RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/17479112http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17479112http://www.w3.org/2000/01/rdf-schema#comment"Apoptosis is a highly controlled process, whose triggering is associated with the activation of caspases. Apoptosis can be induced via a subgroup of the tumor necrosis factor (TNF) receptor superfamily, which recruit and activate pro-caspase-8 and -10. Regulation of apoptosis is achieved by several inhibitors, including c-FLICE-inhibitory protein, which prevents apoptosis by inhibiting the pro-apoptotic activation of upstream caspases. Here we show that the human intracellular serine protease inhibitor (serpin), protease inhibitor 9 (PI9), inhibits TNF-, TNF-related apoptosis-inducing ligand- and Fas ligand-mediated apoptosis in certain TNF-sensitive cell lines. The reactive center P1 residue of PI9 was required for this inhibition since PI9 harboring a Glu --> Ala mutation in its reactive center failed to impair death receptor-induced cell death. This suggests a classical serpin-protease interaction. Indeed, PI9 inhibited apoptotic death by directly interacting with the intermediate active forms of caspase-8 and -10. This indicates that PI9 can regulate pro-apoptotic apical caspases."xsd:string
http://purl.uniprot.org/citations/17479112http://purl.org/dc/terms/identifier"doi:10.1038/sj.cdd.4402152"xsd:string
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/author"Schneider P."xsd:string
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/author"Tschopp J."xsd:string
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/author"Micheau O."xsd:string
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/author"Bovenschen N."xsd:string
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/author"Broekhuizen R."xsd:string
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/author"Kummer J.A."xsd:string
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/author"Quadir R."xsd:string
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/author"Hack C.E."xsd:string
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/author"Strik M.C."xsd:string
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/name"Cell Death Differ"xsd:string
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/pages"1486-1496"xsd:string
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/title"Ectopic expression of the serine protease inhibitor PI9 modulates death receptor-mediated apoptosis."xsd:string
http://purl.uniprot.org/citations/17479112http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/17479112http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17479112
http://purl.uniprot.org/citations/17479112http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17479112
http://purl.uniprot.org/uniprot/P50453#attribution-FE07C3EA807AD08F50803277DF877CA9http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/17479112
http://purl.uniprot.org/uniprot/#_A0A024QZT4-mappedCitation-17479112http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17479112
http://purl.uniprot.org/uniprot/#_P50453-mappedCitation-17479112http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17479112
http://purl.uniprot.org/uniprot/#_Q6N0A8-mappedCitation-17479112http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17479112
http://purl.uniprot.org/uniprot/A0A024QZT4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17479112
http://purl.uniprot.org/uniprot/P50453http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17479112