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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1990-9-26
|
| pubmed:abstractText |
Recent demonstrations of growth factor-stimulated increases in cellular phosphoinositide metabolism suggest that regulatory enzymes of this important signaling pathway may be substrates for growth factor receptor tyrosine kinases. Studies employing phosphotyrosine antibodies, specific phospholipase C antibodies, and purified phospholipase C proteins support the conclusion that the 145-kD phospholipase C-gamma 1 isoenzyme is rapidly and selectively phosphorylated by the activated epidermal growth factor and platelet-derived growth factor receptors. The selective interaction of these receptors with phospholipase C-gamma 1 suggests a novel, direct mechanism for agonist stimulation of phosphoinositide metabolism.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
1042-2196
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
1
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
101-7
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1989
|
| pubmed:articleTitle |
Growth factor signaling pathways: phosphoinositide metabolism and phosphorylation of phospholipase C.
|
| pubmed:affiliation |
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
|