Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 우현애 | * |
dc.date.accessioned | 2020-04-13T16:32:23Z | - |
dc.date.available | 2020-04-13T16:32:23Z | - |
dc.date.issued | 2020 | * |
dc.identifier.issn | 0891-5849 | * |
dc.identifier.issn | 1873-4596 | * |
dc.identifier.other | OAK-26781 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/253829 | - |
dc.description.abstract | Peroxiredoxins (Prxs) are an unusual family of thiol-specific peroxidases that possess a binding site for H 2 O 2 and rely on a conserved cysteine residue for rapid reaction with H 2 O 2 . Among 6 mammalian isoforms (Prx I to VI), Prx I and Prx II are mainly found in the cytosol and nucleus. Prx I and Prx II function as antioxidant enzymes and protein chaperone under oxidative distress conditions. Under oxidative eustress conditions, Prx I and Prx II regulate the levels of H 2 O 2 at specific area of the cells as well as sense and transduce H 2 O 2 signaling to target proteins. Prx I and Prx II are known to be covalently modified on multiple sites: Prx I is hyperoxidized on Cys 52 ; phosphorylated on Ser 32 , Thr 90 , and Tyr 194 ; acetylated on Lys 7 , Lys 16 , Lys 27 , Lys 35 , and Lys 197 ; glutathionylated on Cys 52 , Cys 83 , and Cys 173 ; and nitrosylated on Cys 52 and Cys 83 , whereas Prx II is hyperoxidized on Cys 51 ; phosphorylated on Thr 89 , Ser 112 , and Thr 182 ; acetylated on Ala 2 and Lys 196 ; glutathionylated on Cys 51 and Cys 172 ; and nitrosylated on Cys 51 and Cys 172 . In this review, we describe how these post -translational mod- ifications affect various functions of Prx I and Prx II. | * |
dc.language | English | * |
dc.publisher | ELSEVIER SCIENCE INC | * |
dc.subject | Peroxiredoxin | * |
dc.subject | Peroxidase | * |
dc.subject | Chaperone | * |
dc.subject | 2 O 2 ) | * |
dc.subject | Intracellular messenger | * |
dc.subject | Thiol oxidation | * |
dc.subject | Phosphorylation | * |
dc.subject | Acetylation | * |
dc.subject | Glutathionylation | * |
dc.subject | S-Nitrosylation | * |
dc.title | Multiple functions of 2-Cys peroxiredoxins, I and II, and their regulations via post -translational modifications | * |
dc.type | Article | * |
dc.relation.volume | 152 | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 107 | * |
dc.relation.lastpage | 115 | * |
dc.relation.journaltitle | FREE RADICAL BIOLOGY AND MEDICINE | * |
dc.identifier.wosid | WOS:000542921200003 | * |
dc.identifier.scopusid | 2-s2.0-85081310780 | * |
dc.author.google | Rhee, Sue Goo | * |
dc.author.google | Woo, Hyun Ae | * |
dc.contributor.scopusid | 우현애(8068619500) | * |
dc.date.modifydate | 20240215164922 | * |