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http://purl.uniprot.org/citations/11113115http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11113115http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11113115http://www.w3.org/2000/01/rdf-schema#comment"Apaf1/CED4 family members play central roles in apoptosis regulation as activators of caspase family cell death proteases. These proteins contain a nucleotide-binding (NB) self-oligomerization domain and a caspase recruitment domain (CARD). A novel human protein was identified, NAC, that contains an NB domain and CARD. The CARD of NAC interacts selectively with the CARD domain of Apaf1, a caspase-activating protein that couples mitochondria-released cytochrome c (cyt-c) to activation of cytosolic caspases. Cyt-c-mediated activation of caspases in cytosolic extracts and in cells is enhanced by overexpressing NAC and inhibited by reducing NAC using antisense/DNAzymes. Furthermore, association of NAC with Apaf1 is cyt c-inducible, resulting in a mega-complex (>1 MDa) containing both NAC and Apaf1 and correlating with enhanced recruitment and proteolytic processing of pro-caspase-9. NAC also collaborates with Apaf1 in inducing caspase activation and apoptosis in intact cells, whereas fragments of NAC representing only the CARD or NB domain suppress Apaf1-dependent apoptosis induction. NAC expression in vivo is associated with terminal differentiation of short lived cells in epithelia and some other tissues. The ability of NAC to enhance Apaf1-apoptosome function reveals a novel paradigm for apoptosis regulation."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m006309200"xsd:string
http://purl.uniprot.org/citations/11113115http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m006309200"xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Godzik A."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Godzik A."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Xie Z."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Xie Z."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Krajewski S."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Krajewski S."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Reed J.C."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Reed J.C."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Welsh K."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Welsh K."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Krajewska M."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Krajewska M."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Pio F."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Pio F."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Chu Z.-L."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/author"Chu Z.-L."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11113115http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string