An apoptosis signalling pathway induced by the death domain of FADD selectively kills normal but not cancerous prostate epithelial cells

Cell Death and Differentiation

Volumn 8, Issue 7, 2001, Pages 696-705

  Morgan, M J ^a   Thorburn, J ^b   Thomas, L ^b   Maxwell, T ^c   Brothman, A R ^c   Thorburn, A ^b  

^a UNIVERSITY OF UTAH   (United States)

^b WAKE FOREST SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

Author keywords

Epithelia; FADD; FRET; Prostate cancer

Indexed keywords

ADAPTOR PROTEIN; CASPASE; CASPASE INHIBITOR; FAS ASSOCIATED DEATH DOMAIN PROTEIN; FAS LIGAND; UNCLASSIFIED DRUG; ANTIOXIDANT; BCL2L1 PROTEIN, HUMAN; CARRIER PROTEIN; FADD PROTEIN, HUMAN; FAS ANTIGEN; PROTEIN; PROTEIN BCL 2; PROTEIN BCL X; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; RIPK1 PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 1;

APOPTOSIS; ARTICLE; CANCER CELL; CARCINOGENESIS; CELL DEATH; CELL KILLING; CELL SPECIFICITY; CELL SURVIVAL; CONTROLLED STUDY; ENERGY TRANSFER; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ASSAY; FLUORESCENCE; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROSTATE CANCER; PROSTATE EPITHELIUM; PROTEIN BINDING; PROTEIN DOMAIN; SIGNAL TRANSDUCTION; STROMA CELL; CELL CULTURE; CHEMISTRY; CYTOLOGY; DRUG ANTAGONISM; EPITHELIUM CELL; GENETICS; MALE; METABOLISM; PATHOLOGY; PROSTATE; PROSTATE TUMOR; PROTEIN TERTIARY STRUCTURE; TWO HYBRID SYSTEM;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ANTIGENS, CD95; ANTIOXIDANTS; APOPTOSIS; BCL-X PROTEIN; CARRIER PROTEINS; CASPASES; CELLS, CULTURED; ENZYME ACTIVATION; EPITHELIAL CELLS; FAS-ASSOCIATED DEATH DOMAIN PROTEIN; FLUORESCENCE; HUMANS; MALE; PROSTATE; PROSTATIC NEOPLASMS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEINS; PROTO-ONCOGENE PROTEINS C-BCL-2; RECEPTOR-INTERACTING PROTEIN SERINE-THREONINE KINASES; SIGNAL TRANSDUCTION; TNF RECEPTOR-ASSOCIATED FACTOR 1; TUMOR CELLS, CULTURED; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 0034743157     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4400866     Document Type: Article

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