Receptor interacting protein is ubiquitinated by cellular inhibitor of apoptosis proteins (c-IAP1 and c-IAP2) in vitro

FEBS Letters

Volumn 566, Issue 1-3, 2004, Pages 151-156

  Park, Sun Mi ^a   Yoon, Jong Bok ^a   Lee, Tae H ^a  

^a Yonsei University   (South Korea)

Author keywords

DD, death domain; FADD, Fas associated death domain protein; JNK, c Jun N terminal kinase; RIP, receptor interacting protein; TNFR1, tumor necrosis factor receptor 1; TRADD, TNFR1 associated death domain; TRAF2, TNFR1 associated factor 2

Indexed keywords

CELLULAR INHIBITOR APOPTOSIS PROTEIN 1; CELLULAR INHIBITOR APOPTOSIS PROTEIN 2; PROTEASOME; PROTEIN; RECEPTOR INTERACTING PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; UNCLASSIFIED DRUG;

APOPTOSIS; ARTICLE; EMBRYO; HUMAN; HUMAN CELL; IN VITRO SELECTION; KIDNEY CELL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; STEADY STATE; UBIQUITINATION;

ANIMALS; APOPTOSIS; CELL LINE; GENE DELETION; HUMANS; IMMUNOBLOTTING; INHIBITOR OF APOPTOSIS PROTEINS; MICE; PROTEIN BIOSYNTHESIS; PROTEIN STRUCTURE, TERTIARY; PROTEINS; RECEPTOR-INTERACTING PROTEIN SERINE-THREONINE KINASES; RECEPTORS, TUMOR NECROSIS FACTOR; RECOMBINANT PROTEINS; TRANSFECTION; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES;

INTRACISTERNAL A-PARTICLES;

EID: 2442559290     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.04.021     Document Type: Article

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