{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T12:26:15Z","timestamp":1791116775235,"version":"4.1.0"},"reference-count":59,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2006,3,1]],"date-time":"2006-03-01T00:00:00Z","timestamp":1141171200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2006,3,1]],"date-time":"2006-03-01T00:00:00Z","timestamp":1141171200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2006,3,1]],"date-time":"2006-03-01T00:00:00Z","timestamp":1141171200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2006,3,1]],"date-time":"2006-03-01T00:00:00Z","timestamp":1141171200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2006,3,1]],"date-time":"2006-03-01T00:00:00Z","timestamp":1141171200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2006,3,1]],"date-time":"2006-03-01T00:00:00Z","timestamp":1141171200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2006,3,1]],"date-time":"2006-03-01T00:00:00Z","timestamp":1141171200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2006,3]]},"DOI":"10.1016\/j.jmb.2005.12.030","type":"journal-article","created":{"date-parts":[[2005,12,28]],"date-time":"2005-12-28T09:59:58Z","timestamp":1135763998000},"page":"1036-1048","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":319,"title":["The Oxidation State of DJ-1 Regulates its Chaperone Activity Toward \u03b1-Synuclein"],"prefix":"10.1016","volume":"356","author":[{"given":"Wenbo","family":"Zhou","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Min","family":"Zhu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark A.","family":"Wilson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gregory A.","family":"Petsko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony L.","family":"Fink","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2005.12.030_bib1","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1111\/j.1749-6632.2003.tb07468.x","article-title":"Parkinson's disease and related alpha-synucleinopathies are brain amyloidoses","volume":"991","author":"Trojanowski","year":"2003","journal-title":"Ann. NY Acad. Sci."},{"key":"10.1016\/j.jmb.2005.12.030_bib2","doi-asserted-by":"crossref","first-page":"10737","DOI":"10.1074\/jbc.M010907200","article-title":"Evidence for a partially folded intermediate in alpha-synuclein fibril formation","volume":"276","author":"Uversky","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.12.030_bib3","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1021\/bi991447r","article-title":"Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid","volume":"39","author":"Conway","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.12.030_bib4","doi-asserted-by":"crossref","first-page":"10139","DOI":"10.1021\/bi00032a006","article-title":"Non-A beta component of Alzheimer's disease amyloid (NAC) is amyloidogenic","volume":"34","author":"Iwai","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.12.030_bib5","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1126\/science.1079469","article-title":"Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis","volume":"300","author":"Kayed","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.jmb.2005.12.030_bib6","doi-asserted-by":"crossref","first-page":"7871","DOI":"10.1021\/bi030086j","article-title":"Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease","volume":"42","author":"Volles","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.12.030_bib7","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1038\/416507a","article-title":"Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases","volume":"416","author":"Bucciantini","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2005.12.030_bib8","doi-asserted-by":"crossref","first-page":"4595","DOI":"10.1021\/bi0121353","article-title":"Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism","volume":"41","author":"Volles","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.12.030_bib9","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1002\/jmr.699","article-title":"The effect of macromolecular crowding on protein aggregation and amyloid fibril formation","volume":"17","author":"Munishkina","year":"2004","journal-title":"J. Mol. Recognit."},{"key":"10.1016\/j.jmb.2005.12.030_bib10","doi-asserted-by":"crossref","first-page":"44284","DOI":"10.1074\/jbc.M105343200","article-title":"Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular link between Parkinson's disease and heavy metal exposure","volume":"276","author":"Uversky","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.12.030_bib11","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1126\/science.1082324","article-title":"Initiation and synergistic fibrillization of tau and alpha-synuclein","volume":"300","author":"Giasson","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.jmb.2005.12.030_bib12","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1110\/ps.0230903","article-title":"Polycation-induced oligomerization and accelerated fibrillation of human alpha-synuclein in vitro","volume":"12","author":"Goers","year":"2003","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2005.12.030_bib13","doi-asserted-by":"crossref","first-page":"3235","DOI":"10.1074\/jbc.M208249200","article-title":"Cellular polyamines promote the aggregation of alpha-synuclein","volume":"278","author":"Antony","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.12.030_bib14","doi-asserted-by":"crossref","first-page":"41958","DOI":"10.1074\/jbc.M105022200","article-title":"Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins","volume":"276","author":"Perrin","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.12.030_bib15","doi-asserted-by":"crossref","first-page":"1641","DOI":"10.1074\/jbc.C100560200","article-title":"The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice","volume":"277","author":"Manning-Bog","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.12.030_bib16","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/S0014-5793(01)02597-2","article-title":"Pesticides directly accelerate the rate of alpha-synuclein fibril formation: a possible factor in Parkinson's disease","volume":"500","author":"Uversky","year":"2001","journal-title":"FEBS Letters"},{"key":"10.1016\/j.jmb.2005.12.030_bib17","doi-asserted-by":"crossref","first-page":"11970","DOI":"10.1074\/jbc.M109541200","article-title":"Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins","volume":"277","author":"Uversky","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.12.030_bib18","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0896-6273(01)00462-7","article-title":"beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor","volume":"32","author":"Hashimoto","year":"2001","journal-title":"Neuron"},{"key":"10.1016\/j.jmb.2005.12.030_bib19","doi-asserted-by":"crossref","first-page":"3696","DOI":"10.1021\/bi020604a","article-title":"Beta-synuclein inhibits formation of alpha-synuclein protofibrils: a possible therapeutic strategy against Parkinson's disease","volume":"42","author":"Park","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.12.030_bib20","doi-asserted-by":"crossref","first-page":"1346","DOI":"10.1126\/science.1063522","article-title":"Kinetic stabilization of the alpha-synuclein protofibril by a dopamine- alpha-synuclein adduct","volume":"294","author":"Conway","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.jmb.2005.12.030_bib21","doi-asserted-by":"crossref","first-page":"26846","DOI":"10.1074\/jbc.M403129200","article-title":"The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils","volume":"279","author":"Zhu","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.12.030_bib22","doi-asserted-by":"crossref","first-page":"1513","DOI":"10.1016\/j.chembiol.2004.08.025","article-title":"Rifampicin inhibits alpha-synuclein fibrillation and disaggregates fibrils","volume":"11","author":"Li","year":"2004","journal-title":"Chem. Biol."},{"key":"10.1016\/j.jmb.2005.12.030_bib23","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.M306390200","article-title":"Proteasomal inhibition by alpha -synuclein filaments and oligomers","author":"Lindersson","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.12.030_bib24","doi-asserted-by":"crossref","first-page":"1292","DOI":"10.1126\/science.1101738","article-title":"Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy","volume":"305","author":"Cuervo","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.jmb.2005.12.030_bib25","doi-asserted-by":"crossref","first-page":"1888","DOI":"10.1523\/JNEUROSCI.3809-03.2004","article-title":"Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway","volume":"24","author":"Lee","year":"2004","journal-title":"J. Neurosci."},{"key":"10.1016\/j.jmb.2005.12.030_bib26","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1126\/science.1067389","article-title":"Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease","volume":"295","author":"Auluck","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.jmb.2005.12.030_bib27","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1016\/j.jmb.2004.05.054","article-title":"Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity","volume":"340","author":"Rekas","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2005.12.030_bib28","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1002\/ana.10663","article-title":"Early-onset Parkinson's disease caused by a compound heterozygous DJ-1 mutation","volume":"54","author":"Hague","year":"2003","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.jmb.2005.12.030_bib29","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1126\/science.1077209","article-title":"Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism","volume":"299","author":"Bonifati","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.jmb.2005.12.030_bib30","doi-asserted-by":"crossref","first-page":"1558","DOI":"10.1111\/j.1471-4159.2003.02265.x","article-title":"A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization","volume":"87","author":"Moore","year":"2003","journal-title":"J. Neurochem."},{"key":"10.1016\/j.jmb.2005.12.030_bib31","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1007\/s00109-003-0512-1","article-title":"Linking DJ-1 to neurodegeneration offers novel insights for understanding the pathogenesis of Parkinson's disease","volume":"82","author":"Bonifati","year":"2004","journal-title":"J. Mol. Med."},{"key":"10.1016\/j.jmb.2005.12.030_bib32","doi-asserted-by":"crossref","first-page":"31380","DOI":"10.1074\/jbc.M305878200","article-title":"The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease","volume":"278","author":"Honbou","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.12.030_bib33","doi-asserted-by":"crossref","first-page":"9256","DOI":"10.1073\/pnas.1133288100","article-title":"The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease","volume":"100","author":"Wilson","year":"2003","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2005.12.030_bib34","doi-asserted-by":"crossref","first-page":"44552","DOI":"10.1074\/jbc.M304517200","article-title":"Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain","volume":"278","author":"Lee","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.12.030_bib35","doi-asserted-by":"crossref","first-page":"31372","DOI":"10.1074\/jbc.M304221200","article-title":"Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease","volume":"278","author":"Tao","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.12.030_bib36","doi-asserted-by":"crossref","first-page":"3137","DOI":"10.1073\/pnas.0530312100","article-title":"The 1.6-\u00c5 crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad","volume":"100","author":"Quigley","year":"2003","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2005.12.030_bib37","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S1474-4422(02)00036-4","article-title":"Deciphering Parkinson's disease\u2013PARK8","volume":"1","author":"Bonifati","year":"2002","journal-title":"Lancet Neurol."},{"key":"10.1016\/j.jmb.2005.12.030_bib38","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1002\/ana.10106","article-title":"Localization of autosomal recessive early-onset parkinsonism to chromosome 1p36 (PARK7) in an independent dataset","volume":"51","author":"Bonifati","year":"2002","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.jmb.2005.12.030_bib39","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1080\/10715760100301381","article-title":"DJ-1 is an indicator for endogenous reactive oxygen species elicited by endotoxin","volume":"35","author":"Mitsumoto","year":"2001","journal-title":"Free Radic. Res."},{"key":"10.1016\/j.jmb.2005.12.030_bib40","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1080\/10715760100300831","article-title":"Oxidized forms of peroxiredoxins and DJ-1 on two-dimensional gels increased in response to sublethal levels of paraquat","volume":"35","author":"Mitsumoto","year":"2001","journal-title":"Free Radic. Res."},{"key":"10.1016\/j.jmb.2005.12.030_bib41","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1111\/j.1749-6632.2003.tb07470.x","article-title":"Mitochondria, oxidative damage, and inflammation in Parkinson's disease","volume":"991","author":"Beal","year":"2003","journal-title":"Ann. NY Acad. Sci."},{"key":"10.1016\/j.jmb.2005.12.030_bib42","doi-asserted-by":"crossref","first-page":"S26","DOI":"10.1002\/ana.10483","article-title":"Oxidative stress in Parkinson's disease","volume":"53","author":"Jenner","year":"2003","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.jmb.2005.12.030_bib43","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1038\/nrn983","article-title":"Pathogenesis of Parkinson's disease: dopamine, vesicles and alpha-synuclein","volume":"3","author":"Lotharius","year":"2002","journal-title":"Nature Rev. Neurosci."},{"key":"10.1016\/j.jmb.2005.12.030_bib44","doi-asserted-by":"crossref","first-page":"1342","DOI":"10.1016\/j.bbrc.2003.11.056","article-title":"Down regulation of DJ-1 enhances cell death by oxidative stress, ER stress, and proteasome inhibition","volume":"312","author":"Yokota","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jmb.2005.12.030_bib45","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1016\/j.bbrc.2004.03.110","article-title":"Cysteine-106 of DJ-1 is the most sensitive cysteine residue to hydrogen peroxide-mediated oxidation in vivo in human umbilical vein endothelial cells","volume":"317","author":"Kinumi","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jmb.2005.12.030_bib46","doi-asserted-by":"crossref","first-page":"9103","DOI":"10.1073\/pnas.0402959101","article-title":"The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization","volume":"101","author":"Canet-Aviles","year":"2004","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2005.12.030_bib47","doi-asserted-by":"crossref","first-page":"36588","DOI":"10.1074\/jbc.M304272200","article-title":"L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the uniquitin-proteasome system","volume":"278","author":"Miller","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.12.030_bib48","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1212\/01.WNL.0000083992.28066.7E","article-title":"Assessment of a DJ-1 (PARK7) polymorphism in Finnish PD","volume":"61","author":"Eerola","year":"2003","journal-title":"Neurology"},{"key":"10.1016\/j.jmb.2005.12.030_bib49","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.neulet.2003.08.037","article-title":"Polymorphism in the human DJ-1 gene is not associated with sporadic dementia with Lewy bodies or Parkinson's disease","volume":"352","author":"Morris","year":"2003","journal-title":"Neurosci. Letters"},{"key":"10.1016\/j.jmb.2005.12.030_bib50","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1007\/s00401-004-0834-2","article-title":"Pathological properties of the Parkinson's disease-associated protein DJ-1 in alpha-synucleinopathies and tauopathies: relevance for multiple system atrophy and Pick's disease","volume":"107","author":"Neumann","year":"2004","journal-title":"Acta Neuropathol. (Berl)"},{"key":"10.1016\/j.jmb.2005.12.030_bib51","doi-asserted-by":"crossref","first-page":"e362","DOI":"10.1371\/journal.pbio.0020362","article-title":"DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation","volume":"2","author":"Shendelman","year":"2004","journal-title":"PLoS. Biol."},{"key":"10.1016\/j.jmb.2005.12.030_bib52","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":"10.1016\/j.jmb.2005.12.030_bib53","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3109\/13506129509031881","article-title":"Thioflavine T interaction with amyloid beta-sheet structures","volume":"2","author":"Le Vine","year":"1995","journal-title":"Amyloid"},{"key":"10.1016\/j.jmb.2005.12.030_bib54","doi-asserted-by":"crossref","first-page":"1531","DOI":"10.1073\/pnas.0308089100","article-title":"The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: a member of the DJ-1\/ThiJ\/PfpI superfamily","volume":"101","author":"Wilson","year":"2004","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2005.12.030_bib55","doi-asserted-by":"crossref","first-page":"1524","DOI":"10.1111\/j.1471-4159.2005.03145.x","article-title":"DJ-1 is present in a large molecular complex in human brain tissue and interacts with alpha-synuclein","volume":"93","author":"Meulener","year":"2005","journal-title":"J. Neurochem."},{"key":"10.1016\/j.jmb.2005.12.030_bib56","doi-asserted-by":"crossref","first-page":"985","DOI":"10.1126\/science.290.5493.985","article-title":"Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions","volume":"290","author":"Giasson","year":"2000","journal-title":"Science"},{"key":"10.1016\/j.jmb.2005.12.030_bib57","doi-asserted-by":"crossref","first-page":"6036","DOI":"10.1021\/bi002555c","article-title":"Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism","volume":"40","author":"Nielsen","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.12.030_bib58","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":"10.1016\/j.jmb.2005.12.030_bib59","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1093\/protein\/6.4.383","article-title":"Evaluation of secondary structure proteins from UV circular dichroism spectra using an unsupervised learning neural network","volume":"6","author":"Andrade","year":"1993","journal-title":"Protein Eng"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283605015925?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283605015925?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T20:54:44Z","timestamp":1758315284000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283605015925"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,3]]},"references-count":59,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2006,3]]}},"alternative-id":["S0022283605015925"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2005.12.030","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2006,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The Oxidation State of DJ-1 Regulates its Chaperone Activity Toward \u03b1-Synuclein","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2005.12.030","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2005 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}