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.
To see the data from this visualization as text, click here.
Year | Major Topic | Minor Topic | Total |
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1983 | 1 | 0 | 1 | 1993 | 1 | 0 | 1 | 1994 | 0 | 1 | 1 | 2000 | 0 | 1 | 1 | 2001 | 0 | 2 | 2 | 2002 | 3 | 1 | 4 | 2003 | 1 | 0 | 1 | 2004 | 1 | 1 | 2 | 2005 | 1 | 1 | 2 | 2007 | 1 | 1 | 2 | 2008 | 2 | 0 | 2 | 2009 | 0 | 3 | 3 | 2010 | 1 | 0 | 1 | 2011 | 2 | 0 | 2 | 2012 | 0 | 1 | 1 | 2013 | 1 | 0 | 1 | 2014 | 2 | 0 | 2 | 2015 | 0 | 2 | 2 | 2017 | 1 | 0 | 1 |
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Below are the most recent publications written about "Oxidoreductases" by people in Profiles.
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Lin DL, Cherepanova NA, Bozzacco L, MacDonald MR, Gilmore R, Tai AW. Dengue Virus Hijacks a Noncanonical Oxidoreductase Function of a Cellular Oligosaccharyltransferase Complex. MBio. 2017 Jul 18; 8(4).
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Nyberg M, Heidorn T, Lindblad P. Hydrogen production by the engineered cyanobacterial strain Nostoc PCC 7120 ?hupW examined in a flat panel photobioreactor system. J Biotechnol. 2015 Dec 10; 215:35-43.
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Nambi S, Long JE, Mishra BB, Baker R, Murphy KC, Olive AJ, Nguyen HP, Shaffer SA, Sassetti CM. The Oxidative Stress Network of Mycobacterium tuberculosis Reveals Coordination between Radical Detoxification Systems. Cell Host Microbe. 2015 Jun 10; 17(6):829-37.
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Cherepanova NA, Shrimal S, Gilmore R. Oxidoreductase activity is necessary for N-glycosylation of cysteine-proximal acceptor sites in glycoproteins. J Cell Biol. 2014 Aug 18; 206(4):525-39.
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Sheng Y, Abreu IA, Cabelli DE, Maroney MJ, Miller AF, Teixeira M, Valentine JS. Superoxide dismutases and superoxide reductases. Chem Rev. 2014 Apr 9; 114(7):3854-918.
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Abdeen SK, Del Mare S, Hussain S, Abu-Remaileh M, Salah Z, Hagan J, Rawahneh M, Pu XA, Russell S, Stein JL, Stein GS, Lian JB, Aqeilan RI. Conditional inactivation of the mouse Wwox tumor suppressor gene recapitulates the null phenotype. J Cell Physiol. 2013 Jul; 228(7):1377-82.
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Bouchecareilh M, Hutt DM, Szajner P, Flotte TR, Balch WE. Histone deacetylase inhibitor (HDACi) suberoylanilide hydroxamic acid (SAHA)-mediated correction of a1-antitrypsin deficiency. J Biol Chem. 2012 Nov 2; 287(45):38265-78.
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Lindberg P, Devine E, Stensjö K, Lindblad P. HupW protease specifically required for processing of the catalytic subunit of the uptake hydrogenase in the cyanobacterium Nostoc sp. strain PCC 7120. Appl Environ Microbiol. 2012 Jan; 78(1):273-6.
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Camsund D, Devine E, Holmqvist M, Yohanoun P, Lindblad P, Stensjö K. A HupS-GFP fusion protein demonstrates a heterocyst-specific localization of the uptake hydrogenase in Nostoc punctiforme. FEMS Microbiol Lett. 2011 Mar; 316(2):152-9.
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Kurek KC, Del Mare S, Salah Z, Abdeen S, Sadiq H, Lee SH, Gaudio E, Zanesi N, Jones KB, DeYoung B, Amir G, Gebhardt M, Warman M, Stein GS, Stein JL, Lian JB, Aqeilan RI. Frequent attenuation of the WWOX tumor suppressor in osteosarcoma is associated with increased tumorigenicity and aberrant RUNX2 expression. Cancer Res. 2010 Jul 1; 70(13):5577-86.
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