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http://purl.uniprot.org/citations/21910972http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21910972http://www.w3.org/2000/01/rdf-schema#comment"The cellular RIG-I-like receptor (RLR) senses pathogenic RNA molecular patterns and transmits signals for type I interferon (IFN) production. It acts as a center for antiviral responses, and large numbers of RIG-I (retinoic acid inducible gene-I) interacting proteins are identified as signaling regulators. In the present study, we report PRKRIR, a negative regulator of PKR inhibitor, as a novel RIG-I interacting protein. In HEK293FT cells, PRKRIR synergistically enhances type I IFN production mediated by a signal activated- or constitutively active form of RIG-I. The C-terminal domain of the PRKRIR was required for physical interaction and the signal augmentation. The PRKRIR blocks poly-ubiquitination and protein degradation of RIG-I, thereby increasing cellular levels of RIG-I proteins. Furthermore, overexpression of PRKRIR, along with a signal activated- or constitutively active form of RIG-I, efficiently inhibits virus replication in the infected host. In conclusion, PRKRIR provides a novel positive regulator controlling the RIG-I-IFN production system through protein stability control."xsd:string
http://purl.uniprot.org/citations/21910972http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2011.08.127"xsd:string
http://purl.uniprot.org/citations/21910972http://purl.uniprot.org/core/author"Yoo J.Y."xsd:string
http://purl.uniprot.org/citations/21910972http://purl.uniprot.org/core/author"Now H."xsd:string
http://purl.uniprot.org/citations/21910972http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21910972http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/21910972http://purl.uniprot.org/core/pages"487-493"xsd:string
http://purl.uniprot.org/citations/21910972http://purl.uniprot.org/core/title"A protein-kinase, IFN-inducible double-stranded RNA dependent inhibitor and repressor of p58 (PRKRIR) enhances type I IFN-mediated antiviral response through the stability control of RIG-I protein."xsd:string
http://purl.uniprot.org/citations/21910972http://purl.uniprot.org/core/volume"413"xsd:string
http://purl.uniprot.org/citations/21910972http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21910972
http://purl.uniprot.org/citations/21910972http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21910972
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http://purl.uniprot.org/uniprot/#_B4DWT9-mappedCitation-21910972http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21910972
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http://purl.uniprot.org/uniprot/#_Q3B797-mappedCitation-21910972http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21910972
http://purl.uniprot.org/uniprot/#_Q2YDB3-mappedCitation-21910972http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21910972
http://purl.uniprot.org/uniprot/#_O43422-mappedCitation-21910972http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21910972
http://purl.uniprot.org/uniprot/#_L8E813-mappedCitation-21910972http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21910972
http://purl.uniprot.org/uniprot/#_O95786-mappedCitation-21910972http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21910972
http://purl.uniprot.org/uniprot/B4DWT9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21910972
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http://purl.uniprot.org/uniprot/O95786http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21910972