cDNA cloning of a Novel 85 kd protein that has SH2 domains and regulates binding of PI3-kinase to the PDGF β-receptor

Author:

Escobedo Jaime A.,Navankasattusas Sutip,Kavanaugh W.Michael,Milfay Dale,Fried Victor A.,Williams Lewis T.

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference38 articles.

1. Binding of SH2 domains of PLC-γ1, GAP and src to activated growth factor receptors;Anderson;Science,1990

2. PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells;Auger;Cell,1989

3. Purification and characterization of phosphoinositide 3-kinase from rat liver;Carpenter;J. Biol. Chem.,1990

4. Characterization of pp85, a target of oncogenes and growth factor receptors;Cohen;Mol. Cell. Biol.,1990

5. Tyrosine phosphorylation is a signal for the trafficking of pp85, an 85kDa phosphorylated polypeptide associated with phosphatidylinositol kinase activity;Cohen,1990

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