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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.
James R. Butler, Eugene T. McGuinness
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The NAD Interactome, Identification of Putative New NAD-Binding Proteins

2022
Nicotinamide adenine dinucleotide (NAD) is an essential metabolite in normal cellular physiology and its deregulation may lead to several pathological conditions. NAD interacts with a vast number of proteins, acting as a coenzyme, as a substrate and regulating the interaction between proteins.
Sara Duarte-Pereira   +3 more
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Binding of NAD and NADP dimers to NAD- and NADP-dependent dehydrogenases

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
Interaction of the electrolytically prepared dimers of nicotinamide adenine nucleotide, (NAD)2, and nicotinamide adenine nucleotide phosphate, (NADP)2, with lactate, alcohol, glyceraldehyde 3-phosphate, alpha-glycerophosphate, glutamate and glucose-6-phosphate dehydrogenase has been studied using the quenching of protein fluorescence, kinetics of ...
H. Klukanová, J. Kovár
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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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Bioelectrocatalysis of NAD+ reduction

Journal of Electroanalytical Chemistry, 1992
Abstract A thermokinetic approach to the catalysis of the electrochemical reduction of NAD + by the hydrogenase of Alcaligenes eutrophus H16 is presented. The influence of temperature is weak, with an activation energy of 18 kJ/mol, whereas classical NAD + hydrogenation with gaseous hydrogen shows an activation energy of 34 kJ/mol.
Alain Bergel   +2 more
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NAD+ homeostasis in health and disease

Nature Metabolism, 2020
The conceptual evolution of nicotinamide adenine dinucleotide (NAD+) from being seen as a simple metabolic cofactor to a pivotal cosubstrate for proteins regulating metabolism and longevity, including the sirtuin family of protein deacylases, has led to a new wave of scientific interest in NAD+. NAD+ levels decline during ageing, and alterations in NAD+
Mario Romani   +4 more
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Nad(P)+-nad(p)h models. 57

Tetrahedron, 1986
Abstract NAD(P)H/NAD(P) + and related compounds have intrinsic chirality against the axis alone the C 3 –C carbonyl single bond. A model compound which has a stable conformation with respect to this chirality was synthesized and the conformational relationship between the carbonyl dipole and the reacting hydrogen was studied.
Shinzaburo Oka   +4 more
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Studia nad Bezpieczeństwem

2016
Nr 2 (2017): Studia nad ...
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Reactivation of NAD(H) biosynthetic pathway by exogenous NAD+ in nil cells severely depleted of NAD(H)

Journal of Cellular Physiology, 1983
AbstractThe culture of Nil hamster fibroblasts in MEM lacking nicotinamide (NAm− MEM) leads to: (1) the rapid loss of intracellular total nicotinamide adenine dinucleotide (NAD(H)) content in these cells from a level of 150–200 pmoles/105 cells to less than 20 pmoles/105 cells; (2) the cessation of cell division and inhibition of DNA synthesis; and (3)
Mary K. Lively   +3 more
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