Oxidoreductases
"Oxidoreductases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Descriptor ID |
D010088
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MeSH Number(s) |
D08.811.682
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Concept/Terms |
Oxidoreductases- Oxidoreductases
- Dehydrogenases
- Reductases
- Dehydrogenase
- Reductase
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Below are MeSH descriptors whose meaning is more general than "Oxidoreductases".
Below are MeSH descriptors whose meaning is more specific than "Oxidoreductases".
This graph shows the total number of publications written about "Oxidoreductases" by people in this website by year, and whether "Oxidoreductases" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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1983 | 1 | 0 | 1 | 1990 | 3 | 0 | 3 | 2002 | 1 | 0 | 1 | 2003 | 3 | 0 | 3 | 2006 | 0 | 1 | 1 | 2007 | 1 | 1 | 2 | 2008 | 1 | 0 | 1 | 2009 | 0 | 1 | 1 | 2015 | 0 | 1 | 1 |
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Below are the most recent publications written about "Oxidoreductases" by people in Profiles.
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Ma J, Rixey WG, Alvarez PJ. Increased fermentation activity and persistent methanogenesis in a model aquifer system following source removal of an ethanol blend release. Water Res. 2015 Jan 01; 68:479-86.
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Asghar M, Chugh G, Lokhandwala MF. Inflammation compromises renal dopamine D1 receptor function in rats. Am J Physiol Renal Physiol. 2009 Dec; 297(6):F1543-9.
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Kanan Y, Wicker LD, Al-Ubaidi MR, Mandal NA, Kasus-Jacobi A. Retinol dehydrogenases RDH11 and RDH12 in the mouse retina: expression levels during development and regulation by oxidative stress. Invest Ophthalmol Vis Sci. 2008 Mar; 49(3):1071-8.
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Tu SC. Activity coupling and complex formation between bacterial luciferase and flavin reductases. Photochem Photobiol Sci. 2008 Feb; 7(2):183-8.
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Kanan Y, Kasus-Jacobi A, Moiseyev G, Sawyer K, Ma JX, Al-Ubaidi MR. Retinoid processing in cone and Müller cell lines. Exp Eye Res. 2008 Feb; 86(2):344-54.
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Shen W, Wei Y, Dauk M, Tan Y, Taylor DC, Selvaraj G, Zou J. Involvement of a glycerol-3-phosphate dehydrogenase in modulating the NADH/NAD+ ratio provides evidence of a mitochondrial glycerol-3-phosphate shuttle in Arabidopsis. Plant Cell. 2006 Feb; 18(2):422-41.
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Low JC, Tu SC. Energy transfer evidence for in vitro and in vivo complexes of Vibrio harveyi flavin reductase P and luciferase. Photochem Photobiol. 2003 Apr; 77(4):446-52.
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Kremer L, Dover LG, Morbidoni HR, Vilchèze C, Maughan WN, Baulard A, Tu SC, Honoré N, Deretic V, Sacchettini JC, Locht C, Jacobs WR, Besra GS. Inhibition of InhA activity, but not KasA activity, induces formation of a KasA-containing complex in mycobacteria. J Biol Chem. 2003 Jun 06; 278(23):20547-54.
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Wei CJ, Lei B, Musser JM, Tu SC. Isoniazid activation defects in recombinant Mycobacterium tuberculosis catalase-peroxidase (KatG) mutants evident in InhA inhibitor production. Antimicrob Agents Chemother. 2003 Feb; 47(2):670-5.
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Mîinea C, Kuruvilla R, Merrikh H, Eichberg J. Altered arachidonic acid biosynthesis and antioxidant protection mechanisms in Schwann cells grown in elevated glucose. J Neurochem. 2002 Jun; 81(6):1253-62.
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