Windholz, Martha. The Merck Index: an encyclopedia of chemicals, drugs, and biologicals. 10th. vyd. Rahway NJ, US : Merck, 1983. ISBN 978-0-911910-27-8. S. 909.
The power to reduce: pyridine nucleotides – small molecules with a multitude of functions. Biochem. J., 2007, s. 205–18. DOI: 10.1042/BJ20061638. PMID 17295611.
Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim. Biophys. Acta, 1997, s. 217–34. DOI: 10.1016/S0005-2728(97)00034-0. PMID 9230919.
Structure of lactate dehydrogenase inhibitor generated from coenzyme. Biochemistry, 1979, s. 1212–7. DOI: 10.1021/bi00574a015. PMID 218616.
Fluorescence lifetime imaging of free and protein-bound NADH. Proc. Natl. Acad. Sci. U.S.A., 1992, s. 1271–5. DOI: 10.1073/pnas.89.4.1271. PMID 1741380.
Time-resolved fluorescence studies on NADH bound to mitochondrial malate dehydrogenase. Biochim. Biophys. Acta, 1989, s. 187–90. DOI: 10.1016/0167-4838(89)90159-3. PMID 2910350.
The Free NADH Concentration Is Kept Constant in Plant Mitochondria under Different Metabolic Conditions. Plant Cell, 2006, s. 688–98. DOI: 10.1105/tpc.105.039354. PMID 16461578.
Measurement of tissue purine, pyrimidine, and other nucleotides by radial compression high-performance liquid chromatography. Anal. Biochem., 1984, s. 162–71. DOI: 10.1016/0003-2697(84)90148-9. PMID 6486402.
The simultaneous measurement of nicotinamide adenine dinucleotide and related compounds by liquid chromatography/electrospray ionization tandem mass spectrometry. Anal. Biochem., 2006, s. 282–5. DOI: 10.1016/j.ab.2006.02.017. PMID 16574057.
Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+. Cell, 2007, s. 473–84. DOI: 10.1016/j.cell.2007.03.024. PMID 17482543.
Distribution of mitochondrial NADH fluorescence lifetimes: steady-state kinetics of matrix NADH interactions. Biochemistry, 2005, s. 2585–94. DOI: 10.1021/bi0485124. PMID 15709771.
Identification of the mitochondrial NAD+ transporter in Saccharomyces cerevisiae. J. Biol. Chem., 2006, s. 1524–31. DOI: 10.1074/jbc.M510425200. PMID 16291748.
Srivastava S. Emerging therapeutic roles for NAD(+) metabolism in mitochondrial and age-related disorders. Clinical and Translational Medicine, 2016, s. 25. DOI: 10.1186/s40169-016-0104-7. PMID 27465020.
Regulatory Effects of NAD + Metabolic Pathways on Sirtuin Activity. Progress in Molecular Biology and Translational Science, 2018, s. 71–104. DOI: 10.1016/bs.pmbts.2017.11.012. PMID 29413178.
Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med, 2001, s. 1191–212. DOI: 10.1016/S0891-5849(01)00480-4. PMID 11368918.
The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem. J., 1967, s. 514–27. DOI: 10.1042/bj1030514. PMID 4291787.
Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease. Curr. Opin. Cell Biol., April 2003, s. 241–6. DOI: 10.1016/S0955-0674(03)00006-1. PMID 12648681.
The redox state of free nicotinamide–adenine dinucleotide phosphate in the cytoplasm of rat liver. Biochem. J., 1969, s. 609–19. DOI: 10.1042/bj1150609a. PMID 4391039.
Early Steps in the Biosynthesis of NAD in Arabidopsis Start with Aspartate and Occur in the Plastid. Plant Physiol., 2006, s. 851–7. DOI: 10.1104/pp.106.081091. PMID 16698895.
Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems. Microbiol. Rev., 1 March 1980, s. 83–105. DOI: 10.1128/MMBR.44.1.83-105.1980. PMID 6997723.
Structural and functional properties of NAD kinase, a key enzyme in NADP biosynthesis. Mini Reviews in Medicinal Chemistry, 2006, s. 739–46. DOI: 10.2174/138955706777698688. PMID 16842123.
First Archaeal Inorganic Polyphosphate/ATP-Dependent NAD Kinase, from Hyperthermophilic Archaeon Pyrococcus horikoshii: Cloning, Expression, and Characterization. Appl. Environ. Microbiol., 2005, s. 4352–8. DOI: 10.1128/AEM.71.8.4352-4358.2005. PMID 16085824.
Characterization of Mycobacterium tuberculosis NAD kinase: functional analysis of the full-length enzyme by site-directed mutagenesis. Biochemistry, 2004, s. 7610–7. DOI: 10.1021/bi049650w. PMID 15182203.
Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels. J. Biol. Chem., 2002, s. 18881–90. DOI: 10.1074/jbc.M111773200. PMID 11884393.
Nicotinamide riboside is uniquely and orally bioavailable in mice and humans. Nature Communications, 2016, s. 12948. DOI: 10.1038/ncomms12948. PMID 27721479.
Crystallization of three key glycolytic enzymes of the opportunistic pathogen Cryptosporidium parvum. Biochim. Biophys. Acta, 2005, s. 166–72. DOI: 10.1016/j.bbapap.2005.04.009. PMID 15953771.
Release of beta-nicotinamide adenine dinucleotide upon stimulation of postganglionic nerve terminals in blood vessels and urinary bladder. J Biol Chem, 2004, s. 48893–903. DOI: 10.1074/jbc.M407266200. PMID 15364945.
Crystal structures of Delta1-piperideine-2-carboxylate/Delta1-pyrroline-2-carboxylate reductase belonging to a new family of NAD(P)H-dependent oxidoreductases: conformational change, substrate recognition, and stereochemistry of the reaction. J. Biol. Chem., 2005, s. 40875–84. DOI: 10.1074/jbc.M507399200. PMID 16192274.
Bellamacina CR. The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins. FASEB J., 1 September 1996, s. 1257–69. DOI: 10.1096/fasebj.10.11.8836039. PMID 8836039.
Biochemical and genetic analysis of methylenetetrahydrofolate reductase in Leishmania metabolism and virulence. J. Biol. Chem., 2006, s. 38150–8. DOI: 10.1074/jbc.M608387200. PMID 17032644.
Oxygen Is the High-Energy Molecule Powering Complex Multicellular Life: Fundamental Corrections to Traditional Bioenergetics. ACS Omega, 2020, s. 2221–2233. DOI: 10.1021/acsomega.9b03352. PMID 32064383.
The interaction between the cytosolic pyridine nucleotide redox potential and gluconeogenesis from lactate/pyruvate in isolated rat hepatocytes. Implications for investigations of hormone action. J. Biol. Chem., 15 October 1985, s. 12748–53. Dostupné online. DOI: 10.1016/S0021-9258(17)38940-8. PMID 4044607. Archivované 2008-04-12 na Wayback Machine
Ecto-ADP-ribosyltransferases (ARTs): emerging actors in cell communication and signaling. Curr. Med. Chem., 2004, s. 857–72. DOI: 10.2174/0929867043455611. PMID 15078170.
Guse AH. Biochemistry, biology, and pharmacology of cyclic adenosine diphosphoribose (cADPR). Curr. Med. Chem., 2004, s. 847–55. DOI: 10.2174/0929867043455602. PMID 15078169.
Guse AH. Regulation of calcium signaling by the second messenger cyclic adenosine diphosphoribose (cADPR). Curr. Mol. Med., 2004, s. 239–48. DOI: 10.2174/1566524043360771. PMID 15101682.
Guse AH. Second messenger function and the structure-activity relationship of cyclic adenosine diphosphoribose (cADPR). FEBS J., 2005, s. 4590–7. DOI: 10.1111/j.1742-4658.2005.04863.x. PMID 16156781.
A newly identified DNA ligase of Saccharomyces cerevisiae involved in RAD52-independent repair of DNA double-strand breaks. Genes & Development, 1997, s. 1912–24. DOI: 10.1101/gad.11.15.1912. PMID 9271115.
A conserved NAD binding pocket that regulates protein-protein interactions during aging. Science, 23 March 2017, s. 1312–1317. DOI: 10.1126/science.aad8242. PMID 28336669.
Beta-nicotinamide adenine dinucleotide is an inhibitory neurotransmitter in visceral smooth muscle. Proc. Natl. Acad. Sci. U.S.A., 2007, s. 16359–64. DOI: 10.1073/pnas.0705510104. PMID 17913880.
β-nicotinamide adenine dinucleotide is an enteric inhibitory neurotransmitter in human and nonhuman primate colons. Gastroenterology, 2011, s. 608–617.e6. DOI: 10.1053/j.gastro.2010.09.039. PMID 20875415.
Storage and secretion of beta-NAD, ATP and dopamine in NGF-differentiated rat pheochromocytoma PC12 cells. Eur. J. Neurosci., 2009, s. 756–68. DOI: 10.1111/j.1460-9568.2009.06869.x. PMID 19712094.
Release, neuronal effects and removal of extracellular β-nicotinamide adenine dinucleotide (β-NAD+) in the rat brain. Eur. J. Neurosci., 2012, s. 423–35. DOI: 10.1111/j.1460-9568.2011.07957.x. PMID 22276961.
A lectin receptor kinase as a potential sensor for extracellular nicotinamide adenine dinucleotide in Arabidopsis thaliana. eLife, 2017, s. e25474. DOI: 10.7554/eLife.25474. PMID 28722654.
Sauve AA. NAD+ and vitamin B3: from metabolism to therapies. The Journal of Pharmacology and Experimental Therapeutics, March 2008, s. 883–93. DOI: 10.1124/jpet.107.120758. PMID 18165311.
Nicotinamide adenine dinucleotide metabolism as an attractive target for drug discovery. Expert Opin. Ther. Targets, 2007, s. 695–705. DOI: 10.1517/14728222.11.5.695. PMID 17465726.
The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: Adduct affinity and drug resistance. Proc. Natl. Acad. Sci. U.S.A., 2003, s. 13881–6. DOI: 10.1073/pnas.2235848100. PMID 14623976.
Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid. Nat. Struct. Mol. Biol., 2006, s. 408–13. DOI: 10.1038/nsmb1089. PMID 16648861.
Cofactor mimics as selective inhibitors of NAD-dependent inosine monophosphate dehydrogenase (IMPDH)—the major therapeutic target. Curr. Med. Chem., 2004, s. 887–900. DOI: 10.2174/0929867043455648. PMID 15083807.
Resveratrol prolongs lifespan and retards the onset of age-related markers in a short-lived vertebrate. Curr. Biol., 2006, s. 296–300. DOI: 10.1016/j.cub.2005.12.038. PMID 16461283.
Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature, 2003, s. 191–6. DOI: 10.1038/nature01960. PMID 12939617.
Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature, 2004, s. 686–9. DOI: 10.1038/nature02789. PMID 15254550.
Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging. Cell, 19 December 2013, s. 1624–1638. DOI: 10.1016/j.cell.2013.11.037. PMID 24360282.
The alcoholic ferment of yeast-juice Part II.--The coferment of yeast-juice. Proceedings of the Royal Society of London, 24 October 1906, s. 369–375. DOI: 10.1098/rspb.1906.0070.
Pyridin, der wasserstoffübertragende bestandteil von gärungsfermenten (pyridin-nucleotide). Biochemische Zeitschrift, 1936, s. 291. DOI: 10.1002/hlca.193601901199. (po nemecky)
Bieganowski, P; Brenner, C. Discoveries of Nicotinamide Riboside as a Nutrient and Conserved NRK Genes Establish a Preiss-Handler Independent Route to NAD+ in Fungi and Humans. Cell, 2004, s. 495–502. DOI: 10.1016/S0092-8674(04)00416-7. PMID 15137942.
Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesizing nuclear enzyme. Biochem. Biophys. Res. Commun., 1963, s. 39–43. DOI: 10.1016/0006-291X(63)90024-X. PMID 14019961.
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature, 2000, s. 795–800. DOI: 10.1038/35001622. PMID 10693811.
NiceZyme View of ENZYME: EC 1.6.5.3 [online]. Expasy. Dostupné online.
jbc.org
The interaction between the cytosolic pyridine nucleotide redox potential and gluconeogenesis from lactate/pyruvate in isolated rat hepatocytes. Implications for investigations of hormone action. J. Biol. Chem., 15 October 1985, s. 12748–53. Dostupné online. DOI: 10.1016/S0021-9258(17)38940-8. PMID 4044607. Archivované 2008-04-12 na Wayback Machine
The power to reduce: pyridine nucleotides – small molecules with a multitude of functions. Biochem. J., 2007, s. 205–18. DOI: 10.1042/BJ20061638. PMID 17295611.
Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim. Biophys. Acta, 1997, s. 217–34. DOI: 10.1016/S0005-2728(97)00034-0. PMID 9230919.
Structure of lactate dehydrogenase inhibitor generated from coenzyme. Biochemistry, 1979, s. 1212–7. DOI: 10.1021/bi00574a015. PMID 218616.
Fluorescence lifetime imaging of free and protein-bound NADH. Proc. Natl. Acad. Sci. U.S.A., 1992, s. 1271–5. DOI: 10.1073/pnas.89.4.1271. PMID 1741380.
Time-resolved fluorescence studies on NADH bound to mitochondrial malate dehydrogenase. Biochim. Biophys. Acta, 1989, s. 187–90. DOI: 10.1016/0167-4838(89)90159-3. PMID 2910350.
The Free NADH Concentration Is Kept Constant in Plant Mitochondria under Different Metabolic Conditions. Plant Cell, 2006, s. 688–98. DOI: 10.1105/tpc.105.039354. PMID 16461578.
Measurement of tissue purine, pyrimidine, and other nucleotides by radial compression high-performance liquid chromatography. Anal. Biochem., 1984, s. 162–71. DOI: 10.1016/0003-2697(84)90148-9. PMID 6486402.
The simultaneous measurement of nicotinamide adenine dinucleotide and related compounds by liquid chromatography/electrospray ionization tandem mass spectrometry. Anal. Biochem., 2006, s. 282–5. DOI: 10.1016/j.ab.2006.02.017. PMID 16574057.
Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+. Cell, 2007, s. 473–84. DOI: 10.1016/j.cell.2007.03.024. PMID 17482543.
Distribution of mitochondrial NADH fluorescence lifetimes: steady-state kinetics of matrix NADH interactions. Biochemistry, 2005, s. 2585–94. DOI: 10.1021/bi0485124. PMID 15709771.
Identification of the mitochondrial NAD+ transporter in Saccharomyces cerevisiae. J. Biol. Chem., 2006, s. 1524–31. DOI: 10.1074/jbc.M510425200. PMID 16291748.
Srivastava S. Emerging therapeutic roles for NAD(+) metabolism in mitochondrial and age-related disorders. Clinical and Translational Medicine, 2016, s. 25. DOI: 10.1186/s40169-016-0104-7. PMID 27465020.
Regulatory Effects of NAD + Metabolic Pathways on Sirtuin Activity. Progress in Molecular Biology and Translational Science, 2018, s. 71–104. DOI: 10.1016/bs.pmbts.2017.11.012. PMID 29413178.
Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med, 2001, s. 1191–212. DOI: 10.1016/S0891-5849(01)00480-4. PMID 11368918.
The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem. J., 1967, s. 514–27. DOI: 10.1042/bj1030514. PMID 4291787.
Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease. Curr. Opin. Cell Biol., April 2003, s. 241–6. DOI: 10.1016/S0955-0674(03)00006-1. PMID 12648681.
The redox state of free nicotinamide–adenine dinucleotide phosphate in the cytoplasm of rat liver. Biochem. J., 1969, s. 609–19. DOI: 10.1042/bj1150609a. PMID 4391039.
Early Steps in the Biosynthesis of NAD in Arabidopsis Start with Aspartate and Occur in the Plastid. Plant Physiol., 2006, s. 851–7. DOI: 10.1104/pp.106.081091. PMID 16698895.
Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems. Microbiol. Rev., 1 March 1980, s. 83–105. DOI: 10.1128/MMBR.44.1.83-105.1980. PMID 6997723.
Structural and functional properties of NAD kinase, a key enzyme in NADP biosynthesis. Mini Reviews in Medicinal Chemistry, 2006, s. 739–46. DOI: 10.2174/138955706777698688. PMID 16842123.
First Archaeal Inorganic Polyphosphate/ATP-Dependent NAD Kinase, from Hyperthermophilic Archaeon Pyrococcus horikoshii: Cloning, Expression, and Characterization. Appl. Environ. Microbiol., 2005, s. 4352–8. DOI: 10.1128/AEM.71.8.4352-4358.2005. PMID 16085824.
Characterization of Mycobacterium tuberculosis NAD kinase: functional analysis of the full-length enzyme by site-directed mutagenesis. Biochemistry, 2004, s. 7610–7. DOI: 10.1021/bi049650w. PMID 15182203.
Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels. J. Biol. Chem., 2002, s. 18881–90. DOI: 10.1074/jbc.M111773200. PMID 11884393.
Nicotinamide riboside is uniquely and orally bioavailable in mice and humans. Nature Communications, 2016, s. 12948. DOI: 10.1038/ncomms12948. PMID 27721479.
Crystallization of three key glycolytic enzymes of the opportunistic pathogen Cryptosporidium parvum. Biochim. Biophys. Acta, 2005, s. 166–72. DOI: 10.1016/j.bbapap.2005.04.009. PMID 15953771.
Release of beta-nicotinamide adenine dinucleotide upon stimulation of postganglionic nerve terminals in blood vessels and urinary bladder. J Biol Chem, 2004, s. 48893–903. DOI: 10.1074/jbc.M407266200. PMID 15364945.
Crystal structures of Delta1-piperideine-2-carboxylate/Delta1-pyrroline-2-carboxylate reductase belonging to a new family of NAD(P)H-dependent oxidoreductases: conformational change, substrate recognition, and stereochemistry of the reaction. J. Biol. Chem., 2005, s. 40875–84. DOI: 10.1074/jbc.M507399200. PMID 16192274.
Bellamacina CR. The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins. FASEB J., 1 September 1996, s. 1257–69. DOI: 10.1096/fasebj.10.11.8836039. PMID 8836039.
Biochemical and genetic analysis of methylenetetrahydrofolate reductase in Leishmania metabolism and virulence. J. Biol. Chem., 2006, s. 38150–8. DOI: 10.1074/jbc.M608387200. PMID 17032644.
Oxygen Is the High-Energy Molecule Powering Complex Multicellular Life: Fundamental Corrections to Traditional Bioenergetics. ACS Omega, 2020, s. 2221–2233. DOI: 10.1021/acsomega.9b03352. PMID 32064383.
The interaction between the cytosolic pyridine nucleotide redox potential and gluconeogenesis from lactate/pyruvate in isolated rat hepatocytes. Implications for investigations of hormone action. J. Biol. Chem., 15 October 1985, s. 12748–53. Dostupné online. DOI: 10.1016/S0021-9258(17)38940-8. PMID 4044607. Archivované 2008-04-12 na Wayback Machine
Genome Sequence of the Chemolithoautotrophic Nitrite-Oxidizing Bacterium Nitrobacter winogradskyi Nb-255. Appl. Environ. Microbiol., 2006, s. 2050–63. DOI: 10.1128/AEM.72.3.2050-2063.2006. PMID 16517654.
Ecto-ADP-ribosyltransferases (ARTs): emerging actors in cell communication and signaling. Curr. Med. Chem., 2004, s. 857–72. DOI: 10.2174/0929867043455611. PMID 15078170.
Guse AH. Biochemistry, biology, and pharmacology of cyclic adenosine diphosphoribose (cADPR). Curr. Med. Chem., 2004, s. 847–55. DOI: 10.2174/0929867043455602. PMID 15078169.
Guse AH. Regulation of calcium signaling by the second messenger cyclic adenosine diphosphoribose (cADPR). Curr. Mol. Med., 2004, s. 239–48. DOI: 10.2174/1566524043360771. PMID 15101682.
Guse AH. Second messenger function and the structure-activity relationship of cyclic adenosine diphosphoribose (cADPR). FEBS J., 2005, s. 4590–7. DOI: 10.1111/j.1742-4658.2005.04863.x. PMID 16156781.
A newly identified DNA ligase of Saccharomyces cerevisiae involved in RAD52-independent repair of DNA double-strand breaks. Genes & Development, 1997, s. 1912–24. DOI: 10.1101/gad.11.15.1912. PMID 9271115.
A conserved NAD binding pocket that regulates protein-protein interactions during aging. Science, 23 March 2017, s. 1312–1317. DOI: 10.1126/science.aad8242. PMID 28336669.
Beta-nicotinamide adenine dinucleotide is an inhibitory neurotransmitter in visceral smooth muscle. Proc. Natl. Acad. Sci. U.S.A., 2007, s. 16359–64. DOI: 10.1073/pnas.0705510104. PMID 17913880.
β-nicotinamide adenine dinucleotide is an enteric inhibitory neurotransmitter in human and nonhuman primate colons. Gastroenterology, 2011, s. 608–617.e6. DOI: 10.1053/j.gastro.2010.09.039. PMID 20875415.
Storage and secretion of beta-NAD, ATP and dopamine in NGF-differentiated rat pheochromocytoma PC12 cells. Eur. J. Neurosci., 2009, s. 756–68. DOI: 10.1111/j.1460-9568.2009.06869.x. PMID 19712094.
Release, neuronal effects and removal of extracellular β-nicotinamide adenine dinucleotide (β-NAD+) in the rat brain. Eur. J. Neurosci., 2012, s. 423–35. DOI: 10.1111/j.1460-9568.2011.07957.x. PMID 22276961.
A lectin receptor kinase as a potential sensor for extracellular nicotinamide adenine dinucleotide in Arabidopsis thaliana. eLife, 2017, s. e25474. DOI: 10.7554/eLife.25474. PMID 28722654.
Sauve AA. NAD+ and vitamin B3: from metabolism to therapies. The Journal of Pharmacology and Experimental Therapeutics, March 2008, s. 883–93. DOI: 10.1124/jpet.107.120758. PMID 18165311.
Nicotinamide adenine dinucleotide metabolism as an attractive target for drug discovery. Expert Opin. Ther. Targets, 2007, s. 695–705. DOI: 10.1517/14728222.11.5.695. PMID 17465726.
The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: Adduct affinity and drug resistance. Proc. Natl. Acad. Sci. U.S.A., 2003, s. 13881–6. DOI: 10.1073/pnas.2235848100. PMID 14623976.
Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid. Nat. Struct. Mol. Biol., 2006, s. 408–13. DOI: 10.1038/nsmb1089. PMID 16648861.
Cofactor mimics as selective inhibitors of NAD-dependent inosine monophosphate dehydrogenase (IMPDH)—the major therapeutic target. Curr. Med. Chem., 2004, s. 887–900. DOI: 10.2174/0929867043455648. PMID 15083807.
Nucleoside and non-nucleoside IMP dehydrogenase inhibitors as antitumor and antiviral agents. Curr. Med. Chem., 1999, s. 599–614. PMID 10390603.
Resveratrol prolongs lifespan and retards the onset of age-related markers in a short-lived vertebrate. Curr. Biol., 2006, s. 296–300. DOI: 10.1016/j.cub.2005.12.038. PMID 16461283.
Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature, 2003, s. 191–6. DOI: 10.1038/nature01960. PMID 12939617.
Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature, 2004, s. 686–9. DOI: 10.1038/nature02789. PMID 15254550.
Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging. Cell, 19 December 2013, s. 1624–1638. DOI: 10.1016/j.cell.2013.11.037. PMID 24360282.
Bieganowski, P; Brenner, C. Discoveries of Nicotinamide Riboside as a Nutrient and Conserved NRK Genes Establish a Preiss-Handler Independent Route to NAD+ in Fungi and Humans. Cell, 2004, s. 495–502. DOI: 10.1016/S0092-8674(04)00416-7. PMID 15137942.
Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesizing nuclear enzyme. Biochem. Biophys. Res. Commun., 1963, s. 39–43. DOI: 10.1016/0006-291X(63)90024-X. PMID 14019961.
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature, 2000, s. 795–800. DOI: 10.1038/35001622. PMID 10693811.
Fermentation of sugars and fermentative enzymes [online]. Nobel Foundation. Dostupné online. Archivované 2007-09-27 z originálu.
qmul.ac.uk
chem.qmul.ac.uk
Enzyme Nomenclature, Recommendations for enzyme names from the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology [online]. . Dostupné online. Archivované 2007-12-05 z originálu.
Enzyme Nomenclature, Recommendations for enzyme names from the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology [online]. . Dostupné online. Archivované 2007-12-05 z originálu.
The interaction between the cytosolic pyridine nucleotide redox potential and gluconeogenesis from lactate/pyruvate in isolated rat hepatocytes. Implications for investigations of hormone action. J. Biol. Chem., 15 October 1985, s. 12748–53. Dostupné online. DOI: 10.1016/S0021-9258(17)38940-8. PMID 4044607. Archivované 2008-04-12 na Wayback Machine
