Phosphorylase kinase specificity. A comparative study with cAMP-dependent protein kinase on synthetic peptides and peptide analogs of glycogen synthase and phosphorylase.

This publication has 21 references indexed in Scilit:

• Nuclear magnetic resonance studies of the conformation and kinetics of the peptide-substrate at the active site of bovine heart protein kinase
  Biochemistry, 1981
• Phosphorylation of glycogen synthase by phosphorylase kinase
  FEBS Letters, 1979
• Glycogen Synthase Kinase-2 and Phosphorylase Kinase Are the Same Enzyme
  European Journal of Biochemistry, 1979
• Phosphorylation and inactivation of glycogen synthase by phosphorylase kinase.
  Proceedings of the National Academy of Sciences, 1979
• Phosphorylation-Dephosphorylation of Enzymes
  Annual Review of Biochemistry, 1979
• Phosphorylation of synthetic peptide analogs of the phosphorylatable site of phosphorylase b with phosphorylase kinase
  Biochemical and Biophysical Research Communications, 1979
• Use of a double-headed peptide substrate to study the specificity of cAMP-dependent protein kinase and posphorylase kinase.
  Published by Elsevier ,1978
• Occurrence of phosphorylated residues in predicted β-turns: Implications for β-turn participation in control mechanisms
  Biochemical and Biophysical Research Communications, 1977
• The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liver
  Biochemical and Biophysical Research Communications, 1976
• Protein Phosphorylation
  Annual Review of Biochemistry, 1975