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http://purl.uniprot.org/citations/9642260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9642260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9642260http://www.w3.org/2000/01/rdf-schema#comment"Through specific interactions with members of the tumor necrosis receptor (TNFR) family, adapter molecules such as the serine/threonine (Ser/Thr) kinase RIP mediate divergent signaling pathways including NF-kappaB activation and cell death. In this study, we have identified and characterized a novel 61-kDa protein kinase related to RIP that is a component of both the TNFR-1 and the CD40 signaling complexes. Receptor interacting protein-2 (RIP2) contains an N-terminal domain with homology to Ser/Thr kinases and a C-terminal caspase activation and recruitment domain (CARD), a homophilic interaction motif that mediates the recruitment of caspase death proteases. Overexpression of RIP2 signaled both NF-kappaB activation and cell death. Mutational analysis revealed the pro-apoptotic function of RIP2 to be restricted to its C-terminal CARD domain, whereas the intact molecule was necessary for NF-kappaB activation. RIP2 interacted with other members of the TNFR-1 signaling complex, including inhibitor of apoptosis protein cIAP1 and with members of the TNFR-associated factor (TRAF) family, specifically TRAF1, TRAF5, and TRAF6, but not with TRAF2, TRAF3, or TRAF4. These TRAF interactions mediate the recruitment of RIP2 to receptor signaling complexes."xsd:string
http://purl.uniprot.org/citations/9642260http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.27.16968"xsd:string
http://purl.uniprot.org/citations/9642260http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.27.16968"xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/author"Ni J."xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/author"Ni J."xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/author"Dixit V.M."xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/author"Dixit V.M."xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/author"McCarthy J.V."xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/author"McCarthy J.V."xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/pages"16968-16975"xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/pages"16968-16975"xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/title"RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase."xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/title"RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase."xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/volume"273"xsd:string
http://purl.uniprot.org/citations/9642260http://purl.uniprot.org/core/volume"273"xsd:string
http://purl.uniprot.org/citations/9642260http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9642260
http://purl.uniprot.org/citations/9642260http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9642260
http://purl.uniprot.org/citations/9642260http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9642260
http://purl.uniprot.org/citations/9642260http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9642260