AGGRESCAN: A server for the prediction and evaluation of "hot spots" of aggregation in polypeptides

BMC Bioinformatics

Volumn 8, Issue , 2007, Pages

  Conchillo Solé, Oscar ^a   de Groot, Natalia S ^a   Avilés, Francesc X ^a   Vendrell, Josep ^a   Daura, Xavier ^a,b   Ventura, Salvador ^a  

^a UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

^b INSTITUCIÓ CATALANA DE RECERCA I ESTUDIS AVANÇATS ICREA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION PHENOMENA; AGGREGATION PROPERTY; AMYLOIDOGENIC PROTEINS; CONFORMATIONAL DISEASE; IN-VIVO EXPERIMENTS; NATURAL AMINO ACIDS; PARKINSON'S DISEASE; PROTEIN AGGREGATION;

AMINO ACIDS; DEPOSITION; FORECASTING; POLYPEPTIDES;

RECOMBINANT PROTEINS;

ALPHA SYNUCLEIN; AMYLIN; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; APOLIPOPROTEIN A1; APOLIPOPROTEIN A2; APOLIPOPROTEIN A4; APOLIPOPROTEIN C2; BETA 2 MICROGLOBULIN; FIBRINOGEN; FIBRINOGEN A ALPHA CHAIN; GLYCOPHORIN A; HIGH MOBILITY GROUP B1 PROTEIN; INSULIN; LUNG SURFACTANT; LYSOZYME; MYOGLOBIN; POLYPEPTIDE; PREALBUMIN; PRION PROTEIN; PROLACTIN; PROTEIN ABRI; PROTEIN ADAN; PROTEIN MEDIN; SERUM AMYLOID A; TAU PROTEIN; TROPOELASTIN; UNCLASSIFIED DRUG; PEPTIDE; PROTEIN;

ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; COMPUTER PREDICTION; COMPUTER PROGRAM; GENE MUTATION; PROTEIN AGGREGATION; PROTEIN ANALYSIS; STRUCTURAL BIOINFORMATICS; STRUCTURAL PROTEOMICS; CHEMISTRY; COMPARATIVE STUDY; DRUG DELIVERY SYSTEM; EVALUATION STUDY; GENETICS; HUMAN; METABOLISM; PREDICTIVE VALUE; PROCEDURES; PROTEIN CONFORMATION; TRENDS;

BACTERIA (MICROORGANISMS);

DRUG DELIVERY SYSTEMS; HUMANS; PEPTIDES; PREDICTIVE VALUE OF TESTS; PROTEIN CONFORMATION; PROTEINS; SOFTWARE;

EID: 33947517558     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-8-65     Document Type: Article

References (98)

1. Fink AL Protein aggregation: Folding aggregates, inclusion bodies and amyloid Fold Des 1998 3 R9-23 10.1016/S1359-0278(98)00002-9 9502314
2. Smith A protein misfolding Nature 2003 426 883-8883 10.1038/426883a
3. Ventura S Villaverde A Protein quality in bacterial inclusion bodies Trends Biotechnol 2006 24 4 179-185 10.1016/j.tibtech.2006.02.007 16503059
4. Treuheit MJ Kosky AA Brems DN Inverse relationship of protein concentration and aggregation Pharm Res 2002 19 4 511-516 10.1023/ A:1015108115452 12033388
5. Dobson CM Protein-misfolding diseases: Getting out of shape Nature 2002 418 729-7730 10.1038/418729a 12181546
6. Cohen FE Kelly JW Therapeutic approaches to protein-misfolding diseases Nature 2003 426 905-9909 10.1038/nature02265 14685252
7. Rochet JC Lansbury PT Amyloid fibrillogenesis: Themes and variations Curr Opin Struct Biol 2000 10 60-668 10.1016/S0959-440X(99)00049-4 10679462
8. Stefani M Dobson CM Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution J Mol Med 2003 81 11 678-699 10.1007/s00109-003-0464-5 12942175
9. Ivanova MI Sawaya MR Gingery M Attinger A Eisenberg D An amyloid-forming segment of {beta}2-microglobulin suggests a molecular model for the fibril PNAS 2004 101 29 10584-10589 10.1073/pnas.0403756101 15249659 489978
10. Ventura S Zurdo J Narayanan S Parreno M Mangues R Reif B Chiti F Giannoni E Dobson CM Aviles FX Serrano L Short amino acid stretches can mediate amyloid formation in globular proteins: The Src homology 3 (SH3) case Proc Natl Acad Sci U S A 2004 101 7258-77263 409906 15123800 10.1073/pnas.0308249101
11. Chiti F Dobson CM Protein misfolding, functional amyloid, and human disease Annu Rev Biochem 2006 75 333-366 10.1146/ annurev.biochem.75.101304.123901 16756495
12. de Groot NS Aviles FX Vendrell J Ventura S Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities Febs J 2006 273 3 658-668 10.1111/j.1742-4658.2005.05102.x 16420488
13. de Groot N Pallares I Aviles F Vendrell J Ventura S Prediction of "hot spots" of aggregation in disease-linked polypeptides BMC Structural Biology 2005 5 1 18 1262731 16197548 10.1186/1472-6807-5-18
14. Chiti F Stefani M Taddei N Ramponi G Dobson CM Rationalization of the effects of mutations on peptide and protein aggregation rates Nature 2003 424 6950 805-808 10.1038/nature01891 12917692
15. http://www.expasy.org/tools/pscale/A.A.Swiss-Prot.html
16. Williams AD Portelius E Kheterpal I Guo JT Cook KD Xu Y Wetzel R Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis J Mol Biol 2004 335 3 833-842 10.1016/j.jmb.2003.11.008 14687578
17. Chiti F Webster P Taddei N Clark A Stefani M Ramponi G Dobson CM Designing conditions for in vitro formation of amyloid protofilaments and fibrils Proc Natl Acad Sci U S A 1999 96 7 3590-3594 22338 10097081 10.1073/pnas.96.7.3590
18. Chiti F Calamai M Taddei N Stefani M Ramponi G Dobson CM Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases Proc Natl Acad Sci U S A 2002 99 Suppl 4 16419-16426 139903 12374855 10.1073/pnas.212527999
19. Rojas Quijano FA Morrow D Wise BM Brancia FL Goux WJ Prediction of nucleating sequences from amyloidogenic propensities of tau-related peptides Biochemistry 2006 45 14 4638-4652 10.1021/bi052226q 16584199
20. Ivanova MI Thompson MJ Eisenberg D A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments Proc Natl Acad Sci U S A 2006 103 11 4079-4082 1449649 16537488 10.1073/ pnas.0511298103
21. Fernandez-Escamilla AM Rousseau F Schymkowitz J Serrano L Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins Nat Biotechnol 2004 22 1302-11306 10.1038/nbt1012 15361882
22. DuBay KF Pawar AP Chiti F Zurdo J Dobson CM Vendruscolo M Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains J Mol Biol 2004 341 5 1317-1326 10.1016/j.jmb.2004.06.043 15302561
23. Tartaglia GG Cavalli A Pellarin R Caflisch A Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences Protein Sci 2005 14 10 2723-2734 10.1110/ps.051471205 16195556
24. Idicula-Thomas S Balaji PV Understanding the relationship between the primary structure of proteins and their amyloidogenic propensity: Clues from inclusion body formation Protein Eng Des Sel 2005 18 4 175-180 10.1093/protein/gzi022 15849216
25. Johansson J Weaver TE Tjernberg LO Proteolytic generation and aggregation of peptides from transmembrane regions: Lung surfactant protein C and amyloid beta-peptide Cell Mol Life Sci 2004 61 3 326-335 10.1007/s00018-003-3274-6 14770296
26. Westermark P Johnson KH O'Brien TD Betsholtz C Islet amyloid polypeptide - a novel controversy in diabetes research Diabetologia 1992 35 4 297-303 10.1007/BF00401195 1516756
27. Margittai M Langen R Template-assisted filament growth by parallel stacking of tau Proc Natl Acad Sci U S A 2004 101 28 10278-10283 478563 15240881 10.1073/pnas.0401911101
28. Selkoe DJ Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases Nat Cell Biol 2004 6 11 1054-1061 10.1038/ncb1104-1054 15516999
29. Nelson R Eisenberg D Structural models of amyloid-like fibrils Adv Protein Chem 2006 73 235-282 17190616
30. Pawar AP Dubay KF Zurdo J Chiti F Vendruscolo M Dobson CM Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases J Mol Biol 2005 350 2 379-392 10.1016/j.jmb.2005.04.016 15925383
31. Galzitskaya OV Garbuzynskiy SO Lobanov MY Prediction of amyloidogenic and disordered regions in protein chains PLoS Comput Biol 2006 2 12 e177 1761655 17196033 10.1371/journal.pcbi.0020177
32. Thompson MJ Sievers SA Karanicolas J Ivanova MI Baker D Eisenberg D The 3D profile method for identifying fibril-forming segments of proteins Proc Natl Acad Sci U S A 2006 103 11 4074-4078 1449648 16537487 10.1073/ pnas.0511295103
33. Lopez De La Paz M Goldie K Zurdo J Lacroix E Dobson CM Hoenger A Serrano L De novo designed peptide-based amyloid fibrils Proc Natl Acad Sci U S A 2002 99 25 16052-16057 138563 12456886 10.1073/pnas.252340199
34. Fowler SB Poon S Muff R Chiti F Dobson CM Zurdo J Rational design of aggregation-resistant bioactive peptides: Reengineering human calcitonin Proc Natl Acad Sci U S A 2005 102 29 10105-10110 1174920 16006528 10.1073/pnas.0501215102
35. Esler WP Stimson ER Ghilardi JR Lu YA Felix AM Vinters HV Mantyh PW Lee JP Maggio JE Point substitution in the central hydrophobic cluster of a human beta-amyloid congener disrupts peptide folding and abolishes plaque competence Biochemistry 1996 35 13914-13921 10.1021/bi961302+ 8909288
36. Lambermon MH Rappaport RV McLaurin J Biophysical characterization of longer forms of amyloid beta peptides: Possible contribution to flocculent plaque formation J Neurochem 2005 95 6 1667-1676 10.1111/ j.1471-4159.2005.03497.x 16300644
37. Gamblin TC Berry RW Binder LI Tau polymerization: Role of the amino terminus Biochemistry 2003 42 7 2252-2257 10.1021/bi0272510 12590615
38. Barghorn S Mandelkow E Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments Biochemistry 2002 41 50 14885-14896 10.1021/bi026469j 12475237
39. Li L von Bergen M Mandelkow EM Mandelkow E Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis J Biol Chem 2002 277 44 41390-41400 10.1074/jbc.M206334200 12198126
40. Yao TM Tomoo K Ishida T Hasegawa H Sasaki M Taniguchi T Aggregation analysis of the microtubule binding domain in tau protein by spectroscopic methods J Biochem (Tokyo) 2003 134 1 91-99 12944375
41. Rabzelj S Turk V Zerovnik E In vitro study of stability and amyloid-fibril formation of two mutants of human stefin B (cystatin B) occurring in patients with EPM1 Protein Sci 2005 14 10 2713-2722 10.1110/ ps.051609705 16155205
42. Delibas A Oner A Balci B Demircin G Bulbul M Bek K Erdogan O Baysun S Yilmaz E Genetic risk factors of amyloidogenesis in familial Mediterranean fever Am J Nephrol 2005 25 5 434-440 10.1159/000087824 16118480
43. Jimenez JL Guijarro JI Orlova E Zurdo J Dobson CM Sunde M Saibil HR Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing Embo J 1999 18 4 815-821 1171174 10022824 10.1093/ emboj/18.4.815
44. Bucciantini M Giannoni E Chiti F Baroni F Formigli L Zurdo J Taddei N Ramponi G Dobson CM Stefani M Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases Nature 2002 416 6880 507-511 10.1038/416507a 11932737
45. Ventura S Lacroix E Serrano L Insights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils J Mol Biol 2002 322 1147-11458 10.1016/S0022-2836(02)00783-0 12367534
46. Morel B Casares S Conejero-Lara F A single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: Analysis of the early stages of fibril formation J Mol Biol 2006 356 2 453-468 10.1016/ j.jmb.2005.11.062 16375922
47. Linding R Schymkowitz J Rousseau F Diella F Serrano L A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins J Mol Biol 2004 342 1 345-353 10.1016/j.jmb.2004.06.088 15313629
48. Rousseau F Schymkowitz J Serrano L Protein aggregation and amyloidosis: confusion of the kinds? Curr Opin Struct Biol 2006 16 1 118-126 10.1016/ j.sbi.2006.01.011 16434184
49. Villaverde A Carrio MM Protein aggregation in recombinant bacteria: biological role of inclusion bodies Biotechnol Lett 2003 25 17 1385-1395 10.1023/A:1025024104862 14514038
50. Clackson T Wells JA A hot spot of binding energy in a hormone-receptor interface Science 1995 267 5196 383-386 10.1126/science.7529940 7529940
51. Keskin O Ma B Nussinov R Hot regions in protein - protein interactions: the organization and contribution of structurally conserved hot spot residues J Mol Biol 2005 345 5 1281-1294 10.1016/j.jmb.2004.10.077 15644221
52. El-Agnaf O Gibson G Lee M Wright A Austen BM Properties of neurotoxic peptides related to the Bri gene Protein Pept Lett 2004 11 3 207-212 10.2174/0929866043407156 15182222
53. El-Agnaf OM Nagala S Patel BP Austen BM Non-fibrillar oligomeric species of the amyloid ABri peptide, implicated in familial British dementia, are more potent at inducing apoptotic cell death than protofibrils or mature fibrils J Mol Biol 2001 310 1 157-168 10.1006/jmbi.2001.4743 11419943
54. Goedert M Alpha-synuclein and neurodegenerative diseases Nat Rev Neurosci 2001 2 7 492-501 10.1038/35081564 11433374
55. Bodles AM Guthrie DJ Greer B Irvine GB Identification of the region of non-Abeta component (NAC) of Alzheimer's disease amyloid responsible for its aggregation and toxicity J Neurochem 2001 78 2 384-395 10.1046/ j.1471-4159.2001.00408.x 11461974
56. Miake H Mizusawa H Iwatsubo T Hasegawa M Biochemical characterization of the core structure of alpha-synuclein filaments J Biol Chem 2002 277 21 19213-19219 10.1074/jbc.M110551200 11893734
57. Kallijarvi J Haltia M Baumann MH Amphoterin includes a sequence motif which is homologous to the Alzheimer's beta-amyloid peptide (Abeta), forms amyloid fibrils in vitro, and binds avidly to Abeta Biochemistry 2001 40 34 10032-10037 10.1021/bi002095n 11513581
58. Morimoto A Irie K Murakami K Masuda Y Ohigashi H Nagao M Fukuda H Shimizu T Shirasawa T Analysis of the secondary structure of beta-amyloid (Abeta42) fibrils by systematic proline replacement J Biol Chem 2004 279 50 52781-52788 10.1074/jbc.M406262200 15459202
59. Nichols WC Dwulet FE Liepnieks J Benson MD Variant apolipoprotein AI as a major constituent of a human hereditary amyloid Biochem Biophys Res Commun 1988 156 2 762-768 10.1016/S0006-291X(88)80909-4 3142462
60. Wilson LM Mok YF Binger KJ Griffin MD Mertens HD Lin F Wade JD Gooley PR Howlett GJ A Structural Core Within Apolipoprotein C-II Amyloid Fibrils Identified Using Hydrogen Exchange and Proteolysis J Mol Biol 2007 366 5 1639-1651 10.1016/j.jmb.2006.12.040 17217959
61. Hasegawa K Ohhashi Y Yamaguchi I Takahashi N Tsutsumi S Goto Y Gejyo F Naiki H Amyloidogenic synthetic peptides of beta2-microglobulin - a role of the disulfide bond Biochem Biophys Res Commun 2003 304 1 101-106 10.1016/S0006-291X(03)00543-6 12705891
62. Jones S Manning J Kad NM Radford SE Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro J Mol Biol 2003 325 2 249-257 10.1016/S0022-2836(02)01227-5 12488093
63. Tamburro AM Pepe A Bochicchio B Quaglino D Ronchetti IP Supramolecular amyloid-like assembly of the polypeptide sequence coded by exon 30 of human tropoelastin J Biol Chem 2005 280 4 2682-2690 10.1074/ jbc.M411617200 15550396
64. Hamidi Asl L Liepnieks JJ Uemichi T Rebibou JM Justrabo E Droz D Mousson C Chalopin JM Benson MD Delpech M Grateau G Renal amyloidosis with a frame shift mutation in fibrinogen aalpha-chain gene producing a novel amyloid protein Blood 1997 90 12 4799-4805 9389696
65. Liu W Crocker E Zhang W Elliott JI Luy B Li H Aimoto S Smith SO Structural role of glycine in amyloid fibrils formed from transmembrane alpha-helices Biochemistry 2005 44 9 3591-3597 10.1021/bi047827g 15736968
66. Jimenez JL Nettleton EJ Bouchard M Robinson CV Dobson CM Saibil HR The protofilament structure of insulin amyloid fibrils Proc Natl Acad Sci U S A 2002 99 14 9196-9201 123117 12093917 10.1073/pnas.142459399
67. Scrocchi LA Ha K Chen Y Wu L Wang F Fraser PE Identification of minimal peptide sequences in the (8-20) domain of human islet amyloid polypeptide involved in fibrillogenesis J Struct Biol 2003 141 3 218-227 10.1016/S1047-8477(02)00630-5 12648568
68. Azriel R Gazit E Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation J Biol Chem 2001 276 36 34156-34161 10.1074/jbc.M102883200 11445568
69. Krebs MR Wilkins DK Chung EW Pitkeathly MC Chamberlain AK Zurdo J Robinson CV Dobson CM Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain J Mol Biol 2000 300 3 541-549 10.1006/jmbi.2000.3862 10884350
70. Frare E Polverino De Laureto P Zurdo J Dobson CM Fontana A A highly amyloidogenic region of hen lysozyme J Mol Biol 2004 340 5 1153-1165 10.1016/j.jmb.2004.05.056 15236974
71. Reches M Gazit E Amyloidogenic hexapeptide fragment of medin: Homology to functional islet amyloid polypeptide fragments Amyloid 2004 11 2 81-89 15478463
72. Fandrich M Forge V Buder K Kittler M Dobson CM Diekmann S Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments Proc Natl Acad Sci U S A 2003 100 26 15463-15468 307590 14665689 10.1073/ pnas.0303758100
73. Tagliavini F Prelli F Verga L Giaccone G Sarma R Gorevic P Ghetti B Passerini F Ghibaudi E Forloni G Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro Proc Natl Acad Sci U S A 1993 90 20 9678-9682 47633 8105481 10.1073/pnas.90.20.9678
74. Hinton DR Polk RK Linse KD Weiss MH Kovacs K Garner JA Characterization of spherical amyloid protein from a prolactin-producing pituitary adenoma Acta Neuropathol (Berl) 1997 93 1 43-49 10.1007/s004010050581 9006656
75. Westermark GT Engstrom U Westermark P The N-terminal segment of protein AA determines its fibrillogenic property Biochem Biophys Res Commun 1992 182 1 27-33 10.1016/S0006-291X(05)80107-X 1731787
76. Jarvis JA Kirkpatrick A Craik DJ 1H NMR analysis of fibril-forming peptide fragments of transthyretin Int J Pept Protein Res 1994 44 4 388-398 7875942
77. 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 U S A 2004 101 3 711-716 321745 14715898 10.1073/pnas.0304849101
78. Petkova AT Ishii Y Balbach JJ Antzutkin ON Leapman RD Delaglio F Tycko R A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR Proc Natl Acad Sci U S A 2002 99 26 16742-16747 139214 12481027 10.1073/pnas.262663499
79. Kajava AV Aebi U Steven AC The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin J Mol Biol 2005 348 2 24-252 10.1016/j.jmb.2005.02.029 15811365
80. Ritter C Maddelein ML Siemer AB Luhrs T Ernst M Meier BH Saupe SJ Riek R Correlation of structural elements and infectivity of the HET-s prion Nature 2005 435 7043 844-848 1567094 15944710 10.1038/nature03793
81. Lim KH Nguyen TN Damo SM Mazur T Ball HL Prusiner SB Pines A Wemmer DE Solid-state NMR structural studies of the fibril form of a mutant mouse prion peptide PrP89-143(P101L) Solid State Nucl Magn Reson 2006 29 1-3 183-190 10.1016/j.ssnmr.2005.09.017 16256316
82. Iwata K Fujiwara T Matsuki Y Akutsu H Takahashi S Naiki H Goto Y 3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR Proc Natl Acad Sci U S A 2006 103 48 18119-18124 10.1073/pnas.0607180103 17108084
83. Jaroniec CP MacPhee CE Astrof NS Dobson CM Griffin RG Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril Proc Natl Acad Sci U S A 2002 99 26 16748-16753 139215 12481032 10.1073/ pnas.252625999
84. Yamamoto N Hasegawa K Matsuzaki K Naiki H Yanagisawa K Environment- and mutation-dependent aggregation behavior of Alzheimer amyloid beta-protein J Neurochem 2004 90 1 62-69 10.1111/ j.1471-4159.2004.02459.x 15198667
85. Cannon MJ Williams AD Wetzel R Myszka DG Kinetic analysis of beta-amyloid fibril elongation Anal Biochem 2004 328 1 67-75 10.1016/ j.ab.2004.01.014 15081909
86. Van Nostrand WE Melchor JP Cho HS Greenberg SM Rebeck GW Pathogenic effects of D23N Iowa mutant amyloid beta -protein J Biol Chem 2001 276 35 32860-32866 10.1074/jbc.M104135200 11441013
87. Wurth C Guimard NK Hecht MH Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: An unbiased search for the sequence determinants of Abeta amyloidogenesis J Mol Biol 2002 319 5 1279-1290 10.1016/S0022-2836(02)00399-6 12079364
88. Jarrett JT Berger EP Lansbury PT Jr. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease Biochemistry 1993 32 18 4693-4697 10.1021/bi00069a001 8490014
89. Gamblin TC Chen F Zambrano A Abraha A Lagalwar S Guillozet AL Lu M Fu Y Garcia-Sierra F LaPointe N Miller R Berry RW Binder LI Cryns VL Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease Proc Natl Acad Sci U S A 2003 100 17 10032-10037 187753 12888622 10.1073/pnas.1630428100
90. Barghorn S Zheng-Fischhofer Q Ackmann M Biernat J von Bergen M Mandelkow EM Mandelkow E Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias Biochemistry 2000 39 38 11714-1721 10.1021/bi000850r 10995239
91. Rosso SM van Herpen E Deelen W Kamphorst W Severijnen LA Willemsen R Ravid R Niermeijer MF Dooijes D Smith MJ Goedert M Heutink P van Swieten JC A novel tau mutation, S320F, causes a tauopathy with inclusions similar to those in Pick's disease Ann Neurol 2002 51 3 373-376 10.1002/ ana.10140 11891833
92. Choi W Zibaee S Jakes R Serpell LC Davletov B Crowther RA Goedert M Mutation E46K increases phospholipid binding and assembly into filaments of human alpha-synuclein FEBS Lett 2004 576 3 363-368 10.1016/ j.febslet.2004.09.038 15498564
93. Giasson BI Murray IV Trojanowski JQ Lee VM A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly J Biol Chem 2001 276 4 2380-2386 10.1074/ jbc.M008919200 11060312
94. Green J Goldsbury C Mini T Sunderji S Frey P Kistler J Cooper G Aebi U Full-length rat amylin forms fibrils following substitution of single residues from human amylin J Mol Biol 2003 326 4 1147-1156 10.1016/ S0022-2836(02)01377-3 12589759
95. Sakagashira S Sanke T Hanabusa T Shimomura H Ohagi S Kumagaye KY Nakajima K Nanjo K Missense mutation of amylin gene (S20G) in Japanese NIDDM patients Diabetes 1996 45 9 1279-1281 10.2337/diabetes.45.9.1279 8772735
96. Porte D Jr. Kahn SE Hyperproinsulinemia and amyloid in NIDDM. Clues to etiology of islet beta-cell dysfunction? Diabetes 1989 38 11 1333-1336 10.2337/diabetes.38.11.1333 2695369
97. Salmona M Malesani P De Gioia L Gorla S Bruschi M Molinari A Della Vedova F Pedrotti B Marrari MA Awan T Bugiani O Forloni G Tagliavini F Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106-126 Biochem J 1999 342 (Pt 1) 207-214 1220454 10432318 10.1042/0264-6021:3420207
98. Thompson AJ Barnham KJ Norton RS Barrow CJ The Val-210-Ile pathogenic Creutzfeldt-Jakob disease mutation increases both the helical and aggregation propensities of a sequence corresponding to helix-3 of PrP(C) Biochim Biophys Acta 2001 1544 1-2 242-254 11341933