 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
- Reductases
- Reductase
- Dehydrogenase
- Dehydrogenases
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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.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1991 | 1 | 0 | 1 | | 1993 | 0 | 1 | 1 | | 1994 | 1 | 2 | 3 | | 1995 | 3 | 1 | 4 | | 1996 | 1 | 0 | 1 | | 1997 | 0 | 1 | 1 | | 1998 | 1 | 0 | 1 | | 1999 | 2 | 0 | 2 | | 2000 | 2 | 0 | 2 | | 2001 | 1 | 1 | 2 | | 2002 | 2 | 2 | 4 | | 2003 | 2 | 0 | 2 | | 2004 | 2 | 2 | 4 | | 2005 | 0 | 2 | 2 | | 2006 | 1 | 1 | 2 | | 2007 | 1 | 1 | 2 | | 2008 | 3 | 3 | 6 | | 2009 | 2 | 4 | 6 | | 2010 | 0 | 2 | 2 | | 2011 | 3 | 2 | 5 | | 2012 | 0 | 2 | 2 | | 2014 | 2 | 4 | 6 | | 2015 | 1 | 0 | 1 | | 2016 | 0 | 2 | 2 | | 2018 | 0 | 2 | 2 | | 2019 | 5 | 1 | 6 | | 2020 | 2 | 2 | 4 |
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Below are the most recent publications written about "Oxidoreductases" by people in Profiles.
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Newell F, Wilmott JS, Johansson PA, Nones K, Addala V, Mukhopadhyay P, Broit N, Amato CM, Van Gulick R, Kazakoff SH, Patch AM, Koufariotis LT, Lakis V, Leonard C, Wood S, Holmes O, Xu Q, Lewis K, Medina T, Gonzalez R, Saw RPM, Spillane AJ, Stretch JR, Rawson RV, Ferguson PM, Dodds TJ, Thompson JF, Long GV, Levesque MP, Robinson WA, Pearson JV, Mann GJ, Scolyer RA, Waddell N, Hayward NK. Whole-genome sequencing of acral melanoma reveals genomic complexity and diversity. Nat Commun. 2020 10 16; 11(1):5259.
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Rudolph J, Luger K. The secret life of histones. Science. 2020 07 03; 369(6499):33.
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Copley SD. Evolution of new enzymes by gene duplication and divergence. FEBS J. 2020 04; 287(7):1262-1283.
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Sieber S, Daeppen C, Jenul C, Mannancherril V, Eberl L, Gademann K. Biosynthesis and Structure-Activity Relationship Investigations of the Diazeniumdiolate Antifungal Agent Fragin. Chembiochem. 2020 06 02; 21(11):1587-1592.
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Hamby H, Li B, Shinopoulos KE, Keller HR, Elliott SJ, Dukovic G. Light-driven carbon-carbon bond formation via CO2 reduction catalyzed by complexes of CdS nanorods and a 2-oxoacid oxidoreductase. Proc Natl Acad Sci U S A. 2020 01 07; 117(1):135-140.
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Prates ET, Crowley MF, Skaf MS, Beckham GT. Catalytic Mechanism of Aryl-Ether Bond Cleavage in Lignin by LigF and LigG. J Phys Chem B. 2019 12 05; 123(48):10142-10151.
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Howie HL, Hay AM, de Wolski K, Waterman H, Lebedev J, Fu X, Culp-Hill R, D'Alessandro A, Gorham JD, Ranson MS, Roback JD, Thomson PC, Zimring JC. Differences in Steap3 expression are a mechanism of genetic variation of RBC storage and oxidative damage in mice. Blood Adv. 2019 08 13; 3(15):2272-2285.
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Piquet AL, Khan M, Warner JEA, Wicklund MP, Bennett JL, Leehey MA, Seeberger L, Schreiner TL, Paz Soldan MM, Clardy SL. Novel clinical features of glycine receptor antibody syndrome: A series of 17 cases. Neurol Neuroimmunol Neuroinflamm. 2019 09; 6(5):e592.
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Favazzo LJ, Gill AL, Farnsworth CW, Mooney RA, Gill SR. The Response of nor and nos Contributes to Staphylococcus aureus Virulence and Metabolism. J Bacteriol. 2019 05 01; 201(9).
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Eckert CA, Freed E, Wawrousek K, Smolinski S, Yu J, Maness PC. Inactivation of the uptake hydrogenase in the purple non-sulfur photosynthetic bacterium Rubrivivax gelatinosus CBS enables a biological water-gas shift platform for H2 production. J Ind Microbiol Biotechnol. 2019 Jul; 46(7):993-1002.
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