The Role of Ca2+ and Cyclic AMP in the Phosphorylation of Rat-Liver Soluble Proteins by Endogenous Protein Kinases
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1980.tb06147.x/fullpdf
Reference43 articles.
1. Studies on the role of adenosine 3‘:5‘-monophosphate in the activation of liver phosphorylase.
2. Purification and phosphorylation of rat liver glycogen synthase.
3. Purification and properties of rabbit-liver glycogen synthase
4. The Regulation of Liver Pyruvate Kinase by Phosphorylation—Dephosphorylation
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1. Evidence for the activation of the multifunctional Ca2+/calmodulin-dependent protein kinase in response to hormones that increase intracellular Ca2+.;Journal of Biological Chemistry;1987-07
2. Gluconeogenesis and its regulation;Diabetes / Metabolism Reviews;1987-01
3. Phosphorylation of endogenous proteins, including histones, during initiation of planarian regeneration;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1985-01
4. Endogenous protein phosphorylation in chick and rat brain synaptic membranes;Neuroscience;1983-12
5. Protein kinases in normal human blood cells;American Journal of Hematology;1983-09
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