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dc.contributor.author이서구-
dc.contributor.author배수한-
dc.contributor.author길인섭-
dc.contributor.author우현애-
dc.date.accessioned2017-08-28T22:35:12Z-
dc.date.available2017-08-28T22:35:12Z-
dc.date.issued2012-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://dspace.ewha.ac.kr/handle/2015.oak/222381-
dc.description.abstractPeroxiredoxins (Prxs) contain an active site cysteine that is sensitive to oxidation by H 2O 2. Mammalian cells express six Prx isoforms that are localized to various cellular compartments. The oxidized active site cysteine of Prx can be reduced by a cellular thiol, thus enabling Prx to function as a locally constrained peroxidase. Regulation of Prx via phosphorylation in response to extracellular signals allows the local accumulation of H 2O 2 and thereby enables its messenger function. The fact that the oxidation state of the active site cysteine of Prx can be transferred to other proteins that are less intrinsically susceptible to H 2O 2 also allows Prx to function as an H 2O 2 sensor. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.-
dc.languageEnglish-
dc.titlePeroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides-
dc.typeShort Survey-
dc.relation.issue7-
dc.relation.volume287-
dc.relation.indexSCI-
dc.relation.indexSCIE-
dc.relation.indexSCOPUS-
dc.relation.startpage4403-
dc.relation.lastpage4410-
dc.relation.journaltitleJournal of Biological Chemistry-
dc.identifier.doi10.1074/jbc.R111.283432-
dc.identifier.wosidWOS:000300608500003-
dc.identifier.scopusid2-s2.0-84856940017-
dc.author.googleRhee S.G.-
dc.author.googleWoo H.A.-
dc.author.googleKil I.S.-
dc.author.googleBae S.H.-
dc.contributor.scopusid이서구(7401852092;25923074700)-
dc.contributor.scopusid우현애(8068619500)-
dc.date.modifydate20180302081000-


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