Phorbol ester-induced serine phosphorylation of the insulin receptor decreases its tyrosine kinase activity.

This publication has 50 references indexed in Scilit:

• The Complete Primary Structure of Protein Kinase C—the Major Phorbol Ester Receptor
  Science, 1986
• Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose
  Cell, 1986
• Insulin rapidly stimulates tyrosine phosphorylation of a Mr-185,000 protein in intact cells
  Nature, 1985
• Site-Specific Increased Phosphorylation of pp60 ^{v- src} After Treatment of RSV-Transformed Cells with a Tumor Promoter
  Science, 1985
• Protein kinase C phosphorylates the inhibitory guanine‐nucleotide‐binding regulatory component and apparently suppresses its function in hormonal inhibition of adenylate cyclase
  European Journal of Biochemistry, 1985
• Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes
  Nature, 1985
• Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membrane
  Nature, 1984
• Phosphorylation and dephosphorylation of the insulin receptor: evidence against an intrinsic phosphatase activity
  Biochemistry, 1984
• Effect of a tumour promoter on myogenesis
  Nature, 1977
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970