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http://purl.uniprot.org/citations/16177806http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16177806http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16177806http://www.w3.org/2000/01/rdf-schema#comment"Antiviral immunity against a pathogen is mounted upon recognition by the host of virally associated structures. One of these viral 'signatures', double-stranded (ds) RNA, is a replication product of most viruses within infected cells and is sensed by Toll-like receptor 3 (TLR3) and the recently identified cytosolic RNA helicases RIG-I (retinoic acid inducible gene I, also known as Ddx58) and Mda5 (melanoma differentiation-associated gene 5, also known as Ifih1 or Helicard). Both helicases detect dsRNA, and through their protein-interacting CARD domains, relay an undefined signal resulting in the activation of the transcription factors interferon regulatory factor 3 (IRF3) and NF-kappaB. Here we describe Cardif, a new CARD-containing adaptor protein that interacts with RIG-I and recruits IKKalpha, IKKbeta and IKKvarepsilon kinases by means of its C-terminal region, leading to the activation of NF-kappaB and IRF3. Overexpression of Cardif results in interferon-beta and NF-kappaB promoter activation, and knockdown of Cardif by short interfering RNA inhibits RIG-I-dependent antiviral responses. Cardif is targeted and inactivated by NS3-4A, a serine protease from hepatitis C virus known to block interferon-beta production. Cardif thus functions as an adaptor, linking the cytoplasmic dsRNA receptor RIG-I to the initiation of antiviral programmes."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.org/dc/terms/identifier"doi:10.1038/nature04193"xsd:string
http://purl.uniprot.org/citations/16177806http://purl.org/dc/terms/identifier"doi:10.1038/nature04193"xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Bartenschlager R."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Bartenschlager R."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Curran J."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Curran J."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Hofmann K."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Hofmann K."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Tschopp J."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Tschopp J."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Binder M."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Binder M."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Moradpour D."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Moradpour D."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Meylan E."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/author"Meylan E."xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/pages"1167-1172"xsd:string
http://purl.uniprot.org/citations/16177806http://purl.uniprot.org/core/pages"1167-1172"xsd:string