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http://purl.uniprot.org/citations/10187771http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10187771http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10187771http://www.w3.org/2000/01/rdf-schema#comment"We have previously reported on the death effector domain containing E8 gene product from equine herpesvirus-2, designated FLICE inhibitory protein (v-FLIP), and on its cellular homologue, c-FLIP, which inhibit the activation of caspase-8 by death receptors. Here we report on the structure and function of the E10 gene product of equine herpesvirus-2, designated v-CARMEN, and on its cellular homologue, c-CARMEN, which contain a caspase-recruiting domain (CARD) motif. c-CARMEN is highly homologous to the viral protein in its N-terminal CARD motif but differs in its C-terminal extension. v-CARMEN and c-CARMEN interact directly in a CARD-dependent manner yet reveal different binding specificities toward members of the tumor necrosis factor receptor-associated factor (TRAF) family. v-CARMEN binds to TRAF6 and weakly to TRAF3 and, upon overexpression, potently induces the c-Jun N-terminal kinase (JNK), p38, and nuclear factor (NF)-kappaB transcriptional pathways. c-CARMEN or truncated versions thereof do not appear to induce JNK and NF-kappaB activation by themselves, nor do they affect the JNK and NF-kappaB activating potential of v-CARMEN. Thus, in contrast to the cellular homologue, v-CARMEN may have additional properties in its unique C terminus that allow for an autonomous activator effect on NF-kappaB and JNK. Through activation of NF-kappaB, v-CARMEN may regulate the expression of the cellular and viral genes important for viral replication."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.15.9962"xsd:string
http://purl.uniprot.org/citations/10187771http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.15.9962"xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Rubio V."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Rubio V."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Schneider P."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Schneider P."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Hofmann K."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Hofmann K."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Mattmann C."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Mattmann C."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Thome M."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Thome M."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Tschopp J."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Tschopp J."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Martinon F."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Martinon F."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Steiner V."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/author"Steiner V."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10187771http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string