{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T05:14:49Z","timestamp":1777439689323,"version":"3.51.4"},"reference-count":58,"publisher":"Public Library of Science (PLoS)","issue":"12","license":[{"start":{"date-parts":[[2012,12,13]],"date-time":"2012-12-13T00:00:00Z","timestamp":1355356800000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0050027","type":"journal-article","created":{"date-parts":[[2012,12,13]],"date-time":"2012-12-13T22:04:35Z","timestamp":1355436275000},"page":"e50027","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":37,"title":["Covalent \u03b1-Synuclein Dimers: Chemico-Physical and Aggregation Properties"],"prefix":"10.1371","volume":"7","author":[{"given":"Micaela","family":"Pivato","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Giorgia","family":"De Franceschi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Laura","family":"Tosatto","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Erica","family":"Frare","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dhruv","family":"Kumar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel","family":"Aioanei","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marco","family":"Brucale","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Isabella","family":"Tessari","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marco","family":"Bisaglia","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bruno","family":"Samori","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Patrizia Polverino","family":"de Laureto","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Luigi","family":"Bubacco","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2012,12,13]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/42166","article-title":"Alpha-synuclein in Lewy bodies","volume":"388","author":"MG Spillantini","year":"1997","journal-title":"Nature"},{"key":"ref2","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":"MG Spillantini","year":"1998","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1016\/0022-2836(68)90014-4","article-title":"Cross-\u03b2 conformation in proteins","volume":"32","author":"AJ Geddes","year":"1968","journal-title":"J Mol Biol"},{"key":"ref4","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":"MH Polymeropoulos","year":"1997","journal-title":"Science"},{"key":"ref5","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":"R Krueger","year":"1998","journal-title":"Nat Genet"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1002\/ana.10795","article-title":"The new mutation, E46K, of \u03b1-synuclein causes Parkinson and Lewy Body Dementia","volume":"55","author":"JJ Zarranz","year":"2003","journal-title":"Ann Neurobiol"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1126\/science.1090278","article-title":"alpha-Synuclein locus triplication causes Parkinson's disease","volume":"302","author":"AB Singleton","year":"2003","journal-title":"Science"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1016\/S0140-6736(04)17103-1","article-title":"\u03b1-Synuclein locus duplication as a cause of familiar Parkinson's disease","volume":"364","author":"MC Chartier-Harlin","year":"2004","journal-title":"The Lancet"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1186\/1750-1326-4-9","article-title":"\u03b1-Synuclein and neuronal cell death","volume":"4","author":"MR Cookson","year":"2009","journal-title":"Mol Neurodegen"},{"key":"ref10","first-page":"282","article-title":"Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease","volume":"23","author":"K Ueda","year":"1993","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/1074-5521(95)90071-3","article-title":"The core Alzheimer's peptide NAC forms amyloid fibrils which seed and ae seeded by beta-amyloid: is NAC a common trigger or target in neurodegenerative disease?","volume":"2","author":"H Han","year":"1995","journal-title":"Chem Biol"},{"key":"ref12","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":"J Li","year":"2001","journal-title":"Biochemistry"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1006\/jmbi.1999.3110","article-title":"Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm","volume":"293","author":"PE Wright","year":"1999","journal-title":"J Mol Biol"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1080\/07391102.2003.10506918","article-title":"A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders","volume":"21","author":"VN Uversky","year":"2003","journal-title":"J Biomol Struct Dyn"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"43495","DOI":"10.1074\/jbc.C100551200","article-title":"Stabilization of partially folded conformation during alpha-synuclein oligomerization in both purified and cytosolic preparations","volume":"276","author":"VN Uversky","year":"2001","journal-title":"J Biol Chem"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"10737","DOI":"10.1074\/jbc.M010907200","article-title":"Evidence for a Partially Folded Intermediate in \u03b1-Synuclein Fibril Formation","volume":"276","author":"VN Uversky","year":"2001","journal-title":"J Biol Chem"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1021\/ja044834j","article-title":"Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations","volume":"127","author":"MM Dedmon","year":"2005","journal-title":"J Am Chem Soc"},{"key":"ref18","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":"CW Bertoncini","year":"2005","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1038\/nature10324","article-title":"\u03b1-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation","volume":"477","author":"T Bartels","year":"2011","journal-title":"Nature"},{"key":"ref20","first-page":"2336","article-title":"A soluble \u03b1 synuclein construct forms a dynamic tetramer","volume":"109","author":"W Wang","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"15345","DOI":"10.1074\/jbc.M111.318949","article-title":"Alpha-synuclein in the central nervous system and from erythrocytes, mammalian cells and E. coli exists predominantly as a disordered monomer","volume":"287","author":"B Fauvet","year":"2012","journal-title":"J Biol Chem"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"12345","DOI":"10.1021\/bi00164a008","article-title":"Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB","volume":"31","author":"JT Jarret","year":"1992","journal-title":"Biochemistry"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"19509","DOI":"10.1074\/jbc.274.28.19509","article-title":"\u03b1-Synuclein fibrillogenesis is nucleation dependent","volume":"278","author":"SJ Wood","year":"1999","journal-title":"J Biol Chem"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1016\/j.cell.2012.03.037","article-title":"Direct observation of the interconversion of normal and toxic forms of \u03b1-synuclein","volume":"25","author":"N Cremandes","year":"2012","journal-title":"Cell"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"18344","DOI":"10.1074\/jbc.M000206200","article-title":"Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies","volume":"275","author":"JM Souza","year":"2000","journal-title":"J Biol Chem"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/S0006-8993(02)02498-8","article-title":"Tyrosine 125 of \u03b1-synuclein plays a critical role for dimerization following nitrative stress","volume":"938","author":"T Takahashi","year":"2002","journal-title":"Brain Res"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1021\/bi026528t","article-title":"Oxidative dimer formation is the critical rate-limiting step for Parkinson's disease \u03b1-synuclein fibrillogenesis","volume":"42","author":"S Krishnan","year":"2003","journal-title":"Biochemistry"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.jmb.2009.09.008","article-title":"Molecular insights into the interaction between \u03b1-synuclein and docosahexaenoic acid","volume":"394","author":"G De Franceschi","year":"2009","journal-title":"J Mol Biol"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/0003-2697(89)90602-7","article-title":"Calculation of protein extinction coefficients from amino acid sequence data","volume":"182","author":"SC Gill","year":"1989","journal-title":"Anal Biochem"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1002\/bip.360250307","article-title":"Examination of the secondary structure of proteins by deconvolved FTIR spectra","volume":"25","author":"DM Byler","year":"1986","journal-title":"Biopolymers"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/0079-6107(93)90006-6","article-title":"Quantitative studies ofthe structure ofproteins in solution by Fourier-transform infrared-spectroscopy","volume":"59","author":"JLR Arrondo","year":"1993","journal-title":"Prog Biophys Mol Biol"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1002\/pro.5560020312","article-title":"Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution","volume":"2","author":"H LeVine","year":"1993","journal-title":"Protein Sci"},{"key":"ref33","doi-asserted-by":"crossref","unstructured":"Aioanei D (2012) Lazy Shortest Path Computation in Dynamic Graphs. Computer Science, AGH University of Science and Technology Press, ISSN 1508\u20132806.","DOI":"10.7494\/csci.2012.13.3.113"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"13709","DOI":"10.1021\/bi961799n","article-title":"NACP, a protein implicated in Alzheimer disease comprehension and learning, is natively unfolded","volume":"35","author":"PH Weinreb","year":"1996","journal-title":"Biochemistry"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1021\/bi00053a001","article-title":"Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment","volume":"32","author":"WK Surewicz","year":"1993","journal-title":"Biochemistry"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1042\/bj3190741","article-title":"Fourier transform IR spectroscopic study of hydration-induced structure changes in the solid state of x-gliadins","volume":"319","author":"N Wellner","year":"1996","journal-title":"Biochemistry J"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/S0079-6107(00)00021-3","article-title":"The infrared absorption of amino acid side chains","volume":"74","author":"A Barth","year":"2000","journal-title":"Prog Biophys & Mol Biol"},{"key":"ref38","first-page":"1243","article-title":"Biopolymers","volume":"30","author":"SY Venyaminov","year":"1990","journal-title":"Biopolymers"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"2937","DOI":"10.1111\/j.1432-1033.2004.04220.x","article-title":"The optimization of protein secondary structure determination with infrared and circular dichroism spectra","volume":"271","author":"KA Oberg","year":"2004","journal-title":"Eur J Biochem"},{"key":"ref40","first-page":"783","article-title":"Rapid characterization of peptide secondary structure by FT-IR spectroscopy","volume":"56","author":"A Adochitei","year":"2011","journal-title":"Rev Roum Chim"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"1513","DOI":"10.1366\/0003702934067469","article-title":"Infrared spectroscopic characterization of Alzheimer plaques","volume":"47","author":"H Fabian","year":"1993","journal-title":"Applied Spectroscopy"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"4409","DOI":"10.1021\/bi602461y","article-title":"\u03b1-Synuclein multistate folding thermodynamics: implications for the protein misfolding and aggregation","volume":"46","author":"AC Ferreon","year":"2007","journal-title":"Biochemistry"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"12522","DOI":"10.1021\/bi701128c","article-title":"Sensitive fluorescence polarization technique for rapid screening of \u03b1-synuclein oligomerization\/fibrillization inhibitors","volume":"46","author":"CK Luk","year":"2007","journal-title":"Biochemistry"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/j.jmb.2006.06.055","article-title":"Identification of the core structure of lysozyme amyloid fibrils by proteolysis","volume":"361","author":"E Frare","year":"2006","journal-title":"J Mol Biol"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"4871","DOI":"10.1529\/biophysj.107.127464","article-title":"Concentration dependence of \u03b1-synuclein fibril length assessed by quantitative atomic force microscopy and statistical-mechanical theory","volume":"95","author":"ME van Raaij","year":"2008","journal-title":"Biophys J"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1021\/ar050073t","article-title":"The aggregation and fibrillation of \u03b1-synuclein","volume":"39","author":"AL Fink","year":"2006","journal-title":"Acc Chem Res"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"299","DOI":"10.18388\/abp.2004_3573","article-title":"Probing protein structure by limited proteolysis","volume":"51","author":"A Fontana","year":"2004","journal-title":"Acta Biochim Pol"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.jmb.2003.09.024","article-title":"Protein Aggregation and Amyloid Fibril Formation by an SH3 Domain Probed by Limited Proteolysis","volume":"334","author":"P Polverino de Laureto","year":"2003","journal-title":"J Mol Biol"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1111\/j.1432-1033.1974.tb03671.x","article-title":"Proteinase K from Tritirachium album Limber","volume":"47","author":"W Ebeling","year":"1974","journal-title":"Eur J Biochem"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"19213","DOI":"10.1074\/jbc.M110551200","article-title":"Biochemical characterization of the core structure of alpha-synuclein filaments","volume":"277","author":"H Miake","year":"2002","journal-title":"J Biol Chem"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"13322","DOI":"10.1021\/bi7014053","article-title":"Role of different regions of \u03b1-synuclein in the assembly of fibrils","volume":"46","author":"Z Qin","year":"2007","journal-title":"Biochemistry"},{"key":"ref52","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":"W Zhou","year":"2004","journal-title":"J Biol Chem"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"9863","DOI":"10.1074\/jbc.M710232200","article-title":"Transgenic mice overexpressing tyrosine-to-cysteine mutant human alpha-synuclein: a progressive neurodegenerative model of diffuse Lewy body disease","volume":"283","author":"W Zhou","year":"2008","journal-title":"J Biol Chem"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"13353","DOI":"10.1021\/jp077036z","article-title":"Solid-state NMR spectroscopy reveals that water is nonessential to the core structure of \u03b1-synuclein fibrils","volume":"111","author":"KD Kloepper","year":"2007","journal-title":"J Physical Chem"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"8637","DOI":"10.1073\/pnas.0712179105","article-title":"The fold of \u03b1-synuclein fibrils","volume":"105","author":"M Vilar","year":"2008","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref56","first-page":"L01","article-title":"Electron paramagnetic resonance spectroscopy measures the distance between the external \u03b2-strands of folded \u03b1-synuclein in amyloid fibrils","author":"I Karyagina","year":"2011","journal-title":"Biophy J"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"4897","DOI":"10.1073\/pnas.97.9.4897","article-title":"Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation","volume":"25","author":"LC Serpell","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1016\/j.bbrc.2008.01.091","article-title":"Assembly of alpha-synuclein fibrils in nanoscale studied by peptide truncation and AFM","volume":"368","author":"F Zhang","year":"2008","journal-title":"Biochem Biophys Res Commun"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0050027","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,7,18]],"date-time":"2020-07-18T19:08:12Z","timestamp":1595099292000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0050027"}},"subtitle":[],"editor":[{"given":"Vladimir N.","family":"Uversky","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2012,12,13]]},"references-count":58,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2012,12,13]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0050027","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2012,12,13]]}}}