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

This publication has 9 references indexed in Scilit:

• Regulation in vitro of rat liver pyruvate kinase by phosphorylation-dephosphorylation reactions, catalyzed by cyclic-AMP dependent protein kinases and a histone phosphatase
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1976
• Amino acid sequence at the phosphorylated site of rat liver pyruvate kinase
  Biochemical and Biophysical Research Communications, 1975
• Synthetic substrate for cyclic AMP-dependent protein kinase
  Nature, 1975
• Non-dependence on native structure of pig liver pyruvate kinase when used as a substrate for cyclic 3′,5′-AMP-stimulated protein kinase
  Biochemical and Biophysical Research Communications, 1975
• Bovine brain Na+, K′-stimulated ATP phosphohydrolase studied by a rapid-mixing technique, K′-stimulated liberation of [32P]orthophosphate from [32P]phosphoenzyme and resolution of the dephosphorylation into two phases
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1975
• Peptides from myelin basic protein as substrates for adenosine 3′, 5′-cyclic monophosphate-dependent protein kinases
  Biochemical and Biophysical Research Communications, 1974
• Phosphorylation of purified rat liver pyruvate kinase by cyclic 3′,5′-AMP-stimulated protein kinase
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1974
• Multiplicity of Adenosine 3′,5′-Monophosphate-dependent Protein Kinases from Rat Liver and Mode of Action of Nucleoside 3′,5′-Monophosphate
  Published by Elsevier ,1972
• Solid Phase Peptide Synthesis. I. The Synthesis of a Tetrapeptide
  Journal of the American Chemical Society, 1963