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1

Xu, Xiaowen, Xinxin Wang, Li Zhang, et al. "Nicotinamide adenine dinucleotide treatment confers resistance to neonatal ischemia and hypoxia: effects on neurobehavioral phenotypes." Neural Regeneration Research 19, no. 12 (2024): 2760–72. http://dx.doi.org/10.4103/nrr.nrr-d-23-01490.

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JOURNAL/nrgr/04.03/01300535-202412000-00031/figure1/v/2024-04-08T165401Z/r/image-tiff Neonatal hypoxic-ischemic brain injury is the main cause of hypoxic-ischemic encephalopathy and cerebral palsy. Currently, there are few effective clinical treatments for neonatal hypoxic-ischemic brain injury. Here, we investigated the neuroprotective and molecular mechanisms of exogenous nicotinamide adenine dinucleotide, which can protect against hypoxic injury in adulthood, in a mouse model of neonatal hypoxic-ischemic brain injury. In this study, nicotinamide adenine dinucleotide (5 mg/kg) was intraperit
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2

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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3

Micheli, Vanna, H. Anne Simmonds, and Carlo Ricci. "Regulation of nicotinamide–adenine dinucleotide synthesis in erythrocytes of patients with hypoxanthine–guanine phosphoribosyltransferase deficiency and a patient with phosphoribosylpyrophosphate synthetase superactivity." Clinical Science 78, no. 2 (1990): 239–45. http://dx.doi.org/10.1042/cs0780239.

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1. The synthesis of nicotinamide–adenine dinucleotide from nicotinamide and nicotinic acid was compared over different time scales at both physiological (0.7 μmol/l) and high (0.2–3 mmol/l) substrate concentrations in erythrocytes from three patients with hypoxanthine–guanine phosphoribosyltransferase (hypoxanthine phosphoribosyltransferase, EC 2.4.2.8) deficiency (including one Lesch–Nyhan patient) and from one patient with phosphoribosylpyrophosphate synthetase superactivity. The above disorders are associated with grossly altered erythrocyte nicotinamide-adenine dinucleotide levels. 2. At t
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4

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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5

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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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

Pankiewicz, K., L. Chen, R. Petrelli, et al. "Nicotinamide Adenine Dinucleotide Based Therapeutics." Current Medicinal Chemistry 15, no. 7 (2008): 650–70. http://dx.doi.org/10.2174/092986708783885282.

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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

Merk, Virginia, Eugen Speiser, Wolfgang Werncke, Norbert Esser, and Janina Kneipp. "pH-Dependent Flavin Adenine Dinucleotide and Nicotinamide Adenine Dinucleotide Ultraviolet Resonance Raman (UVRR) Spectra at Intracellular Concentration." Applied Spectroscopy 75, no. 8 (2021): 994–1002. http://dx.doi.org/10.1177/00037028211025575.

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The ultraviolet resonance Raman spectra of the adenine-containing enzymatic redox cofactors nicotinamide adenine dinucleotide and flavin adenine dinucleotide in aqueous solution of physiological concentration are compared with the aim of distinguishing between them and their building block adenine in potential co-occurrence in biological materials. At an excitation wavelength of 266 nm, the spectra are dominated by the strong resonant contribution from adenine; nevertheless, bands assigned to vibrational modes of the nicotinamide and the flavin unit are found to appear at similar signal streng
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10

Stockman, Brian J., Ian J. Lodovice, Douglas A. Fisher, Alexander S. Mccoll, and Zhi Xie. "A Nuclear Magnetic Resonance–Based Functional Assay for Nicotinamide Adenine Dinucleotide Synthetase." Journal of Biomolecular Screening 12, no. 4 (2007): 457–63. http://dx.doi.org/10.1177/1087057107299717.

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Nicotinamide adenine dinucleotide synthetase (NadE) is an essential enzyme for bacterial pathogens and is thus a promising antibacterial target. It catalyzes the conversion of nicotinic acid adenine dinucleotide to nicotinamide adenine dinucleotide. Changes in chemical shifts that occur in the nicotinic acid ring as it is converted to nicotinamide can be used for monitoring the reaction. A robust nuclear magnetic resonance—based activity assay was developed using robotically controlled reaction initiation and quenching. The single-enzyme assay has less potential for false positives compared to
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11

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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12

Pankiewicz, K. W., R. Petrelli, R. Singh, and K. Felczak. "Nicotinamide Adenine Dinucleotide Based Therapeutics, Update." Current Medicinal Chemistry 22, no. 34 (2015): 3991–4028. http://dx.doi.org/10.2174/0929867322666150821100720.

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13

Kim, Jinhyun, Sahng Ha Lee, Florian Tieves, Caroline E. Paul, Frank Hollmann, and Chan Beum Park. "Nicotinamide adenine dinucleotide as a photocatalyst." Science Advances 5, no. 7 (2019): eaax0501. http://dx.doi.org/10.1126/sciadv.aax0501.

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Nicotinamide adenine dinucleotide (NAD+) is a key redox compound in all living cells responsible for energy transduction, genomic integrity, life-span extension, and neuromodulation. Here, we report a new function of NAD+ as a molecular photocatalyst in addition to the biological roles. Our spectroscopic and electrochemical analyses reveal light absorption and electronic properties of two π-conjugated systems of NAD+. Furthermore, NAD+ exhibits a robust photostability under UV-Vis-NIR irradiation. We demonstrate photocatalytic redox reactions driven by NAD+, such as O2 reduction, H2O oxidation
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14

Pehar, Mariana, Benjamin A. Harlan, Kelby M. Killoy, and Marcelo R. Vargas. "Nicotinamide Adenine Dinucleotide Metabolism and Neurodegeneration." Antioxidants & Redox Signaling 28, no. 18 (2018): 1652–68. http://dx.doi.org/10.1089/ars.2017.7145.

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15

Petrelli, Riccardo, Yuk Yin Sham, Liqiang Chen, et al. "Selective inhibition of nicotinamide adenine dinucleotide kinases by dinucleoside disulfide mimics of nicotinamide adenine dinucleotide analogues." Bioorganic & Medicinal Chemistry 17, no. 15 (2009): 5656–64. http://dx.doi.org/10.1016/j.bmc.2009.06.013.

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16

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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17

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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18

Zhang, Xiao-Nan, Albert T. Lam, Qinqin Cheng, et al. "Discovery of an NAD+ analogue with enhanced specificity for PARP1." Chemical Science 13, no. 7 (2022): 1982–91. http://dx.doi.org/10.1039/d1sc06256e.

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An analogue of nicotinamide adenine dinucleotide (NAD+) featuring an azido group at 3′-OH of adenosine moiety is found to possess high specificity for human PARP1-catalyzed protein poly-ADP-ribosylation.
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19

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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20

Matteucci, Federica, Marta Ferrati, Eleonora Spinozzi, et al. "Synthesis, Biological, and Computational Evaluations of Conformationally Restricted NAD-Mimics as Discriminant Inhibitors of Human NMN-Adenylyltransferase Isozymes." Pharmaceuticals 17, no. 6 (2024): 739. http://dx.doi.org/10.3390/ph17060739.

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Nicotinamide adenine dinucleotide (NAD) cofactor metabolism plays a significant role in cancer development. Tumor cells have an increased demand for NAD and ATP to support rapid growth and proliferation. Limiting the amount of available NAD by targeting critical NAD biosynthesis enzymes has emerged as a promising anticancer therapeutic approach. In mammals, the enzyme nicotinamide/nicotinic acid adenylyltransferase (NMNAT) catalyzes a crucial downstream reaction for all known NAD synthesis routes. Novel nicotinamide/nicotinic acid adenine dinucleotide (NAD/NaAD) analogues 1–4, containing a met
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21

Eisenthal, Robert, Peter J. Channon, William J. D. Whish, and Roger Harrison. "The Trifluoroacetylpyridine Analog of Nicotinamide Adenine Dinucleotide." HETEROCYCLES 37, no. 3 (1994): 1459. http://dx.doi.org/10.3987/com-93-s150.

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22

Lin, Hening. "Nicotinamide adenine dinucleotide: beyond a redox coenzyme." Organic & Biomolecular Chemistry 5, no. 16 (2007): 2541. http://dx.doi.org/10.1039/b706887e.

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23

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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24

Jackson, J. B. "The proton-translocating nicotinamide adenine dinucleotide transhydrogenase." Journal of Bioenergetics and Biomembranes 23, no. 5 (1991): 715–41. http://dx.doi.org/10.1007/bf00785998.

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25

Arenas-Jal, Marta, J. M. Suñé-Negre, and Encarna García-Montoya. "Therapeutic potential of nicotinamide adenine dinucleotide (NAD)." European Journal of Pharmacology 879 (July 2020): 173158. http://dx.doi.org/10.1016/j.ejphar.2020.173158.

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26

Guillot, Benoit, Christian Jelsch, and Claude Lecomte. "The oxidized form of nicotinamide adenine dinucleotide." Acta Crystallographica Section C Crystal Structure Communications 56, no. 6 (2000): 726–28. http://dx.doi.org/10.1107/s0108270100001220.

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27

Sharma, Ashutosh. "Photolytic oxidation of reduced nicotinamide adenine dinucleotide." Spectrochimica Acta Part A: Molecular Spectroscopy 48, no. 6 (1992): 893–97. http://dx.doi.org/10.1016/0584-8539(92)80086-c.

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28

Byers, S., D. Anderson, D. Brobst, and F. Cowan. "Automated assay for nicotinamide adenine dinucleotide (NAD+)†‡." Journal of Applied Toxicology 20, S1 (2001): S19—S22. http://dx.doi.org/10.1002/1099-1263(200012)20:1+<::aid-jat694>3.0.co;2-j.

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29

Mukherjee, Sarmistha, Karthikeyani Chellappa, Andrea Moffitt, et al. "Nicotinamide adenine dinucleotide biosynthesis promotes liver regeneration." Hepatology 65, no. 2 (2016): 616–30. http://dx.doi.org/10.1002/hep.28912.

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30

Vinkovic, M., G. Dunn, G. E. Wood, J. Husain, S. P. Wood, and R. Gill. "Cleavage of nicotinamide adenine dinucleotide by the ribosome-inactivating protein fromMomordica charantia." Acta Crystallographica Section F Structural Biology Communications 71, no. 9 (2015): 1152–55. http://dx.doi.org/10.1107/s2053230x15013540.

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The interaction of momordin, a type 1 ribosome-inactivating protein fromMomordica charantia, with NADP+and NADPH has been investigated by X-ray diffraction analysis of complexes generated by co-crystallization and crystal soaking. It is known that the proteins of this family readily cleave the adenine–ribose bond of adenosine and related nucleotides in the crystal, leaving the product, adenine, bound to the enzyme active site. Surprisingly, the nicotinamide–ribose bond of oxidized NADP+is cleaved, leaving nicotinamide bound in the active site in the same position but in a slightly different or
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31

Ghorbania, Fatemeh, Masoomeh Ghorbani та Arezou Ghahghaee. "The Inhibitory Effects of Nucleosides, Nicotinamide Adenine Dinucleotide, Adenosine 5'-Triphosphate, Inosine, Nicotinamide Riboside and Nicotinamide Mononucleotide Against α-Amylase and α-Glucosidase Enzymes". SDRP Journal of Food Science & Technology 5, № 3 (2020): 182–98. http://dx.doi.org/10.25177/jfst.5.4.ra.10644.

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Diabetes is a group of metabolic disorders characterized by a high blood sugar level over a prolonged period of time. Inhibition of carbohydrate hydrolyzing enzymes leads to decrease in the absorption of glucose which is considered as one of the effective managements of diabetes mellitus. Vegetable, fruit, milk and fish are good sources of nucleosides and inosine (INO), nicotinamide riboside (NR) and nicotinamide mononucleotide (NMN) with versatile health benefits. The well-adapted structural features of these compounds for the inhibition/activation of enzymes include several available hydroge
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32

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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33

Shabalin, Konstantin, Kirill Nerinovski, Alexander Yakimov, et al. "NAD Metabolome Analysis in Human Cells Using 1H NMR Spectroscopy." International Journal of Molecular Sciences 19, no. 12 (2018): 3906. http://dx.doi.org/10.3390/ijms19123906.

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Nicotinamide adenine dinucleotide (NAD) and its phosphorylated form, NADP, are the major coenzymes of redox reactions in central metabolic pathways. Nicotinamide adenine dinucleotide is also used to generate second messengers, such as cyclic ADP-ribose, and serves as substrate for protein modifications including ADP-ribosylation and protein deacetylation by sirtuins. The regulation of these metabolic and signaling processes depends on NAD availability. Generally, human cells accomplish their NAD supply through biosynthesis using different forms of vitamin B3: Nicotinamide (Nam) and nicotinic a
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34

Albano, Jeri, Gabriel Dario Patarroyo - Aponte, and Ejaz Mahmood. "Case of acute hepatic injury and elevated ethanol levels in a non-alcoholic adult." BMJ Case Reports 12, no. 11 (2019): e229814. http://dx.doi.org/10.1136/bcr-2019-229814.

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Blood ethanol concentration is measured using different techniques. Gas chromatography/mass spectrometry is used in forensic laboratories to measure whole blood ethanol levels while enzyme immunoassay is often used in hospitals to measure serum or plasma ethanol levels. Lactic acidosis can theoretically cause false elevation of blood ethanol levels measured through enzymatic assay because this method measures the reduction of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide- hydrogen (NADH) via the action of a dehydrogenase. Here, we present a rare incidence of eth
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35

Jiaul Haque, Al-Monsur, Jihye Kim, Gorachand Dutta, Sinyoung Kim, and Haesik Yang. "Redox cycling-amplified enzymatic Ag deposition and its application in the highly sensitive detection of creatine kinase-MB." Chemical Communications 51, no. 77 (2015): 14493–96. http://dx.doi.org/10.1039/c5cc06117b.

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36

Wang, Xiaobin, Yuqing Zhao, Qing Hua, et al. "An ultrasensitive electrochemiluminescence biosensor for the detection of total bacterial count in environmental and biological samples based on a novel sulfur quantum dot luminophore." Analyst 147, no. 8 (2022): 1716–21. http://dx.doi.org/10.1039/d2an00153e.

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37

Janoš, Pavel, Jiří Henych, Jan Pfeifer, et al. "Nanocrystalline cerium oxide prepared from a carbonate precursor and its ability to breakdown biologically relevant organophosphates." Environmental Science: Nano 4, no. 6 (2017): 1283–93. http://dx.doi.org/10.1039/c7en00119c.

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38

Lucena-Cacace, Antonio, ManuelP Jiménez-García, and EvaM Verdugo-Sivianes. "Nicotinamide adenine dinucleotide+ metabolism biomarkers in malignant gliomas." Cancer Translational Medicine 2, no. 6 (2016): 189. http://dx.doi.org/10.4103/2395-3977.196912.

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39

Guillot, Benoit, Claude Lecomte, Alain Cousson, Christian Scherf, and Christian Jelsch. "High-resolution neutron structure of nicotinamide adenine dinucleotide." Acta Crystallographica Section D Biological Crystallography 57, no. 7 (2001): 981–89. http://dx.doi.org/10.1107/s0907444901007120.

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40

Liu, Wujun, Siguo Wu, Shuhua Hou, and Zongbao (Kent) Zhao. "Synthesis of phosphodiester-type nicotinamide adenine dinucleotide analogs." Tetrahedron 65, no. 40 (2009): 8378–83. http://dx.doi.org/10.1016/j.tet.2009.08.007.

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41

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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42

Lee, Jaemoon, Hywyn Churchil, Woo-Baeg Choi, et al. "A chemical synthesis of nicotinamide adenine dinucleotide (NAD+)." Chemical Communications, no. 8 (1999): 729–30. http://dx.doi.org/10.1039/a809930h.

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43

Murray, M. F., M. Nghiem, and A. Srinivasan. "HIV Infection Decreases Intracellular Nicotinamide Adenine Dinucleotide [NAD]." Biochemical and Biophysical Research Communications 212, no. 1 (1995): 126–31. http://dx.doi.org/10.1006/bbrc.1995.1945.

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44

Piechowicz, Joanna, Andrzej Gamian, Danuta Zwolińska, and Dorota Polak-Jonkisz. "Adenine Nucleotide Metabolites in Uremic Erythrocytes as Metabolic Markers of Chronic Kidney Disease in Children." Journal of Clinical Medicine 10, no. 21 (2021): 5208. http://dx.doi.org/10.3390/jcm10215208.

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Chronic kidney disease (CKD) is associated with multifaceted pathophysiological lesions including metabolic pathways in red blood cells (RBC). The aim of the study was to determine the concentration of adenine nucleotide metabolites, i.e., nicotinamide adenine dinucleotide (NAD)-oxidized form, nicotinamide adenine dinucleotide hydrate (NADH)-reduced form, nicotinic acid mononucleotide (NAMN), β-nicotinamide mononucleotide (NMN), nicotinic acid adenine dinucleotide (NAAD), nicotinic acid (NA) and nicotinamide (NAM) in RBC and to determine a relationship between NAD metabolites and CKD progressi
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45

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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46

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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47

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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48

Pankiewicz, Krzysztof W., and Krzysztof Felczak. "From ribavirin to NAD analogues and back to ribavirin in search for anticancer agents." Heterocyclic Communications 21, no. 5 (2015): 249–57. http://dx.doi.org/10.1515/hc-2015-0133.

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AbstractRibavirin, a broad-spectrum antiviral agent is used in the clinic alone or in combination with other antivirals and/or interferons. Numerous structural analogues of ribavirin have been developed, among them tiazofurin, which is inactive against viruses but is a potent anticancer drug. Tiazofurin was found to inhibit nicotinamide adenine dinucleotide (NAD)-dependent inosine monophosphate dehydrogenase (IMPDH) after metabolic conversion into tiazofurin adenine dinucleotide (TAD), which binds well but could not serve as IMPDH cofactor. TAD showed high selectivity against human IMPDH vs. o
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Tóth, Balázs, Iordan Iordanov, and László Csanády. "Ruling out pyridine dinucleotides as true TRPM2 channel activators reveals novel direct agonist ADP-ribose-2′-phosphate." Journal of General Physiology 145, no. 5 (2015): 419–30. http://dx.doi.org/10.1085/jgp.201511377.

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Transient receptor potential melastatin 2 (TRPM2), a Ca2+-permeable cation channel implicated in postischemic neuronal cell death, leukocyte activation, and insulin secretion, is activated by intracellular ADP ribose (ADPR). In addition, the pyridine dinucleotides nicotinamide-adenine-dinucleotide (NAD), nicotinic acid–adenine-dinucleotide (NAAD), and NAAD-2′-phosphate (NAADP) have been shown to activate TRPM2, or to enhance its activation by ADPR, when dialyzed into cells. The precise subset of nucleotides that act directly on the TRPM2 protein, however, is unknown. Here, we use a heterologou
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Yamada, Kentaro, Chizuko Inada, Shuichi Otabe, Naoko Takane, Hideki Hayashi, and Kyohei Nonaka. "Effects of free radical scavengers on cytokine actions on islet cells." Acta Endocrinologica 128, no. 4 (1993): 379–84. http://dx.doi.org/10.1530/acta.0.1280379.

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We investigated the effect of free radical scavengers on the actions of cytokines on islet cells. Interferon-γ and tumor necrosis factor-α reduced the nicotinamide adenine dinucleotide content of mouse islet cells; the combination of interferon-γ (4×105 U/I) and tumor necrosis factor-α (4×105 U/I) caused nicotinamide adenine dinucleotide reduction by ∼40%. Dimethyl urea and dimethyl sulfoxide prevented the decrease, whereas superoxide dismutase, catalase, and mannitol were not effective. Dimethyl urea and dimethyl sulfoxide protected islet cells from the synergistic cytotoxic action of interfe
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