Phosphorylation of specific serine residues in the PKR activation domain of PACT is essential for its ability to mediate apoptosis

Journal of Biological Chemistry

Volumn 281, Issue 46, 2006, Pages 35129-35136

  Peters, Gregory A ^a   Li, Shoudong ^a,b   Sen, Ganes C ^a,b  

^a LERNER RESEARCH INSTITUTE   (United States)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS; ASPARTIC ACID; GEL ANALYSIS; PHOSPHORYLATION;

BIOCHEMICAL ENGINEERING; CELLS; ENZYMES; MUTAGENESIS;

AMINO ACIDS;

ALANINE; ASPARTIC ACID; MUTANT PROTEIN; PEPTIDES AND PROTEINS; PHOSPHOAMINO ACID ANTIBODY; PHOSPHORUS 32; PROTEIN ANTIBODY; PROTEIN KINASE R; PROTEIN PACT; SERINE; THREONINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; APOPTOSIS; ARTICLE; CELL SURVIVAL; CONTROLLED STUDY; ENZYME ACTIVATION; HUMAN; HUMAN CELL; IN VIVO STUDY; ISOTOPE LABELING; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; STRESS; WESTERN BLOTTING; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; APOPTOSIS; BINDING SITES; CELL LINE, TUMOR; EIF-2 KINASE; ENZYME ACTIVATION; GENE EXPRESSION REGULATION; HUMANS; MUTATION; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; RNA-BINDING PROTEINS; SERINE;

EID: 33845746006     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M607714200     Document Type: Article

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