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Dephosphorylation of cardiac myofibril C-protein by protein phosphatase 1 and protein phosphatase 2A
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1987C-protein purified from chicken cardiac myofibrils was phosphorylated with the catalytic subunit of cAMP-dependent protein kinase to nearly 3 mol [32P]phosphate/mol C protein. Digestion of 32P-labeled C-protein with trypsin revealed that the radioactivity was nearly equally distributed in three tryptic peptides which were separated by reversed-phase ...
K K, Schlender +2 more
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Immobilized inhibitor-1 binds and inhibits protein phosphatase 1
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1989Inhibitor-1 is a potent and specific inhibitor of protein phosphatase 1. Phosphorylation by cAMP-dependent protein kinase is required for expression of its inhibitor activity. In the present study, we have used immobilized inhibitor-1 preparations to study the mechanism underlying protein phosphatase 1 inhibition.
V M, Ingebritsen, T S, Ingebritsen
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Interactor-Guided Dephosphorylation by Protein Phosphatase-1
2013Protein phosphatase-1 (PP1) is an essential enzyme for every eukaryotic cell and catalyzes more than half of all protein dephosphorylations at serine and threonine residues. The free catalytic subunit of PP1 shows little substrate selectivity but is tightly regulated in vivo by a large variety of structurally unrelated PP1-interacting proteins (PIPs ...
Shannah, Boens +3 more
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Identification of Cellular Protein Phosphatase-1 Regulators
2007Protein phosphatase-1 (PP1) is a major phosphoserine/phosphothreonine phosphatase that regulates multiple physiological events in all eukaryotic cells. Action of PP1 in cells is dictated by the association of PP1 catalytic subunit with one or more regulatory subunits that define both its catalytic function and subcellular localization.
David W, Roadcap +2 more
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Protein phosphatase 1 – targeted in many directions
Journal of Cell Science, 2002Protein phosphatase 1 (PP1) is a major eukaryotic protein serine/threonine phosphatase that regulates an enormous variety of cellular functions through the interaction of its catalytic subunit (PP1c) with over fifty different established or putative regulatory subunits.
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Regulation of Recombinant PKCα Activity by Protein Phosphatase 1 and Protein Phosphatase 2A
Archives of Biochemistry and Biophysics, 1998The sensitivity of PKC alpha to two protein phosphatases (PP1 and PP2A) has been studied. The results show that both phosphatases reversibly inhibit PKC alpha activity suggesting an effect at PKC autophosphorylation sites and not at transphosphorylation sites.
RICCIARELLI, ROBERTA, AZZI A.
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Protein phosphatase-1 and protein phosphatase-2A from rabbit skeletal muscle.
Methods in enzymology, 1988This chapter describes the purification of two forms of protein phosphatase- 1 (PP-I 1 and PP-l G ), and three forms of protein phosphatase-2A (PP-2A 0 , PP-2A 1 , and PP-2A 2 ) from skeletal muscle. Procedures for isolating the free catalytic subunits (termed PP-l c and PP-2A c ) are documented and the structures of these enzymes are summarized in the
Cohen, Philip +5 more
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