{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T10:24:45Z","timestamp":1791282285127,"version":"4.1.0"},"reference-count":63,"publisher":"Elsevier BV","issue":"17","license":[{"start":{"date-parts":[[2017,4,1]],"date-time":"2017-04-01T00:00:00Z","timestamp":1491004800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,11,12]],"date-time":"2020-11-12T00:00:00Z","timestamp":1605139200000},"content-version":"vor","delay-in-days":1321,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003500","name":"Universit\u00e0 degli Studi di Padova","doi-asserted-by":"publisher","award":["CPDA125928\/12"],"award-info":[{"award-number":["CPDA125928\/12"]}],"id":[{"id":"10.13039\/501100003500","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002803","name":"Fondazione Cariplo","doi-asserted-by":"publisher","award":["2013\u20130964"],"award-info":[{"award-number":["2013\u20130964"]}],"id":[{"id":"10.13039\/501100002803","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000272","name":"National Institute for Health Research","doi-asserted-by":"publisher","award":["MR\/M006646\/1"],"award-info":[{"award-number":["MR\/M006646\/1"]}],"id":[{"id":"10.13039\/501100000272","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":[[2017,4]]},"DOI":"10.1074\/jbc.m116.765149","type":"journal-article","created":{"date-parts":[[2017,2,24]],"date-time":"2017-02-24T01:10:22Z","timestamp":1487898622000},"page":"6927-6937","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":35,"title":["\u03b1-Synuclein structural features inhibit harmful polyunsaturated fatty acid oxidation, suggesting roles in neuroprotection"],"prefix":"10.1016","volume":"292","author":[{"given":"Giorgia","family":"De Franceschi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chiara","family":"Fecchio","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronit","family":"Sharon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3018-3966","authenticated-orcid":false,"given":"Anthony H.V.","family":"Schapira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6423-6539","authenticated-orcid":false,"given":"Christos","family":"Proukakis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0467-864X","authenticated-orcid":false,"given":"Vittorio","family":"Bellotti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0367-6781","authenticated-orcid":false,"given":"Patrizia Polverino","family":"de Laureto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M116.765149_bib1","doi-asserted-by":"crossref","first-page":"6469","DOI":"10.1073\/pnas.95.11.6469","article-title":"\u03b1-Synuclein in filamentous inclusions of Lewy bodies from Parkinson\u2019s disease and dementia with Lewy bodies","volume":"95","author":"Spillantini","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.765149_bib2","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\u2019s disease","volume":"276","author":"Polymeropoulos","year":"1997","journal-title":"Science"},{"key":"10.1074\/jbc.M116.765149_bib3","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":"Kr\u00fcger","year":"1998","journal-title":"Nat. Genet"},{"key":"10.1074\/jbc.M116.765149_bib4","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":"Zarranz","year":"2004","journal-title":"Ann. Neurol"},{"key":"10.1074\/jbc.M116.765149_bib5","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1126\/science.1090278","article-title":"\u03b1-Synuclein locus triplication causes Parkinson\u2019s disease","volume":"302","author":"Singleton","year":"2003","journal-title":"Science"},{"key":"10.1074\/jbc.M116.765149_bib6","doi-asserted-by":"crossref","first-page":"13709","DOI":"10.1021\/bi961799n","article-title":"NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded","volume":"35","author":"Weinreb","year":"1996","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M116.765149_bib7","doi-asserted-by":"crossref","first-page":"9443","DOI":"10.1074\/jbc.273.16.9443","article-title":"Stabilization of \u03b1-synuclein secondary structure upon binding to synthetic membranes","volume":"273","author":"Davidson","year":"1998","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.765149_bib8","doi-asserted-by":"crossref","first-page":"34328","DOI":"10.1074\/jbc.M004345200","article-title":"\u03b1-Synuclein membrane interactions and lipid specificity","volume":"275","author":"Jo","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.765149_bib9","doi-asserted-by":"crossref","first-page":"11282","DOI":"10.1073\/pnas.90.23.11282","article-title":"Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease","volume":"90","author":"U\u00e9da","year":"1993","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.765149_bib10","doi-asserted-by":"crossref","first-page":"292","DOI":"10.5607\/en.2014.23.4.292","article-title":"\u03b1-Synuclein function and dysfunction on cellular membrane","volume":"23","author":"Snead","year":"2014","journal-title":"Exp. Neurobiol"},{"key":"10.1074\/jbc.M116.765149_bib11","doi-asserted-by":"crossref","first-page":"15970","DOI":"10.1021\/ja405993r","article-title":"Membrane remodeling by \u03b1-synuclein and effects on amyloid formation","volume":"135","author":"Jiang","year":"2013","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M116.765149_bib12","doi-asserted-by":"crossref","first-page":"20883","DOI":"10.1074\/jbc.M113.478297","article-title":"\u03b1-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling","volume":"288","author":"Ouberai","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.765149_bib13","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1126\/science.1195227","article-title":"\u03b1-Synuclein promotes SNARE-complex assembly in vivo in vitro","volume":"329","author":"Burr\u00e9","year":"2010","journal-title":"Science"},{"key":"10.1074\/jbc.M116.765149_bib14","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 complex formation","volume":"111","author":"Burr\u00e9","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.765149_bib15","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.plipres.2010.05.004","article-title":"\u03b1-Synuclein, lipids and Parkinson\u2019s disease","volume":"49","author":"Ruip\u00e9rez","year":"2010","journal-title":"Prog. Lipid Res"},{"key":"10.1074\/jbc.M116.765149_bib16","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1016\/j.bbrc.2005.08.072","article-title":"Lipid peroxidation: mechanisms, inhibition, and biological effects","volume":"338","author":"Niki","year":"2005","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.M116.765149_bib17","doi-asserted-by":"crossref","first-page":"5944","DOI":"10.1021\/cr200084z","article-title":"Free radical lipid peroxidation: mechanisms and analysis","volume":"111","author":"Yin","year":"2011","journal-title":"Chem. Rev"},{"key":"10.1074\/jbc.M116.765149_bib18","doi-asserted-by":"crossref","first-page":"e77561","DOI":"10.1371\/journal.pone.0077561","article-title":"The development of a specific and sensitive LC-MS-based method for the detection and quantification of hydroperoxy- and hydroxydocosahexaenoic acids as a tool for lipidomic analysis","volume":"8","author":"Derogis","year":"2013","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.M116.765149_bib19","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/0163-7827(84)90011-0","article-title":"Chemistry of free radical and singlet oxidation of lipids","volume":"23","author":"Frankel","year":"1984","journal-title":"Prog. Lipid Res"},{"key":"10.1074\/jbc.M116.765149_bib20","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1016\/j.freeradbiomed.2011.06.027","article-title":"Lipid peroxidationand neurodegenerative disease","volume":"51","author":"Reed","year":"2011","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/jbc.M116.765149_bib21","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1016\/j.bbadis.2008.12.006","article-title":"Oxidative and nitrosative stress in Parkinson's disease","volume":"1792","author":"Tsang","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.M116.765149_bib22","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.bbr.2008.11.037","article-title":"Targeting oxidative\/nitrergic stress ameliorates motor impairment, and attenuates synaptic mitochondrial dysfunction and lipid peroxidation in two models of Huntington's disease","volume":"199","author":"P\u00e9rez-De La Cruz","year":"2009","journal-title":"Behav. Brain Res"},{"key":"10.1074\/jbc.M116.765149_bib23","doi-asserted-by":"crossref","first-page":"27","DOI":"10.2217\/bmm.09.89","article-title":"Biomarkers of oxidative damage and inflammation in Alzheimer's disease","volume":"4","author":"Galasko","year":"2010","journal-title":"Biomark. Med"},{"key":"10.1074\/jbc.M116.765149_bib24","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1097\/01.jnen.0000179050.54522.5a","article-title":"Evidence of oxidative stress in the neocortex in incidental Lewy body disease","volume":"64","author":"Dalf\u00f3","year":"2005","journal-title":"J. Neuropathol. Exp. Neurol"},{"key":"10.1074\/jbc.M116.765149_bib25","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/S0197-0186(98)00062-X","article-title":"Effects of 4-hydroxynonenal, a lipid peroxidation product, on dopamine transport and Na+\/K+ ATPase in rat striatal synaptosomes","volume":"33","author":"Morel","year":"1998","journal-title":"Neurochem. Int"},{"key":"10.1074\/jbc.M116.765149_bib26","doi-asserted-by":"crossref","first-page":"15610","DOI":"10.1021\/bi061743l","article-title":"\u03b1-Synuclein adopts an \u03b1-helical conformation in the presence of polyunsaturated fatty acids to hinder micelle formation","volume":"45","author":"Broersen","year":"2006","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M116.765149_bib27","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":"De Franceschi","year":"2009","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M116.765149_bib28","doi-asserted-by":"crossref","first-page":"e82732","DOI":"10.1371\/journal.pone.0082732","article-title":"\u03b1-Synuclein oligomers induced by docosahexaenoic acid affect membrane integrity","volume":"8","author":"Fecchio","year":"2013","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.M116.765149_bib29","doi-asserted-by":"crossref","first-page":"22262","DOI":"10.1074\/jbc.M110.202937","article-title":"Structural and morphological characterization of aggregated species of \u03b1-synuclein induced by docosahexaenoic acid","volume":"286","author":"De Franceschi","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.765149_bib30","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.bbapap.2004.10.008","article-title":"Methionine oxidation, \u03b1-synuclein and Parkinson\u2019s disease","volume":"1703","author":"Glaser","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.M116.765149_bib31","doi-asserted-by":"crossref","first-page":"2943","DOI":"10.1021\/ja312415q","article-title":"Site-specific interaction between \u03b1-synuclein and membranes probed by NMR-observed methionine oxidation rates","volume":"135","author":"Maltsev","year":"2013","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M116.765149_bib32","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1089\/ars.2011.4429","article-title":"Lipid peroxidation product 4-hydroxy-2-nonenal promotes seeding-capable oligomer formation and cell-to-cell transfer of \u03b1-synuclein","volume":"18","author":"Bae","year":"2013","journal-title":"Antioxid. Redox Signal"},{"key":"10.1074\/jbc.M116.765149_bib33","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1111\/jnc.12226","article-title":"Oxidative and nitrative \u03b1-synuclein modifications and proteostatic stress: implications for disease mechanisms and interventions in synucleinopathies","volume":"125","author":"Schildknecht","year":"2013","journal-title":"J. Neurochem"},{"key":"10.1074\/jbc.M116.765149_bib34","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1212\/WNL.0b013e31828727ba","article-title":"A novel aS missense mutation in Parkinson disease","volume":"80","author":"Proukakis","year":"2013","journal-title":"Neurology"},{"key":"10.1074\/jbc.M116.765149_bib35","doi-asserted-by":"crossref","first-page":"2395","DOI":"10.1074\/jbc.M114.610527","article-title":"The H50Q mutation induces a 10-fold decrease in the solubility of \u03b1-synuclein","volume":"290","author":"Porcari","year":"2014","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.765149_bib36","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1002\/mds.25421","article-title":"\u03b1-Synuclein p.H50Q, a novel pathogenic mutation for Parkinson\u2019s disease","volume":"28","author":"Appel-Cresswell","year":"2013","journal-title":"Mov. Disord"},{"key":"10.1074\/jbc.M116.765149_bib37","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1002\/mas.20284","article-title":"Mass spectrometric analysis of long-chain lipids","volume":"30","author":"Murphy","year":"2011","journal-title":"Mass Spectrom. Rev"},{"key":"10.1074\/jbc.M116.765149_bib38","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1186\/s13024-015-0004-0","article-title":"Posttranslational modification and mutation of histidine 50 trigger \u03b1-synuclein aggregation and toxicity","volume":"10","author":"Xiang","year":"2015","journal-title":"Mol. Neurodegener"},{"key":"10.1074\/jbc.M116.765149_bib39","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.abb.2013.02.009","article-title":"Oxidation and nitration of \u03b1-synuclein and their implications in neurodegenerative diseases","volume":"533","author":"Chavarr\u00eda","year":"2013","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.M116.765149_bib40","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/S0006-3495(83)84439-7","article-title":"Concentration of oxygen in lipid bilayers using a spin-label method","volume":"41","author":"Subczynski","year":"1983","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.M116.765149_bib41","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/0891-5849(91)90192-6","article-title":"Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes","volume":"11","author":"Esterbauer","year":"1991","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/jbc.M116.765149_bib42","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1007\/s00726-003-0015-y","article-title":"Histidine and lysine as targets of oxidative modification","volume":"25","author":"Uchida","year":"2003","journal-title":"Amino Acids"},{"key":"10.1074\/jbc.M116.765149_bib43","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1042\/BJ20051277","article-title":"Interaction with phospholipids modulates \u03b1-synuclein nitration and lipid-protein adduct formation","volume":"393","author":"Trostchansky","year":"2006","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.M116.765149_bib44","doi-asserted-by":"crossref","first-page":"8135","DOI":"10.1021\/bi052584t","article-title":"\u03b1-Synuclein can function as an antioxidant preventing oxidation of unsaturated lipid in vesicles","volume":"45","author":"Zhu","year":"2006","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M116.765149_bib45","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1016\/j.freeradbiomed.2008.03.022","article-title":"Methionine sulfoxide reductase A protects dopaminergic cells from Parkinson's disease-related insults","volume":"45","author":"Liu","year":"2008","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/jbc.M116.765149_bib46","doi-asserted-by":"crossref","first-page":"21856","DOI":"10.1074\/jbc.M114.553297","article-title":"The H50Q mutation enhances \u03b1-synuclein aggregation, secretion, and toxicity","volume":"289","author":"Khalaf","year":"2014","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.765149_bib47","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.M116.765149_bib48","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\u2019s disease mutation sites","volume":"411","author":"Comellas","year":"2011","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M116.765149_bib49","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.nbd.2014.05.031","article-title":"Lysine residues at the first and second KTKEGV repeats mediate \u03b1-Synuclein binding to membrane phospholipids","volume":"70","author":"Zarbiv","year":"2014","journal-title":"Neurobiol. Dis"},{"key":"10.1074\/jbc.M116.765149_bib50","doi-asserted-by":"crossref","first-page":"2116","DOI":"10.1016\/j.bpj.2010.06.035","article-title":"The N-terminus of the intrinsically disordered protein \u03b1-synuclein triggers membrane binding and helix folding","volume":"99","author":"Bartels","year":"2010","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.M116.765149_bib51","doi-asserted-by":"crossref","first-page":"3827","DOI":"10.1038\/ncomms4827","article-title":"Direct observation of the three regions in \u03b1-synuclein that determine its membrane-bound behaviour","volume":"5","author":"Fusco","year":"2014","journal-title":"Nat. Commun"},{"key":"10.1074\/jbc.M116.765149_bib52","doi-asserted-by":"crossref","first-page":"a009399","DOI":"10.1101\/cshperspect.a009399","article-title":"\u03b1-Synuclein in Parkinson\u2019s disease","volume":"2","author":"Stefanis","year":"2012","journal-title":"Cold Spring Harb. Perspect. Med"},{"key":"10.1074\/jbc.M116.765149_bib53","first-page":"219","article-title":"Role of different regions of \u03b1-synuclein in the interaction with the brain fatty acid DHA","volume":"5","author":"De Franceschi","year":"2014","journal-title":"J. Chromatograph. Separat. Techniq"},{"key":"10.1074\/jbc.M116.765149_bib54","doi-asserted-by":"crossref","first-page":"1268","DOI":"10.1002\/ejlt.201400114","article-title":"Paradox of omega-3 PUFA oxidation","volume":"116","author":"Miyashita","year":"2014","journal-title":"Eur. J. Lipid Sci. Technol"},{"key":"10.1074\/jbc.M116.765149_bib55","doi-asserted-by":"crossref","first-page":"49874","DOI":"10.1074\/jbc.M309127200","article-title":"Altered fatty acid composition of dopaminergic neurons expressing \u03b1-synuclein and human brains with \u03b1-synucleinopathies","volume":"278","author":"Sharon","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.765149_bib56","doi-asserted-by":"crossref","first-page":"2000","DOI":"10.2353\/ajpath.2007.070373","article-title":"Polyunsaturated fatty acids induce \u03b1-synuclein-related pathogenic changes in neuronal cells","volume":"171","author":"Assayag","year":"2007","journal-title":"Am. J. Pathol"},{"key":"10.1074\/jbc.M116.765149_bib57","doi-asserted-by":"crossref","first-page":"1328","DOI":"10.1016\/j.freeradbiomed.2009.02.009","article-title":"Formation of dopamine-mediated \u03b1-synuclein-soluble oligomers requires methionine oxidation","volume":"46","author":"Leong","year":"2009","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/jbc.M116.765149_bib58","doi-asserted-by":"crossref","first-page":"10251","DOI":"10.1038\/ncomms10251","article-title":"Intracellular repair of oxidation-damaged \u03b1-synuclein fails to target C-terminal modification sites","volume":"7","author":"Binolfi","year":"2016","journal-title":"Nat. Commun"},{"key":"10.1074\/jbc.M116.765149_bib59","doi-asserted-by":"crossref","first-page":"2510","DOI":"10.3945\/jn.108.096016","article-title":"Docosahexaenoic acid and the aging brain","volume":"138","author":"Lukiw","year":"2008","journal-title":"J. Nutr"},{"key":"10.1074\/jbc.M116.765149_bib60","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1038\/embor.2010.66","article-title":"\u03b1-Synuclein sequesters arachidonic acid to modulate SNARE-mediated exocytosis","volume":"11","author":"Darios","year":"2010","journal-title":"EMBO Rep"},{"key":"10.1074\/jbc.M116.765149_bib61","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/0003-2697(89)90602-7","article-title":"Calculation of protein extinction coefficients from amino acids sequence data","volume":"182","author":"Gill","year":"1989","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.M116.765149_bib62","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/S0014-5793(02)02638-8","article-title":"Methionine oxidation inhibits fibrillation of human \u03b1-synuclein in vitro","volume":"517","author":"Uversky","year":"2002","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.M116.765149_bib63","volume":"Vol. 2","author":"Means","year":"1971"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820428844?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820428844?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M116.765149","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T12:15:39Z","timestamp":1641298539000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820428844"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,4]]},"references-count":63,"journal-issue":{"issue":"17","published-print":{"date-parts":[[2017,4]]}},"alternative-id":["S0021925820428844"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m116.765149","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2017,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"\u03b1-Synuclein structural features inhibit harmful polyunsaturated fatty acid oxidation, suggesting roles in neuroprotection","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.M116.765149","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}]}}