Phospholipase C-gamma, a substrate for PDGF receptor kinase, is not phosphorylated on tyrosine during the mitogenic response to CSF-1.

Antzeko izenburuak

• Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor.
  nork: Margolis, B, et al.
  Argitaratua: (1990)
• The tyrosine phosphorylated carboxyterminus of the EGF receptor is a binding site for GAP and PLC-gamma.
  nork: Margolis, B, et al.
  Argitaratua: (1990)
• Characterization and cDNA cloning of phospholipase C-gamma, a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase.
  nork: Burgess, W H, et al.
  Argitaratua: (1990)
• Fc epsilon R1-mediated tyrosine phosphorylation of multiple proteins, including phospholipase C gamma 1 and the receptor beta gamma 2 complex, in RBL-2H3 rat basophilic leukemia cells.
  nork: Li, W, et al.
  Argitaratua: (1992)
• The erbB-2 mitogenic signaling pathway: tyrosine phosphorylation of phospholipase C-gamma and GTPase-activating protein does not correlate with erbB-2 mitogenic potency.
  nork: Fazioli, F, et al.
  Argitaratua: (1991)