Site-specific anti-phosphopeptide antibodies: use in assessing insulin receptor serine/threonine phosphorylation state and identification of serine-1327 as a novel site of phorbol ester-induced phosphorylation

This publication has 46 references indexed in Scilit:

• The insulin receptor C-terminus is involved in regulation of the receptor kinase activity
  Biochemistry, 1993
• Phorbol Esters Induce Insulin Receptor Phosphorylation in Transfected Fibroblasts without Affecting Tyrosine Kinase Activity
  Biochemical and Biophysical Research Communications, 1993
• Preparation of Anti-phosphoserine and Anti-phosphothreonine Antibodies and Their Application in the Study of Insulin- and EGF-Induced Phosphorylation
  Biochemical and Biophysical Research Communications, 1993
• Solid‐phase synthesis of a range of O‐phosphorylated peptides by post‐assembly phosphitylation and oxidation
  International Journal of Peptide and Protein Research, 1991
• The carboxyl-terminal domain of the insulin receptor: its potential role in growth-promoting effects
  Biochemistry, 1991
• Insulin binding to its receptor induces a conformational change in the receptor C-terminus
  Biochemistry, 1990
• Threonine 1336 of the human insulin receptor is a major target for phosphorylation by protein kinase C
  Biochemistry, 1990
• Antibodies directed against phosphothreonine residues as potent tools for studying protein phosphorylation
  European Journal of Biochemistry, 1989
• Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose
  Cell, 1986
• Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
  Proceedings of the National Academy of Sciences, 1979