http://purl.uniprot.org/citations/22301134 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/22301134 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/22301134 | http://www.w3.org/2000/01/rdf-schema#comment | "RIG-I and mda-5 are activated by viral RNA and stimulate type I interferon production. Laboratory of genetics and physiology 2 (LGP2) shares homology with RIG-I and mda-5 but lacks the CARD domains required for signaling. The V proteins of paramyxoviruses limit interferon induction by binding mda-5 and preventing its activation; however, they do not bind RIG-I and have not been considered inhibitors of RIG-I signaling. Here we uncover a novel mechanism of RIG-I inhibition in which the V protein of parainfluenzavirus type 5 (PIV5; formerly known as simian virus type 5 [SV5]) interacts with LGP2 and cooperatively inhibits induction by RIG-I ligands. A complex between RIG-I and LGP2 is observed in the presence of PIV5-V, and we propose that this complex is refractory to activation by RIG-I ligands. The V proteins from other paramyxoviruses also bind LGP2 and demonstrate LGP2-dependent inhibition of RIG-I signaling. This is significant, because it demonstrates a general mechanism for the targeting of the RIG-I pathway by paramyxoviruses."xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.org/dc/terms/identifier | "doi:10.1128/jvi.06405-11"xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.org/dc/terms/identifier | "doi:10.1128/jvi.06405-11"xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/author | "Childs K."xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/author | "Childs K."xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/author | "Goodbourn S."xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/author | "Goodbourn S."xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/author | "Randall R."xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/author | "Randall R."xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/name | "J. Virol."xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/name | "J. Virol."xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/pages | "3411-3421"xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/pages | "3411-3421"xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/title | "Paramyxovirus V proteins interact with the RNA Helicase LGP2 to inhibit RIG-I-dependent interferon induction."xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/title | "Paramyxovirus V proteins interact with the RNA Helicase LGP2 to inhibit RIG-I-dependent interferon induction."xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/volume | "86"xsd:string |
http://purl.uniprot.org/citations/22301134 | http://purl.uniprot.org/core/volume | "86"xsd:string |
http://purl.uniprot.org/citations/22301134 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22301134 |
http://purl.uniprot.org/citations/22301134 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22301134 |
http://purl.uniprot.org/citations/22301134 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22301134 |
http://purl.uniprot.org/citations/22301134 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22301134 |