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http://purl.uniprot.org/citations/8631956http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8631956http://www.w3.org/2000/01/rdf-schema#comment"The Caenorhabditis elegans cell death gene, ced-3, encodes one of the two proteins required for apoptosis in this organism. The primary sequence similarities between Ced-3 and the mammalian interleukin-1beta converting enzyme (ICE) suggest that these two proteins may have functionally similar active sites and that Ced-3 may function as a cysteine protease. Here we report that in vitro transcribed and translated Ced-3 protein (p56) underwent rapid processing to smaller fragments. Replacement of the predicted active site cysteine of Ced-3 with serine (C364S) prevented the generation of smaller proteolytic fragments, suggesting that the processing might be an autocatalytic process. Peptide aldehydes with aspartic acid at the P1 position blocked Ced-3 autocatalysis. Furthermore, the protease inhibition profile of Ced-3 was similar to the profile reported for ICE. These functional data demonstrate that Ced-3 is an Asp-dependent cysteine protease with substrate specificity similar to that of ICE. Aurintricarboxylic acid, an inhibitor of apoptosis in mammalian cells, blocked Ced-3 autocatalytic activity, suggesting that an aurintricarboxylic acid-sensitive Ced-3/ICE-related protease might be involved in the apoptosis pathway(s) in mammalian cells."xsd:string
http://purl.uniprot.org/citations/8631956http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.7.3517"xsd:string
http://purl.uniprot.org/citations/8631956http://purl.uniprot.org/core/author"Mankovich J.A."xsd:string
http://purl.uniprot.org/citations/8631956http://purl.uniprot.org/core/author"Ghayur T."xsd:string
http://purl.uniprot.org/citations/8631956http://purl.uniprot.org/core/author"Hugunin M."xsd:string
http://purl.uniprot.org/citations/8631956http://purl.uniprot.org/core/author"Quintal L.J."xsd:string
http://purl.uniprot.org/citations/8631956http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8631956http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/8631956http://purl.uniprot.org/core/pages"3517-3522"xsd:string
http://purl.uniprot.org/citations/8631956http://purl.uniprot.org/core/title"Protease activity of in vitro transcribed and translated Caenorhabditis elegans cell death gene (ced-3) product."xsd:string
http://purl.uniprot.org/citations/8631956http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8631956http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8631956
http://purl.uniprot.org/citations/8631956http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8631956
http://purl.uniprot.org/uniprot/P42573#attribution-7372B5A42123A812447EDF21422B2DFFhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/8631956
http://purl.uniprot.org/uniprot/D3YT61#attribution-7372B5A42123A812447EDF21422B2DFFhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/8631956
http://purl.uniprot.org/uniprot/#_D3YT61-mappedCitation-8631956http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/8631956
http://purl.uniprot.org/uniprot/#_P42573-mappedCitation-8631956http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/8631956
http://purl.uniprot.org/uniprot/P42573http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/8631956
http://purl.uniprot.org/uniprot/D3YT61http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/8631956