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The NAD Biosynthesis Pathway Mediated by Nicotinamide Phosphoribosyltransferase Regulates Sir2 Activity in Mammalian Cells
Open accessAbstract
Recent studies have revealed new roles for NAD and its derivatives in transcriptional regulation. The evolutionarily conserved Sir2 protein family requires NAD for its deacetylase activity and regulates a variety of biological processes, such as stress response, differentiation, metabolism, and aging. Despite its absolute requirement for NAD, the regulation of Sir2 function by NAD biosynthesis pathways is poorly understood in mammals. In this study, we determined the kinetics of the NAD biosynthesis mediated by nicotinamide phosphoribosyltransferase (Nampt) and nicotinamide/nicotinic acid mononucleotide adenylyltransferase (Nmnat), and we examined its effects on the transcriptional regulatory function of the mouse Sir2 ortholog, Sir2alpha, in mouse fibroblasts. We found that Nampt was the rate-limiting component in this mammalian NAD biosynthesis pathway. Increased dosage of Nampt, but not Nmnat, increased the total cellular NAD level and enhanced the transcriptional regulatory activity of the catalytic domain of Sir2alpha recruited onto a reporter gene in mouse fibroblasts. Gene expression profiling with oligonucleotide microarrays also demonstrated a significant correlation between the expression profiles of Nampt- and Sir2alpha-overexpressing cells. These findings suggest that NAD biosynthesis mediated by Nampt regulates the function of Sir2alpha and thereby plays an important role in controlling various biological events in mammals.
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“NMN is an intermediate in the salvage pathway and can be converted to NAD+, bypassing a catalysis of nicotinamide phosphoribosyltransferase (NAMPT), a rate-limiting enzyme in this pathway (10).”
From Nicotinamide riboside and nicotinamide mononucleotide facilitate NAD + synthesis via enterohepatic circulation (2025) · cites this paper as [10]
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“NMN is a substrate for nicotinamide mononucleotide adenylyltransferase (NMNAT), which is an enzyme that converts NMN and adenosine triphosphate to NAD+ and inorganic pyrophosphate (10).”
From Nicotinamide riboside and nicotinamide mononucleotide facilitate NAD + synthesis via enterohepatic circulation (2025) · cites this paper as [10]
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Cites
Efficient selection for high-expression transfectants with a novel eukaryotic vector
Niwa, H., Yamamura, K., & Miyazaki, J. (1991) · Gene · doi:10.1016/0378-1119(91)90434-d · Cited by 5,149
Yang, Y., Dudoit, S., Luu, P., Lin, D., Peng, V., Ngai, J., & Speed, T. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.4.e15 · Cited by 3,722
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
Self-citationStress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239
Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase
Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., & Mayo, M. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600244 · Cited by 2,750
hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,690
Self-citationKaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253
Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081
Self-citationSirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ
Picard, F., Kurtev, M. V., Chung, N., Topark‐Ngarm, A., Senawong, T., de Oliveira, R. M., Leid, M. E., McBurney, M. W., & Guarente, L. (2004) · Nature · doi:10.1038/nature02583 · Cited by 1,943
Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., Kessler, B., Howitz, K. T., Gorospe, M., de Cabo, R., & Sinclair, D. A. (2004) · Science · doi:10.1126/science.1099196 · Cited by 1,924
Flagged first, then by citations
Research works printed but not linked: 4
- Magni, 1999, Adv. Enzymol. Relat. Areas Mol. Biol., 73, 135
- Samal, 1994, Mol. Cell. Biol., 14, 1431
- Neubert, 1964, Biochim. Biophys. Acta, 92, 610
- Picard, 2004, Nature, 429, 771, 10.1038/nature02583 · DOI
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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
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
Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648
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
Ying, W. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1672 · Cited by 1,494
Circadian Control of the NAD + 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
Pearson, K. J., Baur, J. A., Lewis, K. N., Peshkin, L., Price, N. L., Labinskyy, N., Swindell, W. R., Kamara, D., Minor, R. K., Perez, E., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.06.011 · Cited by 1,162
Circadian Clock Feedback Cycle Through NAMPT-Mediated NAD + 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
Self-citationNAD+ 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
Self-citationSIRT1 Functionally Interacts with the Metabolic Regulator and Transcriptional Coactivator PGC-1α
Nemoto, S., Fergusson, M. M., & Finkel, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501485200 · Cited by 1,047
Sundaresan, N. R., Gupta, M., Gene, K., Rajamohan, S. B., Isbatan, A., & Gupta, M. P. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39162 · Cited by 1,006
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 1,006
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
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
Self-citationThe 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
AMPK and SIRT1: a long-standing partnership?
Ruderman, N. B., Julia Xu, X., Nelson, L., Cacicedo, J. M., Saha, A. K., Lan, F., & Ido, Y. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00745.2009 · Cited by 903
Tao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S.-H., Jiang, H., Kim, H.-S., Flynn, C. R., Hill, S., Hayes McDonald, W., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.12.013 · Cited by 899
The PARP Side of the Nucleus: Molecular Actions, Physiological Outcomes, and Clinical Targets
Krishnakumar, R., & Kraus, W. L. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.017 · Cited by 877
Fulco, 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 843
Poly(ADP-ribosyl)ation by PARP-1: `PAR-laying' NAD + into a nuclear signalPreprint
Kim, M. Y., Zhang, T., & Kraus, W. L. (2005) · Genes & Development · doi:10.1101/gad.1331805 · Cited by 826
Sauve, A. A., Wolberger, C., Schramm, V. L., & Boeke, J. D. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133500 · Cited by 763
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Gupte, R., Liu, Z., & Kraus, W. L. (2017) · Genes & Development · doi:10.1101/gad.291518.116 · Cited by 681
“More broadly, a number of studies have shown that modulation of cellular NAD+ levels can regulate the catalytic activities of sirtuins (Anderson et al. 2002, 2003; Araki et al. 2004; Revollo et al. 2004); presumably, similar mechanisms can regulate the catalytic activities of PARPs as well.”
BackgroundPhysiological and pathophysiological roles of NAMPT and NAD metabolism.
Garten, A., Schuster, S., Penke, M., Gorski, T., de Giorgis, T., & Kiess, W. (2015) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.117 · Cited by 708
Sirtuin 1 and Sirtuin 3: Physiological Modulators of Metabolism
Nogueiras, R., Habegger, K. M., Chaudhary, N., Finan, B., Banks, A. S., Dietrich, M. O., Horváth, T. L., Sinclair, D. A., Pfluger, P. T., & Tschöp, M. H. (2012) · Physiological Reviews · doi:10.1152/physrev.00022.2011 · Cited by 724
Regulation of SIRT1 in cellular functions: Role of polyphenols
Chung, S., Yao, H., Caito, S. W., Hwang, J., Arunachalam, G., & Rahman, I. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.05.003 · Cited by 664
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 660
Sirtuins: critical regulators at the crossroads between cancer and aging
Saunders, L. R., & Verdin, E. (2007) · Oncogene · doi:10.1038/sj.onc.1210616 · Cited by 489
Toward a unified theory of caloric restriction and longevity regulation
Sinclair, D. A. (2005) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2005.03.019 · Cited by 568
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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 546
The dynamic regulation of NAD metabolism in mitochondria
Stein, L. R., & Imai, S. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.06.005 · Cited by 558
Self-citationAMPK in skeletal muscle function and metabolism
Kjøbsted, R., Hingst, J. R., Fentz, J., Foretz, M., Sanz, M.-N., Pehmøller, C. K., Shum, M., Marette, A., Mounier, R., Treebak, J. T., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700442r · Cited by 517
Sirtuin Functions in Health and Disease
Yamamoto, H., Schoonjans, K., & Auwerx, J. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0079 · Cited by 480
Sirtuin signaling in cellular senescence and aging
Lee, S.-H., Lee, J.-H., Lee, H., & Min, K. (2019) · BMB Reports · doi:10.5483/bmbrep.2019.52.1.290 · Cited by 449
Targeting Sirtuin 1 to Improve Metabolism: All You Need Is NAD+?
Cantó, C., & Auwerx, J. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.003905 · Cited by 433
Sirtuins — novel therapeutic targets to treat age-associated diseases
Lavu, S., Boss, O., Elliott, P. J., & Lambert, P. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2665 · Cited by 427
Belenky, P., Racette, F. G., Bogan, K. L., McClure, J. M., Smith, J. S., & Brenner, C. (2007) · Cell · doi:10.1016/j.cell.2007.03.024 · Cited by 411
Sirtuins: The ‘ magnificent seven ’, function, metabolism and longevity
Dali‐Youcef, N., Lagouge, M., Froelich, S., Koehl, C., Schoonjans, K., & Auwerx, J. (2007) · Annals of Medicine · doi:10.1080/07853890701408194 · Cited by 402
Biosensor reveals multiple sources for mitochondrial NAD +
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
Caloric restriction, SIRT1 and longevity
Cantó, C., & Auwerx, J. (2009) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2009.03.008 · Cited by 395
Nampt: linking NAD biology, metabolism and cancer
Garten, A., Petzold-Quinque, S., Körner, A., Imai, S., & Kieß, W. (2008) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2008.10.004 · Cited by 399
Self-citationIt 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
Self-citationPillai, J. B., Isbatan, A., Imai, S., & Gupta, M. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506162200 · Cited by 404
Self-citationTen years of NAD-dependent SIR2 family deacetylases: implications for metabolic diseases
Imai, S., & Guarente, L. (2010) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.02.003 · Cited by 394
Self-citationYang, H., Zhang, W., Pan, H., Feldser, H. G., Lainez, E., Miller, C. M., Leung, S., Zhong, Z., Zhao, H., Sweitzer, S. M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046364 · Cited by 393
Seven sirtuins for seven deadly diseases ofaging
Morris, B. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.525 · Cited by 386
Li, X. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gms108 · Cited by 360
Sirtuins mediate mammalian metabolic responses to nutrient availability
Chalkiadaki, A., & Guarente, L. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.225 · Cited by 344
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
Adipose tissue, obesity and adipokines: role in cancer promotion
Booth, A. D., Magnuson, A. M., Fouts, J. K., & Foster, M. T. (2015) · Hormone Molecular Biology and Clinical Investigation · doi:10.1515/hmbci-2014-0037 · Cited by 351
The Dual Role of Sirtuins in Cancer
Bosch‐Presegué, L., & Vaquero, A. (2011) · Genes & Cancer · doi:10.1177/1947601911417862 · Cited by 337
Pathways 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
The Sir2 family of protein deacetylases
Denu, J. M. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2005.08.010 · Cited by 325
Extension of Human Cell Lifespan by Nicotinamide Phosphoribosyltransferase
van der Veer, E., Ho, C. S. W., O’Neil, C. H., Barbosa, N., Scott, R., Cregan, S. P., & Pickering, J. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700018200 · Cited by 329
Ramsey, K. M., Mills, K. F., Satoh, A., & Imai, S. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2007.00355.x · Cited by 321
Self-citationGerhart‐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 336
The secretory function of adipocytes in the physiology of white adipose tissue
Wang, P., Mariman, E., Renes, J., & Keijer, J. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21386 · Cited by 318
The regulation of nicotinamide adenine dinucleotide biosynthesis by Nampt/PBEF/visfatin in mammals
Revollo, J. R., Grimm, A. A., & Imai, S. (2007) · Current Opinion in Gastroenterology · doi:10.1097/mog.0b013e32801b3c8f · Cited by 316
Self-citationMedvedik, O., Lamming, D. W., Kim, K. D., & Sinclair, D. A. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050261 · Cited by 275
Structure of Nampt/PBEF/visfatin, a mammalian NAD+ biosynthetic enzyme
Wang, T., Zhang, X., Bheda, P., Revollo, J. R., Imai, S., & Wolberger, C. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1114 · Cited by 305
Self-citationZhang, T., & Kraus, W. L. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.10.022 · Cited by 314
Rajamohan, S. B., Pillai, V. B., Gupta, M., Sundaresan, N. R., Birukov, K. G., Samant, S. A., Hottiger, M. O., & Gupta, M. P. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00121-09 · Cited by 313
NAD+ and Vitamin B3: From Metabolism to Therapies
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Skeletal muscle NAMPT is induced by exercise in humans
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NAD+ homeostasis in renal health and disease
Ralto, K. M., Rhee, E. P., & Parikh, S. M. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0216-6 · Cited by 293
Van Gool, F., Gallí, M., Gueydan, C., Kruys, V., Prevot, P.-P., Bedalov, A., Mostoslavsky, R., Alt, F. W., De Smedt, T., & Leo, O. (2009) · Nature Medicine · doi:10.1038/nm.1906 · Cited by 285
Wang, P., Xu, T., Guan, Y., Tian, W., Viollet, B., Rui, Y., Zhai, Q., Su, D., & Miao, C. (2011) · Annals of Neurology · doi:10.1002/ana.22236 · Cited by 290
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
Self-citationChang, C., Su, H., Zhang, D., Wang, Y., Shen, Q., Liu, B., Huang, R., Zhou, T., Peng, C., Wong, C. C. L., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.10.037 · Cited by 287
Hsu, C., Oka, S., Shao, D., Hariharan, N., & Sadoshima, J. (2009) · Circulation Research · doi:10.1161/circresaha.109.203703 · Cited by 289
Menssen, A., Hydbring, P., Kapelle, K., Vervoorts, J., Diebold, J., Lüscher, B., Larsson, L., & Hermeking, H. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105304109 · Cited by 275
Molecular basis for the inhibition of human NMPRTase, a novel target for anticancer agents
Khan, J., Tao, X., & Tong, L. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1105 · Cited by 277
Sasaki, Y., Araki, T., & Milbrandt, J. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.2320-06.2006 · Cited by 269
NAD metabolism: Implications in aging and longevity
Yaku, K., Okabe, K., & Nakagawa, T. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.05.006 · Cited by 269
Stein, L. R., & Imai, S. (2014) · The EMBO Journal · doi:10.1002/embj.201386917 · Cited by 265
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Hrubša, M., Siatka, T., Najmanová, I., Vopršalová, M., Krčmová, L. K., Matoušová, K., Javorská, L., Macáková, K., Mercolini, L., Remião, F., et al. (2022) · Nutrients · doi:10.3390/nu14030484 · Cited by 284
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Pissios, P. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.02.004 · Cited by 259
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Sampath, D., Zabka, T. S., Misner, D. L., O’Brien, T., & Dragovich, P. S. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.02.004 · Cited by 258
Hong, S., Moreno‐Navarrete, J. M., Wei, X., Kikukawa, Y., Tzameli, I., Prasad, D., Lee, Y., Asara, J. M., Fernández‐Real, J. M., Maratos–Flier, E., et al. (2015) · Nature Medicine · doi:10.1038/nm.3882 · Cited by 260
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Shats, I., Williams, J. G., Liu, J., Makarov, M. V., Wu, X., Lih, F. B., Deterding, L. J., Lim, C., Xu, X., Randall, T. A., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.02.001 · Cited by 242
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Cantó, C., Sauve, A. A., & Bai, P. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.004 · Cited by 246
Wang, B., Hasan, M. K., Alvarado, E., Yuan, H., Wu, H., & Chen, W. (2010) · Oncogene · doi:10.1038/onc.2010.468 · Cited by 250
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Yoon, M. J., Yoshida, M., Johnson, S., Takikawa, A., Usui, I., Tobe, K., Nakagawa, T., Yoshino, J., & Imai, S. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.04.002 · Cited by 246
Self-citationBusso, N., Karababa, M., Nobile, M., Rolaz, A., Gool, F. V., Gallí, M., Léo, O., So, A. K.-L., & Smedt, T. D. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002267 · Cited by 248
Sasaki, Y., Vohra, B. P. S., Lund, F. E., & Milbrandt, J. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5469-08.2009 · Cited by 252
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
Satoh, A., Brace, C. S., Ben-Josef, G., West, T., Wozniak, D. F., Holtzman, D. M., Herzog, E. D., & Imai, S.-I. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.1385-10.2010 · Cited by 237
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Fu, M., Liu, M., Sauve, A. A., Jiao, X., Zhang, X., Wu, X., Powell, M. J., Yang, T., Gu, W. J., Avantaggiati, M. L., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00289-06 · Cited by 234
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Zhang, T., Berrocal, J. G., Frizzell, K. M., Gamble, M. J., DuMond, M. E., Krishnakumar, R., Yang, T., Sauve, A. A., & Kraus, W. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.016469 · Cited by 234
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Yaku, K., Okabe, K., Hikosaka, K., & Nakagawa, T. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00622 · Cited by 229
Watson, M., Roulston, A., Bélec, L., Billot, X., Marcellus, R., Bédard, D., Bernier, C., Branchaud, S., Chan, H., Dairi, K., et al. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00112-09 · Cited by 229
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Mehmel, M., Jovanović, N. D., & Spitz, U. P. (2020) · Nutrients · doi:10.3390/nu12061616 · Cited by 231
Skokowa, J., Lan, D., Thakur, B. K., Wang, F., Gupta, K., Cario, G., Brechlin, A. M., Schambach, A., Hinrichsen, L., Meyer, G., et al. (2009) · Nature Medicine · doi:10.1038/nm.1913 · Cited by 221
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
Li, Y., Zhang, Y., Dorweiler, B., Cui, D., Wang, T., Woo, C. W., Brunkan, C. S., Wolberger, C., Imai, S., & Tabas, I. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805866200 · Cited by 212
Self-citation
Metadata
- Authors
- Revollo, J. R., Grimm, A. A., & Imai, S.-I.
- Affiliations
- Washington University in St. Louis (US)
- Corresponding author
- Imai, Shin-ichiro
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-12
- Volume
- 279
- Issue
- 49
- Pages
- 50754-50763
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2108536847
- Cited by
- 1,010
- References
- 61
- Citations by year
- 2026: 31 · 2025: 34 · 2024: 54 · 2023: 43 · 2022: 52 · 2021: 49 · 2020: 57 · 2019: 51 · 2018: 56 · 2017: 62 · 2016: 48 · 2015: 51 · 2014: 41 · 2013: 58 · 2012: 55
- FWCI
- 9.04
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Ellison Medical Foundation
- Leukemia and Lymphoma Society
- 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 › Molecular Biology › Nuclear Structure and Function
- Keywords
- NAD biosynthesis, visfatin, nicotinamide mononucleotide adenylyltransferase, rate-limiting enzyme, mouse fibroblasts, gene expression profiling, aging
- MeSH terms
- Animals, Cell Differentiation, Chromatography, High Pressure Liquid, Dose-Response Relationship, Drug, Fibroblasts, Fungal Proteins, Kinetics, Luciferases, NAD, Nicotinamide-Nucleotide Adenylyltransferase, Pentosyltransferases, Phylogeny, Recombinant Proteins, Saccharomyces cerevisiae, Transcription, Genetic, Blotting, Western, Gene Library, Cytokines, Genes, Reporter, DNA, Complementary, Reverse Transcriptase Polymerase Chain Reaction, Catalytic Domain, Oligonucleotide Array Sequence Analysis, Sirtuins, NIH 3T3 Cells, Mice, Nicotinamide Phosphoribosyltransferase, Sirtuin 1
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