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http://purl.uniprot.org/citations/9215629http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9215629http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9215629http://www.w3.org/2000/01/rdf-schema#comment"The Fas cell surface receptor induces apoptosis upon receptor oligomerization. We have identified a novel signaling protein, termed Daxx, that binds specifically to the Fas death domain. Overexpression of Daxx enhances Fas-mediated apoptosis and activates the Jun N-terminal kinase (JNK) pathway. A C-terminal portion of Daxx interacts with the Fas death domain, while a different region activates both JNK and apoptosis. The Fas-binding domain of Daxx is a dominant-negative inhibitor of both Fas-induced apoptosis and JNK activation, while the FADD death domain partially inhibits death but not JNK activation. The Daxx apoptotic pathway is sensitive to both Bcl-2 and dominant-negative JNK pathway components and acts cooperatively with the FADD pathway. Thus, Daxx and FADD define two distinct apoptotic pathways downstream of Fas."xsd:string
http://purl.uniprot.org/citations/9215629http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(00)80294-9"xsd:string
http://purl.uniprot.org/citations/9215629http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(00)80294-9"xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/author"Baltimore D."xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/author"Baltimore D."xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/author"Yang X."xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/author"Yang X."xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/author"Chang H.Y."xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/author"Chang H.Y."xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/author"Khosravi-Far R."xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/author"Khosravi-Far R."xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/pages"1067-1076"xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/pages"1067-1076"xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/title"Daxx, a novel Fas-binding protein that activates JNK and apoptosis."xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/title"Daxx, a novel Fas-binding protein that activates JNK and apoptosis."xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/volume"89"xsd:string
http://purl.uniprot.org/citations/9215629http://purl.uniprot.org/core/volume"89"xsd:string
http://purl.uniprot.org/citations/9215629http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9215629
http://purl.uniprot.org/citations/9215629http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9215629