLSSTNVGSNTY,KCNTATCATQRLANFLVLSSNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00684
IAPP,IAPP,KCNTATCATQRLANFLVHSGNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVLSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00685
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAPLSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00686
IAPP,IAPP,KCNTATCATQRLANFLVRSSNNLGVPLPPTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAPLSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00687
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00688
IAPP,IAPP,KCNTATCATQRLANFLVLSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAPLSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00689
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSGNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00690
IAPP,IAPP,KCNTATCATQRLANFLVRSSNNLGVPLPPTNVGSNTY,KCNTATCATQRLANFLVHSGNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00691
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSGNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00692
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAPLSSTNVGSNTY,KCNTATCATQRLANFLVHSGNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00693
IAPP,IAPP,KCNTATCATQRLANFLVLSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSGNNFGAILSSTNVGSNTY,No effect,No,Yes,NA,NA,NA,NA,10.1039/C7SC00620A,AG00694
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,aB42 inhibits aB40 i ratio 1:9,10.1038/emboj.2010.211,AG00695
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,aB42 accelerates aB40 in ratio 3:7,10.1038/emboj.2010.211,AG00696
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,aB40 inhibits aB42,10.1038/emboj.2010.211,AG00697
CsgA,Amyloid beta,MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1371/journal.ppat.1007978,AG00698
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No information,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,WT-TTR / Abeta (1–42),10.1016/j.febslet.2008.02.034,AG00699
Transthyretin,Amyloid beta,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGEPHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No information,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,"L55P TTR, amyloidogenic / Abeta (1–42)",10.1016/j.febslet.2008.02.034,AG00700
Transthyretin,Amyloid beta,GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTMAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No information,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,"T119M TTR, non- amyloidogenic / Abeta (1–42)",10.1016/j.febslet.2008.02.034,AG00701
Cystatin C,Amyloid beta,MAGPLRAPLLLLAILAVALAVSPAAGSSPGKPPRLVGGPMDASVEEEGVRRALDFAVGEYNKASNDMYHSRALQVVRARKQIVAGVNYFLDVELGRTTCTKTQPNLDNCPFHDQPHLKRKAFCSFQIYAVPWQGTMTLSKSTCQDA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.neurobiolaging.2003.11.006,AG00702
Cystatin C,Amyloid beta,MAGPLRAPLLLLAILAVALAVSPAAGSSPGKPPRLVGGPMDASVEEEGVRRALDFAVGEYNKASNDMYHSRALQVVRARKQIVAGVNYFLDVELGRTTCTKTQPNLDNCPFHDQPHLKRKAFCSFQIYAVPWQGTMTLSKSTCQDA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.neurobiolaging.2003.11.006,AG00703
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.jmb.2018.06.005,AG00704
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.jmb.2018.06.005,AG00705
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.jmb.2018.06.005,AG00706
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.jmb.2018.06.005,AG00707
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.jmb.2018.06.005,AG00708
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.jmb.2018.06.005,AG00709
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.jmb.2018.06.005,AG00710
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No,No,NA,NA,NA,NA,10.1016/j.jmb.2018.06.005,AG00711
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.jmb.2018.06.005,AG00712
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1016/j.jmb.2018.06.005,AG00713
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1074/jbc.C112.400614,AG00714
PrP,Amyloid beta,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSD,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1074/jbc.C112.400614,AG00715
PrP,Amyloid beta,GLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No information,NA,NA,NA,NA,10.1074/jbc.C112.400614,AG00716
PrP,Amyloid beta,QPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1074/jbc.C112.400614,AG00717
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No information,"Yes, direct evidence.",Yes,NA,NA,NA,NA,10.1039/D0CC02463E,AG00719
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No information,"Yes, direct evidence.",Yes,NA,NA,NA,NA,10.1039/D0CC02463E,AG00720
FapC,Alpha-synuclein,GPAEKWKPTPAPTGTVAAAVTDTQVSKDNKFDDTKTLNNAGANGSLSNSKGNLGANIAAGSGNQQDNAAAITSSAGDAATVFAVADIYQESKDNKFTNKGTQNNALLNNSANNSSGNVGVNVAAGQGNQQKNNLAIVTADGKNVAAASNTEQVSLDNHFLNEASSKHSYKPQYVVNNAGLLNSANNASGNIGVNVAAGAGNQQSNTLTLGSGCTVCAAGTGSKLAFLEHHHHHH,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No effect,No,No,NA,NA,NA,NA,10.1021/acsomega.8b03590,AG00721
FapC,Alpha-synuclein,GPAEKWKPTPAPTGTVAAAVTDTQVSKDNKFDDTKTLNNAGANGSLSNSKGNLGANIAAGSGNQQDNAAAITSSAGDAATVFAVADIYQESKDNKFTNKGTQNNALLNNSANNSSGNVGVNVAAGQGNQQKNNLAIVTADGKNVAAASNTEQVSLDNHFLNEASSKHSYKPQYVVNNAGLLNSANNASGNIGVNVAAGAGNQQSNTLTLGSGCTVCAAGTGSKLAFLEHHHHHH,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1021/acsomega.8b03590,AG00722
FapC,Alpha-synuclein,GPAEKWKPTPAPTGTVAAAVTDTQVSKDNKFDDTKTLTSSAGDAATVFAVADIYQESKDNKFTNKGTQVTADGKNVAAASNTEQVSLDNHFLNEASSKHSYKPQYVVLGSGCTVCAAGTGSKLAFLEHHHHHH,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1021/acsomega.8b03590,AG00723
FapC,Alpha-synuclein,GPAEKWKPTPAPTGTVAAAVTDTQVSKDNKFDDTKTLTSSAGDAATVFAVADIYQESKDNKFTNKGTQVTADGKNVAAASNTEQVSLDNHFLNEASSKHSYKPQYVVLGSGCTVCAAGTGSKLAFLEHHHHHH,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1021/acsomega.8b03590,AG00724
FapC,Alpha-synuclein,GPAEKWKPTPAPTGTVAAAVTDTQVSKDNKFDDTKTLTSSAGDAATVFAVADIYQESKDNKFTNKGTQVTADGKNVAAASNTEQVSLDNHFLNEASSKHSYKPQYVVLGSGCTVCAAGTGSKLAFLEHHHHHH,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No effect,No,No,NA,NA,NA,NA,10.1021/acsomega.8b03590,AG00725
Tau,Amyloid beta,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"In the presence of tau, the Abeta amyloid formation was retarded in a concentration-dependent manner",NA,NA,Interactor: Tau 441 Interactee: Amyloid beta 40,10.1021/jacs.7b13623,AG00726
Tau,Amyloid beta,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Our results show that: (1) tau-441 prevents Abeta fibrillation at a stoichiometric Abeta:tau ratio (results by Thioflavin T (ThT) kinetics assay, transmission electron microscopy (TEM), NMR spectroscopy)","Our results show that: (1) tau-441 prevents Abeta fibrillation at a stoichiometric Abeta:tau ratio (results by Thioflavin T (ThT) kinetics assay, transmission electron microscopy (TEM), NMR spectroscopy)","Our results show that: (1) tau-441 prevents Abeta fibrillation at a stoichiometric Abeta:tau ratio (results by Thioflavin T (ThT) kinetics assay, transmission electron microscopy (TEM), NMR spectroscopy)",Interactor: Tau 441 Interactee: Amyloid beta 40 Abeta40:Tau = 1:2,10.1021/jacs.7b13623,AG00727
IAPP,Amyloid beta,ATQRLANFLVHLLLNFGAILS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,"Interactor (L3-GI) = [(N-Me)G24,(N-Me)I26]-( IAPP(8-18) + LLL + IAPP(22-28) )",10.1002/anie.201504973,AG00728
IAPP,Amyloid beta,ATQRLANFLVHVVVNFGAILS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,"Interactor (V3-GI) = [(N-Me)G24,(N-Me)I26]-( IAPP(8-18) + VVV + IAPP(22-28) )",10.1002/anie.201504973,AG00729
IAPP,Amyloid beta,ATQRLANFLVHGGGNFGAILS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No information,No information,NA,NA,NA,NA,10.1002/anie.201504973,AG00730
IAPP,Amyloid beta,ATQRLANFLVHAAANFGAILS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No information,No information,NA,NA,NA,NA,10.1002/anie.201504973,AG00731
IAPP,Amyloid beta,ATQRLANFLVHSSNNFGAILS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No information,No information,NA,NA,NA,NA,10.1002/anie.201504973,AG00732
IAPP,IAPP,ATQRLANFLVHLLLNFGAILS,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1002/anie.201504973,AG00733
IAPP,IAPP,ATQRLANFLVHVVVNFGAILS,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No information,No information,NA,NA,NA,NA,10.1002/anie.201504973,AG00734
IAPP,IAPP,ATQRLANFLVHGGGNFGAILS,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No information,No information,NA,NA,NA,NA,10.1002/anie.201504973,AG00735
IAPP,IAPP,ATQRLANFLVHAAANFGAILS,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No information,No information,NA,NA,NA,NA,10.1002/anie.201504973,AG00736
IAPP,IAPP,ATQRLANFLVHSSNNFGAILS,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No information,No information,NA,NA,NA,NA,10.1002/anie.201504973,AG00737
IAPP,Amyloid beta,ATQRLANFLVHIIINFGAILS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1002/anie.201504973,AG00738
IAPP,Amyloid beta,ATQRLANFLVHFFFNFGAILS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1002/anie.201504973,AG00739
IAPP,Amyloid beta,ATQRLANFLVHRRRNFGAILS,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1002/anie.201504973,AG00740
Alpha-crystallin,Kappa-casein,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK,MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYG LNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHP HPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEI NTVQVTSTAV,No aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1007/s12192-010-0212-z,AG00741
Alpha-casein,Kappa-casein,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYG LNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHP HPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEI NTVQVTSTAV,No aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1007/s12192-010-0212-z,AG00742
Beta-casein,Kappa-casein,MKVLILACLVALALARELEELNVPGEIVESLSSSEESITRINKKIEKFQSEEQQQTEDELQDKIHPFAQTQSLVYPFPGPIPNSLPQNIPPLTQTPVVVPPFLQPEVMGVSKVKEAMAPKHKEMPFPKYPVEPFTESQSLTLTDVENLHLPLPLLQSWMHQPHQPLPPTVMFPPQSVLSLSQSKVLPVPQKAVPYPQRDMPIQAFLLYQEPVLGPVRGPFPIIV,MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYG LNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHP HPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEI NTVQVTSTAV,No aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1007/s12192-010-0212-z,AG00743
Alpha-crystallin,Amyloid beta,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,NA,10.1007/s12192-010-0212-z,AG00744
Tau,Tau,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,FL Tau monomers were seeded with sonicated pre-formed FL Tau fibrils in the presence of poly-L-glutamate,10.1371/journal.pone.0201182,AG00745
Tau,Tau,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1371/journal.pone.0201182,AG00746
Tau,Tau,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1371/journal.pone.0201182,AG00747
Apolipoprotein A-I,Amyloid beta,DEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,We assume that Apolipoprotein A-I (described as bought in Sigma) is a variant from the human plasma,10.1021/bi002186k,AG00748
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,KLVFFAE,No effect,No,No,"When incubated in isolation, a 5% (w/w) TAMRA-Ahx-Abeta16–22:95% Abeta16–22 mixture (20 μM) resulted in a rapid decrease in fluorescence intensity followed by a slower phase that plateaued after 1 hour. In the presence of Abeta40 [1:1 (mol/mol) ratio, 40 μM total peptide concentration, and 2% (v/v) dimethyl sulfoxide (DMSO)], no difference in the rate of fluorescence decrease was observed, indicating that the presence of Abeta40 has no effect on Abeta16–22 aggregation (Fig. 2C).","Sedimentation of the mixed system by centrifugation after 1 hour demonstrated that Abeta40 was present mainly in the supernatant (Fig. 2, D and E). These results demonstrate that Abeta16–22 aggregates rapidly to form amyloid-like fibrils, while Abeta40 remains soluble as monomers/oligomers. Thus, although the rate of Abeta40 aggregation is increased by the presence of Abeta16–22, limited or no co-assembly between the two peptides into fibrils was observed. By contrast, Abeta16–22 aggregation is unaffected by the presence of Abeta40.","Sedimentation of the mixed system by centrifugation after 1 hour demonstrated that Abeta40 was present mainly in the supernatant (Fig. 2, D and E). These results demonstrate that Abeta16–22 aggregates rapidly to form amyloid-like fibrils, while Abeta40 remains soluble as monomers/oligomers. Thus, although the rate of Abeta40 aggregation is increased by the presence of Abeta16–22, limited or no co-assembly between the two peptides into fibrils was observed. By contrast, Abeta16–22 aggregation is unaffected by the presence of Abeta40.","interactor: Abeta (1–40) interactee: Abeta-(16-22) 1:1 (molar ratio) Abeta-(16-22) aggregates more rapidly than Abeta-40 As the assembly kinetics of Abeta16–22 could not be measured using any of the amyloid dyes surveyed at the concentrations used here, a fluorescence quenching assay was developed to determine whether Abeta16–22 aggregates more or less rapidly than Abeta40. For these assays, Abeta16–22 N-terminally labeled with tetramethylrhodamine (TAMRA) was synthesized, including a 6-aminohexanoic acid linker (Ahx) to limit disruption to the native fibril structure that might arise due to the bulky fluorophore.",10.1126/sciadv.aav8216,AG00749
Amyloid beta,Amyloid beta,KLVFFAE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,NA,"We have shown here that Abeta40 monomers and oligomers dock onto the fibril surface, which catalyzes the assembly of antiparallel strand formation in close situ to the parent Abeta16–22 fiber.","PIC experiments performed 5 min and 24 hours after initiating assembly failed to detect cross-links between Abeta*16–22 and Abeta40 (Fig. 5C, fig. S6, and table S2). Instead, all identifiable cross-links were consistent with intermolecular/intramolecular Abeta*16–22 or solvent adducts, indicating that co-assembly into fibrils either is very rare and cannot be detected despite the sensitivity of ESI-MS or does not occur.",interactor: Abeta-(16-22) monomers interactee: Abeta (1–40),10.1126/sciadv.aav8216,AG00750
Amyloid beta,Amyloid beta,KLVFFAE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,NA,"We have shown here that Abeta40 monomers and oligomers dock onto the fibril surface, which catalyzes the assembly of antiparallel strand formation in close situ to the parent Abeta16–22 fiber.","PIC experiments performed 5 min and 24 hours after initiating assembly failed to detect cross-links between Abeta*16–22 and Abeta40 (Fig. 5C, fig. S6, and table S2). Instead, all identifiable cross-links were consistent with intermolecular/intramolecular Abeta*16–22 or solvent adducts, indicating that co-assembly into fibrils either is very rare and cannot be detected despite the sensitivity of ESI-MS or does not occur.",interactor: Abeta-(16-22) fibrils (sonicated and non-sonicated) interactee: Abeta (1–40),10.1126/sciadv.aav8216,AG00751
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Abeta3(pE)-42 with Abeta1-42,10.1038/nature11060,AG00752
Alpha-crystallin,Alpha-crystallin,KFVIFLDVKHFSPEDLTVK,SDRDKFVIFLDVKHF,Faster aggregation,"Yes, direct evidence.",No,"The results show that the presence of increased amounts of aA-(66-80) peptide in the incubation mixture leads to increased aggregation, light scattering and precipitation.",NA,NA,Interactor: bovine alpha-Crystallin (source sequence unavailable) Interactee: human alphaA-(66-80),10.1371/journal.pone.0019291,AG00753
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLG,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,aSyn120 accelerate full-length aSyn,10.1074/jbc.M501508200,AG00754
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,aSyn1q0 accelerate full-length aSyn,10.1074/jbc.M501508200,AG00755
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDP,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,aSyn(A53T )120 accelerate full-length A53T aSyn,10.1074/jbc.M501508200,AG00756
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQE,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,aSyn(A53T )110 accelerate full-length A53T aSyn,10.1074/jbc.M501508200,AG00757
Amyloid beta,Alpha-synuclein,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,HHHHHHMDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,His6 aS+ aB42,10.3390/molecules25030580,AG00758
Amyloid beta,Alpha-synuclein,EFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,HHHHHHMDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,His6 aS+ pGlu aB,10.3390/molecules25030580,AG00759
Amyloid beta,Alpha-synuclein,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,WT aS+ aB42,10.3390/molecules25030580,AG00760
Amyloid beta,Alpha-synuclein,EFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,WT aS+ pGlu aB,10.3390/molecules25030580,AG00761
CsgA,SEVI,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,GIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,"CsgA preformed fibers / 440 μM PAP248-286 (SEVI) CsgA 1%, 2,5%, 5% - mol%, I assumed that it is from E.coli",10.7717/peerj.5,AG00762
CsgB,SEVI,AGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR,GIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMY,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,"CsgB preformed fibers (CsgB 1%, 2,5%, 5% - mol%) / 440 μM PAP248-286; I assumed that it is from E.coli",10.7717/peerj.5,AG00763
CsgA,Amyloid beta,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"CsgA preformed fibers (CsgA 1%, 2,5%, 5% 10% - mol%) / 5 μM Abeta (1–40) CsgA 1%, 2,5%, 5% - mol%, I assumed that it is from E.coli",10.7717/peerj.5,AG00764
CsgB,Amyloid beta,AGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"CsgB preformed fibers (CsgB 10% - mol%) / 5 μM Abeta (1–40) CsgB 1%, 2,5%, 5% - mol%, I assumed that it is from E.coli",10.7717/peerj.5,AG00765
CsgB,IAPP,AGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"CsgB preformed fibers (CsgB 1%, 2,5%, 5%, 10% - mol%) / 2,5 μM IAPP CsgA 1%, 2,5%, 5% - mol%, I assumed that it is from E.coli",10.7717/peerj.5,AG00766
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No,Yes,NA,NA,NA,Preformed Abeta (1–40) (1% - mol%) / 5 μM Abeta (1–40),10.7717/peerj.5,AG00767
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"Preformed Abeta (1–40) (2,5%, 5%, 10% - mol%) / 5 μM Abeta (1–40)",10.7717/peerj.5,AG00768
CsgB,Amyloid beta,AGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,CsgB preformed fibers (CsgB 1% - mol%) / 5 μM Abeta (1–40) CsgB - I assumed that it is from E.coli,10.7717/peerj.5,AG00769
CsgB,Amyloid beta,AGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"CsgB preformed fibers (CsgB 2,5%, 5% - mol%) / 5 μM Abeta (1–40) CsgB - I assumed that it is from E.coli",10.7717/peerj.5,AG00770
CsgA,IAPP,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"CsgA preformed fibers (CsgA 1%, 2,5% - mol%) / 2,5 μM IAPP CsgA - I assumed that it is from E.coli",10.7717/peerj.5,AG00771
CsgA,IAPP,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"CsgA preformed fibers (CsgA 10% - mol%) / 2,5 μM IAPP CsgA - I assumed that it is from E.coli",10.7717/peerj.5,AG00772
CsgA,IAPP,GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,"CsgA preformed fibers (CsgA 5% - mol%) / 2,5 μM IAPP CsgA - I assumed that it is from E.coli",10.7717/peerj.5,AG00773
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,"Yes, direct evidence.",No,"As observed in TEM images, Aß alone formed typical amyloid fibrils, with diameters of ∼10 nm, lengths of 1 µm or more, and a characteristic twisted appearance (Figure 1A).",NA,NA,NA,10.1021/bi0618520,AG00774
Transthyretin,Amyloid beta,MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,No,No,light scattering and electron microscopy clearly showed that TTR strongly suppressed AB aggregation,"Emission spectra of TTR alone and with Aâ showed decreasing fluorescence intensity with increasing AB concentration (Figure 6A), but no shift in the wavelength for maximum fluorescence",NA,NA,10.1021/bi0618520,AG00775
Beta2-microglobulin,Beta2-microglobulin,IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILAHTEFTPTETDTYACRVKHASMAEPKTVYWDRDM,IQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM,Slower aggregation,No,No,NA,NA,NA,mb2m (PDB ID code 1LK2) was mixed with DN6 (PDB ID code 2XKU),10.1016/j.molcel.2014.05.026,AG00776
Beta2-microglobulin,Beta2-microglobulin,IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILAHTEFTPTETDTYACRVKHASMAEPKTVYWDRDM,IQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM,No aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,The dependence of the lag time on the concentration of mb2m added (Figure S1A available online) suggests that inhibition of fibrillation is a kinetically determined process. mb2m (PDB ID code 1LK2) was mixed with DN6 (PDB ID code 2XKU),10.1016/j.molcel.2014.05.026,AG00777
Beta2-microglobulin,Beta2-microglobulin,IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSESKDWSFYILAHTEFTPTETDTYACRVKHASMAEPKTVYWDRDM,IQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM,Slower aggregation,No information,No information,NA,NA,NA,(F56E)mb2m (PDB ID code 1LK2) was mixed with DN6 (PDB ID code 2XKU),10.1016/j.molcel.2014.05.026,AG00778
Beta2-microglobulin,Beta2-microglobulin,IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDESFYILAHTEFTPTETDTYACRVKHASMAEPKTVYWDRDM,IQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM,Slower aggregation,No information,No information,NA,NA,NA,(W60E)mb2m (PDB ID code 1LK2) was mixed with DN6 (PDB ID code 2XKU),10.1016/j.molcel.2014.05.026,AG00779
Beta2-microglobulin,Beta2-microglobulin,IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM,IQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM,Slower aggregation,No information,No information,NA,NA,NA,Hb2m (PDB ID code 2XKS) was mixed with DN6 (PDB ID code 2XKU),10.1016/j.molcel.2014.05.026,AG00780
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,Faster aggregation,Yes; implied by kinetics.,No information,NA,"As shown in Figure 1B, Ab40 accelerated PrP-amyloid formation with a half-saturation concentration very similar to that of Ab42",NA,interactor: Abeta (1–40) interactee: human PrP,10.1002/anie.201800197,AG00781
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,Faster aggregation,Yes; implied by kinetics.,No information,NA,This result confirms that Ab42 can accelerate PrP-amyloid formation at submicromolar concentrations.,NA,interactor: Abeta (1–42) interactee: human PrP,10.1002/anie.201800197,AG00782
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVPFAEDVGSNKGAIIGLMVGGVVIA,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,No effect,No information,No information,"In contrast, F19P substitution completely abolished the amyloidogenic effect of Ab42 (Figure 1C), and no significant difference of t 1/2 was observed even when the highest concentration of F19P (2 mm) was added to the reaction mixture.",NA,NA,interactor: Abeta (1–42) F19P mutant interactee: human PrP,10.1002/anie.201800197,AG00783
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,interactor: Abeta (1–42)  interactee: human PrP deletion(58-91) mutant,10.1002/anie.201800197,AG00784
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,GLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,interactor: Abeta (1–42)  interactee: human PrP deletion(23-123) mutant,10.1002/anie.201800197,AG00785
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,EYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,No effect,No information,No information,NA,NA,NA,interactor: Abeta (1–42)  interactee: human PrP deletion(23-123 and 124-167) mutant,10.1002/anie.201800197,AG00786
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,GLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDTIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,interactor: Abeta (1–42)  interactee: human PrP deletion(23-123 and 168-182) mutant,10.1002/anie.201800197,AG00787
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,GLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNFTETDVKMMERVVEQMCITQYERESQAYYQRGS,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,interactor: Abeta (1–42)  interactee: human PrP deletion(23-123 and 181-196) mutant,10.1002/anie.201800197,AG00788
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,GLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGE,No effect,No information,No information,NA,NA,NA,interactor: Abeta (1–42)  interactee: human PrP deletion(23-123 and 197-230) mutant,10.1002/anie.201800197,AG00789
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,GLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGEITQYERESQAYYQRGS,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,interactor: Abeta (1–42)  interactee: human PrP deletion(23-123 and 197-214) mutant,10.1002/anie.201800197,AG00790
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,GLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCI,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,interactor: Abeta (1–42)  interactee: human PrP deletion(23-123 and 216-230) mutant,10.1002/anie.201800197,AG00791
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,ITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,interactor: Abeta (1–42)  interactee: human PrP deletion(23-123 and 124-167 and 168-181) mutant,10.1002/anie.201800197,AG00792
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,EYSNQNNFVHDCVNNFTETDVKMMERVVEQMCITQYERESQAYYQRGS,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,interactor: Abeta (1–42)  interactee: human PrP deletion(23-123 and 124-167 and 182-196) mutant,10.1002/anie.201800197,AG00793
Amyloid beta,Lysozyme,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,interactor: Abeta (1–42)  interactee: chicken lysozyme,10.1002/anie.201800197,AG00794
Amyloid beta,Lysozyme,DAEFRHDSGYEVHHQKLVPFAEDVGSNKGAIIGLMVGGVVIA,MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,No effect,No information,No information,NA,NA,NA,interactor: Abeta (1–42) F19P mutant interactee: chicken lysozyme,10.1002/anie.201800197,AG00795
Amyloid beta,PrP,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS,No effect,No information,No information,"As shown in Figure 1D, the mature Ab42-fibrils did not exhibit any amyloidogenic effect on PrP even when the highest concentration (2 um) was employed.",NA,NA,interactor: Abeta (1–42) fibrils interactee: human PrP,10.1002/anie.201800197,AG00798
Lysozyme,Alpha-synuclein,MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,No,No,the presence of lysozyme seeds significantly reduced the duration of the lag phase of WT aSyn aggregation (lag phase 19.5 ± 1.7 h). (Fig. S2A),Both green aSyn fibril and red lysozyme fibrils can be individually observed without significant co-localization or overlap. The visual absence of green aSyn fibrils directly extending from red lysozyme fibril indicates that aSyn monomers do not elongate from lysozyme seeds.,NA,"interactor: hen lysozyme interactee: aSyn The lag phase of aSyn aggregation was found to decrease with increasing concentration of lysozyme seeds. & When WT aSyn was aggregated in the presence of a fixed equivalent monomer concentration of lysozyme seeds (Fig. S4), the lag phase was not significantly affected by a change in sonication time (Fig. 3B).",10.1016/j.jbc.2021.100358,AG00799
Lysozyme,Alpha-synuclein,MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,No,No,"Judging from the increase in ThT fluorescenc with time, aggregation of A53T aSyn (Fig. S2B) in presence of lysozyme fibril seeds shows a similar trend to the results obtained with WT aSyn.",Both green aSyn fibril and red lysozyme fibrils can be individually observed without significant co-localization or overlap. The visual absence of green aSyn fibrils directly extending from red lysozyme fibril indicates that aSyn monomers do not elongate from lysozyme seeds.,Both green aSyn fibril and red lysozyme fibrils can be individually observed without significant co-localization or overlap. The visual absence of green aSyn fibrils directly extending from red lysozyme fibril indicates that aSyn monomers do not elongate from lysozyme seeds.,"interactor: hen lysozyme interactee: aSyn A53T The lag phase of aSyn aggregation was found to decrease with increasing concentration of lysozyme seeds. & When WT aSyn was aggregated in the presence of a fixed equivalent monomer concentration of lysozyme seeds (Fig. S4), the lag phase was not significantly affected by a change in sonication time (Fig. 3B).",10.1016/j.jbc.2021.100358,AG00800
Beta-lactoglobulin,Alpha-synuclein,MKCLLLALALTCGAQALIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"Judging from the increase in ThT fluorescence with time (Fig. S2A), the aggregation of WT aSyn (lag phase 41 ± 10 h) could not be cross-seeded by either of the beta-lactoglobulin seed polymorphs (lag phase 47.6 ± 17 h for B100; data for B13 not shown)","Judging from the increase in ThT fluorescence with time (Fig. S2A), the aggregation of WT aSyn (lag phase 41 ± 10 h) could not be cross-seeded by either of the beta-lactoglobulin seed polymorphs (lag phase 47.6 ± 17 h for B100; data for B13 not shown),",NA,interactor: bovine beta-lactoglobulin interactee: aSyn,10.1016/j.jbc.2021.100358,AG00801
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,"Abeta40 aggregation was efficiently seeded by Abeta40 seeds (blue dots, Figure 6b)",NA,NA,interactee - Abeta40 monomers interactor - Abeta40 seeds,10.1074/jbc.M111.264473,AG00806
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"Addition of pure Abeta42 not only does not seed aggregation, but even lengthens the lag phase (black dots, Figure 6b)","Addition of pure Abeta42 not only does not seed aggregation, but even lengthens the lag phase",NA,interactee - Abeta40 monomers interactor - Abeta42 seeds,10.1074/jbc.M111.264473,AG00807
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),Faster aggregation,Yes; implied by kinetics.,No information,"The 1:9 ratio is seeded by any seed (blue dots, Figure 6c)",NA,NA,interactee - mixture of Abeta42:Abeta40 monomers in ratio 1:9 interactor - Abeta40 seeds,10.1074/jbc.M111.264473,AG00808
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),Faster aggregation,Yes; implied by kinetics.,No information,"The 1:9 ratio is seeded by any seed (black dots, Figure 6c)",NA,NA,interactee - mixture of Abeta42:Abeta40 monomers in ratio 1:9 interactor - Abeta42 seeds,10.1074/jbc.M111.264473,AG00809
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),Faster aggregation,Yes; implied by kinetics.,No information,"the 3:7 ratio were equally effectively seeded by any Abeta seed, regardless of whether they were formed from Abeta40 or Abeta42 or a mixture (blue dots, Figure 6d)",NA,NA,interactee - mixture of Abeta42:Abeta40 monomers in ratio 3:7 interactor - Abeta40 seeds,10.1074/jbc.M111.264473,AG00810
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),Faster aggregation,Yes; implied by kinetics.,No information,"the 3:7 ratio were equally effectively seeded by any Abeta seed, regardless of whether they were formed from Abeta40 or Abeta42 or a mixture (black dots, Figure 6d)",NA,NA,interactee - mixture of Abeta42:Abeta40 monomers in ratio 3:7 interactor - Abeta42 seeds,10.1074/jbc.M111.264473,AG00811
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"pure Abeta42 and the 3:7 ratio were equally effectively seeded by any Abeta seed, regardless of whether they were formed from Abeta40 or Abeta42 or a mixture (blue dots, Figure 6e)",NA,NA,interactee - Abeta42 monomers interactor - Abeta40 seeds,10.1074/jbc.M111.264473,AG00812
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"pure Abeta42 and the 3:7 ratio were equally effectively seeded by any Abeta seed, regardless of whether they were formed from Abeta40 or Abeta42 or a mixture (black dots, Figure 6e)",NA,NA,interactee - Abeta42 monomers interactor - Abeta42 seeds,10.1074/jbc.M111.264473,AG00813
Amyloid beta,Amyloid beta,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,"Abeta40 aggregation was efficiently seeded by Abeta40 seeds and the 1:9 ratio seeds leading to elimination of the lag phase (green dots, Figure 6b)",NA,NA,interactee - Abeta40 monomers interactor - mixture of Abeta42:Abeta40 seeds in ratio 1:9,10.1074/jbc.M111.264473,AG00814
Amyloid beta,Amyloid beta,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,"red dots, Figure 6b",NA,NA,interactee - Abeta40 monomers interactor - mixture of Abeta42:Abeta40 seeds in ratio 3:7,10.1074/jbc.M111.264473,AG00815
Amyloid beta,Amyloid beta,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),Faster aggregation,Yes; implied by kinetics.,No information,"The 1:9 ratio is seeded by any seed (green dots, Figure 6c)",NA,NA,interactee - mixture of Abeta42:Abeta40 monomers in ratio 1:9 interactor - mixture of Abeta42:Abeta40 seeds in ratio 1:9,10.1074/jbc.M111.264473,AG00816
Amyloid beta,Amyloid beta,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),Faster aggregation,Yes; implied by kinetics.,No information,"The 1:9 ratio is seeded by any seed (red dots, Figure 6c)",NA,NA,interactee - mixture of Abeta42:Abeta40 monomers in ratio 1:9 interactor - mixture of Abeta42:Abeta40 seeds in ratio 3:7,10.1074/jbc.M111.264473,AG00817
Amyloid beta,Amyloid beta,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),Faster aggregation,Yes; implied by kinetics.,No information,"the 3:7 ratio were equally effectively seeded by any Abeta seed, regardless of whether they were formed from Abeta40 or Abeta42 or a mixture (green dots, Figure 6d)",NA,NA,interactee - mixture of Abeta42:Abeta40 monomers in ratio 3:7 interactor - mixture of Abeta42:Abeta40 seeds in ratio 1:9,10.1074/jbc.M111.264473,AG00818
Amyloid beta,Amyloid beta,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),Faster aggregation,Yes; implied by kinetics.,No information,"the 3:7 ratio were equally effectively seeded by any Abeta seed, regardless of whether they were formed from Abeta40 or Abeta42 or a mixture (red dots, Figure 6d)",NA,NA,interactee - mixture of Abeta42:Abeta40 monomers in ratio 3:7 interactor - mixture of Abeta42:Abeta40 seeds in ratio 3:7,10.1074/jbc.M111.264473,AG00819
Amyloid beta,Amyloid beta,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"pure Abeta42 and the 3:7 ratio were equally effectively seeded by any Abeta seed, regardless of whether they were formed from Abeta40 or Abeta42 or a mixture (green dots, Figure 6e)",NA,NA,interactee - Abeta42 monomers interactor - mixture of Abeta42:Abeta40 seeds in ratio 1:9,10.1074/jbc.M111.264473,AG00820
Amyloid beta,Amyloid beta,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Faster aggregation,Yes; implied by kinetics.,No information,"pure Abeta42 and the 3:7 ratio were equally effectively seeded by any Abeta seed, regardless of whether they were formed from Abeta40 or Abeta42 or a mixture (red dots, Figure 6e)",NA,NA,interactee - Abeta42 monomers interactor - mixture of Abeta42:Abeta40 seeds in ratio 3:7,10.1074/jbc.M111.264473,AG00821
Amyloid beta,Alpha-crystallin,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,SDRDKFVIFLDVKHF,Faster aggregation,Yes; implied by kinetics.,No,"a drastic reduction in the lag time of alphaA(66–80) aggregation was recorded in the presence of Aß(1–40). As it can be seen in Fig. 3B, the lag time was reduced from 16 ± 0.7 to 7 ± 1 h in the presence of Aß(1–40).","a drastic reduction in the lag time of alphaA(66–80) aggregation was recorded in the presence of Aß(1–40). As it can be seen in Fig. 3B, the lag time was reduced from 16 ± 0.7 to 7 ± 1 h in the presence of Aß(1–40).","As can be seen in Fig. 3A, the fibril structures formed by mixture of 90% alphaA(66–80) and 10% Abeta(1–40), did not differ considerably from that of alphaA(66–80) peptide alone, indicating that the majority of fibrils derived from aggregation of alphaA(66–80).",interactor: Aß(1–40) monomers 10% and 50%  interactee: alphaA(66–80) monomers,10.1016/j.ijbiomac.2021.02.111,AG00822
Alpha-crystallin,Alpha-crystallin,SDRDKFVIFLDVKHF,SDRDKFVIFLDVKHF,Faster aggregation,Yes; implied by kinetics.,No,Addition of homologous seeds (pre aggregated alphaA(66–80)) led to a minor enhancement in the aggregation reaction of the freshly dissolved alphaA(66–80) (Fig. 4). The lag time of the seeded reaction was found to be 7 ± 2 h compared to 8 ± 2 h for unseeded reactions. These findings indicate that aggregation patterns of alphaA(66–80) remained unchanged in the presence of homologous or heterologous pre-aggregated fibrils.,Addition of homologous seeds (pre aggregated alphaA(66–80)) led to a minor enhancement in the aggregation reaction of the freshly dissolved alphaA(66–80) (Fig. 4). The lag time of the seeded reaction was found to be 7 ± 2 h compared to 8 ± 2 h for unseeded reactions.,These findings indicate that aggregation patterns of alphaA(66–80) remained unchanged in the presence of homologous or heterologous pre-aggregated fibrils.,"interactor: pre-aggregated alphaΑ(66–80) fibrils, 2,5% interactee: alphaA(66–80) monomers",10.1016/j.ijbiomac.2021.02.111,AG00823
Amyloid beta,Alpha-crystallin,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,SDRDKFVIFLDVKHF,No effect,No,No,"As the data shown in Fig. 5A, the presence of heterologous Abeta(1–40) seeds did not bring any change in the aggregation of pattern of alphaA(66–80). However, the ThT intensity of the seeded reaction was found to be slightly enhanced compared to unseeded reaction that may be possibly due to the presence of Abeta(1–40) seeds. The lag times of seeded and unseeded aggregation reaction remained unchanged (Fig. 5B).","As the data shown in Fig. 5A, the presence of heterologous Abeta(1–40) seeds did not bring any change in the aggregation of pattern of alphaA(66–80). However, the ThT intensity of the seeded reaction was found to be slightly enhanced compared to unseeded reaction that may be possibly due to the presence of Abeta(1–40) seeds.","Consecutively, no significant change was observed in the fibril morphology of alphaA(66–80) fibrils formed in the presence of Abeta(1–40) seed. However, very fewfibrilswere appeared to be elongated and found to be comparatively larger than the majority of the seen in the image. These findings indicate that aggregation patterns of alphaA(66–80) remained unchanged in the presence of homologous or heterologous pre-aggregated fibrils.","interactor: Abeta(1–40) fibrils, 2,5% interactee: alphaA(66–80) monomers",10.1016/j.ijbiomac.2021.02.111,AG00824
Amyloid beta,Amyloid beta,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No,"A significant decrease in the lag time (from 16 ± 5 to 3 ± 0.3 h) was observed for the homologous seeding of Abeta(1–40), indicating a potential seeding behavior.","A significant decrease in the lag time (from 16 ± 5 to 3 ± 0.3 h) was observed for the homologous seeding of Abeta(1–40), indicating a potential seeding behavior.",NA,"interactor: Abeta(1–40) fibrils, 2.5% interactee: Abeta(1–40) monomers",10.1016/j.ijbiomac.2021.02.111,AG00825
proSP-C,Amyloid beta,HMSQKHTEMVLEMSIGAPEAQQRLALSEHLVTTATFSIGSTGLVVYDYQQLLIAYKPAPGTCCYIMKIAPESIPSLEALNRKVHNFQMECSLQAKPAVPTSKLGQAEGRDAGSAPSGGDPAFLGMAVNTLCGEVPLYYI,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No aggregation,Formation of fibrils by the interactee is inhibited,No,"TEM images obtained after incubation for 6 days showed that fibril formation of Abeta1-40 was completely abolished in the presence of CTC even at less than equimolar ratios (Figure 1).  Thioflavin T binding experiments showed that CTC reduces the level of A1-40 polymerization at 1:1, 1:2, and 1:10 molar ratios (Figure 2).",A1-40 was incubated in the presence and absence of CTC at 1:1 and 10:1 molar ratios. TEM images obtained after incubation for 6 days showed that fibril formation of A1-40 was completely abolished in the presence of CTC even at less than equimolar ratios,A1-40 was incubated in the presence and absence of CTC at 1:1 and 10:1 molar ratios. TEM images obtained after incubation for 6 days showed that fibril formation of A1-40 was completely abolished in the presence of CTC even at less than equimolar ratios.,interactor: C-terminal domain of proSP-C (CTC)  interactee: Abeta (1-40),10.1021/bi900135c,AG00826
proSP-C,Medin,HMSQKHTEMVLEMSIGAPEAQQRLALSEHLVTTATFSIGSTGLVVYDYQQLLIAYKPAPGTCCYIMKIAPESIPSLEALNRKVHNFQMECSLQAKPAVPTSKLGQAEGRDAGSAPSGGDPAFLGMAVNTLCGEVPLYYI,EVTGIITQGARNFGSVQFVA,No aggregation,Formation of fibrils by the interactee is inhibited,No,"After incubation for 4 days, medin31-50 showed large amounts of amyloid fibrils as judged by the TEM images (Figure 9A). Addition of CTC at a 1:1 molar ratio completely abolished the formation of fibrils (Figure 9B).","After incubation for 4 days, medin31-50 showed large amounts of amyloid fibrils as judged by the TEM images (Figure 9A). Addition of CTC at a 1:1 molar ratio completely abolished the formation of fibrils (Figure 9B).","After incubation for 4 days, medin31-50 showed large amounts of amyloid fibrils as judged by the TEM images (Figure 9A). Addition of CTC at a 1:1 molar ratio completely abolished the formation of fibrils (Figure 9B).",interactor: C-terminal domain of proSP-C (CTC)  interactee: medin (31-50),10.1021/bi900135c,AG00827
proSP-C,Medin,HMSQKHTEMVLEMSIGAPEAQQRLALSEHLVTTATFSIGSTGLVVYDYQQLLIAYKPAPGTCCYIMKIAPESIPSLEALNRKVHNFQMECSLQAKPAVPTSKLGQAEGRDAGSAPSGGDPAFLGMAVNTLCGEVPLYYI,RLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQFVA,No aggregation,Formation of fibrils by the interactee is inhibited,No,"Full-length medin after 14-21 days formed amyloid fibrils that appeared to be longer than the ones seen with medin31-50. Fibril formation of medin1-50 was likewise prevented by the presence of CTC (Figure 9C,D). These results further strengthen the emerging picture that CTC can recognize and bind peptide species on the pathway to amyloid fibrils and prevent them from polymerizing.","Full-length medin after 14-21 days formed amyloid fibrils that appeared to be longer than the ones seen with medin31-50. Fibril formation of medin1-50 was likewise prevented by the presence of CTC (Figure 9C,D). These results further strengthen the emerging picture that CTC can recognize and bind peptide species on the pathway to amyloid fibrils and prevent them from polymerizing.","Full-length medin after 14-21 days formed amyloid fibrils that appeared to be longer than the ones seen with medin31-50. Fibril formation of medin1-50 was likewise prevented by the presence of CTC (Figure 9C,D). These results further strengthen the emerging picture that CTC can recognize and bind peptide species on the pathway to amyloid fibrils and prevent them from polymerizing.",interactor: C-terminal domain of proSP-C (CTC)  interactee: medin (1-50),10.1021/bi900135c,AG00828
TDP-43,Amyloid beta,MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRTSQAHRVITKTKATCRGSQTRPSVLEITLIVALILVQQLVGDQHPMQGRAVVLMEALAQAWILSLLAGECRQWGCGWLV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,whereas the lag time was significantly prolonged to ~75 h in the presence of TDP-43. The final ThT signal of Abeta with TDP-43 was reduced to ~50% compared with the signal of Abeta alone (Figure 1a).,whereas the lag time was significantly prolonged to ~75 h in the presence of TDP-43. The final ThT signal of Abeta with TDP-43 was reduced to ~50% compared with the signal of Abeta alone (Figure 1a).,NA,"interactor: 0.25 μM, TDP-43 FL interactee: 25 μM Abeta (1–40)   We further found that the inhibition of Aß fibrillization by TDP-43 only occurs in the early and intermediate stages of Aß fibrillization, but not in the fibrillar stage and the seeding reaction. The result demonstrated that TDP-43 does not affect mature Aß fibrils and cannot block fibril growth once the fibril nucleus was added.",10.1038/s41467-020-19786-7,AG00829
TDP-43,Amyloid beta,MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRTSQAHRVITKTKATCRGSQTRPSVLEITLIVALILVQQLVGDQHPMQGRAVVLMEALAQAWILSLLAGECRQWGCGWLV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No,No,"TDP-43 was introduced to the Abeta fibril solution (Fig. 1g), TDP- 43 could not alter the status of Abeta fibrils. The ThT signal of Abeta fibrils remained the same during the observation.",also used immunogold TEM to observe the possible location of TDP-43 in Abeta fibrils by immunogold labeling of TDP-43. We found that some immunogold labeled TDP-43 attached to Abeta fibrils especially at the clusters of fibrils,"also used immunogold TEM to observe the possible location of TDP-43 in Abeta fibrils by immunogold labeling of TDP-43. We found that some immunogold labeled TDP-43 attached to Abeta fibrils especially at the clusters of fibrils (Supplementary Fig. 2d), but no apparent morphological changes of Abeta fibrils were observed.","interactor: 0.25 μM, TDP-43 FL interactee: 25 μM Abeta (1–40) preformed fibrils  We further found that the inhibition of Aß fibrillization by TDP-43 only occurs in the early and intermediate stages of Aß fibrillization, but not in the fibrillar stage and the seeding reaction. The result demonstrated that TDP-43 does not affect mature Aß fibrils and cannot block fibril growth once the fibril nucleus was added.",10.1038/s41467-020-19786-7,AG00830
TDP-43,Amyloid beta,MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRTSQAHRVITKTKATCRGSQTRPSVLEITLIVALILVQQLVGDQHPMQGRAVVLMEALAQAWILSLLAGECRQWGCGWLV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No effect,No information,No information,"The results showed that Abeta fibrillization kinetics with the seeding remained the same with or without TDP-43 (Fig. 1h), indicating that TDP-43 could not prevent Abeta fibril growth by seeding.",NA,NA,"interactor: 0.25 μM, TDP-43 FL interactee: 25 μM Abeta (1–40) monomers & 10% preformed Abeta fibrils seeds  We further found that the inhibition of Aß fibrillization by TDP-43 only occurs in the early and intermediate stages of Aß fibrillization, but not in the fibrillar stage and the seeding reaction. The result demonstrated that TDP-43 does not affect mature Aß fibrils and cannot block fibril growth once the fibril nucleus was added.",10.1038/s41467-020-19786-7,AG00831
TDP-43,Amyloid beta,MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRTSQAHRVITKTKATCRGSQTRPSVLEITLIVALILVQQLVGDQHPMQGRAVVLMEALAQAWILSLLAGECRQWGCGWLV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"Consistent with previous results, TDP-43 added to Abeta monomer effectively blocked Abeta fibrillization (Fig. 1e).","Consistent with previous results, TDP-43 added to Abeta monomer effectively blocked Abeta fibrillization (Fig. 1e).",NA,"interactor: 0.25 μM, TDP-43 FL interactee: 25 μM Abeta (1–40) monomers   We further found that the inhibition of Aß fibrillization by TDP-43 only occurs in the early and intermediate stages of Aß fibrillization, but not in the fibrillar stage and the seeding reaction. The result demonstrated that TDP-43 does not affect mature Aß fibrils and cannot block fibril growth once the fibril nucleus was added.",10.1038/s41467-020-19786-7,AG00832
TDP-43,Amyloid beta,MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRTSQAHRVITKTKATCRGSQTRPSVLEITLIVALILVQQLVGDQHPMQGRAVVLMEALAQAWILSLLAGECRQWGCGWLV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"When TDP-43 was added to the Abeta oligomer solution (Fig. 1f), it is still able to potently inhibit Abeta fibrillization even Abeta already formed oligomeric species, Fig. 1f","When TDP-43 was added to the Abeta oligomer solution (Fig. 1f), it is still able to potently inhibit Abeta fibrillization even Abeta already formed oligomeric species, Fig. 1f",NA,"interactor: 0.25 μM, TDP-43 FL interactee:  25 μM Abeta (1–40) oligomers   We further found that the inhibition of Aß fibrillization by TDP-43 only occurs in the early and intermediate stages of Aß fibrillization, but not in the fibrillar stage and the seeding reaction. The result demonstrated that TDP-43 does not affect mature Aß fibrils and cannot block fibril growth once the fibril nucleus was added.",10.1038/s41467-020-19786-7,AG00833
TDP-43,Amyloid beta,QKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHN,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No information,"However, the other TDP-43 variants did not significantly affect Abeta42 fibrillization, Fig. 4Supplementary",NA,NA,"interactor: 0.23 μM, TDP-43_RRM1 + 2, residue 101-265  interactee: 25 μM Abeta (1–42)   We further found that the inhibition of Aß fibrillization by TDP-43 only occurs in the early and intermediate stages of Aß fibrillization, but not in the fibrillar stage and the seeding reaction. The result demonstrated that TDP-43 does not affect mature Aß fibrils and cannot block fibril growth once the fibril nucleus was added.",10.1038/s41467-020-19786-7,AG00834
TDP-43,Amyloid beta,MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No information,"However, the other TDP-43 variants did not significantly affect Abeta42 fibrillization, Fig. 4Supplementary",NA,NA,"interactor: 0.23 μM, TDP-43_N-term, residue 1–100 interactee: 25 μM Abeta (1–42)  We further found that the inhibition of Aß fibrillization by TDP-43 only occurs in the early and intermediate stages of Aß fibrillization, but not in the fibrillar stage and the seeding reaction. The result demonstrated that TDP-43 does not affect mature Aß fibrils and cannot block fibril growth once the fibril nucleus was added.",10.1038/s41467-020-19786-7,AG00835
TDP-43,Amyloid beta,MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHN,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No effect,No information,No information,"However, the other TDP-43 variants did not significantly affect Abeta42 fibrillization, Fig. 4Supplementary",NA,NA,"interactor: 0.23 μM, TDP-43_265, residue 1–265 interactee: 25 μM Abeta (1–42)   We further found that the inhibition of Aß fibrillization by TDP-43 only occurs in the early and intermediate stages of Aß fibrillization, but not in the fibrillar stage and the seeding reaction. The result demonstrated that TDP-43 does not affect mature Aß fibrils and cannot block fibril growth once the fibril nucleus was added.",10.1038/s41467-020-19786-7,AG00836
TDP-43,Amyloid beta,MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRTSQAHRVITKTKATCRGSQTRPSVLEITLIVALILVQQLVGDQHPMQGRAVVLMEALAQAWILSLLAGECRQWGCGWLV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,The ThT result showed that full-length TDP-43 still significantly inhibited Abeta42 fibrillization by retarding the lag time from 20 h to 40 h,The ThT result showed that full-length TDP-43 still significantly inhibited Abeta42 fibrillization by retarding the lag time from 20 h to 40 h,NA,"interactor: 0.23 μM, TDP-43 FL interactee: 25 μM Abeta (1–42)  We further found that the inhibition of Aß fibrillization by TDP-43 only occurs in the early and intermediate stages of Aß fibrillization, but not in the fibrillar stage and the seeding reaction. The result demonstrated that TDP-43 does not affect mature Aß fibrils and cannot block fibril growth once the fibril nucleus was added.",10.1038/s41467-020-19786-7,AG00837
TDP-43,Amyloid beta,MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHN,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"Surprisingly, TDP-43_265 and TDP-43_N-term exhibited strong inhibition on Abeta fibrillization; TDP-43_265 prolonged the lag time from 50 h to125 h, and reduced the ThT signal to ~9%.","Surprisingly, TDP-43_265 and TDP-43_N-term exhibited strong inhibition on Abeta fibrillization; TDP-43_265 prolonged the lag time from 50 h to125 h, and reduced the ThT signal to ~9%.",NA,"interactor: 0.25 μM, TDP-43_265, residue 1–265 interactee: 25 μM Abeta (1–40)   We further found that the inhibition of Aß fibrillization by TDP-43 only occurs in the early and intermediate stages of Aß fibrillization, but not in the fibrillar stage and the seeding reaction. The result demonstrated that TDP-43 does not affect mature Aß fibrils and cannot block fibril growth once the fibril nucleus was added.",10.1038/s41467-020-19786-7,AG00838
TDP-43,Amyloid beta,MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAV,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"Surprisingly, TDP-43_265 and TDP-43_N-term exhibited strong inhibition on Abeta fibrillization; TDP-43_N-term prolonged the lag time of Abeta from 50 h to ~90 h and reduced ThT intensity to 75% compared with that of the Abeta only control","Surprisingly, TDP-43_265 and TDP-43_N-term exhibited strong inhibition on Abeta fibrillization; TDP-43_N-term prolonged the lag time of Abeta from 50 h to ~90 h and reduced ThT intensity to 75% compared with that of the Abeta only control",NA,"interactor: 0.25 μM, TDP-43_N-term, residue 1–100  interactee: 25 μM Abeta (1–40)  We further found that the inhibition of Aß fibrillization by TDP-43 only occurs in the early and intermediate stages of Aß fibrillization, but not in the fibrillar stage and the seeding reaction. The result demonstrated that TDP-43 does not affect mature Aß fibrils and cannot block fibril growth once the fibril nucleus was added.",10.1038/s41467-020-19786-7,AG00839
TDP-43,Amyloid beta,QKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHN,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"TDP-43_RRM1 + 2 did not have much inhibitory effect on Abeta fibrillization, with the lag time of Abeta slightly prolonged from 50 h to 55 h, and the final ThT intensity slightly affected (decreased to ~90%).","TDP-43_RRM1 + 2 did not have much inhibitory effect on Abeta fibrillization, with the lag time of Abeta slightly prolonged from 50 h to 55 h, and the final ThT intensity slightly affected (decreased to ~90%).",NA,"interactor: 0.25 μM, TDP-43_RRM1 + 2, residue 101-265   interactee: 25 μM Abeta (1–40)   We further found that the inhibition of Aß fibrillization by TDP-43 only occurs in the early and intermediate stages of Aß fibrillization, but not in the fibrillar stage and the seeding reaction. The result demonstrated that TDP-43 does not affect mature Aß fibrils and cannot block fibril growth once the fibril nucleus was added.",10.1038/s41467-020-19786-7,AG00840
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No,"the results of the ThT assay (Figure 3a) were confirmed by TEM which showed that while fibrils were major assemblies present in 7 days aged IAPP amorphous aggregates were the main species visible on the grids in the 7 days aged mixtures of IAPP with the mimics (Supporting Figure S2). It appears thus, that interaction of each of these two mimics, which in isolation exhibit similar CD spectra, with mainly unordered IAPP results in formation of ordered hetero-oligomers of similar overall structure. The mimics were found to bind IAPP monomers and low-molecular-weight oligomers with low nanomolar affinities and to form soluble, nonfibrillar, and ordered hetero-oligomers (see text and Figure S3 in the Supporting Information).",NA,with mainly unordered IAPP results in formation of ordered hetero-oligomers of similar overall structure.,"interactee: IAPP, interactor: IAPP-FA, analogue with methylation at F23 and A25",10.1002/anie.201302840,AG00841
IAPP,IAPP,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No information,Formation of fibrils by the interactee is inhibited,No,NA,"TEM which showed that while fibrils were major assemblies present in 7 days aged IAPP, amorphous aggregates were the main species visible on the grids in the 7 days aged mixtures of IAPP with the mimics (Supporting Figure S2).","TEM which showed that while fibrils were major assemblies present in 7 days aged IAPP, amorphous aggregates were the main species visible on the grids in the 7 days aged mixtures of IAPP with the mimics (Supporting Figure S2).","interactee: IAPP, interactor: IAPP-IL, analogue with methylation at I26 and L27",10.1002/anie.201302840,AG00842
IAPP,Amyloid beta,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,"By contrast, mainly round or amorphous aggregates were found in the 3 days aged mixtures of Abeta40 with IAPP-FA or IAPP-AL. At the 7 days incubation time point, round or amorphous aggregates and few fibrils were found in the mixtures.","Far-UV CD, TEM, and fluorescence spectroscopy suggested that the mimics bind Ab40 monomers and low-molecular-weight oligomers with nanomolar affinities and form soluble, nonfibrillar, and ordered hetero-oligomers","interactee: Amyloid beta, interactor: IAPP-FA, analogue with methylation at F23 and A25",10.1002/anie.201302840,AG00843
IAPP,Amyloid beta,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,No information,Formation of fibrils by the interactee is inhibited,No,NA,whereas round or amorphous aggregates (except for 3 days aged Abeta40-IAPP-IL mixture where no assemblies were found) were main species present in the mixtures (Supporting Figure S4),"Far-UV CD, TEM, and fluorescence spectroscopy suggested that the mimics bind Ab40 monomers and low-molecular-weight oligomers with nanomolar affinities and form soluble, nonfibrillar, and ordered hetero-oligomers","interactee: Amyloid beta, interactor: IAPP-IL, analogue with methylation at I26 and L27",10.1002/anie.201302840,AG00844
PrP,S100A9,KKRPKP,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIE HIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,Faster aggregation,Yes; implied by kinetics.,No information,S100A9 fibrillated much faster in the presence of both NCAM1-PrP (Figure 1A) and NCAM1-Abeta (Figure 1B) compared to S100A9 alone,NA,NA,"interactee: S100A9, interactor: NCAM1-PrP (aa 23-28)",10.1021/acschembio.9b00394,AG00845
PrP,S100A9,KKRPKP,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIE HIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"Importantly, the addition of NCAM1-PrP fibrils to S100A9 did not enhance its amyloid kinetics, i.e., did not cause an amyloid seeding effect the small decrease of ThT signal in the mixture of S100A9 with NCAM1-PrP fibrils may be related to the dispersive effect of the latter (Figure 3F).",NA,NA,"interactee: S100A9, interactor: NCAM1-PrP (aa 23-28) preformed fibrils",10.1021/acschembio.9b00394,AG00846
Amyloid beta,S100A9,KKLVFF,MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIE HIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP,No effect,No information,No information,The incubation of S100A9 with up to 100 µM of either the NCAM1 or KKLVFF peptide did not cause significant changes in its amyloid kinetics monitored by ThT assay; Some decrease of ThT signal in these mixtures may reflect a dispersing effect in increasingly heterogeneous solutions.,NA,NA,"interactee: S100A9, interactor: fragment of Abeta (aa 16-20)",10.1021/acschembio.9b00394,AG00847
Alpha-crystallin,Amyloid beta,DFVIFLDVKHFSPEDLTVK,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"Mixtures containing Abeta1–40 showed a significant increase in fluorescence, whereas those with mini-alphaA or alphaA-crystallin showed no increase in fluorescence (Fig. 3), suggesting the inhibition of fibril formation by the chaperones.","The addition of mini-alphaA-crystallin to the incubation mixture suppressed fibril formation of Abeta peptides. At 1:0.5 (w/w) ratio of Abeta and mini-alphaA-crystallin incubation, there was a significant decrease in fibril formation when compared to control (Figs.2B and 2E). At 1:1 (w/w) concentration, there was almost complete inhibition of the characteristic Aß fibrils (Figs. 2C and 2F). However, the electron micrographs with these concentrations showed some amorphous aggregates similar to mini-alphaA-crystallin aggregates formed after 3-day incu bation (Fig. 2G).",NA,"interactee: Abeta(1-40) interactor: mini-alphaA-crystallin with D, not K as a first residue in order to increase the solubility of the peptide",10.1023/B:MCBI.0000049373.15558.b8,AG00848
Alpha-crystallin,Amyloid beta,DFVIFLDVKHFSPEDLTVK,EDVGSNKGAIIGLM,No information,Formation of fibrils by the interactee is inhibited,No,"Although TEM revealed that mixtures with Abeta22–35 showed fibrils, these preparations did not show an increase in ThT fluorescence. Weak binding of ThT to Abeta22–35 fibrils has also been reported by Levine [39].","The addition of mini-alphaA-crystallin to the incubation mixture suppressed fibril formation of Abeta peptides. At 1:0.5 (w/w) ratio of Abeta and mini-alphaA-crystallin incubation, there was a significant decrease in fibril formation when compared to control (Figs.2B and 2E). At 1:1 (w/w) concentration, there was almost complete inhibition of the characteristic Aß fibrils (Figs. 2C and 2F). However, the electron micrographs with these concentrations showed some amorphous aggregates similar to mini-alphaA-crystallin aggregates formed after 3-day incu bation (Fig. 2G).",NA,"interactee: Abeta(22-35) interactor: mini-alphaA-crystallin, with D, not K as a first residue in order to increase the solubility of the peptide",10.1023/B:MCBI.0000049373.15558.b8,AG00849
Alpha-crystallin,Amyloid beta,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"Mixtures containing Abeta1–40 showed a significant increase in fluorescence, whereas those with mini-alphaA or alphaA-crystallin showed no increase in fluorescence (Fig. 3), suggesting the inhibition of fibril formation by the chaperones.","We have observed that the whole protein alphaA-crystallin can also inhibit Abeta aggregation, similar to the effects of mini-alphaA-crystallin (photomicrograph not shown).",NA,"interactee: Abeta(1-40) interactor: bovine alphaA-crystallin; The alphaA-crystallin subunit was separated from alphaB-crystallin in HPLC by passing the purified alpha-crystallin fraction through a C18 column over a linear gradient of water and acetonitrile containing 0.1% TFA. The alphaA-crystallin fraction was dried on a speedvac, resuspended in phosphate buffer saline containing 6 M urea and refolded by dialyzing out the urea extensively against phosphate buffer saline.",10.1023/B:MCBI.0000049373.15558.b8,AG00850
Alpha-crystallin,Amyloid beta,SEQUENCEUNAVAILABLE(PROTEINCOMPLEX),EDVGSNKGAIIGLM,No information,Formation of fibrils by the interactee is inhibited,No,"Although TEM revealed that mixtures with Abeta22–35 showed fibrils, these preparations did not show an increase in ThT fluorescence. Weak binding of ThT to Abeta22–35 fibrils has also been reported by Levine [39].","We have observed that the whole protein alphaA-crystallin can also inhibit Abeta aggregation, similar to the effects of mini-alphaA-crystallin (photomicrograph not shown).",NA,"interactee: Abeta(22-35) interactor: bovine alphaA-crystallin; The alphaA-crystallin subunit was separated from alphaB-crystallin in HPLC by passing the purified alpha-crystallin fraction through a C18 column over a linear gradient of water and acetonitrile containing 0.1% TFA. The alphaA-crystallin fraction was dried on a speedvac, resuspended in phosphate buffer saline containing 6 M urea and refolded by dialyzing out the urea extensively against phosphate buffer saline.",10.1023/B:MCBI.0000049373.15558.b8,AG00851
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKREEFPTDLKPEEVAQEAAEEPLIEPLMEPEGESYEDPPQEEYQEYEPEA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,AAA + AAB https://docs.google.com/spreadsheets/d/1iw01b0ETsFroHftdIJS8YyNIEm8AeobE6WhiJRe8VcY/edit?usp=sharing,10.1016/j.jmb.2018.05.024,AG00852
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSMAKEGVVAAAEKTKQGVTEAAEKTKEGVLYVGSKTREGVVQGVASVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No effect,No information,Yes,NA,NA,NA,AAA + BAA https://docs.google.com/spreadsheets/d/1iw01b0ETsFroHftdIJS8YyNIEm8AeobE6WhiJRe8VcY/edit?usp=sharing,10.1016/j.jmb.2018.05.024,AG00853
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSMAKEGVVAAAEKTKQGVTEAAEKTKEGVLYVGSKTREGVVQGVASVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKREEFPTDLKPEEVAQEAAEEPLIEPLMEPEGESYEDPPQEEYQEYEPEA,No effect,No information,No information,NA,NA,NA,AAA + BAB https://docs.google.com/spreadsheets/d/1iw01b0ETsFroHftdIJS8YyNIEm8AeobE6WhiJRe8VcY/edit?usp=sharing,10.1016/j.jmb.2018.05.024,AG00854
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSMAKEGVVAAAEKTKQGVTEAAEKTKEGVLYVGSKTREGVVQGVASVAEKTKEQASHLGGAVFSGAGNIAAATGLVKREEFPTDLKPEEVAQEAAEEPLIEPLMEPEGESYEDPPQEEYQEYEPEA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,"interactee: BBB, interactor: AAA https://docs.google.com/spreadsheets/d/1iw01b0ETsFroHftdIJS8YyNIEm8AeobE6WhiJRe8VcY/edit?usp=sharing",10.1016/j.jmb.2018.05.024,AG00855
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSMAKEGVVAAAEKTKQGVTEAAEKTKEGVLYVGSKTREGVVQGVASVAEKTKEQASHLGGAVFSGAGNIAAATGLVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,"interactee: BBA, interactor: AAA https://docs.google.com/spreadsheets/d/1iw01b0ETsFroHftdIJS8YyNIEm8AeobE6WhiJRe8VcY/edit?usp=sharing",10.1016/j.jmb.2018.05.024,AG00856
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQASHLGGAVFSGAGNIAAATGLVKREEFPTDLKPEEVAQEAAEEPLIEPLMEPEGESYEDPPQEEYQEYEPEA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,"interactee: ABB, interactor: AAA https://docs.google.com/spreadsheets/d/1iw01b0ETsFroHftdIJS8YyNIEm8AeobE6WhiJRe8VcY/edit?usp=sharing",10.1016/j.jmb.2018.05.024,AG00857
Alpha-synuclein,Alpha-synuclein,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQASHLGGAVFSGAGNIAAATGLVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,"interactee: ABA, interactor: AAA https://docs.google.com/spreadsheets/d/1iw01b0ETsFroHftdIJS8YyNIEm8AeobE6WhiJRe8VcY/edit?usp=sharing",10.1016/j.jmb.2018.05.024,AG00858
Alpha-synuclein,Tau,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKEAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,Faster aggregation,Yes; implied by kinetics.,No information,NA,"B, ThT kinetics of and Tau23 (100 μm, right panel) amyloid aggregation facilitated by the alpha-syn monomer at the indicated molar ratios at 37 °C.",NA,interactee: Tau23; https://docs.google.com/spreadsheets/d/1a2i4Ao4ZUayJrKWmuc9SBQW15NZGoWNFDoQsCJKx-Sw/edit?usp=sharing,10.1074/jbc.RA119.012284,AG00859
Alpha-synuclein,Tau,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,Faster aggregation,"Yes, direct evidence.",Yes,NA,"We directly visualized the nanogold particles in -syn–induced Tau fibrils under NS-EM (Fig. 1E and Fig. S3), confirming that K19 fibrils induced by -syn contained the -syn protein.",NA,Interactee: the three microtubule-binding fragments of Tau-K19 https://docs.google.com/spreadsheets/d/1a2i4Ao4ZUayJrKWmuc9SBQW15NZGoWNFDoQsCJKx-Sw/edit?usp=sharing,10.1074/jbc.RA119.012284,AG00860
Tau,Alpha-synuclein,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKEAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No information,NA,"A, ThT kinetics of alpha-syn (100 μm) aggregation facilitated by Tau23 (right panel) at the indicated molar ratios at 37 °C.",NA,"Compared with the monomeric form, preformed fibrils of Tau23 exhibited enhanced activity in promoting alpha-syn fibrillation at the same concentration but both forms accelerate alpha-syn fibrillation https://docs.google.com/spreadsheets/d/1a2i4Ao4ZUayJrKWmuc9SBQW15NZGoWNFDoQsCJKx-Sw/edit?usp=sharing",10.1074/jbc.RA119.012284,AG00861
Tau,Alpha-synuclein,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,"Yes, direct evidence.",Yes,NA,NA,NA,"Interactor: the three microtubule-binding fragment of Tau-K19  Compared with the monomeric form, preformed fibrils of K19 exhibited enhanced activity in promoting alpha-syn fibrillation at the same concentration but both forms accelerate alpha-syn fibrillation https://docs.google.com/spreadsheets/d/1a2i4Ao4ZUayJrKWmuc9SBQW15NZGoWNFDoQsCJKx-Sw/edit?usp=sharing",10.1074/jbc.RA119.012284,AG00862
Alpha-synuclein,Tau,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPDEEGYQDYEPEA,MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKEAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL,Faster aggregation,Yes; implied by kinetics.,No information,NA,phosphorylation mimic (S129D) of alpha-syn significantly enhances co-aggregation of Tau and alpha-syn. We performed a ThT kinetics assay of the fibrillation of Tau23 (12.5 μm) in the presence of alpha-syn (6.25 μm) and alpha-syn S129D (6.25 μm) at 37 °C in fibrillation buffer,NA,"Interactor: S129D, mimicking Ser129-phosphorylated alpha-syn   Tau23 https://docs.google.com/spreadsheets/d/1a2i4Ao4ZUayJrKWmuc9SBQW15NZGoWNFDoQsCJKx-Sw/edit?usp=sharing",10.1074/jbc.RA119.012284,AG00863
Alpha-synuclein,Tau,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPDEEGYQDYEPEA,QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE,Faster aggregation,Yes; implied by kinetics.,No information,NA,phosphorylation mimic (S129D) of alpha-syn significantly enhances co-aggregation of Tau and alpha-syn. We performed a ThT kinetics assay of the fibrillation of K19 (12.5 μm) in the presence of alpha-syn (6.25 μm) and alpha-syn S129D (6.25 μm) at 37 °C in fibrillation buffer,NA,"Interactor: S129D, mimicking Ser129-phosphorylated alpha-syn   Interactee: the three microtubule-binding fragment of Tau-K19 https://docs.google.com/spreadsheets/d/1a2i4Ao4ZUayJrKWmuc9SBQW15NZGoWNFDoQsCJKx-Sw/edit?usp=sharing",10.1074/jbc.RA119.012284,AG00864
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSD,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSD,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interactor: human PrP 23-144 fibrils Interactee: human PrP 23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00865
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDW,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDW,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interactor: mouse PrP 23-144 fibrils Interactee: mouse PrP 23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00866
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGND,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGND,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interactor: Syrian hamster PrP 23-144 fibrils Interactee: Syrian hamster PrP 23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00867
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSD,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDW,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interator: human PrP 23-144 fibrils Interactee: mouse PrP 23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00868
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDW,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSD,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interactor: mouse PrP 23-144 fibrils Interactee: human PrP 23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00869
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSD,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGND,No effect,No,No information,NA,NA,NA,Interactor: human PrP 23-144 fibrils Interactee: Syrian hamster 23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00870
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGND,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSD,No effect,No,Yes,NA,NA,NA,Interactor: Syrian hamster PrP23-144 fibrils Interactee: human PrP 23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00871
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGND,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDW,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interactor: Syrian hamster PrP23-144 fibrils Interactee: mouse PrP23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00872
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDW,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGND,No effect,No,No information,NA,NA,NA,Interactor: mouse PrP23-144 fibrils Interactee: Syrian hamster PrP23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00873
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGSD,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDW,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interactor: human PrP23-144 I138M mutant (fibrils) Interactee: mouse PrP23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00874
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGSD,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSD,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interactor: human PrP23-144 I138M mutant (fibrils) Interactee: human PrP23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00875
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGSD,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGND,No effect,No,No information,NA,NA,NA,Interactor: human PrP23-144 I138M mutant (fibrils) Interactee: Syrian hamster PrP23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00876
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGSD,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGND,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interactor: human PrP23-144 I138M/I139M mutant (fibrils) Interactee: Syrian hamster PrP23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00877
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGSD,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDW,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interactor: human PrP23-144 I138M/I139M mutant (fibrils) Interactee: mouse PrP23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00878
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGSD,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSD,No effect,No,No information,NA,NA,NA,Interactor: human PrP23-144 I138M/I139M mutant (fibrils) Interactee: human PrP23-144 monomers https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00879
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGSD,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGSD,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interactor: human PrP23-144 I138M/I139M mutant (fibrils) Interactee: human PrP23-144 I138M mutant (fibrils) https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00880
PrP,PrP,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGSD,KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGSD,No effect,No,No information,NA,NA,NA,Interactor: human PrP23-144 I138M mutant (fibrils) Interactee: human PrP23-144 I138M/I139M mutant (fibrils) https://docs.google.com/spreadsheets/d/1sZnZqolAA3fKWDYoGa07zboS257L4e_eP5j6n_R1vqU/edit?usp=sharing,10.1016/S1097-2765(04)00155-8,AG00881
Amyloid beta,Alpha-synuclein,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,No information,"Yes, direct evidence.",No information,NA,"At longer periods of incubation, Abeta and alpha-syn alone, and the mixture formed fibrils of approximately 11 nm in diameter that increased in number in the samples containing a mixture of Abeta and alpha-syn (Figure 6F–I).",NA,NA,10.1371/journal.pone.0003135,AG00882
Insulin,IAPP,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1002/anie.200602034,AG00883
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,NA,10.1002/anie.200602034,AG00884
Insulin,IAPP,FVNQHLCGSHLVEALYLVCGERGFFYTPKT,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Human insulin B chain as interactor,10.1002/anie.200602034,AG00885
Insulin,IAPP,GIVEQCCTSICSLYQLENYCN,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Human insulin A chain as interactor,10.1002/anie.200602034,AG00886
Insulin,IAPP,SHLVEALYLV,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,Human insulin B chain (9-18) as interactor,10.1002/anie.200602034,AG00887
Insulin,IAPP,HLVEALYLVC,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,Human insulin B chain (10-19) as interactor,10.1002/anie.200602034,AG00888
Insulin,IAPP,LVEALYLVCG,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,Human insulin B chain (11-20) as interactor,10.1002/anie.200602034,AG00889
Amyloid beta,Insulin,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,interactor: Abeta (1–42) interactee: bovine insulin,10.1002/anie.201800197,AG00890
Amyloid beta,Insulin,DAEFRHDSGYEVHHQKLVPFAEDVGSNKGAIIGLMVGGVVIA,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,No effect,No information,No information,NA,NA,NA,interactor: Abeta (1–42) F19P mutant interactee: bovine insulin,10.1002/anie.201800197,AG00891
Amyloid beta,Insulin,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,"On the D-Phe surface, the Abeta/insulin mixture or Abeta alone formed long unbranched fibrils. However, the Abeta/ insulin mixture or Abeta alone formed amorphous aggregates on the L-Phe surface.","Interactions were examined on a D-phenylalanine- modified surface, as well as on L-phenylalanine-modified surface. The ThT fluorescence of cross-aggregates on the L-Phe surface was weaker than that on D-Phe surface. The results clearly indicated surface chirality can strongly influence the structure, morphology, and cellular responses of the cross-aggregates of Abeta and insulin. On a D-Phe surface, Abeta induced insulin to undergo fibrillation and lose its bioactivity. In contrast, on an L-Phe surface, insulin and Abeta formed non-toxic amorphous aggregates, while insulin retained its native bioactivity and mitigated the Abeta-induced toxicity. This work offers new insights that may help us to understand insulin resistance in AD.",10.1007/s12274-018-1995-y,AG00892
Insulin,Insulin,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,Yes,"ThT fluorescence intensity was gradually decreased in bovine insulin seeded with human insulin seeds, (Fig. 4 A, orange bars); meanwhile, it was gradually increased in human insulin seeded with bovine insulin seeds (Fig. 4 A, blue bars).",NA,"AFM observation successfully revealed the inheritance or change of fibril thickness (Fig. 5 B). The thicknesses of self-seeded human and bovine insulin were 12.1 5 2.0 and 6.9 5 1.2 nm, respectively (n ¼ 20), both of which were almost the same as those of the spontaneously formed human and bovine insulin fibrils. The thicknesses of the cross-seeded human and bovine insulin, on the other hand, were 15.1 5 1.9 and 6.9 5 1.3 nm, respectively (n ¼ 20). The value of the cross-seeded bovine insulin supports the deviation to bovine-like fibril structure, and the thickest value of the cross-seeded human insulin strongly supports the formation of a new type of fibrils.",Human insulin was seeded with bovine insulin seeds,10.1016/j.bpj.2020.12.005,AG00893
Insulin,Insulin,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"ThT fluorescence intensity was gradually decreased in bovine insulin seeded with human insulin seeds, (Fig. 4 A, orange bars); meanwhile, it was gradually increased in human insulin seeded with bovine insulin seeds (Fig. 4 A, blue bars).",NA,"AFM observation successfully revealed the inheritance or change of fibril thickness (Fig. 5 B). The thicknesses of self-seeded human and bovine insulin were 12.1 5 2.0 and 6.9 5 1.2 nm, respectively (n ¼ 20), both of which were almost the same as those of the spontaneously formed human and bovine insulin fibrils. The thicknesses of the cross-seeded human and bovine insulin, on the other hand, were 15.1 5 1.9 and 6.9 5 1.3 nm, respectively (n ¼ 20). The value of the cross-seeded bovine insulin supports the deviation to bovine-like fibril structure",Bovine insulin was seeded with human insulin seeds,10.1016/j.bpj.2020.12.005,AG00894
Sup35,Insulin,GNNQQNY,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,No effect,No information,No information,No remarkable difference in the turbidity changebetween the INS solutions with and without the GNNQQNY aggre-gates was observed (Fig. 4a). The CD spectra of the two INS solutionsat day 3 were nearly identical to that of a fresh INS solution(Fig. 4b). Similar trends in the turbidity and CD spectral changeswere observed for the HSA and LYS solutions,NA,NA,NA,10.1016/j.colsurfb.2016.10.011,AG00895
Sup35,Insulin,GNNQQNY,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,cross-seeding of the GNNQQNY aggregate appeared to potentially promote the amyloid fibril formation of the heterogeneous INS [INS – insulin],NA,10.1016/j.colsurfb.2016.10.011,AG00896
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,Addition of as little as 2 μM insulin to a 25 μM IAPP reaction increases the time for conversion eightfold (Figure 1a).,NA,NA,"0,5-5 μM insulin / 25 μM IAPP",10.1016/j.jmb.2003.10.045,AG00897
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,Figure 2,NA,NA,2 μM insulin / 10 μM IAPP,10.1016/j.jmb.2003.10.045,AG00898
Insulin,Insulin,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,"Interactor: preformed full lenght insulin, interactee: full length insulin",10.1016/j.jmb.2006.05.007,AG00899
Lysozyme,Insulin,MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGN,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,No effect,No information,No information,"This effect was shown to be sequence-specific, as the addition of 5% (w/w) lysozyme fibrils had no detectable effect on the fibrillization kinetics of insulin.","This effect was shown to be sequence-specific, as the addition of 5% (w/w) lysozyme fibrils had no detectable effect on the fibrillization kinetics of insulin.",NA,"Interactor: preformed lysozyme, interactee: full length insulin",10.1016/j.jmb.2006.05.007,AG00900
Transthyretin,Insulin,YTIAALLSPYS,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,No effect,No information,No information,"The incubation of TTR105-115 with insulin had no observable effect on the aggregation of insulin, with the kinetic trace virtually overlying that of the control (Figure 8)","The incubation of TTR105-115 with insulin had no observable effect on the aggregation of insulin, with the kinetic trace virtually overlying that of the control (Figure 8)",NA,"Interactor: human 105-115TTR, interactee: full length insulin",10.1016/j.jmb.2006.05.007,AG00901
Insulin,Amyloid beta,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,Slower aggregation,"Yes, direct evidence.",Yes,"The lag time of Abeta42 fibril formation increased with insulin concentration from 4 hours in the absence of insulin to above 24 hours in the presence of 120 µM insulin (Fig. 4b, blue curve). Concomitantly, the equilibrium ThT fluorescence intensity of 40 µM Abeta42 decreased with insulin concentration and approached zero in the presence of 120 µM insulin (Fig. 4b, red curve","When Aß42 samples were co-incubated with 40 µM insulin (Figure 5, second panel), quasi-spherical conformations dominated the morphology after incubation for 0 and 4 h. After incubation for 8 h, we noted an emergence of short protofibrils, which appeared to be thicker than the protofibril formed by Aß42 alone.; 40 µM Aß42 samples co-incubated with 100 µM insulin for 0, 4, and 8 h. Again, quasi-spherical conformations dominated the morphology after incubation for 0 and 4 h, whereas after incubation for 8 h, we observed short fibril adjacent to quasi-spherical conformations",NA,"Human insulin 10, 20, 40, 80, 100 μM / Abeta (1–42) 40 μM; Quiescent Incubation; insulin significantly affected the lag time of Abeta42 fibril formation at both low and high but not as much at intermediate insulin concentrations. (0, 10, 20, 40, 80, 100, 120 μM); The AFM images are thus consistent with the ThT fluorescence data and support our conclusion that insulin inhibits Aß42 fibril formation in a concentration-dependent manner.",10.1021/acs.biochem.9b00696,AG00902
Insulin,Amyloid beta,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA,No aggregation,"Yes, direct evidence.",No,The results presented above provide evidence that insulin inhibited Aß42 fibril formation in a concentration-dependent way and that 120 µM insulin can fully inhibit fibril formation of 40 µM Aß42,"Our results show that insulin inhibited Aß42 fibril formation in a concentration-dependent way, such that fibril formation of 40 µM Aß42 was fully inhibited by 120 µM insulin for at least 24 h of co-incubation. (Figure 5) 40 µM Aß42 samples coincubated with 180 µM insulin for 0, 4, and 8 h. None of these images showed protofibrillar or fibrillar assemblies. Instead, we observed quasi-spherical and larger, irregularly shaped morphologies. (Figure 5)",NA,"Human insulin 120, 180 μM / Abeta (1–42) 40 μM; Quiescent Incubation;",10.1021/acs.biochem.9b00696,AG00903
Insulin,Amyloid beta,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Faster aggregation,Yes; implied by kinetics.,No information,"When we added monomeric insulin to 2 or 10 μM preformed Abeta fibrils, we observed a clear increase in final fluorescence intensity especially with the higher Abeta fibril concentration (Figure 2B).",NA,NA,NA,10.1021/acschemneuro.5b00325,AG00904
Amyloid beta,Insulin,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No information,"in the presence of Abeta, insulin forms ThT-active aggregates (or coaggregates) under conditions where it otherwise does not aggregate.; Abeta Fibrils Promote Insulin Aggregation",NA,NA,NA,10.1021/acschemneuro.5b00325,AG00905
Insulin,Amyloid beta,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"when monomeric Abeta was incubated together with preincubated insulin aggregates, however, the resulting ThT fluorescence levels were lower than for pure Abeta samples, suggesting that insulin aggregates prevent amyloid Abeta fibrillation (Figure 2C).",NA,NA,NA,10.1021/acschemneuro.5b00325,AG00906
Insulin,Insulin,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKTKR,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Faster aggregation,Yes; implied by kinetics.,No,"Time traces of fluorescence intensity exhibit no lag phases, while in the absence of seeds but under otherwise identical experimental conditions, ThT emission remains at the “zero” level for the first 5 and 10 h for KR and BI, respectively (data not shown). Figure 2B",NA,NA,interactor: 1% seeds LysB31-ArgB32 human insulin analog interactee: bovine insulin  40°C,10.1021/bi301144d,AG00907
Insulin,Insulin,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKTKR,Faster aggregation,Yes; implied by kinetics.,No,"Time traces of fluorescence intensity exhibit no lag phases, while in the absence of seeds but under otherwise identical experimental conditions, ThT emission remains at the “zero” level for the first 5 and 10 h for KR and BI, respectively (data not shown). The quasi-sigmoidal shape of time traces in Figure 2D suggests a pronounced acceleration of fibrillation that is typically associated with secondary nucleation events but could also be caused by the greater brittleness of [KR]BI fibrils",NA,NA,interactor: 1% seeds bovine insulin interactee: LysB31-ArgB32 human insulin analog 40°C,10.1021/bi301144d,AG00908
Insulin,Insulin,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Faster aggregation,Yes; implied by kinetics.,No,"Time traces of fluorescence intensity exhibit no lag phases, while in the absence of seeds but under otherwise identical experimental conditions, ThT emission remains at the “zero” level for the first 5 and 10 h for KR and BI, respectively (data not shown). Figure 2A",NA,NA,interactor: 1% seeds bovine insulin interactee: bovine insulin  40°C,10.1021/bi301144d,AG00909
Insulin,Insulin,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKTKR,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKTKR,Faster aggregation,Yes; implied by kinetics.,No,"Time traces of fluorescence intensity exhibit no lag phases, while in the absence of seeds but under otherwise identical experimental conditions, ThT emission remains at the “zero” level for the first 5 and 10 h for KR and BI, respectively (data not shown). Figure 2C",NA,NA,interactor: 1% seeds LysB31-ArgB32 human insulin analog interactee: LysB31-ArgB32 human insulin analog 40°C,10.1021/bi301144d,AG00910
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"The results, shown in Figure 2, confirm that insulin is an effective inhibitor of the formation of amyloid by IAPP.",NA,NA,NA,10.1021/bi4015488,AG00911
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,TPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,"An increase in T50 was observed for all proIAPP1–48:insulin ratios tested, and the inhibitory effect of insulin was dose-dependent.",NA,NA,NA,10.1021/bi4015488,AG00912
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No,No information,"Insulin was a much less effective inhibitor when HS was present, although there were modest effects on the time required to complete amyloid formation, and the effects of insulin were dose-dependent. However, even at a 1:5 IAPP:insulin ratio, IAPP formed amyloid without an apparent lag phase in the presence of HS (Figure 4A).",NA,NA,Effects of insulin on the formation of amyloid by IAPP in the presence of Heperan Sulfate - Insulin Is a Significantly Less Effective Inhibitor in the Presence of Heparan Sulfate,10.1021/bi4015488,AG00913
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,TPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No,No information,Insulin barely showed any inhibitory effect at 20:1 and 5:1 proIAPP1–48:insulin ratios in the presence of HS.,NA,NA,"Effects of insulin on the formation of amyloid by proIAPP1–48 in the presence of Heperan Sulfate.; Concentrations (interactee to interactor): 20:1, 5:1",10.1021/bi4015488,AG00914
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,TPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,"Effects of insulin on the formation of amyloid by proIAPP1–48 in the presence of Heperan Sulfate.; Concentrations (interactee to interactor): 1:1, 1:5",10.1021/bi4015488,AG00915
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,NA,10.1021/bi4015488,AG00916
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No,No information,"In addition, insulin was a much less effective inhibitor of the formation of amyloid by IAPP in the presence of HS (Figure 6B).",NA,NA,Inhibition by insulin of the formation of amyloid by IAPP in the presence of Heperan Sulfate in buffer without HFIP,10.1021/bi4015488,AG00917
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,TPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,Inhibition by insulin of the formation of amyloid by proIAPP1–48 in the absence of Heperan Sulfate in buffer without HFIP.,10.1021/bi4015488,AG00918
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,TPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No effect,No,No information,The time required to complete the formation of amyloid by proIAPP1–48 in the presence of insulin is nearly the same as that without insulin (Figure 7B).,NA,NA,Inhibition by insulin of the formation of amyloid by proIAPP1–48 in the presence of Heperan Sulfate in buffer without HFIP.,10.1021/bi4015488,AG00919
Albumin,Insulin,DTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPENLPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAKEYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEYGFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTEDYLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKAFDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENFVAFVDKCCAADDKEACFAVEGPKLVVSTQTALA,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1021/bi501333q,AG00920
Insulin,Albumin,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,DTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPENLPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAKEYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEYGFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTEDYLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKAFDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENFVAFVDKCCAADDKEACFAVEGPKLVVSTQTALA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1021/bi501333q,AG00921
Lysozyme,Insulin,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1021/bi501333q,AG00922
Insulin,Lysozyme,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,Yes; implied by kinetics.,Yes,NA,NA,NA,NA,10.1021/bi501333q,AG00923
Insulin,Insulin,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,NA,10.1021/bi501333q,AG00924
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No information,"Yes, direct evidence.",Yes,NA,NA,NA,"That is probably human insulin but they did not write it in the article. It is about hIAPP in type II diabetes, so we suspected it is about human insulin.",10.1039/C1CC14285B,AG00925
Insulin,Insulin,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,NA,"(B) Effect of seeding on insulin fibrillation. The seeds of different origins were added at 5% (W/W). The experiments were conducted under acidic conditions (20% acetic acid, pH 2.0) containing 50 mM NaCl at 60 °C. The plots are an average of three independent experiments.",NA,"Interactor: insulin fibrils, Interactee: insulin monomers",10.1039/D0RA05414C,AG00926
Alpha-crystallin,Insulin,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,NA,"(B) Effect of seeding on insulin fibrillation. The seeds of different origins were added at 5% (W/W). The experiments were conducted under acidic conditions (20% acetic acid, pH 2.0) containing 50 mM NaCl at 60 °C.",NA,Interactor: alpha-crystallin B chain,10.1039/D0RA05414C,AG00927
Insulin,Insulin,GIVEQCCTSICSLYQLENYCN,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,NA,"(B) Effect of seeding on insulin fibrillation. The seeds of different origins were added at 5% (W/W). The experiments were conducted under acidic conditions (20% acetic acid, pH 2.0) containing 50 mM NaCl at 60 °C.",NA,Interactor: Insulin A chain,10.1039/D0RA05414C,AG00928
Insulin,Insulin,FVNQHLCGSHLVEALYLVCGERGFFYTPKT,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,NA,"(B) Effect of seeding on insulin fibrillation. The seeds of different origins were added at 5% (W/W). The experiments were conducted under acidic conditions (20% acetic acid, pH 2.0) containing 50 mM NaCl at 60 °C.",NA,Interactor: Insulin B chain,10.1039/D0RA05414C,AG00929
Alpha-crystallin,Insulin,MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFCGPKIQTGLDATHAERAIPVSREEKPTSAPSS,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Slower aggregation,Formation of fibrils by the interactee is inhibited,Yes,NA,"(B) Effect of seeding on insulin fibrillation. The seeds of different origins were added at 5% (W/W). The experiments were conducted under acidic conditions (20% acetic acid, pH 2.0) containing 50 mM NaCl at 60 °C.",NA,Interactor: alpha-crystallin A chain,10.1039/D0RA05414C,AG00930
Alpha-crystallin,Insulin,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEM,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Slower aggregation,Formation of fibrils by the interactee is inhibited,Yes,NA,"The impact of urea and seeding on the kinetics of insulin fibrillation. (B) Effect of seeding on insulin fibrillation. The seeds of different origins were added at 5% (W/W). The experiments were conducted under acidic conditions (20% acetic acid, pH 2.0) containing 50 mM NaCl at 60 °C. The plots are an average of three independent experiments.",NA,interactor: N-terminal domain of alphaB-Cry (alphaB-NTD),10.1039/D0RA05414C,AG00931
Alpha-crystallin,Insulin,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interaction examined in the presence of urea (2.5M and 7M) which was added to the mixture of the interactee + interactor Interactor: alpha-crystallin B chain,10.1039/D0RA05414C,AG00932
Insulin,Insulin,GIVEQCCTSICSLYQLENYCN,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interaction examined in the presence of urea (2.5M and 7M) which was added to the mixture of the interactee + interactor Interactor: Insulin A chain,10.1039/D0RA05414C,AG00933
Insulin,Insulin,FVNQHLCGSHLVEALYLVCGERGFFYTPKT,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interaction examined in the presence of urea (2.5M and 7M) which was added to the mixture of the interactee + interactor Interactor: Insulin B chain,10.1039/D0RA05414C,AG00934
Alpha-crystallin,Insulin,MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSG,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interaction examined in the presence of urea (2.5M and 7M) which was added to the mixture of the interactee + interactor Interactor: alpha crystallin A chain,10.1039/D0RA05414C,AG00935
Alpha-crystallin,Insulin,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFSTATSLSPFYLRPPSFLRAPSWIDTGLSEM,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,No effect,No,No information,NA,NA,NA,Interaction examined in the presence of urea (2.5M and 7M) which was added to the mixture of the interactee + interactor Interactor: alpha-Crystallin B chain N domain,10.1039/D0RA05414C,AG00936
Insulin,Insulin,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interaction examined in the presence of urea (2.5M and 7M) which was added to the mixture of the interactee + interactor  Interactee + interactor: insulin,10.1039/D0RA05414C,AG00937
Alpha-crystallin,Insulin,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interaction examined in the presence of urea 2.5M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. Interactor: alpha-crystallin B chain,10.1039/D0RA05414C,AG00938
Alpha-crystallin,Insulin,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interaction examined in the presence of urea 7.0M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. Interactor: alpha-crystallin B chain,10.1039/D0RA05414C,AG00939
Insulin,Insulin,GIVEQCCTSICSLYQLENYCN,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interaction examined in the presence of urea 2.5M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. Interactor: insulin A chain,10.1039/D0RA05414C,AG00940
Insulin,Insulin,GIVEQCCTSICSLYQLENYCN,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interaction examined in the presence of urea 7.0M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. Interactor: insulin A chain,10.1039/D0RA05414C,AG00941
Insulin,Insulin,FVNQHLCGSHLVEALYLVCGERGFFYTPKT,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,Interaction examined in the presence of urea 2.5M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. Interactor: insulin B chain,10.1039/D0RA05414C,AG00942
Insulin,Insulin,FVNQHLCGSHLVEALYLVCGERGFFYTPKT,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,Interaction examined in the presence of urea 7.0M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. Interactor: insulin B chain,10.1039/D0RA05414C,AG00943
Alpha-crystallin,Insulin,MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFCGPKIQTGLDATHAERAIPVSREEKPTSAPSS,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interaction examined in the presence of urea 2.5 M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. Interactor: alpha-crystallin A chain,10.1039/D0RA05414C,AG00944
Alpha-crystallin,Insulin,MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFCGPKIQTGLDATHAERAIPVSREEKPTSAPSS,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Slower aggregation,Formation of fibrils by the interactee is inhibited,No information,NA,NA,NA,Interaction examined in the presence of urea 7.0M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. Interactor: alpha-crystallin A chain,10.1039/D0RA05414C,AG00945
Alpha-crystallin,Insulin,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEM,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No information,NA,NA,NA,Interaction examined in the presence of urea 2.5 M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. Interactor: alpha-crystallin B chain N domain,10.1039/D0RA05414C,AG00946
Alpha-crystallin,Insulin,MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEM,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,No effect,No,No information,NA,NA,NA,Interaction examined in the presence of urea 7.0M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. Interactor: alpha-crystallin B chain N domain,10.1039/D0RA05414C,AG00947
Insulin,Insulin,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interaction examined in the presence of urea 2.5 M added to the interactee (insulin). The interactor was added after the incubation of interactee (insulin) with urea.,10.1039/D0RA05414C,AG00948
Insulin,Insulin,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,Interaction examined in the presence of urea 7.0 M added to the interactee (insulin). The interactor was added after the incubation of interactee (insulin) with urea.,10.1039/D0RA05414C,AG00949
Insulin,IAPP,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY,No aggregation,Formation of fibrils by the interactee is inhibited,No,"In the solution that contained a mixture of hIAPP and insulin, no amyloid fibrils were observed, but there were large amorphous aggregates (Figure 7B). No precipitate was present in preparations of insulin alone. These data suggest that, although insulin is capable of preventing hIAPP from forming fibrils, this interaction results in precipitation of amorphous aggregates.",NA,NA,NA,10.1042/bj20030852,AG00950
Insulin,Sup35,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,Faster aggregation,Yes; implied by kinetics.,No information,"However, bovine pancreas insulin and human Ig light-chain amyloids, which lack Q
N-rich regions, did stimulate NM conversion (Fig. 3D), and the degree of stimulation decreased when less amyloid was added.",NA,NA,Interactor: bovine pancreas insulin fibers Interactee: Sup35 (NM prion domain),10.1073/pnas.0404968101,AG00951
Insulin,Sup35,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVND,No effect,No,No,The ability to stimulate NM conversion was specific to the amyloid form: 50% soluble insulin failed to stimulate NM conversion (Fig. 3D).,NA,NA,Interactor: soluble insulin Interactee: Sup35 (NM prion domain),10.1073/pnas.0404968101,AG00952
Insulin,Alpha-synuclein,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA,Faster aggregation,Yes; implied by kinetics.,No,"The lag time before fibril extension became shorter with increasing amounts of preformed seeds (1, 5, 10% v/v) for all three proteins.",NA,NA,"bovine insulin seeds (1, 5, 10% v/v) / halphaSyn; seed = sonicated preformed fibrils",10.1074/jbc.M508623200,AG00953
Insulin,Lysozyme,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL,Faster aggregation,"Yes, direct evidence.",No information,NA,NA,NA,bovine insulin,10.1110/ps.04707004,AG00954
Lysozyme,Insulin,MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGN,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No information,"In order to account for the possibility that the formation of HCF iwas caused by a crowding effect, rather than LF themselves, insulin aggregation was carried out in the presence of 200 µM lysozyme monomers (Supplementary Material Figure S7). The presence of lysozyme monomers reduced the t50 value, similarly as 2 µM LF, however, they did not cause such an increase in ThT fluorescence intensity or changes to insulin fibril secondary structure (Supplementary Material Figure S7) as was the case with 200 µM LF. As lysozyme fibrils appeared to have an effect on nucleation, as well as the aggregation curve slope value (possible faster rate of elongation), seeded aggregation experiments were carried out in the absence or presence of 2 µM or 200 µM LF (Figure 4, Supplementary Material Figure S8). When seeded aggregation occurred in the AC solution without any lysozyme fibrils, we observed typical seed-concentration-dependent kinetics (Figure 4A). The same was true when there was 2 µM of LF added to the solution (Figure 4B). In both cases, the overall ThT fluorescence intensity remained relatively low, however, there was a slightly higher end-point intensity when there was a large concentration of insulin seed added (Figure 4A,B,F). The average t50 values of samples without LF were higher throughout the entire seed concentration range when compared to the 2 µM LF samples, and both followed a linear trend, which converged at higher seed concentrations (Figure 4E). The slope values were also slightly higher in the case of 2 µM LF, which was observed in the spontaneous aggregation experiment as well (Figure 1E).",NA,"Seeing as the presence of LF had such a significant effect on insulin fibril formation, and the ThT fluorescence intensity hints at the formation of a different aggregate conformation, atomic force microscopy (AFM) images were acquired to examine if there were any changes to fibril morphology. When there was a small concentration of LF added to the sample, there were no significant changes observed (Figure 2A,C), and average fibril height and width remained even (5 nm and 27 nm, respectively). When 200 µM of LF was present, it became extremely difficult to differentiate between insulin and lysozyme fibrils, as thereInt. J. Mol. Sci. 2021, 22, 1775 4 of 11 was a high propensity towards cluster formation (Figure 2B,D). One aspect worth noting was that when insulin was aggregated with 200 µM LF, the clusters were significantly more massive than in the control LF samples (Figure 2B,D). Due to such cluster formation, it was impossible to draw any conclusions about the effect LF had on insulin fibril morphology (single fibril width, height, and length could not be accurately measured), which requires an alternative method to determine whether there were any LF-induced structural changes",NA,10.3390/ijms22041775,AG00955
Insulin,Insulin,GIVEQCCASVCSLYQLENYCN,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Faster aggregation,Yes; implied by kinetics.,No,"Addition of 5% (w/w) A-chain or B-chain fibrils did not abolish the lag phase completely, although the lag time was reduced significantly in each case.",NA,NA,"interactor: chain A bovine insulin fibrils, interactee: full lenght bovine insulin",10.1016/j.jmb.2006.05.007,AG00956
Insulin,Insulin,FVNQHLCGSHLVEALYLVCGERGFFYTPKA,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Faster aggregation,Yes; implied by kinetics.,No,"Addition of 5% (w/w) A-chain or B-chain fibrils did not abolish the lag phase completely, although the lag time was reduced significantly in each case.",NA,NA,"interactor: chain B bovine insulin fibrils, interactee: full lenght bovine insulin",10.1016/j.jmb.2006.05.007,AG00957
Insulin,Insulin,GIVEQCCASVCSLYQLENYCN,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"At a molar ratio of 0.1, the soluble A-chain increased the lag time for insulin fibrillization from 500 min to 950 min, whilst ratios of 0.2 and 0.3 resulted in inhibition such that the lag times could not be resolved within the 2000 min duration of the measurements (Figure 6 (a))",NA,NA,"interactor: soluble chain A bovine insulin (molar ratio of 0.1, 0.2, 0.3), interactee: full lenght bovine insulin",10.1016/j.jmb.2006.05.007,AG00958
Insulin,Insulin,FVNQHLCGSHLVEALYLVCGERGFFYTPKA,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,"Here, increasing ratios of soluble B-chain extended the lag time for insulin aggregation and resulted in lower levels of solution turbidity, indicating that the final quantities of aggregated material formed in these reactions was reduced relative to the control in the absence of B-chain (Figure 6 (b))",NA,NA,"interactor: soluble chain B bovine insulin, interactee: full lenght bovine insulin",10.1016/j.jmb.2006.05.007,AG00959
Insulin,Insulin,GIVEQCCASVCSLYQLENYCN,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,No aggregation,Formation of fibrils by the interactee is inhibited,No,"At a molar ratio of 0.4, the lag phase was of a length similar to that of the control containing no A-chain peptide, although the rate of growth was much slower and the extent of solution turbidity was greater. ; At the highest molar ratio examined (0.5) the lag phase was reduced to less than 250 min and again the rate of growth was slower relative to the control. ; These samples were examined by TEM and were found to contain almost no fibrillar material; instead, they contained large amorphous aggregates (Figure 7 (c) and (d))",NA,NA,"interactor: soluble chain A bovine insulin (molar ratio of 0.4, 0.5), interactee: full lenght bovine insulin",10.1016/j.jmb.2006.05.007,AG00960
Insulin,Insulin,GIVEQCCASVCSLYQLENYCN,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Faster aggregation,Yes; implied by kinetics.,No,"In the absence of exogenous peptide, the rate of aggregation was 0.15(±0.004) min−1, whilst in the presence of A and B-chain, the rates of aggregation were 0.11(±0.002) min−1 and 0.12(±0.003) min−1, respectively. ; the final absorbance of the sample containing the Achain peptide was almost twice as high as that for the control",NA,NA,"interactor: soluble chain A bovine insulin (molar ratio 0.2), interactee: full lenght bovine insulin self-seeded by insulin fibrils 5% (w/w)",10.1016/j.jmb.2006.05.007,AG00961
Insulin,Insulin,FVNQHLCGSHLVEALYLVCGERGFFYTPKA,>chainA GIVEQCCASVCSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKA,Faster aggregation,Yes; implied by kinetics.,No,"In the absence of exogenous peptide, the rate of aggregation was 0.15(±0.004) min−1, whilst in the presence of A and B-chain, the rates of aggregation were 0.11(±0.002) min−1 and 0.12(±0.003) min−1, respectively.",NA,NA,"interactor: soluble chain B bovine insulin (molar ratio 0.2), interactee: full lenght bovine insulin self-seeded by insulin fibrils 5% (w/w)",10.1016/j.jmb.2006.05.007,AG00962
Insulin,Insulin,MDHHHHHHWIHRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEIRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDVLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKKHMGIVEQCCTSICSLYQLENYCN,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,NA,NA,NA,"interactor: A-chain fused to human alphaB-Cry (alphaB-AC), interactee: monomeric insulin",10.1039/D0RA05414C,AG00963
Insulin,Insulin,MDIAIHHPWIHRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEIRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDVLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKKHMFVNQHLCGSHLVEALYLVCGERGFFYTPKT,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Slower aggregation,Formation of fibrils by the interactee is inhibited,No,NA,NA,NA,"interactor: B-chain fused to human alphaB-Cry (alphaB-BC), interactee: monomeric insulin",10.1039/D0RA05414C,AG00964
Insulin,Insulin,MDHHHHHHWIHRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEIRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDVLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKKHMGIVEQCCTSICSLYQLENYCN,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,"When compared to fibrillation of insulin by itself at 2.0 M urea concentration (lag time 110 min, Fig. 6A), in the co-presence of 2.5 M urea and seeds from different proteins, a significant enhancement (but to different degrees) in fibrillation kinetics was observed in all cases except foraB-NTDseeds (Fig. 9A)",NA,NA,"Interaction examined in the presence of urea (2.5M and 7M) which was added to the mixture of the interactee + interactor ; interactor: A-chain fused to human alphaB-Cry (alphaB-AC), interactee: monomeric insulin",10.1039/D0RA05414C,AG00965
Insulin,Insulin,MDIAIHHPWIHRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEIRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDVLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKKHMFVNQHLCGSHLVEALYLVCGERGFFYTPKT,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,"When compared to fibrillation of insulin by itself at 2.0 M urea concentration (lag time 110 min, Fig. 6A), in the co-presence of 2.5 M urea and seeds from different proteins, a significant enhancement (but to different degrees) in fibrillation kinetics was observed in all cases except foraB-NTDseeds (Fig. 9A)",NA,NA,"Interaction examined in the presence of urea (2.5M and 7M) which was added to the mixture of the interactee + interactor ; interactor: B-chain fused to human alphaB-Cry (alphaB-BC), interactee: monomeric insulin",10.1039/D0RA05414C,AG00966
Insulin,Insulin,MDHHHHHHWIHRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEIRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDVLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKKHMGIVEQCCTSICSLYQLENYCN,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,"For the set of samples where insulin was pre-incubated with 2.5 M urea (Fig. 9C), adding the seeds increased the rate of fibrillation",NA,NA,"Interaction examined in the presence of urea 2.5M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. ; interactor: A-chain fused to human alphaB-Cry (alphaB-AC), interactee: monomeric insulin",10.1039/D0RA05414C,AG00967
Insulin,Insulin,MDIAIHHPWIHRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEIRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDVLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKKHMFVNQHLCGSHLVEALYLVCGERGFFYTPKT,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,"For the set of samples where insulin was pre-incubated with 2.5 M urea (Fig. 9C), adding the seeds increased the rate of fibrillation",NA,NA,"Interaction examined in the presence of urea 2.5M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. ; interactor: B-chain fused to human alphaB-Cry (alphaB-BC), interactee: monomeric insulin",10.1039/D0RA05414C,AG00968
Insulin,Insulin,MDHHHHHHWIHRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEIRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDVLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKKHMGIVEQCCTSICSLYQLENYCN,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,Faster aggregation,Yes; implied by kinetics.,No,"aB-AC, insulin, aB-Cry, A-chain, and aB-Cry exhibited fibrillation accelerating effect in decreasing order, respectively",NA,NA,"Interaction examined in the presence of urea 7.0M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. ; interactor: A-chain fused to human alphaB-Cry (alphaB-AC), interactee: monomeric insulin",10.1039/D0RA05414C,AG00969
Insulin,Insulin,MDIAIHHPWIHRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEIRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDVLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKKHMFVNQHLCGSHLVEALYLVCGERGFFYTPKT,>chainA GIVEQCCTSICSLYQLENYCN >chainB FVNQHLCGSHLVEALYLVCGERGFFYTPKT,No effect,No,No,aB-BC and a B-NTD showed similar kinetic in these stepwise sequential incubation experiments as compared to 7.0 M urea only.,NA,NA,"Interaction examined in the presence of urea 7.0M added to the interactee (insulin). The interactor was added after the incubation of interactee with urea. ; interactor: B-chain fused to human alphaB-Cry (alphaB-BC), interactee: monomeric insulin",10.1039/D0RA05414C,AG00970