 Quinone Reductases
"Quinone Reductases" 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.
NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.
| Descriptor ID |
D011808
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| MeSH Number(s) |
D08.811.682.608.800
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| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Quinone Reductases".
Below are MeSH descriptors whose meaning is more specific than "Quinone Reductases".
This graph shows the total number of publications written about "Quinone Reductases" by people in this website by year, and whether "Quinone Reductases" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
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| 2004 | 1 | 0 | 1 | | 2007 | 1 | 0 | 1 | | 2011 | 2 | 1 | 3 | | 2013 | 0 | 1 | 1 | | 2014 | 1 | 0 | 1 | | 2020 | 1 | 0 | 1 |
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Below are the most recent publications written about "Quinone Reductases" by people in Profiles.
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Friederich MW, Elias AF, Kuster A, Laugwitz L, Larson AA, Landry AP, Ellwood-Digel L, Mirsky DM, Dimmock D, Haven J, Jiang H, MacLean KN, Styren K, Schoof J, Goujon L, Lefrancois T, Friederich M, Coughlin CR, Banerjee R, Haack TB, Van Hove JLK. Pathogenic variants in SQOR encoding sulfide:quinone oxidoreductase are a potentially treatable cause of Leigh disease. J Inherit Metab Dis. 2020 09; 43(5):1024-1036.
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Rudolph J, Erbse AH, Behlen LS, Copley SD. A radical intermediate in the conversion of pentachlorophenol to tetrachlorohydroquinone by Sphingobium chlorophenolicum. Biochemistry. 2014 Oct 21; 53(41):6539-49.
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Yadid I, Rudolph J, Hlouchova K, Copley SD. Sequestration of a highly reactive intermediate in an evolving pathway for degradation of pentachlorophenol. Proc Natl Acad Sci U S A. 2013 Jun 11; 110(24):E2182-90.
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Copley SD, Rokicki J, Turner P, Daligault H, Nolan M, Land M. The whole genome sequence of Sphingobium chlorophenolicum L-1: insights into the evolution of the pentachlorophenol degradation pathway. Genome Biol Evol. 2012; 4(2):184-98.
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Yan C, Dufour M, Siegel D, Reigan P, Gomez J, Shieh B, Moody CJ, Ross D. Indolequinone inhibitors of NRH:quinone oxidoreductase 2. Characterization of the mechanism of inhibition in both cell-free and cellular systems. Biochemistry. 2011 Aug 09; 50(31):6678-88.
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Dufour M, Yan C, Siegel D, Colucci MA, Jenner M, Oldham NJ, Gomez J, Reigan P, Li Y, De Matteis CI, Ross D, Moody CJ. Mechanism-based inhibition of quinone reductase 2 (NQO2): selectivity for NQO2 over NQO1 and structural basis for flavoprotein inhibition. Chembiochem. 2011 May 16; 12(8):1203-8.
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Yan C, Kepa JK, Siegel D, Stratford IJ, Ross D. Dissecting the role of multiple reductases in bioactivation and cytotoxicity of the antitumor agent 2,5-diaziridinyl-3-(hydroxymethyl)-6-methyl-1,4-benzoquinone (RH1). Mol Pharmacol. 2008 Dec; 74(6):1657-65.
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Zheng S, Byrd AS, Fischer BM, Grover AR, Ghio AJ, Voynow JA. Regulation of MUC5AC expression by NAD(P)H:quinone oxidoreductase 1. Free Radic Biol Med. 2007 May 01; 42(9):1398-408.
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Ross D. Quinone reductases multitasking in the metabolic world. Drug Metab Rev. 2004 Oct; 36(3-4):639-54.
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Kwiek JJ, Haystead TA, Rudolph J. Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines. Biochemistry. 2004 Apr 20; 43(15):4538-47.
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