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http://purl.uniprot.org/citations/10198631http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10198631http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10198631http://www.w3.org/2000/01/rdf-schema#comment"Bcl-2 family members that have only a single Bcl-2 homology domain, BH3, are potent inducers of apoptosis, and some appear to play a critical role in developmentally programmed cell death. We examined the regulation of the proapoptotic activity of the BH3-only protein Bim. In healthy cells, most Bim molecules were bound to LC8 cytoplasmic dynein light chain and thereby sequestered to the microtubule-associated dynein motor complex. Certain apoptotic stimuli disrupted the interaction between LC8 and the dynein motor complex. This freed Bim to translocate together with LC8 to Bcl-2 and to neutralize its antiapoptotic activity. This process did not require caspase activity and therefore constitutes an initiating event in apoptosis signaling."xsd:string
http://purl.uniprot.org/citations/10198631http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(00)80456-6"xsd:string
http://purl.uniprot.org/citations/10198631http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(00)80456-6"xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/author"Huang D.C."xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/author"Huang D.C."xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/author"King S.M."xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/author"King S.M."xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/author"Strasser A."xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/author"Strasser A."xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/author"Puthalakath H."xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/author"Puthalakath H."xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/author"O'Reilly L.A."xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/author"O'Reilly L.A."xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/pages"287-296"xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/pages"287-296"xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/title"The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex."xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/title"The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex."xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/volume"3"xsd:string
http://purl.uniprot.org/citations/10198631http://purl.uniprot.org/core/volume"3"xsd:string