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http://purl.uniprot.org/citations/19667203http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19667203http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19667203http://www.w3.org/2000/01/rdf-schema#comment"NOD1 and NOD2 are members of the NOD-like receptor (NLR) protein family that are involved in sensing the presence of pathogens and are a component of the innate immune system. Upon activation by specific bacterial peptides derived from peptidoglycans, NODs interact via a CARD-CARD interaction with the receptor-interacting protein kinase RIP2, an inducer of NF-kappaB activation. In this report, we show that NOD signaling is dependent on XIAP, a member of the inhibitor of apoptosis protein (IAP) family. Cells deficient in XIAP exhibit a marked reduction in NF-kappaB activation induced by microbial NOD ligands and by over-expression of NOD1 or NOD2. Moreover, we show that XIAP interacts with RIP2 via its BIR2 domain, which could be disrupted by XIAP antagonists SMAC and SMAC-mimicking compounds. Both NOD1 and NOD2 associated with XIAP in a RIP2-dependent manner, providing evidence that XIAP associates with the NOD signalosome. Taken together, our data suggest a role for XIAP in regulating innate immune responses by interacting with NOD1 and NOD2 through interaction with RIP2."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0907131106"xsd:string
http://purl.uniprot.org/citations/19667203http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0907131106"xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Huang Z."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Huang Z."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Krieg A."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Krieg A."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Le Negrate G."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Le Negrate G."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Reed J.C."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Reed J.C."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Welsh K."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Welsh K."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Correa R.G."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Correa R.G."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Knoefel W.T."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Knoefel W.T."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Garrison J.B."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/author"Garrison J.B."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/19667203http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string