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http://purl.uniprot.org/citations/21642987http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21642987http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21642987http://www.w3.org/2000/01/rdf-schema#comment"Antiviral innate immunity relies on the recognition of microbial structures. One such structure is viral RNA that carries a triphosphate group on its 5' terminus (PPP-RNA). By an affinity proteomics approach with PPP-RNA as the 'bait', we found that the antiviral protein IFIT1 (interferon-induced protein with tetratricopeptide repeats 1) mediated binding of a larger protein complex containing other IFIT family members. IFIT1 bound PPP-RNA with nanomolar affinity and required the arginine at position 187 in a highly charged carboxy-terminal groove of the protein. In the absence of IFIT1, the growth and pathogenicity of viruses containing PPP-RNA was much greater. In contrast, IFIT proteins were dispensable for the clearance of pathogens that did not generate PPP-RNA. On the basis of this specificity and the great abundance of IFIT proteins after infection, we propose that the IFIT complex antagonizes viruses by sequestering specific viral nucleic acids."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.org/dc/terms/identifier"doi:10.1038/ni.2048"xsd:string
http://purl.uniprot.org/citations/21642987http://purl.org/dc/terms/identifier"doi:10.1038/ni.2048"xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Bennett K.L."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Bennett K.L."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Buerckstuemmer T."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Buerckstuemmer T."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Burkard T.R."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Burkard T.R."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Colinge J."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Colinge J."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Mueller M."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Mueller M."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Superti-Furga G."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Superti-Furga G."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Ruelicke T."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Ruelicke T."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Krieger S."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Krieger S."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Weber F."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Weber F."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Pichlmair A."xsd:string
http://purl.uniprot.org/citations/21642987http://purl.uniprot.org/core/author"Pichlmair A."xsd:string