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dbo:abstract
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- La xantina deshidrogenasa (EC 1.17.3.2, EC 1.17.1.4), conocida también por su símbolo XDH, es una enzima que cataliza la siguiente reacción química: xantina + NAD+ + H2O urato + NADH + H+ Por lo tanto los tres sustratos de esta enzima son xantina, NAD+ y agua; mientras que sus tres productos son urato, NADH y un ion hidrógeno. La enzima se encuentra codificada por el gen Xdh. (es)
- La xantina deshidrogenasa (EC 1.17.3.2, EC 1.17.1.4), conocida también por su símbolo XDH, es una enzima que cataliza la siguiente reacción química: xantina + NAD+ + H2O urato + NADH + H+ Por lo tanto los tres sustratos de esta enzima son xantina, NAD+ y agua; mientras que sus tres productos son urato, NADH y un ion hidrógeno. La enzima se encuentra codificada por el gen Xdh. (es)
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dbo:casNumber
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dbo:ecNumber
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dbo:hgncid
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dbo:omim
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dbo:pdb
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dbo:symbol
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dbo:wikiPageID
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prop-es:altsymbols
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- ; XO; XOR (es)
- ; XO; XOR (es)
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prop-es:authorSeparator
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prop-es:autor
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- Amaya Y (es)
- Battelli MG, Lorenzoni E (es)
- Blake DR (es)
- Cejková J, Ardan T, Filipec M, Midelfart A (es)
- Corte ED, Stirpe F (es)
- Frandsen U (es)
- Frederiks WM, Vreeling-Sindelárová H (es)
- Frei E (es)
- Halila R (es)
- Hellsten Y (es)
- Hille R (es)
- Huecksteadt TP (es)
- Ichida K (es)
- Kamatani N (es)
- Laan M (es)
- Martelin E, Palvimo JJ, Lapatto R, Raivio KO (es)
- Meneshian A, Bulkley GB (es)
- Minoshima S (es)
- N, Nishino T (es)
- Newaz MA, Adeeb NN (es)
- Noda K (es)
- Orthenblad N (es)
- Parzen SD, Fox AS (es)
- Rajagopalan KV, Handler P (es)
- Rouquette M (es)
- Rytkönen EM (es)
- Saksela M, Raivio KO (es)
- Satoh A, Sasago S, Takahashi S, Kato N (es)
- Smith ST, Rajagopalan KV, Handler P (es)
- Sopko B (es)
- Stevens C (es)
- Stiborová M (es)
- Wang Y (es)
- Xu P (es)
- Xu P, Huecksteadt TP, Harrison R, Hoidal JR (es)
- Xu P, Huecksteadt TP, Hoidal JR (es)
- Zhu XL (es)
- Many A, Westerhausen-Larson A, Kanbour-Shakir A, Roberts JM (es)
- Parschat K, Canne C, Huttermann J, Kappl R, Fetzner S (es)
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- Amaya Y (es)
- Battelli MG, Lorenzoni E (es)
- Blake DR (es)
- Cejková J, Ardan T, Filipec M, Midelfart A (es)
- Corte ED, Stirpe F (es)
- Frandsen U (es)
- Frederiks WM, Vreeling-Sindelárová H (es)
- Frei E (es)
- Halila R (es)
- Hellsten Y (es)
- Hille R (es)
- Huecksteadt TP (es)
- Ichida K (es)
- Kamatani N (es)
- Laan M (es)
- Martelin E, Palvimo JJ, Lapatto R, Raivio KO (es)
- Meneshian A, Bulkley GB (es)
- Minoshima S (es)
- N, Nishino T (es)
- Newaz MA, Adeeb NN (es)
- Noda K (es)
- Orthenblad N (es)
- Parzen SD, Fox AS (es)
- Rajagopalan KV, Handler P (es)
- Rouquette M (es)
- Rytkönen EM (es)
- Saksela M, Raivio KO (es)
- Satoh A, Sasago S, Takahashi S, Kato N (es)
- Smith ST, Rajagopalan KV, Handler P (es)
- Sopko B (es)
- Stevens C (es)
- Stiborová M (es)
- Wang Y (es)
- Xu P (es)
- Xu P, Huecksteadt TP, Harrison R, Hoidal JR (es)
- Xu P, Huecksteadt TP, Hoidal JR (es)
- Zhu XL (es)
- Many A, Westerhausen-Larson A, Kanbour-Shakir A, Roberts JM (es)
- Parschat K, Canne C, Huttermann J, Kappl R, Fetzner S (es)
- Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF (es)
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prop-es:año
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prop-es:casNumber
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prop-es:chembl
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prop-es:displayAuthors
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prop-es:doi
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prop-es:ecNumber
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prop-es:ecnumber
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prop-es:geneatlasImage
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- PBB_GE_XDH_210301_at_tn.png (es)
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prop-es:goCode
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prop-es:hgncid
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prop-es:homologene
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prop-es:hsEnsembl
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- ENSG00000158125 (es)
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prop-es:hsGenlocChr
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prop-es:hsRefseqmrna
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prop-es:hsRefseqprotein
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prop-es:imageSource
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- PDB rendering based on 1fiq. (es)
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prop-es:iubmbEcNumber
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prop-es:last
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prop-es:mgiid
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prop-es:mmEnsembl
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- ENSMUSG00000024066 (es)
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prop-es:mmEntrezgene
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prop-es:mmGenlocChr
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prop-es:mmGenlocDb
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prop-es:mmGenlocEnd
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prop-es:mmGenlocStart
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prop-es:mmRefseqmrna
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- NM_011723 (es)
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prop-es:mmRefseqprotein
|
- NP_035853 (es)
- NP_035853 (es)
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prop-es:mmUniprot
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prop-es:name
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- Xantina deshidrogenasa (es)
- Xantina deshidrogenasa (es)
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prop-es:número
|
- 1 (xsd:integer)
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- Pt 1 (es)
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prop-es:omim
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prop-es:path
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- PBB/7498 (es)
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prop-es:pdb
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prop-es:publicación
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- S (es)
- J. Biol. Chem. (es)
- Placenta (es)
- Carcinogenesis (es)
- Chem. Rev. (es)
- Gene (es)
- Biochem. Biophys. Res. Commun. (es)
- Biochem. J. (es)
- Biochim. Biophys. Acta. (es)
- FEBS Lett. (es)
- Proc. Natl. Acad. Sci. U.S.A. (es)
- Biochem. Soc. Trans. (es)
- J. Clin. Invest. (es)
- Genomics (es)
- Histol. Histopathol. (es)
- Cytogenet. Cell Genet. (es)
- J. Physiol. (es)
- Acta Histochem. (es)
- Gene. (es)
- Med. J. Malaysia (es)
- Microcirculation (es)
- S (es)
- J. Biol. Chem. (es)
- Placenta (es)
- Carcinogenesis (es)
- Chem. Rev. (es)
- Gene (es)
- Biochem. Biophys. Res. Commun. (es)
- Biochem. J. (es)
- Biochim. Biophys. Acta. (es)
- FEBS Lett. (es)
- Proc. Natl. Acad. Sci. U.S.A. (es)
- Biochem. Soc. Trans. (es)
- J. Clin. Invest. (es)
- Genomics (es)
- Histol. Histopathol. (es)
- Cytogenet. Cell Genet. (es)
- J. Physiol. (es)
- Acta Histochem. (es)
- Gene. (es)
- Med. J. Malaysia (es)
- Microcirculation (es)
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prop-es:páginas
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prop-es:symbol
| |
prop-es:título
|
- Xanthine oxidoreductase and xanthine oxidase in human cornea (es)
- Purification and properties of chicken liver xanthine dehydrogenase (es)
- The physiology of endothelial xanthine oxidase: from urate catabolism to reperfusion injury to inflammatory signal transduction (es)
- Molecular cloning, tissue expression of human xanthine dehydrogenase (es)
- Mapping of the gene for human xanthine dehydrogenase to band p23 of chromosome 2 (es)
- Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria (es)
- Detection of xanthine oxidase in human plasma (es)
- The Mononuclear Molybdenum Enzymes (es)
- Purification of Xanthine Dehydrogenase from Drosophila Melanogaster (es)
- Nuclear factor Y activates the human xanthine oxidoreductase gene promoter (es)
- The human gene for xanthine dehydrogenase is localized on chromosome band 2q22 (es)
- Xanthine oxidase/dehydrogenase is present in human placenta (es)
- Molecular cloning and characterization of the human xanthine dehydrogenase gene (es)
- Ultrastructural localization of xanthine oxidoreductase activity in isolated rat liver cells (es)
- Cloning and expression in vitro of human xanthine dehydrogenase/oxidase (es)
- Cloning of the cDNA encoding human xanthine dehydrogenase : structural analysis of the protein and chromosomal location of the gene (es)
- Expression of xanthine oxidase activity in human endothelial cells as a function of cell density (es)
- Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization (es)
- Purification and properties of xanthine dehydroganase from Micrococcus lactilyticus (es)
- Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus (es)
- Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver (es)
- Regulation of xanthine dehydrogenase in rat liver in response to peroxisome proliferators (es)
- Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion (es)
- Carcinogenic aristolochic acids upon activation by DT-diaphorase form adducts found in DNA of patients with Chinese herbs nephropathy (es)
- Xanthine oxidase in human skeletal muscle following eccentric exercise: a role in inflammation (es)
- Assignment of human xanthine dehydrogenase gene to chromosome 2p22 (es)
- The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase into oxidase and purification of the enzyme (es)
- Xanthine oxidoreductase and xanthine oxidase in human cornea (es)
- Purification and properties of chicken liver xanthine dehydrogenase (es)
- The physiology of endothelial xanthine oxidase: from urate catabolism to reperfusion injury to inflammatory signal transduction (es)
- Molecular cloning, tissue expression of human xanthine dehydrogenase (es)
- Mapping of the gene for human xanthine dehydrogenase to band p23 of chromosome 2 (es)
- Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria (es)
- Detection of xanthine oxidase in human plasma (es)
- The Mononuclear Molybdenum Enzymes (es)
- Purification of Xanthine Dehydrogenase from Drosophila Melanogaster (es)
- Nuclear factor Y activates the human xanthine oxidoreductase gene promoter (es)
- The human gene for xanthine dehydrogenase is localized on chromosome band 2q22 (es)
- Xanthine oxidase/dehydrogenase is present in human placenta (es)
- Molecular cloning and characterization of the human xanthine dehydrogenase gene (es)
- Ultrastructural localization of xanthine oxidoreductase activity in isolated rat liver cells (es)
- Cloning and expression in vitro of human xanthine dehydrogenase/oxidase (es)
- Cloning of the cDNA encoding human xanthine dehydrogenase : structural analysis of the protein and chromosomal location of the gene (es)
- Expression of xanthine oxidase activity in human endothelial cells as a function of cell density (es)
- Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization (es)
- Purification and properties of xanthine dehydroganase from Micrococcus lactilyticus (es)
- Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus (es)
- Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver (es)
- Regulation of xanthine dehydrogenase in rat liver in response to peroxisome proliferators (es)
- Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion (es)
- Carcinogenic aristolochic acids upon activation by DT-diaphorase form adducts found in DNA of patients with Chinese herbs nephropathy (es)
- Xanthine oxidase in human skeletal muscle following eccentric exercise: a role in inflammation (es)
- Assignment of human xanthine dehydrogenase gene to chromosome 2p22 (es)
- The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase into oxidase and purification of the enzyme (es)
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- Structure. (es)
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dct:subject
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rdf:type
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rdfs:comment
|
- La xantina deshidrogenasa (EC 1.17.3.2, EC 1.17.1.4), conocida también por su símbolo XDH, es una enzima que cataliza la siguiente reacción química: xantina + NAD+ + H2O urato + NADH + H+ Por lo tanto los tres sustratos de esta enzima son xantina, NAD+ y agua; mientras que sus tres productos son urato, NADH y un ion hidrógeno. La enzima se encuentra codificada por el gen Xdh. (es)
- La xantina deshidrogenasa (EC 1.17.3.2, EC 1.17.1.4), conocida también por su símbolo XDH, es una enzima que cataliza la siguiente reacción química: xantina + NAD+ + H2O urato + NADH + H+ Por lo tanto los tres sustratos de esta enzima son xantina, NAD+ y agua; mientras que sus tres productos son urato, NADH y un ion hidrógeno. La enzima se encuentra codificada por el gen Xdh. (es)
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rdfs:label
|
- Xantina deshidrogenasa (es)
- Xantina deshidrogenasa (es)
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owl:sameAs
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prov:wasDerivedFrom
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foaf:isPrimaryTopicOf
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is owl:sameAs
of | |
is foaf:primaryTopic
of | |