Results 91 to 100 of about 18,302 (116)
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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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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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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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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
2014Nicotinamide 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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Subcellular NAD+ pools are interconnected and buffered by mitochondrial NAD+
Nature MetabolismThe coenzyme NAD+ is consumed by signalling enzymes, including poly-ADP-ribosyltransferases (PARPs) and sirtuins. Ageing is associated with a decrease in cellular NAD+ levels, but how cells cope with persistently decreased NAD+ concentrations is unclear.
Lena E. Høyland +23 more
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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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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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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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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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NAD+ Availability and Proteotoxicity
NeuroMolecular Medicine, 2009It 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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