Specificity of a rat liver protein phosphatase active on caseins phosophorylated by two cAMP-independent protein kinases
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(81)81000-9/fullpdf
Reference29 articles.
1. Non-dependence on native structure of pig liver pyruvate kinase when used as a substrate for cyclic 3′,5′-AMP-stimulated protein kinase
2. The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liver
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1. Specific dephosphorylation of phosphopeptides by the yeast alkaline phosphatase encoded by PHO8 gene;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1993-06
2. An investigation of the substrate specificity of protein phosphatase 2C using synthetic peptide substrates; comparison with protein phosphatase 2A;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1990-02
3. Filaggrins;Cellular and Molecular Biology of Intermediate Filaments;1990
4. Characterization of an Epidermal Phosphatase Specific for Filaggrin Phosphorylated by Casein Kinase II;Journal of Investigative Dermatology;1988-12
5. Identification of pseudo ‘phosphothreonyl-specific’ protein phosphatase T with a fraction of polycation-stimulated protein phosphatase 2A;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1988-02
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