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NAD+ and cardiovascular diseases

Clinica Chimica Acta, 2021
Nicotinamide adenine dinucleotide (NAD) plays pivotal roles in controlling many biochemical processes. 'NAD' refers to the chemical backbone irrespective of charge, whereas 'NAD+' and 'NADH' refers to oxidized and reduced forms, respectively. NAD+/NADH ratio is essential for maintaining cellular reduction-oxidation (redox) homeostasis and for ...
Qiuzhen, Lin   +4 more
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Adriamycin-catalyzed aerobic photooxidation of NAD dimers to NAD+

Biochimica et Biophysica Acta (BBA) - General Subjects, 1989
The photooxidation of the dimers of nicotinamide adenine dinucleotide, (NAD)2, is catalyzed by adriamycin under aerobic conditions. (NAD)2 and O2 react in 1:1 molar ratio to yield 2 mol of NAD+. Experiments carried out by irradiating at 340 and 485 nm, corresponding to the absorption maxima of (NAD)2 and adriamycin, respectively, clearly indicate that ...
V, Carelli   +5 more
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NAD on the rise again

Nature Metabolism, 2020
Maintaining cellular NAD levels through supplementation with intermediates of NAD synthesis has considerable health benefits. A new study demonstrates that the reduced form of nicotinamide riboside, NRH, can be converted to NAD in a biosynthetic pathway that involves adenosine kinase, thus strongly boosting NAD levels in cells and tissues.
Mathias Ziegler, Andrey A. Nikiforov
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Extraction and Measurement of NAD(P)+ and NAD(P)H

2014
Nicotinamide adenine dinucleotides are critical redox-active substrates for countless catabolic and anabolic reactions. Ratios of NAD(+) to NADH and NADP(+) to NADPH are therefore considered key indicators of the overall intracellular redox potential and metabolic state.
Kern, Suzanne E.   +2 more
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NAD+ kinase—A review

International Journal of Biochemistry, 1985
NAD+ kinase catalyzes the only (known) biochemical reaction leading to the production of NADP+ from NAD+. Most evidence indicates it is found in the cytoplasm, but reports of its presence in (other) cell bodies can not be discounted. Viewed as a protein, our knowledge of NADK composition and architecture is rudimentary.
E T, McGuinness, J R, Butler
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Turnover of NAD in bacteria

Biochimica et Biophysica Acta (BBA) - General Subjects, 1967
Abstract The turnover of NAD was investigated in 4 bacteria; strains with different requirements for niacin and niacinamide: the niacinamide type, Staphylococcus aureus 209P, which prefers niacinamide to niacin, and Lactobacillus fructosus 353, which strictly requires niacinamide; the niacin type, Leuconostoc mesenteroides IFO 3426, which ...
M, Iizuka, D, Mizuno
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Niacin, NAD and malformations

Archives of Disease in Childhood, 2017
It’s rare for a single paper to claim to have not only discovered a new mechanism for disease but also a means of preventing it. A paper from Sydney, Australia, which at first sight appears somewhat obscure and theoretical, does just that (Shi H et al. NEJM 2017. doi: 10.1056/NEJMoa1616361). It combines genetic studies on four families with mouse model
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NAD+ Availability and Proteotoxicity

NeuroMolecular Medicine, 2009
It has been shown that NAD(+) availability is important for neuronal survival following ischemia (Liu et al., Neuromolecular Med 11:28-42, 2009). It is proposed here that NAD(+) may also control proteotoxicity by influencing both formation and catabolism of altered proteins.
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Evolving concepts in NAD+ metabolism

Cell Metabolism, 2021
Eduardo N. Chini   +2 more
exaly  

NAD+ Boosting Strategies

Nicotinamide adenine dinucleotide (oxidized form, NAD+) serves as a co-substrate and co-enzyme in cells to execute its key roles in cell signalling pathways and energetic metabolism, arbitrating cell survival and death. It was discovered in 1906 by Arthur Harden and William John Young in yeast extract which could accelerate alcohol fermentation.
Jared, Rice   +2 more
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