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
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| MeSH Number(s) |
D08.811.682.608
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| 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.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2001 | 3 | 0 | 3 |
| 2003 | 0 | 2 | 2 |
| 2005 | 1 | 1 | 2 |
| 2008 | 1 | 0 | 1 |
| 2009 | 0 | 2 | 2 |
| 2018 | 1 | 0 | 1 |
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Below are the most recent publications written about "NADH, NADPH Oxidoreductases" by people in Profiles.
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Rodriguez F, Iniguez E, Pena Contreras G, Ahmed H, Costa TEMM, Skouta R, Maldonado RA. Development of Thiophene Compounds as Potent Chemotherapies for the Treatment of Cutaneous Leishmaniasis Caused by Leishmania major. Molecules. 2018 07 04; 23(7).
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Ogungbe IV, Setzer WN. Comparative molecular docking of antitrypanosomal natural products into multiple Trypanosoma brucei drug targets. Molecules. 2009 Apr 14; 14(4):1513-36.
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Riebe O, Fischer RJ, Wampler DA, Kurtz DM, Bahl H. Pathway for H2O2 and O2 detoxification in Clostridium acetobutylicum. Microbiology (Reading). 2009 Jan; 155(Pt 1):16-24.
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Hillmann F, Riebe O, Fischer RJ, Mot A, Caranto JD, Kurtz DM, Bahl H. Reductive dioxygen scavenging by flavo-diiron proteins of Clostridium acetobutylicum. FEBS Lett. 2009 Jan 05; 583(1):241-5.
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Silaghi-Dumitrescu R, Kurtz DM, Ljungdahl LG, Lanzilotta WN. X-ray crystal structures of Moorella thermoacetica FprA. Novel diiron site structure and mechanistic insights into a scavenging nitric oxide reductase. Biochemistry. 2005 May 03; 44(17):6492-501.
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Mittal MK, Misra S, Owais M, Goyal N. Expression, purification, and characterization of Leishmania donovani trypanothione reductase in Escherichia coli. Protein Expr Purif. 2005 Apr; 40(2):279-86.
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Suzuki Y, Yoshimaru T, Matsui T, Inoue T, Niide O, Nunomura S, Ra C. Fc epsilon RI signaling of mast cells activates intracellular production of hydrogen peroxide: role in the regulation of calcium signals. J Immunol. 2003 Dec 01; 171(11):6119-27.
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Silaghi-Dumitrescu R, Coulter ED, Das A, Ljungdahl LG, Jameson GN, Huynh BH, Kurtz DM. A flavodiiron protein and high molecular weight rubredoxin from Moorella thermoacetica with nitric oxide reductase activity. Biochemistry. 2003 Mar 18; 42(10):2806-15.
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Coulter ED, Kurtz DM. A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: catalytic electron transfer to rubrerythrin and two-iron superoxide reductase. Arch Biochem Biophys. 2001 Oct 01; 394(1):76-86.
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Das A, Coulter ED, Kurtz DM, Ljungdahl LG. Five-gene cluster in Clostridium thermoaceticum consisting of two divergent operons encoding rubredoxin oxidoreductase- rubredoxin and rubrerythrin-type A flavoprotein- high-molecular-weight rubredoxin. J Bacteriol. 2001 Mar; 183(5):1560-7.