Linked Life Data

15189129

Source:http://linkedlifedata.com/resource/pubmed/id/15189129

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2004-6-10
pubmed:abstractText
Many proteins present on cell surfaces and located in extracellular fluids contain cysteine and methionine residues that are subject to oxidation. These proteins, which include transporters, receptors, and enzymes, respond to variations in the extracellular thiol/disulfide redox environment. Changes in activity of these proteins can alter the ability of organs to function normally and influence processes such as nutritional absorption, secretory function, neurotransmission, and susceptibility to toxicants. In addition, extracellular redox can regulate tissue homeostasis through effects on cell proliferation, differentiation, apoptosis, and immune function. Consequently, extracellular redox can have important influences on health status and disease states and thus could be a target for nutritional interventions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0199-9885
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
481-509
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Extracellular thiols and thiol/disulfide redox in metabolism.
pubmed:affiliation
Nutrition and Health Sciences Program, Emory University, Atlanta, Georgia 30322, USA. smoriar@emory.edu
pubmed:publicationType
Journal Article, Review