Linked Life Data

7771771

Source:http://linkedlifedata.com/resource/pubmed/id/7771771

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-7-3
pubmed:abstractText
Protein S-thiolation/dethiolation, i.e., the oxidation of protein sulfhydryls to mixed disulfides and their reduction back to sulfhydryls, is an early cellular response to oxidative stress (1-5). This response may be elicited by oxidative phenomena of diverse origins, and the few cases that have been studied extensively give a limited insight into the metabolic roles and the molecular mechanism of the process. Much of our current understanding arose from experiences with isolated proteins containing "reactive" sulfhydryls (6, 7), but recent experiments at the cellular level have begun to reveal interesting insights that suggest a complexity and importance not appreciated previously (8). This article will discuss the current status of experiments that relate to both the role of the cellular process and to the reactivity of selected proteins that participate in the cellular processes. The discussion will center on the role of glutathione, a molecule of central interest in every aspect of protein S-thiolation and dethiolation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
319
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation.
pubmed:affiliation
Department of Biochemistry and Biophysics, Iowa State University, Ames, Iowa 50011, USA.
pubmed:publicationType
Journal Article, Comparative Study, Review