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http://purl.uniprot.org/citations/29844315http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29844315http://www.w3.org/2000/01/rdf-schema#comment"Endoplasmic reticulum (ER) stress contributes to the development and progression of many chronic inflammatory diseases, including type 2 diabetes, obesity, atherosclerosis, neurodegenerative diseases, and cancer. ER stress has been reported to induce inflammasome activation and release of mature IL-1β, which contributes to many inflammatory diseases. The molecular mechanisms that activate the inflammasome during ER stress are still poorly understood. Here we report that the kinase receptor-interacting protein 1 (RIP1) plays an important role in ER stress-induced activation of inflammasome. Inhibition of RIP1 kinase activity by Necrostatin-1 or siRNA-mediated RIP1 knockdown significantly reduced ER stress-induced caspase-1 cleavage and IL-1β secretion in both bone marrow-derived macrophages (BMDMs) and J774A.1 macrophages. We speculate that the mitochondria fission factor dynamin-related protein 1 (DRP1) and reactive oxygen species (ROS) might function as the effectors downstream of RIP1 to mediate inflammasome activation. Our study reveals a critical role for RIP1 in regulating ER stress-induced inflammation responses, and proposes RIP1 as a potential pharmaceutical target to treat diseases resulting from unresolved ER stress-related inflammation."xsd:string
http://purl.uniprot.org/citations/29844315http://purl.org/dc/terms/identifier"doi:10.1038/s41419-018-0694-7"xsd:string
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/author"Gao Y."xsd:string
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/author"Lin H."xsd:string
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/author"Sun Q."xsd:string
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/author"Tao L."xsd:string
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/author"Wang J."xsd:string
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/author"Zhang J."xsd:string
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/author"Xu X."xsd:string
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/author"Wen J."xsd:string
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/author"Weng D."xsd:string
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/name"Cell Death Dis"xsd:string
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/pages"641"xsd:string
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/title"The kinase receptor-interacting protein 1 is required for inflammasome activation induced by endoplasmic reticulum stress."xsd:string
http://purl.uniprot.org/citations/29844315http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/29844315http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/29844315
http://purl.uniprot.org/citations/29844315http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/29844315
http://purl.uniprot.org/uniprot/#_Q13546-mappedCitation-29844315http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/29844315
http://purl.uniprot.org/uniprot/#_Q60855-mappedCitation-29844315http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/29844315
http://purl.uniprot.org/uniprot/Q13546http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/29844315
http://purl.uniprot.org/uniprot/Q60855http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/29844315