The influence of basic residues on the substrate specificity of protein kinase C.

This publication has 37 references indexed in Scilit:

• Nonmuscle myosin phosphorylation sites for calcium-dependent and calcium-independent protein kinases
  Biochemical and Biophysical Research Communications, 1986
• 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
• Distinct structural requirements of Ca²⁺/phospholipid‐dependent protein kinase (protein kinase C) and cAMP‐dependent protein kinase as evidenced by synthetic peptide substrates
  FEBS Letters, 1985
• Protein kinase C phosphorylates the synthetic peptide Arg-Arg-Lys-Ala-Ser-Gly-Pro-Pro-Val in the presence of phospholipid plus either Ca2+ or a phorbol ester tumor promoter
  Biochemical and Biophysical Research Communications, 1984
• Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membrane
  Nature, 1984
• Phosphorylation of ribosomal protein S6 and a peptide analogue of S6 by a protease-activated kinase isolated from rat liver
  FEBS Letters, 1984
• Protein kinase C: Rapid enzyme purification and substrate-dependence of the diacylglycerol effect
  Biochemical and Biophysical Research Communications, 1984
• The calmodulin‐dependent glycogen synthase kinase from rabbit skeletal muscle
  European Journal of Biochemistry, 1983
• Myosin light chain kinase binding to plastic
  FEBS Letters, 1982
• Amino acid sequence at the site on rabbit skeletal muscle glycogen synthase phosphorylated by the endogenous glycogen synthase kinase‐2 activity
  FEBS Letters, 1979