NAD+ homeostasis in health and disease
Open accessAbstract
The conceptual evolution of nicotinamide adenine dinucleotide (NAD+) from being seen as a simple metabolic cofactor to a pivotal cosubstrate for proteins regulating metabolism and longevity, including the sirtuin family of protein deacylases, has led to a new wave of scientific interest in NAD+. NAD+ levels decline during ageing, and alterations in NAD+ homeostasis can be found in virtually all age-related diseases, including neurodegeneration, diabetes and cancer. In preclinical settings, various strategies to increase NAD+ levels have shown beneficial effects, thus starting a competitive race to discover marketable NAD+ boosters to improve healthspan and lifespan. Here, we review the basics of NAD+ biochemistry and metabolism, and its roles in health and disease, and we discuss current challenges and the future translational potential of NAD+ research.
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NAD+ homeostasis is required for the proper function of various metabolic tissues, including fat, muscle, intestines, kidneys and liver.
“Accordingly, NAD+ homeostasis is required for the proper function of various metabolic tissues, including fat, muscle, intestines, kidneys and liver (reviewed in72).”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [72]
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1 retracted
Age related changes in NAD+ metabolism oxidative stress and Sirt1 activity in wistar rats
Braidy, N., Guillemin, G. J., Mansour, H., Chan-Ling, T., Poljak, A., & Grant, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019194 · Cited by 594 · see citing works
RetractedUniProt: a worldwide hub of protein knowledge
The UniProt Consortium (2019) · Nucleic Acids Research · doi:10.1093/nar/gky1049 · Cited by 7,698 · see citing works
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510 · see citing works
AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300 · see citing works
Self-citationNutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160 · see citing works
Niacin in Patients with Low HDL Cholesterol Levels Receiving Intensive Statin Therapy
The AIM-HIGH Investigators (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1107579 · Cited by 2,911 · see citing works
A subcellular map of the human proteome
Thul, P. J., Åkesson, L., Wiking, M., Mahdessian, D., Geladaki, A., Ait Blal, H., Alm, T., Asplund, A., Björk, L., Breckels, L. M., et al. (2017) · Science · doi:10.1126/science.aal3321 · Cited by 2,813 · see citing works
Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253 · see citing works
Brown, G., Albers, J. J., Fisher, L. D., Schaefer, S. M., Lin, J.-T., Kaplan, C., Zhao, X.-Q., Bisson, B. D., Fitzpatrick, V. F., & Dodge, H. T. (1990) · New England Journal of Medicine · doi:10.1056/nejm199011083231901 · Cited by 2,159 · see citing works
Mammalian Sirtuins: Biological Insights and Disease Relevance
Haigis, M. C., & Sinclair, D. A. (2010) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092250 · Cited by 2,085 · see citing works
Sirtuins as regulators of metabolism and healthspan
Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008 · see citing works
Self-citationBrown, B. G., Zhao, X.-Q., Chait, A., Fisher, L. D., Cheung, M. C., Morse, J. S., Dowdy, A. A., Marino, E. K., Bolson, E. L., Alaupovic, P., et al. (2001) · New England Journal of Medicine · doi:10.1056/nejmoa011090 · Cited by 1,979 · see citing works
Effects of extended-release niacin with laropiprant in high-risk patients
The HPS2-THRIVE Collaborative Group (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1300955 · Cited by 1,668 · see citing works
Blankenhorn, D. H. (1987) · JAMA · doi:10.1001/jama.1987.03390230069027 · Cited by 1,654 · see citing works
Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648 · see citing works
Self-citationYing, W. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1672 · Cited by 1,494 · see citing works
Gomes, A. P., Price, N. L., Ling, A. J. Y., Moslehi, J. J., Montgomery, M. K., Rajman, L., White, J. P., Teodoro, J. S., Wrann, C. D., Hubbard, B. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.11.037 · Cited by 1,482 · see citing works
NAD+ and sirtuins in aging and disease
Imai, S.-I., & Guarente, L. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.04.002 · Cited by 1,481 · see citing works
Nakahata, Y., Kaluzova, M., Grimaldi, B., Sahar, S., Hirayama, J., Chen, D., Guarente, L. P., & Sassone-Corsi, P. (2008) · Cell · doi:10.1016/j.cell.2008.07.002 · Cited by 1,427 · see citing works
Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409 · see citing works
SIRT1 regulates circadian clock gene expression through PER2 deacetylation
Asher, G., Gatfield, D., Stratmann, M., Reinke, H., Dibner, C., Kreppel, F., Mostoslavsky, R., Alt, F. W., & Schibler, U. (2008) · Cell · doi:10.1016/j.cell.2008.06.050 · Cited by 1,376 · see citing works
Yoshino, J., Mills, K. F., Yoon, M. J., & Imai, S.-I. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.014 · Cited by 1,340 · see citing works
NAD <sup>+</sup> in aging, metabolism, and neurodegeneration
Verdin, E. (2015) · Science · doi:10.1126/science.aac4854 · Cited by 1,319 · see citing works
Axonal pathology in traumatic brain injury
Johnson, V. E., Stewart, W., & Smith, D. H. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2012.01.013 · Cited by 1,273 · see citing works
Zhang, H., Ryu, D., Wu, Y., Gariani, K., Wang, X., Luan, P., D’Amico, D., Ropelle, E. R., Lutolf, M. P., Aebersold, R., et al. (2016) · Science · doi:10.1126/science.aaf2693 · Cited by 1,255 · see citing works
Self-citationCantó, C., Houtkooper, R. H., Pirinen, E., Youn, D. Y., Oosterveer, M. H., Cen, Y., Fernandez-Marcos, P. J., Yamamoto, H., Andreux, P. A., Cettour-Rose, P., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.022 · Cited by 1,238 · see citing works
Self-citationMouchiroud, L., Houtkooper, R. H., Moullan, N., Katsyuba, E., Ryu, D., Cantó, C., Mottis, A., Jo, Y.-S., Viswanathan, M., Schoonjans, K., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.016 · Cited by 1,210 · see citing works
Self-citationCircadian Control of the NAD <sup>+</sup> Salvage Pathway by CLOCK-SIRT1
Nakahata, Y., Sahar, S., Astarita, G., Kaluzova, M., & Sassone-Corsi, P. (2009) · Science · doi:10.1126/science.1170803 · Cited by 1,198 · see citing works
Circadian Clock Feedback Cycle Through NAMPT-Mediated NAD <sup>+</sup> Biosynthesis
Ramsey, K. M., Yoshino, J., Brace, C. S., Abrassart, D., Kobayashi, Y., Marcheva, B., Hong, H.-K., Chong, J. L., Buhr, E. D., Lee, C., et al. (2009) · Science · doi:10.1126/science.1171641 · Cited by 1,126 · see citing works
NAD+ Intermediates: The Biology and Therapeutic Potential of NMN and NR
Yoshino, J., Baur, J. A., & Imai, S.-I. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.11.002 · Cited by 1,061 · see citing works
Increased Nuclear NAD Biosynthesis and SIRT1 Activation Prevent Axonal Degeneration
Araki, T., Sasaki, Y., & Milbrandt, J. (2004) · Science · doi:10.1126/science.1098014 · Cited by 1,060 · see citing works
Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors
Rutter, J., Reick, M., Wu, L. C., & McKnight, S. L. (2001) · Science · doi:10.1126/science.1060698 · Cited by 1,059 · see citing works
NAD+ metabolism in health and disease
Belenky, P. A., Bogan, K. L., & Brenner, C. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.006 · Cited by 983 · see citing works
The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
Landry, J., Sutton, A., Tafrov, S. T., Heller, R. C., Stebbins, J., Pillus, L., & Sternglanz, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.110148297 · Cited by 970 · see citing works
Nutrient-Sensitive Mitochondrial NAD+ Levels Dictate Cell Survival
Yang, H., Yang, T., Baur, J. A., Perez, E., Matsui, T., Carmona, J. J., Lamming, D. W., Souza-Pinto, N. C., Bohr, V. A., Rosenzweig, A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.07.035 · Cited by 950 · see citing works
Hematopoietic stem cell: self‐renewal versus differentiation
Seita, J., & Weissman, I. L. (2010) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.86 · Cited by 925 · see citing works
Cantó, C., Jiang, L. Q., Deshmukh, A. S., Mataki, C., Coste, A., Lagouge, M., Zierath, J. R., & Auwerx, J. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.02.006 · Cited by 921 · see citing works
Self-citationSRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1
Pacholec, M., Bleasdale, J. E., Chrunyk, B., Cunningham, D., Flynn, D., Garofalo, R. S., Griffith, D., Griffor, M., Loulakis, P., Pabst, B., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.088682 · Cited by 915 · see citing works
Nampt/PBEF/Visfatin Regulates Insulin Secretion in β Cells as a Systemic NAD Biosynthetic Enzyme
Revollo, J. R., Körner, A., Mills, K. F., Satoh, A., Wang, T., Garten, A., Dasgupta, B., Sasaki, Y., Wolberger, C., Townsend, R. R., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.09.003 · Cited by 911 · see citing works
Camacho-Pereira, J., Tarragó, M. G., Chini, C. C. S., Nin, V., Escande, C., Warner, G. M., Puranik, A. S., Schoon, R. A., Reid, J. M., Galina, A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.006 · Cited by 901 · see citing works
The secret life of NAD+: an old metabolite controlling new metabolic signaling pathways
Houtkooper, R. H., Cantó, C., Wanders, R. J., & Auwerx, J. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0026 · Cited by 899 · see citing works
Self-citationArterial Biology for the Investigation of the Treatment Effects of Reducing Cholesterol (ARBITER) 2
Taylor, A. J., Sullenberger, L. E., Lee, H. J., Lee, J. K., & Grace, K. A. (2004) · Circulation · doi:10.1161/01.cir.0000148955.19792.8d · Cited by 889 · see citing works
Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence
Rajman, L., Chwalek, K., & Sinclair, D. A. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.02.011 · Cited by 865 · see citing works
PARP-1 inhibition increases mitochondrial metabolism through SIRT1 activation
Bai, P., Cantó, C., Oudart, H., Brunyánszki, A., Cen, Y., Thomas, C., Yamamoto, H., Huber, A., Kiss, B., Houtkooper, R. H., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.004 · Cited by 837 · see citing works
Self-citationFulco, M., Cen, Y., Zhao, P., Hoffman, E. P., McBurney, M. W., Sauve, A. A., & Sartorelli, V. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.02.004 · Cited by 821 · see citing works
Choi, S. H., Bylykbashi, E., Chatila, Z. K., Lee, S. W., Pulli, B., Clemenson, G. D., Kim, E., Rompala, A., Oram, M. K., Asselin, C., et al. (2018) · Science · doi:10.1126/science.aan8821 · Cited by 802 · see citing works
Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.019 · Cited by 787 · see citing works
SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
Nakagawa, T., Lomb, D. J., Haigis, M. C., & Guarente, L. (2009) · Cell · doi:10.1016/j.cell.2009.02.026 · Cited by 787 · see citing works
Poly(ADP-Ribose) in the Cellular Response to DNA Damage
Berger, N. A. (1985) · Radiation Research · doi:10.2307/3576299 · Cited by 777 · see citing works
Bieganowski, P., & Brenner, C. (2004) · Cell · doi:10.1016/s0092-8674(04)00416-7 · Cited by 750 · see citing works
PARP-2, A Novel Mammalian DNA Damage-dependent Poly(ADP-ribose) Polymerase
Amé, J., Rolli, V., Schreiber, V., Niedergang, C., Apiou, F., Decker, P., Muller, S., Höger, T. H., Murcia, J. M., & de MURCIA, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17860 · Cited by 744 · see citing works
The power to reduce: pyridine nucleotides—small molecules with a multitude of functions
Pollak, N., Dölle, C., & Ziegler, M. (2007) · Biochemical Journal · doi:10.1042/bj20061638 · Cited by 730 · see citing works
Potential roles of gut microbiome and metabolites in modulating ALS in mice
Blacher, E., Bashiardes, S., Shapiro, H., Rothschild, D., Mor, U., Dori-Bachash, M., Kleimeyer, C., Moresi, C., Harnik, Y., Zur, M., et al. (2019) · Nature · doi:10.1038/s41586-019-1443-5 · Cited by 700 · see citing works
Nicotinamide riboside is uniquely and orally bioavailable in mice and humans
Trammell, S. A. J., Schmidt, M. S., Weidemann, B. J., Redpath, P., Jaksch, F., Dellinger, R. W., Li, Z., Abel, E. D., Migaud, M. E., & Brenner, C. (2016) · Nature Communications · doi:10.1038/ncomms12948 · Cited by 697 · see citing works
Di Lisa, F., Menabò, R., Canton, M., Barile, M., & Bernardi, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006825200 · Cited by 678 · see citing works
Circadian Clock NAD + Cycle Drives Mitochondrial Oxidative Metabolism in Mice
Peek, C. B., Affinati, A. H., Ramsey, K. M., Kuo, H.-Y., Yu, W., Sena, L. A., Ilkayeva, O., Marcheva, B., Kobayashi, Y., Omura, C., et al. (2013) · Science · doi:10.1126/science.1243417 · Cited by 658 · see citing works
Absence of Wallerian Degeneration does not Hinder Regeneration in Peripheral Nerve
Lunn, E. R., Perry, V. H., Brown, M. C., Rosen, H., & Gordon, S. (1989) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1989.tb00771.x · Cited by 646 · see citing works
The NAD metabolome — a key determinant of cancer cell biology
Chiarugi, A., Dölle, C., Felici, R., & Ziegler, M. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3340 · Cited by 645 · see citing works
Enhancing mitochondrial proteostasis reduces amyloid-β proteotoxicity
Sorrentino, V., Romani, M., Mouchiroud, L., Beck, J. S., Zhang, H., D’Amico, D., Moullan, N., Potenza, F., Schmid, A. W., Rietsch, S., et al. (2017) · Nature · doi:10.1038/nature25143 · Cited by 630 · see citing works
Self-citationQin, W., Yang, T., Ho, L., Zhao, Z., Wang, J., Chen, L., Zhao, W., Thiyagarajan, M., MacGrogan, D., Rodgers, J. T., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602909200 · Cited by 626 · see citing works
Essuman, K., Summers, D. W., Sasaki, Y., Mao, X., DiAntonio, A., & Milbrandt, J. (2017) · Neuron · doi:10.1016/j.neuron.2017.02.022 · Cited by 619 · see citing works
The Exercise Pressor Reflex: Its Cardiovascular Effects, Afferent Mechanisms, and Central Pathways
Mitchell, J. H., Kaufman, M. P., & Iwamoto, G. A. (1983) · Annual Review of Physiology · doi:10.1146/annurev.ph.45.030183.001305 · Cited by 618 · see citing works
Vitamin B <sub>3</sub> modulates mitochondrial vulnerability and prevents glaucoma in aged mice
Williams, P. A., Harder, J. M., Foxworth, N. E., Cochran, K. E., Philip, V. M., Porciatti, V., Smithies, O., & John, S. W. M. (2017) · Science · doi:10.1126/science.aal0092 · Cited by 617 · see citing works
SIRT1 Mediates Central Circadian Control in the SCN by a Mechanism that Decays with Aging
Chang, H.-C., & Guarente, L. (2013) · Cell · doi:10.1016/j.cell.2013.05.027 · Cited by 615 · see citing works
Wallerian degeneration of injured axons and synapses is delayed by a Ube4b/Nmnat chimeric gene
Mack, T. G. A., Reiner, M., Beirowski, B., Mi, W., Emanuelli, M., Wagner, D., Thomson, D., Gillingwater, T., Court, F., Conforti, L., et al. (2001) · Nature Neuroscience · doi:10.1038/nn770 · Cited by 611 · see citing works
SARM1 activation triggers axon degeneration locally via NAD <sup>+</sup> destruction
Gerdts, J., Brace, E. J., Sasaki, Y., DiAntonio, A., & Milbrandt, J. (2015) · Science · doi:10.1126/science.1258366 · Cited by 593 · see citing works
Martens, C. R., Denman, B. A., Mazzo, M. R., Armstrong, M. L., Reisdorph, N., McQueen, M. B., Chonchol, M., & Seals, D. R. (2018) · Nature Communications · doi:10.1038/s41467-018-03421-7 · Cited by 588 · see citing works
Clapper, D. L., Walseth, T. F., Dargie, P. J., & Lee, H. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47970-7 · Cited by 568 · see citing works
Tissue-specific regulation of SIRT1 by calorie restriction
Chen, D., Bruno, J., Easlon, E., Lin, S.-J., Cheng, H.-L., Alt, F. W., & Guarente, L. (2008) · Genes & Development · doi:10.1101/gad.1650608 · Cited by 567 · see citing works
Quantitative Analysis of NAD Synthesis-Breakdown Fluxes
Liu, L., Su, X., Quinn, W. J., Hui, S., Krukenberg, K., Frederick, D. W., Redpath, P., Zhan, L., Chellappa, K., White, E., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.03.018 · Cited by 564 · see citing works
PGC1α drives NAD biosynthesis linking oxidative metabolism to renal protection
Tran, M. T., Zsengellér, Z. K., Berg, A. H., Khankin, E. V., Bhasin, M., Kim, W., Clish, C. B., Stillman, I. E., Karumanchi, S. A., Rhee, E. P., et al. (2016) · Nature · doi:10.1038/nature17184 · Cited by 539 · see citing works
Berger, F., Lau, C., Dahlmann, M., & Ziegler, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508660200 · Cited by 508 · see citing works
NAD(+) in aging: molecular mechanisms and translational implications
Fang, E. F., Lautrup, S., Hou, Y., Demarest, T. G., Croteau, D. L., Mattson, M. P., & Bohr, V. A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.08.001 · Cited by 501 · see citing works
Macrophage de novo NAD+ synthesis specifies immune function in aging and inflammation
Minhas, P. S., Liu, L., Moon, P. K., Joshi, A. U., Dove, C., Mhatre, S., Contrepois, K., Wang, Q., Lee, B. A., Coronado, M., et al. (2019) · Nature Immunology · doi:10.1038/s41590-018-0255-3 · Cited by 501 · see citing works
Impairment of an endothelial NAD(+)-H2S signaling network is a reversible cause of vascular aging
Das, A., Huang, G. X., Bonkowski, M. S., Longchamp, A., Li, C., Schultz, M. B., Kim, L.-J., Osborne, B., Joshi, S., Lu, Y., et al. (2018) · Cell · doi:10.1016/j.cell.2018.02.008 · Cited by 496 · see citing works
Nicotinamide N-methyltransferase knockdown protects against diet-induced obesity
Kraus, D., Yang, Q., Kong, D., Banks, A. S., Zhang, L., Rodgers, J. T., Pirinen, E., Pulinilkunnil, T., Gong, F., Wang, Y.-C., et al. (2014) · Nature · doi:10.1038/nature13198 · Cited by 487 · see citing works
Hasegawa, K., Wakino, S., Šimić, P., Sakamaki, Y., Minakuchi, H., Fujimura, K., Hosoya, K., Komatsu, M., Kaneko, Y., Kanda, T., et al. (2013) · Nature Medicine · doi:10.1038/nm.3363 · Cited by 485 · see citing works
Mitochondrial Complex I Deficiency Increases Protein Acetylation and Accelerates Heart Failure
Karamanlidis, G., Lee, C. F., Garcia‐Menendez, L., Kolwicz, S. C., Suthammarak, W., Gong, G., Sedensky, M. M., Morgan, P. G., Wang, W., & Tian, R. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.07.002 · Cited by 469 · see citing works
Elhassan, Y. S., Kluckova, K., Fletcher, R. S., Schmidt, M. S., Garten, A., Doig, C. L., Cartwright, D. M., Oakey, L., Burley, C. V., Jenkinson, N., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.043 · Cited by 448 · see citing works
Protective effects of sirtuins in cardiovascular diseases: from bench to bedside
Winnik, S. H., Auwerx, J. H., Sinclair, D. A., & Matter, C. M. (2015) · European Heart Journal · doi:10.1093/eurheartj/ehv290 · Cited by 443 · see citing works
Self-citationSIRT3 Reverses Aging-Associated Degeneration
Brown, K., Xie, S., Qiu, X., Mohrin, M., Shin, J., Liu, Y., Zhang, D., Scadden, D. T., & Chen, D. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.005 · Cited by 436 · see citing works
De novo NAD+ synthesis enhances mitochondrial function and improves health
Katsyuba, E., Mottis, A., Ziętak, M., Franco, F., van der Velpen, V., Gariani, K., Ryu, D., Cialabrini, L., Matilainen, O., Liscio, P., et al. (2018) · Nature · doi:10.1038/s41586-018-0645-6 · Cited by 436 · see citing works
Self-citationSantomauro, A. T., Boden, G., Silva, M. E., Rocha, D. M., Santos, R. F., Ursich, M. J., Strassmann, P. G., & Wajchenberg, B. L. (1999) · Diabetes · doi:10.2337/diabetes.48.9.1836 · Cited by 431 · see citing works
Mihaylova, M. M., Cheng, C.-W., Cao, A. Q., Tripathi, S., Mana, M. D., Bauer-Rowe, K. E., Abu-Remaileh, M., Clavain, L., Erdemir, A., Lewis, C. A., et al. (2018) · Cell Stem Cell · doi:10.1016/j.stem.2018.04.001 · Cited by 428 · see citing works
Pillai, V. B., Sundaresan, N. R., Kim, G. H., Gupta, M., Rajamohan, S. B., Pillai, J. B., Samant, S. A., Ravindra, P. A., Isbatan, A., & Gupta, M. P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.077271 · Cited by 420 · see citing works
Biosensor reveals multiple sources for mitochondrial NAD <sup>+</sup>
Cambronne, X. A., Stewart, M. L., Kim, D., Jones-Brunette, A. M., Morgan, R. K., Farrens, D. L., Cohen, M. S., & Goodman, R. H. (2016) · Science · doi:10.1126/science.aad5168 · Cited by 407 · see citing works
Extracellular vesicle-contained eNAMPT delays aging and extends lifespan in mice
Yoshida, M., Satoh, A., Lin, J. B., Mills, K. F., Sasaki, Y., Rensing, N., Wong, M., Apte, R. S., & Imai, S.-I. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.05.015 · Cited by 407 · see citing works
Biosynthesis of Diphosphopyridine Nucleotide
Preiss, J., & Handler, P. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64789-1 · Cited by 403 · see citing works
Picciotto, N. E., Gano, L. B., Johnson, L. C., Martens, C. R., Sindler, A. L., Mills, K. F., Imai, S., & Seals, D. R. (2016) · Aging Cell · doi:10.1111/acel.12461 · Cited by 396 · see citing works
Laurent, G., German, N. J., Saha, A. K., de Boer, V. C. J., Davies, M. N., Koves, T. R., Dephoure, N., Fischer, F. F., Boanca, G., Vaitheesvaran, B., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.05.012 · Cited by 394 · see citing works
It takes two to tango: NAD(+) and sirtuins in aging/longevity control
Imai, S.-I., & Guarente, L. (2016) · npj Aging and Mechanisms of Disease · doi:10.1038/npjamd.2016.17 · Cited by 394 · see citing works
Pillai, J. B., Isbatan, A., Imai, S., & Gupta, M. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506162200 · Cited by 391 · see citing works
Sirtuin 3-dependent mitochondrial dynamic improvements protect against acute kidney injury.
Morigi, M., Perico, L., Rota, C., Longaretti, L., Conti, S., Rottoli, D., Novelli, R., Remuzzi, G., & Benigni, A. (2015) · Journal of Clinical Investigation · doi:10.1172/jci77632 · Cited by 388 · see citing works
Effective treatment of mitochondrial myopathy by nicotinamide riboside, a vitamin B3
Khan, N. A., Auranen, M., Paetau, I., Pirinen, E., Euro, L., Forsström, S., Pasila, L., Velagapudi, V., Carroll, C. J., Auwerx, J., et al. (2014) · EMBO Molecular Medicine · doi:10.1002/emmm.201403943 · Cited by 385 · see citing works
Self-citationTarragó, M. G., Chini, C. C. S., Kanamori, K. S., Warner, G. M., Caride, A., de Oliveira, G. C., Rud, M., Samani, A., Hein, K. Z., Huang, R., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.03.016 · Cited by 384 · see citing works
NRK1 controls nicotinamide mononucleotide and nicotinamide riboside metabolism in mammalian cells
Ratajczak, J., Joffraud, M., Trammell, S. A. J., Ras, R., Canela, N., Boutant, M., Kulkarni, S. S., Rodrigues, M., Redpath, P., Migaud, M. E., et al. (2016) · Nature Communications · doi:10.1038/ncomms13103 · Cited by 378 · see citing works
Self-citationDe novo NAD+ biosynthetic impairment in acute kidney injury in humans
Mehr, A. P., Tran, M. T., Ralto, K. M., Leaf, D. E., Washco, V., Messmer, J., Lerner, A., Kher, A., Kim, S. H., Khoury, C. C., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0138-z · Cited by 370 · see citing works
Gariani, K., Menzies, K. J., Ryu, D., Wegner, C. J., Wang, X., Ropelle, E. R., Moullan, N., Zhang, H., Perino, A., Lemos, V., et al. (2016) · Hepatology · doi:10.1002/hep.28245 · Cited by 368 · see citing works
Self-citationLoss of NAD Homeostasis Leads to Progressive and Reversible Degeneration of Skeletal Muscle
Frederick, D. W., Loro, E., Liu, L., Davila, A., Chellappa, K., Silverman, I. M., Quinn, W. J., Gosai, S. J., Tichy, E. D., Davis, J. G., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.07.005 · Cited by 367 · see citing works
Circadian Reprogramming in the Liver Identifies Metabolic Pathways of Aging
Sato, S., Solanas, G., Peixoto, F. O., Bee, L., Symeonidi, A., Schmidt, M. S., Brenner, C., Masri, S., Benitah, S. A., & Sassone‐Corsi, P. (2017) · Cell · doi:10.1016/j.cell.2017.07.042 · Cited by 359 · see citing works
Nicotinamide Riboside Preserves Cardiac Function in a Mouse Model of Dilated Cardiomyopathy
Diguet, N., Trammell, S. A. J., Tannous, C., Deloux, R., Piquereau, J., Mougenot, N., Gouge, A., Gressette, M., Manoury, B., Blanc, J., et al. (2018) · Circulation · doi:10.1161/circulationaha.116.026099 · Cited by 358 · see citing works
Regulation of intracellular levels of NAD: A novel role for CD38
Aksoy, P., White, T. A., Thompson, M., & Chini, E. N. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.05.042 · Cited by 353 · see citing works
A local mechanism mediates NAD-dependent protection of axon degeneration
Wang, J., Zhai, Q., Chen, Y., Lin, E., Gu, W., McBurney, M. W., & He, Z. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504028 · Cited by 352 · see citing works
Discovery of a Proneurogenic, Neuroprotective Chemical
Pieper, A. A., Xie, S., Capota, E., Estill, S. J., Zhong, J., Long, J. M., Becker, G. L., Huntington, P. J., Goldman, S. E., Shen, C.-H., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.018 · Cited by 350 · see citing works
Gong, B., Pan, Y., Vempati, P., Zhao, W., Knable, L., Ho, L., Wang, J., Sastre, M., Ono, K., Sauve, A. A., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.12.005 · Cited by 345 · see citing works
NAD+-Dependent Activation of Sirt1 Corrects the Phenotype in a Mouse Model of Mitochondrial Disease
Cerutti, R., Pirinen, E., Lamperti, C., Marchet, S., Sauve, A. A., Li, W., Leoni, V., Schon, E. A., Dantzer, F., Auwerx, J., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.001 · Cited by 343 · see citing works
Self-citationMechanisms of Muscle Degeneration, Regeneration, and Repair in the Muscular Dystrophies
Wallace, G. Q., & McNally, E. M. (2008) · Annual Review of Physiology · doi:10.1146/annurev.physiol.010908.163216 · Cited by 343 · see citing works
Poly(ADP-ribose) polymerase 1 participates in the phase entrainment of circadian clocks to feeding
Asher, G., Reinke, H., Altmeyer, M., Gutierrez-Arcelus, M., Hottiger, M. O., & Schibler, U. (2010) · Cell · doi:10.1016/j.cell.2010.08.016 · Cited by 340 · see citing works
ENZYMATIC SYNTHESIS OF TRIPHOSPHOPYRIDINE NUCLEOTIDE
Kornberg, A. (1950) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)56515-7 · Cited by 339 · see citing works
Normalization of NAD + Redox Balance as a Therapy for Heart Failure
Lee, C. F., Chavez, J. D., Garcia‐Menendez, L., Choi, Y. S., Roe, N. D., Chiao, Y. A., Edgar, J. S., Goo, Y. A., Goodlett, D. R., Bruce, J. E., et al. (2016) · Circulation · doi:10.1161/circulationaha.116.022495 · Cited by 337 · see citing works
Schöndorf, D. C., Ivanyuk, D., Baden, P., Sanchez-Martinez, A., De Cicco, S., Yu, C., Giunta, I., Schwarz, L. K., Di Napoli, G., Panagiotakopoulou, V., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.05.009 · Cited by 337 · see citing works
van Roermund, C. W. T., Elgersma, Y., Singh, N., Wanders, R. J. A., & Tabak, H. F. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07354.x · Cited by 336 · see citing works
Flavonoid Apigenin Is an Inhibitor of the NAD+ase CD38
Escande, C., Nin, V., Price, N. L., Capellini, V., Gomes, A. P., Barbosa, M. T., O’Neil, L., White, T. A., Sinclair, D. A., & Chini, E. N. (2013) · Diabetes · doi:10.2337/db12-1139 · Cited by 332 · see citing works
Protein acetylation in metabolism – metabolites and cofactors
Menzies, K. J., Zhang, H., Katsyuba, E., & Auwerx, J. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.181 · Cited by 331 · see citing works
Self-citationPathways and Subcellular Compartmentation of NAD Biosynthesis in Human Cells
Nikiforov, A., Dölle, C., Niere, M., & Ziegler, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213298 · Cited by 326 · see citing works
Gerhart‐Hines, Z., Dominy, J. E., Blättler, S. M., Jedrychowski, M. P., Banks, A. S., Lim, J.-H., Chim, H., Gygi, S. P., & Puigserver, P. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.12.005 · Cited by 323 · see citing works
Deletion of Nicotinamide Nucleotide Transhydrogenase
Freeman, H. C., Hugill, A. J., Dear, N. T., Ashcroft, F. M., & Cox, R. (2006) · Diabetes · doi:10.2337/db06-0358 · Cited by 321 · see citing works
Sirt1 activation protects the mouse renal medulla from oxidative injury
He, W., Wang, Y., Zhang, M., Li, Y., Davis, L. S., Fan, H. X., Yang, H., Fogo, A. B., Zent, R., Harris, R. C., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci41563 · Cited by 316 · see citing works
The Role of PARP-1 and PARP-2 Enzymes in Metabolic Regulation and Disease
Bai, P., & Cantó, C. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.06.016 · Cited by 312 · see citing works
Yamamoto, T., Byun, J., Zhai, P., Ikeda, Y., Oka, S., & Sadoshima, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098972 · Cited by 305 · see citing works
mTORC1 and SIRT1 Cooperate to Foster Expansion of Gut Adult Stem Cells during Calorie Restriction
Igarashi, M., & Guarente, L. (2016) · Cell · doi:10.1016/j.cell.2016.05.044 · Cited by 302 · see citing works
Nicotinamide Riboside Opposes Type 2 Diabetes and Neuropathy in Mice
Trammell, S. A. J., Weidemann, B. J., Chadda, A., Yorek, M. S., Holmes, A., Coppey, L. J., Obrosov, A., Kardon, R. H., Yorek, M. A., & Brenner, C. (2016) · Scientific Reports · doi:10.1038/srep26933 · Cited by 301 · see citing works
Skeletal muscle NAMPT is induced by exercise in humans
Costford, S. R., Bajpeyi, S., Pasarica, M., Albarado, D. C., Thomas, S. C., Xie, H., Church, T. S., Jubrias, S. A., Conley, K. E., & Smith, S. R. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00318.2009 · Cited by 297 · see citing works
Partitioning Circadian Transcription by SIRT6 Leads to Segregated Control of Cellular Metabolism
Masri, S., Rigor, P., Cervantes, M., Ceglia, N., Sebastian, C., Xiao, C., Roqueta-Rivera, M., Deng, C., Osborne, T. F., Mostoslavsky, R., et al. (2014) · Cell · doi:10.1016/j.cell.2014.06.050 · Cited by 292 · see citing works
Slc12a8 is a nicotinamide mononucleotide transporter
Grozio, A., Mills, K. F., Yoshino, J., Bruzzone, S., Sociali, G., Tokizane, K., Lei, H. C., Cunningham, R., Sasaki, Y., Migaud, M. E., et al. (2019) · Nature Metabolism · doi:10.1038/s42255-018-0009-4 · Cited by 287 · see citing works
Tarantini, S., Valcarcel‐Ares, M. N., Tóth, P., Yabluchanskiy, A., Tucsek, Z., Kiss, T., Hertelendy, P., Kinter, M. T., Ballabh, P., Süle, Z., et al. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101192 · Cited by 285 · see citing works
Reconstructing eukaryotic NAD metabolism.
Rongvaux, A., Andris, F., Gool, F. V., & Leo, O. (2003) · Bioessays · doi:10.1002/bies.10297 · Cited by 284 · see citing works
Hsu, C., Oka, S., Shao, D., Hariharan, N., & Sadoshima, J. (2009) · Circulation Research · doi:10.1161/circresaha.109.203703 · Cited by 284 · see citing works
Ronchi, J. A., Figueira, T. R., Ravagnani, F. G., Oliveira, H. C. F., Vercesi, A. E., & Castilho, R. F. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.049 · Cited by 283 · see citing works
Exercise alters SIRT1, SIRT6, NAD and NAMPT levels in skeletal muscle of aged rats
Koltai, E., Szabo, Z., Atalay, M., Boldogh, I., Naito, H., Goto, S., Nyakas, C., & Radak, Z. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.11.002 · Cited by 283 · see citing works
Dollerup, O. L., Christensen, B., Svart, M., Schmidt, M. S., Sulek, K., Ringgaard, S., Stødkilde-Jørgensen, H., Møller, N., Brenner, C., Treebak, J. T., et al. (2018) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/nqy132 · Cited by 282 · see citing works
Location of T cell and major histocompatibility complex antigens in the human thymus.
Bhan, A. K., Reinherz, E. L., Poppema, S., McCluskey, R. T., & Schlossman, S. F. (1980) · The Journal of Experimental Medicine · doi:10.1084/jem.152.4.771 · Cited by 281 · see citing works
Brown, K. D., Maqsood, S., Huang, J.-Y., Pan, Y., Harkcom, W., Li, W., Sauve, A., Verdin, E., & Jaffrey, S. R. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.11.003 · Cited by 277 · see citing works
Lethal Cardiomyopathy in Mice Lacking Transferrin Receptor in the Heart
Xu, W., Barrientos, T., Mao, L., Rockman, H. A., Sauve, A. A., & Andrews, N. C. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.023 · Cited by 274 · see citing works
Specification of haematopoietic stem cell fate via modulation of mitochondrial activity
Vannini, N., Girotra, M., Naveiras, O., Nikitin, G. F., Campos, V., Giger, S., Roch, A., Auwerx, J. H., & Lütolf, M. P. (2016) · Nature Communications · doi:10.1038/ncomms13125 · Cited by 272 · see citing works
Self-citationCD38 and CD157: A long journey from activation markers to multifunctional molecules
Quarona, V., Zaccarello, G., Chillemi, A., Brunetti, E., Singh, V. K., Ferrero, E., Funaro, A., Horenstein, A. L., & Malavasi, F. (2013) · Cytometry Part B Clinical Cytometry · doi:10.1002/cyto.b.21092 · Cited by 269 · see citing works
Sasaki, Y., Araki, T., & Milbrandt, J. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.2320-06.2006 · Cited by 269 · see citing works
Cameron, A. M., Castoldi, A., Sanin, D. E., Flachsmann, L. J., Field, C. S., Puleston, D. J., Kyle, R. L., Patterson, A. E., Hässler, F., Buescher, J. M., et al. (2019) · Nature Immunology · doi:10.1038/s41590-019-0336-y · Cited by 269 · see citing works
Rine, J., Strathern, J. N., Hicks, J. B., & Herskowitz, I. (1979) · Genetics · doi:10.1093/genetics/93.4.877 · Cited by 268 · see citing works
Stein, L. R., & Imai, S. (2014) · The EMBO Journal · doi:10.1002/embj.201386917 · Cited by 265 · see citing works
Airhart, S. E., Shireman, L. M., Risler, L. J., Anderson, G. D., Gowda, G. A. N., Raftery, D., Tian, R., Shen, D. D., & O’Brien, K. D. (2017) · PLoS ONE · doi:10.1371/journal.pone.0186459 · Cited by 260 · see citing works
NAD captureSeq indicates NAD as a bacterial cap for a subset of regulatory RNAs
Cahová, H., Winz, M., Höfer, K., Nübel, G., & Jäschke, A. (2014) · Nature · doi:10.1038/nature14020 · Cited by 259 · see citing works
Ryu, D., Zhang, H., Ropelle, E. R., Sorrentino, V., Mázala, D. A. G., Mouchiroud, L., Marshall, P. L., Campbell, M. D., Ali, A. S., Knowels, G. M., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf5504 · Cited by 256 · see citing works
Self-citationPirinen, E., Cantó, C., Jo, Y. S., Morato, L., Zhang, H., Menzies, K. J., Williams, E. G., Mouchiroud, L., Moullan, N., Hagberg, C., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.002 · Cited by 254 · see citing works
Self-citationBarbosa, M. T., Soares, S. M., Novak, C. M., Sinclair, D. A., Levine, J. A., Aksoy, P., & Chini, E. N. (2007) · The FASEB Journal · doi:10.1096/fj.07-8290com · Cited by 249 · see citing works
A rise in NAD precursor nicotinamide mononucleotide (NMN) after injury promotes axon degeneration
Di Stefano, M., Nascimento-Ferreira, I., Orsomando, G., Mori, V, Gilley, J., Brown, R., Janeckova, L., Vargas, M. E., Worrell, L. A., Loreto, A., et al. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.164 · Cited by 246 · see citing works
P7C3 Neuroprotective Chemicals Function by Activating the Rate-Limiting Enzyme in NAD Salvage
Wang, G., Han, T., Nijhawan, D., Theodoropoulos, P., Naidoo, J., Yadavalli, S., Mirzaei, H., Pieper, A. A., Ready, J. M., & McKnight, S. L. (2014) · Cell · doi:10.1016/j.cell.2014.07.040 · Cited by 243 · see citing works
Liu, D., Pitta, M., Jiang, H., Lee, J.-H., Zhang, G., Chen, X., Kawamoto, E. M., & Mattson, M. P. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.11.020 · Cited by 238 · see citing works
Guan, Y., Wang, S.-R., Huang, X.-Z., Xie, Q.-H., Xu, Y.-Y., Shang, D., & Hao, C.-M. (2017) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016040385 · Cited by 238 · see citing works
Metabolic regulation of transcription through compartmentalized NAD + biosynthesis
Ryu, K. W., Nandu, T. S., Kim, J., Challa, S., DeBerardinis, R. J., & Kraus, W. L. (2018) · Science · doi:10.1126/science.aan5780 · Cited by 232 · see citing works
Mendoza‐Alvarez, H., & Álvarez-González, R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41568-2 · Cited by 227 · see citing works
The mechanism of RNA 5′ capping with NAD+, NADH and desphospho-CoA
Bird, J. G., Zhang, Y., Tian, Y., Panova, N., Barvı́k, I., Greene, L., Liu, M., Buckley, B., Krásný, L., Lee, J. K., et al. (2016) · Nature · doi:10.1038/nature18622 · Cited by 226 · see citing works
Jiao, X., Doamekpor, S. K., Bird, J. G., Nickels, B. E., Tong, L., Hart, R. P., & Kiledjian, M. (2017) · Cell · doi:10.1016/j.cell.2017.02.019 · Cited by 225 · see citing works
Modulating NAD+ metabolism, from bench to bedside
Katsyuba, E., & Auwerx, J. H. (2017) · The EMBO Journal · doi:10.15252/embj.201797135 · Cited by 224 · see citing works
Self-citationIdentification of the Mitochondrial NAD+ Transporter in Saccharomyces cerevisiae
Todisco, S., Agrimi, G., Castegna, A., & Palmieri, F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510425200 · Cited by 223 · see citing works
Villines, T. C., Stanek, E. J., Devine, P. J., Turco, M., Miller, M., Weissman, N. J., Griffen, L., & Taylor, A. J. (2010) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2010.03.017 · Cited by 223 · see citing works
Increased podocyte Sirtuin-1 function attenuates diabetic kidney injury
Hong, Q., Zhang, L., Das, B., Li, Z., Liu, B., Cai, G., Chen, X., Chuang, P. Y., He, J. C., & Lee, K. (2018) · Kidney International · doi:10.1016/j.kint.2017.12.008 · Cited by 222 · see citing works
Vannini, N., Campos, V., Girotra, M., Trachsel, V., Rojas-Sutterlin, S., Tratwal, J., Ragusa, S., Stefanidis, E., Ryu, D., Rainer, P. Y., et al. (2019) · Cell Stem Cell · doi:10.1016/j.stem.2019.02.012 · Cited by 218 · see citing works
Self-citationWang, X., Hu, X., Yang, Y., Takata, T., & Sakurai, T. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.060 · Cited by 217 · see citing works
Stromsdorfer, K. L., Yamaguchi, S., Yoon, M. J., Moseley, A. C., Franczyk, M. P., Kelly, S. C., Qi, N., Imai, S.-I., & Yoshino, J. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.027 · Cited by 213 · see citing works
Conze, D., Brenner, C., & Kruger, C. L. (2019) · Scientific Reports · doi:10.1038/s41598-019-46120-z · Cited by 210 · see citing works
Tischler, M. E., Friedrichs, D., Coll, K. E., & WILLIAMSON, J. R. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90346-0 · Cited by 209 · see citing works
Inhibition of De Novo NAD + Synthesis by Oncogenic URI Causes Liver Tumorigenesis through DNA Damage
Tummala, K. S., Gomes, A. L., Yilmaz, M., Graña‐Castro, O., Bakiri, L., Ruppen, I., Ximénez‐Embún, P., Sheshappanavar, V., Rodriguez‐Justo, M., Pisano, D. G., et al. (2014) · Cancer Cell · doi:10.1016/j.ccell.2014.10.002 · Cited by 207 · see citing works
Hara, N., Yamada, K., Shibata, T., Osago, H., Hashimoto, T., & Tsuchiya, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610357200 · Cited by 205 · see citing works
LC/MS analysis of cellular RNA reveals NAD-linked RNA
Chen, Y. G., Kowtoniuk, W. E., Agarwal, I., Shen, Y., & Liu, D. R. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.235 · Cited by 205 · see citing works
Peled, T., Shoham, H., Aschengrau, D., Yackoubov, D., Frei, G. M., Rosenheimer, N. G., Lerrer, B., Cohen, H. Y., Nagler, A., Fibach, E., et al. (2011) · Experimental Hematology · doi:10.1016/j.exphem.2011.12.005 · Cited by 199 · see citing works
Gaikwad, A. S., Long, D. J., Stringer, J. L., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101053200 · Cited by 198 · see citing works
TARGETED, LCMS-BASED METABOLOMICS FOR QUANTITATIVE MEASUREMENT OF NAD + METABOLITES
Trammell, S. A. J., & Brenner, C. (2013) · Computational and Structural Biotechnology Journal · doi:10.5936/csbj.201301012 · Cited by 193 · see citing works
NMNAT1 inhibits axon degeneration via blockade of SARM1-mediated NAD+ depletion
Sasaki, Y., Nakagawa, T., Mao, X., DiAntonio, A., & Milbrandt, J. (2016) · eLife · doi:10.7554/elife.19749 · Cited by 192 · see citing works
NAD metabolism fuels human and mouse intestinal inflammation
Gerner, R. R., Klepsch, V., Macheiner, S., Arnhard, K., Adolph, T. E., Grander, C., Wieser, V., Pfister, A., Moser, P., Hermann-Kleiter, N., et al. (2018) · Gut · doi:10.1136/gutjnl-2017-314241 · Cited by 192 · see citing works
Wellman, A. S., Metukuri, M. R., Kazgan, N., Xu, X., Xu, Q., Ren, N. S. X., Czopik, A., Shanahan, M. T., Kang, A., Chen, W., et al. (2017) · Gastroenterology · doi:10.1053/j.gastro.2017.05.022 · Cited by 191 · see citing works
Irie, J., Inagaki, E., Fujita, M., Nakaya, H., Mitsuishi, M., Yamaguchi, S., Yamashita, K., Shigaki, S., Ono, T., Yukioka, H., et al. (2020) · Endocrine Journal · doi:10.1507/endocrj.ej19-0313 · Cited by 191 · see citing works
Inhibition of Nicotinamide Phosphoribosyltransferase
Pittelli, M., Formentini, L., Faraco, G., Lapucci, A., Rapizzi, E., Cialdai, F., Romano, G., Moneti, G., Moroni, F., & Chiarugi, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.136739 · Cited by 189 · see citing works
Emanuelli, M., Carnevali, F., Saccucci, F., Pierella, F., Amici, A., Raffaelli, N., & Magni, G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008700200 · Cited by 189 · see citing works
Genetic modifiers of the phenotype of mice deficient in mitochondrial superoxide dismutase
Huang, T., Naeemuddin, M., Elchuri, S. V., Yamaguchi, M., Kozy, H. M., Carlson, E. J., & Epstein, C. J. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl034 · Cited by 188 · see citing works
Telomere Dysfunction Induces Sirtuin Repression that Drives Telomere-Dependent Disease
Amano, H., Chaudhury, A., Rodriguez-Aguayo, C., Lu, L., Akhanov, V., Catic, A., Popov, Y. V., Verdin, E., Johnson, H., Stossi, F., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.03.001 · Cited by 182 · see citing works
Bajaj, M., Suraamornkul, S., Romanelli, A., Cline, G. W., Mandarino, L. J., Shulman, G. I., & DeFronzo, R. A. (2005) · Diabetes · doi:10.2337/diabetes.54.11.3148 · Cited by 181 · see citing works
Dellinger, R. W., Santos, S. R., Morris, M., Evans, M., Alminana, D., Guarente, L., & Marcotulli, E. (2017) · npj Aging and Mechanisms of Disease · doi:10.1038/s41514-017-0016-9 · Cited by 181 · see citing works
Zhao, Z. Y., Xie, X. J., Li, W. H., Liu, J., Chen, Z., Zhang, B., Li, T., Li, S. L., Lu, J. G., Zhang, L., et al. (2019) · iScience · doi:10.1016/j.isci.2019.05.001 · Cited by 179 · see citing works
REVIEW: Vitamin transport and homeostasis in mammalian brain: focus on Vitamins B and E
Spector, R., & Johanson, C. E. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04773.x · Cited by 175 · see citing works
The Membrane-Bound Enzyme CD38 Exists in Two Opposing Orientations
Zhao, Y. J., Lam, C. M. C., & Lee, H. C. (2012) · Science Signaling · doi:10.1126/scisignal.2002700 · Cited by 173 · see citing works
Aksoy, P., Escande, C., White, T. A., Thompson, M., Soares, S. M., Benech, J. C., & Chini, E. N. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.08.066 · Cited by 173 · see citing works
Structural and Functional Characterization of Human NAD Kinase
Lerner, F., Niere, M., Ludwig, A., & Ziegler, M. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5735 · Cited by 172 · see citing works
Kitani, T., Okuno, S., & Fujisawa, H. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00476-9 · Cited by 171 · see citing works
Turunc Bayrakdar, E., Uyanikgil, Y., Kanit, L., Koylu, E., & Yalcin, A. (2014) · Free Radical Research · doi:10.3109/10715762.2013.857018 · Cited by 169 · see citing works
Boosting NAD+ with a small molecule that activates NAMPT
Gardell, S. J., Hopf, M., Khan, A., Dispagna, M., Hampton Sessions, E., Falter, R., Kapoor, N., Brooks, J., Culver, J., Petucci, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11078-z · Cited by 169 · see citing works
Nicotinamide suppresses hyperphosphatemia in hemodialysis patients
Takahashi, Y., Tanaka, A., Nakamura, T., et al. (2004) · Kidney International · doi:10.1111/j.1523-1755.2004.00482.x · Cited by 168 · see citing works
PARP inhibition protects against alcoholic and non-alcoholic steatohepatitis
Mukhopadhyay, P., Horváth, B., Rajesh, M., Varga, Z. V., Gariani, K., Ryu, D., Cao, Z., Holovac, E., Park, O., Zhou, Z., et al. (2016) · Journal of Hepatology · doi:10.1016/j.jhep.2016.10.023 · Cited by 168 · see citing works
Self-citationGariani, K., Ryu, D., Menzies, K. J., Yi, H.-S., Stein, S., Zhang, H., Perino, A., Lemos, V., Katsyuba, E., Jha, P., et al. (2017) · Journal of Hepatology · doi:10.1016/j.jhep.2016.08.024 · Cited by 167 · see citing works
Self-citationThe alcoholic ferment of yeast-juice
Harden, A., & Young, W. J. (1906) · Proceedings of the Royal Society of London Series B Containing Papers of a Biological Character · doi:10.1098/rspb.1906.0029 · Cited by 162 · see citing works
Bone Marrow Failure Following Severe Injury in Humans
Livingston, D. H., Anjaria, D. J., Wu, J. C., Hauser, C. J., Chang, V. T.-S., Deitch, E. A., & Rameshwar, P. (2003) · Annals of Surgery · doi:10.1097/01.sla.0000094441.38807.09 · Cited by 161 · see citing works
Pathophysiological relevance of mitochondria in NAD+ metabolism
Lisa, F. D., & Ziegler, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02198-6 · Cited by 161 · see citing works
Metabolic Profiling of Alternative NAD Biosynthetic Routes in Mouse Tissues
Mori, V., Amici, A., Mazzola, F., Stefano, M. D., Conforti, L., Magni, G., Ruggieri, S., Raffaelli, N., & Orsomando, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113939 · Cited by 158 · see citing works
Macrodomain-containing proteins: regulating new intracellular functions of mono(ADP-ribosyl)ation
Feijs, K. L. H., Forst, A. H., Verheugd, P., & Lüscher, B. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3601 · Cited by 154 · see citing works
Jin, L., Galonek, H. L., Israelian, K., Choy, W., Morrison, M. C., Xia, Y. X., Wang, X., Xu, Y., Yang, Y., Smith, J. J., et al. (2009) · Protein Science · doi:10.1002/pro.50 · Cited by 153 · see citing works
Oh, G., Kim, H., Choi, J.-H., Shen, A., Choe, S., Karna, A., Lee, S., Jo, H.-J., Yang, S., Kwak, T. H., et al. (2013) · Kidney International · doi:10.1038/ki.2013.330 · Cited by 147 · see citing works
Dollerup, O. L., Chubanava, S., Agerholm, M., Søndergård, S. D., Altıntaş, A., Møller, A. B., Høyer, K. F., Ringgaard, S., Stødkilde‐Jørgensen, H., Lavery, G. G., et al. (2020) · The Journal of Physiology · doi:10.1113/jp278752 · Cited by 145 · see citing works
Gene therapy targeting SARM1 blocks pathological axon degeneration in mice
Geisler, S., Huang, S. X., Strickland, A., Doan, R. A., Summers, D. W., Mao, X., Park, J., DiAntonio, A., & Milbrandt, J. (2019) · Journal of Experimental Medicine · doi:10.1084/jem.20181040 · Cited by 145 · see citing works
Cho, K.-H., Kim, H., Rodríguez‐Iturbe, B., & Vaziri, N. D. (2009) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00126.2009 · Cited by 144 · see citing works
SIRT3 attenuates palmitate-induced ROS production and inflammation in proximal tubular cells
Koyama, T., Kume, S., Koya, D., Araki, S., Isshiki, K., Chin‒Kanasaki, M., Sugimoto, T., Haneda, M., Sugaya, T., Kashiwagi, A., et al. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.028 · Cited by 142 · see citing works
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Hallmarks of aging: An expanding universe
López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2023) · Cell · doi:10.1016/j.cell.2022.11.001 · Cited by 6,549 · see citing works
NAD+ metabolism and its roles in cellular processes during ageing
Covarrubias, A. J., Perrone, R., Grozio, A., & Verdin, E. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00313-x · Cited by 1,617 · see citing works
Microbiota–gut–brain axis and its therapeutic applications in neurodegenerative diseases
Loh, J. S., Mak, W. Q., Tan, L. K. S., Ng, C. X., Chan, H. H., Yeow, S. H., Foo, J. B., Ong, Y. S., How, C. W., & Khaw, K. Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01743-1 · Cited by 1,193 · see citing works
Mittelbrunn, M., & Kroemer, G. (2021) · Nature Immunology · doi:10.1038/s41590-021-00927-z · Cited by 702 · see citing works
Nicotinamide mononucleotide increases muscle insulin sensitivity in prediabetic women
Yoshino, M., Yoshino, J., Kayser, B. D., Patti, G. J., Franczyk, M. P., Mills, K. F., Sindelar, M., Pietka, T., Patterson, B. W., Imai, S.-I., et al. (2021) · Science · doi:10.1126/science.abe9985 · Cited by 439 · see citing works
CD38 ecto-enzyme in immune cells is induced during aging and regulates NAD+ and NMN levels
Chini, C. C. S., Peclat, T. R., Warner, G. M., Kashyap, S., Espindola-Netto, J. M., de Oliveira, G. C., Gomez, L. S., Hogan, K. A., Tarragó, M. G., Puranik, A. S., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-00298-z · Cited by 349 · see citing works
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Seale, K., Horvath, S., Teschendorff, A., Eynon, N., & Voisin, S. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-022-00477-6 · Cited by 274 · see citing works
Mithaiwala, M. N., Santana-Coelho, D., Porter, G. A., & O’Connor, J. C. (2021) · Cells · doi:10.3390/cells10061548 · Cited by 190 · see citing works
Luukkonen, P. K., Qadri, S., Ahlholm, N., Porthan, K., Männistö, V., Sammalkorpi, H., Penttilä, A. K., Hakkarainen, A., Lehtimäki, T. E., Gaggini, M., et al. (2022) · Journal of Hepatology · doi:10.1016/j.jhep.2021.10.013 · Cited by 170 · see citing works
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Girardi, E., Agrimi, G., Goldmann, U., Fiume, G., Lindinger, S., Sedlyarov, V., Srndic, I., Gürtl, B., Agerer, B., Kartnig, F., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19871-x · Cited by 123 · see citing works
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Hofer, S. J., Davinelli, S., Bergmann, M., Scapagnini, G., & Madeo, F. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.717343 · Cited by 109 · see citing works
Okabe, K., Yaku, K., Uchida, Y., Fukamizu, Y., Sato, T., Sakurai, T., Tobe, K., & Nakagawa, T. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.868640 · Cited by 105 · see citing works
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Yang, S., Park, J. H., & Lu, H.-C. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00634-3 · Cited by 94 · see citing works
Ren, Z., Xu, Y., Li, T., Sun, W., Tang, Z., Wang, Y., Zhou, K., Li, J., Ding, Q., Liang, K., et al. (2022) · Animal Nutrition · doi:10.1016/j.aninu.2022.06.009 · Cited by 44 · see citing works
Lai, X., Huang, S., Lin, S., Pu, L., Wang, Y., Lin, Y., Huang, W., & Wang, Z. (2022) · Stem Cell Research & Therapy · doi:10.1186/s13287-021-02688-w · Cited by 26 · see citing works
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Franczyk, M. P., Qi, N., Stromsdorfer, K. L., Li, C., Yamaguchi, S., Itoh, H., Yoshino, M., Sasaki, Y., Brookheart, R. T., Finck, B. N., et al. (2021) · Endocrinology · doi:10.1210/endocr/bqab006 · Cited by 23 · see citing works
- Authors
- Katsyuba, E., Romani, M., Hofer, D., & Auwerx, J.
- Affiliations
- École Polytechnique Fédérale de Lausanne (CH)
- Thermo Fisher Scientific (Switzerland) (CH)
- Corresponding author
- Auwerx, Johan
- Venue
- Nature Metabolism
- Published
- 2020-01-20
- Volume
- 2
- Issue
- 1
- Pages
- 9-31
- ISSN
- 2522-5812 (ISSN-L)
- OpenAlex
- W3000157665
- Cited by
- 627
- References
- 456
- Citations by year
- 2026: 102 · 2025: 101 · 2024: 92 · 2023: 110 · 2022: 110 · 2021: 77 · 2020: 34 · 2018: 1
- FWCI
- 10.28
- Type
- journal article
- Language
- en
- Open access
- green
- infoscience.epfl.ch
- Licence
- Locations
- Nature Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- National Institute on Aging (R01AG043930)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- NAD+ homeostasis, NAD+ metabolism, sirtuins, aging, age-related diseases, neurodegeneration, diabetes mellitus, cancer, healthspan, lifespan
- MeSH terms
- Animals, Disease, Glycolysis, Homeostasis, Humans, Longevity, Metabolism, NAD, NADP, Oxidation-Reduction, Phosphorylation, Subcellular Fractions, Sirtuins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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