Structure, formation and propagation of amyloid fibrils

Current Pharmaceutical Design

Volumn 14, Issue 30, 2008, Pages 3205-3218

  Goto, Yuji ^a   Yagi, Hisashi ^a   Yamaguchi, Keiichi ^a,c   Chatani, Eri ^a,d   Ban, Tadato ^b  

^a OSAKA UNIVERSITY   (Japan)

^b National Institute of Advanced Industrial Science and Technology   (Japan)

^c GIFU UNIVERSITY   (Japan)

^d RITSUMEIKAN UNIVERSITY   (Japan)

Author keywords

2 microglobulin; Amyloid; Amyloid ; Dialysis related amyloidosis; Protein misfolding; Total internal fluorescence microscopy

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40];

ALZHEIMER DISEASE; FLUORESCENCE MICROSCOPY; HUMAN; INHERITANCE; MOLECULAR MECHANICS; MORPHOLOGICAL ADAPTATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REVIEW; STRUCTURE ANALYSIS; ULTRASOUND; ANIMAL; BIOSYNTHESIS; CHEMICAL STRUCTURE; CHEMISTRY; HYDROGEN BOND; METABOLISM; PROTEIN BINDING; PROTEIN FOLDING;

AMYLOID; ANIMALS; HUMANS; HYDROGEN BONDING; MICROSCOPY, FLUORESCENCE; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY;

EID: 59649087258     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161208786404146     Document Type: Review

References (121)

1. Sipe JD. Amyloidosis. Annu Rev Biochem 1992; 61: 947-975.
2. Kelly JW. Alternative conformations of amyloidogenic proteins govern their behavior. Curr Opin Struct Biol 1996; 6: 11-17.
3. Rochet JC, Lansbury PT, Jr. Amyloid fibrillogenesis: Themes and variations. Curr Opin Struct Biol 2000; 10: 60-68.
4. Dobson CM. Protein folding and misfolding. Nature 2003; 426: 884-890
5. Uversky VN, Fink AL. Conformational constraints for amyloid fibrillation: The importance of being unfolded. Biochim Biophys Acta 2004; 1698: 131-153.
6. Naiki H, Hashimoto N, Suzuki S, Kimura H, Nakakuki K, Gejyo F. Establishment of a kinetic model of dialysis-related amyloid fibril extension in vivo. Amyloid 1997; 4: 223-232.
7. Sela M, White FH Jr, Anfinsen CB. Reductive cleavage of disulfide bridges in ribonuclease. Science 1957; 125: 691-692.
8. Ohnishi S, Koide A, Koide S. Solution conformation and amyloid-like fibril formation of a polar peptide derived from a beta-hairpin in the OspA single-layer beta-sheet. J Mol Biol 2000; 301: 477-489.
9. MacPhee CE, Dobson CM. Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin. J Mol Biol 2000; 297: 1203-1215.
10. Fowler DM, Koulov AV, Balch WE, Kelly JW. Functional amyloid - from bacteria to humans. Trends Biochem Sci 2007; 32: 217-224.
11. Fowler DM, Koulov AV, Alory-Jost C, Marks MS, Balch WE, Kelly JW. Functional amyloid formation within mammalian tissue. PLoS Biol 2006; 4: e6.
12. Fandrich M, Dobson CM. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J 2002; 21: 5682-5690.
13. Chatani E, Kato M, Kawai T, Naiki H, Goto Y. Main-chain dominated amyloid structures demonstrated by the effect of high pressure. J Mol Biol 2005; 352: 941-951.
14. Chatani E, Goto Y. Structural stability of amyloid fibrils of beta(2)-microglobulin in comparison with its native fold. Biochim Biophys Acta 2005; 1753: 64-75.
15. Gejyo F, Yamada T, Odani S, Nakagawa Y, Arakawa M, Kunitomo T, et al. A new form of amyloid protein associated with chronic hemodialysis was identified as beta 2-microglobulin. Biochem Biophys Res Commun 1985; 129: 701-706.
16. Yamamoto S, Gejyo F. Historical background and clinical treatment of dialysis-related amyloidosis. Biochim Biophys Acta 2005; 1753: 4-10
17. Bjorkman PJ, Saper MA, Samraoui B, Bennett WS, Strominger JL, Wiley DC. Structure of the human class I histocompatibility antigen, HLA-A2. Nature 1987; 329: 506-512.
18. Trinh CH, Smith DP, Kalverda AP, Phillips SE, Radford SE. Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties. Proc Natl Acad Sci USA 2002; 99: 9771-9776
19. Kihara M, Chatani E, Iwata K, Yamamoto K, Matsuura T, Nakagawa A, et al. Conformation of amyloid fibrils of beta2-microglobulin probed by tryptophan mutagenesis. J Biol Chem 2006; 281: 31061-31069.
20. McParland VJ, Kad NM, Kalverda AP, Brown A, Kirwin-Jones P, Hunter MG, et al. Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro. Biochemistry 2000; 39: 8735-8746
21. Esposito G, Michelutti R, Verdone G, Viglino P, Hernandez H, Robinson CV, et al. Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci 2000; 9: 831-845.
22. Kad NM, Thomson NH, Smith DP, Smith DA, Radford SE. Beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro. J Mol Biol 2001; 313: 559-571.
23. Smith DP, Radford SE. Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro. Protein Sci 2001; 10: 1775-1784.
24. Chiti F, Mangione P, Andreola A, Giorgetti S, Stefani M, Dobson CM, et al. Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin. J Mol Biol 2001; 307: 379-391.
25. Hong DP, Gozu M, Hasegawa K, Naiki H, Goto Y. Conformation of beta 2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond. J Biol Chem 2002; 277: 21554-21560.
26. Hoshino M, Katou H, Hagihara Y, Hasegawa K, Naiki H, Goto Y. Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange. Nat Struct Biol 2002; 9: 332-336.
27. Kozhukh GV, Hagihara Y, Kawakami T, Hasegawa K, Naiki H, Goto Y. Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I. J Biol Chem 2002; 277: 1310-1315.
28. Ohhashi Y, Hagihara Y, Kozhukh G, Hoshino M, Hasegawa K, Yamaguchi I, et al. The intrachain disulfide bond of beta(2)-microglobulin is not essential for the immunoglobulin fold at neural pH, but is essential for amyloid fibril formation at acidic pH. J Biochem 2002; 131: 45-52.
29. Chiba T, Hagihara Y, Higurashi T, Hasegawa K, Naiki H, Goto Y. Amyloid fibril formation in the context of full-length protein: Effects of proline mutations on the amyloid fibril formation of beta2-microglobulin. J Biol Chem 2003; 278: 47016-47024.
30. Smith DP, Jones S, Serpell LC, Sunde M, Radford SE. A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation. J Mol Biol 2003; 330: 943-954.
31. McParland VJ, Kalverda AP, Homans SW, Radford SE. Structural properties of an amyloid precursor of beta(2)-microglobulin. Nat Struct Biol 2002; 9: 326-331.
32. Kad NM, Myers SL, Smith DP, Smith DA, Radford SE, Thomson NH. Hierarchical assembly of beta2-microglobulin amyloid in vitro revealed by atomic force microscopy. J Mol Biol 2003; 330: 785-797.
33. Ivanova MI, Sawaya MR, Gingery M, Attinger A, Eisenberg D. An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril. Proc Natl Acad Sci USA 2004; 101: 10584-10589
34. Kihara M, Chatani E, Sakai M, Hasegawa K, Naiki H, Goto Y. Seeding-dependent maturation of beta2-microglobulin amyloid fibrils at neutral pH. J Biol Chem 2005; 280: 12012-12018.
35. Corazza A, Pettirossi F, Viglino P, Verdone G, Garcia J, Dumy P, et al. Properties of some variants of human beta2-microglobulin and amyloidogenesis. J Biol Chem 2004; 279: 9176-9189.
36. Ohhashi Y, Kihara M, Naiki H, Goto Y. Ultrasonication-induced amyloid fibril formation of beta2-microglobulin. J Biol Chem 2005; 280: 32843-32848.
37. Eakin CM, Berman AJ, Miranker AD. A native to amyloidogenic transition regulated by a backbone trigger. Nat Struct Mol Biol 2006; 13: 202-208.
38. Jahn TR, Parker MJ, Homans SW, Radford SE. Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat Struct Mol Biol 2006; 13: 195-201.
39. Sasahara K, Yagi H, Naiki H, Goto Y. Heat-triggered conversion of protofibrils into mature amyloid fibrils of beta2-microglobulin. Biochemistry 2007; 46: 3286-3293.
40. Fogolari F, Corazza A, Viglino P, Zuccato P, Pieri L, Faccioli P, et al. Molecular dynamics simulation suggests possible interaction patterns at early steps of beta2-microglobulin aggregation. Biophys J 2007; 92: 1673-1681.
41. Serpell LC, Berriman J, Jakes R, Goedert M, Crowther RA. Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation. Proc Natl Acad Sci USA 2000; 97: 4897-4902
42. Jimenez JL, Nettleton EJ, Bouchard M, Robinson CV, Dobson CM, Saibil HR. The protofilament structure of insulin amyloid fibrils. Proc Natl Acad Sci USA 2002; 99: 9196-9201.
43. Katou H, Kanno T, Hoshino M, Hagihara Y, Tanaka H, Kawai T, et al. The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR. Protein Sci 2002; 11: 2218-2229.
44. Yamaguchi K, Katou H, Hoshino M, Hasegawa K, Naiki H, Goto Y. Core and heterogeneity of beta2-microglobulin amyloid fibrils as revealed by H/D exchange. J Mol Biol 2004; 338: 559-571.
45. Hiramatsu H, Goto Y, Naiki H, Kitagawa T. Core structure of amyloid fibril proposed from IR-microscope linear dichroism. J Am Chem Soc 2004; 126: 3008-3009.
46. Hiramatsu H, Goto Y, Naiki H, Kitagawa T. Structural model of the amyloid fibril formed by beta(2)-microglobulin #21-31 fragment based on vibrational spectroscopy. J Am Chem Soc 2005; 127: 7988-7989.
47. Kardos J, Okuno D, Kawai T, Hagihara Y, Yumoto N, Kitagawa T, et al. Structural studies reveal that the diverse morphology of beta(2)-microglobulin aggregates is a reflection of different molecular architectures. Biochim Biophys Acta 2005; 1753: 108-120.
48. Jahn TR, Tennent GA, Radford SE. A common {beta}-sheet Architecture underlies in vitro and in vivo {beta}2-microglobulin amyloid fibrils. J Biol Chem 2008; 283: 17279-17286.
49. Esposito G, Ricagno S, Corazza A, Rennella E, Gumral D, Mimmi MC, et al. The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties. J Mol Biol 2008; 378: 885-895.
50. Petkova AT, Ishii Y, Balbach JJ, Antzutkin ON, Leapman RD, Delaglio F, et al. A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci USA 2002; 99: 16742-16747.
51. Jaroniec CP, MacPhee CE, Bajaj VS, McMahon MT, Dobson CM, Griffin RG. High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proc Natl Acad Sci USA 2004; 101: 711-716.
52. Naito A, Kamihira M, Inoue R, Saito H. Structural diversity of amyloid fibril formed in human calcitonin as revealed by site-directed 13C solid-state NMR spectroscopy. Magn Reson Chem 2004; 42: 247-257.
53. Luhrs T, Ritter C, Adrian M, Riek-Loher D, Bohrmann B, Dobeli H, et al. 3D structure of Alzheimer's amyloid-beta(1-42) fibrils. Proc Natl Acad Sci USA 2005; 102: 17342-17347.
54. Ritter C, Maddelein ML, Siemer AB, Luhrs T, Ernst M, Meier BH, et al. Correlation of structural elements and infectivity of the HET-s prion. Nature 2005; 435: 844-848.
55. Heise H, Hoyer W, Becker S, Andronesi OC, Riedel D, Baldus M. Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR. Proc Natl Acad Sci USA 2005; 102: 15871-15876.
56. Chimon S, Shaibat MA, Jones CR, Calero DC, Aizezi B, Ishii Y. Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's beta-amyloid. Nat Struct Mol Biol 2007.
57. Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 2005; 307: 262-265.
58. Vilar M, Chou HT, Luhrs T, Maji SK, Riek-Loher D, Verel R, et al. The fold of alpha-synuclein fibrils. Proc Natl Acad Sci USA 2008; 105: 8637-8642.
59. Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH. Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science 2008; 319: 1523-1526.
60. Shivaprasad S, Wetzel R. An intersheet packing interaction in A beta fibrils mapped by disulfide cross-linking. Biochemistry 2004; 43: 15310-15317.
61. Ohhashi Y, Hasegawa K, Naiki H, Goto Y. Optimum amyloid fibril formation of a peptide fragment suggests the amyloidogenic preference of beta2-microglobulin under physiological conditions. J Biol Chem 2004; 279: 10814-10821.
62. Yamaguchi K, Naiki H, Goto Y. Mechanism by which the amyloid-like fibrils of a beta 2-microglobulin fragment are induced by fluorine-substituted alcohols. J Mol Biol 2006; 363: 279-288.
63. Yamaguchi K, Takahashi S, Kawai T, Naiki H, Goto Y. Seeding-dependent propagation and maturation of amyloid fibril conformation. J Mol Biol 2005; 352: 952-960.
64. Iwata K, Fujiwara T, Matsuki Y, Akutsu H, Takahashi S, Naiki H, et al. 3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR. Proc Natl Acad Sci USA 2006; 103: 18119-18124.
65. Cornilescu G, Delaglio F, Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 1999; 13: 289-302.
66. Kardos J, Yamamoto K, Hasegawa K, Naiki H, Goto Y. Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry. J Biol Chem 2004; 279: 55308-55314.
67. Chatani E, Naiki H, Goto Y. Seeding-dependent propagation and maturation of beta2-microglobulin amyloid fibrils under high pressure. J Mol Biol 2006; 359: 1086-1096.
68. Sasahara K, Naiki H, Goto Y. Kinetically controlled thermal response of beta2-microglobulin amyloid fibrils. J Mol Biol 2005; 352: 700-711.
69. Sasahara K, Naiki H, Goto Y. Exothermic effects observed upon heating of beta2-microglobulin monomers in the presence of amyloid seeds. Biochemistry 2006; 45: 8760-8769.
70. Li R, Woodward C. The hydrogen exchange core and protein folding. Protein Sci 1999; 8: 1571-1590.
71. Englander SW. Protein folding intermediates and pathways studied by hydrogen exchange. Annu Rev Biophys Biomol Struct 2000; 29: 213-238
72. Hoshino M, Katou H, Yamaguchi K, Goto Y. Dimethylsulfoxide-quenched hydrogen/deuterium exchange method to study amyloid fibril structure. Biochim Biophys Acta 2007; 1768: 1886-1899.
73. Hirota-Nakaoka N, Hasegawa K, Naiki H, Goto Y. Dissolution of beta2-microglobulin amyloid fibrils by dimethylsulfoxide. J Biochem (Tokyo) 2003; 134: 159-164.
74. van Rijswijk MH, Donker AJ, Ruinen L. Dimethylsulphoxide in amyloidosis. Lancet 1979; 1: 207-208.
75. Nurmi MJ, Ekfors TO, Rajala PO, Puntala PV. Intravesical dimethyl sulfoxide instillations in the treatment of secondary amyloidosis of the bladder. J Urol 1990; 143: 808-810.
76. Monti M, Principe S, Giorgetti S, Mangione P, Merlini G, Clark A, et al. Topological investigation of amyloid fibrils obtained from beta2-microglobulin. Protein Sci 2002; 11: 2362-2369.
77. Kheterpal I, Williams A, Murphy C, Bledsoe B, Wetzel R. Structural features of the Abeta amyloid fibril elucidated by limited proteolysis. Biochemistry 2001; 40: 11757-11767.
78. Kheterpal I, Lashuel HA, Hartley DM, Walz T, Lansbury PT, Jr., Wetzel R. Abeta protofibrils possess a stable core structure resistant to hydrogen exchange. Biochemistry 2003; 42: 14092-14098.
79. Carulla N, Caddy GL, Hall DR, Zurdo J, Gairi M, Feliz M, et al. Molecular recycling within amyloid fibrils. Nature 2005; 436: 554-558
80. Gosal WS, Morten IJ, Hewitt EW, Smith DA, Thomson NH, Radford SE. Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. J Mol Biol 2005; 351: 850-864.
81. Wadai H, Yamaguchi K, Takahashi S, Kanno T, Kawai T, Naiki H, et al. Stereospecific amyloid-like fibril formation by a peptide fragment of beta2-microglobulin. Biochemistry 2005; 44: 157-164.
82. Whittemore NA, Mishra R, Kheterpal I, Williams AD, Wetzel R, Serpersu EH. Hydrogen-deuterium (H/D) exchange mapping of Abeta 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy. Biochemistry 2005; 44: 4434-4441.
83. Olofsson A, Sauer-Eriksson AE, Ohman A. The solvent protection of alzheimer amyloid-beta-(1-42) fibrils as determined by solution NMR spectroscopy. J Biol Chem 2006; 281: 477-483.
84. Kuwata K, Matumoto T, Cheng H, Nagayama K, James TL, Roder H. NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126. Proc Natl Acad Sci USA 2003; 100: 14790-14795.
85. Toyama BH, Kelly MJ, Gross JD, Weissman JS. The structural basis of yeast prion strain variants. Nature 2007; 449: 233-237.
86. Ban T, Hamada D, Hasegawa K, Naiki H, Goto Y. Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. J Biol Chem 2003; 278: 16462-16465.
87. Ban T, Hoshino M, Takahashi S, Hamada D, Hasegawa K, Naiki H, et al. Direct observation of Abeta amyloid fibril growth and inhibition. J Mol Biol 2004; 344: 757-767.
88. Ban T, Morigaki K, Yagi H, Kawasaki T, Kobayashi A, Yuba S, et al. Real-time and single fibril observation of the formation of amyloid beta spherulitic structures. J Biol Chem 2006; 281: 33677-33683.
89. Ban T, Yamaguchi K, Goto Y. Direct observation of amyloid fibril growth, propagation, and adaptation. Acc Chem Res 2006; 39: 663-670.
90. Ban T, Goto Y. Direct observation of amyloid growth monitored by total internal reflection fluorescence microscopy. Methods Enzymol 2006; 413: 91-102.
91. Funatsu T, Harada Y, Tokunaga M, Saito K, Yanagida T. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 1995; 374: 555-559.
92. Yamasaki R, Hoshino M, Wazawa T, Ishii Y, Yanagida T, Kawata Y, et al. Single molecular observation of the interaction of GroEL with substrate proteins. J Mol Biol 1999; 292: 965-972.
93. Wazawa T, Ueda M. Total internal reflection fluorescence microscopy in single molecule nanobioscience. Adv Biochem Eng Biotechnol 2005; 95: 77-106.
94. Naiki H, Higuchi K, Hosokawa M, Takeda T. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal Biochem 1989; 177: 244-249.
95. Hoyer W, Cherny D, Subramaniam V, Jovin TM. Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy. J Mol Biol 2004; 340: 127-139.
96. Kowalewski T, Holtzman DM. In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: New insights into mechanism of beta-sheet formation. Proc Natl Acad Sci USA 1999; 96: 3688-3693.
97. Blackley HK, Sanders GH, Davies MC, Roberts CJ, Tendler SJ, Wilkinson MJ. In-situ atomic force microscopy study of beta-amyloid fibrillization. J Mol Biol 2000; 298: 833-840.
98. Zhu M, Souillac PO, Ionescu-Zanetti C, Carter SA, Fink AL. Surface-catalyzed amyloid fibril formation. J Biol Chem 2002; 277: 50914-50922.
99. Jin LW, Claborn KA, Kurimoto M, Geday MA, Maezawa I, Sohraby F, et al. Imaging linear birefringence and dichroism in cerebral amyloid pathologies. Proc Natl Acad Sci USA 2003; 100: 15294-15298.
100. Hsiao K, Chapman P, Nilsen S, Eckman C, Harigaya Y, Younkin S, et al. Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice. Science 1996; 274: 99-102.
101. Manuelidis L, Fritch W, Xi YG. Evolution of a strain of CJD that induces BSE-like plaques. Science 1997; 277: 94-98.
102. Harper JD, Lansbury PT, Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem 1997; 66: 385-407.
103. Krebs MR, Macphee CE, Miller AF, Dunlop IE, Dobson CM, Donald AM. The formation of spherulites by amyloid fibrils of bovine insulin. Proc Natl Acad Sci USA 2004; 101: 14420-14424.
104. Rogers SS, Krebs MR, Bromley EH, van der Linden E, Donald AM. Optical microscopy of growing insulin amyloid spherulites on surfaces in vitro. Biophys J 2006; 90: 1043-1054.
105. Raffen R, Dieckman LJ, Szpunar M, Wunschl C, Pokkuluri PR, Dave P, et al. Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains. Protein Sci 1999; 8: 509-517.
106. Sagis LM, Veerman C, van der Linden E. Mesoscopic properties of semiflexible amyloid fibrils. Langmuir 2004; 20: 924-927.
107. Fezoui Y, Hartley DM, Walsh DM, Selkoe DJ, Osterhout JJ, Teplow DB. A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils. Nat Struct Biol 2000; 7: 1095-1099.
108. Yagi H, Ban T, Morigaki K, Naiki H, Goto Y. Visualization and classification of amyloid beta supramolecular assemblies. Biochemistry 2007; 46: 15009-15017.
109. Sasahara K, Yagi H, Sakai M, Naiki H, Goto Y. Amyloid nucleation triggered by agitation of beta2-microglobulin under acidic and neutral pH conditions. Biochemistry 2008; 47: 2650-2660.
110. Chiti F, Bucciantini M, Capanni C, Taddei N, Dobson CM, Stefani M. Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain. Protein Sci 2001; 10: 2541-2547.
111. Li HT, Du HN, Tang L, Hu J, Hu HY. Structural transformation and aggregation of human alpha-synuclein in trifluoroethanol: Non-amyloid component sequence is essential and beta-sheet formation is prerequisite to aggregation. Biopolymers 2002; 64: 221-226.
112. Kanno T, Yamaguchi K, Naiki H, Goto Y, Kawai T. Association of thin filaments into thick filaments revealing the structural hierarchy of amyloid fibrils. J Struct Biol 2005; 149: 213-218.
113. Collinge J. Prion diseases of humans and animals: Their causes and molecular basis. Annu Rev Neurosci 2001; 24: 519-550.
114. Chien P, Weissman JS, DePace AH. Emerging principles of conformation-based prion inheritance. Annu Rev Biochem 2004; 73: 617-656.
115. Legname G, Baskakov IV, Nguyen HO, Riesner D, Cohen FE, DeArmond SJ, et al. Synthetic mammalian prions. Science 2004; 305: 673-676
116. Jones EM, Surewicz WK. Fibril conformation as the basis of species-and strain-dependent seeding specificity of mammalian prion amyloids. Cell 2005; 121: 63-72.
117. Tanaka M, Chien P, Yonekura K, Weissman JS. Mechanism of cross-species prion transmission: An infectious conformation compatible with two highly divergent yeast prion proteins. Cell 2005; 121: 49-62.
118. Nagai Y, Inui T, Popiel HA, Fujikake N, Hasegawa K, Urade Y, et al. A toxic monomeric conformer of the polyglutamine protein. Nat Struct Mol Biol 2007; 14: 332-340.
119. Dieterle F, Marrer E, Suzuki E, Grenet O, Cordier A, Vonderscher J. Monitoring kidney safety in drug development: Emerging technologies and their implications. Curr Opin Drug Discov Devel 2008; 11(1): 60-71.
120. Hintersteiner M, Auer M. Single-bead, single-molecule, single-cell fluorescence: Technologies for drug screening and target validation. Ann N Y Acad Sci 2008; 1130: 1-11.
121. Takeuchi M, Yamagishi S. Possible involvement of advanced glycation end-products (AGEs) in the pathogenesis of Alzheimer's disease. Curr Pharm Des 2008; 14(10): 973-8.