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.

MeSH information

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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
MeSH Number(s)	D08.811.682
Concept/Terms	Oxidoreductases Oxidoreductases Reductases Reductase Dehydrogenase Dehydrogenases Oxidase Oxidase Oxidases

Below are MeSH descriptors whose meaning is more general than "Oxidoreductases".

Chemicals and Drugs [D]
Enzymes and Coenzymes [D08]
Enzymes [D08.811]
Oxidoreductases [D08.811.682]

Below are MeSH descriptors whose meaning is related to "Oxidoreductases".

publications

Timeline | Most Recent

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.

Bar chart showing 79 publications over 27 distinct years, with a maximum of 10 publications in 2006

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
1994	1	0	1
1995	1	0	1
1996	3	1	4
1997	1	1	2
1998	3	0	3
1999	0	1	1
2000	0	2	2
2001	1	3	4
2002	4	0	4
2003	6	0	6
2004	4	2	6
2005	7	0	7
2006	10	0	10
2007	7	0	7
2008	0	1	1
2009	0	1	1
2010	1	1	2
2011	0	1	1
2012	3	0	3
2013	1	1	2
2014	2	1	3
2015	1	0	1
2017	1	1	2
2018	0	1	1
2019	0	1	1
2020	2	0	2
2021	0	1	1

Below are the most recent publications written about "Oxidoreductases" by people in Profiles.

Shi K, Radhakrishnan M, Dai X, Rosen BP, Wang G. NemA Catalyzes Trivalent Organoarsenical Oxidation and Is Regulated by the Trivalent Organoarsenical-Selective Transcriptional Repressor NemR. Environ Sci Technol. 2021 05 04; 55(9):6485-6494.

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Bell A, Severi E, Lee M, Monaco S, Latousakis D, Angulo J, Thomas GH, Naismith JH, Juge N. Uncovering a novel molecular mechanism for scavenging sialic acids in bacteria. J Biol Chem. 2020 10 02; 295(40):13724-13736.

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Mondal A, Singh SK, Manna T, Husain SM. Chemoenzymatic, biomimetic total synthesis of (-)-rugulosin B, C and rugulin analogues and their biosynthetic implications. Chem Commun (Camb). 2020 Mar 17; 56(22):3337-3340.

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Kallianpur KJ, Walker M, Gerschenson M, Shikuma CM, Gangcuangco LMA, Kohorn L, Libutti DE, Nir TM, Jahanshad N, Thompson PM, Paul R. Systemic Mitochondrial Oxidative Phosphorylation Protein Levels Correlate with Neuroimaging Measures in Chronically HIV-Infected Individuals. AIDS Res Hum Retroviruses. 2020 01; 36(1):83-91.

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Saha N, Mondal A, Witte K, Singh SK, Müller M, Husain SM. Monomeric Dihydroanthraquinones: A Chemoenzymatic Approach and its (Bio)synthetic Implications for Bisanthraquinones. Chemistry. 2018 Jan 26; 24(6):1283-1286.

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Abanda NN, Djieugoué JY, Lim E, Pefura-Yone EW, Mbacham WF, Vernet G, Penlap VM, Eyangoh SI, Taylor DW, Leke RGF. Diagnostic accuracy and usefulness of the Genotype MTBDRplus assay in diagnosing multidrug-resistant tuberculosis in Cameroon? a cross-sectional study. BMC Infect Dis. 2017 05 31; 17(1):379.

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So CR, Scancella JM, Fears KP, Essock-Burns T, Haynes SE, Leary DH, Diana Z, Wang C, North S, Oh CS, Wang Z, Orihuela B, Rittschof D, Spillmann CM, Wahl KJ. Oxidase Activity of the Barnacle Adhesive Interface Involves Peroxide-Dependent Catechol Oxidase and Lysyl Oxidase Enzymes. ACS Appl Mater Interfaces. 2017 Apr 05; 9(13):11493-11505.

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Chen J, Bhattacharjee H, Rosen BP. ArsH is an organoarsenical oxidase that confers resistance to trivalent forms of the herbicide monosodium methylarsenate and the poultry growth promoter roxarsone. Mol Microbiol. 2015 Jun; 96(5):1042-52.

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Tsuji Y, Vanholme R, Tobimatsu Y, Ishikawa Y, Foster CE, Kamimura N, Hishiyama S, Hashimoto S, Shino A, Hara H, Sato-Izawa K, Oyarce P, Goeminne G, Morreel K, Kikuchi J, Takano T, Fukuda M, Katayama Y, Boerjan W, Ralph J, Masai E, Kajita S. Introduction of chemically labile substructures into Arabidopsis lignin through the use of LigD, the Ca-dehydrogenase from Sphingobium sp. strain SYK-6. Plant Biotechnol J. 2015 Aug; 13(6):821-32.

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Quintana AM, Geiger EA, Achilly N, Rosenblatt DS, Maclean KN, Stabler SP, Artinger KB, Appel B, Shaikh TH. Hcfc1b, a zebrafish ortholog of HCFC1, regulates craniofacial development by modulating mmachc expression. Dev Biol. 2014 Dec 01; 396(1):94-106.

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