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http://purl.uniprot.org/citations/21827944http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21827944http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21827944http://www.w3.org/2000/01/rdf-schema#comment"The apoptotic protease-activating factor 1 (Apaf-1) relays the death signal in the mitochondrial pathway of apoptosis. Apaf-1 oligomerizes on binding of mitochondrially released cytochrome c into the heptameric apoptosome complex to ignite the downstream cascade of caspases. Here, we present the 3.0 Å crystal structure of full-length murine Apaf-1 in the absence of cytochrome c. The structure shows how the mammalian death switch is kept in its "off" position. By comparing the off state with a recent cryo-electron microscopy derived model of Apaf-1 in its apoptosomal conformation, we depict the molecular events that transform Apaf-1 from autoinhibited monomer to a building block of the caspase-activating apoptosome. Moreover, we have solved the crystal structure of the R265S mutant of full-length murine Apaf-1 in the absence of cytochrome c to 3.55 Å resolution and we show that proper function of Apaf-1 relies on R265 in the vicinity of the bound nucleotide."xsd:string
http://purl.uniprot.org/citations/21827944http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2011.05.013"xsd:string
http://purl.uniprot.org/citations/21827944http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2011.05.013"xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/author"Eschenburg S."xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/author"Eschenburg S."xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/author"Reubold T.F."xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/author"Reubold T.F."xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/author"Wohlgemuth S."xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/author"Wohlgemuth S."xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/pages"1074-1083"xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/pages"1074-1083"xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/title"Crystal structure of full-length Apaf-1: how the death signal is relayed in the mitochondrial pathway of apoptosis."xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/title"Crystal structure of full-length Apaf-1: how the death signal is relayed in the mitochondrial pathway of apoptosis."xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/21827944http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/21827944http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21827944
http://purl.uniprot.org/citations/21827944http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21827944
http://purl.uniprot.org/citations/21827944http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21827944
http://purl.uniprot.org/citations/21827944http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21827944