Mechanisms of amyloid fibril formation

Biochemistry (Moscow)

Volumn 79, Issue 13, 2014, Pages 1515-1527

  Dovidchenko, N V ^a   Leonova, E I ^a   Galzitskaya, O V ^a  

^a INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

Author keywords

aggregation kinetics; Alzheimer's disease; oligomer particles; prion; stress granules; thioflavin T

Indexed keywords

ARANEAE;

AMYLOID;

ALZHEIMER DISEASE; AMYLOIDOSIS; CHEMISTRY; CYSTIC FIBROSIS; HUMAN; HUNTINGTON DISEASE; PARKINSON DISEASE; PROTEIN CONFORMATION; PROTEIN FOLDING;

ALZHEIMER DISEASE; AMYLOID; AMYLOIDOSIS; CYSTIC FIBROSIS; HUMANS; HUNTINGTON DISEASE; PARKINSON DISEASE; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 84920559149     PISSN: 00062979     EISSN: 16083040     Source Type: Journal    
DOI: 10.1134/S0006297914130057     Document Type: Review

References (142)

1. Anfinsen, C. B. (1973) Principles that govern the folding of protein chains, Science, 181, 223-230.
2. Neumann, M., Rademakers, R., Roeber, S., Baker, M., Kretzschmar, H. A., and Mackenzie, I. R. A. (2009) A new subtype of frontotemporal lobar degeneration with FUS pathology, Brain J. Neurol., 132, 2922-2931.
3. Doi, H., Koyano, S., Suzuki, Y., Nukina, N., and Kuroiwa, Y. (2010) The RNA-binding protein FUS/TLS is a common aggregate-interacting protein in polyglutamine diseases, Neurosci. Res., 66, 131-133.
4. Kwiatkowski, T. J., Jr., Bosco, D. A., Leclerc, A. L., Tamrazian, E., Vanderburg, C. R., Russ, C., Davis, A., Gilchrist, J., Kasarskis, E. J., Munsat, T., Valdmanis, P., Rouleau, G. A., Hosler, B. A., Cortelli, P., de Jong, P. J., Yoshinaga, Y., Haines, J. L., Pericak-Vance, M. A., Yan, J., Ticozzi, N., Siddique, T., McKenna-Yasek, D., Sapp, P. C., Horvitz, H. R., Landers, J. E., and Brown, R. H., Jr. (2009) Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis, Science, 323, 1205-1208.
5. Vance, C., Rogelj, B., Hortobagyi, T., De Vos, K. J., Nishimura, A. L., Sreedharan, J., Hu, X., Smith, B., Ruddy, D., Wright, P., Ganesalingam, J., Williams, K. L., Tripathi, V., Al-Saraj, S., Al-Chalabi, A., Leigh, P. N., Blair, I. P., Nicholson, G., de Belleroche, J., Gallo, J.-M., Miller, C. C., and Shaw, C. E. (2009) Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6, Science, 323, 1208-1211.
6. Sunde, M., and Blake, C. (1997) The structure of amyloid fibrils by electron microscopy and X-ray diffraction, Adv. Protein Chem., 50, 123-159.
7. Perutz, M. F., Finch, J. T., Berriman, J., and Lesk, A. (2002) Amyloid fibers are water-filled nanotubes, Proc. Natl. Acad. Sci. USA, 99, 5591-5595.
8. Virchow, R. (1857) Neue beobacktungen uber amyloid degeneration, Virchows Arch. Pathol. Anat. Physiol., 11, 188-189.
9. Divry, P., and Florkin, M. (1927) Sur les proprietes optiques de l'amyloide, Comptes Rendus. Soc. Biol., 97, 1808-1810.
10. Pras, M., Schubert, M., Zucker-Franklin, D., Rimon, A., and Franklin, E. C. (1968) The characterization of soluble amyloid prepared in water, J. Clin. Invest., 47, 924-933.
11. Bennhold, H. (1923) Uber die Ausscheidung intravenous einverbleibten Kongorotes bei den verschiedensten Erkrankungen insbesondere bei amyloidosis, Dtsch. Arch. Klin. Med., 142, 32-46.
12. Ouchi, E., Nomura, N., Watabe, S., Seiji, K., and Sato, J. (1976) Clinical significance of Congo red test, Tohoku J. Exp. Med., 118, 191-198.
13. Linke, R. (2006) Congo red staining of amyloid: improvements and practical guide for a more precise diagnosis of amyloid and the different amyloidoses, in Protein Reviews, Vol. 4, Protein Misfolding, Aggregation and Conformational Diseases (Uversky, V., and Fink, A., eds.) Springer, pp. 239-276.
14. Groenning, M. (2010) Binding mode of thioflavin T and other molecular probes in the context of amyloid fibrils-current status, J. Chem. Biol., 3, 1-18.
15. Xu, H., He, X., Zheng, H., Huang, L. J., Hou, F., Yu, Z., de la Cruz, M. J., Borkowski, B., Zhang, X., Chen, Z. J., and Jiang, Q.-X. (2014) Structural basis for the prion-like MAVS filaments in antiviral innate immunity, eLife, 3, e01489.
16. Narkiewicz, J., Giachin, G., and Legname, G. (2014) In vitro aggregation assays for the characterization of α-synuclein prion-like properties, Prion, 8, 19-32.
17. Sydow, A., and Mandelkow, E.-M. (2010) "Prion-like" propagation of mouse and human τ aggregates in an inducible mouse model of tauopathy, Neurodegener. Dis., 7, 28-31.
18. Kato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., Grishin, N. V., Frantz, D. E., Schneider, J. W., Chen, S., Li, L., Sawaya, M. R., Eisenberg, D., Tycko, R., and McKnight, S. L. (2012) Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels, Cell, 149, 753-767.
19. Sulatskaya, A., and Kuznetsova, I. (2010) Interaction of thioflavin T with amyloid fibrils as an instrument for study their structure, Tsitologiya, 52, 955-959.
20. Biancalana, M., and Koide, S. (2010) Molecular mechanism of thioflavin T binding to amyloid fibrils, Biochim. Biophys. Acta, 1804, 1405-1412.
21. Gendoo, D. M. A., and Harrison, P. M. (2011) Origins and evolution of the HET-s prion-forming protein: searching for other amyloid-forming solenoids, PloS One, 6, e27342.
22. King, O. D., Gitler, A. D., and Shorter, J. (2012) The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease, Brain Res., 1462, 61-80.
23. Aguzzi, A., and Rajendran, L. (2009) The transcellular spread of cytosolic amyloids, prions, and prionoids, Neuron, 64, 783-790.
24. Prusiner, S. B., Scott, M. R., DeArmond, S. J., and Cohen, F. E. (1998) Prion protein biology, Cell, 93, 337-348.
25. Halfmann, R., Alberti, S., and Lindquist, S. (2010) Prions, protein homeostasis, and phenotypic diversity, Trends Cell Biol., 20, 125-133.
26. Hou, F., Sun, L., Zheng, H., Skaug, B., Jiang, Q.-X., and Chen, Z. J. (2011) MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response, Cell, 146, 448-461.
27. Bailey, C. H., Kandel, E. R., and Si, K. (2004) The persistence of long-term memory: a molecular approach to self-sustaining changes in learning-induced synaptic growth, Neuron, 44, 49-57.
28. Gilks, N., Kedersha, N., Ayodele, M., Shen, L., Stoecklin, G., Dember, L. M., and Anderson, P. (2004) Stress granule assembly is mediated by prion-like aggregation of TIA-1, Mol. Biol. Cell, 15, 5383-5398.
29. Shorter, J., and Lindquist, S. (2004) Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers, Science, 304, 1793-1797.
30. Halfmann, R., Alberti, S., Krishnan, R., Lyle, N., O'Donnell, C. W., King, O. D., Berger, B., Pappu, R. V., and Lindquist, S. (2011) Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins, Mol. Cell, 43, 72-84.
31. Han, T. W., Kato, M., Xie, S., Wu, L. C., Mirzaei, H., Pei, J., Chen, M., Xie, Y., Allen, J., Xiao, G., and McKnight, S. L. (2012) Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies, Cell, 149, 768-779.
32. Sun, Z., Diaz, Z., Fang, X., Hart, M. P., Chesi, A., Shorter, J., and Gitler, A. D. (2011) Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS, PLoS Biol., 9, e1000614.
33. Wickner, R. B., Taylor, K. L., Edskes, H. K., and Maddelein, M. L. (2000) Prions: portable prion domains, Curr. Biol. CB, 10, 335-337.
34. Li, L., and Lindquist, S. (2000) Creating a protein-based element of inheritance, Science, 287, 661-664.
35. Kaiser, T. E., Intine, R. V., and Dundr, M. (2008) De novo formation of a subnuclear body, Science, 322, 1713-1717.
36. Shevtsov, S. P., and Dundr, M. (2011) Nucleation of nuclear bodies by RNA, Nat. Cell Biol., 13, 167-173.
37. Li, Y. R., King, O. D., Shorter, J., and Gitler, A. D. (2013) Stress granules as crucibles of ALS pathogenesis, J. Cell Biol., 201, 361-372.
38. Cushman, M., Johnson, B. S., King, O. D., Gitler, A. D., and Shorter, J. (2010) Prion-like disorders: blurring the divide between transmissibility and infectivity, J. Cell Sci., 123, 1191-1201.
39. Frost, B., and Diamond, M. I. (2010) Prion-like mechanisms in neurodegenerative diseases, Nat. Rev. Neurosci., 11, 155-159.
40. Braak, H., Rub, U., Gai, W. P., and Del Tredici, K. (2003) Idiopathic Parkinson's disease: possible routes by which vulnerable neuronal types may be subject to neuroinvasion by an unknown pathogen, J. Neural Transm., 110, 517-536.
41. Ravits, J. M., and La Spada, A. R. (2009) ALS motor phenotype heterogeneity, focality, and spread: deconstructing motor neuron degeneration, Neurology, 73, 805-811.
42. Selkoe, D. J. (1999) Translating cell biology into therapeutic advances in Alzheimer's disease, Nature, 399, 23-31.
43. Alberti, S., Halfmann, R., King, O., Kapila, A., and Lindquist, S. (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins, Cell, 137, 146-158.
44. Dormann, D., Rodde, R., Edbauer, D., Bentmann, E., Fischer, I., Hruscha, A., Than, M. E., Mackenzie, I. R. A., Capell, A., Schmid, B., Neumann, M., and Haass, C. (2010) ALS-associated fused in sarcoma (FUS) mutations disrupt transportin-mediated nuclear import, EMBO J., 29, 2841-2857.
45. Gal, J., Zhang, J., Kwinter, D. M., Zhai, J., Jia, H., Jia, J., and Zhu, H. (2011) Nuclear localization sequence of FUS and induction of stress granules by ALS mutants, Neurobiol. Aging, 32, 27-40.
46. Ito, D., Seki, M., Tsunoda, Y., Uchiyama, H., and Suzuki, N. (2011) Nuclear transport impairment of amyotrophic lateral sclerosis-linked mutations in FUS/TLS, Ann. Neurol., 69, 152-162.
47. Kino, Y., Washizu, C., Aquilanti, E., Okuno, M., Kurosawa, M., Yamada, M., Doi, H., and Nukina, N. (2011) Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations, Nucleic Acids Res., 39, 2781-2798.
48. Niu, C., Zhang, J., Gao, F., Yang, L., Jia, M., Zhu, H., and Gong, W. (2012) FUS-NLS/transportin 1 complex structure provides insights into the nuclear targeting mechanism of FUS and the implications in ALS, PloS One, 7, e47056.
49. Zhang, Z. C., and Chook, Y. M. (2012) Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the fused in sarcoma protein (FUS), Proc. Natl. Acad. Sci. USA, 109, 12017-12021.
50. Seyfried, N. T., Gozal, Y. M., Donovan, L. E., Herskowitz, J. H., Dammer, E. B., Xia, Q., Ku, L., Chang, J., Duong, D. M., Rees, H. D., Cooper, D. S., Glass, J. D., Gearing, M., Tansey, M. G., Lah, J. J., Feng, Y., Levey, A. I., and Peng, J. (2012) Quantitative analysis of the detergent-insoluble brain proteome in frontotemporal lobar degeneration using SILAC internal standards, J. Proteome Res., 11, 2721-2738.
51. Klar, J., Sobol, M., Melberg, A., Mabert, K., Ameur, A., Johansson, A. C. V., Feuk, L., Entesarian, M., Orlen, H., Casar-Borota, O., and Dahl, N. (2013) Welander distal myopathy caused by an ancient founder mutation in TIA1 associated with perturbed splicing, Hum. Mutat., 34, 572-577.
52. Sawaya, M. R., Sambashivan, S., Nelson, R., Ivanova, M. I., Sievers, S. A., Apostol, M. I., Thompson, M. J., Balbirnie, M., Wiltzius, J. J. W., McFarlane, H. T., Madsen, A. O., Riekel, C., and Eisenberg, D. (2007) Atomic structures of amyloid cross-β spines reveal varied steric zippers, Nature, 447, 453-457.
53. Chapman, M. R., Robinson, L. S., Pinkner, J. S., Roth, R., Heuser, J., Hammar, M., Normark, S., and Hultgren, S. J. (2002) Role of Escherichia coli curli operons in directing amyloid fiber formation, Science, 295, 851-855.
54. Claessen, D., Rink, R., de Jong, W., Siebring, J., de Vreugd, P., Boersma, F. G. H., Dijkhuizen, L., and Wosten, H. A. B. (2003) A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils, Genes Dev., 17, 1714-1726.
55. Berson, J. F., Theos, A. C., Harper, D. C., Tenza, D., Raposo, G., and Marks, M. S. (2003) Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis, J. Cell Biol., 161, 521-533.
56. Tompa, P., and Friedrich, P. (1998) Prion proteins as memory molecules: an hypothesis, Neuroscience, 86, 1037-1043.
57. Onoguchi, K., Onomoto, K., Takamatsu, S., Jogi, M., Takemura, A., Morimoto, S., Julkunen, I., Namiki, H., Yoneyama, M., and Fujita, T. (2010) Virus-infection or 5'ppp-RNA activates antiviral signal through redistribution of IPS-1 mediated by MFN1, PloS Pathog., 6, e1001012.
58. Jacobs, J. L., and Coyne, C. B. (2013) Mechanisms of MAVS regulation at the mitochondrial membrane, J. Mol. Biol., 425, 5009-5019.
59. Glenner, G. G., Ein, D., Eanes, E. D., Bladen, H. A., Terry, W., and Page, D. L. (1971) Creation of "amyloid" fibrils from Bence Jones proteins in vitro, Science, 174, 712-714.
60. Levin, M., Franklin, E. C., Frangione, B., and Pras, M. (1972) The amino acid sequence of a major non-immunoglobulin component of some amyloid fibrils, J. Clin. Invest., 51, 2773-2776.
61. Glenner, G. G., Terry, W., Harada, M., Isersky, C., and Page, D. (1971) Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses, Science, 172, 1150-1151.
62. Terry, W. D., Page, D. L., Kimura, S., Isobe, T., Osserman, E. F., and Glenner, G. G. (1973) Structural identity of Bence-Jones and amyloid fibril proteins in a patient with plasma cell dyscrasia and amyloidosis, J. Clin. Invest., 52, 1276-1281.
63. Buxbaum, J. (1992) Mechanisms of disease: monoclonal immunoglobulin deposition. Amyloidosis, light chain deposition disease, and light and heavy chain deposition disease, Hematol. Oncol. Clin. North Am., 6, 323-346.
64. Buxbaum, J. (1986) Aberrant immunoglobulin synthesis in light chain amyloidosis. Free light chain and light chain fragment production by human bone marrow cells in short-term tissue culture, J. Clin. Invest., 78, 798-806.
65. Linke, R. P., Zucker-Franklin, D., and Franklin, E. D. (1973) Morphologic, chemical, and immunologic studies of amyloid-like fibrils formed from Bence-Jones proteins by proteolysis, J. Immunol. Baltim. Md 1950, 111, 10-23.
66. Stevens, F. J. (2000) Four structural risk factors identify most fibril-forming κ light chains, Amyloid Int. J. Exp. Clin. Investig. Off. J. Int. Soc. Amyloidosis, 7, 200-211.
67. Hurle, M. R., Helms, L. R., Li, L., Chan, W., and Wetzel, R. (1994) A role for destabilizing amino acid replacements in light-chain amyloidosis, Proc. Natl. Acad. Sci. USA, 91, 5446-5450.
68. Kaplan, B., Vidal, R., Kumar, A., Ghiso, J., Frangione, B., and Gallo, G. (1997) Amino-terminal identity of co-existent amyloid and non-amyloid immunoglobulin κ light chain deposits. A human disease to study alterations of protein conformation, Clin. Exp. Immunol., 110, 472-478.
69. Putnam, F. W., Easley, C. W., Lynn, L. T., Ritchie, A. E., and Phelps, R. A. (1959) The heat precipitation of Bence-Jones proteins. I. Optimum conditions, Arch. Biochem. Biophys., 83, 115-130.
70. Solomon, A., Weiss, D. T., and Kattine, A. A. (1991) Nephrotoxic potential of Bence-Jones proteins, N. Engl. J. Med., 324, 1845-1851.
71. Eulitz, M., Weiss, D. T., and Solomon, A. (1990) Immunoglobulin heavy-chain-associated amyloidosis, Proc. Natl. Acad. Sci. USA, 87, 6542-6546.
72. Benditt, E. P., Eriksen, N., Hermodson, M. A., and Ericsson, L. H. (1971) The major proteins of human and monkey amyloid substance: common properties including unusual N-terminal amino acid sequences, FEBS Lett., 19, 169-173.
73. Sletten, K., and Husby, G. (1974) The complete amino-acid sequence of non-immunoglobulin amyloid fibril protein AS in rheumatoid arthritis, Eur. J. Biochem. FEBS, 41, 117-125.
74. Manley, P. N., Ancsin, J. B., and Kisilevsky, R. (2006) Rapid recycling of cholesterol: the joint biologic role of C-reactive protein and serum amyloid A, Med. Hypotheses, 66, 784-792.
75. Chapman, M. R., Robinson, L. S., Pinkner, J. S., Roth, R., Heuser, J., Hammar, M., Normark, S., and Hultgren, S. J. (2002) Role of Escherichia coli curli operons in directing amyloid fiber formation, Science, 295, 851-855.
76. Rocken, C., and Shakespeare, A. (2002) Pathology, diagnosis and pathogenesis of AA amyloidosis, Virchows Arch. Int. J. Pathol., 440, 111-122.
77. Skinner, M., and Cohen, A. S. (1988) Amyloid P component, Methods Enzymol., 163, 523-536.
78. Ancsin, J. B. (2003) Amyloidogenesis: historical and modern observations point to heparan sulfate proteoglycans as a major culprit, Amyloid Int. J. Exp. Clin. Investig. Off. J. Int. Soc. Amyloidosis, 10, 67-79.
79. Gallo, G., Wisniewski, T., Choi-Miura, N. H., Ghiso, J., and Frangione, B. (1994) Potential role of apolipoprotein-E in fibrillogenesis, Am. J. Pathol., 145, 526-530.
80. Tennent, G. A., Lovat, L. B., and Pepys, M. B. (1995) Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis, Proc. Natl. Acad. Sci. USA, 92, 4299-4303.
81. Husby, G., and Natvig, J. B. (1974) A serum component related to nonimmunoglobulin amyloid protein AS, a possible precursor of the fibrils, J. Clin. Invest., 53, 1054-1061.
82. Husby, G., Husebekk, A., Skogen, B., Sletten, K., Marhaug, G., Magnus, J., and Syversen, V. (1988) Serum amyloid A (SAA) - the precursor of protein AA in secondary amyloidosis, Adv. Exp. Med. Biol., 243, 185-192.
83. Westermark, P., Wernstedt, C., Wilander, E., Hayden, D. W., O'Brien, T. D., and Johnson, K. H. (1987) Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells, Proc. Natl. Acad. Sci. USA, 84, 3881-3885.
84. Masters, C. L., Multhaup, G., Simms, G., Pottgiesser, J., Martins, R. N., and Beyreuther, K. (1985) Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels, EMBO J., 4, 2757-2763.
85. Oesch, B., Westaway, D., Walchli, M., McKinley, M. P., Kent, S. B., Aebersold, R., Barry, R. A., Tempst, P., Teplow, D. B., and Hood, L. E. (1985) A cellular gene encodes scrapie PrP 27-30 protein, Cell, 40, 735-746.
86. Vidal, R., Frangione, B., Rostagno, A., Mead, S., Revesz, T., Plant, G., and Ghiso, J. (1999) A stop-codon mutation in the BRI gene associated with familial British dementia, Nature, 399, 776-781.
87. Glenner, G. G. (1980) Amyloid deposits and amyloidosis. The β-fibrilloses (first of two parts), N. Engl. J. Med., 302, 1283-1292.
88. Glenner, G. G., and Wong, C. W. (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein, Biochem. Biophys. Res. Commun., 120, 885-890.
89. Gruys, E., and Snel, F. W. (1994) Animal models for reactive amyloidosis, Baillieres Clin. Rheumatol., 8, 599-611.
90. Solomon, A., Weiss, D. T., Schell, M., Hrncic, R., Murphy, C. L., Wall, J., McGavin, M. D., Pan, H. J., Kabalka, G. W., and Paulus, M. J. (1999) Transgenic mouse model of AA amyloidosis, Am. J. Pathol., 154, 1267-1272.
91. Liu, Y., Cui, D., Hoshii, Y., Kawano, H., Une, Y., Gondo, T., and Ishihara, T. (2007) Induction of murine AA amyloidosis by various homogeneous amyloid fibrils and amyloid-like synthetic peptides, Scand. J. Immunol., 66, 495-500.
92. Johan, K., Westermark, G., Engstrom, U., Gustavsson, A., Hultman, P., and Westermark, P. (1998) Acceleration of amyloid protein A amyloidosis by amyloid-like synthetic fibrils, Proc. Natl. Acad. Sci. USA, 95, 2558-2563.
93. Lundmark, K., Westermark, G. T., Olsen, A., and Westermark, P. (2005) Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: cross-seeding as a disease mechanism, Proc. Natl. Acad. Sci. USA, 102, 6098-6102.
94. Korenaga, T., Fu, X., Xing, Y., Matsusita, T., Kuramoto, K., Syumiya, S., Hasegawa, K., Naiki, H., Ueno, M., Ishihara, T., Hosokawa, M., Mori, M., and Higuchi, K. (2004) Tissue distribution, biochemical properties, and transmission of mouse type A AApoAII amyloid fibrils, Am. J. Pathol., 164, 1597-1606.
95. Xing, Y., Nakamura, A., Chiba, T., Kogishi, K., Matsushita, T., Li, F., Guo, Z., Hosokawa, M., Mori, M., and Higuchi, K. (2001) Transmission of mouse senile amyloidosis, Lab. Invest., 81, 493-499.
96. Elliott-Bryant, R., and Cathcart, E. S. (1998) Amyloid enhancing factor and dietary transmission in accelerated amyloid A amyloidosis, Clin. Immunol. Immunopathol., 88, 65-69.
97. Yan, J., Fu, X., Ge, F., Zhang, B., Yao, J., Zhang, H., Qian, J., Tomozawa, H., Naiki, H., Sawashita, J., Mori, M., and Higuchi, K. (2007) Cross-seeding and cross-competition in mouse apolipoprotein A-II amyloid fibrils and protein A amyloid fibrils, Am. J. Pathol., 171, 172-180.
98. Bales, K. R., Verina, T., Dodel, R. C., Du, Y., Altstiel, L., Bender, M., Hyslop, P., Johnstone, E. M., Little, S. P., Cummins, D. J., Piccardo, P., Ghetti, B., and Paul, S. M. (1997) Lack of apolipoprotein E dramatically reduces amyloid β-peptide deposition, Nat. Genet., 17, 263-264.
99. Wisniewski, T., Castano, E. M., Golabek, A., Vogel, T., and Frangione, B. (1994) Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro, Am. J. Pathol., 145, 1030-1035.
100. Holtzman, D. M. (2004) In vivo effects of ApoE and clusterin on amyloid-β metabolism and neuropathology, J. Mol. Neurosci. MN, 23, 247-254.
101. Vidal, J., Verchere, C. B., Andrikopoulos, S., Wang, F., Hull, R. L., Cnop, M., Olin, K. L., LeBoeuf, R. C., O'Brien, K. D., Chait, A., and Kahn, S. E. (2003) The effect of apolipoprotein E deficiency on islet amyloid deposition in human islet amyloid polypeptide transgenic mice, Diabetologia, 46, 71-79.
102. Kindy, M. S., and Rader, D. J. (1998) Reduction in amyloid A amyloid formation in apolipoprotein-E-deficient mice, Am. J. Pathol., 152, 1387-1395.
103. Elliott-Bryant, R., and Cathcart, E. S. (1997) Apolipoprotein E and apolipoprotein A-1 knock-out mice readily develop amyloid A protein amyloidosis, Clin. Immunol. Immunopathol., 85, 104-108.
104. Botto, M., Hawkins, P. N., Bickerstaff, M. C., Herbert, J., Bygrave, A. E., McBride, A., Hutchinson, W. L., Tennent, G. A., Walport, M. J., and Pepys, M. B. (1997) Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene, Nat. Med., 3, 855-859.
105. Togashi, S., Lim, S. K., Kawano, H., Ito, S., Ishihara, T., Okada, Y., Nakano, S., Kinoshita, T., Horie, K., Episkopou, V., Gottesman, M. E., Costantini, F., Shimada, K., and Maeda, S. (1997) Serum amyloid P component enhances induction of murine amyloidosis, Lab. Investig. J. Tech. Methods Pathol., 77, 525-531.
106. Castillo, G. M., Lukito, W., Wight, T. N., and Snow, A. D. (1999) The sulfate moieties of glycosaminoglycans are critical for the enhancement of β-amyloid protein fibril formation, J. Neurochem., 72, 1681-1687.
107. Li, J.-P., Galvis, M. L. E., Gong, F., Zhang, X., Zcharia, E., Metzger, S., Vlodavsky, I., Kisilevsky, R., and Lindahl, U. (2005) In vivo fragmentation of heparan sulfate by heparanase overexpression renders mice resistant to amyloid protein A amyloidosis, Proc. Natl. Acad. Sci. USA, 102, 6473-6477.
108. Ailles, L., Kisilevsky, R., and Young, I. D. (1993) Induction of perlecan gene expression precedes amyloid formation during experimental murine AA amyloidogenesis, Lab. Investig. J. Tech. Methods Pathol., 69, 443-448.
109. Elimova, E., Kisilevsky, R., Szarek, W. A., and Ancsin, J. B. (2004) Amyloidogenesis recapitulated in cell culture: a peptide inhibitor provides direct evidence for the role of heparan sulfate and suggests a new treatment strategy, FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol., 18, 1749-1751.
110. Lundmark, K., Westermark, G. T., Nystrom, S., Murphy, C. L., Solomon, A., and Westermark, P. (2002) Transmissibility of systemic amyloidosis by a prion-like mechanism, Proc. Natl. Acad. Sci. USA, 99, 6979-6984.
111. Solomon, I. H., Schepker, J. A., and Harris, D. A. (2010) Prion neurotoxicity: insights from prion protein mutants, Curr. Issues Mol. Biol., 12, 51-61.
112. Sandberg, M. K., Al-Doujaily, H., Sharps, B., Clarke, A. R., and Collinge, J. (2011) Prion propagation and toxicity in vivo occur in two distinct mechanistic phases, Nature, 470, 540-542.
113. Dovidchenko, N. V., Finkelstein, A. V., and Galzitskaya, O. V. (2014) How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. I. Modeling the amyloid protofibril formation, J. Phys. Chem. B, 118, 1189-1197.
114. Chayen, N. E. (2005) Methods for separating nucleation and growth in protein crystallization, Prog. Biophys. Mol. Biol., 88, 329-337.
115. Naiki, H., Hashimoto, N., Suzuki, S., Kimura, H., Nakakuki, K., and Gejyo, F. (1997) Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro, Amyloid, 4, 223-232.
116. Serio, T. R., Cashikar, A. G., Kowal, A. S., Sawicki, G. J., Moslehi, J. J., Serpell, L., Arnsdorf, M. F., and Lindquist, S. L. (2000) Nucleated conformational conversion and the replication of conformational information by a prion determinant, Science, 289, 1317-1321.
117. Uversky, V. N., Li, J., Souillac, P., Millett, I. S., Doniach, S., Jakes, R., Goedert, M., and Fink, A. L. (2002) Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of α-synuclein assembly by β- and γ-synucleins, J. Biol. Chem., 277, 11970-11978.
118. Pedersen, J. S., Christensen, G., and Otzen, D. E. (2004) Modulation of S6 fibrillation by unfolding rates and gatekeeper residues, J. Mol. Biol., 341, 575-588.
119. Fezoui, Y., and Teplow, D. B. (2002) Kinetic studies of amyloid β-protein fibril assembly. Differential effects of α-helix stabilization, J. Biol. Chem., 277, 36948-36954.
120. Tanaka, M., Chien, P., Yonekura, K., and Weissman, J. S. (2005) Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins, Cell, 121, 49-62.
121. Wright, C. F., Teichmann, S. A., Clarke, J., and Dobson, C. M. (2005) The importance of sequence diversity in the aggregation and evolution of proteins, Nature, 438, 878-881.
122. Krebs, M. R. H., Morozova-Roche, L. A., Daniel, K., Robinson, C. V., and Dobson, C. M. (2004) Observation of sequence specificity in the seeding of protein amyloid fibrils, Protein Sci. Publ. Protein Soc., 13, 1933-1938.
123. Harper, J. D., Lieber, C. M., and Lansbury, P. T., Jr. (1997) Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein, Chem. Biol., 4, 951-959.
124. Harper, J. D., Wong, S. S., Lieber, C. M., and Lansbury, P. T. (1997) Observation of metastable Abeta amyloid protofibrils by atomic force microscopy, Chem. Biol., 4, 119-125.
125. Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., and Teplow, D. B. (1997) Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate, J. Biol. Chem., 272, 22364-22372.
126. Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., and Teplow, D. B. (1999) Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates, J. Biol. Chem., 274, 25945-25952.
127. Conway, K. A., Harper, J. D., and Lansbury, P. T., Jr. (2000) Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid, Biochemistry, 39, 2552-2563.
128. Kayed, R., Sokolov, Y., Edmonds, B., McIntire, T. M., Milton, S. C., Hall, J. E., and Glabe, C. G. (2004) Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases, J. Biol. Chem., 279, 46363-46366.
129. Ionescu-Zanetti, C., Khurana, R., Gillespie, J. R., Petrick, J. S., Trabachino, L. C., Minert, L. J., Carter, S. A., and Fink, A. L. (1999) Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy, Proc. Natl. Acad. Sci. USA, 96, 13175-13179.
130. Quintas, A., Vaz, D. C., Cardoso, I., Saraiva, M. J., and Brito, R. M. (2001) Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants, J. Biol. Chem., 276, 27207-27213.
131. Gosal, W. S., Morten, I. J., Hewitt, E. W., Smith, D. A., Thomson, N. H., and Radford, S. E. (2005) Competing pathways determine fibril morphology in the self-assembly of β2-microglobulin into amyloid, J. Mol. Biol., 351, 850-864.
132. Malisauskas, M., Zamotin, V., Jass, J., Noppe, W., Dobson, C. M., and Morozova-Roche, L. A. (2003) Amyloid protofilaments from the calcium-binding protein equine lysozyme: formation of ring and linear structures depends on pH and metal ion concentration, J. Mol. Biol., 330, 879-890.
133. Plakoutsi, G., Taddei, N., Stefani, M., and Chiti, F. (2004) Aggregation of the acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation, J. Biol. Chem., 279, 14111-14119.
134. Bader, R., Bamford, R., Zurdo, J., Luisi, B. F., and Dobson, C. M. (2006) Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation, J. Mol. Biol., 356, 189-208.
135. Morozova-Roche, L. A., Zamotin, V., Malisauskas, M., Ohman, A., Chertkova, R., Lavrikova, M. A., Kostanyan, I. A., Dolgikh, D. A., and Kirpichnikov, M. P. (2004) Fibrillation of carrier protein albebetin and its biologically active constructs. Multiple oligomeric intermediates and pathways, Biochemistry, 43, 9610-9619.
136. Petty, S. A., Adalsteinsson, T., and Decatur, S. M. (2005) Correlations among morphology, β-sheet stability, and molecular structure in prion peptide aggregates, Biochemistry, 44, 4720-4726.
137. Petty, S. A., and Decatur, S. M. (2005) Inter-sheet rearrangement of polypeptides during nucleation of β-sheet aggregates, Proc. Natl. Acad. Sci. USA, 102, 14272-14277.
138. Bitan, G., Kirkitadze, M. D., Lomakin, A., Vollers, S. S., Benedek, G. B., and Teplow, D. B. (2003) Amyloid β-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways, Proc. Natl. Acad. Sci. USA, 100, 330-335.
139. Roher, A. E., Chaney, M. O., Kuo, Y. M., Webster, S. D., Stine, W. B., Haverkamp, L. J., Woods, A. S., Cotter, R. J., Tuohy, J. M., Krafft, G. A., Bonnell, B. S., and Emmerling, M. R. (1996) Morphology and toxicity of Abeta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease, J. Biol. Chem., 271, 20631-20635.
140. Podlisny, M. B., Ostaszewski, B. L., Squazzo, S. L., Koo, E. H., Rydell, R. E., Teplow, D. B., and Selkoe, D. J. (1995) Aggregation of secreted amyloid β-protein into sodium dodecyl sulfate-stable oligomers in cell culture, J. Biol. Chem., 270, 9564-9570.
141. Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B., and Selkoe, D. J. (2000) The oligomerization of amyloid β-protein begins intracellularly in cells derived from human brain, Biochemistry, 39, 10831-10839.
142. Modler, A. J., Gast, K., Lutsch, G., and Damaschun, G. (2003) Assembly of amyloid protofibrils via critical oligomers - a novel pathway of amyloid formation, J. Mol. Biol., 325, 135-148.