Heparin inhibition and polyamine stimulation of a glycogen synthase kinase (PC0.7) from rabbit skeletal muscle
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference42 articles.
1. Multiple phosphorylation of rabbit skeletal muscle glycogen synthase. Comparison of the actions of different protein kinases capable of catalyzing phosphorylation in vitro.
2. Characterization of a rabbit skeletal muscle protein kinase (PC0.7) able to phosphorylate glycogen synthase and phosvitin.
3. Phosphorylation of glycogen synthase and of the beta subunit of eukaryotic initiation factor two by a common protein kinase.
4. Rabbit liver glycogen synthase kinases. Characterization of a protein kinase (PC0.7) able to phosphorylate glycogen synthase and phosvitin.
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1. Protein kinases phosphorylating acidic ribosomal proteins from yeast cells;Folia Microbiologica;1999-04
2. Casein kinase II activity and polyamine-stimulated protein phosphorylation of cytosolic and plasma membrane proteins in bovine sperm;Archives of Biochemistry and Biophysics;1989-05
3. Inhibitory effect of polycations on phosphorylation of glycogen synthase by glycogen synthase kinase 3;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1989-05
4. Inhibition of the β-Adrenergic Receptor Kinase by Polyanions;Journal of Biological Chemistry;1989-04
5. Polyamines stimulate the activity of glycogen synthase (casein) kinase-1 from bovine kidney and different rat tissues;Archives of Biochemistry and Biophysics;1988-11
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