CD38 NAD NADH metabolic agingNAD and ADNAD usesNAD and agingNAD and redox resveratrol and agingNAD - less as we age - metabolism and agingReferences

  1. ^ Jump up to: a b c Pollak N, Dölle C, Ziegler M (2007). “The power to reduce: pyridine nucleotides – small molecules with a multitude of functions”. Biochem. J. 402 (2): 205–18. doi:10.1042/BJ20061638. PMC 1798440. PMID 17295611. 
  2. ^ Jump up to: a b c d e f Belenky P, Bogan KL, Brenner C (2007). “NAD+ metabolism in health and disease” (PDF). Trends Biochem. Sci. 32 (1): 12–9. doi:10.1016/j.tibs.2006.11.006. PMID 17161604. Retrieved 2007-12-23. 
  3. Jump up ^ Unden G, Bongaerts J (1997). “Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors”. Biochim. Biophys. Acta 1320 (3): 217–34. doi:10.1016/S0005-2728(97)00034-0. PMID 9230919. 
  4. Jump up ^ Windholz, Martha (1983). The Merck Index: an encyclopedia of chemicals, drugs, and biologicals (10th ed.). Rahway NJ, US: Merck. p. 909. ISBN 0-911910-27-1. 
  5. Jump up ^ Biellmann JF, Lapinte C, Haid E, Weimann G (1979). “Structure of lactate dehydrogenase inhibitor generated from coenzyme”. Biochemistry 18 (7): 1212–7. doi:10.1021/bi00574a015. PMID 218616. 
  6. ^ Jump up to: a b Dawson, R. Ben (1985). Data for biochemical research (3rd ed.). Oxford: Clarendon Press. p. 122. ISBN 0-19-855358-7. 
  7. ^ Jump up to: a b Lakowicz JR, Szmacinski H, Nowaczyk K, Johnson ML (1992). “Fluorescence lifetime imaging of free and protein-bound NADH”. Proc. Natl. Acad. Sci. U.S.A. 89 (4): 1271–5. Bibcode:1992PNAS…89.1271L. doi:10.1073/pnas.89.4.1271. PMC 48431. PMID 1741380. 
  8. Jump up ^ Jameson DM, Thomas V, Zhou DM (1989). “Time-resolved fluorescence studies on NADH bound to mitochondrial malate dehydrogenase”. Biochim. Biophys. Acta 994 (2): 187–90. doi:10.1016/0167-4838(89)90159-3. PMID 2910350. 
  9. Jump up ^ Kasimova MR, Grigiene J, Krab K, Hagedorn PH, Flyvbjerg H, Andersen PE, Møller IM (2006). “The Free NADH Concentration Is Kept Constant in Plant Mitochondria under Different Metabolic Conditions”. Plant Cell 18 (3): 688–98. doi:10.1105/tpc.105.039354. PMC 1383643. PMID 16461578. 
  10. Jump up ^ Reiss PD, Zuurendonk PF, Veech RL (1984). “Measurement of tissue purine, pyrimidine, and other nucleotides by radial compression high-performance liquid chromatography”. Anal. Biochem. 140 (1): 162–71. doi:10.1016/0003-2697(84)90148-9. PMID 6486402. 
  11. Jump up ^ Yamada K, Hara N, Shibata T, Osago H, Tsuchiya M (2006). “The simultaneous measurement of nicotinamide adenine dinucleotide and related compounds by liquid chromatography/electrospray ionization tandem mass spectrometry”. Anal. Biochem. 352 (2): 282–5. doi:10.1016/j.ab.2006.02.017. PMID 16574057. 
  12. ^ Jump up to: a b Yang H, Yang T, Baur JA, Perez E, Matsui T, Carmona JJ, Lamming DW, Souza-Pinto NC, Bohr VA, Rosenzweig A, de Cabo R, Sauve AA, Sinclair DA (2007). “Nutrient-Sensitive Mitochondrial NAD+ Levels Dictate Cell Survival”. Cell 130 (6): 1095–107. doi:10.1016/j.cell.2007.07.035. PMC 3366687. PMID 17889652. 
  13. Jump up ^ Belenky P, Racette FG, Bogan KL, McClure JM, Smith JS, Brenner C (2007). “Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+“. Cell 129 (3): 473–84. doi:10.1016/j.cell.2007.03.024. PMID 17482543. 
  14. Jump up ^ Blinova K, Carroll S, Bose S, Smirnov AV, Harvey JJ, Knutson JR, Balaban RS (2005). “Distribution of mitochondrial NADH fluorescence lifetimes: steady-state kinetics of matrix NADH interactions”. Biochemistry 44 (7): 2585–94. doi:10.1021/bi0485124. PMID 15709771. 
  15. Jump up ^ Todisco S, Agrimi G, Castegna A, Palmieri F (2006). “Identification of the mitochondrial NAD+ transporter in Saccharomyces cerevisiae“. J. Biol. Chem. 281 (3): 1524–31. doi:10.1074/jbc.M510425200. PMID 16291748. 
  16. Jump up ^ Schafer FQ, Buettner GR (2001). “Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple”. Free Radic Biol Med 30 (11): 1191–212. doi:10.1016/S0891-5849(01)00480-4. PMID 11368918. 
  17. Jump up ^ Williamson DH, Lund P, Krebs HA (1967). “The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver”. Biochem. J. 103 (2): 514–27. PMC 1270436. PMID 4291787. 
  18. Jump up ^ Zhang Q, Piston DW, Goodman RH (2002). “Regulation of corepressor function by nuclear NADH”. Science 295 (5561): 1895–7. doi:10.1126/science.1069300. PMID 11847309. 
  19. Jump up ^ Lin SJ, Guarente L (April 2003). “Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease”. Curr. Opin. Cell Biol. 15 (2): 241–6. doi:10.1016/S0955-0674(03)00006-1. PMID 12648681. 
  20. Jump up ^ Veech RL, Eggleston LV, Krebs HA (1969). “The redox state of free nicotinamide–adenine dinucleotide phosphate in the cytoplasm of rat liver”. Biochem. J. 115 (4): 609–19. PMC 1185185. PMID 4391039. 
  21. Jump up ^ Katoh A, Uenohara K, Akita M, Hashimoto T (2006). “Early Steps in the Biosynthesis of NAD in Arabidopsis Start with Aspartate and Occur in the Plastid”. Plant Physiol. 141 (3): 851–7. doi:10.1104/pp.106.081091. PMC 1489895. PMID 16698895. 
  22. Jump up ^ Foster JW, Moat AG (1 March 1980). “Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems”. Microbiol. Rev. 44 (1): 83–105. PMC 373235. PMID 6997723. 
  23. Jump up ^ Magni G, Orsomando G, Raffaelli N (2006). “Structural and functional properties of NAD kinase, a key enzyme in NADP biosynthesis”. Mini reviews in medicinal chemistry 6 (7): 739–46. doi:10.2174/138955706777698688. PMID 16842123. 
  24. Jump up ^ Sakuraba H, Kawakami R, Ohshima T (2005). “First Archaeal Inorganic Polyphosphate/ATP-Dependent NAD Kinase, from Hyperthermophilic Archaeon Pyrococcus horikoshii: Cloning, Expression, and Characterization”. Appl. Environ. Microbiol. 71 (8): 4352–8. doi:10.1128/AEM.71.8.4352-4358.2005. PMC 1183369. PMID 16085824. 
  25. Jump up ^ Raffaelli N, Finaurini L, Mazzola F, Pucci L, Sorci L, Amici A, Magni G (2004). “Characterization of Mycobacterium tuberculosis NAD kinase: functional analysis of the full-length enzyme by site-directed mutagenesis”. Biochemistry 43 (23): 7610–7. doi:10.1021/bi049650w. PMID 15182203. 
  26. Jump up ^ Anderson RM, Bitterman KJ, Wood JG, Medvedik O, Cohen H, Lin SS, Manchester JK, Gordon JI, Sinclair DA (2002). “Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels”. J. Biol. Chem. 277 (21): 18881–90. doi:10.1074/jbc.M111773200. PMID 11884393. 
  27. Jump up ^ Billington RA, Travelli C, Ercolano E, Galli U, Roman CB, Grolla AA, Canonico PL, Condorelli F, Genazzani AA (2008). “Characterization of NAD Uptake in Mammalian Cells”. J. Biol. Chem. 283 (10): 6367–74. doi:10.1074/jbc.M706204200. PMID 18180302. 
  28. Jump up ^ Henderson LM (1983). “Niacin”. Annu. Rev. Nutr. 3: 289–307. doi:10.1146/annurev.nu.03.070183.001445. PMID 6357238. 
  29. ^ Jump up to: a b Rongvaux A, Andris F, Van Gool F, Leo O (2003). “Reconstructing eukaryotic NAD metabolism”. BioEssays 25 (7): 683–90. doi:10.1002/bies.10297. PMID 12815723. 
  30. Jump up ^ Ma B, Pan SJ, Zupancic ML, Cormack BP (2007). “Assimilation of NAD+ precursors in Candida glabrata“. Mol. Microbiol. 66 (1): 14–25. doi:10.1111/j.1365-2958.2007.05886.x. PMID 17725566. 
  31. Jump up ^ Reidl J, Schlör S, Kraiss A, Schmidt-Brauns J, Kemmer G, Soleva E (2000). “NADP and NAD utilization in Haemophilus influenzae“. Mol. Microbiol. 35 (6): 1573–81. doi:10.1046/j.1365-2958.2000.01829.x. PMID 10760156. 
  32. Jump up ^ Gerdes SY, Scholle MD, D’Souza M, Bernal A, Baev MV, Farrell M, Kurnasov OV, Daugherty MD, Mseeh F, Polanuyer BM, Campbell JW, Anantha S, Shatalin KY, Chowdhury SA, Fonstein MY, Osterman AL (2002). “From Genetic Footprinting to Antimicrobial Drug Targets: Examples in Cofactor Biosynthetic Pathways”. J. Bacteriol. 184 (16): 4555–72. doi:10.1128/JB.184.16.4555-4572.2002. PMC 135229. PMID 12142426. 
  33. Jump up ^ Senkovich O, Speed H, Grigorian A, et al. (2005). “Crystallization of three key glycolytic enzymes of the opportunistic pathogen Cryptosporidium parvum“. Biochim. Biophys. Acta 1750 (2): 166–72. doi:10.1016/j.bbapap.2005.04.009. PMID 15953771. 
  34. ^ Jump up to: a b c Smyth LM, Bobalova J, Mendoza MG, Lew C, Mutafova-Yambolieva VN (2004). “Release of beta-nicotinamide adenine dinucleotide upon stimulation of postganglionic nerve terminals in blood vessels and urinary bladder”. J Biol Chem. 279 (47): 48893–903. doi:10.1074/jbc.M407266200. PMID 15364945. 
  35. ^ Jump up to: a b c Billington RA, Bruzzone S, De Flora A, Genazzani AA, Koch-Nolte F, Ziegler M, Zocchi E (2006). “Emerging functions of extracellular pyridine nucleotides”. Mol Med. 12 (11–12): 324–7. doi:10.2119/2006-00075.Billington. PMC 1829198. PMID 17380199. 
  36. Jump up ^ “Enzyme Nomenclature, Recommendations for enzyme names from the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology”. Retrieved 2007-12-06. 
  37. Jump up ^ “NiceZyme View of ENZYME: EC 1.6.5.3”. Expasy. Retrieved 2007-12-16. 
  38. Jump up ^ Lesk AM (1995). “NAD-binding domains of dehydrogenases”. Curr. Opin. Struct. Biol. 5 (6): 775–83. doi:10.1016/0959-440X(95)80010-7. PMID 8749365. 
  39. ^ Jump up to: a b Rao ST, Rossmann MG (1973). “Comparison of super-secondary structures in proteins”. J Mol Biol 76 (2): 241–56. doi:10.1016/0022-2836(73)90388-4. PMID 4737475. 
  40. Jump up ^ Goto M, Muramatsu H, Mihara H, Kurihara T, Esaki N, Omi R, Miyahara I, Hirotsu K (2005). “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. 280 (49): 40875–84. doi:10.1074/jbc.M507399200. PMID 16192274. 
  41. ^ Jump up to: a b Bellamacina CR (1 September 1996). “The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins”. FASEB J. 10 (11): 1257–69. PMID 8836039. 
  42. Jump up ^ Carugo O, Argos P (1997). “NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding”. Proteins 28 (1): 10–28. doi:10.1002/(SICI)1097-0134(199705)28:1<10::AID-PROT2>3.0.CO;2-N. PMID 9144787. 
  43. Jump up ^ Vickers TJ, Orsomando G, de la Garza RD, Scott DA, Kang SO, Hanson AD, Beverley SM (2006). “Biochemical and genetic analysis of methylenetetrahydrofolate reductase in Leishmania metabolism and virulence”. J. Biol. Chem. 281 (50): 38150–8. doi:10.1074/jbc.M608387200. PMID 17032644. 
  44. Jump up ^ Bakker BM, Overkamp KM, Kötter P, Luttik MA, Pronk JT (2001). “Stoichiometry and compartmentation of NADH metabolism in Saccharomyces cerevisiae“. FEMS Microbiol. Rev. 25 (1): 15–37. doi:10.1111/j.1574-6976.2001.tb00570.x. PMID 11152939. 
  45. Jump up ^ Rich PR (2003). “The molecular machinery of Keilin’s respiratory chain”. Biochem. Soc. Trans. 31 (Pt 6): 1095–105. doi:10.1042/BST0311095. PMID 14641005. 
  46. Jump up ^ Heineke D, Riens B, Grosse H, Hoferichter P, Peter U, Flügge UI, Heldt HW (1991). “Redox Transfer across the Inner Chloroplast Envelope Membrane”. Plant Physiol 95 (4): 1131–1137. doi:10.1104/pp.95.4.1131. PMC 1077662. PMID 16668101. 
  47. ^ Jump up to: a b Nicholls DG; Ferguson SJ (2002). Bioenergetics 3 (1st ed.). Academic Press. ISBN 0-12-518121-3. 
  48. Jump up ^ Sistare FD, Haynes RC (15 October 1985). “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. 260 (23): 12748–53. PMID 4044607. 
  49. Jump up ^ Freitag A, Bock E (1990). “Energy conservation in Nitrobacter“. FEMS Microbiology Letters 66 (1–3): 157–62. doi:10.1111/j.1574-6968.1990.tb03989.x. 
  50. Jump up ^ Starkenburg SR, Chain PS, Sayavedra-Soto LA, Hauser L, Land ML, Larimer FW, Malfatti SA, Klotz MG, Bottomley PJ, Arp DJ, Hickey WJ (2006). “Genome Sequence of the Chemolithoautotrophic Nitrite-Oxidizing Bacterium Nitrobacter winogradskyi Nb-255″. Appl. Environ. Microbiol. 72 (3): 2050–63. doi:10.1128/AEM.72.3.2050-2063.2006. PMC 1393235. PMID 16517654. 
  51. Jump up ^ Ziegler M (2000). “New functions of a long-known molecule. Emerging roles of NAD in cellular signaling”. Eur. J. Biochem. 267 (6): 1550–64. doi:10.1046/j.1432-1327.2000.01187.x. PMID 10712584. 
  52. ^ Jump up to: a b Diefenbach J, Bürkle A (2005). “Introduction to poly(ADP-ribose) metabolism”. Cell. Mol. Life Sci. 62 (7–8): 721–30. doi:10.1007/s00018-004-4503-3. PMID 15868397. 
  53. Jump up ^ Berger F, Ramírez-Hernández MH, Ziegler M (2004). “The new life of a centenarian: signaling functions of NAD(P)”. Trends Biochem. Sci. 29 (3): 111–8. doi:10.1016/j.tibs.2004.01.007. PMID 15003268. 
  54. Jump up ^ Corda D, Di Girolamo M (2003). “New Embo Member’s Review: Functional aspects of protein mono-ADP-ribosylation”. EMBO J. 22 (9): 1953–8. doi:10.1093/emboj/cdg209. PMC 156081. PMID 12727863. 
  55. ^ Jump up to: a b Bürkle A (2005). “Poly(ADP-ribose). The most elaborate metabolite of NAD+“. FEBS J. 272 (18): 4576–89. doi:10.1111/j.1742-4658.2005.04864.x. PMID 16156780. 
  56. Jump up ^ Seman M, Adriouch S, Haag F, Koch-Nolte F (2004). “Ecto-ADP-ribosyltransferases (ARTs): emerging actors in cell communication and signaling”. Curr. Med. Chem. 11 (7): 857–72. doi:10.2174/0929867043455611. PMID 15078170. 
  57. Jump up ^ Chen YG, Kowtoniuk WE, Agarwal I, Shen Y, Liu DR (December 2009). “LC/MS analysis of cellular RNA reveals NAD-linked RNA”. Nat Chem Biol 5 (12): 879–881. doi:10.1038/nchembio.235. PMC 2842606. PMID 19820715. 
  58. Jump up ^ Guse AH (2004). “Biochemistry, biology, and pharmacology of cyclic adenosine diphosphoribose (cADPR)”. Curr. Med. Chem. 11 (7): 847–55. doi:10.2174/0929867043455602. PMID 15078169. 
  59. Jump up ^ Guse AH (2004). “Regulation of calcium signaling by the second messenger cyclic adenosine diphosphoribose (cADPR)”. Curr. Mol. Med. 4 (3): 239–48. doi:10.2174/1566524043360771. PMID 15101682. 
  60. Jump up ^ Guse AH (2005). “Second messenger function and the structure-activity relationship of cyclic adenosine diphosphoribose (cADPR)”. FEBS J. 272 (18): 4590–7. doi:10.1111/j.1742-4658.2005.04863.x. PMID 16156781. 
  61. Jump up ^ North BJ, Verdin E (2004). “Sirtuins: Sir2-related NAD-dependent protein deacetylases”. Genome Biol 5 (5): 224. doi:10.1186/gb-2004-5-5-224. PMC 416462. PMID 15128440. 
  62. Jump up ^ Blander G, Guarente L (2004). “The Sir2 family of protein deacetylases”. Annu. Rev. Biochem. 73: 417–35. doi:10.1146/annurev.biochem.73.011303.073651. PMID 15189148. 
  63. Jump up ^ Trapp J, Jung M (2006). “The role of NAD+ dependent histone deacetylases (sirtuins) in ageing”. Curr Drug Targets 7 (11): 1553–60. doi:10.2174/1389450110607011553. PMID 17100594. 
  64. Jump up ^ Wilkinson A, Day J, Bowater R (2001). “Bacterial DNA ligases”. Mol. Microbiol. 40 (6): 1241–8. doi:10.1046/j.1365-2958.2001.02479.x. PMID 11442824. 
  65. Jump up ^ Schär P, Herrmann G, Daly G, Lindahl T (1997). “A newly identified DNA ligase of Saccharomyces cerevisiae involved in RAD52-independent repair of DNA double-strand breaks”. Genes & Development 11 (15): 1912–24. doi:10.1101/gad.11.15.1912. PMC 316416. PMID 9271115. 
  66. Jump up ^ Ziegler M, Niere M (2004). “NAD+ surfaces again”. Biochem. J. 382 (Pt 3): e5–6. doi:10.1042/BJ20041217. PMC 1133982. PMID 15352307. 
  67. Jump up ^ Koch-Nolte F, Fischer S, Haag F, Ziegler M (2011). “Compartmentation of NAD+-dependent signalling”. FEBS Lett. 585 (11): 1651–6. doi:10.1016/j.febslet.2011.03.045. PMID 21443875. 
  68. Jump up ^ Breen LT, Smyth LM, Yamboliev IA, Mutafova-Yambolieva VN (2006). “beta-NAD is a novel nucleotide released on stimulation of nerve terminals in human urinary bladder detrusor muscle”. Am. J. Physiol. Renal Physiol. 290 (2): F486–95. doi:10.1152/ajprenal.00314.2005. PMID 16189287. 
  69. ^ Jump up to: a b Mutafova-Yambolieva VN, Hwang SJ, Hao X, Chen H, Zhu MX, Wood JD, Ward SM, Sanders KM (2007). “Beta-nicotinamide adenine dinucleotide is an inhibitory neurotransmitter in visceral smooth muscle”. Proc. Natl. Acad. Sci. U.S.A. 104 (41): 16359–64. doi:10.1073/pnas.0705510104. PMC 2042211. PMID 17913880. 
  70. ^ Jump up to: a b Hwang SJ, Durnin L, Dwyer L, Rhee PL, Ward SM, Koh SD, Sanders KM, Mutafova-Yambolieva VN (2011). “β-nicotinamide adenine dinucleotide is an enteric inhibitory neurotransmitter in human and nonhuman primate colons”. Gastroenterology 140 (2): 608–617.e6. doi:10.1053/j.gastro.2010.09.039. PMC 3031738. PMID 20875415. 
  71. Jump up ^ Yamboliev IA, Smyth LM, Durnin L, Dai Y, Mutafova-Yambolieva VN (2009). “Storage and secretion of beta-NAD, ATP and dopamine in NGF-differentiated rat pheochromocytoma PC12 cells”. Eur. J. Neurosci. 30 (5): 756–68. doi:10.1111/j.1460-9568.2009.06869.x. PMC 2774892. PMID 19712094. 
  72. Jump up ^ Durnin L, Dai Y, Aiba I, Shuttleworth CW, Yamboliev IA, Mutafova-Yambolieva VN (2012). “Release, neuronal effects and removal of extracellular β-nicotinamide adenine dinucleotide (β-NAD+) in the rat brain”. Eur. J. Neurosci. 35 (3): 423–35. doi:10.1111/j.1460-9568.2011.07957.x. PMC 3270379. PMID 22276961. 
  73. Jump up ^ Sauve AA (March 2008). “NAD+ and vitamin B3: from metabolism to therapies”. The Journal of Pharmacology and Experimental Therapeutics 324 (3): 883–93. doi:10.1124/jpet.107.120758. PMID 18165311. 
  74. Jump up ^ Khan JA, Forouhar F, Tao X, Tong L (2007). “Nicotinamide adenine dinucleotide metabolism as an attractive target for drug discovery”. Expert Opin. Ther. Targets 11 (5): 695–705. doi:10.1517/14728222.11.5.695. PMID 17465726. 
  75. Jump up ^ Kaneko S, Wang J, Kaneko M, Yiu G, Hurrell JM, Chitnis T, Khoury SJ, He Z (2006). “Protecting axonal degeneration by increasing nicotinamide adenine dinucleotide levels in experimental autoimmune encephalomyelitis models”. J. Neurosci. 26 (38): 9794–804. doi:10.1523/JNEUROSCI.2116-06.2006. PMID 16988050. 
  76. Jump up ^ Swerdlow RH (1998). “Is NADH effective in the treatment of Parkinson’s disease?”. Drugs Aging 13 (4): 263–8. doi:10.2165/00002512-199813040-00002. PMID 9805207. 
  77. Jump up ^ Timmins GS, Deretic V (2006). “Mechanisms of action of isoniazid”. Mol. Microbiol. 62 (5): 1220–7. doi:10.1111/j.1365-2958.2006.05467.x. PMID 17074073. 
  78. Jump up ^ Rawat R, Whitty A, Tonge PJ (2003). “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. 100 (24): 13881–6. Bibcode:2003PNAS..10013881R. doi:10.1073/pnas.2235848100. PMC 283515. PMID 14623976. 
  79. Jump up ^ Argyrou A, Vetting MW, Aladegbami B, Blanchard JS (2006). “Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid”. Nat. Struct. Mol. Biol. 13 (5): 408–13. doi:10.1038/nsmb1089. PMID 16648861. 
  80. Jump up ^ Gomes AP, Price NL, Ling AJ, Moslehi JJ, Montgomery MK, Rajman L, White JP, Teodoro JS, Wrann CD, Hubbard BP, Mercken EM, Palmeira CM, de Cabo R, Rolo AP, Turner N, Bell EL, Sinclair DA (December 19, 2013). “Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging”. Cell 155 (7): 1624–1638. doi:10.1016/j.cell.2013.11.037. PMID 24360282. 
  81. ^ Jump up to: a b Pankiewicz KW, Patterson SE, Black PL, Jayaram HN, Risal D, Goldstein BM, Stuyver LJ, Schinazi RF (2004). “Cofactor mimics as selective inhibitors of NAD-dependent inosine monophosphate dehydrogenase (IMPDH)—the major therapeutic target”. Curr. Med. Chem. 11 (7): 887–900. doi:10.2174/0929867043455648. PMID 15083807. 
  82. Jump up ^ Franchetti P, Grifantini M (1999). “Nucleoside and non-nucleoside IMP dehydrogenase inhibitors as antitumor and antiviral agents”. Curr. Med. Chem. 6 (7): 599–614. PMID 10390603. 
  83. Jump up ^ Kim EJ, Um SJ (2008). “SIRT1: roles in aging and cancer”. BMB Rep 41 (11): 751–6. doi:10.5483/BMBRep.2008.41.11.751. PMID 19017485. 
  84. Jump up ^ Valenzano DR, Terzibasi E, Genade T, Cattaneo A, Domenici L, Cellerino A (2006). “Resveratrol prolongs lifespan and retards the onset of age-related markers in a short-lived vertebrate”. Curr. Biol. 16 (3): 296–300. doi:10.1016/j.cub.2005.12.038. PMID 16461283. 
  85. Jump up ^ Howitz KT, Bitterman KJ, Cohen HY, Lamming DW, Lavu S, Wood JG, Zipkin RE, Chung P, Kisielewski A, Zhang LL, Scherer B, Sinclair DA (2003). “Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan”. Nature 425 (6954): 191–6. Bibcode:2003Natur.425..191H. doi:10.1038/nature01960. PMID 12939617. 
  86. Jump up ^ Wood JG, Rogina B, Lavu S, Howitz K, Helfand SL, Tatar M, Sinclair D (2004). “Sirtuin activators mimic caloric restriction and delay ageing in metazoans”. Nature 430 (7000): 686–9. Bibcode:2004Natur.430..686W. doi:10.1038/nature02789. PMID 15254550. 
  87. Jump up ^ Rizzi M, Schindelin H (2002). “Structural biology of enzymes involved in NAD and molybdenum cofactor biosynthesis”. Curr. Opin. Struct. Biol. 12 (6): 709–20. doi:10.1016/S0959-440X(02)00385-8. PMID 12504674. 
  88. Jump up ^ Begley TP, Kinsland C, Mehl RA, Osterman A, Dorrestein P (2001). “The biosynthesis of nicotinamide adenine dinucleotides in bacteria”. Vitam. Horm. Vitamins & Hormones 61: 103–19. doi:10.1016/S0083-6729(01)61003-3. ISBN 978-0-12-709861-6. PMID 11153263. 
  89. Jump up ^ http://www.cdc.gov/meningitis/lab-manual/chpt09-id-characterization-hi.html
  90. Jump up ^ Harden, A; Young, WJ (24 October 1906). “The alcoholic ferment of yeast-juice Part II.–The coferment of yeast-juice”. Proceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character 78 (526): 369–375. doi:10.1098/rspb.1906.0070. JSTOR 80144. 
  91. Jump up ^ “Fermentation of sugars and fermentative enzymes” (PDF). Nobel Lecture, 23 May 1930. Nobel Foundation. Retrieved 2007-09-30. 
  92. Jump up ^ Warburg O, Christian W (1936). “Pyridin, der wasserstoffübertragende bestandteil von gärungsfermenten (pyridin-nucleotide)” [Pyridin, the hydrogen-transferring component of the fermentation enzymes (pyridine nucleotide)]. Biochemische Zeitschrift (in German) 287: 291. doi:10.1002/hlca.193601901199. 
  93. Jump up ^ Elvehjem CA, Madden RJ, Strong FM, Woolley DW (1938). “The isolation and identification of the anti-black tongue factor” (PDF). J. Biol. Chem. 123 (1): 137–49. 
  94. Jump up ^ Axelrod AE, Madden RJ, Elvehjem CA (1939). “The effect of a nicotinic acid deficiency upon the coenzyme I content of animal tissues” (PDF). J. Biol. Chem. 131 (1): 85–93. 
  95. Jump up ^ Kornberg A (1948). “The participation of inorganic pyrophosphate in the reversible enzymatic synthesis of diphosphopyridine nucleotide” (PDF). J. Biol. Chem. 176 (3): 1475–76. PMID 18098602. 
  96. Jump up ^ Friedkin M, Lehninger AL (1 April 1949). “Esterification of inorganic phosphate coupled to electron transport between dihydrodiphosphopyridine nucleotide and oxygen”. J. Biol. Chem. 178 (2): 611–23. PMID 18116985. 
  97. Jump up ^ Preiss J, Handler P (1958). “Biosynthesis of diphosphopyridine nucleotide. I. Identification of intermediates”. J. Biol. Chem. 233 (2): 488–92. PMID 13563526. 
  98. Jump up ^ Preiss J, Handler P (1958). “Biosynthesis of diphosphopyridine nucleotide. II. Enzymatic aspects”. J. Biol. Chem. 233 (2): 493–500. PMID 13563527. 
  99. Jump up ^ Bieganowski, P; Brenner, C (2004). “Discoveries of Nicotinamide Riboside as a Nutrient and Conserved NRK Genes Establish a Preiss-Handler Independent Route to NAD+ in Fungi and Humans”. Cell 117 (4): 495–502. doi:10.1016/S0092-8674(04)00416-7. PMID 15137942. 
  100. Jump up ^ Chambon P, Weill JD, Mandel P (1963). “Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesizing nuclear enzyme”. Biochem. Biophys. Res. Commun. 11: 39–43. doi:10.1016/0006-291X(63)90024-X. PMID 14019961. 
  101. Jump up ^ Clapper DL, Walseth TF, Dargie PJ, Lee HC (15 July 1987). “Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate”. J. Biol. Chem. 262 (20): 9561–8. PMID 3496336. 
  102. Jump up ^ Imai S, Armstrong CM, Kaeberlein M, Guarente L (2000). “Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase”. Nature 403 (6771): 795–800. Bibcode:2000Natur.403..795I. doi:10.1038/35001622. PMID 10693811.