The actions of cyclic AMP on biosynthetic processes are mediated indirectly by cyclic AMP-dependent protein kinase

This publication has 70 references indexed in Scilit:

• Calmodulin‐dependent multiprotein kinase and protein kinase C phosphorylate the same site on HMG‐CoA reductase as the AMP‐activated protein kinase
  FEBS Letters, 1990
• Identification of three in vivo phosphorylation sites on the glycogen‐binding subunit of protein phosphatase 1 from rabbit skeletal muscle, and their response to adrenaline
  FEBS Letters, 1990
• Regulation of protein phosphatase‐1_G from rabbit skeletal muscle
  European Journal of Biochemistry, 1989
• Negative interactions between phosphorylation of acetyl‐CoA carboxylase by the cyclic AMP‐dependent and AMP‐activated protein kinases
  FEBS Letters, 1988
• Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl‐CoA carboxylase
  European Journal of Biochemistry, 1988
• Phosphorylation of the glycogen‐binding subunit of protein phosphatase‐1_G in response to adrenalin
  FEBS Letters, 1988
• The low activity of acetyl‐CoA car☐ylase in basal and glucagon‐stimulated hepatocytes is due to phosphorylation by the AMP‐activated protein kinase and not cyclic AMP‐dependent protein kinase
  FEBS Letters, 1988
• Phosphorylase a is an allosteric inhibitor of the glycogen and microsomal forms of rat hepatic protein phosphatase‐1
  FEBS Letters, 1986
• Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle
  FEBS Letters, 1982
• Effect of epinephrine and insulin on the phosphorylation of phosphorylase phosphatase inhibitor 1 in perfused rat skeletal muscle
  FEBS Letters, 1980