Linked Life Data

11978480

Source:http://linkedlifedata.com/resource/pubmed/id/11978480

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2002-4-29
pubmed:abstractText
The oxidative modification of proteins by reactive species is implicated in the etiology or progression of a panoply of disorders and diseases. The level of these modified molecules can be quantitated by measurement of the protein carbonyl content, which has been shown to increase in a variety of diseases and processes, notably during aging. For the most part, oxidatively modified proteins are not repaired and must be removed by proteolytic degradation, a process which normally proceeds very efficiently, from microorganisms to mammals. In eukaryotes, removal is usually carried out by the proteosome, which selectively degrades oxidatively modified proteins, whether they be damaged by reactive oxygen species or specifically oxidized by cellular regulatory processes. The molecular deficiencies that cause accumulation of oxidatively modified proteins are not identified, but regardless of cause, the accumulation is likely to disrupt normal cellular function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0891-5849
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
790-6
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Carbonyl modified proteins in cellular regulation, aging, and disease.
pubmed:affiliation
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892-0312, USA. rlevine@nih.gov
pubmed:publicationType
Journal Article, Review