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1

Sadia, Ashraf, Dixit S., W. Ramteke Pramod, and Z. Rizvi Ahsan. "Interactive Role of Brassinosteroids and Calcium Ameliorates in Response to the Aluminium Toxicity in Plants." International Journal of Trend in Scientific Research and Development 3, no. 6 (2019): 183–203. https://doi.org/10.5281/zenodo.3589673.

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Aluminum toxicity is considered one of the major growth limiting factors for crop production on acid soils worldwide, and pose a major challenge to agriculture sustainability. At low pH, the most toxic form of Al 3 is released into the soil and causes extensive damage to plants, especially in the root. To develop high tolerance against Al toxicity is the prime concern of plant science. Research has reported that the Brassinosteroids play a diverse role in plant growth, development and stress response. Although the BRs have been exhaustively studied, a comprehensive overview of the manner in wh
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2

AMAO, YUTAKA, TOSHIAKI KAMACHI, and ICHIRO OKURA. "Photoinduced Hydrogen Evolution with Hydrogenase and Water-soluble Viologen-linked Zinc Porphyrins." Journal of Porphyrins and Phthalocyanines 02, no. 03 (1998): 201–7. http://dx.doi.org/10.1002/(sici)1099-1409(199805/06)2:3<201::aid-jpp64>3.0.co;2-x.

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A series of water-soluble viologen-linked zinc porphyrins with different methylene chain lengths (n = 3−6) between porphyrin and viologen, ZnP ( C n V )4, were synthesized and characterized. The intra- molecular electron transfer rate constants from the porphyrin moiety of ZnP (Cn V )4 to viologen were measured by using fluorescence lifetime and laser flash photolysis. Both the photoexcited singlet state and the triplet state of the porphyrin were quenched by the bonded viologen. These compounds were applied to photoinduced hydrogen evolution in the system containing nicotinamide-adenine dinuc
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3

Cassatella, M. A., L. Hartman, B. Perussia, and G. Trinchieri. "Tumor necrosis factor and immune interferon synergistically induce cytochrome b-245 heavy-chain gene expression and nicotinamide-adenine dinucleotide phosphate hydrogenase oxidase in human leukemic myeloid cells." Journal of Clinical Investigation 83, no. 5 (1989): 1570–79. http://dx.doi.org/10.1172/jci114054.

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4

Frederick, David W., Sophie Trefely, Alexia Buas, et al. "Stable isotope labeling by essential nutrients in cell culture (SILEC) for accurate measurement of nicotinamide adenine dinucleotide metabolism." Analyst 142, no. 23 (2017): 4431–37. http://dx.doi.org/10.1039/c7an01378g.

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Nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP) are conserved metabolic cofactors that mediate reduction-oxidation (redox) reactions throughout all domains of life.
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5

Alberty, R. A. "Thermodynamics of Reactions of Nicotinamide Adenine Dinucleotide and Nicotinamide Adenine Dinucleotide Phosphate." Archives of Biochemistry and Biophysics 307, no. 1 (1993): 8–14. http://dx.doi.org/10.1006/abbi.1993.1552.

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6

Lee, H. J., and G. G. Chang. "Interactions of nicotinamide-adenine dinucleotide phosphate analogues and fragments with pigeon liver malic enzyme. Synergistic effect between the nicotinamide and adenine moieties." Biochemical Journal 245, no. 2 (1987): 407–14. http://dx.doi.org/10.1042/bj2450407.

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The structural requirements of the NADP+ molecule as a coenzyme in the oxidative decarboxylation reaction catalysed by pigeon liver malic enzyme were studied by kinetic and fluorimetric analyses with various NADP+ analogues and fragments. The substrate L-malate had little effect on the nucleotide binding. Etheno-NADP+, 3-acetylpyridine-adenine dinucleotide phosphate, and nicotinamide-hypoxanthine dinucleotide phosphate act as alternative coenzymes for the enzyme. Their kinetic parameters were similar to that of NADP+. Thionicotinamide-adenine dinucleotide phosphate, 3-aminopyridine-adenine din
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7

Popova, Olga, Daria Bylinskaya, Anastasia Nikitina та Olga Ukrainskaya. "The role of nicotinamide-β-adenine dinucleotide phosphate-H-cytochrome P450 oxidoreductase in the activation of cytochromes". BIO Web of Conferences 181 (2025): 01027. https://doi.org/10.1051/bioconf/202518101027.

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The aim of this theoretical study is to investigate the mechanisms of action of these enzymes in the context of metabolism in highly productive animals. The relevance is due to the active development of agriculture and increased interest in a detailed study of the cytochrome P450 system for obtaining high-quality livestock products. This work highlights the functional significance of the enzyme Nicotinamide-β- adenine dinucleotide phosphate-H-cytochrome P450 oxidoreductase in the processes of activation of cytochromes P450. An analysis of existing data on the interaction of Nicotinamide-β-aden
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8

Kova´rˇ, J., J. Tura´nek, C. Hlava´cˇ, V. Vala, and V. Kahle. "Liquid chromatographic separations of dimers of nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate." Journal of Chromatography A 319 (January 1985): 341–49. http://dx.doi.org/10.1016/s0021-9673(01)90570-9.

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9

Arsić, Biljana. "Mechanisms of actions of coenzymes." Chemia Naissensis 1, no. 1 (2018): 153–86. http://dx.doi.org/10.46793/chemn1.1.153a.

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Each living species uses coenzymes in numerous important reactions catalyzed by enzymes. There are two types of coenzymes depending on the interaction with apoenzymes: coenzymes frequently called co-substrates and coenzymes known as prosthetic groups. Main metabolic roles of co-substrates (adenosine triphosphate (ATP), S-adenosyl methionine, uridine diphosphate glucose, nicotinamide adenine dinucleotide (NAD+) and nicotinamide adenine dinucleotide phosphate (NADP+), coenzyme A (CoA), tetrahydrofolate and ubiquinone (Q)) and prosthetic groups (flavin mononucleotide (FMN) and flavin adenine dinu
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10

Mohelnikova-Duchonova, Beatrice, Lenka Marsakova, David Vrana, et al. "Superoxide Dismutase and Nicotinamide Adenine Dinucleotide Phosphate." Pancreas 40, no. 1 (2011): 72–78. http://dx.doi.org/10.1097/mpa.0b013e3181f74ad7.

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11

VanLinden, Magali R., Renate Hvidsten Skoge, and Mathias Ziegler. "Discovery, metabolism and functions of NAD and NADP." Biochemist 37, no. 1 (2015): 9–13. http://dx.doi.org/10.1042/bio03701009.

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Nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP) are two major players in metabolism as they participate as electron carriers in a multitude of redox reactions. Moreover, they act in life and death decisions on a cellular level in all known life forms. NAD and NADP both exist in two states; the oxidized forms are characterized by a positive charge on the nicotinamide (Nam) moiety, denoted NAD+ and NADP+ respectively. The reduced forms are denoted NADH and NADPH (Figure 1).
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12

Nesi, Marina, Marcella Chiari, Giacomo Carrea, Gianluca Ottolina, and Pier Giorgio Righetti. "Capillary electrophoresis of nicotinamide—adenine dinucleotide and nicotinamide—adenine dinucleotide phosphate derivatives in coated tubular columns." Journal of Chromatography A 670, no. 1-2 (1994): 215–21. http://dx.doi.org/10.1016/0021-9673(94)80297-1.

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13

Zhang, Fang-Jie, Qu-Ming Gu, Peicheng Jing, and Charles J. Sih. "Enzymatic cyclization of nicotinamide adenine dinucleotide phosphate (NADP)." Bioorganic & Medicinal Chemistry Letters 5, no. 19 (1995): 2267–72. http://dx.doi.org/10.1016/0960-894x(95)00393-8.

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14

Takizawa, Kohei, Koji Muramatsu, Kouji Maruyama, et al. "Metabolic Profiling of Human Gastric Cancer Cells Treated With Salazosulfapyridine." Technology in Cancer Research & Treatment 19 (January 1, 2020): 153303382092862. http://dx.doi.org/10.1177/1533033820928621.

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Purpose: The adhesion molecule cluster of differentiation 44v9 interacts with and stabilizes the cystine/glutamate exchanger protein, which functions as a transporter of cystine. Stabilized cystine/glutamate exchanger increases extracellular cystine uptake and enhances glutathione production. Augmented levels of reduced glutathione mitigate reactive oxygen species and protect cancer cells from apoptosis. Salazosulfapyridine blocks cystine/glutamate exchanger activity and mitigates the supply of cystine to increase intracellular ROS production, thereby increasing cell susceptibility to apoptosi
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15

Rutter, Guy A., and Elisa A. Bellomo. "Ca2+ signalling: a new route to NAADP." Biochemical Journal 411, no. 1 (2008): e1-e3. http://dx.doi.org/10.1042/bj20080282.

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NAADP (nicotinic acid–adenine dinucleotide phosphate) is a derivative of NADP (nicotinamide–adenine dinucleotide phosphate), which differs by the presence of a nicotinic acid instead of a nicotinamide moiety. This small structural difference makes NAADP one of the most powerful second messengers known, able to mobilize intracellular Ca2+ in a wide range of cellular models, ranging from invertebrates to mammals. Despite this, our understanding of NAADP homoeostasis, metabolism and physiological action is still limited. A new report by Vasudevan and colleagues in this issue of the Biochemical Jo
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16

Kinoshita, Hiroyuki, Naoyuki Matsuda, Hikari Kaba, et al. "Roles of Phosphatidylinositol 3-Kinase-Akt and NADPH Oxidase in Adenosine 5′-Triphosphate–Sensitive K + Channel Function Impaired by High Glucose in the Human Artery." Hypertension 52, no. 3 (2008): 507–13. http://dx.doi.org/10.1161/hypertensionaha.108.118216.

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The present study was designed to examine roles of the phosphatidylinositol 3-kinase-Akt pathway and reduced nicotinamide-adenine dinucleotide phosphate oxidases in the reduced ATP-sensitive K + channel function via superoxide produced by high glucose in the human artery. We evaluated the activity of the phosphatidylinositol 3-kinase-Akt pathway, as well as reduced nicotinamide-adenine dinucleotide phosphate oxidases, the intracellular levels of superoxide and ATP-sensitive K + channel function in the human omental artery without endothelium. Levels of the p85-α subunit and reduced nicotinamid
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17

Sergeeva, I. V., N. I. Kamzalakova, E. P. Tikhonova, and G. V. Bulygin. "Metabolic changes in the lymphocytes during influenza." Kazan medical journal 93, no. 4 (2012): 580–84. http://dx.doi.org/10.17816/kmj1547.

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Aim. To assess the nature and intensity of metabolic processes in lymphocytes of patients with influenza according to the activity of intracellular enzymes in comparison to the severity of the disease. Methods. Determined were the enzymatic parameters of lymphocytes of 45 patients aged 18 to 42 years with a diagnosis of «influenza». Two groups of patients were formed: with moderate (24 patients) and severe (21 patients) course of the disease. Used as controls were the values the activity of intracellular enzymes of lymphocytes of 37 practically healthy individuals of comparable age. Results. I
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18

Maier, Kristopher G. "Nicotinamide Adenine Dinucleotide Phosphate Oxidase and Diabetes: Vascular Implications." Vascular and Endovascular Surgery 42, no. 4 (2008): 305–13. http://dx.doi.org/10.1177/1538574408320172.

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19

Kushwaha, Prem Prakash, Sanjay Gupta, Atul Kumar Singh, Kumari Sunita Prajapati, Mohd Shuaib, and Shashank Kumar. "MicroRNA Targeting Nicotinamide Adenine Dinucleotide Phosphate Oxidases in Cancer." Antioxidants & Redox Signaling 32, no. 5 (2020): 267–84. http://dx.doi.org/10.1089/ars.2019.7918.

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20

Lambeth, J. David. "Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases." Current Opinion in Hematology 9, no. 1 (2002): 11–17. http://dx.doi.org/10.1097/00062752-200201000-00003.

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21

Bidwell, Joseph P., and John E. Stuehr. "Kinetic and thermodynamic study of the interactions of nickel(II) with nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate." Inorganic Chemistry 29, no. 6 (1990): 1143–47. http://dx.doi.org/10.1021/ic00331a007.

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22

Guse, Andreas H. "Enzymology of Ca2+-Mobilizing Second Messengers Derived from NAD: From NAD Glycohydrolases to (Dual) NADPH Oxidases." Cells 12, no. 4 (2023): 675. http://dx.doi.org/10.3390/cells12040675.

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Nicotinamide adenine dinucleotide (NAD) and its 2′-phosphorylated cousin NADP are precursors for the enzymatic formation of the Ca2+-mobilizing second messengers adenosine diphosphoribose (ADPR), 2′-deoxy-ADPR, cyclic ADPR, and nicotinic acid adenine dinucleotide phosphate (NAADP). The enzymes involved are either NAD glycohydrolases CD38 or sterile alpha toll/interleukin receptor motif containing-1 (SARM1), or (dual) NADPH oxidases (NOX/DUOX). Enzymatic function(s) are reviewed and physiological role(s) in selected cell systems are discussed.
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23

Bonanno, Adele, Irene Pérez-Herráez, Elena Zaballos-García, and Julia Pérez-Prieto. "Gold nanoclusters for ratiometric sensing of pH in extremely acidic media." Chemical Communications 56, no. 4 (2020): 587–90. http://dx.doi.org/10.1039/c9cc08539d.

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AuNCs capped with β-nicotinamide adenine dinucleotide phosphate exhibit an outstanding performance as ratiometric, fluorescent pH sensors in extremely acid media (0.6–2.7) and in the 7.0–9.2 pH range; the nanocluster itself is the fluorophore.
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24

Ito, Hiroki, Takuya Terai, Kenjiro Hanaoka, et al. "Detection of NAD(P)H-dependent enzyme activity with dynamic luminescence quenching of terbium complexes." Chemical Communications 51, no. 39 (2015): 8319–22. http://dx.doi.org/10.1039/c5cc01613d.

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We developed a practical and general luminescence assay platform for reduced nicotinamide adenine dinucleotide (phosphate) (NAD(P)H)-dependent enzymes by exploiting dynamic luminescence quenching of some Tb<sup>3+</sup> complexes by NAD(P)H.
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25

Reitman, Zachary J., Sergey A. Sinenko, Eric P. Spana, and Hai Yan. "Genetic dissection of leukemia-associated IDH1 and IDH2 mutants and D-2-hydroxyglutarate in Drosophila." Blood 125, no. 2 (2015): 336–45. http://dx.doi.org/10.1182/blood-2014-05-577940.

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Key Points Homologs to cancer-derived IDH1 and IDH2 mutants produce D-2HG and drive expansion of Drosophila blood cells. In flies, mutant Idh interacts with genes that regulate reduced nicotinamide adenine dinucleotide phosphate, reactive oxygen species, and apoptosis.
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26

Gasperi, Valeria, Matteo Sibilano, Isabella Savini, and Maria Catani. "Niacin in the Central Nervous System: An Update of Biological Aspects and Clinical Applications." International Journal of Molecular Sciences 20, no. 4 (2019): 974. http://dx.doi.org/10.3390/ijms20040974.

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Niacin (also known as “vitamin B3” or “vitamin PP”) includes two vitamers (nicotinic acid and nicotinamide) giving rise to the coenzymatic forms nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP). The two coenzymes are required for oxidative reactions crucial for energy production, but they are also substrates for enzymes involved in non-redox signaling pathways, thus regulating biological functions, including gene expression, cell cycle progression, DNA repair and cell death. In the central nervous system, vitamin B3 has long been recognized as a ke
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27

Popova, Olga, Daria Bylinskaya, Anastasia Nikitina та Olga Ukrainskaya. "The processes of the catalytic cycle of the cytochrome system associated with its activation by means of the enzyme Nicotinamide-β-adenine dinucleotide phosphate-H-ferrihemoprotein oxidoreductase". BIO Web of Conferences 181 (2025): 01026. https://doi.org/10.1051/bioconf/202518101026.

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The paper presents a theoretical study of the molecular mechanism of activation of the cytochrome P450 system by the enzyme Nicotinamide-β-adenine dinucleotide phosphate-H-ferrihemoprotein oxidoreductase in the catalytic cycle. The relevance of studying cytochrome P450 enzymes and their activator is determined by the development of methods for effective diagnostics of hepatobiliary pathologies. It was found that the enzyme Nicotinamide-β-adenine dinucleotide phosphate-H-ferrihemoprotein oxidoreductase functions as a redox “partner” for cytochromes P450. An electrochemical method used to study
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28

Zerez, CR, EF Jr Roth, S. Schulman, and KR Tanaka. "Increased nicotinamide adenine dinucleotide content and synthesis in Plasmodium falciparum-infected human erythrocytes." Blood 75, no. 8 (1990): 1705–10. http://dx.doi.org/10.1182/blood.v75.8.1705.1705.

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Abstract Plasmodium falciparum-infected red blood cells (RBCs) are characterized by increases in the activity of glycolytic enzymes. Because nicotinamide adenine dinucleotide (NAD) and NAD phosphate (NADP) are cofactors in the reactions of glycolysis and pentose phosphate shunt, we have examined NAD and NADP content in P. falciparum-infected RBCs. Although NADP content was not significantly altered, NAD content was increased approximately 10-fold in infected RBCs (66% parasitemia) compared with uninfected control RBCs. To determine the mechanism for the increase in NAD content, we examined the
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29

Zerez, CR, EF Jr Roth, S. Schulman, and KR Tanaka. "Increased nicotinamide adenine dinucleotide content and synthesis in Plasmodium falciparum-infected human erythrocytes." Blood 75, no. 8 (1990): 1705–10. http://dx.doi.org/10.1182/blood.v75.8.1705.bloodjournal7581705.

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Plasmodium falciparum-infected red blood cells (RBCs) are characterized by increases in the activity of glycolytic enzymes. Because nicotinamide adenine dinucleotide (NAD) and NAD phosphate (NADP) are cofactors in the reactions of glycolysis and pentose phosphate shunt, we have examined NAD and NADP content in P. falciparum-infected RBCs. Although NADP content was not significantly altered, NAD content was increased approximately 10-fold in infected RBCs (66% parasitemia) compared with uninfected control RBCs. To determine the mechanism for the increase in NAD content, we examined the activity
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30

Nakamura, Brooke N., Thomas J. Fielder, Yvonne D. Hoang, et al. "Lack of Maternal Glutamate Cysteine Ligase Modifier Subunit (Gclm) Decreases Oocyte Glutathione Concentrations and Disrupts Preimplantation Development in Mice." Endocrinology 152, no. 7 (2011): 2806–15. http://dx.doi.org/10.1210/en.2011-0207.

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Glutathione (GSH) is the most abundant intracellular thiol and an important regulator of cellular redox status. Mice that lack the modifier subunit of glutamate cysteine ligase (Gclm), the rate-limiting enzyme in GSH synthesis, have decreased GSH synthesis. Nicotinamide nucleotide transhydrogenase, an inner mitochondrial membrane protein, catalyzes the interconversion of reduced nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide phosphate; reduced nicotinamide adenine dinucleotide phosphate is required for reduction of GSH disulfide. Previous work supports roles fo
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31

Dowden, James, Christelle Moreau, Richard S. Brown, Georgina Berridge, Antony Galione, and Barry V. L. Potter. "Chemical Synthesis of the Second Messenger Nicotinic Acid Adenine Dinucleotide Phosphate by Total Synthesis of Nicotinamide Adenine Dinucleotide Phosphate." Angewandte Chemie International Edition 43, no. 35 (2004): 4637–40. http://dx.doi.org/10.1002/anie.200460054.

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32

Dowden, James, Christelle Moreau, Richard S. Brown, Georgina Berridge, Antony Galione, and Barry V. L. Potter. "Chemical Synthesis of the Second Messenger Nicotinic Acid Adenine Dinucleotide Phosphate by Total Synthesis of Nicotinamide Adenine Dinucleotide Phosphate." Angewandte Chemie 116, no. 35 (2004): 4737–40. http://dx.doi.org/10.1002/ange.200460054.

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33

Zachos, Ioannis, Manuel Döring, Georg Tafertshofer, Robert C. Simon, and Volker Sieber. "carba Nicotinamide Adenine Dinucleotide Phosphate: Robust Cofactor for Redox Biocatalysis." Angewandte Chemie International Edition 60, no. 26 (2021): 14701–6. http://dx.doi.org/10.1002/anie.202017027.

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34

Brandes, Ralf P., and Katrin Schröder. "Composition and Functions of Vascular Nicotinamide Adenine Dinucleotide Phosphate Oxidases." Trends in Cardiovascular Medicine 18, no. 1 (2008): 15–19. http://dx.doi.org/10.1016/j.tcm.2007.11.001.

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35

Kwaifa, Ibrahim Kalle, Osaro Erhabor, Abdulrahman Yakubu, et al. "Pathophysiology and current laboratory investigations of Glucose-6-Phosphate dehydrogenase deficiency." Sokoto Journal of Medical Laboratory Science 10, no. 1 (2025): 358–79. https://doi.org/10.4314/sokjmls.v10i1.35.

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Glucose-6-phosphate dehydrogenase catalyses the rate-determining step in the pentose phosphate pathway. Its activity is a key determinant of the reduced nicotinamide adenine dinucleotide phosphate to oxidized nicotinamide adenine dinucleotide phosphate (NADPH-to-NADP+) ratio in the cytoplasm and thus contributes to the replenishment of the antioxidant glutathione system. Glucose-6-phosphate dehydrogenase deficiency is a common X-linked human enzyme defect of red blood cells. Individuals with this gene defect appear normal until exposed to oxidative stress which induces haemolysis but it is inf
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Chongdar, Nipa, Krzysztof Pawlak, Olaf Rüdiger, et al. "Spectroscopic and biochemical insight into an electron-bifurcating [FeFe] hydrogenase." JBIC Journal of Biological Inorganic Chemistry 25, no. 1 (2019): 135–49. http://dx.doi.org/10.1007/s00775-019-01747-1.

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Abstract The heterotrimeric electron-bifurcating [FeFe] hydrogenase (HydABC) from Thermotoga maritima (Tm) couples the endergonic reduction of protons (H+) by dihydronicotinamide adenine dinucleotide (NADH) (∆G0 ≈ 18 kJ mol−1) to the exergonic reduction of H+ by reduced ferredoxin (Fdred) (∆G0 ≈ − 16 kJ mol−1). The specific mechanism by which HydABC functions is not understood. In the current study, we describe the biochemical and spectroscopic characterization of TmHydABC recombinantly produced in Escherichia coli and artificially maturated with a synthetic diiron cofactor. We found that TmHy
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37

Makarov, Mikhail V., Samuel A. J. Trammell, and Marie E. Migaud. "The chemistry of the vitamin B3 metabolome." Biochemical Society Transactions 47, no. 1 (2018): 131–47. http://dx.doi.org/10.1042/bst20180420.

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Abstract The functional cofactors derived from vitamin B3 are nicotinamide adenine dinucleotide (NAD+), its phosphorylated form, nicotinamide adenine dinucleotide phosphate (NADP+) and their reduced forms (NAD(P)H). These cofactors, together referred as the NAD(P)(H) pool, are intimately implicated in all essential bioenergetics, anabolic and catabolic pathways in all forms of life. This pool also contributes to post-translational protein modifications and second messenger generation. Since NAD+ seats at the cross-road between cell metabolism and cell signaling, manipulation of NAD+ bioavailab
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38

Luo, Jun, and Li Yang. "Role of nicotinamide adenine dinucleotide phosphate-oxidase family in liver fibrogenesis." World Chinese Journal of Digestology 16, no. 16 (2008): 1768. http://dx.doi.org/10.11569/wcjd.v16.i16.1768.

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39

Scott, Barry. "Conservation of fungal and animal nicotinamide adenine dinucleotide phosphate oxidase complexes." Molecular Microbiology 95, no. 6 (2015): 910–13. http://dx.doi.org/10.1111/mmi.12946.

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40

Zhou, Ying, Junchao Wu, Rui Sheng, et al. "Reduced Nicotinamide Adenine Dinucleotide Phosphate Inhibits MPTP-Induced Neuroinflammation and Neurotoxicity." Neuroscience 391 (November 2018): 140–53. http://dx.doi.org/10.1016/j.neuroscience.2018.08.032.

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41

Markham, Kelli A., R. Steven Sikorski, and Amnon Kohen. "Purification, analysis, and preservation of reduced nicotinamide adenine dinucleotide 2′-phosphate." Analytical Biochemistry 322, no. 1 (2003): 26–32. http://dx.doi.org/10.1016/j.ab.2003.07.010.

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42

Hou, Liyan, Lin Zhang, Jau-Shyong Hong, Dan Zhang, Jie Zhao, and Qingshan Wang. "Nicotinamide Adenine Dinucleotide Phosphate Oxidase and Neurodegenerative Diseases: Mechanisms and Therapy." Antioxidants & Redox Signaling 33, no. 5 (2020): 374–93. http://dx.doi.org/10.1089/ars.2019.8014.

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43

Clark, Andrea J., Roberto Romero, and Howard R. Petty. "Improved detection of nicotinamide adenine dinucleotide phosphate oscillations within human neutrophils." Cytometry Part A 77A, no. 10 (2010): 976–82. http://dx.doi.org/10.1002/cyto.a.20961.

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44

Li, Qiang, Kang Huang, Tianyi Ma, et al. "Metoprolol Protects Against Arginine Vasopressin-Induced Cellular Senescence in H9C2 Cardiomyocytes by Regulating the Sirt1/p53/p21 Axis." Cardiovascular Toxicology 22, no. 2 (2021): 99–107. http://dx.doi.org/10.1007/s12012-021-09704-8.

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AbstractCardiomyocyte senescence is involved in the pathological mechanism of cardiac diseases. Metoprolol is a β1 receptor blocker used for the treatment of hypertension. Recent studies show that Metoprolol can protect cardiomyocytes against ischemia injury. The present study aims to investigate the protective effects of Metoprolol against arginine vasopressin (AVP)-induced cellular senescence in cultured cardiomyocytes. The cell proliferation assay and cytotoxicity lactate dehydrogenase assay showed that the highest tolerated dosage of Metoprolol in H9C2 cardiomyocytes was optimized as 10 µM
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Clément, David A., Clarisse Leseigneur, Muriel Gelin, et al. "New Chemical Probe Targeting Bacterial NAD Kinase." Molecules 25, no. 21 (2020): 4893. http://dx.doi.org/10.3390/molecules25214893.

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Nicotinamide adenine dinucleotide (NAD) kinases are essential and ubiquitous enzymes involved in the tight regulation of NAD/nicotinamide adenine dinucleotide phosphate (NADP) levels in many metabolic pathways. Consequently, they represent promising therapeutic targets in cancer and antibacterial treatments. We previously reported diadenosine derivatives as NAD kinase inhibitors with bactericidal activities on Staphylococcus aureus. Among them, one compound (namely NKI1) was found effective in vivo in a mouse infection model. With the aim to gain detailed knowledge about the selectivity and me
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Horsefield, Shane, Hayden Burdett, Xiaoxiao Zhang, et al. "NAD+ cleavage activity by animal and plant TIR domains in cell death pathways." Science 365, no. 6455 (2019): 793–99. http://dx.doi.org/10.1126/science.aax1911.

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SARM1 (sterile alpha and TIR motif containing 1) is responsible for depletion of nicotinamide adenine dinucleotide in its oxidized form (NAD+) during Wallerian degeneration associated with neuropathies. Plant nucleotide-binding leucine-rich repeat (NLR) immune receptors recognize pathogen effector proteins and trigger localized cell death to restrict pathogen infection. Both processes depend on closely related Toll/interleukin-1 receptor (TIR) domains in these proteins, which, as we show, feature self-association–dependent NAD+ cleavage activity associated with cell death signaling. We further
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47

Badawy, Abdulla A.-B. "Kynurenine Pathway of Tryptophan Metabolism: Regulatory and Functional Aspects." International Journal of Tryptophan Research 10 (January 1, 2017): 117864691769193. http://dx.doi.org/10.1177/1178646917691938.

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Regulatory and functional aspects of the kynurenine (K) pathway (KP) of tryptophan (Trp) degradation are reviewed. The KP accounts for ~95% of dietary Trp degradation, of which 90% is attributed to the hepatic KP. During immune activation, the minor extrahepatic KP plays a more active role. The KP is rate-limited by its first enzyme, Trp 2,3-dioxygenase (TDO), in liver and indoleamine 2,3-dioxygenase (IDO) elsewhere. TDO is regulated by glucocorticoid induction, substrate activation and stabilization by Trp, cofactor activation by heme, and end-product inhibition by reduced nicotinamide adenin
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48

Protasov, Evgeniy, Larisa Koleva, Elizaveta Bovt, Fazoil I. Ataullakhanov, and Elena Sinauridze. "Theoretical Analysis of the Built-in Metabolic Pathway Effect on the Metabolism of Erythrocyte-Bioreactors That Neutralize Ammonium." Metabolites 11, no. 1 (2021): 36. http://dx.doi.org/10.3390/metabo11010036.

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The limitations of the efficiency of ammonium-neutralizing erythrocyte-bioreactors based on glutamate dehydrogenase and alanine aminotransferase reactions were analyzed using a mathematical model. At low pyruvate concentrations in the external medium (below about 0.3 mM), the main limiting factor is the rate of pyruvate influx into the erythrocyte from the outside, and at higher concentrations, it is the disappearance of a steady state in glycolysis if the rate of ammonium processing is higher than the critical value (about 12 mM/h). This rate corresponds to different values of glutamate dehyd
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49

G., Sri Manjula, D.V. Ramanjaneyulu, E. Muralinath, et al. "An Indications, Off-Label Uses, Mechanism of Action, Pharmacokinetics, Administration, Adverse Effects, Contra Indications of Niacin B3." Journal of Applied Nursing Research and Education 3, no. 1 (2024): 1–8. https://doi.org/10.5281/zenodo.13954350.

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<em>Niacin, also known as vitamin B3, belongs to the water-soluble B complex group and is </em><em>observed in various foods </em><em>namely bran, yeast, eggs, peanuts, poultry, red meat, fish, whole-grain cereals, legumes, and seeds. This essential vitamin plays a role in cellular metabolism as a vital component</em><em> especially in the oxidized state of nicotinamide adenine dinucleotide (NAD, or coenzyme 1) and the reduced form of nicotinamide adenine dinucleotide phosphate (NADP, or coenzyme 2). These coenzymes</em><em> are involved in an active manner particularly in essential oxidation-
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Dang, Pham My-Chan, Jennifer L. Johnson, and Bernard M. Babior. "Binding of Nicotinamide Adenine Dinucleotide Phosphate to the Tetratricopeptide Repeat Domains at the N-Terminus of p67PHOX, a Subunit of the Leukocyte Nicotinamide Adenine Dinucleotide Phosphate Oxidase†." Biochemistry 39, no. 11 (2000): 3069–75. http://dx.doi.org/10.1021/bi9919807.

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