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Cited by 245

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity.

Open access
Gould, K L, Hunter, T·1988·Molecular and Cellular Biology

Abstract

We have shown previously that pp60c-src is a substrate for protein kinase C in vivo and that the target of protein kinase C phosphorylation in mammalian pp60c-src is serine 12. We now demonstrate that in addition to tumor promoters, all activators of phosphatidylinositol turnover that we have tested in fibroblasts (platelet-derived growth factor, fibroblast growth factor, serum, vasopressin, sodium orthovanadate, and prostaglandin F2 alpha) lead to the phosphorylation of pp60c-src at serine 12. In addition to stimulating serine 12 phosphorylation in pp60c-src, platelet-derived growth factor treatment of quiescent fibroblasts induces phosphorylation of one or two additional serine residues and one tyrosine residue within the N-terminal 16 kilodaltons of the enzyme and activates its immune complex protein-tyrosine kinase activity.

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Metadata

Authors
Gould, K. L., & Hunter, T.
Venue
Molecular and Cellular Biology
Published
1988-08
Volume
8
Issue
8
Pages
3345-3356
ISSN
  • 0270-7306 (ISSN-L)
  • 1098-5549
OpenAlex
W1854914172
Cited by
245
References
1
FWCI
9.15
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity. https://app.cochat.ai/papers/10.1128/mcb.8.8.3345
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Gould, K. L., & Hunter, T. (1988). Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.8.8.3345

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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