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http://purl.uniprot.org/citations/7538907http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7538907http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7538907http://www.w3.org/2000/01/rdf-schema#comment"Using the cytoplasmic domain of Fas in the yeast two-hybrid system, we have identified a novel interacting protein, FADD, which binds Fas and Fas-FD5, a mutant of Fas possessing enhanced killing activity, but not the functionally inactive mutants Fas-LPR and Fas-FD8. FADD contains a death domain homologous to the death domains of Fas and TNFR-1. A point mutation in FADD, analogous to the lpr mutation of Fas, abolishes its ability to bind Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in MCF7 and BJAB cells induces apoptosis, which, like Fas-induced apoptosis, is blocked by CrmA, a specific inhibitor of the interleukin-1 beta-converting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas."xsd:string
http://purl.uniprot.org/citations/7538907http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(95)90071-3"xsd:string
http://purl.uniprot.org/citations/7538907http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(95)90071-3"xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/author"O'Rourke K."xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/author"O'Rourke K."xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/author"Dixit V.M."xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/author"Dixit V.M."xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/author"Tewari M."xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/author"Tewari M."xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/author"Chinnaiyan A.M."xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/author"Chinnaiyan A.M."xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/pages"505-512"xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/pages"505-512"xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/title"FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis."xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/title"FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis."xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/volume"81"xsd:string
http://purl.uniprot.org/citations/7538907http://purl.uniprot.org/core/volume"81"xsd:string
http://purl.uniprot.org/citations/7538907http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7538907
http://purl.uniprot.org/citations/7538907http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7538907