 NAD
"NAD" 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 coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
| Descriptor ID |
D009243
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| MeSH Number(s) |
D03.438.759.646.138.694 D08.211.589 D13.695.667.138.694 D13.695.827.068.694
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| Concept/Terms |
NAD- NAD
- Dihydronicotinamide Adenine Dinucleotide
- Adenine Dinucleotide, Dihydronicotinamide
- Dinucleotide, Dihydronicotinamide Adenine
- Nadide
- DPN
- Nicotinamide-Adenine Dinucleotide
- Dinucleotide, Nicotinamide-Adenine
- Nicotinamide Adenine Dinucleotide
- Coenzyme I
- Diphosphopyridine Nucleotide
- Nucleotide, Diphosphopyridine
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Below are MeSH descriptors whose meaning is more general than "NAD".
Below are MeSH descriptors whose meaning is more specific than "NAD".
This graph shows the total number of publications written about "NAD" by people in this website by year, and whether "NAD" 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 |
|---|
| 1980 | 0 | 1 | 1 | | 1985 | 0 | 1 | 1 | | 1990 | 0 | 1 | 1 | | 1993 | 0 | 1 | 1 | | 2002 | 0 | 1 | 1 | | 2004 | 1 | 1 | 2 | | 2006 | 1 | 0 | 1 | | 2008 | 0 | 1 | 1 | | 2009 | 1 | 0 | 1 | | 2012 | 1 | 1 | 2 | | 2015 | 0 | 1 | 1 | | 2017 | 0 | 1 | 1 |
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Below are the most recent publications written about "NAD" by people in Profiles.
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Yang L, Bose S, Ngo AH, Do LH. Innocent But Deadly: Nontoxic Organoiridium Catalysts Promote Selective Cancer Cell Death. ChemMedChem. 2017 Feb 20; 12(4):292-299.
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Makowska-Grzyska M, Kim Y, Gorla SK, Wei Y, Mandapati K, Zhang M, Maltseva N, Modi G, Boshoff HI, Gu M, Aldrich C, Cuny GD, Hedstrom L, Joachimiak A. Mycobacterium tuberculosis IMPDH in Complexes with Substrates, Products and Antitubercular Compounds. PLoS One. 2015; 10(10):e0138976.
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Nicholls C, Pinto AR, Li H, Li L, Wang L, Simpson R, Liu JP. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) induces cancer cell senescence by interacting with telomerase RNA component. Proc Natl Acad Sci U S A. 2012 Aug 14; 109(33):13308-13.
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Cohen BW, Polyansky DE, Achord P, Cabelli D, Muckerman JT, Tanaka K, Thummel RP, Zong R, Fujita E. Steric effect for proton, hydrogen-atom, and hydride transfer reactions with geometric isomers of NADH-model ruthenium complexes. Faraday Discuss. 2012; 155:129-44; discussion 207-22.
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Khoury GA, Fazelinia H, Chin JW, Pantazes RJ, Cirino PC, Maranas CD. Computational design of Candida boidinii xylose reductase for altered cofactor specificity. Protein Sci. 2009 Oct; 18(10):2125-38.
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Ampapathi RS, Creath AL, Lou DI, Craft JW, Blanke SR, Legge GB. Order-disorder-order transitions mediate the activation of cholera toxin. J Mol Biol. 2008 Mar 28; 377(3):748-60.
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Shen W, Wei Y, Dauk M, Tan Y, Taylor DC, Selvaraj G, Zou J. Involvement of a glycerol-3-phosphate dehydrogenase in modulating the NADH/NAD+ ratio provides evidence of a mitochondrial glycerol-3-phosphate shuttle in Arabidopsis. Plant Cell. 2006 Feb; 18(2):422-41.
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Russell TR, Tu SC. Aminobacter aminovorans NADH:flavin oxidoreductase His140: a highly conserved residue critical for NADH binding and utilization. Biochemistry. 2004 Oct 12; 43(40):12887-93.
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Russell TR, Demeler B, Tu SC. Kinetic mechanism and quaternary structure of Aminobacter aminovorans NADH:flavin oxidoreductase: an unusual flavin reductase with bound flavin. Biochemistry. 2004 Feb 17; 43(6):1580-90.
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Mîinea C, Kuruvilla R, Merrikh H, Eichberg J. Altered arachidonic acid biosynthesis and antioxidant protection mechanisms in Schwann cells grown in elevated glucose. J Neurochem. 2002 Jun; 81(6):1253-62.
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