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http://purl.uniprot.org/citations/19521662http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19521662http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19521662http://www.w3.org/2000/01/rdf-schema#comment"Toll-like receptors (TLRs) act as sensors of microbial components and elicit innate immune responses. All TLR signaling pathways activate the nuclear factor-kappaB (NF-kappaB), which controls the expression of inflammatory cytokine genes. Transforming growth factor-beta-activated kinase 1 (TAK1) is a serine/threonine protein kinase that is critically involved in the activation of NF-kappaB by tumor necrosis factor (TNFalpha), interleukin-1beta (IL-1beta) and TLR ligands. In this study, we identified a novel protein, WD40 domain repeat protein 34 (WDR34) as a TAK1-interacting protein in yeast two-hybrid screens. WDR34 interacted with TAK1, TAK1-binding protein 2 (TAB2), TAK1-binding protein 3 (TAB3) and tumor necrosis factor receptor-associated factor 6 (TRAF6) in overexpression and under physiological conditions. Overexpression of WDR34 inhibited IL-1beta-, polyI:C- and lipopolysaccharide (LPS)-induced but not TNFalpha-induced NF-kappaB activation, whereas knockdown of WDR34 by a RNA-interference construct potentiated NF-kappaB activation by these ligands. Our findings suggest that WDR34 is a TAK1-associated inhibitor of the IL-1R/TLR3/TLR4-induced NF-kappaB activation pathway."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.org/dc/terms/identifier"doi:10.1007/s00018-009-0059-6"xsd:string
http://purl.uniprot.org/citations/19521662http://purl.org/dc/terms/identifier"doi:10.1007/s00018-009-0059-6"xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/author"Gao D."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/author"Gao D."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/author"Li B."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/author"Li B."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/author"Yang Y."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/author"Yang Y."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/author"Wang R."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/author"Wang R."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/author"Zhai Z."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/author"Zhai Z."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/author"Chen D.Y."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/author"Chen D.Y."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/name"Cell. Mol. Life Sci."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/name"Cell. Mol. Life Sci."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/pages"2573-2584"xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/pages"2573-2584"xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/title"WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-induced NF-kappaB activation pathway."xsd:string
http://purl.uniprot.org/citations/19521662http://purl.uniprot.org/core/title"WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-induced NF-kappaB activation pathway."xsd:string