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http://purl.uniprot.org/citations/34990937http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34990937http://www.w3.org/2000/01/rdf-schema#comment"TANK-binding kinase 1 (TBK1) plays a pivotal role in antiviral innate immunity. TBK1 mediates the activation of interferon regulatory factor (IRF) 3, leading to the induction of type I IFNs (IFN-α/β) and of NF-κB signal transduction following viral infections. TBK1 must be tightly regulated to effectively control viral infections and maintain immune homeostasis. Here, we found that E3 ubiquitin ligase RNF19a mediated K48-linked ubiquitination and proteasomal degradation of TBK1. Specifically, the silence of RNF19a enhanced the production of type I interferons and suppressed RNA viral replication. Our results uncover that RNF19a acts as a negative mediator in the RIG-I signaling pathway to attenuate antiviral immune responses and suggest RNF19a as a potential therapy target in clinical infectious and inflammatory diseases."xsd:string
http://purl.uniprot.org/citations/34990937http://purl.org/dc/terms/identifier"doi:10.1016/j.molimm.2021.12.021"xsd:string
http://purl.uniprot.org/citations/34990937http://purl.uniprot.org/core/author"Huang L."xsd:string
http://purl.uniprot.org/citations/34990937http://purl.uniprot.org/core/author"Cao X."xsd:string
http://purl.uniprot.org/citations/34990937http://purl.uniprot.org/core/author"Yang Y."xsd:string
http://purl.uniprot.org/citations/34990937http://purl.uniprot.org/core/author"Yang A."xsd:string
http://purl.uniprot.org/citations/34990937http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/34990937http://purl.uniprot.org/core/name"Mol Immunol"xsd:string
http://purl.uniprot.org/citations/34990937http://purl.uniprot.org/core/pages"1-6"xsd:string
http://purl.uniprot.org/citations/34990937http://purl.uniprot.org/core/title"RNF19a inhibits antiviral immune response to RNA viruses through degradation of TBK1."xsd:string
http://purl.uniprot.org/citations/34990937http://purl.uniprot.org/core/volume"143"xsd:string
http://purl.uniprot.org/citations/34990937http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34990937
http://purl.uniprot.org/citations/34990937http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/34990937
http://purl.uniprot.org/uniprot/#_A1L361-mappedCitation-34990937http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34990937
http://purl.uniprot.org/uniprot/#_Q3THP3-mappedCitation-34990937http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34990937
http://purl.uniprot.org/uniprot/#_P50636-mappedCitation-34990937http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34990937
http://purl.uniprot.org/uniprot/#_Q3TM18-mappedCitation-34990937http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34990937
http://purl.uniprot.org/uniprot/#_Q9WUN2-mappedCitation-34990937http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34990937
http://purl.uniprot.org/uniprot/P50636http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34990937
http://purl.uniprot.org/uniprot/Q3TM18http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34990937
http://purl.uniprot.org/uniprot/A1L361http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34990937
http://purl.uniprot.org/uniprot/Q9WUN2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34990937
http://purl.uniprot.org/uniprot/Q3THP3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34990937