(en) Windholz, Martha (1983). The Merck Index: an encyclopedia of chemicals, drugs, and biologicals, 10th. Merck, Rahway NJ, US, 909. ISBN 978-0-911910-27-8.
(en) Belenky P, Racette FG, Bogan KL, et al. (2007). Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+. Cell129 (3): 473–84. PMID17482543. DOI: 10.1016/j.cell.2007.03.024. Vrije toegang
(en) Gomes AP, Price NL, Ling AJ, Moslehi JJ, et al. (2013). Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging. Cell155 (7): 1624–1638. PMID24360282. DOI: 10.1016/j.cell.2013.11.037. Vrije toegang
cshlp.org
genesdev.cshlp.org
(en) 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 & Development11 (15): 1912–24. PMID9271115. DOI: 10.1101/gad.11.15.1912. Vrije toegang
doi.org
(en) Yaku K, Okabe K, Nakagawa T. (2018). NAD metabolism: Implications in aging and longevity. Ageing Research Reviews47: 1-17. PMID29883761. DOI: 10.1016/j.arr.2018.05.006.
(en) Aman Y, Qui Y, Tao J, Fang, E. (2018). Therapeutic potential of boosting NAD+ in aging and age-related diseases. Translational Medicine of Aging2: 30-37. DOI: 10.1016/j.tma.2018.08.003.
(en) Armenta-Medina D, Segovia L, Perez-Rueda E (2014). Comparative genomics of nucleotide metabolism: a tour to the past of the three cellular domains of life. BMC Genomics15 (1): 800. PMID25230797. DOI: 10.1186/1471-2164-15-800. Vrije toegang
(en) Unden G, Bongaerts J (1997). Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim. Biophys. Acta1320 (3): 217–34. PMID9230919. DOI: 10.1016/S0005-2728(97)00034-0.
(en) 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. PMID17295611. DOI: 10.1042/BJ20061638.
(en) Biellmann JF, Lapinte C, et al. (1979). Structure of lactate dehydrogenase inhibitor generated from coenzyme. Biochemistry18 (7): 1212–7. PMID218616. DOI: 10.1021/bi00574a015.
(en) 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. PMID1741380. DOI: 10.1073/pnas.89.4.1271. Vrije toegang
(en) Jameson DM, Thomas V, Zhou DM (1989). Time-resolved fluorescence studies on NADH bound to mitochondrial malate dehydrogenase. Biochim. Biophys. Acta994 (2): 187–90. PMID2910350. DOI: 10.1016/0167-4838(89)90159-3.
(en) 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. PMID16698895. DOI: 10.1104/pp.106.081091. Vrije toegang
(en) Raffaelli N, Finaurini L, Mazzola F, et al. (2004). Characterization of Mycobacterium tuberculosis NAD kinase: functional analysis of the full-length enzyme by site-directed mutagenesis. Biochemistry43 (23): 7610–7. PMID15182203. DOI: 10.1021/bi049650w.
(en) Cantó C, Menzies K & Auwerx J (2015). NAD+ metabolism and the control of energy homeostasis - a balancing act between mitochondria and the nucleus. Cell metab.22 (1): 31-53. DOI: 10.1016/j.cmet.2015.05.023. Vrije toegang
(en) Anderson RM, Bitterman KJ, Wood JG, Medvedik O, et al. (2002). Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels. J. Biol. Chem.277 (21): 18881–90. PMID11884393. DOI: 10.1074/jbc.M111773200.
(en) Trammell SA, Schmidt MS, Weidemann BJ, et al. (2016). Nicotinamide riboside is uniquely and orally bioavailable in mice and humans. Nature Communications7. PMID27721479. DOI: 10.1038/ncomms12948. Vrije toegang
(en) Stein L, & Imai S. (2012). The dynamic regulation of NAD metabolism in mitochondria. Trends Endocrinol Metab.23 (9): 420–428. DOI: 10.1016/j.tem.2012.06.005.. Vrije toegang
(en) Rongvaux A, Andris F, Van Gool F, Leo O (2003). Reconstructing eukaryotic NAD metabolism. BioEssays25 (7): 683–90. PMID12815723. DOI: 10.1002/bies.10297.
(en) Xie W, Xu A, Yeung ES (2009). Determination of NAD+ and NADH level in a single cell under H2O2 stress by capillary electrophoresis. Analytical Chemistry81 (3): 1280–4. PMID19178345. DOI: 10.1021/ac802249m. Vrije toegang
(en) Blinova K, Carroll S, Bose S, et al. (2005). Distribution of mitochondrial NADH fluorescence lifetimes: steady-state kinetics of matrix NADH interactions. Biochemistry44 (7): 2585–94. PMID15709771. DOI: 10.1021/bi0485124.
(en) 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. PMID16574057. DOI: 10.1016/j.ab.2006.02.017.
(en) Belenky P, Racette FG, Bogan KL, et al. (2007). Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+. Cell129 (3): 473–84. PMID17482543. DOI: 10.1016/j.cell.2007.03.024. Vrije toegang
(en) 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 Med30 (11): 1191–212. PMID11368918. DOI: 10.1016/S0891-5849(01)00480-4.
(en) Goto M, Muramatsu H, Mihara H, et al. (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. PMID16192274. DOI: 10.1074/jbc.M507399200.
(en) 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. PMID17032644. DOI: 10.1074/jbc.M608387200.
(en) 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. PMID11152939. DOI: 10.1111/j.1574-6976.2001.tb00570.x.
(en) Rich PR (2003). The molecular machinery of Keilin's respiratory chain. Biochem. Soc. Trans.31 (Pt 6): 1095–105. PMID14641005. DOI: 10.1042/BST0311095.
(en) Freitag A, Bock E (1990). Energy conservation in Nitrobacter. FEMS Microbiology Letters66 (1–3): 157–62. DOI: 10.1111/j.1574-6968.1990.tb03989.x.
(en) 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 Chem279 (47): 48893–903. PMID15364945. DOI: 10.1074/jbc.M407266200.
(en) 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. PMID16189287. DOI: 10.1152/ajprenal.00314.2005.
(en) 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. PMID17913880. DOI: 10.1073/pnas.0705510104. Vrije toegang
(en) Durnin L, Dai Y, Aiba I, Shuttleworth CW (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. PMID22276961. DOI: 10.1111/j.1460-9568.2011.07957.x.
(en) Wang C, Zhou M, Zhang X, Yao J, Zhang Y, Mou Z (2017). A lectin receptor kinase as a potential sensor for extracellular nicotinamide adenine dinucleotide in Arabidopsis thaliana. eLife6: e25474. DOI: 10.7554/eLife.25474. Vrije toegang
(en) Ziegler M (2000). New functions of a long-known molecule. Emerging roles of NAD in cellular signaling. Eur. J. Biochem.267 (6): 1550–64. PMID10712584. DOI: 10.1046/j.1432-1327.2000.01187.x.
(en) Corda D, Di Girolamo M (2003). New Embo Member's Review: Functional aspects of protein mono-ADP-ribosylation. EMBO J.22 (9): 1953–8. PMID12727863. DOI: 10.1093/emboj/cdg209. Vrije toegang
(en) Guse AH (2005). Second messenger function and the structure-activity relationship of cyclic adenosine diphosphoribose (cADPR). FEBS J.272 (18): 4590–7. PMID16156781. DOI: 10.1111/j.1742-4658.2005.04863.x.
(en) Trapp J, Jung M (2006). The role of NAD+ dependent histone deacetylases (sirtuins) in ageing. Curr Drug Targets7 (11): 1553–60. PMID17100594. DOI: 10.2174/1389450110607011553.
(en) 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 & Development11 (15): 1912–24. PMID9271115. DOI: 10.1101/gad.11.15.1912. Vrije toegang
(en) Li J, Bonkowski MS, Moniot S, Zhang D, Hubbard BP, Ling AJY, Rajman LA, et al. (2017). A conserved NAD binding pocket that regulates protein-protein interactions during aging. Science355 (6331): 1312–1317. PMID28336669. DOI: 10.1126/science.aad8242. Vrije toegang
(en) Khan JA, Forouhar F, Tao X, Tong L (2007). Nicotinamide adenine dinucleotide metabolism as an attractive target for drug discovery. Expert Opin. Ther. Targets11 (5): 695–705. PMID17465726. DOI: 10.1517/14728222.11.5.695.
(en) Pankiewicz KW, Patterson SE, Black PL, Jayaram HN, Risal D, et al. (2004). Cofactor mimics as selective inhibitors of NAD-dependent inosine monophosphate dehydrogenase (IMPDH)—the major therapeutic target. Curr. Med. Chem.11 (7): 887–900. PMID15083807. DOI: 10.2174/0929867043455648.
(en) 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. PMID16461283. DOI: 10.1016/j.cub.2005.12.038.
(en) Gomes AP, Price NL, Ling AJ, Moslehi JJ, et al. (2013). Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging. Cell155 (7): 1624–1638. PMID24360282. DOI: 10.1016/j.cell.2013.11.037. Vrije toegang
(en) Katsyuba E, Romani M, Hofer D, Auwerx J. (2020). NAD+ homeostasis in health and disease. Nature Metabolism2: 9-31. DOI: 0.1038/s42255-019-0161-5.
(en) 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. PMID14623976. DOI: 10.1073/pnas.2235848100. Vrije toegang
(en) Harden, A, Young, WJ (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. Vrije toegang
(de) Warburg O, Christian W (1936). Pyridin, der wasserstoffübertragende bestandteil von gärungsfermenten (pyridin-nucleotide). Biochemische Zeitschrift287. DOI: 10.1002/hlca.193601901199.
elifesciences.org
(en) Wang C, Zhou M, Zhang X, Yao J, Zhang Y, Mou Z (2017). A lectin receptor kinase as a potential sensor for extracellular nicotinamide adenine dinucleotide in Arabidopsis thaliana. eLife6: e25474. DOI: 10.7554/eLife.25474. Vrije toegang
jbc.org
(en) Carl Bernofsky & Soo-Young C. Wanda (1982). Formation of Reduced Nicotinamide Adenine Dinucleotide Peroxide. The Journal Of Biological Chemistry257 (12): 6809-6817. PMID7045095. Vrije toegang
(en) Trammell SA, Schmidt MS, Weidemann BJ, et al. (2016). Nicotinamide riboside is uniquely and orally bioavailable in mice and humans. Nature Communications7. PMID27721479. DOI: 10.1038/ncomms12948. Vrije toegang
nih.gov
ncbi.nlm.nih.gov
(en) Yaku K, Okabe K, Nakagawa T. (2018). NAD metabolism: Implications in aging and longevity. Ageing Research Reviews47: 1-17. PMID29883761. DOI: 10.1016/j.arr.2018.05.006.
(en) Armenta-Medina D, Segovia L, Perez-Rueda E (2014). Comparative genomics of nucleotide metabolism: a tour to the past of the three cellular domains of life. BMC Genomics15 (1): 800. PMID25230797. DOI: 10.1186/1471-2164-15-800. Vrije toegang
(en) Carl Bernofsky & Soo-Young C. Wanda (1982). Formation of Reduced Nicotinamide Adenine Dinucleotide Peroxide. The Journal Of Biological Chemistry257 (12): 6809-6817. PMID7045095. Vrije toegang
(en) Unden G, Bongaerts J (1997). Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim. Biophys. Acta1320 (3): 217–34. PMID9230919. DOI: 10.1016/S0005-2728(97)00034-0.
(en) 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. PMID17295611. DOI: 10.1042/BJ20061638.
(en) Biellmann JF, Lapinte C, et al. (1979). Structure of lactate dehydrogenase inhibitor generated from coenzyme. Biochemistry18 (7): 1212–7. PMID218616. DOI: 10.1021/bi00574a015.
(en) 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. PMID1741380. DOI: 10.1073/pnas.89.4.1271. Vrije toegang
(en) Jameson DM, Thomas V, Zhou DM (1989). Time-resolved fluorescence studies on NADH bound to mitochondrial malate dehydrogenase. Biochim. Biophys. Acta994 (2): 187–90. PMID2910350. DOI: 10.1016/0167-4838(89)90159-3.
(en) Foster JW, Moat AG (1980). Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems. Microbiol. Rev.44 (1): 83–105. PMID6997723. Vrije toegang
(en) 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. PMID16698895. DOI: 10.1104/pp.106.081091. Vrije toegang
(en) Raffaelli N, Finaurini L, Mazzola F, et al. (2004). Characterization of Mycobacterium tuberculosis NAD kinase: functional analysis of the full-length enzyme by site-directed mutagenesis. Biochemistry43 (23): 7610–7. PMID15182203. DOI: 10.1021/bi049650w.
(en) Cantó C, Menzies K & Auwerx J (2015). NAD+ metabolism and the control of energy homeostasis - a balancing act between mitochondria and the nucleus. Cell metab.22 (1): 31-53. DOI: 10.1016/j.cmet.2015.05.023. Vrije toegang
(en) Anderson RM, Bitterman KJ, Wood JG, Medvedik O, et al. (2002). Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels. J. Biol. Chem.277 (21): 18881–90. PMID11884393. DOI: 10.1074/jbc.M111773200.
(en) Trammell SA, Schmidt MS, Weidemann BJ, et al. (2016). Nicotinamide riboside is uniquely and orally bioavailable in mice and humans. Nature Communications7. PMID27721479. DOI: 10.1038/ncomms12948. Vrije toegang
(en) Stein L, & Imai S. (2012). The dynamic regulation of NAD metabolism in mitochondria. Trends Endocrinol Metab.23 (9): 420–428. DOI: 10.1016/j.tem.2012.06.005.. Vrije toegang
(en) Rongvaux A, Andris F, Van Gool F, Leo O (2003). Reconstructing eukaryotic NAD metabolism. BioEssays25 (7): 683–90. PMID12815723. DOI: 10.1002/bies.10297.
(en) Xie W, Xu A, Yeung ES (2009). Determination of NAD+ and NADH level in a single cell under H2O2 stress by capillary electrophoresis. Analytical Chemistry81 (3): 1280–4. PMID19178345. DOI: 10.1021/ac802249m. Vrije toegang
(en) Blinova K, Carroll S, Bose S, et al. (2005). Distribution of mitochondrial NADH fluorescence lifetimes: steady-state kinetics of matrix NADH interactions. Biochemistry44 (7): 2585–94. PMID15709771. DOI: 10.1021/bi0485124.
(en) 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. PMID16574057. DOI: 10.1016/j.ab.2006.02.017.
(en) Belenky P, Racette FG, Bogan KL, et al. (2007). Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+. Cell129 (3): 473–84. PMID17482543. DOI: 10.1016/j.cell.2007.03.024. Vrije toegang
(en) 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 Med30 (11): 1191–212. PMID11368918. DOI: 10.1016/S0891-5849(01)00480-4.
(en) Goto M, Muramatsu H, Mihara H, et al. (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. PMID16192274. DOI: 10.1074/jbc.M507399200.
(en) Carugo O, Argos P (1997). NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding. Proteins28 (1): 10–28. PMID9144787.
(en) 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. PMID17032644. DOI: 10.1074/jbc.M608387200.
(en) 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. PMID11152939. DOI: 10.1111/j.1574-6976.2001.tb00570.x.
(en) Rich PR (2003). The molecular machinery of Keilin's respiratory chain. Biochem. Soc. Trans.31 (Pt 6): 1095–105. PMID14641005. DOI: 10.1042/BST0311095.
(en) Sistare FD, Haynes RC (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. PMID4044607. Vrije toegang
(en) 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 Chem279 (47): 48893–903. PMID15364945. DOI: 10.1074/jbc.M407266200.
(en) 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. PMID16189287. DOI: 10.1152/ajprenal.00314.2005.
(en) 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. PMID17913880. DOI: 10.1073/pnas.0705510104. Vrije toegang
(en) Durnin L, Dai Y, Aiba I, Shuttleworth CW (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. PMID22276961. DOI: 10.1111/j.1460-9568.2011.07957.x.
(en) Ziegler M (2000). New functions of a long-known molecule. Emerging roles of NAD in cellular signaling. Eur. J. Biochem.267 (6): 1550–64. PMID10712584. DOI: 10.1046/j.1432-1327.2000.01187.x.
(en) Corda D, Di Girolamo M (2003). New Embo Member's Review: Functional aspects of protein mono-ADP-ribosylation. EMBO J.22 (9): 1953–8. PMID12727863. DOI: 10.1093/emboj/cdg209. Vrije toegang
(en) Guse AH (2005). Second messenger function and the structure-activity relationship of cyclic adenosine diphosphoribose (cADPR). FEBS J.272 (18): 4590–7. PMID16156781. DOI: 10.1111/j.1742-4658.2005.04863.x.
(en) Trapp J, Jung M (2006). The role of NAD+ dependent histone deacetylases (sirtuins) in ageing. Curr Drug Targets7 (11): 1553–60. PMID17100594. DOI: 10.2174/1389450110607011553.
(en) 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 & Development11 (15): 1912–24. PMID9271115. DOI: 10.1101/gad.11.15.1912. Vrije toegang
(en) Li J, Bonkowski MS, Moniot S, Zhang D, Hubbard BP, Ling AJY, Rajman LA, et al. (2017). A conserved NAD binding pocket that regulates protein-protein interactions during aging. Science355 (6331): 1312–1317. PMID28336669. DOI: 10.1126/science.aad8242. Vrije toegang
(en) Khan JA, Forouhar F, Tao X, Tong L (2007). Nicotinamide adenine dinucleotide metabolism as an attractive target for drug discovery. Expert Opin. Ther. Targets11 (5): 695–705. PMID17465726. DOI: 10.1517/14728222.11.5.695.
(en) Pankiewicz KW, Patterson SE, Black PL, Jayaram HN, Risal D, et al. (2004). Cofactor mimics as selective inhibitors of NAD-dependent inosine monophosphate dehydrogenase (IMPDH)—the major therapeutic target. Curr. Med. Chem.11 (7): 887–900. PMID15083807. DOI: 10.2174/0929867043455648.
(en) 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. PMID16461283. DOI: 10.1016/j.cub.2005.12.038.
(en) Gomes AP, Price NL, Ling AJ, Moslehi JJ, et al. (2013). Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging. Cell155 (7): 1624–1638. PMID24360282. DOI: 10.1016/j.cell.2013.11.037. Vrije toegang
(en) 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. PMID14623976. DOI: 10.1073/pnas.2235848100. Vrije toegang
(en) Xie W, Xu A, Yeung ES (2009). Determination of NAD+ and NADH level in a single cell under H2O2 stress by capillary electrophoresis. Analytical Chemistry81 (3): 1280–4. PMID19178345. DOI: 10.1021/ac802249m. Vrije toegang
plantphysiol.org
(en) 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. PMID16698895. DOI: 10.1104/pp.106.081091. Vrije toegang
pnas.org
(en) 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. PMID1741380. DOI: 10.1073/pnas.89.4.1271. Vrije toegang
royalsocietypublishing.org
(en) Harden, A, Young, WJ (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. Vrije toegang
web.archive.org
(en) Sistare FD, Haynes RC (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. PMID4044607. Vrije toegang