Results 241 to 250 of about 923,736 (263)
Some of the next articles are maybe not open access.
Adriamycin-catalyzed aerobic photooxidation of NAD dimers to NAD+
Biochimica et Biophysica Acta (BBA) - General Subjects, 1989The 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 ...
A. Finazzi Agrò +5 more
openaire +3 more sources
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
openaire +3 more sources
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
openaire +3 more sources
Science, 2004
Identified 15 years ago, the Wld mouse carries a spontaneous mutation that encodes a fusion protein with neuroprotective properties. In a Perspective, [Simon][1] discusses new work ([ Araki et al .][2]) that identifies the Nmnat1 fragment of the fusion protein as mediating neuroprotection by boosting NAD biosynthesis and increasing the activity of the ...
Antonio Bedalov, Julian A. Simon
openaire +2 more sources
Identified 15 years ago, the Wld mouse carries a spontaneous mutation that encodes a fusion protein with neuroprotective properties. In a Perspective, [Simon][1] discusses new work ([ Araki et al .][2]) that identifies the Nmnat1 fragment of the fusion protein as mediating neuroprotection by boosting NAD biosynthesis and increasing the activity of the ...
Antonio Bedalov, Julian A. Simon
openaire +2 more sources
Coordinate Conversion from Nad to Nad
Journal of Surveying Engineering, 1988A method for converting North American Datum (NAD) 27 coordinates to NAD 83 coordinates is presented. The method is tested on over 1,000 control points, known in both NAD 27 and NAD 83, obtained from the National Geodetic Survey. Input data are maintained as geodetic latitude and longitude to allow for nationwide application.
openaire +2 more sources
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 ...
Den'ichi Mizuno, Masahiko Iizuka
openaire +3 more sources
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 ...
Den'ichi Mizuno, Masahiko Iizuka
openaire +3 more sources
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.
Dianne K. Newman +4 more
openaire +4 more sources
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
openaire +3 more sources
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
openaire +3 more sources
The NAD Interactome, Identification of Putative New NAD-Binding Proteins
2022Nicotinamide 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
openaire +2 more sources
NAD-dependent inhibition of the NAD-glycohydrolase activity in A549 cells
Molecular and Cellular Biochemistry, 2002NAD glycohydrolases are enzymes that catalyze the hydrolysis of NAD to produce ADP-ribose and nicotinamide. Regulation of these enzymes has not been fully elucidated. We have identified a NAD-glycohydrolase activity associated with the outer surface of the plasma membrane in human lung epithelial cell line A549. This activity is negatively regulated by
Enrico Balducci, L.G. Micossi
openaire +3 more sources
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
openaire +3 more sources
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
openaire +3 more sources