NADH, NADPH Oxidoreductases
"NADH, NADPH 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.
A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
| Descriptor ID |
D009247
|
| MeSH Number(s) |
D08.811.682.608
|
| Concept/Terms |
NADH, NADPH Oxidoreductases- NADH, NADPH Oxidoreductases
- NADPH Oxidoreductases NADH
- Oxidoreductases NADH, NADPH
- Oxidoreductases, NADH, NADPH
|
Below are MeSH descriptors whose meaning is more general than "NADH, NADPH Oxidoreductases".
Below are MeSH descriptors whose meaning is more specific than "NADH, NADPH Oxidoreductases".
This graph shows the total number of publications written about "NADH, NADPH Oxidoreductases" by people in this website by year, and whether "NADH, NADPH 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 |
|---|
| 1996 | 1 | 0 | 1 |
| 2002 | 1 | 1 | 2 |
| 2003 | 0 | 1 | 1 |
| 2007 | 1 | 0 | 1 |
| 2020 | 0 | 1 | 1 |
To return to the timeline,
click here.
Below are the most recent publications written about "NADH, NADPH Oxidoreductases" by people in Profiles.
-
Goodman RP, Markhard AL, Shah H, Sharma R, Skinner OS, Clish CB, Deik A, Patgiri A, Hsu YH, Masia R, Noh HL, Suk S, Goldberger O, Hirschhorn JN, Yellen G, Kim JK, Mootha VK. Hepatic NADH reductive stress underlies common variation in metabolic traits. Nature. 2020 07; 583(7814):122-126.
-
Nelson EJ, Tanudra A, Chowdhury A, Kane AV, Qadri F, Calderwood SB, Coburn J, Camilli A. High prevalence of spirochetosis in cholera patients, Bangladesh. Emerg Infect Dis. 2009 Apr; 15(4):571-3.
-
Eun YJ, Kurt N, Sekhar A, Cavagnero S. Thermodynamic and kinetic characterization of apoHmpH, a fast-folding bacterial globin. J Mol Biol. 2008 Feb 22; 376(3):879-97.
-
Tam NN, Leav I, Ho SM. Sex hormones induce direct epithelial and inflammation-mediated oxidative/nitrosative stress that favors prostatic carcinogenesis in the noble rat. Am J Pathol. 2007 Oct; 171(4):1334-41.
-
Wendt MC, Daiber A, Kleschyov AL, M?lsch A, Sydow K, Schulz E, Chen K, Keaney JF, Lass?gue B, Walter U, Griendling KK, M?nzel T. Differential effects of diabetes on the expression of the gp91phox homologues nox1 and nox4. Free Radic Biol Med. 2005 Aug 01; 39(3):381-91.
-
Cooke G, Duclairoir FM, John P, Polwart N, Rotello VM. Model systems for flavoenzyme activity: flavin-functionalised SAMs as models for probing redox modulation through hydrogen bonding. Chem Commun (Camb). 2003 Oct 07; (19):2468-9.
-
Jung C, Higgins CM, Xu Z. Mitochondrial electron transport chain complex dysfunction in a transgenic mouse model for amyotrophic lateral sclerosis. J Neurochem. 2002 Nov; 83(3):535-45.
-
Seo BB, Nakamaru-Ogiso E, Flotte TR, Yagi T, Matsuno-Yagi A. A single-subunit NADH-quinone oxidoreductase renders resistance to mammalian nerve cells against complex I inhibition. Mol Ther. 2002 Sep; 6(3):336-41.
-
Scheffler IE, Yadava N. Molecular genetics of the mammalian NADH-ubiquinone oxidoreductase. J Bioenerg Biomembr. 2001 Jun; 33(3):243-50.
-
Niemz A, Rotello VM. Model systems for flavoenzyme activity. The effects of specific hydrogen bonds on the 13C and 1H NMR of flavins. J Mol Recognit. 1996 Mar-Apr; 9(2):158-62.