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http://purl.uniprot.org/citations/12715897http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12715897http://www.w3.org/2000/01/rdf-schema#comment"Cellular defense systems against reactive oxygen species (ROS) include thioredoxin reductase (TrxR) and glutathione reductase (GR). They generate sulfhydryl-reducing systems which are coupled to antioxidant enzymes, the thioredoxin and glutathione peroxidases (TPx and GPx). The fruit fly Drosophila lacks a functional GR, suggesting that the thioredoxin system is the major source for recycling glutathione. Whole genome in silico analysis identified two non-selenium containing putative GPx genes. We examined the biochemical characteristics of one of these gene products and found that it lacks GPx activity and functions as a TPx. Transgene-dependent overexpression of the newly identified Glutathione peroxidase homolog with thioredoxin peroxidase activity (Gtpx-1) gene increases resistance to experimentally induced oxidative stress, but does not compensate for the loss of catalase, an enzyme which, like GTPx-1, functions to eliminate hydrogen peroxide. The results suggest that GTPx-1 is part of the Drosophila Trx antioxidant defense system but acts in a genetically distinct pathway or in a different cellular compartment than catalase."xsd:string
http://purl.uniprot.org/citations/12715897http://purl.org/dc/terms/identifier"doi:10.1515/bc.2003.052"xsd:string
http://purl.uniprot.org/citations/12715897http://purl.uniprot.org/core/author"Becker K."xsd:string
http://purl.uniprot.org/citations/12715897http://purl.uniprot.org/core/author"Phillips J.P."xsd:string
http://purl.uniprot.org/citations/12715897http://purl.uniprot.org/core/author"Rahlfs S."xsd:string
http://purl.uniprot.org/citations/12715897http://purl.uniprot.org/core/author"Jackle H."xsd:string
http://purl.uniprot.org/citations/12715897http://purl.uniprot.org/core/author"Missirlis F."xsd:string
http://purl.uniprot.org/citations/12715897http://purl.uniprot.org/core/author"Bauer H."xsd:string
http://purl.uniprot.org/citations/12715897http://purl.uniprot.org/core/author"Hilliker A."xsd:string
http://purl.uniprot.org/citations/12715897http://purl.uniprot.org/core/author"Dimopoulos N."xsd:string
http://purl.uniprot.org/citations/12715897http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12715897http://purl.uniprot.org/core/name"Biol Chem"xsd:string
http://purl.uniprot.org/citations/12715897http://purl.uniprot.org/core/pages"463-472"xsd:string
http://purl.uniprot.org/citations/12715897http://purl.uniprot.org/core/title"A putative glutathione peroxidase of Drosophila encodes a thioredoxin peroxidase that provides resistance against oxidative stress but fails to complement a lack of catalase activity."xsd:string
http://purl.uniprot.org/citations/12715897http://purl.uniprot.org/core/volume"384"xsd:string
http://purl.uniprot.org/citations/12715897http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12715897
http://purl.uniprot.org/citations/12715897http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12715897
http://purl.uniprot.org/uniprot/Q4V6H2#attribution-88764CFF32E69A2E7FF768C375A1E592http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12715897
http://purl.uniprot.org/uniprot/Q8IRD4#attribution-0AA812349FE35CD8F3491CFDCEAAE86Dhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12715897
http://purl.uniprot.org/uniprot/Q8IRD4#attribution-35A991D77FCD2E801D89391B81374B9Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12715897
http://purl.uniprot.org/uniprot/Q9VZQ8#attribution-0AA812349FE35CD8F3491CFDCEAAE86Dhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12715897
http://purl.uniprot.org/uniprot/Q9VZQ8#attribution-35A991D77FCD2E801D89391B81374B9Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12715897
http://purl.uniprot.org/uniprot/Q8IRD3#attribution-0AA812349FE35CD8F3491CFDCEAAE86Dhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12715897
http://purl.uniprot.org/uniprot/Q8IRD3#attribution-35A991D77FCD2E801D89391B81374B9Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12715897