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http://purl.uniprot.org/citations/17415523http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17415523http://www.w3.org/2000/01/rdf-schema#comment"Monothiol glutaredoxins with the CGFS sequence at the active site are widespread among prokaryotes and eukaryotes. Two subclasses exist, those with a single glutaredoxin domain and those with a thioredoxin-like region followed by one or more glutaredoxin domains. Studies in Saccharomyces cerevisiae have demonstrated the role of the Grx5 protein in the biogenesis of iron-sulfur clusters. Grx5 homologues in other eukaryotes could carry out similar functions. Two S. cerevisiae monothiol glutaredoxins with the thioredoxin-like extension, Grx3 and Grx4, are modulators of the transcriptional activator Aft1, which regulates iron uptake in yeast. The human PICOT protein is a Grx3/Grx4 homologue with the same hybrid primary structure that regulates protein kinase C activity and may participate in physiological processes such as control of cardiac function. Therefore, monothiol glutaredoxins share a common basic structural motif and biochemical mechanism of action, while participating in a diversity of cellular functions as protein redox regulators."xsd:string
http://purl.uniprot.org/citations/17415523http://purl.org/dc/terms/identifier"doi:10.1007/s00018-007-6554-8"xsd:string
http://purl.uniprot.org/citations/17415523http://purl.uniprot.org/core/author"Herrero E."xsd:string
http://purl.uniprot.org/citations/17415523http://purl.uniprot.org/core/author"de la Torre-Ruiz M.A."xsd:string
http://purl.uniprot.org/citations/17415523http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17415523http://purl.uniprot.org/core/name"Cell Mol Life Sci"xsd:string
http://purl.uniprot.org/citations/17415523http://purl.uniprot.org/core/pages"1518-1530"xsd:string
http://purl.uniprot.org/citations/17415523http://purl.uniprot.org/core/title"Monothiol glutaredoxins: a common domain for multiple functions."xsd:string
http://purl.uniprot.org/citations/17415523http://purl.uniprot.org/core/volume"64"xsd:string
http://purl.uniprot.org/citations/17415523http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17415523
http://purl.uniprot.org/citations/17415523http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17415523
http://purl.uniprot.org/uniprot/#_Q03835-mappedCitation-17415523http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17415523
http://purl.uniprot.org/uniprot/#_P22149-mappedCitation-17415523http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17415523
http://purl.uniprot.org/uniprot/#_P32642-mappedCitation-17415523http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17415523
http://purl.uniprot.org/uniprot/#_Q02784-mappedCitation-17415523http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17415523
http://purl.uniprot.org/uniprot/Q03835http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17415523
http://purl.uniprot.org/uniprot/P22149http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17415523
http://purl.uniprot.org/uniprot/Q02784http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17415523
http://purl.uniprot.org/uniprot/P32642http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17415523