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http://purl.uniprot.org/citations/10364242http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10364242http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10364242http://www.w3.org/2000/01/rdf-schema#comment"Molecules that regulate NF-kappaB activation play critical roles in apoptosis and inflammation. We describe the cloning of the cellular homolog of the equine herpesvirus-2 protein E10 and show that both proteins regulate apoptosis and NF-kappaB activation. These proteins were found to contain N-terminal caspase-recruitment domains (CARDs) and novel C-terminal domains (CTDs) and were therefore named CLAPs (CARD-like apoptotic proteins). The cellular and viral CLAPs induce apoptosis downstream of caspase-8 by activating the Apaf-1-caspase-9 pathway and activate NF-kappaB by acting upstream of the NF-kappaB-inducing kinase, NIK, and the IkB kinase, IKKalpha. Deletion of either the CARD or the CTD domain inhibits both activities. The CARD domain was found to be important for homo- and heterodimerization of CLAPs. Substitution of the CARD domain with an inducible FKBP12 oligomerization domain produced a molecule that can induce NF-kappaB activation, suggesting that the CARD domain functions as an oligomerization domain, whereas the CTD domain functions as the effector domain in the NF-kappaB activation pathway. Expression of the CARD domain of human CLAP abrogates tumor necrosis factor-alpha-induced NF-kappaB activation, suggesting that cellular CLAP plays an essential role in this pathway of NF-kappaB activation."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.25.17946"xsd:string
http://purl.uniprot.org/citations/10364242http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.25.17946"xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Tsichlis P.N."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Tsichlis P.N."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Alnemri E.S."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Alnemri E.S."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Poyet J.-L."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Poyet J.-L."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Lin J.-H."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Lin J.-H."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Fernandes-Alnemri T."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Fernandes-Alnemri T."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Ahmad M."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Ahmad M."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Srinivasula S.M."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/author"Srinivasula S.M."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/pages"17946-17954"xsd:string
http://purl.uniprot.org/citations/10364242http://purl.uniprot.org/core/pages"17946-17954"xsd:string