Summary pp6OC-S'C is phosphorylated in vivo at tyrosine 527, a residue not present in
pp60v-Jrc (its transforming homolog), and not at tyrosine 416, its site of in vitro …

We introduced two mutations into the carboxy-terminal regulatory region of chicken pp60”*
rC. One, F527, replaces tyrosine 527 with phenylalanine. The other, Am517, produces a …

To investigate the importance of tyrosine phosphorylation in the regulation of pp60c-src, we
have substituted phenylalanine for tyrosine at positions 416, 519, and 527. Cells expressing …

We show that overexpressed pp60 c-src is phosphorylated at Tyr-416 and has increased
specific kinase activity when isolated from cells incubated with vanadate, a tyrosine …

The tyrosine protein kinase activities of pp60 c-src and pp60 v-src were compared. The
activities were qualitatively similar in vitro when the src proteins were bound in an immune …

Phosphorylation of pp60 c-src at Tyr-527, six residues from the carboxy terminus, has been
implicated in regulation of the protein-tyrosine kinase activity of pp60 c-src. Here we show …

The overexpression of the c-src gene product, pp60c-src, in avian and rodent embryo cells is
not sufficient to induce cellular transformation. In this study we report that structural …

In previous studies examining the potential role of pp60 c-src in cellular proliferation, we
demonstrated that C3H10T1/2 murine embryo fibroblasts overexpressing transfected …

We recently identified a novel protein tyrosine kinase that specifically phosphorylates
truncated pp60 c-src (M r= 53,000) at a tyrosine residue (s) distinct from its …

We have previously found that Rous sarcoma virus variants in which the viral src (v-src)
gene is replaced by the cellular src (c-src) gene have no transforming activity. In this study …