Phosphorylation at conserved carboxyl-terminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C

Journal of Biological Chemistry

Volumn 272, Issue 29, 1997, Pages 18382-18390

  Edwards, Amelia S ^a   Newton, Alexandra C ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE; CALCIUM ION; GLUTAMIC ACID; PEPTIDE; PHOSPHATIDYLSERINE; PROTEIN KINASE C; SERINE;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME PHOSPHORYLATION; ENZYME STABILITY; ENZYME SUBSTRATE; HYDROPHOBICITY; INSECT; LEPIDOPTERA; MEMBRANE BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN;

ALANINE; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALCIUM; CELL LINE; CONSERVED SEQUENCE; DNA PRIMERS; ENZYME STABILITY; GLUTAMIC ACID; GLYCEROL; KINETICS; LIPOSOMES; MODELS, STRUCTURAL; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; POINT MUTATION; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION; PROTEIN KINASE C; RECOMBINANT PROTEINS; SERINE; SPODOPTERA; THERMODYNAMICS; TRANSFECTION;

ANIMALIA; INSECTA; LEPIDOPTERA;

EID: 0030875555     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.29.18382     Document Type: Article

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