References
- Pepys M. Pathogenesis, diagnosis and treatment of systemic amyloidosis. Phil Trans Soc Lond B 2001; 356:203 - 211
- Fowler DM, Koulov AV, Alory-Jost C, et al. Functional amyloid formation within mammalian tissue. PLoS Biol 2006; 4:6
- Friedrich NaK A. Zur amyloidfrage. Arch Pathol Anat Physiol Klin Med 1859; 16:50 - 65
- Divry P, Florkin M. Sur les proprietes optiques de l'amyloid. Societe de Biologie 1927; 97:180 - 181
- Cohen AS, Calkins E. Electron microscopic observation on a fibrous component in amyloid of diverse origins. Nature 1959; 183:1202 - 1203
- Cohen AS, Calkins E. The isolation of amyloid fibrils and a study of the effect of collagenase and hyaluronidase. J Cell Biol 1964; 21:481 - 486
- Eanes ED, Glenner GG. X-ray diffraction studies on amyloid filaments. J Histochem Cytochem 1968; 16:673 - 677
- Glenner G, Ein D, Eanes E, et al. Creation of “Amyloid” Fibrils from Bence Jones Proteins. Science 1971; 174:712 - 714
- Sunde M, Serpell L, Bartlam M, et al. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J Mol Biol 1997; 273:729 - 739
- Glenner GG, Terry W, Harada M, et al. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. Science 1971; 172:1150 - 1151
- Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136 - 144
- Glenner GG, Wong CW. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 1984; 120:885 - 890
- Botto M, Hawkins PN, Bickerstaff MC, et al. Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene. Nat Med 1997; 3:855 - 859
- Hawkins PN, Myers MJ, Lavender JP, et al. Diagnostic radionuclide imaging of amyloid: biological targeting by circulating human serum amyloid P component. Lancet 1988; 1:1413 - 1418
- La Spada AR, Wilson EM, Lubahn DB, et al. Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature 1991; 352:77 - 79
- Colon W, Kelly JW. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 1992; 31:8654 - 8660
- Serpell L. Alzheimer's amyloid fibrils: structure and assembly. Biochim Biophys Acta 2000; 1502:16 - 30
- McParland VJ, Kad NM, Kalverda AP, et al. Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro. Biochemistry 2000; 39:8735 - 8746
- Jahn TR, Parker MJ, Homans SW, et al. Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat Struct Mol Biol 2006; 13:195 - 201
- Eakin CM, Berman AJ, Miranker AD. A native to amyloidogenic transition regulated by a backbone trigger. Nat Struct Mol Biol 2006; 13:202 - 208
- Come J, Fraser P, Lansbury PJ. A Kinetic Model for Amyloid Formation In the Prion Diseases, Importance of Seeding. PNAS USA 1993; 90:5959 - 5963
- Lomakin A, Chung DS, Benedek GB, et al. On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants. Proc Natl Acad Sci USA 1996; 93:1125 - 1129
- Walsh DM, Hartley DM, Kusumoto Y, et al. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J Biol Chem 1999; 274:25945 - 25952
- Ding TT, Harper JD. Wetzel R. Analysis of amyloid-beta assemblies using tapping mode atomic force microscopy under ambient conditions. Methods in Enzymology: Amyloid, prions and other protein aggregates. Vol 309 1999; Academic press 510 - 525
- Roher AE, Baudry J, Chaney MO, et al. Oligomerizaiton and fibril asssembly of the amyloid-beta protein. Biochim Biophys Acta 2000; 1502:31 - 43
- Harper JD, Wong SS, Lieber CM, et al. Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer‘s disease. Biochemistry 1999; 38:8972 - 8980
- Podlisny MB, Ostaszewski BL, Squazzo SL, et al. Aggregation of secreted amyloid beta-protein into sodium dodecyl sulfate-stable oligomers in cell culture. J Biol Chem 1995; 270:9564 - 9570
- Lambert MP, Barlow AK, Chromy BA, et al. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA 1998; 95:6448 - 6453
- Harper JD, Wong SS, Lieber CM, et al. Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chem Biol 1997; 4:119 - 125
- Perutz M, Johnson T, Suzuki M, et al. Glutamine Repeats as Polar Zippers: Their Possible Role in Inherited Neurodegenerative Diseases. PNAS USA 1994; 91:5355 - 5358
- Schlunegger MP, Bennett MJ, Eisenberg D. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv Protein Chem 1997; 50:61 - 122
- Staniforth RA, Giannini S, Higgins LD, et al. Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. Embo J 2001; 20:4774 - 4781
- Dobson CM. Protein folding and misfolding. Nature 2003; 426:884 - 890
- Malisauskas M, Zamotin V, Jass J, et al. 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 2003; 330:879 - 890
- Bemporad F, Taddei N, Stefani M, et al. Assessing the role of aromatic residues in the amyloid aggregation of human muscle acyphophatase. Protein Science 2006; 15:862 - 870
- De la Paz M, Serrano L. Sequence deteminants of amyloid fibril formation. Proc Natl Acad Sci USA 2004; 101:87 - 92
- DuBay KF, Pawar AP, Chiti F, et al. Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. J Mol Biol 2004; 341:1317 - 1326
- Pawar AP, Dubay KF, Zurdo J, et al. Prediction of “aggregation-prone” and “aggregation-susceptible” regions in proteins associated with neurodegenerative disease. J Mol Biol 2005; 350:379 - 392
- Zibaee S, Makin OS, Goedert M, et al. A simple algorithm locates beta-strands in the amyloid fibril core of alpha-synuclein, Abeta and tau using the amino acid sequence alone. Protein Sci 2007; 16:906 - 918
- Fernandez-Escamilla AM, Rousseau F, Schymkowitz J, et al. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat Biotechnol 2004; 22:1302 - 1306
- Makin OS, Sikorski P, Serpell LC. Diffraction to study protein and peptide assemblies. Curr Opin Chem Biol 2006; 10:417 - 422
- Tycko R. Insights into the amyloid folding problem from solid-state NMR. Biochemistry 2003; 42:3151 - 3159
- Der-Sarkissian A, Jao CC, Chen J, et al. Structural organisation of alpha-synuclein studied by site-directed spin labelling. J Biol Chem 2003; 278:37530 - 37535
- Jayasinghe SA, Langen R. Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling. J Biol Chem 2004; 279:48420 - 48425
- Torok M, Milton S, Kayed R, et al. Structural and dynamic features of Alzheimer's Abeta peptide in amyloid fibrils studied by site-directed spin labelling. J Biol Chem 2002; 277:40810 - 40815
- Goldsbury C, Kistler J, Aebi U, et al. Watching amyloid fibrils grow by time-lapse atomic force microscopy. J Mol Biol 1999; 285:33 - 39
- Serpell L, Sunde M, Benson M, et al. The protofilament substructure of amyloid fibrils. J Mol Biol 2000; 300:1033 - 1039
- Jimenez JL, Guijarro JI, Orlova E, et al. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J 1999; 18:815 - 821
- Jimenez JL, Tennent G, Pepys MB, et al. Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy. J Mol Biol 2001; 311:241 - 247
- Jimenez JL, Nettleton EJ, Bouchard M, et al. The protofilament structure of insulin amyloid fibrils. Proc Natl Acad Sci USA 2002; 99:9196 - 9201
- Goldsbury C, Kistler J, Aebi U, et al. Watching amyloid fibrils grow by time-lapse atomic force microscopy. J Mol Biol 1999; 285:33 - 39
- Sachse C, Xu C, Wieligmann K, et al. Quaternary structure of a mature amyloid fibril from Alzheimer's Abeta(1–40) peptide. J Mol Biol 2006; 362:347 - 354
- Blake C, Serpell L. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous b-helix. Structure 1996; 4:989 - 998
- Inouye H, Fraser P, Kirschner D. Structure of β-Crystallite Assemblies by Alzheimer Amyloid Protein Analogues: Analysis by X-Ray Diffraction. Biophys J 1993; 64:502 - 519
- Geddes AJ, Parker KD, Atkins EDT, et al. “Cross β” Conformation in Protein. J Mol Biol 1968; 32:343 - 358
- Makin OS, Sikorski P, Serpell LC. Diffraction to study protein and peptide assemblies. Curr Opin Chem Biol 2006; 10:417 - 422
- Makin OS, Atkins E, Sikorski P, et al. Molecular basis for amyloid fibril formation and stability. Proc Natl Acad Sci USA 2005; 102:315 - 320
- Makin OS, Serpell LC. Structures for amyloid fibrils. FEBS J 2005; 272:5950 - 5961
- Nelson R, Eisenberg D. Recent atomic models of amyloid fibril structure. Curr Opin Struct Biol 2006; 16:260 - 265
- Sawaya MR, Sambashivan S, Nelson R, et al. Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 2007; 447:453 - 457
- Tycko R. Progress towards a molecular-level structural understanding of amyloid fibrils. Curr Opin Struct Biol 2004; 14:96 - 103
- Naito A, Kamihira M, Inoue R, et al. 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
- Gordon DJ, Balbach JJ, Tycko R, et al. Increasing the amphiphilicity of an amyloidogenic peptide changes the beta-sheet structure in the fibrils from antiparallel to parallel. Biophys J 2004; 86:428 - 434
- Balbach JJ, Petkova AT, Oyler NA, et al. Supramolecular structure in full-length Alzheimer's b-amyloid fibrils: evidence for parallel b-sheet organisation from solid state nuclear magnetic resonance. Biophys J 2002; 83:1205 - 1216
- Petkova AT, Buntkowsky G, Dyda F, et al. Solid state NMR reveals a pH-dependent anti-parallel beta-sheet registry in fibrils formed by a beta-amyloid peptide. J Mol Biol 2004; 335:247 - 260
- Petkova AT, Leapman RD, Guo Z, et al. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 2005; 307:262 - 265
- Petkova AT, Ishii Y, Balbach JJ, 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
- Luhrs T, Ritter C, Adrian M, et al. 3D structure of Alzheimer's amyloid-beta(1–42) fibrils. Proc Natl Acad Sci USA 2005; 102:17342 - 17347
- Vestergaard B, Groenning M, Roessle M, et al. A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils. PLoS Biol 2007; 5:134
- Hardy J, Allsop D. Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol Sci 1991; 12:383 - 388
- Lue LF, Kuo YM, Roher AE, et al. Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am J Pathol 1999; 155:853 - 862
- Naslund J, Haroutunian V, Mohs R, et al. Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline. Jama 2000; 283:1571 - 1577
- Wang J, Dickson DW, Trojanowski JQ, et al. The levels of soluble versus insoluble brain Abeta distinguish Alzheimer's disease from normal and pathologic aging. Exp Neurol 1999; 158:328 - 337
- Hock C, Konietzko U, Papassotiropoulos A, et al. Generation of antibodies specific for beta-amyloid by vaccination of patients with Alzheimer's disease. Nature Medicine 2002; 8:0 - 5
- Smith JF, Knowles TP, Dobson CM, et al. Characterization of the nanoscale properties of individual amyloid fibrils. Proc Natl Acad Sci USA 2006; 103:15806 - 15811
- Chapman MR, Robinson LS, Pinkner JS, et al. Role of Escherichia coli curli operons in directing amyloid fiber formation. Science 2002; 295:851 - 855
- Robinson LS, Ashman EM, Hultgren SJ, et al. Secretion of curli fiber subunits is mediated by the outer membrane-localized CsgG protein. Mol Microbiol 2006; 59:870 - 881
- Sunde M, Kwan AH, Templeton MD, et al. Structural analysis of hydrophobins. Micron 2007; 39:773 - 784
- Uptain SM, Lindquist S. Prions as protein-based genetic elements. Annu Rev Microbiol 2002; 56:703 - 741
- Scheibel T, Parthasarathy R, Sawicki G, et al. Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition. Proc Natl Acad Sci USA 2003; 100:4527 - 4532
- Baldwin AJ, Bader R, Christodoulou J, et al. Cytochrome display on amyloid fibrils. Journal of the American Chemical Society 2006; 128:2162 - 2163
- Reches M, Gazit E. Casting metal nanowires within discrete self-assembled peptide nanotubes. Science 2003; 300:625 - 627
- Serpell LC, Benson M, Liepnieks JJ, et al. Structural analyses of fibrinogen amyloid fibrils. Amyloid 2007; 14:199 - 203