{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T03:49:43Z","timestamp":1792122583618,"version":"4.4.0"},"reference-count":142,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2013,8,19]],"date-time":"2013-08-19T00:00:00Z","timestamp":1376870400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"},{"start":{"date-parts":[[2013,8,19]],"date-time":"2013-08-19T00:00:00Z","timestamp":1376870400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001809","name":"Natural Science Foundation of China","doi-asserted-by":"crossref","award":["81172971"],"award-info":[{"award-number":["81172971"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"Natural Science Foundation of China","doi-asserted-by":"crossref","award":["81222043"],"award-info":[{"award-number":["81222043"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100004602","name":"Program for New Century Excellent Talents in University","doi-asserted-by":"crossref","award":["NECT11-0170"],"award-info":[{"award-number":["NECT11-0170"]}],"id":[{"id":"10.13039\/501100004602","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2013,11]]},"DOI":"10.1002\/prot.24338","type":"journal-article","created":{"date-parts":[[2013,6,12]],"date-time":"2013-06-12T22:34:43Z","timestamp":1371076483000},"page":"1862-1873","source":"Crossref","is-referenced-by-count":62,"title":["Disulfide bonds in amyloidogenesis diseases related proteins"],"prefix":"10.1002","volume":"81","author":[{"given":"Yang","family":"Li","sequence":"first","affiliation":[{"name":"Tongji School of Pharmacy; Huazhong University of Science and Technology; Wuhan Hubei People's Republic of China 430030"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juan","family":"Yan","sequence":"additional","affiliation":[{"name":"Tongji School of Pharmacy; Huazhong University of Science and Technology; Wuhan Hubei People's Republic of China 430030"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xin","family":"Zhang","sequence":"additional","affiliation":[{"name":"Tongji School of Pharmacy; Huazhong University of Science and Technology; Wuhan Hubei People's Republic of China 430030"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kun","family":"Huang","sequence":"additional","affiliation":[{"name":"Tongji School of Pharmacy; Huazhong University of Science and Technology; Wuhan Hubei People's Republic of China 430030"},{"name":"Centre for Biomedicine Research; Wuhan Institute of Biotechnology; Wuhan Hubei People's Republic of China 430074"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2013,8,19]]},"reference":[{"key":"10.1002\/prot.24338-BIB0001|prot24338-cit-0001","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1007\/s00109-003-0464-5","article-title":"Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution","volume":"81","author":"Stefani","year":"2003","journal-title":"J Mol Med (Berl)"},{"key":"10.1002\/prot.24338-BIB0002|prot24338-cit-0002","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.bbapap.2003.12.008","article-title":"Conformational constraints for amyloid fibrillation: the importance of being unfolded","volume":"1698","author":"Uversky","year":"2004","journal-title":"Biochim Biophys Acta"},{"key":"10.1002\/prot.24338-BIB0003|prot24338-cit-0003","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1126\/science.1566067","article-title":"Alzheimer's disease: the amyloid cascade hypothesis","volume":"256","author":"Hardy","year":"1992","journal-title":"Science"},{"key":"10.1002\/prot.24338-BIB0004|prot24338-cit-0004","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/S0092-8674(00)81163-0","article-title":"Prion protein biology","volume":"93","author":"Prusiner","year":"1998","journal-title":"Cell"},{"key":"10.1002\/prot.24338-BIB0005|prot24338-cit-0005","doi-asserted-by":"crossref","first-page":"6469","DOI":"10.1073\/pnas.95.11.6469","article-title":"alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies","volume":"95","author":"Spillantini","year":"1998","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0006|prot24338-cit-0006","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1093\/brain\/awh704","article-title":"Disulphide-reduced superoxide dismutase-1 in CNS of transgenic amyotrophic lateral sclerosis models","volume":"129","author":"Jonsson","year":"2006","journal-title":"Brain"},{"key":"10.1002\/prot.24338-BIB0007|prot24338-cit-0007","doi-asserted-by":"crossref","first-page":"6077","DOI":"10.1210\/jc.2005-0044","article-title":"Prognostic impact of serum calcitonin and carcinoembryonic antigen doubling-times in patients with medullary thyroid carcinoma","volume":"90","author":"Barbet","year":"2005","journal-title":"J Clin Endocrinol Metab"},{"key":"10.1002\/prot.24338-BIB0008|prot24338-cit-0008","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1006\/jsbi.2000.4270","article-title":"Abnormal tau-containing filaments in neurodegenerative diseases","volume":"130","author":"Crowther","year":"2000","journal-title":"J Struct Biol"},{"key":"10.1002\/prot.24338-BIB0009|prot24338-cit-0009","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1038\/362553a0","article-title":"Human lysozyme gene mutations cause hereditary systemic amyloidosis","volume":"362","author":"Pepys","year":"1993","journal-title":"Nature"},{"key":"10.1002\/prot.24338-BIB0010|prot24338-cit-0010","first-page":"291","article-title":"The pancreatic islet cells in insular amyloidosis in human diabetic and non-diabetic adults","volume":"81","author":"Westermark","year":"1973","journal-title":"Acta Pathol Microbiol Scand A"},{"key":"10.1002\/prot.24338-BIB0011|prot24338-cit-0011","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1016\/S0092-8674(00)81369-0","article-title":"Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice","volume":"87","author":"Mangiarini","year":"1996","journal-title":"Cell"},{"key":"10.1002\/prot.24338-BIB0012|prot24338-cit-0012","doi-asserted-by":"crossref","first-page":"3881","DOI":"10.1073\/pnas.84.11.3881","article-title":"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","volume":"84","author":"Westermark","year":"1987","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0013|prot24338-cit-0013","first-page":"49","article-title":"Amyloidosis of the islets of Langerhans","volume":"38","author":"Ehrlich","year":"1961","journal-title":"A restudy of islet hyalin in diabetic and non-diabetic individuals. Am J Pathol"},{"key":"10.1002\/prot.24338-BIB0014|prot24338-cit-0014","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1021\/js960297s","article-title":"Toward understanding insulin fibrillation","volume":"86","author":"Brange","year":"1997","journal-title":"J Pharm Sci"},{"key":"10.1002\/prot.24338-BIB0015|prot24338-cit-0015","doi-asserted-by":"crossref","first-page":"43909","DOI":"10.1074\/jbc.M105956200","article-title":"Systemic amyloid deposits in familial British dementia","volume":"276","author":"Ghiso","year":"2001","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0016|prot24338-cit-0016","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1007\/BF00194306","article-title":"Hereditary cystatin C amyloid angiopathy: identification of the disease-causing mutation and specific diagnosis by polymerase chain reaction based analysis","volume":"89","author":"Abrahamson","year":"1992","journal-title":"Hum Genet"},{"key":"10.1002\/prot.24338-BIB0017|prot24338-cit-0017","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1038\/ng0595-94","article-title":"Expression analysis of the ataxin-1 protein in tissues from normal and spinocerebellar ataxia type 1 individuals","volume":"10","author":"Servadio","year":"1995","journal-title":"Nat Genet"},{"key":"10.1002\/prot.24338-BIB0018|prot24338-cit-0018","doi-asserted-by":"crossref","first-page":"2843","DOI":"10.1073\/pnas.87.7.2843","article-title":"Fibril in senile systemic amyloidosis is derived from normal transthyretin","volume":"87","author":"Westermark","year":"1990","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0019|prot24338-cit-0019","doi-asserted-by":"crossref","first-page":"1928","DOI":"10.1038\/ki.1997.262","article-title":"Histological prevalence of beta 2-microglobulin amyloidosis in hemodialysis: a prospective post-mortem study","volume":"51","author":"Jadoul","year":"1997","journal-title":"Kidney Int"},{"key":"10.1002\/prot.24338-BIB0020|prot24338-cit-0020","first-page":"323","article-title":"Mechanisms of disease: monoclonal immunoglobulin deposition","volume":"6","author":"Buxbaum","year":"1992","journal-title":"Amyloidosis, light chain deposition disease, and light and heavy chain deposition disease. Hematol Oncol Clin North Am"},{"key":"10.1002\/prot.24338-BIB0021|prot24338-cit-0021","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1038\/ng0393-252","article-title":"Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain","volume":"3","author":"Benson","year":"1993","journal-title":"Nat Genet"},{"key":"10.1002\/prot.24338-BIB0022|prot24338-cit-0022","doi-asserted-by":"crossref","first-page":"2186","DOI":"10.1046\/j.1432-1327.2000.01219.x","article-title":"Toxicity of non-abeta component of Alzheimer's disease amyloid, and N-terminal fragments thereof, correlates to formation of beta-sheet structure and fibrils","volume":"267","author":"Bodles","year":"2000","journal-title":"Eur J Biochem"},{"key":"10.1002\/prot.24338-BIB0023|prot24338-cit-0023","doi-asserted-by":"crossref","first-page":"55","DOI":"10.3109\/13506129809007291","article-title":"Gelsolin-related familial amyloidosis, Finnish type (FAF), and its variants found worldwide","volume":"5","author":"Kiuru","year":"1998","journal-title":"Amyloid"},{"key":"10.1002\/prot.24338-BIB0024|prot24338-cit-0024","doi-asserted-by":"crossref","first-page":"2091","DOI":"10.1161\/01.CIR.0000034511.06350.DF","article-title":"Atrial amyloidosis: an arrhythmogenic substrate for persistent atrial fibrillation","volume":"106","author":"Rocken","year":"2002","journal-title":"Circulation"},{"key":"10.1002\/prot.24338-BIB0025|prot24338-cit-0025","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1038\/352077a0","article-title":"Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy","volume":"352","author":"La Spada","year":"1991","journal-title":"Nature"},{"key":"10.1002\/prot.24338-BIB0026|prot24338-cit-0026","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1006\/jmbi.1997.1348","article-title":"Common core structure of amyloid fibrils by synchrotron X-ray diffraction","volume":"273","author":"Sunde","year":"1997","journal-title":"J Mol Biol"},{"key":"10.1002\/prot.24338-BIB0027|prot24338-cit-0027","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1146\/annurev.neuro.26.010302.081142","article-title":"Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders","volume":"26","author":"Caughey","year":"2003","journal-title":"Annu Rev Neurosci"},{"key":"10.1002\/prot.24338-BIB0028|prot24338-cit-0028","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1038\/nature02261","article-title":"Protein folding and misfolding","volume":"426","author":"Dobson","year":"2003","journal-title":"Nature"},{"key":"10.1002\/prot.24338-BIB0029|prot24338-cit-0029","doi-asserted-by":"crossref","first-page":"21","DOI":"10.4049\/jimmunol.110.1.21","article-title":"Fibrillar assemblage of variable segments of immunoglobulin light chains: an electron microscopic study","volume":"110","author":"Shirahama","year":"1973","journal-title":"J Immunol"},{"key":"10.1002\/prot.24338-BIB0030|prot24338-cit-0030","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1093\/emboj\/18.4.815","article-title":"Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing","volume":"18","author":"Jimenez","year":"1999","journal-title":"EMBO J"},{"key":"10.1002\/prot.24338-BIB0031|prot24338-cit-0031","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/S0925-4439(00)00029-6","article-title":"Alzheimer's amyloid fibrils: structure and assembly","volume":"1502","author":"Serpell","year":"2000","journal-title":"Biochim Biophys Acta"},{"key":"10.1002\/prot.24338-BIB0032|prot24338-cit-0032","doi-asserted-by":"crossref","first-page":"3590","DOI":"10.1073\/pnas.96.7.3590","article-title":"Designing conditions for in vitro formation of amyloid protofilaments and fibrils","volume":"96","author":"Chiti","year":"1999","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0033|prot24338-cit-0033","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1038\/nature01891","article-title":"Rationalization of the effects of mutations on peptide and protein aggregation rates","volume":"424","author":"Chiti","year":"2003","journal-title":"Nature"},{"key":"10.1002\/prot.24338-BIB0034|prot24338-cit-0034","doi-asserted-by":"crossref","first-page":"7048","DOI":"10.1002\/anie.201100986","article-title":"Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein","volume":"50","author":"Mossuto","year":"2011","journal-title":"Angew Chem Int Ed Engl"},{"key":"10.1002\/prot.24338-BIB0035|prot24338-cit-0035","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1007\/s00249-010-0576-0","article-title":"Effects of dithiothreitol on the amyloid fibrillogenesis of hen egg-white lysozyme","volume":"39","author":"Wang","year":"2010","journal-title":"Eur Biophys J"},{"key":"10.1002\/prot.24338-BIB0036|prot24338-cit-0036","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/j.jmb.2006.05.007","article-title":"The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner","volume":"360","author":"Devlin","year":"2006","journal-title":"J Mol Biol"},{"key":"10.1002\/prot.24338-BIB0037|prot24338-cit-0037","doi-asserted-by":"crossref","first-page":"5794","DOI":"10.1021\/bi900219c","article-title":"Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking","volume":"48","author":"Huang","year":"2009","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0038|prot24338-cit-0038","doi-asserted-by":"crossref","first-page":"962","DOI":"10.1016\/j.biochi.2011.02.006","article-title":"Effect of sodium tetrathionate on amyloid fibril: Insight into the role of disulfide bond in amyloid progression","volume":"93","author":"Sarkar","year":"2011","journal-title":"Biochimie"},{"key":"10.1002\/prot.24338-BIB0039|prot24338-cit-0039","doi-asserted-by":"crossref","first-page":"1619","DOI":"10.1016\/j.bbapap.2007.08.016","article-title":"Promotion of insulin aggregation by protein disulfide isomerase","volume":"1774","author":"Maeda","year":"2007","journal-title":"Biochim Biophys Acta"},{"key":"10.1002\/prot.24338-BIB0040|prot24338-cit-0040","doi-asserted-by":"crossref","first-page":"614","DOI":"10.2174\/138920309789630534","article-title":"The role of thiols and disulfides on protein stability","volume":"10","author":"Trivedi","year":"2009","journal-title":"Curr Protein Pept Sci"},{"key":"10.1002\/prot.24338-BIB0041|prot24338-cit-0041","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/S0959-440X(98)80016-X","article-title":"The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways","volume":"8","author":"Kelly","year":"1998","journal-title":"Curr Opin Struct Biol"},{"key":"10.1002\/prot.24338-BIB0042|prot24338-cit-0042","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S0968-0004(99)01445-0","article-title":"Protein misfolding, evolution and disease","volume":"24","author":"Dobson","year":"1999","journal-title":"Trends Biochem Sci"},{"key":"10.1002\/prot.24338-BIB0043|prot24338-cit-0043","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/S0959-440X(99)00049-4","article-title":"Amyloid fibrillogenesis: themes and variations","volume":"10","author":"Rochet","year":"2000","journal-title":"Curr Opin Struct Biol"},{"key":"10.1002\/prot.24338-BIB0044|prot24338-cit-0044","doi-asserted-by":"crossref","first-page":"4207","DOI":"10.1021\/bi992922o","article-title":"Disulfide bonds and protein folding","volume":"39","author":"Wedemeyer","year":"2000","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0045|prot24338-cit-0045","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/S0969-2126(00)00065-4","article-title":"Volume changes on protein folding","volume":"2","author":"Harpaz","year":"1994","journal-title":"Structure"},{"key":"10.1002\/prot.24338-BIB0046|prot24338-cit-0046","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1017\/S1462399407000385","article-title":"Novel therapeutic strategies for the treatment of protein-misfolding diseases","volume":"9","author":"Rochet","year":"2007","journal-title":"Expert Rev Mol Med"},{"key":"10.1002\/prot.24338-BIB0047|prot24338-cit-0047","doi-asserted-by":"crossref","first-page":"10278","DOI":"10.1021\/bi060879g","article-title":"Structure-specific effects of protein topology on cross-beta assembly: studies of insulin fibrillation","volume":"45","author":"Huang","year":"2006","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0048|prot24338-cit-0048","doi-asserted-by":"crossref","first-page":"11263","DOI":"10.1073\/pnas.0704307104","article-title":"Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS","volume":"104","author":"Banci","year":"2007","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0049|prot24338-cit-0049","doi-asserted-by":"crossref","first-page":"23459","DOI":"10.1074\/jbc.M110336200","article-title":"HLA-B27 misfolding is associated with aberrant intermolecular disulfide bond formation (dimerization) in the endoplasmic reticulum","volume":"277","author":"Dangoria","year":"2002","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0050|prot24338-cit-0050","doi-asserted-by":"crossref","first-page":"28087","DOI":"10.1074\/jbc.M704465200","article-title":"Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1","volume":"282","author":"Niwa","year":"2007","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0051|prot24338-cit-0051","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1073\/pnas.97.1.145","article-title":"NMR solution structure of the human prion protein","volume":"97","author":"Zahn","year":"2000","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0052|prot24338-cit-0052","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.cell.2005.02.011","article-title":"In vitro generation of infectious scrapie prions","volume":"121","author":"Castilla","year":"2005","journal-title":"Cell"},{"key":"10.1002\/prot.24338-BIB0053|prot24338-cit-0053","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1126\/science.1100195","article-title":"Synthetic mammalian prions","volume":"305","author":"Legname","year":"2004","journal-title":"Science"},{"key":"10.1002\/prot.24338-BIB0054|prot24338-cit-0054","doi-asserted-by":"crossref","first-page":"2079","DOI":"10.1126\/science.274.5295.2079","article-title":"Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity","volume":"274","author":"Telling","year":"1996","journal-title":"Science"},{"key":"10.1002\/prot.24338-BIB0055|prot24338-cit-0055","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1006\/jtbi.2000.2112","article-title":"Thiol-disulfide interchange a potential key to conformational change associated with amyloid fibril formation","volume":"206","author":"Feughelman","year":"2000","journal-title":"J Theor Biol"},{"key":"10.1002\/prot.24338-BIB0056|prot24338-cit-0056","doi-asserted-by":"crossref","first-page":"4334","DOI":"10.1073\/pnas.071066598","article-title":"A role for intermolecular disulfide bonds in prion diseases?","volume":"98","author":"Welker","year":"2001","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0057|prot24338-cit-0057","doi-asserted-by":"crossref","first-page":"4127","DOI":"10.1021\/bi027218d","article-title":"In vitro amplification of protease-resistant prion protein requires free sulfhydryl groups","volume":"42","author":"Lucassen","year":"2003","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0058|prot24338-cit-0058","doi-asserted-by":"crossref","first-page":"2457","DOI":"10.1097\/00001756-199808030-00006","article-title":"The importance of the disulfide bond in prion protein conversion","volume":"9","author":"Herrmann","year":"1998","journal-title":"Neuroreport"},{"key":"10.1002\/prot.24338-BIB0059|prot24338-cit-0059","doi-asserted-by":"crossref","first-page":"1935","DOI":"10.1126\/science.283.5409.1935","article-title":"Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations","volume":"283","author":"Jackson","year":"1999","journal-title":"Science"},{"key":"10.1002\/prot.24338-BIB0060|prot24338-cit-0060","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1016\/j.bbapap.2005.10.014","article-title":"Modulation of prion protein structure by pressure and temperature","volume":"1764","author":"Torrent","year":"2006","journal-title":"Biochim Biophys Acta"},{"key":"10.1002\/prot.24338-BIB0061|prot24338-cit-0061","doi-asserted-by":"crossref","first-page":"5528","DOI":"10.1021\/bi952965e","article-title":"High-level expression and characterization of a purified 142-residue polypeptide of the prion protein","volume":"35","author":"Mehlhorn","year":"1996","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0062|prot24338-cit-0062","doi-asserted-by":"crossref","first-page":"1711","DOI":"10.1016\/S0006-3495(02)75523-9","article-title":"The role of dimerization in prion replication","volume":"82","author":"Tompa","year":"2002","journal-title":"Biophys J"},{"key":"10.1002\/prot.24338-BIB0063|prot24338-cit-0063","doi-asserted-by":"crossref","first-page":"3295","DOI":"10.1021\/bi026872q","article-title":"Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization","volume":"42","author":"Kazlauskaite","year":"2003","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0064|prot24338-cit-0064","doi-asserted-by":"crossref","first-page":"36859","DOI":"10.1074\/jbc.274.52.36859","article-title":"Membrane environment alters the conformational structure of the recombinant human prion protein","volume":"274","author":"Morillas","year":"1999","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0065|prot24338-cit-0065","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1006\/jmbi.2001.5322","article-title":"Binding of prion protein to lipid membranes and implications for prion conversion","volume":"315","author":"Sanghera","year":"2002","journal-title":"J Mol Biol"},{"key":"10.1002\/prot.24338-BIB0066|prot24338-cit-0066","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1038\/382180a0","article-title":"NMR structure of the mouse prion protein domain PrP(121-321)","volume":"382","author":"Riek","year":"1996","journal-title":"Nature"},{"key":"10.1002\/prot.24338-BIB0067|prot24338-cit-0067","doi-asserted-by":"crossref","first-page":"10086","DOI":"10.1073\/pnas.94.19.10086","article-title":"Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform","volume":"94","author":"James","year":"1997","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0068|prot24338-cit-0068","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/S0891-5849(00)00430-5","article-title":"Thioredoxin converts the Syrian hamster (29-231) recombinant prion protein to an insoluble form","volume":"30","author":"Requena","year":"2001","journal-title":"Free Radic Biol Med"},{"key":"10.1002\/prot.24338-BIB0069|prot24338-cit-0069","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1007\/s10059-009-0089-9","article-title":"Disulfide bond as a structural determinant of prion protein membrane insertion","volume":"27","author":"Shin","year":"2009","journal-title":"Mol Cells"},{"key":"10.1002\/prot.24338-BIB0070|prot24338-cit-0070","first-page":"505","article-title":"High-resolution structure (1.33 A) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus","volume":"52","author":"Vaney","year":"1996","journal-title":"Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission. Acta Crystallogr D Biol Crystallogr"},{"key":"10.1002\/prot.24338-BIB0071|prot24338-cit-0071","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1038\/385787a0","article-title":"Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis","volume":"385","author":"Booth","year":"1997","journal-title":"Nature"},{"key":"10.1002\/prot.24338-BIB0072|prot24338-cit-0072","doi-asserted-by":"crossref","first-page":"6419","DOI":"10.1021\/bi983037t","article-title":"Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants","volume":"38","author":"Canet","year":"1999","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0073|prot24338-cit-0073","doi-asserted-by":"crossref","first-page":"2790","DOI":"10.1021\/bi00225a008","article-title":"A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme","volume":"30","author":"Goldberg","year":"1991","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0074|prot24338-cit-0074","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1002\/pro.5560030603","article-title":"Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme","volume":"3","author":"Goldberg","year":"1994","journal-title":"Protein Sci"},{"key":"10.1002\/prot.24338-BIB0075|prot24338-cit-0075","doi-asserted-by":"crossref","first-page":"19128","DOI":"10.1016\/S0021-9258(17)32284-6","article-title":"The role of the thiol\/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase","volume":"269","author":"Puig","year":"1994","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0076|prot24338-cit-0076","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S0927-7765(99)00140-X","article-title":"Improved refolding of denatured\/reduced lysozyme using disulfide-carrying polymeric microspheres","volume":"18","author":"Shimizu","year":"2000","journal-title":"Colloids Surf B Biointerfaces"},{"key":"10.1002\/prot.24338-BIB0077|prot24338-cit-0077","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1093\/jb\/117.2.369","article-title":"Effects of additives on irreversible inactivation of lysozyme at neutral pH and 100 degrees C","volume":"117","author":"Tomizawa","year":"1995","journal-title":"J Biochem"},{"key":"10.1002\/prot.24338-BIB0078|prot24338-cit-0078","doi-asserted-by":"crossref","first-page":"4547","DOI":"10.1046\/j.1432-1033.2003.03850.x","article-title":"Prevention of thermal inactivation and aggregation of lysozyme by polyamines","volume":"270","author":"Kudou","year":"2003","journal-title":"Eur J Biochem"},{"key":"10.1002\/prot.24338-BIB0079|prot24338-cit-0079","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1042\/BJ20071499","article-title":"How do surfactants and DTT affect the size, dynamics, activity and growth of soluble lysozyme aggregates?","volume":"415","author":"Kumar","year":"2008","journal-title":"Biochem J"},{"key":"10.1002\/prot.24338-BIB0080|prot24338-cit-0080","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1016\/j.bbrc.2009.02.103","article-title":"Amyloid fibrillation of hen egg-white lysozyme is inhibited by TCEP","volume":"381","author":"Wang","year":"2009","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1002\/prot.24338-BIB0081|prot24338-cit-0081","doi-asserted-by":"crossref","first-page":"10516","DOI":"10.1073\/pnas.0502515102","article-title":"Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis","volume":"102","author":"Rodriguez","year":"2005","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0082|prot24338-cit-0082","doi-asserted-by":"crossref","first-page":"e5004","DOI":"10.1371\/journal.pone.0005004","article-title":"Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase","volume":"4","author":"Oztug Durer","year":"2009","journal-title":"PLoS One"},{"key":"10.1002\/prot.24338-BIB0083|prot24338-cit-0083","first-page":"2645","article-title":"On the stability of bovine superoxide dismutase","volume":"248","author":"Forman","year":"1973","journal-title":"The effects of metals. J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0084|prot24338-cit-0084","doi-asserted-by":"crossref","first-page":"7043","DOI":"10.1016\/S0021-9258(19)44691-7","article-title":"Subunit structure of human superoxide dismutase","volume":"247","author":"Hartz","year":"1972","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0085|prot24338-cit-0085","first-page":"54558","article-title":"Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant","volume":"279","author":"Doucette","year":"2004","journal-title":"Insights into the molecular basis for dimer stability. J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0086|prot24338-cit-0086","doi-asserted-by":"crossref","first-page":"2333","DOI":"10.1074\/jbc.M506497200","article-title":"Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form","volume":"281","author":"Banci","year":"2006","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0087|prot24338-cit-0087","doi-asserted-by":"crossref","first-page":"47998","DOI":"10.1074\/jbc.M406021200","article-title":"The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status","volume":"279","author":"Arnesano","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0088|prot24338-cit-0088","doi-asserted-by":"crossref","first-page":"18663","DOI":"10.1073\/pnas.0807058105","article-title":"Initiation and elongation in fibrillation of ALS-linked superoxide dismutase","volume":"105","author":"Chattopadhyay","year":"2008","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0089|prot24338-cit-0089","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1016\/j.bbamcr.2006.05.003","article-title":"Activation of superoxide dismutases: putting the metal to the pedal","volume":"1763","author":"Culotta","year":"2006","journal-title":"Biochim Biophys Acta"},{"key":"10.1002\/prot.24338-BIB0090|prot24338-cit-0090","unstructured":"Dickinson AG Outram GW The scrapie replication-site hypothesis and its implications in the nervous system Prusiner SB Hadlow WJ New York Academic Press 1979 13 31"},{"key":"10.1002\/prot.24338-BIB0091|prot24338-cit-0091","doi-asserted-by":"crossref","first-page":"24167","DOI":"10.1074\/jbc.M802083200","article-title":"Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis","volume":"283","author":"Furukawa","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0092|prot24338-cit-0092","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1089\/ars.2006.8.847","article-title":"Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis","volume":"8","author":"Furukawa","year":"2006","journal-title":"Antioxid Redox Signal"},{"key":"10.1002\/prot.24338-BIB0093|prot24338-cit-0093","doi-asserted-by":"crossref","first-page":"13528","DOI":"10.1074\/jbc.M800564200","article-title":"A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis","volume":"283","author":"Karch","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0094|prot24338-cit-0094","doi-asserted-by":"crossref","first-page":"866","DOI":"10.1074\/jbc.M705657200","article-title":"Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis","volume":"283","author":"Cozzolino","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0095|prot24338-cit-0095","doi-asserted-by":"crossref","first-page":"e36989","DOI":"10.1371\/journal.pone.0036989","article-title":"Disulfide bridges remain intact while native insulin converts into amyloid fibrils","volume":"7","author":"Kurouski","year":"2012","journal-title":"PLoS One"},{"key":"10.1002\/prot.24338-BIB0096|prot24338-cit-0096","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S1016-8478(23)13808-8","article-title":"Role of disulfide bonds in the structure and activity of human insulin","volume":"16","author":"Chang","year":"2003","journal-title":"Mol Cells"},{"key":"10.1002\/prot.24338-BIB0097|prot24338-cit-0097","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1038\/nsb0295-129","article-title":"Structure of a protein in a kinetic trap","volume":"2","author":"Hua","year":"1995","journal-title":"Nat Struct Biol"},{"key":"10.1002\/prot.24338-BIB0098|prot24338-cit-0098","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1006\/jmbi.1996.0648","article-title":"Mapping the functional surface of insulin by design: structure and function of a novel A-chain analogue","volume":"264","author":"Hua","year":"1996","journal-title":"J Mol Biol"},{"key":"10.1002\/prot.24338-BIB0099|prot24338-cit-0099","doi-asserted-by":"crossref","first-page":"9196","DOI":"10.1073\/pnas.142459399","article-title":"The protofilament structure of insulin amyloid fibrils","volume":"99","author":"Jimenez","year":"2002","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0100|prot24338-cit-0100","doi-asserted-by":"crossref","first-page":"16701","DOI":"10.1021\/bi051658y","article-title":"Independent heterologous fibrillation of insulin and its B-chain peptide","volume":"44","author":"Hong","year":"2005","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0101|prot24338-cit-0101","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1023\/A:1018981208076","article-title":"Moisture-induced aggregation of lyophilized insulin","volume":"11","author":"Costantino","year":"1994","journal-title":"Pharm Res"},{"key":"10.1002\/prot.24338-BIB0102|prot24338-cit-0102","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1016\/j.bbrc.2012.05.133","article-title":"Dissecting the role of disulfide bonds on the amyloid formation of insulin","volume":"423","author":"Li","year":"2012","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1002\/prot.24338-BIB0103|prot24338-cit-0103","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1056\/NEJM200008103430607","article-title":"Islet amyloid and type 2 diabetes mellitus","volume":"343","author":"Hoppener","year":"2000","journal-title":"N Engl J Med"},{"key":"10.1002\/prot.24338-BIB0104|prot24338-cit-0104","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1007\/BF00274799","article-title":"Islet amyloid polypeptide-like immunoreactivity in the islet B cells of type 2 (non-insulin-dependent) diabetic and non-diabetic individuals","volume":"30","author":"Westermark","year":"1987","journal-title":"Diabetologia"},{"key":"10.1002\/prot.24338-BIB0105|prot24338-cit-0105","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/S0140-6736(87)90825-7","article-title":"Islet amyloid formed from diabetes-associated peptide may be pathogenic in type-2 diabetes","volume":"2","author":"Clark","year":"1987","journal-title":"Lancet"},{"key":"10.1002\/prot.24338-BIB0106|prot24338-cit-0106","doi-asserted-by":"crossref","first-page":"9662","DOI":"10.1073\/pnas.86.24.9662","article-title":"Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus","volume":"86","author":"Roberts","year":"1989","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0107|prot24338-cit-0107","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0167-0115(02)00252-5","article-title":"Islet amyloid polypeptide inhibits glucagon release and exerts a dual action on insulin release from isolated islets","volume":"111","author":"Akesson","year":"2003","journal-title":"Regul Pept"},{"key":"10.1002\/prot.24338-BIB0108|prot24338-cit-0108","doi-asserted-by":"crossref","first-page":"5035","DOI":"10.1210\/endo.142.11.8593","article-title":"Inhibition of central amylin signaling increases food intake and body adiposity in rats","volume":"142","author":"Rushing","year":"2001","journal-title":"Endocrinology"},{"key":"10.1002\/prot.24338-BIB0109|prot24338-cit-0109","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.jmb.2005.02.029","article-title":"The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin","volume":"348","author":"Kajava","year":"2005","journal-title":"J Mol Biol"},{"key":"10.1002\/prot.24338-BIB0110|prot24338-cit-0110","doi-asserted-by":"crossref","first-page":"13505","DOI":"10.1021\/bi701427q","article-title":"Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR","volume":"46","author":"Luca","year":"2007","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0111|prot24338-cit-0111","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/j.jmb.2008.05.013","article-title":"Prediction of aggregation-prone regions in structured proteins","volume":"380","author":"Tartaglia","year":"2008","journal-title":"J Mol Biol"},{"key":"10.1002\/prot.24338-BIB0112|prot24338-cit-0112","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1006\/jsbi.2000.4268","article-title":"Amyloid fibril formation from full-length and fragments of amylin","volume":"130","author":"Goldsbury","year":"2000","journal-title":"J Struct Biol"},{"key":"10.1002\/prot.24338-BIB0113|prot24338-cit-0113","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1110\/ps.041051205","article-title":"Contribution of the intrinsic disulfide to the assembly mechanism of islet amyloid","volume":"14","author":"Koo","year":"2005","journal-title":"Protein Sci"},{"key":"10.1002\/prot.24338-BIB0114|prot24338-cit-0114","doi-asserted-by":"crossref","first-page":"9900","DOI":"10.1021\/bi800828u","article-title":"Amylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state","volume":"47","author":"Yonemoto","year":"2008","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0115|prot24338-cit-0115","doi-asserted-by":"crossref","first-page":"7071","DOI":"10.1021\/jp100205w","article-title":"Effect of the disulfide bond on the monomeric structure of human amylin studied by combined Hamiltonian and temperature replica exchange molecular dynamics simulations","volume":"114","author":"Laghaei","year":"2010","journal-title":"J Phys Chem B"},{"key":"10.1002\/prot.24338-BIB0116|prot24338-cit-0116","doi-asserted-by":"crossref","first-page":"2948","DOI":"10.1016\/j.bpj.2009.08.041","article-title":"Evidence for a partially structured state of the amylin monomer","volume":"97","author":"Vaiana","year":"2009","journal-title":"Biophys J"},{"key":"10.1002\/prot.24338-BIB0117|prot24338-cit-0117","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/j.biotechadv.2004.09.002","article-title":"Formation of disulfide bonds in proteins and peptides","volume":"23","author":"Bulaj","year":"2005","journal-title":"Biotechnol Adv"},{"key":"10.1002\/prot.24338-BIB0118|prot24338-cit-0118","doi-asserted-by":"crossref","first-page":"7100","DOI":"10.1021\/bi100583x","article-title":"A disulfide-linked amyloid-beta peptide dimer forms a protofibril-like oligomer through a distinct pathway from amyloid fibril formation","volume":"49","author":"Yamaguchi","year":"2010","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0119|prot24338-cit-0119","doi-asserted-by":"crossref","first-page":"10128","DOI":"10.1074\/jbc.M307563200","article-title":"Tyrosine-to-cysteine modification of human alpha-synuclein enhances protein aggregation and cellular toxicity","volume":"279","author":"Zhou","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0120|prot24338-cit-0120","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.1021\/bi901753h","article-title":"The clustering and spatial arrangement of beta-sheet sequence, but not order, govern alpha-synuclein fibrillogenesis","volume":"49","author":"Suk","year":"2010","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0121|prot24338-cit-0121","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1016\/j.biotechadv.2011.07.013","article-title":"Disulfide bond formation and its impact on the biological activity and stability of recombinant therapeutic proteins produced by Escherichia coli expression system","volume":"29","author":"Zhang","year":"2011","journal-title":"Biotechnol Adv"},{"key":"10.1002\/prot.24338-BIB0122|prot24338-cit-0122","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1006\/jmbi.2000.3893","article-title":"What can disulfide bonds tell us about protein energetics, function and folding: simulations and bioninformatics analysis","volume":"300","author":"Abkevich","year":"2000","journal-title":"J Mol Biol"},{"key":"10.1002\/prot.24338-BIB0123|prot24338-cit-0123","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1126\/science.1072994","article-title":"The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics","volume":"297","author":"Hardy","year":"2002","journal-title":"Science"},{"key":"10.1002\/prot.24338-BIB0124|prot24338-cit-0124","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1038\/418291a","article-title":"Neurodegenerative disease: amyloid pores from pathogenic mutations","volume":"418","author":"Lashuel","year":"2002","journal-title":"Nature"},{"key":"10.1002\/prot.24338-BIB0125|prot24338-cit-0125","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1074\/jbc.M505091200","article-title":"Scanning cysteine mutagenesis analysis of Abeta-(1-40) amyloid fibrils","volume":"281","author":"Shivaprasad","year":"2006","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0126|prot24338-cit-0126","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1021\/bi051952q","article-title":"Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils","volume":"45","author":"Petkova","year":"2006","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0127|prot24338-cit-0127","doi-asserted-by":"crossref","first-page":"35317","DOI":"10.1074\/jbc.M303547200","article-title":"Alzheimer beta-amyloid homodimers facilitate A beta fibrillization and the generation of conformational antibodies","volume":"278","author":"Schmechel","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0128|prot24338-cit-0128","doi-asserted-by":"crossref","first-page":"15310","DOI":"10.1021\/bi048019s","article-title":"An intersheet packing interaction in A beta fibrils mapped by disulfide cross-linking","volume":"43","author":"Shivaprasad","year":"2004","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0129|prot24338-cit-0129","doi-asserted-by":"crossref","first-page":"15595","DOI":"10.1073\/pnas.1001740107","article-title":"Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering","volume":"107","author":"Sandberg","year":"2010","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0130|prot24338-cit-0130","doi-asserted-by":"crossref","first-page":"507","DOI":"10.2174\/138920308785915218","article-title":"Alpha-synuclein misfolding and neurodegenerative diseases","volume":"9","author":"Uversky","year":"2008","journal-title":"Curr Protein Pept Sci"},{"key":"10.1002\/prot.24338-BIB0131|prot24338-cit-0131","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1097\/00005072-199603000-00001","article-title":"Neuropathology of Parkinson's disease","volume":"55","author":"Forno","year":"1996","journal-title":"J Neuropathol Exp Neurol"},{"key":"10.1002\/prot.24338-BIB0132|prot24338-cit-0132","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1126\/science.276.5321.2045","article-title":"Mutation in the alpha-synuclein gene identified in families with Parkinson's disease","volume":"276","author":"Polymeropoulos","year":"1997","journal-title":"Science"},{"key":"10.1002\/prot.24338-BIB0133|prot24338-cit-0133","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1038\/ng0298-106","article-title":"Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease","volume":"18","author":"Kruger","year":"1998","journal-title":"Nat Genet"},{"key":"10.1002\/prot.24338-BIB0134|prot24338-cit-0134","doi-asserted-by":"crossref","first-page":"16873","DOI":"10.1074\/jbc.M210136200","article-title":"Lipid binding inhibits alpha-synuclein fibril formation","volume":"278","author":"Zhu","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1002\/prot.24338-BIB0135|prot24338-cit-0135","doi-asserted-by":"crossref","first-page":"13322","DOI":"10.1021\/bi7014053","article-title":"Role of different regions of alpha-synuclein in the assembly of fibrils","volume":"46","author":"Qin","year":"2007","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0136|prot24338-cit-0136","doi-asserted-by":"crossref","first-page":"1430","DOI":"10.1073\/pnas.0407146102","article-title":"Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein","volume":"102","author":"Bertoncini","year":"2005","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1002\/prot.24338-BIB0137|prot24338-cit-0137","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/S0014-5793(01)03121-0","article-title":"Trimethylamine-N-oxide-induced folding of alpha-synuclein","volume":"509","author":"Uversky","year":"2001","journal-title":"FEBS Lett"},{"key":"10.1002\/prot.24338-BIB0138|prot24338-cit-0138","doi-asserted-by":"crossref","first-page":"11604","DOI":"10.1021\/bi010616g","article-title":"Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein","volume":"40","author":"Li","year":"2001","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0139|prot24338-cit-0139","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/S0161-813X(02)00066-9","article-title":"Conformational behavior of human alpha-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T","volume":"23","author":"Li","year":"2002","journal-title":"Neurotoxicology"},{"key":"10.1002\/prot.24338-BIB0140|prot24338-cit-0140","doi-asserted-by":"crossref","first-page":"2720","DOI":"10.1021\/bi027166s","article-title":"Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membranes","volume":"42","author":"Munishkina","year":"2003","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0141|prot24338-cit-0141","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1021\/bi062068i","article-title":"Isomers of human alpha-synuclein stabilized by disulfide bonds exhibit distinct structural and aggregative properties","volume":"46","author":"Jiang","year":"2007","journal-title":"Biochemistry"},{"key":"10.1002\/prot.24338-BIB0142|prot24338-cit-0142","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1016\/j.febslet.2011.01.009","article-title":"The role of the C-terminus of human alpha-synuclein: Intra-disulfide bonds between the C-terminus and other regions stabilize non-fibrillar monomeric isomers","volume":"585","author":"Hong","year":"2011","journal-title":"FEBS Lett"}],"container-title":["Proteins: Structure, Function, and Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fprot.24338","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fprot.24338","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/onlinelibrary.wiley.com\/wol1\/doi\/10.1002\/prot.24338\/fullpdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,5,12]],"date-time":"2024-05-12T09:05:40Z","timestamp":1715504740000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/prot.24338"}},"subtitle":["Disulfide and Amyloidogenecity"],"short-title":[],"issued":{"date-parts":[[2013,8,19]]},"references-count":142,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2013,11]]}},"URL":"https:\/\/doi.org\/10.1002\/prot.24338","archive":["Portico"],"relation":{},"ISSN":["0887-3585"],"issn-type":[{"value":"0887-3585","type":"print"}],"subject":[],"published":{"date-parts":[[2013,8,19]]}}}