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http://purl.uniprot.org/citations/17090549http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17090549http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17090549http://www.w3.org/2000/01/rdf-schema#comment"Bcl-2 is the best characterized member of a large family of proteins that regulate apoptosis. Although it is established that Bcl-2 localized at the mitochondria functions as an anti-apoptotic protein, the function of Bcl-2 at the nucleus remains unclear. Recently we showed that nuclear compartment-associated Bcl-2 inhibits transcription factor activation. Based on this observation, we hypothesized that presence of Bcl-2 at the nucleus may induce rather than protect cells from apoptosis. Here we investigated the putative apoptotic role of nuclear compartment-associated Bcl-2. Additionally, we examined the role of the Bcl-2 BH4 domain in mediating binding to FKBP38, the Bcl-2 mitochondrial chaperone. Our results demonstrate a novel, pro-apoptotic function for nuclear Bcl-2 and identify the Bcl-2 BH4 domain as a key regulator in mediating Bcl-2/FKBP38 binding. These results indicate that Bcl-2 has a dual role as both a protector and a killer and that the ability to switch roles depends on Bcl-2 subcellular localization."xsd:string
http://purl.uniprot.org/citations/17090549http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m606181200"xsd:string
http://purl.uniprot.org/citations/17090549http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m606181200"xsd:string
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/author"Portier B.P."xsd:string
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/author"Portier B.P."xsd:string
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/author"Taglialatela G."xsd:string
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/author"Taglialatela G."xsd:string
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/pages"40493-40502"xsd:string
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/pages"40493-40502"xsd:string
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/title"Bcl-2 localized at the nuclear compartment induces apoptosis after transient overexpression."xsd:string
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/title"Bcl-2 localized at the nuclear compartment induces apoptosis after transient overexpression."xsd:string
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/volume"281"xsd:string
http://purl.uniprot.org/citations/17090549http://purl.uniprot.org/core/volume"281"xsd:string
http://purl.uniprot.org/citations/17090549http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17090549
http://purl.uniprot.org/citations/17090549http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17090549
http://purl.uniprot.org/citations/17090549http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17090549
http://purl.uniprot.org/citations/17090549http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17090549
http://purl.uniprot.org/uniprot/Q14318http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17090549
http://purl.uniprot.org/uniprot/P10415http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17090549