Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 이서구 | * |
dc.contributor.author | 우현애 | * |
dc.date.accessioned | 2016-08-28T12:08:56Z | - |
dc.date.available | 2016-08-28T12:08:56Z | - |
dc.date.issued | 2011 | * |
dc.identifier.issn | 1523-0864 | * |
dc.identifier.other | OAK-7761 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/221773 | - |
dc.description.abstract | Peroxiredoxins (Prxs) are a family of peroxidases that reduce peroxides, with a conserved cysteine residue (the peroxidatic Cys) serving as the site of oxidation by peroxides. Peroxides oxidize the peroxidatic Cys-SH to Cys-SOH, which then reacts with another cysteine residue (typically the resolving Cys [C R]) to form a disulfide that is subsequently reduced by an appropriate electron donor. On the basis of the location or absence of the C R, Prxs are classified into 2-Cys, atypical 2-Cys, and 1-Cys Prx subfamilies. In addition to their peroxidase activity, members of the 2-Cys Prx subfamily appear to serve as peroxide sensors for other proteins and as molecular chaperones. During catalysis, the peroxidatic Cys-SOH of 2-Cys Prxs is occasionally further oxidized to Cys-SO 2H before disulfide formation, resulting in inactivation of peroxidase activity. This hyperoxidation, which is reversed by the ATP-dependent enzyme sulfiredoxin, modulates the sensor and chaperone functions of 2-Cys Prxs. The peroxidase activity of 2-Cys Prxs is extensively regulated via tyrosine and threonine phosphorylation, which allows modulation of the local concentration of the intracellular messenger H 2O 2. Finally, 2-Cys Prxs interact with a variety of proteins, with such interaction having been shown to modulate the function of the binding partners in a reciprocal manner. © 2011 Mary Ann Liebert, Inc. | * |
dc.language | English | * |
dc.title | Multiple functions of peroxiredoxins: Peroxidases, sensors and regulators of the intracellular messenger H 2O 2, and protein chaperones | * |
dc.type | Review | * |
dc.relation.issue | 3 | * |
dc.relation.volume | 15 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 781 | * |
dc.relation.lastpage | 794 | * |
dc.relation.journaltitle | Antioxidants and Redox Signaling | * |
dc.identifier.doi | 10.1089/ars.2010.3393 | * |
dc.identifier.wosid | WOS:000292446300012 | * |
dc.identifier.scopusid | 2-s2.0-79951643450 | * |
dc.author.google | Rhee S.G. | * |
dc.author.google | Woo H.A. | * |
dc.contributor.scopusid | 이서구(7401852092) | * |
dc.contributor.scopusid | 우현애(8068619500) | * |
dc.date.modifydate | 20240423081003 | * |