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http://purl.uniprot.org/citations/12244325http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12244325http://www.w3.org/2000/01/rdf-schema#comment"Thioredoxin 1 (Trx) is a known redox regulator that is implicated in the redox control of cell growth and apoptosis inhibition. Here we show that Trx is essential for maintaining the content of S-nitrosylated molecules in endothelial cells. Trx itself is S-nitrosylated at cysteine 69 under basal conditions, and this S-nitrosylation is required for scavenging reactive oxygen species and for preserving the redox regulatory activity of Trx. S-nitrosylation of Trx also contributes to the anti-apoptotic function of Trx. Thus, Trx can exert its complete redox regulatory and anti-apoptotic functions in endothelial cells only when cysteine 69 is S-nitrosylated."xsd:string
http://purl.uniprot.org/citations/12244325http://purl.org/dc/terms/identifier"doi:10.1038/ncb851"xsd:string
http://purl.uniprot.org/citations/12244325http://purl.uniprot.org/core/author"Hoffmann J."xsd:string
http://purl.uniprot.org/citations/12244325http://purl.uniprot.org/core/author"Dimmeler S."xsd:string
http://purl.uniprot.org/citations/12244325http://purl.uniprot.org/core/author"Zeiher A.M."xsd:string
http://purl.uniprot.org/citations/12244325http://purl.uniprot.org/core/author"Berk B.C."xsd:string
http://purl.uniprot.org/citations/12244325http://purl.uniprot.org/core/author"Tischler V."xsd:string
http://purl.uniprot.org/citations/12244325http://purl.uniprot.org/core/author"Haendeler J."xsd:string
http://purl.uniprot.org/citations/12244325http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12244325http://purl.uniprot.org/core/name"Nat Cell Biol"xsd:string
http://purl.uniprot.org/citations/12244325http://purl.uniprot.org/core/pages"743-749"xsd:string
http://purl.uniprot.org/citations/12244325http://purl.uniprot.org/core/title"Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69."xsd:string
http://purl.uniprot.org/citations/12244325http://purl.uniprot.org/core/volume"4"xsd:string
http://purl.uniprot.org/citations/12244325http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12244325
http://purl.uniprot.org/citations/12244325http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12244325
http://purl.uniprot.org/uniprot/#_H9ZYJ2-mappedCitation-12244325http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12244325
http://purl.uniprot.org/uniprot/#_P10599-mappedCitation-12244325http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12244325
http://purl.uniprot.org/uniprot/H9ZYJ2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12244325
http://purl.uniprot.org/uniprot/P10599http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12244325