 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 |
|---|
| 1993 | 0 | 1 | 1 | | 1994 | 1 | 2 | 3 | | 1995 | 2 | 1 | 3 | | 1997 | 0 | 1 | 1 | | 1999 | 2 | 0 | 2 | | 2000 | 2 | 0 | 2 | | 2001 | 1 | 1 | 2 | | 2002 | 1 | 2 | 3 | | 2003 | 2 | 0 | 2 | | 2004 | 2 | 2 | 4 | | 2005 | 0 | 2 | 2 | | 2006 | 1 | 1 | 2 | | 2007 | 1 | 0 | 1 | | 2008 | 2 | 2 | 4 | | 2009 | 2 | 3 | 5 | | 2010 | 0 | 1 | 1 | | 2011 | 1 | 2 | 3 | | 2012 | 0 | 1 | 1 | | 2014 | 1 | 2 | 3 | | 2016 | 0 | 1 | 1 | | 2018 | 0 | 1 | 1 | | 2019 | 3 | 1 | 4 | | 2020 | 2 | 1 | 3 |
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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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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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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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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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Laje K, Seger M, Dungan B, Cooke P, Polle J, Holguin FO. Phytoene Accumulation in the Novel Microalga Chlorococcum sp. Using the Pigment Synthesis Inhibitor Fluridone. Mar Drugs. 2019 Mar 22; 17(3).
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Boddicker AM, Mosier AC. Genomic profiling of four cultivated Candidatus Nitrotoga spp. predicts broad metabolic potential and environmental distribution. ISME J. 2018 12; 12(12):2864-2882.
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Hromada SE, Hilbrands AM, Wolf EM, Ross JL, Hegg TR, Roth AG, Hollowell MT, Anderson CE, Benson DE. Protein oxidation involved in Cys-Tyr post-translational modification. J Inorg Biochem. 2017 11; 176:168-174.
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