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http://purl.uniprot.org/citations/33132160http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/33132160http://www.w3.org/2000/01/rdf-schema#comment"Split luciferase complementary assay has been used to investigate the effect of WD domain deletion on Apaf-1 oligomerization. Apaf-1 is an adaptor molecule in formation of apoptosome that activates caspase-9, an activation that is a key event in the mitochondrial cell death pathway. Structural studies suggest that normally Apaf-1 is held in an inactive conformation by intramolecular interactions between Apaf-1's nucleotide binding domain and one of its WD40 domains (WD1). In the prevailing model of Apaf-1 activation, cytochrome c binds to sites in WD1 and in Apaf-1's second WD40 domain (WD2), moving WD1 and WD2 closer together and rotating WD1 away from the nucleotide binding domain. This allows Apaf-1 to bind dATP or ATP and to form the apoptosome, which activates caspase-9. This model predicts that cytochrome c binding to both WD domains is necessary for apoptosome formation and that an Apaf-1 with only WD1 will be locked in an inactive conformation that cannot be activated by cytochrome c. Here we investigated the effect of removing one WD domain (Apaf-1 1-921) on Apaf-1 interactions and caspase activation. Apaf-1 1-921 could not activate caspase-9, even in the presence of cytochrome c. These data show that a single WD domain is sufficient to lock Apaf-1 in an inactive state and this state cannot be altered by cytochrome c."xsd:string
http://purl.uniprot.org/citations/33132160http://purl.org/dc/terms/identifier"doi:10.1016/j.biochi.2020.10.013"xsd:string
http://purl.uniprot.org/citations/33132160http://purl.uniprot.org/core/author"Hosseinkhani S."xsd:string
http://purl.uniprot.org/citations/33132160http://purl.uniprot.org/core/author"Fearnhead H.O."xsd:string
http://purl.uniprot.org/citations/33132160http://purl.uniprot.org/core/author"Eriksson L.A."xsd:string
http://purl.uniprot.org/citations/33132160http://purl.uniprot.org/core/author"Nikkhah M."xsd:string
http://purl.uniprot.org/citations/33132160http://purl.uniprot.org/core/author"Tashakor A."xsd:string
http://purl.uniprot.org/citations/33132160http://purl.uniprot.org/core/author"Noori A.R."xsd:string
http://purl.uniprot.org/citations/33132160http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/33132160http://purl.uniprot.org/core/name"Biochimie"xsd:string
http://purl.uniprot.org/citations/33132160http://purl.uniprot.org/core/pages"23-29"xsd:string
http://purl.uniprot.org/citations/33132160http://purl.uniprot.org/core/title"Loss of WD2 subdomain of Apaf-1 forms an apoptosome structure which blocks activation of caspase-3 and caspase-9."xsd:string
http://purl.uniprot.org/citations/33132160http://purl.uniprot.org/core/volume"180"xsd:string
http://purl.uniprot.org/citations/33132160http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/33132160
http://purl.uniprot.org/citations/33132160http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/33132160
http://purl.uniprot.org/uniprot/#_A7E2A2-mappedCitation-33132160http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33132160
http://purl.uniprot.org/uniprot/#_A5YM44-mappedCitation-33132160http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33132160
http://purl.uniprot.org/uniprot/#_O14727-mappedCitation-33132160http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33132160
http://purl.uniprot.org/uniprot/O14727http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/33132160
http://purl.uniprot.org/uniprot/A5YM44http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/33132160
http://purl.uniprot.org/uniprot/A7E2A2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/33132160