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http://purl.uniprot.org/citations/20692228http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20692228http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20692228http://www.w3.org/2000/01/rdf-schema#comment"Selenoprotein K (SelK), an endoplasmic reticulum (ER) resident protein, its biological function has been less-well studied. To investigate the role of SelK in the ER stress response, effects of SelK gene silence and ER stress agents on expression of SelK and cell apoptosis in HepG2 cells were studied. The results showed that SelK was regulated by ER stress agents, Tunicamycin (Tm) and beta-Mercaptoethanol (beta-ME), in HepG2 cells. Moreover, the SelK gene silence by RNA interference could significantly aggravate HepG2 cell death and apoptosis induced by the ER stress agents. These results suggest that SelK is an ER stress-regulated protein and plays an important role in protecting HepG2 cells from ER stress agent-induced apoptosis."xsd:string
http://purl.uniprot.org/citations/20692228http://purl.org/dc/terms/identifier"doi:10.1016/j.abb.2010.08.001"xsd:string
http://purl.uniprot.org/citations/20692228http://purl.org/dc/terms/identifier"doi:10.1016/j.abb.2010.08.001"xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/author"Huang K."xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/author"Huang K."xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/author"Jia Y."xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/author"Jia Y."xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/author"Zhou J."xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/author"Zhou J."xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/author"Du S."xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/author"Du S."xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/pages"137-143"xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/pages"137-143"xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/title"SelK is a novel ER stress-regulated protein and protects HepG2 cells from ER stress agent-induced apoptosis."xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/title"SelK is a novel ER stress-regulated protein and protects HepG2 cells from ER stress agent-induced apoptosis."xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/volume"502"xsd:string
http://purl.uniprot.org/citations/20692228http://purl.uniprot.org/core/volume"502"xsd:string
http://purl.uniprot.org/citations/20692228http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20692228
http://purl.uniprot.org/citations/20692228http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20692228