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http://purl.uniprot.org/citations/15001576http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15001576http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15001576http://www.w3.org/2000/01/rdf-schema#comment"The tumor necrosis factor receptor-associated factor (TRAF) protein family members are critically involved in activation of NF-kappaB, JNK, and p38 activation triggered by tumor necrosis factor (TNF) receptor family members and toll/interleukin-1 receptor (TIR)-containing receptors. TRAF proteins (except for TRAF1) contain an N-terminal RING finger domain that is essential for their functions. In this report, we identified a protein designated as TRAF7, which contains a RING finger domain and a zinc finger domain that are mostly conserved with those of TRAFs. TRAF7 also contains seven WD40 repeats at its C terminus. TRAF7 specifically interacted with MEKK3 and potentiated MEKK3-mediated AP1 and CHOP activation. Depletion of TRAF7 by antisense RNA inhibited MEKK3-mediated AP1 and CHOP activation. Moreover, overexpression of TRAF7 induced caspase-dependent apoptosis. Domain mapping experiments indicated that TRAF7 potentiated MEKK3-mediated AP1 and CHOP activation and induced apoptosis through distinct domains. Our studies identified a novel TRAF family member that is involved in MEKK3 signaling and apoptosis."xsd:string
http://purl.uniprot.org/citations/15001576http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c400063200"xsd:string
http://purl.uniprot.org/citations/15001576http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c400063200"xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/author"Xu L.-G."xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/author"Xu L.-G."xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/author"Shu H.-B."xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/author"Shu H.-B."xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/author"Li L.-Y."xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/author"Li L.-Y."xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/pages"17278-17282"xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/pages"17278-17282"xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/title"TRAF7 potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis."xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/title"TRAF7 potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis."xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15001576http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15001576http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15001576
http://purl.uniprot.org/citations/15001576http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15001576
http://purl.uniprot.org/citations/15001576http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15001576
http://purl.uniprot.org/citations/15001576http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15001576