Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-12-24
pubmed:abstractText
Human immunodeficiency virus type-1 Tat protein is phosphorylated by protein kinase C in a calcium-, diacylglycerol-, and phosphatidylserine-dependent manner. Maximum phosphorylation is reached at a stoichiometry of between 0.45 and 0.5 mol of phosphate per mol of Tat. Several Tat peptides, containing serine at position 46, are the only ones which are phosphorylated at significant rates. Several other Tat peptides containing potential protein kinase C phosphorylation sites are not phosphorylated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
335
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8-12
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
In vitro phosphorylation of human immunodeficiency virus type 1 Tat protein by protein kinase C: evidence for the phosphorylation of amino acid residue serine-46.
pubmed:affiliation
Biochemistry Department, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.