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http://purl.uniprot.org/citations/29520027http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29520027http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29520027http://www.w3.org/2000/01/rdf-schema#comment"Lipopolysaccharide (LPS) of Gram-negative bacteria can elicit a strong immune response. Although extracellular LPS is sensed by TLR4 at the cell surface and triggers a transcriptional response, cytosolic LPS binds and activates non-canonical inflammasome caspases, resulting in pyroptotic cell death, as well as canonical NLRP3 inflammasome-dependent cytokine release. Contrary to the highly regulated multiprotein platform required for caspase-1 activation in the canonical inflammasomes, the non-canonical mouse caspase-11 and the orthologous human caspase-4 function simultaneously as innate sensors and effectors, and their regulation is unclear. Here we show that the oxidized phospholipid 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine (oxPAPC) inhibits the non-canonical inflammasome in macrophages, but not in dendritic cells. Aside from a TLR4 antagonistic role, oxPAPC binds directly to caspase-4 and caspase-11, competes with LPS binding, and consequently inhibits LPS-induced pyroptosis, IL-1β release and septic shock. Therefore, oxPAPC and its derivatives might provide a basis for therapies that target non-canonical inflammasomes during Gram-negative bacterial sepsis."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.org/dc/terms/identifier"doi:10.1038/s41467-018-03409-3"xsd:string
http://purl.uniprot.org/citations/29520027http://purl.org/dc/terms/identifier"doi:10.1038/s41467-018-03409-3"xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Monack D.M."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Monack D.M."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Dorfleutner A."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Dorfleutner A."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Stehlik C."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Stehlik C."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Gangopadhyay A."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Gangopadhyay A."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Ratsimandresy R.A."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Ratsimandresy R.A."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Morris E.P."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Morris E.P."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Chu L.H."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Chu L.H."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Indramohan M."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/author"Indramohan M."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/name"Nat. Commun."xsd:string
http://purl.uniprot.org/citations/29520027http://purl.uniprot.org/core/name"Nat. Commun."xsd:string