Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis

Apoptosis

Volumn 6, Issue 5, 2001, Pages 319-330

  Bae, J ^a   Hsu, S Y ^a   Leo, C P ^a   Zell, K ^a   Hsueh, A J W ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Apoptosis; BAD; Bcl 2; Phosphorylation; Programmed cell death; Yeast two hybrid

Indexed keywords

PHOSPHOTRANSFERASE; PROTEIN BAD; PROTEIN BCL 2; PROTEIN BCL W; PROTEIN BCL X; PROTEIN BFL 1; PROTEIN BHRF 1; PROTEIN CED 9; PROTEIN MCL 1; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ANIMAL CELL; APOPTOSIS; ARTICLE; BINDING SITE; CHO CELL; CONTROLLED STUDY; ENZYME ACTIVATION; GENE SEQUENCE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; SEQUENCE HOMOLOGY;

14-3-3 PROTEINS; AMINO ACID SEQUENCE; ANIMALS; APOPTOSIS; BCL-ASSOCIATED DEATH PROTEIN; BINDING SITES; CARRIER PROTEINS; CHO CELLS; CONSERVED SEQUENCE; CRICETINAE; ESCHERICHIA COLI; EVOLUTION, MOLECULAR; HUMANS; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PROTO-ONCOGENE PROTEINS C-BCL-2; SEQUENCE HOMOLOGY, AMINO ACID; TRANSFECTION; TWO-HYBRID SYSTEM TECHNIQUES; TYROSINE 3-MONOOXYGENASE; YEASTS; ZEBRAFISH PROTEINS;

EID: 0034811108     PISSN: 13608185     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1011319901057     Document Type: Article

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