The phosphopeptide-binding specificity of Src family SH2 domains

This publication has 51 references indexed in Scilit:

• Transformation by polyoma virus middle T-antigen involves the binding and tyrosine phosphorylation of Shc
  Nature, 1994
• Interaction of Shc with the ζ Chain of the T Cell Receptor Upon T Cell Activation
  Science, 1993
• Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras
  Nature, 1993
• Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling
  Nature, 1993
• The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
  Nature, 1993
• The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors.
  Molecular and Cellular Biology, 1992
• The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
  Cell, 1992
• A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction
  Cell, 1992
• PDGF stimulation of inositol phospholipid hydrolysis requires PLC-γ1 phosphorylation on tyrosine residues 783 and 1254
  Cell, 1991
• Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the src homology units SH2 and SH3
  Nucleic Acids Research, 1990