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http://purl.uniprot.org/citations/9384385http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9384385http://www.w3.org/2000/01/rdf-schema#comment"The Caenorhabditis elegans gene ced-9 prevents cells from undergoing programmed cell death and encodes a protein similar to the mammalian cell-death inhibitor Bcl-2. We show here that the CED-9 protein is a substrate for the C. elegans cell-death protease CED-3, which is a member of a family of cysteine proteases first defined by CED-3 and human interleukin-1beta converting enzyme (ICE). CED-9 can be cleaved by CED-3 at two sites near its amino terminus, and the presence of at least one of these sites is important for complete protection by CED-9 against cell death. Cleavage of CED-9 by CED-3 generates a carboxy-terminal product that resembles Bcl-2 in sequence and in function. Bcl-2 and the baculovirus protein p35, which inhibits cell death in different species through a mechanism that depends on the presence of its cleavage site for the CED-3/ICE family of proteases, inhibit cell death additively in C. elegans. Our results indicate that CED-9 prevents programmed cell death in C. elegans through two distinct mechanisms: first, CED-9 may, by analogy with p35, directly inhibit the CED-3 protease by an interaction involving the CED-3 cleavage sites in CED-9; second, CED-9 may directly or indirectly inhibit CED-3 by means of a protective mechanism similar to that used by mammalian Bcl-2."xsd:string
http://purl.uniprot.org/citations/9384385http://purl.org/dc/terms/identifier"doi:10.1038/36889"xsd:string
http://purl.uniprot.org/citations/9384385http://purl.uniprot.org/core/author"Horvitz H.R."xsd:string
http://purl.uniprot.org/citations/9384385http://purl.uniprot.org/core/author"Xue D."xsd:string
http://purl.uniprot.org/citations/9384385http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9384385http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/9384385http://purl.uniprot.org/core/pages"305-308"xsd:string
http://purl.uniprot.org/citations/9384385http://purl.uniprot.org/core/title"Caenorhabditis elegans CED-9 protein is a bifunctional cell-death inhibitor."xsd:string
http://purl.uniprot.org/citations/9384385http://purl.uniprot.org/core/volume"390"xsd:string
http://purl.uniprot.org/citations/9384385http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9384385
http://purl.uniprot.org/citations/9384385http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9384385
http://purl.uniprot.org/uniprot/P42573#attribution-C7E34B8EB9C26CA22F59C22A6D98BA2Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9384385
http://purl.uniprot.org/uniprot/P41958#attribution-1B0C8E7C79F0CE9D2E04547255F9F9FDhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9384385
http://purl.uniprot.org/uniprot/D3YT61#attribution-C7E34B8EB9C26CA22F59C22A6D98BA2Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9384385
http://purl.uniprot.org/uniprot/#_D3YT61-mappedCitation-9384385http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9384385
http://purl.uniprot.org/uniprot/#_P41958-mappedCitation-9384385http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9384385
http://purl.uniprot.org/uniprot/#_P42573-mappedCitation-9384385http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9384385
http://purl.uniprot.org/uniprot/P42573http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9384385
http://purl.uniprot.org/uniprot/P41958http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9384385
http://purl.uniprot.org/uniprot/D3YT61http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9384385