Linked Life Data

21341108

Source:http://linkedlifedata.com/resource/pubmed/id/21341108

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2011-2-22
pubmed:abstractText
Posttranslational modification has long been recognized as a way in which the properties of proteins may be subtly altered after synthesis of the polypeptide chain is complete. Amongst the moieties most commonly encountered covalently attached to proteins are oligosaccharides, phosphate, acetyl, formyl, and nucleosides. Posttranslational covalent modification of protein by phosphorylation is one of the most prevalent and best understood mechanisms employed in cellular regulation (1-9). Protein kinases catalyze the transfer of the ?-phosphoryl group of adenosine triphosphate (ATP) to an acceptor protein substrate. The activity of the enzyme is determined by the transfer of (32)P (labeled ?-phosphate) from [?-(32)P] ATP to protein substrate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1940-6029
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
312
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
305-24
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Assay and purification of calmodulin-dependent protein kinase.
pubmed:affiliation
Department of Pathology, Saskatoon Cancer Centre, College of Medicine, University of Saskatchewan, Sakatoon, Saskatchewan, Canada.
pubmed:publicationType
Journal Article