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http://purl.uniprot.org/citations/11432859http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11432859http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11432859http://www.w3.org/2000/01/rdf-schema#comment"The production of bio-active interleukin-1beta (IL-1beta), a pro-inflammatory cytokine, is mediated by activated caspase-1. One of the known molecular mechanisms underlying pro-caspase-1 processing and activation involves binding of the caspase-1 prodomain to a caspase recruitment domain (CARD)-containing serine/threonine kinase known as RIP2/CARDIAK/RICK. We have identified a novel protein, COP (CARD only protein), which has a high degree of sequence identity to the caspase-1 prodomain. COP binds to both RIP2 and the caspase-1 prodomain and inhibits RIP2-induced caspase-1 oligomerization. COP inhibits caspase-1-induced IL-1beta secretion as well as lipopolysaccharide-induced IL-1beta secretion in transfected cells. Our data indicate that COP can regulate IL-1beta secretion, implying that COP may play a role in down-regulating inflammatory responses analogous to the CARD protein ICEBERG."xsd:string
http://purl.uniprot.org/citations/11432859http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m101415200"xsd:string
http://purl.uniprot.org/citations/11432859http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m101415200"xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/author"Lee S.H."xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/author"Lee S.H."xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/author"Reed J.C."xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/author"Reed J.C."xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/author"Stehlik C."xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/author"Stehlik C."xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/pages"34495-34500"xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/pages"34495-34500"xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/title"Cop, a caspase recruitment domain-containing protein and inhibitor of caspase-1 activation processing."xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/title"Cop, a caspase recruitment domain-containing protein and inhibitor of caspase-1 activation processing."xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11432859http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11432859http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11432859
http://purl.uniprot.org/citations/11432859http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11432859
http://purl.uniprot.org/citations/11432859http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11432859
http://purl.uniprot.org/citations/11432859http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11432859