 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 |
|---|
| 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 | 1 | 0 | 1 | | 2001 | 1 | 0 | 1 | | 2002 | 2 | 1 | 3 | | 2003 | 2 | 0 | 2 | | 2004 | 0 | 2 | 2 | | 2005 | 0 | 2 | 2 | | 2006 | 2 | 1 | 3 | | 2007 | 1 | 1 | 2 | | 2008 | 2 | 3 | 5 | | 2009 | 2 | 5 | 7 | | 2010 | 0 | 2 | 2 | | 2011 | 3 | 2 | 5 | | 2012 | 1 | 3 | 4 | | 2013 | 1 | 0 | 1 | | 2014 | 3 | 4 | 7 | | 2015 | 1 | 0 | 1 | | 2016 | 0 | 3 | 3 | | 2018 | 0 | 1 | 1 | | 2019 | 4 | 1 | 5 | | 2020 | 1 | 2 | 3 | | 2023 | 0 | 2 | 2 |
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Below are the most recent publications written about "Oxidoreductases" by people in Profiles.
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Mitchell ME, Gatzeva-Topalova PZ, Bargmann AD, Sammakia T, Sousa MC. Targeting the Conformational Change in ArnA Dehydrogenase for Selective Inhibition of Polymyxin Resistance. Biochemistry. 2023 07 18; 62(14):2216-2227.
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Kuatsjah E, Zahn M, Chen X, Kato R, Hinchen DJ, Konev MO, Katahira R, Orr C, Wagner A, Zou Y, Haugen SJ, Ramirez KJ, Michener JK, Pickford AR, Kamimura N, Masai E, Houk KN, McGeehan JE, Beckham GT. Biochemical and structural characterization of a sphingomonad diarylpropane lyase for cofactorless deformylation. Proc Natl Acad Sci U S A. 2023 01 24; 120(4):e2212246120.
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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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Hengel H, Bosso-Lef?vre C, Grady G, Szenker-Ravi E, Li H, Pierce S, Lebigot ?, Tan TT, Eio MY, Narayanan G, Utami KH, Yau M, Handal N, Deigendesch W, Keimer R, Marzouqa HM, Gunay-Aygun M, Muriello MJ, Verhelst H, Weckhuysen S, Mahida S, Naidu S, Thomas TG, Lim JY, Tan ES, Haye D, Willemsen MAAP, Oegema R, Mitchell WG, Pierson TM, Andrews MV, Willing MC, Rodan LH, Barakat TS, van Slegtenhorst M, Gavrilova RH, Martinelli D, Gilboa T, Tamim AM, Hashem MO, AlSayed MD, Abdulrahim MM, Al-Owain M, Awaji A, Mahmoud AAH, Faqeih EA, Asmari AA, Algain SM, Jad LA, Aldhalaan HM, Helbig I, Koolen DA, Riess A, Kraegeloh-Mann I, Bauer P, Gulsuner S, Stamberger H, Ng AYJ, Tang S, Tohari S, Keren B, Schultz-Rogers LE, Klee EW, Barresi S, Tartaglia M, Mor-Shaked H, Maddirevula S, Begtrup A, Telegrafi A, Pfundt R, Sch?le R, Ciruna B, Bonnard C, Pouladi MA, Stewart JC, Claridge-Chang A, Lefeber DJ, Alkuraya FS, Mathuru AS, Venkatesh B, Barycki JJ, Simpson MA, Jamuar SS, Sch?ls L, Reversade B. Loss-of-function mutations in UDP-Glucose 6-Dehydrogenase cause recessive developmental epileptic encephalopathy. Nat Commun. 2020 01 30; 11(1):595.
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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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