Nonactivated phosphorylase kinase is a phosphoprotein: differentiation of two classes of endogenous phosphoserine residues by phosphorus-31-NMR spectroscopy and phosphatase sensitivity
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00296a018
Reference35 articles.
1. Phosphorus Assay in Column Chromatography
2. Stimulation of phosphorylase kinase autophosphorylation by peptide analogs of phosphorylase.
3. The Subunit Structure of Rabbit-Skeletal-Muscle Phosphorylase Kinase, and the Molecular Basis of Its Activation Reactions
4. The Role of Cyclic-AMP-Dependent Protein Kinase in the Regulation of Glycogen Metabolism in Mammalian Skeletal Muscle
5. Phosphorylation of rabbit skeletal muscle phosphorylase kinase by cyclic GMP-dependent protein kinase
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1. Phosphorylation and Flexibility of Cyclic-AMP-Dependent Protein Kinase (PKA) Using 31P NMR Spectroscopy;Biochemistry;2002-04-18
2. Characterization of the cardiac troponin I phosphorylation domain by 31P nuclear magnetic resonance spectroscopy;Biochemistry;1993-12-01
3. The multiphosphorylation domain of the phosphorylase kinase alpha M and alpha L subunits is a hotspot of differential mRNA processing and of molecular evolution.;Journal of Biological Chemistry;1993-11
4. Localization of phosphoserine residues in the a subunit of rabbit skeletal muscle phosphorylase kinase;European Journal of Biochemistry;1990-03
5. [13] Phosphorus-31 nuclear magnetic resonance of phosphoproteins;Methods in Enzymology;1989
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