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http://purl.uniprot.org/citations/9395403http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9395403http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9395403http://www.w3.org/2000/01/rdf-schema#comment"Caspases are a family of cysteine proteases implicated in the biochemical and morphological changes that occur during apoptosis (programmed cell death). The loop domain of Bcl-2 is cleaved at Asp34 by caspase-3 (CPP32) in vitro, in cells overexpressing caspase-3, and after induction of apoptosis by Fas ligation and interleukin-3 withdrawal. The carboxyl-terminal Bcl-2 cleavage product triggered cell death and accelerated Sindbis virus-induced apoptosis, which was dependent on the BH3 homology and transmembrane domains of Bcl-2. Inhibitor studies indicated that cleavage of Bcl-2 may further activate downstream caspases and contribute to amplification of the caspase cascade. Cleavage-resistant mutants of Bcl-2 had increased protection from interleukin-3 withdrawal and Sindbis virus-induced apoptosis. Thus, cleavage of Bcl-2 by caspases may ensure the inevitability of cell death."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.org/dc/terms/identifier"doi:10.1126/science.278.5345.1966"xsd:string
http://purl.uniprot.org/citations/9395403http://purl.org/dc/terms/identifier"doi:10.1126/science.278.5345.1966"xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Hardwick J.M."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Hardwick J.M."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Kastan M.B."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Kastan M.B."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Ueno K."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Ueno K."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Ravi R."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Ravi R."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Clem R.J."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Clem R.J."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Kirsch D.G."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Kirsch D.G."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Cheng E.H.-Y."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Cheng E.H.-Y."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Bedi A."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/author"Bedi A."xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/9395403http://purl.uniprot.org/core/name"Science"xsd:string