The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110.

S B Kanner(University of Virginia Health System), A B Reynolds(University of Virginia Health System), Hwa‐Chain Robert Wang(University of Virginia Health System), R R Vines(University of Virginia Health System), J.T. Parsons(University of Virginia Health System)
The EMBO Journal
July 1, 1991
10.1002/j.1460-2075.1991.tb07693.x
Cited by 219Open Access
Full Text

Abstract

Related Papers

Oligonucleotide-Directed Mutagenesis: A Simple Method Using Two Oligonucleotide Primers and a Single-Stranded DNA Template
Mark J. Zoller, Michael J. Smith|DNA|1984|906
Binding of SH2 Domains of Phospholipase Cγ1, GAP, and Src to Activated Growth Factor Receptors
Deborah H. Anderson, Christine Koch, Laura Grey et al.|Science|1990|614
Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src
Helen Piwnica‐Worms, Kim B. Saunders, Thomas M. Roberts et al.|Cell|1987|538
Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins
Andrius Kazlauskas, Jonathan A. Cooper|Cell|1989|519
Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses
Leah Lipsich, Angela Lewis, Joan S. Brugge|Journal of Virology|1983|517