Linked Life Data

17662654

Source:http://linkedlifedata.com/resource/pubmed/id/17662654

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2007-8-28
pubmed:abstractText
Reversible protein S-glutathionylation (protein-SSG) is an important post-translational modification, providing protection of protein cysteines from irreversible oxidation and serving to transduce redox signals. Analogous to phosphatases, glutaredoxin (GRx) enzymes catalyze deglutathionylation of proteins, regulating diverse intracellular signaling pathways. Recently, other enzymes have been reported to exhibit deglutathionylating activity, but their contribution to intracellular protein deglutathionylation is uncertain. Currently, no enzyme has been shown to serve as a catalyst of S-glutathionylation in situ, although potential prototypes are reported, including human GRx1 and the pi isoform of glutathione-S-transferase (GSTpi). Further insight into cellular mechanisms of protein glutathionylation and deglutathionylation will enrich our understanding of redox signal transduction and potentially identify new therapeutic targets for diseases in which oxidative stress perturbs normal redox signaling. Accordingly, this review focuses primarily on mechanisms of catalysis in mammalian systems.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1471-4892
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
381-91
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress.
pubmed:affiliation
Department of Pharmacology, School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, and the Louis Stokes Cleveland Veterans Affairs Medical Research Center, Cleveland, OH 44106-4965, United States.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Review, Research Support, N.I.H., Extramural