Direct binding of Fas-associated death domain (FADD) to the tumor necrosis factor-related apoptosis-inducing ligand receptor DR5 is regulated by the death effector domain of FADD

Journal of Biological Chemistry

Volumn 279, Issue 31, 2004, Pages 32780-32785

  Thomas, Lance R ^a   Henson, Adrianna ^a   Reed, John C ^b   Salsbury, Freddie R ^c   Thorburn, Andrew ^a  

^a WAKE FOREST SCHOOL OF MEDICINE   (United States)

^b BURNHAM INSTITUTE   (United States)

^c WAKE FOREST UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATOMS; GENETIC ENGINEERING; MOLECULAR DYNAMICS; TUMORS;

APOPTOSIS; DEATH DOMAIN INTERACTIONS; FAS-ASSOCIATED DEATH DOMAINS (FADD); TUMOR NECROSIS;

BIOCHEMISTRY;

APOPTOSIS INDUCING LIGAND RECEPTOR DR5; CASPASE; FAS ANTIGEN; FAS ASSOCIATED DEATH DOMAIN; RECEPTOR; TUMOR NECROSIS FACTOR RECEPTOR; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UNCLASSIFIED DRUG;

APOPTOSIS; ARTICLE; CONTROLLED STUDY; GENE MUTATION; HUMAN; HUMAN CELL; LEUKEMIA CELL LINE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; TWO HYBRID SYSTEM;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ANIMALS; ANTIGENS, CD95; APOPTOSIS; CARRIER PROTEINS; CASPASES; CELL LINE; CLONING, MOLECULAR; ENZYME ACTIVATION; GREEN FLUORESCENT PROTEINS; HELA CELLS; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; JURKAT CELLS; LIGANDS; LUMINESCENT PROTEINS; MICE; MODELS, MOLECULAR; MUTATION; NUCLEAR PROTEINS; PLASMIDS; PRECIPITIN TESTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, TNF-RELATED APOPTOSIS-INDUCING LIGAND; RECEPTORS, TUMOR NECROSIS FACTOR; SIGNAL TRANSDUCTION; THERMODYNAMICS; TWO-HYBRID SYSTEM TECHNIQUES; VALINE;

EID: 3543032779     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M401680200     Document Type: Article

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