{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T12:35:45Z","timestamp":1767962145189,"version":"3.49.0"},"reference-count":27,"publisher":"Public Library of Science (PLoS)","issue":"5","content-domain":{"domain":["www.ploscompbiol.org"],"crossmark-restriction":false},"short-container-title":["PLoS Comput Biol"],"DOI":"10.1371\/journal.pcbi.1000383","type":"journal-article","created":{"date-parts":[[2009,5,7]],"date-time":"2009-05-07T21:06:49Z","timestamp":1241730409000},"page":"e1000383","update-policy":"https:\/\/doi.org\/10.1371\/journal.pcbi.corrections_policy","source":"Crossref","is-referenced-by-count":24,"title":["A Structure-Based Approach for Detection of Thiol Oxidoreductases and Their Catalytic Redox-Active Cysteine Residues"],"prefix":"10.1371","volume":"5","author":[{"given":"Stefano M.","family":"Marino","sequence":"first","affiliation":[]},{"given":"Vadim N.","family":"Gladyshev","sequence":"additional","affiliation":[]}],"member":"340","published-online":{"date-parts":[[2009,5,8]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"484","DOI":"10.2174\/138920307782411464","article-title":"\u201cForbidden\u201d disulfides: their role as redox switches.","volume":"8","author":"MA Wouters","year":"2007","journal-title":"Curr Protein Pept Sci"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1146\/annurev.biochem.72.121801.161459","article-title":"Protein disulfide bond formation in prokaryotes.","volume":"72","author":"H Kadokura","year":"2003","journal-title":"Annu Rev Biochem"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1139\/o06-186","article-title":"ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations.","volume":"84","author":"P Maattanen","year":"2006","journal-title":"Biochem Cell Biol"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"1378","DOI":"10.1042\/BST0331378","article-title":"Oxidoreduction of protein thiols in redox regulation.","volume":"33","author":"P Ghezzi","year":"2005","journal-title":"Biochem Soc Trans"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"H1227","DOI":"10.1152\/ajpheart.01162.2006","article-title":"Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system.","volume":"292","author":"C Berndt","year":"2007","journal-title":"Am J Physiol Heart Circ Physiol"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"980","DOI":"10.1038\/nature02075","article-title":"ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin.","volume":"425","author":"B Biteau","year":"2003","journal-title":"Nature"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1146\/annurev.pharmtox.44.101802.121735","article-title":"Protein sulfenic acids in redox signaling.","volume":"44","author":"LB Poole","year":"2004","journal-title":"Annu Rev Pharmacol Toxicol"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1110\/ps.073096508","article-title":"Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid.","volume":"17","author":"FR Salsbury Jr","year":"2008","journal-title":"Protein Sci"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1089\/ars.2007.1716","article-title":"Molecular mechanisms and potential clinical significance of S-glutathionylation.","volume":"10","author":"I Dalle-Donne","year":"2008","journal-title":"Antioxid Redox Signal"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"7420","DOI":"10.1073\/pnas.0600729103","article-title":"Identification of S-nitrosylation motifs by site-specific mapping of the S-nitrosocysteine proteome in human vascular smooth muscle cells.","volume":"103","author":"TM Greco","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1110\/ps.073252408","article-title":"Prediction of reversibly oxidized protein cysteine thiols using protein structure properties.","volume":"17","author":"R Sanchez","year":"2008","journal-title":"Protein Sci"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1126\/science.1133114","article-title":"High-throughput identification of catalytic redox-active cysteine residues.","volume":"315","author":"DE Fomenko","year":"2007","journal-title":"Science"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/j.jmb.2003.09.062","article-title":"Structure-based active site profiles for genome analysis and functional family subclassification.","volume":"334","author":"SA Cammer","year":"2003","journal-title":"J Mol Biol"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"1908","DOI":"10.1093\/bioinformatics\/bti315","article-title":"Q-SiteFinder: an energy-based method for the prediction of protein-ligand binding sites.","volume":"21","author":"AT Laurie","year":"2005","journal-title":"Bioinformatics"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/0022-2836(92)91009-E","article-title":"Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin.","volume":"224","author":"D Bashford","year":"1992","journal-title":"J Mol Biol"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1016\/S0006-3495(94)80925-7","article-title":"Environmental effects on the protonation states of active site residues in bacteriorhodopsin.","volume":"66","author":"RV Sampogna","year":"1994","journal-title":"Biophys J"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"12473","DOI":"10.1073\/pnas.211436698","article-title":"THEMATICS: a simple computational predictor of enzyme function from structure.","volume":"98","author":"MJ Ondrechen","year":"2001","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref18","doi-asserted-by":"crossref","DOI":"10.1002\/0471250953.bi0806s6","article-title":"Identifying functional sites based on prediction of charged group behavior.","volume":"8","author":"MJ Ondrechen","year":"2004","journal-title":"Curr Protoc Bioinformatics Chapter"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"W368","DOI":"10.1093\/nar\/gki464","article-title":"H++: a server for estimating pKas and adding missing hydrogens to macromolecules.","volume":"33","author":"JC Gordon","year":"2005","journal-title":"Nucleic Acids Res"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"11109","DOI":"10.1073\/pnas.0611636104","article-title":"Molecular mechanism of thioredoxin regulation in photosynthetic A2B2-glyceraldehyde-3-phosphate dehydrogenase.","volume":"104","author":"S Fermani","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1111\/j.1742-4658.2006.05577.x","article-title":"The thioredoxin-independent isoform of chloroplastic glyceraldehyde-3-phosphate dehydrogenase is selectively regulated by glutathionylation.","volume":"274","author":"M Zaffagnini","year":"2007","journal-title":"FEBS J"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1016\/S0925-4439(97)00084-7","article-title":"Inactivation of glyceraldehyde 3-phosphate dehydrogenase by sugars, prednisolone-21-hemisuccinate, cyanate and other small molecules.","volume":"1362","author":"DW Hook","year":"1997","journal-title":"Biochim Biophys Acta"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"4984","DOI":"10.1016\/S0021-9258(18)68884-2","article-title":"The effect of H2O2 upon thioredoxin-enriched lens epithelial cells.","volume":"263","author":"A Spector","year":"1988","journal-title":"J Biol Chem"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1006\/exer.2001.1103","article-title":"Effect of H(2)O(2)on human lens epithelial cells and the possible mechanism for oxidative damage repair by thioltransferase.","volume":"74","author":"KY Xing","year":"2002","journal-title":"Exp Eye Res"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"8506","DOI":"10.1073\/pnas.132142799","article-title":"All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade.","volume":"99","author":"J Messens","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"e1000266","DOI":"10.1371\/journal.pcbi.1000266","article-title":"Partial order optimum likelihood (POOL): maximum likelihood prediction of protein active site residues using 3D structure and sequence properties.","volume":"5","author":"W Tong","year":"2009","journal-title":"PLoS Comput Biol"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"i258","DOI":"10.1093\/bioinformatics\/bti1039","article-title":"Prediction of active sites for protein structures from computed chemical properties.","volume":"21","author":"J Ko","year":"2005","journal-title":"Bioinformatics"}],"container-title":["PLoS Computational Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pcbi.1000383","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,10,5]],"date-time":"2021-10-05T02:32:52Z","timestamp":1633401172000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pcbi.1000383"}},"subtitle":[],"editor":[{"given":"Jacquelyn S.","family":"Fetrow","sequence":"first","affiliation":[]}],"short-title":[],"issued":{"date-parts":[[2009,5,8]]},"references-count":27,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2009,5,8]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pcbi.1000383","relation":{},"ISSN":["1553-7358"],"issn-type":[{"value":"1553-7358","type":"electronic"}],"subject":[],"published":{"date-parts":[[2009,5,8]]}}}