Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-8-20
pubmed:abstractText
Antigen-receptor signaling requires Src-family kinases to initiate tyrosine phosphorylation. CD45 dephosphorylates the inhibitory site in Src-family kinases before antigen-receptor engagement and thus serves to 'prime' the kinases. It has been unclear why CD45 does not also dephosphorylate 'activated' kinases or motifs within the cytoplasmic domains of antigen-receptors and thus prevent signal transduction. Recent reports raise the possibility that CD45 is excluded from engaged antigen-receptors by mechanisms that may include the formation of lipid microdomains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0952-7915
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
270-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
The regulation of antigen-receptor signaling by protein tyrosine phosphatases: a hole in the story.
pubmed:affiliation
Howard Hughes Medical Institute, Box 8118, Departments of Pathology andMolecular Microbiology, Washington University School of Medicine, St Louis, MO 63110, USA. mthomas@pathbox.wustl.edu
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't