A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1.

Lignende værker

• SH2 domains prevent tyrosine dephosphorylation of the EGF receptor: identification of Tyr992 as the high-affinity binding site for SH2 domains of phospholipase C gamma.
  af: Rotin, D, et al.
  Udgivet: (1992)
• Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor.
  af: Margolis, B, et al.
  Udgivet: (1990)
• Receptor for acidic fibroblast growth factor is related to the tyrosine kinase encoded by the fms-like gene (FLG).
  af: Ruta, M, et al.
  Udgivet: (1989)
• Characterization and cDNA cloning of phospholipase C-gamma, a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase.
  af: Burgess, W H, et al.
  Udgivet: (1990)
• Phospholipase C-gamma, a substrate for PDGF receptor kinase, is not phosphorylated on tyrosine during the mitogenic response to CSF-1.
  af: Downing, J R, et al.
  Udgivet: (1989)