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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1987-11-18
|
| pubmed:abstractText |
Protein-tyrosine kinase activities have appeared so far to be intrinsic for two classes of proteins: the transforming proteins of certain retroviral oncogenes and the membrane receptors for certain cellular growth factors. In this latter family, the protein-tyrosine kinase is activated upon binding of the growth factor to its receptor and phosphorylates both the receptor itself and other cell target proteins. Growth factor receptors are transmembrane glycoproteins able to undergo not only autophosphorylation but also phosphorylation by other protein kinases (e.g., protein kinase C). Both autophosphorylation and heterologous phosphorylation of the receptor are regulatory events for the ligand binding and protein-tyrosine kinase intrinsic activities of the growth factor receptors.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0300-9084
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
69
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
379-85
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading | |
| pubmed:year |
1987
|
| pubmed:articleTitle |
Membrane receptors with protein-tyrosine kinase activity.
|
| pubmed:affiliation |
INSERM U244, DRF/LBIO/BRCE, Centre d'Etudes Nucléaires, Grenoble, France.
|
| pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|