{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,5]],"date-time":"2025-11-05T06:34:52Z","timestamp":1762324492432,"version":"3.37.3"},"reference-count":7,"publisher":"Oxford University Press (OUP)","issue":"22","license":[{"start":{"date-parts":[[2019,6,14]],"date-time":"2019-06-14T00:00:00Z","timestamp":1560470400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100009473","name":"University of M\u00e1laga","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100009473","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2019,11,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:sec>\n                  <jats:title>Motivation<\/jats:title>\n                  <jats:p>The oxidation of protein-bound methionine to form methionine sulfoxide has traditionally been regarded as an oxidative damage. However, growing evidences support the view of this reversible reaction also as a regulatory post-translational modification. Thus, the oxidation of methionine residues has been reported to have multiple and varied implications for protein function. However, despite the importance of this modification and the abundance of reports, all these data are scattered in the literature. No database\/resource on methionine sulfoxidation exists currently. Since this information is useful to gain further insights into the redox regulation of cellular proteins, we have created a primary database of experimentally confirmed sulfoxidation sites.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Results<\/jats:title>\n                  <jats:p>MetOSite currently contains 7242 methionine sulfoxide sites found in 3562 different proteins from 23 species, with Homo sapiens, Arabidopsis thaliana and Bacillus cereus as the main contributors. Each collected site has been classified according to the effect of its sulfoxidation on the biological properties of the modified protein. Thus, MetOSite documents cases where the sulfoxidation of methionine leads to (i) gain of activity, (ii) loss of activity, (iii) increased protein\u2013protein interaction susceptibility, (iv) decreased protein\u2013protein interaction susceptibility, (v) changes in protein stability and (vi) changes in subcellular location.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Availability and implementation<\/jats:title>\n                  <jats:p>MetOSite is available at https:\/\/metosite.uma.es.<\/jats:p>\n               <\/jats:sec>","DOI":"10.1093\/bioinformatics\/btz462","type":"journal-article","created":{"date-parts":[[2019,6,6]],"date-time":"2019-06-06T19:14:26Z","timestamp":1559848466000},"page":"4849-4850","source":"Crossref","is-referenced-by-count":13,"title":["MetOSite: an integrated resource for the study of methionine residues sulfoxidation"],"prefix":"10.1093","volume":"35","author":[{"given":"H\u00e9ctor","family":"Valverde","sequence":"first","affiliation":[{"name":"Departamento de Biolog\u00eda Molecular y Bioqu\u00edmica, Universidad de M\u00e1laga , M\u00e1laga 29071, Spain"}]},{"given":"Francisco R","family":"Cant\u00f3n","sequence":"additional","affiliation":[{"name":"Departamento de Biolog\u00eda Molecular y Bioqu\u00edmica, Universidad de M\u00e1laga , M\u00e1laga 29071, Spain"}]},{"given":"Juan Carlos","family":"Aledo","sequence":"additional","affiliation":[{"name":"Departamento de Biolog\u00eda Molecular y Bioqu\u00edmica, Universidad de M\u00e1laga , M\u00e1laga 29071, Spain"}]}],"member":"286","published-online":{"date-parts":[[2019,6,14]]},"reference":[{"key":"2023013108351116700_btz462-B1","doi-asserted-by":"crossref","first-page":"9493","DOI":"10.1073\/pnas.1300578110","article-title":"Methionine oxidation activates a transcription factor in response to oxidative stress","volume":"110","author":"Drazic","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2023013108351116700_btz462-B2","doi-asserted-by":"crossref","first-page":"e1005297","DOI":"10.1371\/journal.pgen.1005297","article-title":"Reversible oxidation of a conserved methionine in the nuclear export sequence determines subcellular distribution and activity of the fungal nitrate regulator NirA","volume":"11","author":"Gallmetzer","year":"2015","journal-title":"PLoS Genet"},{"key":"2023013108351116700_btz462-B3","first-page":"e1005297","article-title":"Oxidation of I\u03baB\u03b1 at methionine 45 is one cause of taurine chloramine-induced inhibition of NF-\u03baB activation","volume":"11","author":"Kanayama","year":"2002","journal-title":"PLoS Genet"},{"key":"2023013108351116700_btz462-B4","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/j.molcel.2013.06.019","article-title":"MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation","volume":"51","author":"Lee","year":"2013","journal-title":"Mol. Cell"},{"key":"2023013108351116700_btz462-B5","doi-asserted-by":"crossref","first-page":"15036","DOI":"10.1073\/pnas.93.26.15036","article-title":"Methionine residues as endogenous antioxidants in proteins","volume":"93","author":"Levine","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2023013108351116700_btz462-B6","doi-asserted-by":"crossref","first-page":"34979","DOI":"10.1074\/jbc.M112.374504","article-title":"The methionine-aromatic motif plays a unique role in stabilizing protein structure","volume":"287","author":"Valley","year":"2012","journal-title":"J. Biol. Chem"},{"key":"2023013108351116700_btz462-B7","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/srep40403","article-title":"Methionine residues around phosphorylation sites are preferentially oxidized in vivo under stress conditions","volume":"7","author":"Veredas","year":"2017","journal-title":"Sci. Rep"}],"container-title":["Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/bioinformatics\/advance-article-pdf\/doi\/10.1093\/bioinformatics\/btz462\/28885535\/btz462.pdf","content-type":"application\/pdf","content-version":"am","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article-pdf\/35\/22\/4849\/48978190\/bioinformatics_35_22_4849.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article-pdf\/35\/22\/4849\/48978190\/bioinformatics_35_22_4849.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,1,31]],"date-time":"2023-01-31T17:45:19Z","timestamp":1675187119000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article\/35\/22\/4849\/5514041"}},"subtitle":[],"editor":[{"given":"Alfonso","family":"Valencia","sequence":"additional","affiliation":[]}],"short-title":[],"issued":{"date-parts":[[2019,6,14]]},"references-count":7,"journal-issue":{"issue":"22","published-print":{"date-parts":[[2019,11,1]]}},"URL":"https:\/\/doi.org\/10.1093\/bioinformatics\/btz462","relation":{},"ISSN":["1367-4803","1367-4811"],"issn-type":[{"type":"print","value":"1367-4803"},{"type":"electronic","value":"1367-4811"}],"subject":[],"published-other":{"date-parts":[[2019,11,15]]},"published":{"date-parts":[[2019,6,14]]}}}