| http://purl.uniprot.org/citations/12517450 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12517450 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12517450 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/12517450 | http://www.w3.org/2000/01/rdf-schema#comment | "Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant enzymes that also control cytokine-induced peroxide levels which mediate signal transduction in mammalian cells. Prxs can be regulated by changes to phosphorylation, redox and possibly oligomerization states. Prxs are divided into three classes: typical 2-Cys Prxs; atypical 2-Cys Prxs; and 1-Cys Prxs. All Prxs share the same basic catalytic mechanism, in which an active-site cysteine (the peroxidatic cysteine) is oxidized to a sulfenic acid by the peroxide substrate. The recycling of the sulfenic acid back to a thiol is what distinguishes the three enzyme classes. Using crystal structures, a detailed catalytic cycle has been derived for typical 2-Cys Prxs, including a model for the redox-regulated oligomeric state proposed to control enzyme activity."xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0968-0004(02)00003-8"xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/author | "Schroder E."xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/author | "Schroder E."xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/author | "Poole L.B."xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/author | "Poole L.B."xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/author | "Wood Z.A."xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/author | "Wood Z.A."xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/author | "Robin Harris J."xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/author | "Robin Harris J."xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/name | "Trends Biochem. Sci."xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/name | "Trends Biochem Sci"xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/pages | "32-40"xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/pages | "32-40"xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/title | "Structure, mechanism and regulation of peroxiredoxins."xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/title | "Structure, mechanism and regulation of peroxiredoxins."xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/volume | "28"xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://purl.uniprot.org/core/volume | "28"xsd:string |
| http://purl.uniprot.org/citations/12517450 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12517450 |
| http://purl.uniprot.org/citations/12517450 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12517450 |