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http://purl.uniprot.org/citations/15347790http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15347790http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15347790http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/15347790http://www.w3.org/2000/01/rdf-schema#comment"Synechocystis PCC 6803 contains two types of glutathione peroxidase-like proteins (GPX-1 and GPX-2) that utilize NADPH but not reduced glutathione and unsaturated fatty acid hydroperoxides or alkyl hydroperoxides. The steady-state transcript level of gpx-1 gradually increased under oxidative stress conditions imposed by high light intensity, high salinity, or application of methylviologen or t-butyl hydroperoxide in the wild-type and GPX-2 knock-out mutant (gpx-2Delta) cells. To examine the ability of GPX-1, GPX-2, and thioredoxin peroxidase to scavenge lipid hydroperoxide in vivo, we measured the photosynthetic evolution of O(2) and the level of lipid peroxidation in the wild-type and each type of mutant cell after the application of t-butyl hydroperoxide or H(2)O(2). The data reported here indicate that GPX-1 and GPX-2 are essential for the removal of lipid hydroperoxides under normal and stress conditions, leading to the protection of membrane integrity."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.org/dc/terms/identifier"doi:10.1104/pp.104.044842"xsd:string
http://purl.uniprot.org/citations/15347790http://purl.org/dc/terms/identifier"doi:10.1104/pp.104.044842"xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/author"Nakano Y."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/author"Nakano Y."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/author"Takeda T."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/author"Takeda T."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/author"Yoshimura K."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/author"Yoshimura K."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/author"Shigeoka S."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/author"Shigeoka S."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/author"Tamoi M."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/author"Tamoi M."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/author"Gaber A."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/author"Gaber A."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/name"Plant Physiol."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/name"Plant Physiol."xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/pages"2855-2861"xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/pages"2855-2861"xsd:string
http://purl.uniprot.org/citations/15347790http://purl.uniprot.org/core/title"Induction and functional analysis of two reduced nicotinamide adenine dinucleotide phosphate-dependent glutathione peroxidase-like proteins in Synechocystis PCC 6803 during the progression of oxidative stress."xsd:string