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http://purl.uniprot.org/citations/35941131http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35941131http://www.w3.org/2000/01/rdf-schema#comment"Deubiquitinating enzymes (DUBs) regulate numerous cellular functions by removing ubiquitin modifications. We examined the effects of 88 human DUBs on linear ubiquitin chain assembly complex (LUBAC)-induced NF-κB activation, and identified OTUD1 as a potent suppressor. OTUD1 regulates the canonical NF-κB pathway by hydrolyzing K63-linked ubiquitin chains from NF-κB signaling factors, including LUBAC. OTUD1 negatively regulates the canonical NF-κB activation, apoptosis, and necroptosis, whereas OTUD1 upregulates the interferon (IFN) antiviral pathway. Mass spectrometric analysis showed that OTUD1 binds KEAP1, and the N-terminal intrinsically disordered region of OTUD1, which contains an ETGE motif, is indispensable for the KEAP1-binding. Indeed, OTUD1 is involved in the KEAP1-mediated antioxidant response and reactive oxygen species (ROS)-induced cell death, oxeiptosis. In Otud1-/--mice, inflammation, oxidative damage, and cell death were enhanced in inflammatory bowel disease, acute hepatitis, and sepsis models. Thus, OTUD1 is a crucial regulator for the inflammatory, innate immune, and oxidative stress responses and ROS-associated cell death pathways."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.org/dc/terms/identifier"doi:10.1038/s41419-022-05145-5"xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/author"Shimizu K."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/author"Takahashi H."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/author"Tokunaga F."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/author"Sawasaki T."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/author"Kosako H."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/author"Gi M."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/author"Tsuruta D."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/author"Oikawa D."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/author"Shiota M."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/author"Hosomi S."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/author"Wanibuchi H."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/author"Komakura K."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/name"Cell Death Dis"xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/pages"694"xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/title"OTUD1 deubiquitinase regulates NF-kappaB- and KEAP1-mediated inflammatory responses and reactive oxygen species-associated cell death pathways."xsd:string
http://purl.uniprot.org/citations/35941131http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/35941131http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/35941131
http://purl.uniprot.org/citations/35941131http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/35941131
http://purl.uniprot.org/uniprot/#_Q15628-mappedCitation-35941131http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35941131
http://purl.uniprot.org/uniprot/#_P21580-mappedCitation-35941131http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35941131
http://purl.uniprot.org/uniprot/#_P0CG47-mappedCitation-35941131http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35941131