Results 251 to 260 of about 923,736 (263)

Subcellular NAD+ pools are interconnected and buffered by mitochondrial NAD+

Nature Metabolism
The 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, Magali R. VanLinden, Marc Niere, Øyvind Strømland, Suraj Sharma, Jörn Dietze, Ingvill Tolås, Eva Lucena, Ersilia Bifulco, Lars J. Sverkeli, Camila Cimadamore-Werthein, Hanan Ashrafi, Kjellfrid F. Haukanes, Barbara van der Hoeven, Christian Dölle, Cédric Davidsen, Ina K. N. Pettersen, Karl J. Tronstad, Svein A. Mjøs, Faisal Hayat, Mikhail V. Makarov, Marie E. Migaud, Ines Heiland, Mathias Ziegler   +23 more
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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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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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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, Maurice Comtat, Jean Cantet   +2 more
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Studia nad Bezpieczeństwem

2016
Nr 2 (2017): Studia nad ...
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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, Satoshi Ushida, Yuji Ishihara, Masanori Kashiwagi, Atsuyoshi Ohno   +4 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, Elena Katsyuba, Dina Hofer, Dina Hofer, Johan Auwerx   +4 more
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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, Kenneth G. Mandel, Donald Lombardi, Harold Amos   +3 more
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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, Sofie, Lautrup, Evandro F, Fang   +2 more
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Immobilization of NAD Kinase

Annals of the New York Academy of Sciences, 1984
Xinsong Ji, Zhong Yi Yuan, Huixian Li, Shuhuang Liu   +3 more
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