Linked Life Data

3047204

Source:http://linkedlifedata.com/resource/pubmed/id/3047204

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1988-10-17
pubmed:abstractText
The age-related accumulation of abnormal forms of enzymes is attributable to posttranslational modification of protein structure and to a progressive loss with age of proteases that preferentially degrade the modified forms. The protein modifications include, but are not limited to: the oxidation of amino acid side chains (especially, side chains of prolyl, arginyl, lysyl and histidinyl residues) by mixed-function oxidation systems; the deamidation of asparaginyl and glutaminyl residues; the racemization and isomerization of aspartyl and asparaginyl residues; the isomerization of prolyl residues; the oxidation of cysteine sulfhydryl groups; and spontaneous changes in protein conformation that are apparently unlinked to changes in amino acid composition. Evidence supporting the roles of these protein modifications and of the proteases that degrade abnormal enzymes during aging is discussed, as well as a consideration of some technical limitations of the methods used in their study.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-1422
pubmed:author
pubmed:issnType
Print
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
B112-20
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Protein modification in aging.
pubmed:affiliation
Laboratory of Biochemistry, National Heart, Lung and Blood Institute, Bethesda MD 20892.
pubmed:publicationType
Journal Article, Review