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1
Inactivation of rabbit muscle phosphorylase phosphatase by cyclic AMP-dependent kinas.
Proc Natl Acad Sci U S A. 1975 Aug;72(8):3004-8. doi: 10.1073/pnas.72.8.3004.
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Separation and characterization of two phosphorylase phosphatase inhibitors from rabbit skeletal muscle.
Eur J Biochem. 1976 Nov 15;70(2):419-26. doi: 10.1111/j.1432-1033.1976.tb11032.x.
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A second heat-stable protein inhibitor of phosphorylase phosphatase from rabbit muscle.
FEBS Lett. 1976 Mar 1;62(3):326-9. doi: 10.1016/0014-5793(76)80086-5.
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Protein inhibitors of phosphorylase phosphatase and cyclic AMP-dependent protein kinase from rabbit skeleta muscle.
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The hormonal control of glycogen metabolism: the amino acid sequence at the phosphorylation site of protein phosphatase inhibitor-1.
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The regulation of glycogen metabolism. Purification and characterisation of protein phosphatase inhibitor-1 from rabbit skeletal muscle.
Eur J Biochem. 1978 Jun 15;87(2):341-51. doi: 10.1111/j.1432-1033.1978.tb12383.x.
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Reversible phosphorylation and inactivation of acetyl-CoA carboxylase from lactating rat mammary gland by cyclic AMP-dependent protein kinase.
Eur J Biochem. 1980 Sep;110(1):167-77. doi: 10.1111/j.1432-1033.1980.tb04852.x.
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Specificity of a protein phosphatase inhibitor from rabbit skeletal muscle.
Biochem J. 1977 Feb 15;162(2):435-44. doi: 10.1042/bj1620435.
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Role of phosphorylase kinase and cyclic AMP-dependent protein kinase in the regulation of phosphorylase phosphatase.
Biochem Soc Trans. 1978;6(1):21-5. doi: 10.1042/bst0060021.
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The control of phosphorylase phosphatase by cAMP-dependent protein kinase.
FEBS Lett. 1977 Oct 15;82(2):269-72. doi: 10.1016/0014-5793(77)80600-5.
引用本文的文献
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The split protein phosphatase system.
Biochem J. 2018 Dec 6;475(23):3707-3723. doi: 10.1042/BCJ20170726.
2
Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1.
Mol Cell Biol. 2001 Oct;21(20):6841-50. doi: 10.1128/MCB.21.20.6841-6850.2001.
3
Regulation of chromosome segregation by Glc8p, a structural homolog of mammalian inhibitor 2 that functions as both an activator and an inhibitor of yeast protein phosphatase 1.
Mol Cell Biol. 1995 Nov;15(11):6064-74. doi: 10.1128/MCB.15.11.6064.
4
In vivo modulation of rat liver 3-hydroxy-3-methylglutaryl-coenzyme A reductase, reductase kinase, and reductase kinase kinase by mevalonolactone.
Proc Natl Acad Sci U S A. 1984 Dec;81(23):7293-7. doi: 10.1073/pnas.81.23.7293.
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Liver phosphorylase phosphatase.
Mol Cell Biochem. 1982 Nov 12;49(1):3-15. doi: 10.1007/BF00230991.
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A partial view of the mechanism of insulin action.
Diabetologia. 1981 Oct;21(4):347-62. doi: 10.1007/BF00252681.
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Adrenal glucocorticoid permissive regulation of muscle glycogenolysis: action on protein phosphatase(s) and its inhibitor(s).
Proc Natl Acad Sci U S A. 1980 Oct;77(10):5711-5. doi: 10.1073/pnas.77.10.5711.
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Identification and partial characterization of a latent ATP, Mg-dependent protein phosphatase in rabbit skeletal muscle cytosol.
Mol Cell Biochem. 1989 May 4;87(1):31-9. doi: 10.1007/BF00421080.
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Characterization and regulation of reductase kinase, a protein kinase that modulates the enzymic activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase.
Proc Natl Acad Sci U S A. 1979 Sep;76(9):4375-9. doi: 10.1073/pnas.76.9.4375.
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Control of rat skeletal-muscle phosphorylase phosphatase activity by adrenaline.
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DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS.
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Studies on UDPG-glycogen transglucosylase. I. Preparation and differentiation of two activities of UDPG-glycogen transglucosylase from rat skeletal muscle.
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A method for determining the sedimentation behavior of enzymes: application to protein mixtures.
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Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels.
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Properties of a phosphoprotein phosphatase from bovine heart with activity on glycogen synthase, phosphorylase, and histone.
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Substrate specificity of glycogen synthase phosphatase from bovine heart: action on phosphorylase a and histone.
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Rabbit red cell cyclic AMP-dependent protein kinase. I. Reversible subunit interaction.
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Activation of glycogen synthetase and inactivation of phosphorylase kinase by the same phosphoprotein phosphatase.
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Glycogen synthetase-D phosphatase. I. Some new properties of the partially purified enzyme from rabbit skeletal muscle.
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Measurement of cyclic 3',5'-denosine monophosphate by the activation of skeletal muscle protein kinase.
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