Insulin stimulation of the insulin receptor kinase can occur in the complete absence of beta subunit autophosphorylation.

This publication has 46 references indexed in Scilit:

• Alteration of intramolecular disulfides in insulin receptor/kinase by insulin and dithiothreitol: insulin potentiates the apparent dithiothreitol-dependent subunit reduction of insulin receptor
  Biochemistry, 1986
• Kinetic evidence for activating and non-activating components of autophosphorylation of the insulin receptor protein kinase
  Biochemical and Biophysical Research Communications, 1986
• Incorporation of the purified human placental insulin receptor into phospholipid vesicles
  Biochemistry, 1985
• Phosphorylation and dephosphorylation of the insulin receptor: evidence against an intrinsic phosphatase activity
  Biochemistry, 1984
• Mutagenesis of Fujinami Sarcoma Virus: Evidence that tyrosine phosphorylation of P130gag-fps modulates its biological activity
  Cell, 1984
• Stimulation of tyrosine-specific phosphorylation in vitro by insulin-like growth factor I
  Nature, 1983
• The .beta. subunit of the insulin receptor kinase is an insulin-activated protein
  Biochemistry, 1983
• Transforming capacities of avian erythroblastosis virus mutants deleted in the erbA or erbB oncogenes
  Cell, 1983
• Epidermal growth factor induces rapid tyrosine phosphorylation of proteins in A431 human tumor cells
  Cell, 1981
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970