Phosphorylation and inactivation of rat hepatocyte glycogen synthase by phorbol esters and mezerein
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference23 articles.
1. Glycogen Synthase and Glycogen Synthase Kinases
2. The role of protein phosphorylation in neural and hormonal control of cellular activity
3. Purification and phosphorylation of rat liver glycogen synthase.
4. Phosphorylation and inactivation of liver glycogen synthase by liver protein kinases.
5. Phosphorylation of rabbit liver glycogen synthase by multiple protein kinases.
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1. Control of Liver Glycogen Synthase Activity and Intracellular Distribution by Phosphorylation;Journal of Biological Chemistry;2009-03
2. Inactivation of protein kinase C in rat liver during late hypoglycemic phase of sepsis;Molecular and Cellular Biochemistry;1998
3. Protein kinase C and insulin receptor β-subunit serine phosphorylation in cultured foetal rat hepatocytes;Molecular and Cellular Endocrinology;1994-10
4. Reciprocal effects of the protein kinase C inhibitors staurosporine and H-7 on the regulation of glycogen synthase and phosphorylase in the primary culture of hepatocytes;Metabolism;1993-11
5. Insulin-mimetic actions of phorbol ester in cultured adult rat hepatocytes. Lack of phorbol-ester-elicited inhibition of the insulin signal;Biochemical Journal;1993-01-15
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