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Volumn 86, Issue , 2017, Pages 69-95

Structural studies of amyloid proteins at the molecular level

Author keywords

Amyloid symmetry; Cryo electron microscopy; Cryo EM; Polymorphs; Solid state nuclear magnetic resonance; SsNMR; Steric zipper; X ray diffraction

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID PROTEIN; ASPARAGINE; GLUTAMINE; OLIGOMER; PRION PROTEIN; SERINE; THREONINE; TYROSINE;

EID: 85019910780     PISSN: 00664154     EISSN: 15454509     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-061516-045104     Document Type: Article
Times cited : (395)

References (100)
  • 1
    • 84908547666 scopus 로고    scopus 로고
    • Nomenclature 2014: Amyloid fibril proteins and clinical classification of the amyloidosis
    • Sipe JD, Benson MD, Buxbaum JN, Ikeda S, Merlini G, et al. (2014). Nomenclature 2014: amyloid fibril proteins and clinical classification of the amyloidosis. Amyloid 21(4): 221-24
    • (2014) Amyloid , vol.21 , Issue.4 , pp. 221-224
    • Sipe, J.D.1    Benson, M.D.2    Buxbaum, J.N.3    Ikeda, S.4    Merlini, G.5
  • 2
    • 0001419932 scopus 로고
    • The X-ray interpretation of denaturation and the structure of the seed globulins
    • Astbury WT, Dickinson S, Bailey K. (1935). The X-ray interpretation of denaturation and the structure of the seed globulins. Biochem. J. 29(10): 2351-60.1
    • (1935) Biochem. J. , vol.29 , Issue.10 , pp. 2351-23511
    • Astbury, W.T.1    Dickinson, S.2    Bailey, K.3
  • 3
    • 0000573263 scopus 로고
    • Configurations of polypeptide chainswith favored orientations around single bonds: Two new pleated sheets
    • Pauling L, Corey RB. (1951). Configurations of polypeptide chainswith favored orientations around single bonds: two new pleated sheets. PNAS 37(11): 729-40
    • (1951) PNAS , vol.37 , Issue.11 , pp. 729-740
    • Pauling, L.1    Corey, R.B.2
  • 4
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-βspine of amyloid-like fibrils
    • Nelson R, Sawaya MR, Balbirnie M, Madsen Aø, Riekel C, et al. (2005). Structure of the cross-βspine of amyloid-like fibrils. Nature 435(7043): 773-78
    • (2005) Nature , vol.435 , Issue.7043 , pp. 773-778
    • Nelson, R.1    Sawaya, M.R.2    Balbirnie, M.3    Madsen, A.Ø.4    Riekel, C.5
  • 5
    • 0001611370 scopus 로고
    • Electron microscopic observations on a fibrous component in amyloid of diverse origins
    • Cohen AS, Calkins E. (1959). Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature 183(4669): 1202-3
    • (1959) Nature , vol.183 , Issue.4669 , pp. 1202-1203
    • Cohen, A.S.1    Calkins, E.2
  • 6
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes ED, Glenner GG. (1968). X-ray diffraction studies on amyloid filaments. J. Histochem. Cytochem. 16(11): 673-77
    • (1968) J. Histochem. Cytochem , vol.16 , Issue.11 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 8
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ. (2002). The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297(5580): 353-56
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 9
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimer's disease
    • Goedert M, Spillantini MG. (2006). A century of Alzheimer's disease. Science 314(5800): 777-81
    • (2006) Science , vol.314 , Issue.5800 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 10
    • 70350061949 scopus 로고    scopus 로고
    • Multimodal techniques for diagnosis and prognosis of Alzheimer's disease
    • Perrin RJ, Fagan AM, Holtzman DM. (2009). Multimodal techniques for diagnosis and prognosis of Alzheimer's disease. Nature 461(7266): 916-22
    • (2009) Nature , vol.461 , Issue.7266 , pp. 916-922
    • Perrin, R.J.1    Fagan, A.M.2    Holtzman, D.M.3
  • 11
    • 0023905906 scopus 로고
    • Clinical, pathological, and neurochemical changes in dementia: A subgroup with preserved mental status and numerous neocortical plaques
    • Katzman R, Terry R, DeTeresa R, Brown T, Davies P, et al. (1988). Clinical, pathological, and neurochemical changes in dementia: a subgroup with preserved mental status and numerous neocortical plaques. Ann. Neurol. 23(2): 138-44
    • (1988) Ann. Neurol , vol.23 , Issue.2 , pp. 138-144
    • Katzman, R.1    Terry, R.2    DeTeresa, R.3    Brown, T.4    Davies, P.5
  • 12
    • 0030614627 scopus 로고    scopus 로고
    • Observation ofmetastable Aβamyloid protofibrils by atomic force microscopy
    • Harper JD, Wong SS, Lieber CM, Lansbury PT. (1997). Observation ofmetastable Aβamyloid protofibrils by atomic force microscopy. Chem. Biol. 4(2): 119-25
    • (1997) Chem. Biol , vol.4 , Issue.2 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 13
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis: Detection of a protofibrillar intermediate
    • Walsh DM, Lomakin A, Benedek GB, Condron MM, Teplow DB. (1997). Amyloid β-protein fibrillogenesis: detection of a protofibrillar intermediate. J. Biol. Chem. 272(35): 22364-72
    • (1997) J. Biol. Chem , vol.272 , Issue.35 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 14
    • 84886788712 scopus 로고    scopus 로고
    • A folding transition underlies the emergence of membrane affinity in amyloid-β
    • Nag S, Sarkar B, Chandrakesan M, Abhyanakar R, Bhowmik D, et al. (2013). A folding transition underlies the emergence of membrane affinity in amyloid-β. Phys. Chem. Chem. Phys. 15(44): 19129-33
    • (2013) Phys. Chem. Chem. Phys , vol.15 , Issue.44 , pp. 19129-19133
    • Nag, S.1    Sarkar, B.2    Chandrakesan, M.3    Abhyanakar, R.4    Bhowmik, D.5
  • 15
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Aβoligomer and Alzheimer's disease: An emperor in need of clothes
    • Benilova I, Karran E, De Strooper B. (2012). The toxic Aâoligomer and alzheimer's disease: An emperor in need of clothes. Nat. Neurosci. 15(3): 349-57
    • (2012) Nat. Neurosci , vol.15 , Issue.3 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 16
    • 0028172886 scopus 로고
    • Β-Amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo A, Yankner BA. (1994). β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. PNAS 91(25): 12243-47
    • (1994) PNAS , vol.91 , Issue.25 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 17
    • 79952742454 scopus 로고    scopus 로고
    • In vivo demonstration thatα-synuclein oligomers are toxic
    • Winner B, Jappelli R, Maji SK, Desplats PA, Boyer L, et al. (2011). In vivo demonstration thatα-synuclein oligomers are toxic. PNAS 108(10): 4194-99
    • (2011) PNAS , vol.108 , Issue.10 , pp. 4194-4199
    • Winner, B.1    Jappelli, R.2    Maji, S.K.3    Desplats, P.A.4    Boyer, L.5
  • 18
    • 84862701723 scopus 로고    scopus 로고
    • Fibrillar α-synuclein and Huntingtin exon 1 assemblies are toxic to the cells
    • Pieri L, Madiona K, Bousset L, Melki R. (2012). Fibrillar α-synuclein and Huntingtin exon 1 assemblies are toxic to the cells. Biophys. J. 102(12): 2894-905
    • (2012) Biophys. J. , vol.102 , Issue.12 , pp. 2894-2905
    • Pieri, L.1    Madiona, K.2    Bousset, L.3    Melki, R.4
  • 19
    • 85009453255 scopus 로고    scopus 로고
    • Time-resolved studies define the nature of toxic IAPP intermediates providing insight for anti-amyloidosis therapeutics
    • Abedini A, Plesner A, Cao P, Ridgway Z, Zhang J, et al. (2016). Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics. eLife 5: e12977
    • (2016) ELife , vol.5 , pp. e12977
    • Abedini, A.1    Plesner, A.2    Cao, P.3    Ridgway, Z.4    Zhang, J.5
  • 21
    • 84906257696 scopus 로고    scopus 로고
    • The physical chemistry of the amyloid phenomenon: Thermodynamics and kinetics of filamentous protein aggregation
    • Buell AK, Dobson CM, Knowles TPJ. (2014). The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation. Essays Biochem. 56: 11-39
    • (2014) Essays Biochem , vol.56 , pp. 11-39
    • Buell, A.K.1    Dobson, C.M.2    Knowles, T.P.J.3
  • 22
    • 0025801516 scopus 로고
    • Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro
    • Gustavsson A, Engström U, Westermark P. (1991). Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro. Biochem. Biophys. Res. Commun. 175(3): 1159-64
    • (1991) Biochem. Biophys. Res. Commun , vol.175 , Issue.3 , pp. 1159-1164
    • Gustavsson, A.1    Engström, U.2    Westermark, P.3
  • 23
    • 0026675307 scopus 로고
    • Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
    • Colon W, Kelly JW. (1992). Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31(36): 8654-60
    • (1992) Biochemistry , vol.31 , Issue.36 , pp. 8654-8660
    • Colon, W.1    Kelly, J.W.2
  • 24
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth DR, Sunde M, Bellotti V, Robinson CV, Hutchinson WL, et al. (1997). Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385(6619): 787-93
    • (1997) Nature , vol.385 , Issue.6619 , pp. 787-793
    • Booth, D.R.1    Sunde, M.2    Bellotti, V.3    Robinson, C.V.4    Hutchinson, W.L.5
  • 26
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fändrich M, Fletcher MA, Dobson CM. (2001). Amyloid fibrils from muscle myoglobin. Nature 410(6825): 165-66
    • (2001) Nature , vol.410 , Issue.6825 , pp. 165-166
    • Fändrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 27
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fändrich M, Dobson CM. (2002). The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J. 21(21): 5682-90
    • (2002) EMBO J. , vol.21 , Issue.21 , pp. 5682-5690
    • Fändrich, M.1    Dobson, C.M.2
  • 28
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the amylome, proteins capable of forming amyloid-like fibrils
    • Goldschmidt L, Teng PK, Riek R, Eisenberg D. (2010). Identifying the amylome, proteins capable of forming amyloid-like fibrils. PNAS 107(8): 3487-92
    • (2010) PNAS , vol.107 , Issue.8 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4
  • 29
    • 78650202063 scopus 로고    scopus 로고
    • Functional amyloid: Turning swords into plowshares
    • Otzen D. (2010). Functional amyloid: turning swords into plowshares. Prion 4(4): 256-64
    • (2010) Prion , vol.4 , Issue.4 , pp. 256-264
    • Otzen, D.1
  • 30
    • 84906267564 scopus 로고    scopus 로고
    • Functional amyloid: Widespread in nature, diverse in purpose
    • Pham CLL, Kwan AH, Sunde M. (2014). Functional amyloid: widespread in nature, diverse in purpose. Essays Biochem. 56: 207-19
    • (2014) Essays Biochem , vol.56 , pp. 207-219
    • Pham, C.L.L.1    Kwan, A.H.2    Sunde, M.3
  • 31
    • 0036468673 scopus 로고    scopus 로고
    • Role of Escherichia coli curli operons in directing amyloid fiber formation
    • Chapman MR, Robinson LS, Pinkner JS, Roth R, Heuser J, et al. (2002). Role of Escherichia coli curli operons in directing amyloid fiber formation. Science 295(5556): 851-55
    • (2002) Science , vol.295 , Issue.5556 , pp. 851-855
    • Chapman, M.R.1    Robinson, L.S.2    Pinkner, J.S.3    Roth, R.4    Heuser, J.5
  • 32
    • 67650809307 scopus 로고    scopus 로고
    • Functional amyloids as natural storage of peptide hormones in pituitary secretory granules
    • Maji SK, Perrin MH, Sawaya MR, Jessberger S, Vadodaria K, et al. (2009). Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938): 328-32
    • (2009) Science , vol.325 , Issue.5938 , pp. 328-332
    • Maji, S.K.1    Perrin, M.H.2    Sawaya, M.R.3    Jessberger, S.4    Vadodaria, K.5
  • 34
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation ofRNAgranules: Low complexity sequence domains form dynamic fibers within hydrogels
    • Kato M, Han TW, Xie S, Shi K, Du X, et al. (2012). Cell-free formation ofRNAgranules: Low complexity sequence domains form dynamic fibers within hydrogels. Cell 149(4): 753-67
    • (2012) Cell , vol.149 , Issue.4 , pp. 753-767
    • Kato, M.1    Han, T.W.2    Xie, S.3    Shi, K.4    Du, X.5
  • 35
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the Aplysia CPEB has prion-like properties
    • Si K, Lindquist S, Kandel ER. (2003). A neuronal isoform of the Aplysia CPEB has prion-like properties. Cell 115(7): 879-91
    • (2003) Cell , vol.115 , Issue.7 , pp. 879-891
    • Si, K.1    Lindquist, S.2    Kandel, E.R.3
  • 36
    • 79961211353 scopus 로고    scopus 로고
    • Nanomechanics of functional and pathological amyloid materials
    • Knowles TPJ, Buehler MJ. (2011). Nanomechanics of functional and pathological amyloid materials. Nat. Nanotechnol. 6(8): 469-79
    • (2011) Nat. Nanotechnol , vol.6 , Issue.8 , pp. 469-479
    • Knowles, T.P.J.1    Buehler, M.J.2
  • 37
    • 84891951870 scopus 로고    scopus 로고
    • Designed amyloid fibers as materials for selective carbon dioxide capture
    • Li D, Furukawa H, Deng H, Liu C, Yaghi OM, Eisenberg DS. (2014). Designed amyloid fibers as materials for selective carbon dioxide capture. PNAS 111(1): 191-96
    • (2014) PNAS , vol.111 , Issue.1 , pp. 191-196
    • Li, D.1    Furukawa, H.2    Deng, H.3    Liu, C.4    Yaghi, O.M.5    Eisenberg, D.S.6
  • 38
    • 0035956924 scopus 로고    scopus 로고
    • An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid
    • Balbirnie M, Grothe R, Eisenberg DS. (2001). An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid. PNAS 98(5): 2375-80
    • (2001) PNAS , vol.98 , Issue.5 , pp. 2375-2380
    • Balbirnie, M.1    Grothe, R.2    Eisenberg, D.S.3
  • 39
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie JU, Lüthy R, Eisenberg D. (1991). A method to identify protein sequences that fold into a known three-dimensional structure. Science 253(5016): 164-70
    • (1991) Science , vol.253 , Issue.5016 , pp. 164-170
    • Bowie, J.U.1    Lüthy, R.2    Eisenberg, D.3
  • 41
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-βspines reveal varied steric zippers
    • Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, et al. (2007). Atomic structures of amyloid cross-βspines reveal varied steric zippers. Nature 447(7143): 453-57
    • (2007) Nature , vol.447 , Issue.7143 , pp. 453-457
    • Sawaya, M.R.1    Sambashivan, S.2    Nelson, R.3    Ivanova, M.I.4    Sievers, S.A.5
  • 43
    • 67650022868 scopus 로고    scopus 로고
    • Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process
    • Wiltzius JJW, Sievers SA, Sawaya MR, Eisenberg D. (2009). Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process. Protein Sci. 18(7): 1521-30
    • (2009) Protein Sci , vol.18 , Issue.7 , pp. 1521-1530
    • Wiltzius, J.J.W.1    Sievers, S.A.2    Sawaya, M.R.3    Eisenberg, D.4
  • 44
    • 77956941468 scopus 로고    scopus 로고
    • Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease
    • Apostol MI, Sawaya MR, Cascio D, Eisenberg D. (2010). Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease. J. Biol. Chem. 285(39): 29671-75
    • (2010) J. Biol. Chem , vol.285 , Issue.39 , pp. 29671-29675
    • Apostol, M.I.1    Sawaya, M.R.2    Cascio, D.3    Eisenberg, D.4
  • 45
    • 79953183597 scopus 로고    scopus 로고
    • Atomic structures suggest determinants of transmission barriers in mammalian prion disease
    • Apostol MI, Wiltzius JJW, Sawaya MR, Cascio D, Eisenberg D. (2011). Atomic structures suggest determinants of transmission barriers in mammalian prion disease. Biochemistry 50(13): 2456-63
    • (2011) Biochemistry , vol.50 , Issue.13 , pp. 2456-2463
    • Apostol, M.I.1    Wiltzius, J.J.W.2    Sawaya, M.R.3    Cascio, D.4    Eisenberg, D.5
  • 48
    • 84891959532 scopus 로고    scopus 로고
    • Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS
    • Ivanova MI, Sievers SA, Guenther EL, Johnson LM, Winkler DD, et al. (2014). Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS. PNAS 111(1): 197-201
    • (2014) PNAS , vol.111 , Issue.1 , pp. 197-201
    • Ivanova, M.I.1    Sievers, S.A.2    Guenther, E.L.3    Johnson, L.M.4    Winkler, D.D.5
  • 49
    • 84871398573 scopus 로고    scopus 로고
    • Out-of-register β-sheets suggest a pathway to toxic amyloid aggregates
    • Liu C, Zhao M, Jiang L, Cheng P-N, Park J, et al. (2012). Out-of-register β-sheets suggest a pathway to toxic amyloid aggregates. PNAS 109(51): 20913-18
    • (2012) PNAS , vol.109 , Issue.51 , pp. 20913-20918
    • Liu, C.1    Zhao, M.2    Jiang, L.3    Cheng, P.-N.4    Park, J.5
  • 50
    • 84978036723 scopus 로고    scopus 로고
    • Crystal structures of IAPP amyloidogenic segments reveal a novel packing motif of out-of-register beta sheets
    • Soriaga AB, Sangwan S, Macdonald R, Sawaya MR, Eisenberg D. (2016). Crystal structures of IAPP amyloidogenic segments reveal a novel packing motif of out-of-register beta sheets. J. Phys. Chem. B 120(26): 5810-16
    • (2016) J. Phys. Chem. B , vol.120 , Issue.26 , pp. 5810-5816
    • Soriaga, A.B.1    Sangwan, S.2    Macdonald, R.3    Sawaya, M.R.4    Eisenberg, D.5
  • 51
    • 84957910884 scopus 로고    scopus 로고
    • A designed inhibitor of p53 aggregation rescues p53 tumor suppression in ovarian carcinomas
    • Soragni A, Janzen DM, Johnson LM, Lindgren AG, Thai-Quynh Nguyen A, et al. (2016). A designed inhibitor of p53 aggregation rescues p53 tumor suppression in ovarian carcinomas. Cancer Cell 29(1): 90-103
    • (2016) Cancer Cell , vol.29 , Issue.1 , pp. 90-103
    • Soragni, A.1    Janzen, D.M.2    Johnson, L.M.3    Lindgren, A.G.4    Thai-Quynh Nguyen, A.5
  • 52
    • 84891709353 scopus 로고    scopus 로고
    • A serendipitous survey of prediction algorithms for amyloidogenicity
    • Roland BP, Kodali R, Mishra R, Wetzel R. (2013). A serendipitous survey of prediction algorithms for amyloidogenicity. Biopolymers 100(6): 780-89
    • (2013) Biopolymers , vol.100 , Issue.6 , pp. 780-789
    • Roland, B.P.1    Kodali, R.2    Mishra, R.3    Wetzel, R.4
  • 53
    • 79953765150 scopus 로고    scopus 로고
    • Solid-state NMR studies of amyloid fibril structure
    • Tycko R. (2011). Solid-state NMR studies of amyloid fibril structure. Annu. Rev. Phys. Chem. 62: 279-99
    • (2011) Annu. Rev. Phys. Chem , vol.62 , pp. 279-299
    • Tycko, R.1
  • 54
    • 66149140617 scopus 로고    scopus 로고
    • Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure
    • Paravastu AK, Qahwash I, Leapman RD, Meredith SC, Tycko R. (2009). Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure. PNAS 106(18): 7443-48
    • (2009) PNAS , vol.106 , Issue.18 , pp. 7443-7448
    • Paravastu, A.K.1    Qahwash, I.2    Leapman, R.D.3    Meredith, S.C.4    Tycko, R.5
  • 55
    • 84923368907 scopus 로고    scopus 로고
    • How cryo-EM is revolutionizing structural biology
    • Bai X, McMullan G, Scheres SHW. (2015). How cryo-EM is revolutionizing structural biology. Trends Biochem. Sci. 40(1): 49-57
    • (2015) Trends Biochem. Sci , vol.40 , Issue.1 , pp. 49-57
    • Bai, X.1    McMullan, G.2    Scheres, S.H.W.3
  • 57
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence MC, Colman PM. (1993). Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234(4): 946-50
    • (1993) J. Mol. Biol , vol.234 , Issue.4 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 58
    • 84875454954 scopus 로고    scopus 로고
    • The zipper groups of the amyloid state of proteins
    • Stroud JC. (2013). The zipper groups of the amyloid state of proteins. Acta Crystallogr. Sect.D69(Pt 4): 540-45
    • (2013) Acta Crystallogr. Sect.D , vol.69 , Issue.PT4 , pp. 540-545
    • Stroud, J.C.1
  • 59
    • 67349152747 scopus 로고    scopus 로고
    • Globular tetramers of β2-microglobulin assemble into elaborate amyloid fibrils
    • White HE, Hodgkinson JL, Jahn TR, Cohen-Krausz S, Gosal WS, et al. (2009). Globular tetramers of β2-microglobulin assemble into elaborate amyloid fibrils. J. Mol. Biol. 389(1): 48-57
    • (2009) J. Mol. Biol , vol.389 , Issue.1 , pp. 48-57
    • White, H.E.1    Hodgkinson, J.L.2    Jahn, T.R.3    Cohen-Krausz, S.4    Gosal, W.S.5
  • 60
  • 62
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electronmicroscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jiménez JL, Guijarro JI, Orlova E, Zurdo J, Dobson CM, et al. (1999). Cryo-electronmicroscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18(4): 815-21
    • (1999) EMBO J. , vol.18 , Issue.4 , pp. 815-821
    • Jiménez, J.L.1    Guijarro, J.I.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5
  • 63
    • 0020491376 scopus 로고
    • Structure ofβ-sheets: Origin of the righthanded twist and of the increased stability of antiparallel over parallel sheets
    • Chou KC, Pottle M, Némethy G, Ueda Y, Scheraga HA. (1982). Structure ofβ-sheets: origin of the righthanded twist and of the increased stability of antiparallel over parallel sheets. J. Mol. Biol. 162(1): 89-112
    • (1982) J. Mol. Biol , vol.162 , Issue.1 , pp. 89-112
    • Chou, K.C.1    Pottle, M.2    Némethy, G.3    Ueda, Y.4    Scheraga, H.A.5
  • 64
    • 84983638394 scopus 로고    scopus 로고
    • Atomic-resolution structure of a diseaserelevant Aβ(1-42) amyloid fibril
    • Wälti MA, Ravotti F, Arai H, Glabe CG, Wall JS, et al. (2016). Atomic-resolution structure of a diseaserelevant Aβ(1-42) amyloid fibril. PNAS 113(34): e4976-84
    • (2016) PNAS , vol.113 , Issue.34 , pp. e4976-e4984
    • Wälti, M.A.1    Ravotti, F.2    Arai, H.3    Glabe, C.G.4    Wall, J.S.5
  • 65
    • 84982685920 scopus 로고    scopus 로고
    • Atomic resolution structure of monomorphic Aβ42 amyloid fibrils
    • Colvin MT, Silvers R, Ni QZ, Can TV, Sergeyev IV, et al. (2016). Atomic resolution structure of monomorphic Aβ42 amyloid fibrils. J. Am. Chem. Soc. 138(30): 9663-74
    • (2016) J. Am. Chem. Soc , vol.138 , Issue.30 , pp. 9663-9674
    • Colvin, M.T.1    Silvers, R.2    Ni, Q.Z.3    Can, T.V.4    Sergeyev, I.V.5
  • 67
    • 77957324146 scopus 로고    scopus 로고
    • Atomic-resolution threedimensional structure of HET-s 218-289) amyloid fibrils by solid-state NMR spectroscopy
    • Van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, et al. (2010). Atomic-resolution threedimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy. J. Am. Chem. Soc. 132(39): 13765-75
    • (2010) J. Am. Chem. Soc , vol.132 , Issue.39 , pp. 13765-13775
    • Van Melckebeke, H.1    Wasmer, C.2    Lange, A.3    Ab, E.4    Loquet, A.5
  • 68
    • 78650982368 scopus 로고    scopus 로고
    • B2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages
    • Liu C, Sawaya MR, Eisenberg D. (2011). B2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages. Nat. Struct. Mol. Biol. 18(1): 49-55
    • (2011) Nat. Struct. Mol. Biol , vol.18 , Issue.1 , pp. 49-55
    • Liu, C.1    Sawaya, M.R.2    Eisenberg, D.3
  • 71
    • 2342444028 scopus 로고    scopus 로고
    • Seeding specificity in amyloid growth induced by heterologous fibrils
    • O'Nuallain B, Williams AD, Westermark P, Wetzel R. (2004). Seeding specificity in amyloid growth induced by heterologous fibrils. J. Biol. Chem. 279(17): 17490-99
    • (2004) J. Biol. Chem , vol.279 , Issue.17 , pp. 17490-17499
    • O'Nuallain, B.1    Williams, A.D.2    Westermark, P.3    Wetzel, R.4
  • 72
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • Petkova AT, Leapman RD, Guo Z, Yau W-M, Mattson MP, Tycko R. (2005). Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science 307(5707): 262-65
    • (2005) Science , vol.307 , Issue.5707 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5    Tycko, R.6
  • 73
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
    • Petkova AT, YauW-M, Tycko R. (2006). Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils. Biochemistry 45(2): 498-512
    • (2006) Biochemistry , vol.45 , Issue.2 , pp. 498-512
    • Petkova, A.T.1    YauW-M Tycko, R.2
  • 74
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
    • Paravastu AK, Leapman RD, Yau W-M, Tycko R. (2008). Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils. PNAS 105(47): 18349-54
    • (2008) PNAS , vol.105 , Issue.47 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.-M.3    Tycko, R.4
  • 75
    • 84920175943 scopus 로고    scopus 로고
    • Atomic-resolution threedimensional structure of amyloid β fibrils bearing the Osaka mutation
    • Schütz AK, Vagt T, Huber M, Ovchinnikova OY, Cadalbert R, et al. (2015). Atomic-resolution threedimensional structure of amyloid β fibrils bearing the Osaka mutation. Angew. Chem. Int. Ed. Engl. 54(1): 331-35
    • (2015) Angew. Chem. Int. Ed. Engl , vol.54 , Issue.1 , pp. 331-335
    • Schütz, A.K.1    Vagt, T.2    Huber, M.3    Ovchinnikova, O.Y.4    Cadalbert, R.5
  • 76
    • 84930413213 scopus 로고    scopus 로고
    • Aβ 1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
    • Xiao Y, Ma B, McElheny D, Parthasarathy S, Long F, et al. (2015). Aβ(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease. Nat. Struct. Mol. Biol. 22(6): 499-505
    • (2015) Nat. Struct. Mol. Biol , vol.22 , Issue.6 , pp. 499-505
    • Xiao, Y.1    Ma, B.2    McElheny, D.3    Parthasarathy, S.4    Long, F.5
  • 77
    • 84942909501 scopus 로고    scopus 로고
    • Peptide dimer structure in an Aβ 1-42) fibril visualized with cryo-EM
    • Schmidt M, Rohou A, Lasker K, Yadav JK, Schiene-Fischer C, et al. (2015). Peptide dimer structure in an Aβ(1-42) fibril visualized with cryo-EM. PNAS 112(38): 11858-63
    • (2015) PNAS , vol.112 , Issue.38 , pp. 11858-11863
    • Schmidt, M.1    Rohou, A.2    Lasker, K.3    Yadav, J.K.4    Schiene-Fischer, C.5
  • 79
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, et al. (1997). Mutation in the α-synuclein gene identified in families with Parkinson's disease. Science 276(5321): 2045-47
    • (1997) Science , vol.276 , Issue.5321 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5
  • 80
    • 0034922671 scopus 로고    scopus 로고
    • Identification of the region of non-Aβ component (NAC) of Alzheimer's disease amyloid responsible for its aggregation and toxicity
    • Bodles AM, Guthrie DJ, Greer B, Irvine GB. (2001). Identification of the region of non-Aβ component (NAC) of Alzheimer's disease amyloid responsible for its aggregation and toxicity. J. Neurochem. 78(2): 384-95
    • (2001) J. Neurochem , vol.78 , Issue.2 , pp. 384-395
    • Bodles, A.M.1    Guthrie, D.J.2    Greer, B.3    Irvine, G.B.4
  • 81
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly
    • Giasson BI, Murray IV, Trojanowski JQ, Lee VM. (2001). A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly. J. Biol. Chem. 276(4): 2380-86
    • (2001) J. Biol. Chem , vol.276 , Issue.4 , pp. 2380-2386
    • Giasson, B.I.1    Murray, I.V.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 82
    • 84942522975 scopus 로고    scopus 로고
    • Structure of the toxic core of α-synuclein from invisible crystals
    • Rodriguez JA, Ivanova MI, Sawaya MR, Cascio D, Reyes FE, et al. (2015). Structure of the toxic core of α-synuclein from invisible crystals. Nature 525(7570): 486-90
    • (2015) Nature , vol.525 , Issue.7570 , pp. 486-490
    • Rodriguez, J.A.1    Ivanova, M.I.2    Sawaya, M.R.3    Cascio, D.4    Reyes, F.E.5
  • 83
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka M, Chien P, Naber N, Cooke R, Weissman JS. (2004). Conformational variations in an infectious protein determine prion strain differences. Nature 428(6980): 323-28
    • (2004) Nature , vol.428 , Issue.6980 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 85
    • 0031720905 scopus 로고    scopus 로고
    • Eight prion strains have PrPSc molecules with different conformations
    • Safar J, Wille H, Itri V, Groth D, Serban H, et al. (1998). Eight prion strains have PrPSc molecules with different conformations. Nat. Med. 4(10): 1157-65
    • (1998) Nat. Med , vol.4 , Issue.10 , pp. 1157-1165
    • Safar, J.1    Wille, H.2    Itri, V.3    Groth, D.4    Serban, H.5
  • 86
    • 0027195933 scopus 로고
    • Seeding one-dimensional crystallization of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT. (1993). Seeding one-dimensional crystallization of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73(6): 1055-58
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 87
    • 84862620376 scopus 로고    scopus 로고
    • A unifying role for prions in neurodegenerative diseases
    • Prusiner SB. (2012). A unifying role for prions in neurodegenerative diseases. Science 336(6088): 1511-13
    • (2012) Science , vol.336 , Issue.6088 , pp. 1511-1513
    • Prusiner, S.B.1
  • 88
    • 72149125838 scopus 로고    scopus 로고
    • The transcellular spread of cytosolic amyloids, prions, and prionoids
    • Aguzzi A, Rajendran L. (2009). The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 64(6): 783-90
    • (2009) Neuron , vol.64 , Issue.6 , pp. 783-790
    • Aguzzi, A.1    Rajendran, L.2
  • 89
    • 84869109864 scopus 로고    scopus 로고
    • Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • Luk KC, Kehm V, Carroll J, Zhang B, O'Brien P, et al. (2012). Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 338(6109): 949-53
    • (2012) Science , vol.338 , Issue.6109 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O'Brien, P.5
  • 90
    • 84861758226 scopus 로고    scopus 로고
    • Trans-cellular propagation of tau aggregation by fibrillar species
    • Kfoury N, Holmes BB, Jiang H, Holtzman DM, Diamond MI. (2012). Trans-cellular propagation of tau aggregation by fibrillar species. J. Biol. Chem. 287(23): 19440-51
    • (2012) J. Biol. Chem , vol.287 , Issue.23 , pp. 19440-19451
    • Kfoury, N.1    Holmes, B.B.2    Jiang, H.3    Holtzman, D.M.4    Diamond, M.I.5
  • 91
    • 78149392229 scopus 로고    scopus 로고
    • Peripherally applied Aβ-containing inoculates induce cerebral β-amyloidosis
    • Eisele YS, Obermüller U, Heilbronner G, Baumann F, Kaeser SA, et al. (2010). Peripherally applied Aβ-containing inoculates induce cerebral β-amyloidosis. Science 330(6006): 980-82
    • (2010) Science , vol.330 , Issue.6006 , pp. 980-982
    • Eisele, Y.S.1    Obermüller, U.2    Heilbronner, G.3    Baumann, F.4    Kaeser, S.A.5
  • 92
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, et al. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300(5618): 486-89
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5
  • 93
    • 84863986886 scopus 로고    scopus 로고
    • Oligomeric intermediates in amyloid formation: Structure determination and mechanisms of toxicity
    • Fändrich M. (2012). Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity. J. Mol. Biol. 421(4-5): 427-40
    • (2012) J. Mol. Biol , vol.421 , Issue.4-5 , pp. 427-440
    • Fändrich, M.1
  • 94
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • Haass C, Selkoe DJ. (2007). Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat. Rev. Mol. Cell Biol. 8(2): 101-12
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 97
    • 84861206757 scopus 로고    scopus 로고
    • Toxic fibrillar oligomers of amyloid-β have cross-β structure
    • Stroud JC, Liu C, Teng PK, Eisenberg D. (2012). Toxic fibrillar oligomers of amyloid-β have cross-β structure. PNAS 109(20): 7717-22
    • (2012) PNAS , vol.109 , Issue.20 , pp. 7717-7722
    • Stroud, J.C.1    Liu, C.2    Teng, P.K.3    Eisenberg, D.4
  • 98
    • 84907916691 scopus 로고    scopus 로고
    • Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers
    • Gu L, Liu C, Stroud JC, Ngo S, Jiang L, Guo Z. (2014). Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers. J. Biol. Chem. 289(39): 27300-313
    • (2014) J. Biol. Chem , vol.289 , Issue.39 , pp. 27300-27313
    • Gu, L.1    Liu, C.2    Stroud, J.C.3    Ngo, S.4    Jiang, L.5    Guo, Z.6
  • 100
    • 85009477015 scopus 로고    scopus 로고
    • Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity
    • Krotee P, Rodriguez JA, Sawaya MR, Cascio D, Reyes FE, et al. (2017). Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity. eLife 6: e19273
    • (2017) ELife , vol.6 , pp. e19273
    • Krotee, P.1    Rodriguez, J.A.2    Sawaya, M.R.3    Cascio, D.4    Reyes, F.E.5


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