{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T17:58:16Z","timestamp":1792173496962,"version":"4.4.0"},"reference-count":53,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2018,1,1]],"date-time":"2018-01-01T00:00:00Z","timestamp":1514764800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,27]],"date-time":"2020-08-27T00:00:00Z","timestamp":1598486400000},"content-version":"vor","delay-in-days":969,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["ZIA HL001055-10"],"award-info":[{"award-number":["ZIA HL001055-10"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2018,1]]},"DOI":"10.1074\/jbc.m117.812388","type":"journal-article","created":{"date-parts":[[2017,11,30]],"date-time":"2017-11-30T20:15:23Z","timestamp":1512072923000},"page":"767-776","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":115,"title":["Structural features of \u03b1-synuclein amyloid fibrils revealed by Raman spectroscopy"],"prefix":"10.1016","volume":"293","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9310-4882","authenticated-orcid":false,"given":"Jessica D.","family":"Flynn","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryan P.","family":"McGlinchey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"suffix":"III","given":"Robert L.","family":"Walker","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0506-8349","authenticated-orcid":false,"given":"Jennifer C.","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M117.812388_bib1","doi-asserted-by":"crossref","first-page":"2055","DOI":"10.1016\/S0140-6736(09)60492-X","article-title":"Parkinson's disease","volume":"373","author":"Lees","year":"2009","journal-title":"Lancet"},{"key":"10.1074\/jbc.M117.812388_bib2","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1038\/nrn983","article-title":"Pathogenesis of Parkinson's disease: dopamine, vesicles and \u03b1-synuclein","volume":"3","author":"Lotharius","year":"2002","journal-title":"Nat. Rev. Neurosci"},{"key":"10.1074\/jbc.M117.812388_bib3","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. Rev. Biochem"},{"key":"10.1074\/jbc.M117.812388_bib4","doi-asserted-by":"crossref","first-page":"S16","DOI":"10.1016\/j.parkreldis.2015.08.015","article-title":"Phenotypic spectrum of \u03b1-synuclein mutations: new insights from patients and cellular models","volume":"22","author":"Petrucci","year":"2016","journal-title":"Parkinsonism Relat. Disord"},{"key":"10.1074\/jbc.M117.812388_bib5","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1126\/science.276.5321.2045","article-title":"Mutation in the \u03b1-synuclein gene identified in families with Parkinson's disease","volume":"276","author":"Polymeropoulos","year":"1997","journal-title":"Science"},{"key":"10.1074\/jbc.M117.812388_bib6","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.arr.2014.04.002","article-title":"Genetic variants and animal models in SNCA and Parkinson disease","volume":"15","author":"Deng","year":"2014","journal-title":"Ageing Res. Rev"},{"key":"10.1074\/jbc.M117.812388_bib7","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1021\/bi991447r","article-title":"Fibrils formed in vitro from \u03b1-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid","volume":"39","author":"Conway","year":"2000","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M117.812388_bib8","doi-asserted-by":"crossref","first-page":"9843","DOI":"10.1074\/jbc.274.14.9843","article-title":"Both familial Parkinson's disease mutations accelerate \u03b1-synuclein aggregation","volume":"274","author":"Narhi","year":"1999","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.812388_bib9","doi-asserted-by":"crossref","first-page":"1318","DOI":"10.1038\/3311","article-title":"Accelerated in vitro fibril formation by a mutant \u03b1-synuclein linked to early-onset Parkinson disease","volume":"4","author":"Conway","year":"1998","journal-title":"Nat. Med"},{"key":"10.1074\/jbc.M117.812388_bib10","doi-asserted-by":"crossref","first-page":"6925","DOI":"10.1021\/bi400999d","article-title":"The Parkinson's disease-associated H50Q mutation accelerates \u03b1-synuclein aggregation in vitro","volume":"52","author":"Ghosh","year":"2013","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M117.812388_bib11","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 \u03b1-synuclein","volume":"40","author":"Li","year":"2001","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M117.812388_bib12","doi-asserted-by":"crossref","first-page":"7800","DOI":"10.1074\/jbc.M411638200","article-title":"The E46K mutation in \u03b1-synuclein increases amyloid fibril formation","volume":"280","author":"Greenbaum","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.812388_bib13","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1002\/ana.23894","article-title":"G51D \u03b1-synuclein mutation causes a novel Parkinsonian-pyramidal syndrome","volume":"73","author":"Lesage","year":"2013","journal-title":"Ann. Neurol"},{"key":"10.1074\/jbc.M117.812388_bib14","doi-asserted-by":"crossref","first-page":"2235","DOI":"10.1021\/acschemneuro.7b00149","article-title":"Perturbation in long-range contacts modulates kinetics of amyloid formation in \u03b1-synuclein familial mutants","volume":"8","author":"Ranjan","year":"2017","journal-title":"ACS Chem. Neurosci"},{"key":"10.1074\/jbc.M117.812388_bib15","doi-asserted-by":"crossref","first-page":"E4","DOI":"10.1038\/nature12125","article-title":"Properties of native brain \u03b1-synuclein","volume":"498","author":"Burr\u00e9","year":"2013","journal-title":"Nature"},{"key":"10.1074\/jbc.M117.812388_bib16","doi-asserted-by":"crossref","first-page":"E4274","DOI":"10.1073\/pnas.1416598111","article-title":"\u03b1-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE","volume":"111","author":"Burr\u00e9","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M117.812388_bib17","doi-asserted-by":"crossref","first-page":"6371","DOI":"10.1074\/jbc.M112.403311","article-title":"In vivo cross-linking reveals principally oligomeric forms of \u03b1-synuclein and \u03b2-synuclein in neurons and non-neural cells","volume":"288","author":"Dettmer","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.812388_bib18","first-page":"1","article-title":"\u03b1-Synuclein in Parkinson's disease","volume":"4","author":"Stefanis","year":"2014","journal-title":"Cold Spring Harb. Perspect. Med"},{"key":"10.1074\/jbc.M117.812388_bib19","doi-asserted-by":"crossref","first-page":"24526","DOI":"10.1038\/srep24526","article-title":"Structural and functional properties of prefibrillar \u03b1-synuclein oligomers","volume":"6","author":"Pieri","year":"2016","journal-title":"Sci. Rep"},{"key":"10.1074\/jbc.M117.812388_bib20","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1038\/nrn3406","article-title":"The many faces of \u03b1-synuclein: from structure and toxicity to therapeutic target","volume":"14","author":"Lashuel","year":"2013","journal-title":"Nat. Rev. Neurosci"},{"key":"10.1074\/jbc.M117.812388_bib21","doi-asserted-by":"crossref","first-page":"15345","DOI":"10.1074\/jbc.M111.318949","article-title":"\u03b1-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer","volume":"287","author":"Fauvet","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.812388_bib22","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/S0304-3940(00)01440-3","article-title":"Characterisation of isolated \u03b1-synuclein filaments from substantia nigra of Parkinson's disease brain","volume":"292","author":"Crowther","year":"2000","journal-title":"Neurosci. Lett"},{"key":"10.1074\/jbc.M117.812388_bib23","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1038\/nsmb.3194","article-title":"Solid-state NMR structure of a pathogenic fibril of full-length human \u03b1-synuclein","volume":"23","author":"Tuttle","year":"2016","journal-title":"Nat. Struct. Mol. Biol"},{"key":"10.1074\/jbc.M117.812388_bib24","doi-asserted-by":"crossref","first-page":"4897","DOI":"10.1073\/pnas.97.9.4897","article-title":"Fiber diffraction of synthetic \u03b1-synuclein filaments shows amyloid-like cross-beta conformation","volume":"97","author":"Serpell","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M117.812388_bib25","doi-asserted-by":"crossref","first-page":"24970","DOI":"10.1074\/jbc.M700368200","article-title":"Investigation of \u03b1-synuclein fibril structure by site-directed spin labeling","volume":"282","author":"Chen","year":"2007","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.812388_bib26","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1038\/nature15368","article-title":"Structure of the toxic core of \u03b1-synuclein from invisible crystals","volume":"525","author":"Rodriguez","year":"2015","journal-title":"Nature"},{"key":"10.1074\/jbc.M117.812388_bib27","doi-asserted-by":"crossref","first-page":"2310","DOI":"10.1074\/jbc.M115.698787","article-title":"\u03b1-Synuclein amyloid fibrils with two entwined, asymmetrically associated protofibrils","volume":"291","author":"Dearborn","year":"2016","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.812388_bib28","doi-asserted-by":"crossref","first-page":"8637","DOI":"10.1073\/pnas.0712179105","article-title":"The fold of \u03b1-synuclein fibrils","volume":"105","author":"Vilar","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M117.812388_bib29","doi-asserted-by":"crossref","first-page":"15871","DOI":"10.1073\/pnas.0506109102","article-title":"Molecular-level secondary structure, polymorphism, and dynamics of full-length \u03b1-synuclein fibrils studied by solid-state NMR","volume":"102","author":"Heise","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M117.812388_bib30","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1038\/nature14547","article-title":"\u03b1-Synuclein strains cause distinct synucleinopathies after local and systemic administration","volume":"522","author":"Peelaerts","year":"2015","journal-title":"Nature"},{"key":"10.1074\/jbc.M117.812388_bib31","doi-asserted-by":"crossref","first-page":"22715","DOI":"10.1074\/jbc.M011499200","article-title":"Is Congo Red an amyloid-specific dye?","volume":"276","author":"Khurana","year":"2001","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.812388_bib32","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1002\/pro.5560020312","article-title":"Thioflavine T interaction with synthetic Alzheimer's disease \u03b2-amyloid peptides: detection of amyloid aggregation in solution","volume":"2","author":"Levine","year":"1993","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.M117.812388_bib33","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.bbamem.2011.07.032","article-title":"Biophysics of \u03b1-synuclein membrane interactions","volume":"1818","author":"Pfefferkorn","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.M117.812388_bib34","doi-asserted-by":"crossref","first-page":"9322","DOI":"10.1073\/pnas.1500937112","article-title":"Cysteine cathepsins are essential in lysosomal degradation of \u03b1-synuclein","volume":"112","author":"McGlinchey","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M117.812388_bib35","doi-asserted-by":"crossref","first-page":"3881","DOI":"10.1021\/acs.biochem.7b00360","article-title":"Taking a bite out of amyloid: Mechanistic insights into \u03b1-synuclein degradation by cathepsin L","volume":"56","author":"McGlinchey","year":"2017","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M117.812388_bib36","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.pep.2006.02.009","article-title":"Preparation of \u03b1-synuclein fibrils for solid-state NMR: expression, purification, and incubation of wild-type and mutant forms","volume":"48","author":"Kloepper","year":"2006","journal-title":"Protein Expr. Purif"},{"key":"10.1074\/jbc.M117.812388_bib37","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1146\/annurev.physchem.57.032905.104521","article-title":"Raman crystallography and other biochemical applications of Raman microscopy","volume":"57","author":"Carey","year":"2006","journal-title":"Annu. Rev. Phys. Chem"},{"key":"10.1074\/jbc.M117.812388_bib38","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1002\/jrs.4335","article-title":"Raman spectroscopy of proteins: a review","volume":"44","author":"Rygula","year":"2013","journal-title":"J. Raman Spectrosc"},{"key":"10.1074\/jbc.M117.812388_bib39","doi-asserted-by":"crossref","first-page":"4967","DOI":"10.1039\/C5AN00342C","article-title":"Exploring structure and formation mechanism of amyloid fibrils by Raman spectroscopy","volume":"140","author":"Kurouski","year":"2015","journal-title":"Analyst"},{"key":"10.1074\/jbc.M117.812388_bib40","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1016\/j.jsb.2017.06.002","article-title":"Tracking the amyloidogenic core of IAPP amyloid fibrils: insights from micro-Raman spectroscopy","volume":"199","author":"Louros","year":"2017","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.M117.812388_bib41","doi-asserted-by":"crossref","first-page":"2399","DOI":"10.1021\/ja0356176","article-title":"Raman spectroscopic characterization of secondary structure in natively unfolded proteins: \u03b1-synuclein","volume":"126","author":"Maiti","year":"2004","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M117.812388_bib42","doi-asserted-by":"crossref","first-page":"910","DOI":"10.1002\/jrs.5149","article-title":"Raman optical activity of human \u03b1-synuclein in intrinsically disordered, micelle-bound \u03b1-helical, molten globule and oligomeric \u03b2-sheet state","volume":"48","author":"Mensch","year":"2017","journal-title":"J. Raman Spectrosc"},{"key":"10.1074\/jbc.M117.812388_bib43","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.jmb.2005.10.071","article-title":"Secondary structure of \u03b1-synuclein oligomers: characterization by Raman and atomic force microscopy","volume":"355","author":"Apetri","year":"2006","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M117.812388_bib44","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/0003-2697(89)90046-8","article-title":"Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T","volume":"177","author":"Naiki","year":"1989","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.M117.812388_bib45","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/S0076-6879(99)09020-5","article-title":"Quantification of \u03b2-sheet amyloid fibril structures with thioflavin T","volume":"309","author":"LeVine","year":"1999","journal-title":"Methods Enzymol"},{"key":"10.1074\/jbc.M117.812388_bib46","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":"Uversky","year":"2001","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M117.812388_bib47","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1529\/biophysj.105.066761","article-title":"micro-Raman spectroscopy detects individual neoplastic and normal hematopoietic cells","volume":"90","author":"Chan","year":"2006","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.M117.812388_bib48","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1080\/05704920701551530","article-title":"Raman spectroscopy of biological tissues","volume":"42","author":"Movasaghi","year":"2007","journal-title":"Appl. Spectrosc. Rev"},{"key":"10.1074\/jbc.M117.812388_bib49","doi-asserted-by":"crossref","first-page":"9228","DOI":"10.1038\/srep09228","article-title":"Structure based aggregation studies reveal the presence of helix-rich intermediate during \u03b1-synuclein aggregation","volume":"5","author":"Ghosh","year":"2015","journal-title":"Sci. Rep"},{"key":"10.1074\/jbc.M117.812388_bib50","doi-asserted-by":"crossref","first-page":"10019","DOI":"10.1021\/ja021464v","article-title":"A new perspective on \u03b2-sheet structures using vibrational Raman optical activity: from poly(l-lysine) to the prion protein","volume":"125","author":"McColl","year":"2003","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M117.812388_bib51","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1016\/j.jmb.2011.06.026","article-title":"Structured regions of \u03b1-synuclein fibrils include the early-onset Parkinson's disease mutation sites","volume":"411","author":"Comellas","year":"2011","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M117.812388_bib52","doi-asserted-by":"crossref","first-page":"2575","DOI":"10.1038\/ncomms3575","article-title":"Structural and functional characterization of two \u03b1-synuclein strains","volume":"4","author":"Bousset","year":"2013","journal-title":"Nat. Commun"},{"key":"10.1074\/jbc.M117.812388_bib53","doi-asserted-by":"crossref","first-page":"4615","DOI":"10.1021\/jp908092e","article-title":"Tryptophan probes at the \u03b1-synuclein and membrane interface","volume":"114","author":"Pfefferkorn","year":"2010","journal-title":"J. Phys. Chem. B"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820396538?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820396538?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M117.812388","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,3,15]],"date-time":"2024-03-15T01:43:58Z","timestamp":1710467038000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820396538"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,1]]},"references-count":53,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2018,1]]}},"alternative-id":["S0021925820396538"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m117.812388","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2018,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural features of \u03b1-synuclein amyloid fibrils revealed by Raman spectroscopy","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.M117.812388","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"name":"copyright","label":"Copyright"}]}}