http://purl.uniprot.org/citations/9857046 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9857046 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9857046 | http://www.w3.org/2000/01/rdf-schema#comment | "Proteases of the caspase family play a central role in the execution of programmed cell death in all metazoans examined. The Caenorhabditis elegans caspase CED-3 is essential for programmed cell death in this organism. Three additional C. elegans caspase-related genes, csp-1 (caspase homolog-1), which encodes the csp-1A, csp-1B, and csp-1C RNA species; csp-2, which encodes the csp-2A and csp-2B RNA species; and csp-3 are identified. CSP-1A, CSP-1B, CSP-2A, and CSP-2B proteins are similar in sequence to caspase proproteins. CSP-1C is similar only to large caspase subunits, and CSP-3 is similar only to small caspase subunits. CSP-1B can be activated to become a cysteine protease by processing at internal aspartate residues. Activated CSP-1B can cleave the CSP-1B, CED-3, and CSP-2B proproteins, and activated CED-3 can cleave the CED-3 and CSP-2B proproteins. Inhibitor and synthetic substrate studies further suggest that activated CSP-1B and activated CED-3 have different substrate specificities. These results suggest that C. elegans encodes several caspases that might act in proteolytic cascades to regulate processes such as programmed cell death."xsd:string |
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http://purl.uniprot.org/citations/9857046 | http://purl.uniprot.org/core/author | "Shaham S."xsd:string |
http://purl.uniprot.org/citations/9857046 | http://purl.uniprot.org/core/author | "Shaham S."xsd:string |
http://purl.uniprot.org/citations/9857046 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9857046 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9857046 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/9857046 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/9857046 | http://purl.uniprot.org/core/pages | "35109-35117"xsd:string |
http://purl.uniprot.org/citations/9857046 | http://purl.uniprot.org/core/pages | "35109-35117"xsd:string |
http://purl.uniprot.org/citations/9857046 | http://purl.uniprot.org/core/title | "Identification of multiple Caenorhabditis elegans caspases and their potential roles in proteolytic cascades."xsd:string |
http://purl.uniprot.org/citations/9857046 | http://purl.uniprot.org/core/title | "Identification of multiple Caenorhabditis elegans caspases and their potential roles in proteolytic cascades."xsd:string |
http://purl.uniprot.org/citations/9857046 | http://purl.uniprot.org/core/volume | "273"xsd:string |
http://purl.uniprot.org/citations/9857046 | http://purl.uniprot.org/core/volume | "273"xsd:string |
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