Cyclic AMP stimulated phosphorylation of liver pyruvate kinase in hepatocytes
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference23 articles.
1. Phosphorylation of purified rat liver pyruvate kinase by cyclic 3′,5′-AMP-stimulated protein kinase
2. Comparative kinetic studies on the L-type pyruvate kinase from rat liver and the enzyme phosphorylated by cyclic 3′,5′-AMP-stimulated protein kinase
3. Rapid Reciprocal Changes in Rat Hepatic Glycolytic Enzyme and Fructose Diphosphatase Activities following Insulin and Glucagon Injection
4. Regulation in vitro and in vivo of Adenosine 3':5'-monophosphate-Dependent Inactivation of Rat-Liver Pyruvate Kinase Type L
5. Hepatic pyruvate kinase. Regulation by glucagon, cyclic adenosine 3'-5'-monophosphate, and insulin in the perfused rat liver.
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1. Regulation of Fructose-Bisphosphatase Activity;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
2. Local and systemic alterations in cyclic 3′,5′ AMP phosphodiesterase activity in relation to tail regeneration under hypothyroidism and T4 replacement in the lizard,Mabuya carinata;Molecular Reproduction and Development;1996-09
3. In vivo regulation of glycolytic and gluconeogenic enzyme gene expression in newborn rat liver.;Journal of Clinical Investigation;1988-06-01
4. Stimulation of pyruvate kinase phosphatase activity by insulin in isolated rat hepatocytes;Biochemical and Biophysical Research Communications;1986-01
5. Insulin and glucagon's reciprocal mediation of a dual regulation mechanism for pyruvate kinase;Biochemical and Biophysical Research Communications;1984-10
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