| Literature DB >> 2460746 |
T E Kmiecik1, P J Johnson, D Shalloway.
Abstract
We show that overexpressed pp60c-src is phosphorylated at Tyr-416 and has increased specific kinase activity when isolated from cells incubated with vanadate, a tyrosine phosphatase inhibitor. This supports the hypothesis that transient Tyr-416 phosphorylation modulates the activity of overexpressed pp60c-src in vivo. Mutagenesis indicates that Tyr-416 modulates pp60v-src activity as well.Entities:
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Year: 1988 PMID: 2460746 PMCID: PMC365532 DOI: 10.1128/mcb.8.10.4541-4546.1988
Source DB: PubMed Journal: Mol Cell Biol ISSN: 0270-7306 Impact factor: 4.272