Protein Kinase C Inhibition of the Epidermal Growth Factor Receptor Tyrosine Protein Kinase Activity is Independent of the Oligomeric State of the Receptor

This publication has 31 references indexed in Scilit:

• The epidermal growth factor receptor as a multifunctional allosteric protein
  Biochemistry, 1988
• Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor
  Biochemistry, 1987
• Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activation
  Biochemistry, 1987
• Allosteric regulation of the epidermal growth factor receptor kinase.
  The Journal of cell biology, 1986
• Epidermal growth factor (EGF) promotes phosphorylation at threonine-654 of the EGF receptor: possible role of protein kinase C in homologous regulation of the EGF receptor.
  The Journal of cell biology, 1986
• Protein kinase C phosphorylation at Thr 654 of the unoccupied EGF receptor and EGF binding regulate functional receptor loss by independent mechanisms
  Cell, 1986
• Intrapeptide autophosphorylation of the epidermal growth factor receptor: regulation of kinase catalytic function by receptor dimerization
  Biochemistry, 1985
• Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membrane
  Nature, 1984
• “Western Blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
  Analytical Biochemistry, 1981
• Local aggregation of hormone–receptor complexes is required for activation by epidermal growth factor
  Nature, 1979