Abstract
The ras proto-oncogene products appear to relay intracellular signals via the Ras guanosine triphosphatase (GTPase) activator protein, GAP. In dog epithelial cells expressing human platelet-derived growth factor (PDGF) receptors, binding of PDGF caused approximately one-tenth of the total GAP molecules to complex with the receptor. Studies with mutant PDGF receptors showed that maximum association required both receptor kinase activity and phosphorylatable tyrosine residues at both the identified sites of receptor autophosphorylation.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 6:10 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 12, 2024, 5:25 a.m.) |
Indexed | 3 weeks, 1 day ago (Aug. 2, 2025, 12:09 a.m.) |
Issued | 35 years, 4 months ago (March 30, 1990) |
Published | 35 years, 4 months ago (March 30, 1990) |
Published Print | 35 years, 4 months ago (March 30, 1990) |
@article{Kazlauskas_1990, title={Binding of GAP to Activated PDGF Receptors}, volume={247}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.2157284}, DOI={10.1126/science.2157284}, number={4950}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Kazlauskas, Andrius and Ellis, Christine and Pawson, Tony and Cooper, Jonathan A.}, year={1990}, month=mar, pages={1578–1581} }