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http://purl.uniprot.org/citations/23143230http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23143230http://www.w3.org/2000/01/rdf-schema#comment"Aldo-keto reductase 1a4 (AKR1a4; EC 1.1.1.2) is the mouse orthologue of human aldehyde reductase (AKR1a1), the founding member of the AKR family. As an NADPH-dependent enzyme, AKR1a4 catalyses the conversion of D-glucuronate to L-gulonate. AKR1a4 is involved in ascorbate biosynthesis in mice, but has also recently been found to interact with SMAR1, providing a novel mechanism of ROS regulation by ATM. Here, the crystal structure of AKR1a4 in its apo form at 1.64 Å resolution as well as the characterization of the binding of AKR1a4 to NADPH and P44, a peptide derived from SMAR1, is presented."xsd:string
http://purl.uniprot.org/citations/23143230http://purl.org/dc/terms/identifier"doi:10.1107/s1744309112037128"xsd:string
http://purl.uniprot.org/citations/23143230http://purl.uniprot.org/core/author"Jia Z."xsd:string
http://purl.uniprot.org/citations/23143230http://purl.uniprot.org/core/author"Faucher F."xsd:string
http://purl.uniprot.org/citations/23143230http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23143230http://purl.uniprot.org/core/name"Acta Crystallogr Sect F Struct Biol Cryst Commun"xsd:string
http://purl.uniprot.org/citations/23143230http://purl.uniprot.org/core/pages"1271-1274"xsd:string
http://purl.uniprot.org/citations/23143230http://purl.uniprot.org/core/title"High-resolution structure of AKR1a4 in the apo form and its interaction with ligands."xsd:string
http://purl.uniprot.org/citations/23143230http://purl.uniprot.org/core/volume"68"xsd:string
http://purl.uniprot.org/citations/23143230http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23143230
http://purl.uniprot.org/citations/23143230http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23143230
http://purl.uniprot.org/uniprot/#_Q540D7-mappedCitation-23143230http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23143230
http://purl.uniprot.org/uniprot/#_Q80XJ7-mappedCitation-23143230http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23143230
http://purl.uniprot.org/uniprot/#_Q810X5-mappedCitation-23143230http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23143230
http://purl.uniprot.org/uniprot/#_Q3UJW9-mappedCitation-23143230http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23143230
http://purl.uniprot.org/uniprot/#_Q9JII6-mappedCitation-23143230http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23143230
http://purl.uniprot.org/uniprot/Q80XJ7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23143230
http://purl.uniprot.org/uniprot/Q540D7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23143230
http://purl.uniprot.org/uniprot/Q9JII6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23143230
http://purl.uniprot.org/uniprot/Q3UJW9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23143230
http://purl.uniprot.org/uniprot/Q810X5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23143230