Phosphoprotein inhibitor CPI-17 specificity depends on allosteric regulation of protein phosphathase-1 by regulatory subunits

Proceedings of the National Academy of Sciences of the United States of America

Volumn 101, Issue 24, 2004, Pages 8888-8893

  Eto, Masumi ^a   Kitazawa, Toshio ^b   Brautigan, David L ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

^b BOSTON BIOMEDICAL RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALYCULIN A; GLYCOGEN; HOLOENZYME; INHIBITOR PROTEIN; MYOSIN PHOSPHATASE; PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEIN CPI 17; PROTEIN KINASE C; UNCLASSIFIED DRUG;

AFFINITY CHROMATOGRAPHY; ALLOSTERISM; ANIMAL TISSUE; ARTICLE; CELL LYSATE; DEPHOSPHORYLATION; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME SUBUNIT; MALE; NONHUMAN; PRIORITY JOURNAL; SMOOTH MUSCLE CONTRACTION;

ALLOSTERIC REGULATION; ANIMALS; BINDING SITES; CERCOPITHECUS AETHIOPS; COS CELLS; ENZYME INHIBITORS; FEMORAL ARTERY; HOLOENZYMES; HUMANS; MICE; MUSCLE PROTEINS; MUSCLE, SMOOTH, VASCULAR; MYOSIN-LIGHT-CHAIN PHOSPHATASE; NIH 3T3 CELLS; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN SUBUNITS; PROTEINS; RABBITS; RECOMBINANT FUSION PROTEINS;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 2942674285     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0307812101     Document Type: Article

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