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http://purl.uniprot.org/citations/16645094http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16645094http://www.w3.org/2000/01/rdf-schema#comment"Accumulation of misfolded protein in the endoplasmic reticulum (ER) triggers an adaptive stress response-termed the unfolded protein response (UPR)-mediated by the ER transmembrane protein kinase and endoribonuclease inositol-requiring enzyme-1alpha (IRE1alpha). We investigated UPR signaling events in mice in the absence of the proapoptotic BCL-2 family members BAX and BAK [double knockout (DKO)]. DKO mice responded abnormally to tunicamycin-induced ER stress in the liver, with extensive tissue damage and decreased expression of the IRE1 substrate X-box-binding protein 1 and its target genes. ER-stressed DKO cells showed deficient IRE1alpha signaling. BAX and BAK formed a protein complex with the cytosolic domain of IRE1alpha that was essential for IRE1alpha activation. Thus, BAX and BAK function at the ER membrane to activate IRE1alpha signaling and to provide a physical link between members of the core apoptotic pathway and the UPR."xsd:string
http://purl.uniprot.org/citations/16645094http://purl.org/dc/terms/identifier"doi:10.1126/science.1123480"xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/author"Bernasconi P."xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/author"Lee A.H."xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/author"Brandt G.S."xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/author"Bassik M.C."xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/author"Glimcher L.H."xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/author"Schinzel A."xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/author"Hetz C."xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/author"Korsmeyer S.J."xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/author"Fisher J."xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/author"Antonsson B."xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/author"Iwakoshi N.N."xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/pages"572-576"xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/title"Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha."xsd:string
http://purl.uniprot.org/citations/16645094http://purl.uniprot.org/core/volume"312"xsd:string
http://purl.uniprot.org/citations/16645094http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16645094
http://purl.uniprot.org/citations/16645094http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16645094
http://purl.uniprot.org/uniprot/Q16611#attribution-63C891CE6A3F07432A662B1F2480F11Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16645094
http://purl.uniprot.org/uniprot/Q07812#attribution-63C891CE6A3F07432A662B1F2480F11Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16645094
http://purl.uniprot.org/uniprot/O75460#attribution-63C891CE6A3F07432A662B1F2480F11Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16645094
http://purl.uniprot.org/uniprot/P17861#attribution-63C891CE6A3F07432A662B1F2480F11Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16645094