Results 121 to 130 of about 192,695 (172)
Some of the next articles are maybe not open access.
NAD+-pyridoxine and NAD+-pyridoxamine complexes
Biochimica et Biophysica Acta (BBA) - General Subjects, 1971Abstract 1. 1. NAD+-pyridoxamine complexes were studied by fluorescence techniques at 30° over a pH range of 8.4–10.0. 2. 2. The polarization factor was seen to increase with increasing NAD+ concentration in all cases. 3. 3. Fluorescence quenching studis established large complex formation constants for both complexes. 4. 4.
V.D. Anand, W.R. Carper
openaire +1 more source
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
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 +1 more source
NAD+ and cardiovascular diseases
Clinica Chimica Acta, 2021Nicotinamide 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
openaire +2 more sources
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 ...
V, Carelli +5 more
openaire +2 more sources
Evidence for binding of NAD dimers to NAD-dependent dehydrogenases
Biochimica et Biophysica Acta (BBA) - Enzymology, 1981The binding of dimers of nicotinamide adenine dinucleotide, (NAD)2, to lactate, malate and alcohol dehydrogenase has been studied by the fluorescence quenching technique. While the alcohol dehydrogenase shows a low binding ability, malate and lactate dehydrogenases have been found to bind (NAD)2 in a specific way with high affinity.
FINAZZI AGRÒ A. +4 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 +2 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 +2 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.
Kern, Suzanne E. +2 more
openaire +3 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.
E T, McGuinness, J R, Butler
openaire +2 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.
E T, McGuinness, J R, Butler
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 ...
M, Iizuka, D, Mizuno
openaire +2 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 ...
M, Iizuka, D, Mizuno
openaire +2 more sources