Slowing ageing by design: the rise of NAD+ and sirtuin-activating compounds

The Hallmarks of Aging

López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982 · see citing works

Resveratrol improves health and survival of mice on a high-calorie diet

Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290 · see citing works

Resveratrol Improves Mitochondrial Function and Protects against Metabolic Disease by Activating SIRT1 and PGC-1α

Lagouge, M., Argmann, C., Gerhart-Hines, Z., Meziane, H., Lerin, C., Daussin, F., Messadeq, N., Milne, J., Lambert, P., Elliott, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.11.013 · Cited by 4,057 · see citing works

Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan

Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796 · 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

A C. elegans mutant that lives twice as long as wild type

Kenyon, C., Chang, J., Gensch, E., Rudner, A., & Tabtiang, R. (1993) · Nature · doi:10.1038/366461a0 · Cited by 3,387 · 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

Nutrient 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

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 · see citing works

The genetics of ageing

Kenyon, C. J. (2010) · Nature · doi:10.1038/nature08980 · Cited by 2,739 · see citing works

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 2,653 · see citing works

The Effect of Retarded Growth Upon the Length of Life Span and Upon the Ultimate Body Size

McCay, C. M., Crowell, M. F., & Maynard, L. A. (1935) · The Journal of Nutrition · doi:10.1093/jn/10.1.63 · Cited by 2,264 · see citing works

The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms

Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253 · 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

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 · 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

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 · see citing works

Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans

Tissenbaum, H. A., & Guarente, L. (2001) · Nature · doi:10.1038/35065638 · Cited by 1,918 · see citing works

Sirtuin activators mimic caloric restriction and delay ageing in metazoans

Wood, J. G., Rogina, B., Lavu, S., Howitz, K., Helfand, S. L., Tatar, M., & Sinclair, D. (2004) · Nature · doi:10.1038/nature02789 · Cited by 1,868 · see citing works

Requirement of NAD and <i>SIR2</i> for Life-Span Extension by Calorie Restriction in <i>Saccharomyces cerevisiae</i>

Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775 · see citing works

Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes

Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707 · see citing works

SIRT1 is required for AMPK activation and the beneficial effects of resveratrol on mitochondrial function

Price, N. L., Gomes, A. P., Ling, A. J. Y., Duarte, F. V., Martin-Montalvo, A., North, B. J., Agarwal, B., Ye, L., Ramadori, G., Teodoro, J. S., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.003 · Cited by 1,602 · see citing works

Extrachromosomal rDNA circles—a cause of aging in yeast

Sinclair, D. A., & Guarente, L. (1997) · Cell · doi:10.1016/s0092-8674(00)80493-6 · Cited by 1,500 · see citing works

Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging

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

Metformin improves healthspan and lifespan in mice

Martin-Montalvo, A., Mercken, E. M., Mitchell, S. J., Palacios, H. H., Mote, P. L., Scheibye-Knudsen, M., Gomes, A. P., Ward, T. M., Minor, R. K., Blouin, M.-J., et al. (2013) · Nature Communications · doi:10.1038/ncomms3192 · Cited by 1,445 · see citing works

Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase

Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429 · 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

Sir2 mediates longevity in the fly through a pathway related to calorie restriction

Rogina, B., & Helfand, S. L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404184101 · Cited by 1,361 · see citing works

Resveratrol Ameliorates Aging-Related Metabolic Phenotypes by Inhibiting cAMP Phosphodiesterases

Park, S. J., Ahmad, F., Philp, A., Baar, K., Williams, T., Luo, H., Ke, H., Rehmann, H., Taussig, R., Brown, A. L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.01.017 · Cited by 1,352 · see citing works

Nicotinamide Mononucleotide, a Key NAD+ Intermediate, Treats the Pathophysiology of Diet- and Age-Induced Diabetes in Mice

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

Calorie Restriction-like Effects of 30 Days of Resveratrol Supplementation on Energy Metabolism and Metabolic Profile in Obese Humans

Timmers, S., Konings, E., Bilet, L., Houtkooper, R. H., van de Weijer, T., Goossens, G. H., Hoeks, J., van der Krieken, S., Ryu, D., Kersten, S., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.10.002 · Cited by 1,320 · see citing works

NAD ⁺ repletion improves mitochondrial and stem cell function and enhances life span in mice

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

The NAD+ Precursor Nicotinamide Riboside Enhances Oxidative Metabolism and Protects against High-Fat Diet-Induced Obesity

Cantó, 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

Regulation of pgc-1α, a nodal regulator of mitochondrial biogenesis

Fernandez-Marcos, P. J., & Auwerx, J. (2011) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.110.001917 · Cited by 1,237 · see citing works

The NAD+/Sirtuin Pathway Modulates Longevity through Activation of Mitochondrial UPR and FOXO Signaling

Mouchiroud, 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

SIRT4 Inhibits Glutamate Dehydrogenase and Opposes the Effects of Calorie Restriction in Pancreatic β Cells

Haigis, M. C., Mostoslavsky, R., Haigis, K. M., Fahie, K., Christodoulou, D. C., Murphy, A. J., Valenzuela, D. M., Yancopoulos, G. D., Karow, M., Blander, G., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.057 · Cited by 1,162 · see citing works

SIRT1 and other sirtuins in metabolism

Chang, H.-C., & Guarente, L. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.12.001 · Cited by 1,138 · see citing works

SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis

Kim, D., Nguyen, M. D., Dobbin, M. M., Fischer, A., Sananbenesi, F., Rodgers, J. T., Delalle, I., Baur, J. A., Sui, G., Armour, S. M., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601758 · Cited by 1,074 · see citing works

The sirtuin SIRT6 regulates lifespan in male mice

Kanfi, Y., Naiman, S., Amir, G., Peshti, V., Zinman, G., Nahum, L., Bar-Joseph, Z., & Cohen, H. Y. (2012) · Nature · doi:10.1038/nature10815 · Cited by 1,059 · see citing works

A mutation in the age-1 gene in Caenorhabditis elegans lengthens life and reduces hermaphrodite fertility.

Friedman, D. B., & Johnson, T. E. (1988) · Genetics · doi:10.1093/genetics/118.1.75 · Cited by 1,011 · see citing works

Inhibition of Silencing and Accelerated Aging by Nicotinamide, a Putative Negative Regulator of Yeast Sir2 and Human SIRT1

Bitterman, K. J., Anderson, R. M., Cohen, H. Y., Latorre-Esteves, M., & Sinclair, D. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205670200 · Cited by 1,002 · 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

Sirt1 protects against high-fat diet-induced metabolic damage

Pfluger, P. T., Herranz, D., Velasco-Miguel, S., Serrano, M., & Tschöp, M. H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802917105 · Cited by 928 · see citing works

SRT1720, 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

CD38 Dictates Age-Related NAD Decline and Mitochondrial Dysfunction through an SIRT3-Dependent Mechanism

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

SIRT6 Promotes DNA Repair Under Stress by Activating PARP1

Mao, Z., Hine, C., Tian, X., Van Meter, M., Au, M., Vaidya, A., Seluanov, A., & Gorbunova, V. (2011) · Science · doi:10.1126/science.1202723 · Cited by 867 · see citing works

Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology

Malavasi, F., Deaglio, S., Funaro, A., Ferrero, E., Horenstein, A. L., Ortolan, E., Vaisitti, T., & Aydin, S. (2008) · Physiological Reviews · doi:10.1152/physrev.00035.2007 · Cited by 862 · see citing works

SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging

Oberdoerffer, P., Michan, S., McVay, M., Mostoslavsky, R., Vann, J., Park, S.-K., Hartlerode, A., Stegmuller, J., Hafner, A., Loerch, P., et al. (2008) · Cell · doi:10.1016/j.cell.2008.10.025 · Cited by 852 · see citing works

SIRT1 Modulation of the Acetylation Status, Cytosolic Localization, and Activity of LKB1

Lan, F., Cacicedo, J. M., Ruderman, N., & Ido, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805711200 · Cited by 825 · see citing works

Glucose Restriction Inhibits Skeletal Myoblast Differentiation by Activating SIRT1 through AMPK-Mediated Regulation of Nampt

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 821 · see citing works

SIRT1 Regulates Hepatocyte Lipid Metabolism through Activating AMP-activated Protein Kinase

Hou, X., Xu, S., Maitland-Toolan, K. A., Sato, K., Jiang, B., Ido, Y., Lan, F., Walsh, K., Wierzbicki, M., Verbeuren, T. J., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802187200 · Cited by 778 · see citing works

A randomized, double-blind, placebo-controlled trial of resveratrol for Alzheimer disease

Turner, R. S., Thomas, R. G., Craft, S., van Dyck, C. H., Mintzer, J. E., Reynolds, B., Brewer, J. B., Rissman, R. A., Raman, R., Aisen, P. S. S., et al. (2015) · Neurology · doi:10.1212/wnl.0000000000002035 · Cited by 752 · see citing works

The first identification of lysine malonylation substrates and its regulatory enzyme

Peng, C., Lu, Z., Xie, Z., Cheng, Z., Chen, Y., Tan, M., Luo, H., Zhang, Y., He, W., Yang, K., et al. (2011) · Molecular &amp; Cellular Proteomics · doi:10.1074/mcp.m111.012658 · Cited by 751 · see citing works

Substrate-specific activation of sirtuins by resveratrol

Kaeberlein, M., McDonagh, T., Heltweg, B., Hixon, J., Westman, E. A., Caldwell, S. D., Napper, A., Curtis, R., DiStefano, P. S., Fields, S., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500655200 · Cited by 745 · see citing works

Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae

Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., & Sinclair, D. A. (2003) · Nature · doi:10.1038/nature01578 · Cited by 736 · see citing works

Sirt1 Extends Life Span and Delays Aging in Mice through the Regulation of Nk2 Homeobox 1 in the DMH and LH

Satoh, A., Brace, C. S., Rensing, N., Cliften, P. F., Wozniak, D. F., Herzog, E. D., Yamada, K. A., & Imai, S. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.07.013 · Cited by 734 · see citing works

SIRT1 transgenic mice show phenotypes resembling calorie restriction

Bordone, L., Cohen, D., Robinson, A., Motta, M. C., Van Veen, E., Czopik, A., Steele, A. D., Crowe, H., Marmor, S., Luo, J., et al. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00335.x · Cited by 722 · see citing works

Specific SIRT1 Activation Mimics Low Energy Levels and Protects against Diet-Induced Metabolic Disorders by Enhancing Fat Oxidation

Feige, J. N., Lagouge, M., Canto, C., Strehle, A., Houten, S. M., Milne, J. C., Lambert, P. D., Mataki, C., Elliott, P. J., & Auwerx, J. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.017 · Cited by 719 · see citing works

Four Genes Responsible for a Position Effect on Expression From HML and HMR in Saccharomyces cerevisiae

Rine, J., & Herskowitz, I. (1987) · Genetics · doi:10.1093/genetics/116.1.9 · Cited by 711 · see citing works

The effect of retarded growth upon the length of life span and upon the ultimate body size. 1935.

Cm, M., Crowell, M. F., & MAYNARD, L. A. (1989) · PubMed · Cited by 670 · see citing works

The histone deacetylase SIRT6 is a tumor suppressor that controls cancer metabolism

Sebastián, C., Zwaans, B. M. M., Silberman, D. M., Gymrek, M., Goren, A., Zhong, L., Ram, O., Truelove, J., Guimaraes, A. R., Toiber, D., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.047 · Cited by 660 · see citing works

Activation of the Protein Deacetylase SIRT6 by Long-chain Fatty Acids and Widespread Deacylation by Mammalian Sirtuins

Feldman, J. L., Baeza, J., & Denu, J. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.511261 · Cited by 637 · see citing works

SirT1 Gain of Function Increases Energy Efficiency and Prevents Diabetes in Mice

Banks, A. S., Kon, N., Knight, C. M., Matsumoto, M., Juárez, R. G., Rossetti, L., Gu, W. J., & Accili, D. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.014 · Cited by 636 · see citing works

Rapamycin‐mediated lifespan increase in mice is dose and sex dependent and metabolically distinct from dietary restriction

Miller, R. A., Harrison, D. E., Astle, C. M., Fernández, E., Flurkey, K., Han, M. L., Javors, M. A., Li, X., Nadon, N. L., Nelson, J. F., et al. (2013) · Aging Cell · doi:10.1111/acel.12194 · Cited by 624 · see citing works

Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila

Burnett, C., Valentini, S., Cabreiro, F., Goss, M., Somogyvári, M., Piper, M. D., Hoddinott, M., Sutphin, G. L., Leko, V., McElwee, J. J., et al. (2011) · Nature · doi:10.1038/nature10296 · Cited by 624 · see citing works

Evidence for a Common Mechanism of SIRT1 Regulation by Allosteric Activators

Hubbard, B. P., Gomes, A. P., Dai, H., Li, J., Case, A. W., Considine, T., Riera, T. V., Lee, J. E., Yen, E. S., Lamming, D. W., et al. (2013) · Science · doi:10.1126/science.1231097 · Cited by 618 · 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

The Mammalian SIR2α Protein Has a Role in Embryogenesis and Gametogenesis

McBurney, M. W., Yang, X., Jardine, K., Hixon, M., Boekelheide, K., Webb, J. R., Lansdorp, P. M., & Lemieux, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.38-54.2003 · Cited by 611 · see citing works

SARM1 activation triggers axon degeneration locally via NAD ⁺ 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

A low dose of dietary resveratrol partially mimics caloric restriction and retards aging parameters in mice

Barger, J. L., Kayo, T., Vann, J. M., Arias, E. B., Wang, J., Hacker, T. A., Wang, Y., Raederstorff, D., Morrow, J. D., Leeuwenburgh, C., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002264 · Cited by 580 · see citing works

Different dietary restriction regimens extend lifespan by both independent and overlapping genetic pathways in C. elegans

Greer, E. L., & Brunet, A. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00459.x · Cited by 574 · see citing works

Acetylation of the C Terminus of Ku70 by CBP and PCAF Controls Bax-Mediated Apoptosis

Cohen, H. Y., Lavu, S., Bitterman, K. J., Hekking, B., Imahiyerobo, T. A., Miller, C. M., Frye, R. A., Ploegh, H. L., Kessler, B. M., & Sinclair, D. A. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00094-2 · Cited by 574 · see citing works

Small molecule SIRT1 activators for the treatment of aging and age-related diseases

Hubbard, B. P., & Sinclair, D. A. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.12.004 · Cited by 572 · see citing works

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 561 · see citing works

Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1- O- acetyl-ADP-ribose

Tanner, K. G., Landry, J. W., Sternglanz, R., & Denu, J. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250422697 · Cited by 557 · see citing works

The multifaceted functions of sirtuins in cancer

Chalkiadaki, A., & Guarente, L. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3985 · Cited by 501 · see citing works

Mutation in the silencing gene S/R4 can delay aging in S. cerevisiae

Kennedy, B. K., Austriaco, N. P. G., Zhang, J., & Guarente, L. (1995) · Cell · doi:10.1016/0092-8674(95)90499-9 · Cited by 499 · 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

Resveratrol supplementation improves glycemic control in type 2 diabetes mellitus

Bhatt, J. K., Thomas, S., & Nanjan, M. J. (2012) · Nutrition Research · doi:10.1016/j.nutres.2012.06.003 · Cited by 475 · see citing works

SIRT6 represses LINE1 retrotransposons by ribosylating KAP1 but this repression fails with stress and age

Van Meter, M., Kashyap, M., Rezazadeh, S., Geneva, A. J., Morello, T. D., Seluanov, A., & Gorbunova, V. (2014) · Nature Communications · doi:10.1038/ncomms6011 · Cited by 455 · see citing works

High-Dose Resveratrol Supplementation in Obese Men

Poulsen, M. M., Vestergaard, P. F., Clasen, B. F., Radko, Y., Christensen, L. P., Stødkilde-Jørgensen, H., Møller, N., Jessen, N., Pedersen, S. B., & Jørgensen, J. O. L. (2013) · Diabetes · doi:10.2337/db12-0975 · Cited by 455 · see citing works

Resveratrol and Clinical Trials: The Crossroad from In Vitro Studies to Human Evidence

Tomé‐Carneiro, J., Larrosa, M., González‐Sarrías, A., Tomás-Barberán, F. A., García‐Conesa, M., & Espı́n, J. C. (2013) · Current Pharmaceutical Design · doi:10.2174/13816128113199990407 · Cited by 451 · see citing works

SirT1 Regulates Energy Metabolism and Response to Caloric Restriction in Mice

Boily, G., Seifert, E. L., Bevilacqua, L., He, X. H., Sabourin, G., Estey, C., Moffat, C., Crawford, S., Saliba, S., Jardine, K., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001759 · Cited by 444 · see citing works

Sir2-Independent Life Span Extension by Calorie Restriction in Yeast

Kaeberlein, M., Kirkland, K. T., Fields, S., & Kennedy, B. K. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020296 · Cited by 441 · see citing works

Effects of resveratrol on lifespan in Drosophila melanogaster and Caenorhabditis elegans

Bass, T. M., Weinkove, D., Houthoofd, K., Gems, D., & Partridge, L. (2007) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.07.007 · Cited by 435 · see citing works

A Role for SIR-2.1 Regulation of ER Stress Response Genes in Determining C. elegans Life Span

Viswanathan, M., Kim, S. K., Berdichevsky, A., & Guarente, L. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.09.017 · Cited by 409 · see citing works

Longitudinal Trajectories of Arterial Stiffness and the Role of Blood Pressure

AlGhatrif, M., Strait, J. B., Morrell, C. H., Canepa, M., Wright, J. G., Elango, P., Scuteri, A., Najjar, S. S., Ferrucci, L., & Lakatta, E. G. (2013) · Hypertension · doi:10.1161/hypertensionaha.113.01445 · Cited by 409 · see citing works

The SIRT1 Activator SRT1720 Extends Lifespan and Improves Health of Mice Fed a Standard Diet

Mitchell, S. J., Martín‐Montalvo, A., Mercken, E. M., Palacios, H. H., Ward, T. M., Abulwerdi, G. A., Minor, R. K., Vlasuk, G. P., Ellis, J. L., Sinclair, D. A., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.01.031 · Cited by 399 · see citing works

SIRT1 Negatively Regulates the Mammalian Target of Rapamycin

Ghosh, H. S., McBurney, M., & Robbins, P. D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009199 · Cited by 397 · see citing works

Poly(ADP-ribose) Polymerase-1-dependent Cardiac Myocyte Cell Death during Heart Failure Is Mediated by NAD+ Depletion and Reduced Sir2α Deacetylase Activity

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 functions and modulation: from chemistry to the clinic

Carafa, V., Rotili, D., Forgione, M., Cuomo, F., Serretiello, E., Hailu, G. S., Jarho, E., Lahtela-Kakkonen, M., Mai, A., & Altucci, L. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0224-3 · Cited by 387 · 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

Mechanism of inhibition of bovine F 1 -ATPase by resveratrol and related polyphenols

Gledhill, J. R., Montgomery, M. G., Leslie, A. G. W., & Walker, J. E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706290104 · Cited by 379 · see citing works

Redistribution of silencing proteins from telomeres to the nucleolus is associated with extension of life span in S. cerevisiae

Kennedy, B. K., Gotta, M., Sinclair, D. A., Mills, K., McNabb, D. S., Murthy, M., Pak, S. M., Laroche, T., Gasser, S. M., & Guarente, L. (1997) · Cell · doi:10.1016/s0092-8674(00)80219-6 · Cited by 375 · see citing works

Cardioprotection by resveratrol: A human clinical trial in patients with stable coronary artery disease

Magyar, K., Halmosi, R., Pálfi, A., Fehér, G., Czopf, L., Fulop, A., Battyány, I., Sümegi, B., Tóth, K., & Szabados, E. (2012) · Clinical Hemorheology and Microcirculation · doi:10.3233/ch-2011-1424 · Cited by 364 · see citing works

A high-fat diet and NAD(+) activate Sirt1 to rescue premature aging in Cockayne syndrome

Scheibye-Knudsen, M., Mitchell, S. J., Fang, E. F., Iyama, T., Ward, T., Wang, J., Dunn, C. A., Singh, N., Veith, S., Hasan-Olive, M. M., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.10.005 · Cited by 352 · see citing works

Conserved role of SIRT1 orthologs in fasting-dependent inhibition of the lipid/cholesterol regulator SREBPPreprint

Walker, A. K., Yang, F., Jiang, K., Ji, J., Watts, J. L., Purushotham, A., Boss, O., Hirsch, M. L., Ribich, S. A., Smith, J. J., et al. (2010) · Genes & Development · doi:10.1101/gad.1901210 · Cited by 352 · see citing works

Nicotinamide riboside restores cognition through an upregulation of proliferator-activated receptor-γ coactivator 1α regulated β-secretase 1 degradation and mitochondrial gene expression in Alzheimer's mouse models

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

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

SirT1 inhibition reduces IGF-I/IRS-2/Ras/ERK1/2 signaling and protects neurons

Li, Y., Xu, W., McBurney, M. W., & Longo, V. D. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.05.004 · Cited by 331 · see citing works

The cAMP/PKA Pathway Rapidly Activates SIRT1 to Promote Fatty Acid Oxidation Independently of Changes in NAD+

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

Age‐associated loss of Sirt1‐mediated enhancement of glucose‐stimulated insulin secretion in beta cell‐specific Sirt1‐overexpressing (BESTO) mice

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 · see citing works

Of mice and men: the benefits of caloric restriction, exercise, and mimetics

Mercken, E. M., Carboneau, B. A., Krzysik-Walker, S. M., & de Cabo, R. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2011.11.005 · Cited by 318 · see citing works

SIRT6 protects against pathological damage caused by diet‐induced obesity

Kanfi, Y., Peshti, V., Gil, R., Naiman, S., Nahum, L., Levin, E., Kronfeld‐Schor, N., & Cohen, H. Y. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2009.00544.x · Cited by 311 · see citing works

Xenohormesis: Sensing the Chemical Cues of Other Species

Howitz, K. T., & Sinclair, D. A. (2008) · Cell · doi:10.1016/j.cell.2008.04.019 · Cited by 301 · see citing works

SRT1720 improves survival and healthspan of obese mice

Minor, R. K., Baur, J. A., Gomes, A. P., Ward, T. M., Csiszár, A., Mercken, E. M., Abdelmohsen, K., Shin, Y., Cantó, C., Scheibye‐Knudsen, M., et al. (2011) · Scientific Reports · doi:10.1038/srep00070 · Cited by 297 · see citing works

Manipulation of a Nuclear NAD+ Salvage Pathway Delays Aging without Altering Steady-state NAD+ Levels

Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., Cohen, H. Y., Lin, S., Manchester, J. K., Gordon, J. I., & Sinclair, D. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111773200 · Cited by 295 · see citing works

Pilot study of resveratrol in older adults with impaired glucose tolerance

Crandall, J. P., Oram, V., Trandafirescu, G., Reid, M., Kishore, P., Hawkins, M., Cohen, H. W., & Barzilai, N. (2012) · The Journals of Gerontology: Series A · doi:10.1093/gerona/glr235 · Cited by 281 · see citing works

Activation of SIRT3 by the NAD(+) precursor nicotinamide riboside protects from noise-induced hearing loss

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

Acute resveratrol supplementation improves flow-mediated dilatation in overweight/obese individuals with mildly elevated blood pressure

Wong, R. H. X., Howe, P. R. C., Buckley, J. D., Coates, A. M., Kunz, I., & Berry, N. M. (2011) · Nutrition, Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2010.03.003 · 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

Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington’s disease

Pallos, J., Bodai, L., Lukácsovich, T., Purcell, J. M., Steffan, J. S., Thompson, L. M., & Marsh, J. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn273 · Cited by 265 · see citing works

Overlapping and distinct functions for a Caenorhabditis elegans SIR2 and DAF-16/FOXO

Wang, Y., & Tissenbaum, H. A. (2005) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2005.09.005 · Cited by 263 · see citing works

Nicotinamide N-methyltransferase regulates hepatic nutrient metabolism through Sirt1 protein stabilization

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 258 · see citing works

Role of NAD+ in the Deacetylase Activity of the SIR2-like Proteins

Landry, J. W., Slama, J. T., & Sternglanz, R. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3854 · Cited by 254 · see citing works

Effects of resveratrol on the rat brain respiratory chain.

Zini, R., Morin, C., Bertelli, A., Bertelli, A., & Tillement, J. P. (1999) · PubMed · Cited by 252 · see citing works

SIRT6 suppresses pancreatic cancer through control of Lin28b

Kugel, S., Sebastián, C., Fitamant, J., Ross, K., Saha, S., Jain, E., Gladden, A., Arora, K. S., Kato, Y., Rivera, M., et al. (2016) · Cell · doi:10.1016/j.cell.2016.04.033 · Cited by 251 · 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

SIRT1-Mediated eNAMPT Secretion from Adipose Tissue Regulates Hypothalamic NAD+ and Function in Mice

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 242 · see citing works

Three Mutants That Extend Both Mean and Maximum Life Span of the Nematode, Caenorhabditis Elegans, Define the Age-1 Gene

Friedman, D. B., & Johnson, T. E. (1988) · Journal of Gerontology · doi:10.1093/geronj/43.4.b102 · Cited by 240 · see citing works

Resveratrol Improves Adipose Insulin Signaling and Reduces the Inflammatory Response in Adipose Tissue of Rhesus Monkeys on High-Fat, High-Sugar Diet

Jiménez, Y., Mattison, J. A., Pearson, K. J., Martín‐Montalvo, A., Palacios, H. H., Sossong, A. M., Ward, T. M., Younts, C. M., Lewis, K. N., Allard, J. S., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.09.004 · Cited by 240 · see citing works

Role of sirtuins in lifespan regulation is linked to methylation of nicotinamide

Schmeisser, K., Mansfeld, J., Kuhlow, D., Weimer, S., Priebe, S., Heiland, I., Birringer, M., Groth, M., Segref, A., Kanfi, Y., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1352 · Cited by 236 · see citing works

SRT 2104 extends survival of male mice on a standard diet and preserves bone and muscle mass

Mercken, E. M., Mitchell, S. J., Martín‐Montalvo, A., Minor, R. K., Almeida, M., Gomes, A. P., Scheibye‐Knudsen, M., Palacios, H. H., Licata, J. J., Zhang, Y., et al. (2014) · Aging Cell · doi:10.1111/acel.12220 · Cited by 235 · see citing works

An accelerated assay for the identification of lifespan-extending interventions in <i>Drosophila</i> melanogaster

Bauer, J. H., Goupil, S., Garber, G. B., & Helfand, S. L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403493101 · Cited by 234 · see citing works

HST2 Mediates SIR2 -Independent Life-Span Extension by Calorie Restriction

Lamming, D. W., Latorre‐Esteves, M., Medvedik, O., Wong, S. N., Tsang, F. A., Wang, C., Lin, S.-J., & Sinclair, D. A. (2005) · Science · doi:10.1126/science.1113611 · Cited by 228 · see citing works

Turning enzymes ON with small molecules

Zorn, J. A., & Wells, J. A. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.318 · Cited by 220 · see citing works

Crystallographic structure of a small molecule SIRT1 activator-enzyme complex

Dai, H., Case, A. W., Riera, T. V., Considine, T., Lee, J. E., Hamuro, Y., Zhao, H., Jiang, Y., Sweitzer, S. M., Pietrak, B., et al. (2015) · Nature Communications · doi:10.1038/ncomms8645 · Cited by 217 · see citing works

Substrate Specificity and Kinetic Mechanism of the Sir2 Family of NAD+-Dependent Histone/Protein Deacetylases

Borra, M. T., Langer, M. R., Slama, J. T., & Denu, J. M. (2004) · Biochemistry · doi:10.1021/bi049592e · Cited by 214 · see citing works

Autophagy mediates pharmacological lifespan extension by spermidineand resveratrol

Morselli, E., Galluzzi, L., Kepp, O., Criollo, A., Maiuri, M. C., Tavernarakis, N., Madeo, F., & Kroemer, G. (2009) · Aging · doi:10.18632/aging.100110 · Cited by 213 · see citing works

SIRT1 Activation by Small Molecules

Dai, H., Kustigian, L. M., Carney, D. P., Case, A. W., Considine, T., Hubbard, B. P., Perni, R. B., Riera, T. V., Szczepankiewicz, B. G., Vlasuk, G. P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.133892 · Cited by 211 · 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

Resveratrol Prevents High Fat/Sucrose Diet-Induced Central Arterial Wall Inflammation and Stiffening in Nonhuman Primates

Mattison, J. A., Wang, M., Bernier, M., Zhang, J., Park, S. S., Maudsley, S. R., An, S. S., Santhanam, L., Martin, B., Faulkner, S., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.018 · Cited by 206 · see citing works

Quantitative Acetylome Analysis Reveals the Roles of SIRT1 in Regulating Diverse Substrates and Cellular Pathways

Chen, Y., Zhao, W., Yang, J. S., Cheng, Z., Luo, H., Lu, Z., Tan, M., Gu, W. J., & Zhao, Y. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.019547 · Cited by 202 · see citing works

NAD ⁺ metabolism: A therapeutic target for age-related metabolic disease

Mouchiroud, L., Houtkooper, R. H., & Auwerx, J. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.789479 · Cited by 193 · see citing works

Regulation of Caenorhabditis elegans lifespan by sir-2.1 transgenes

Viswanathan, M., & Guarente, L. (2011) · Nature · doi:10.1038/nature10440 · Cited by 191 · see citing works

Kinetic and Structural Basis for Acyl-Group Selectivity and NAD+ Dependence in Sirtuin-Catalyzed Deacylation

Feldman, J. L., Dittenhafer‐Reed, K. E., Kudo, N., Thelen, J. N., Ito, A., Yoshida, M., & Denu, J. M. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00150 · Cited by 189 · see citing works

Regulation of WRN Protein Cellular Localization and Enzymatic Activities by SIRT1-mediated Deacetylation

Li, K., Casta, A., Wang, R., Lozada, E., Fan, W., Kane, S. E., Ge, Q., Gu, W. J., Orren, D. K., & Luo, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709707200 · Cited by 177 · see citing works

Resveratrol Inhibits mTOR Signaling by Promoting the Interaction between mTOR and DEPTOR

Liu, M., Wilk, S. A., Wang, A., Zhou, L., Wang, R.-H., Ogawa, W., Deng, C., Dong, L., & Liu, F. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.169284 · Cited by 177 · see citing works

Resveratrol treatment as an adjunct to pharmacological management in type 2 diabetes mellitus—systematic review and meta‐analysis

Hausenblas, H. A., Schoulda, J. A., & Smoliga, J. M. (2014) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201400173 · Cited by 175 · see citing works

SIRT1 and AMPK in regulating mammalian senescence: A critical review and a working model

Wang, Y., Liang, Y. Q., & Vanhoutte, P. M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.11.047 · Cited by 175 · see citing works

Caloric restriction: From soup to nuts

Spindler, S. R. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.10.003 · Cited by 168 · see citing works

Resveratrol Levels and All-Cause Mortality in Older Community-Dwelling Adults

Semba, R. D., Ferrucci, L., Bartali, B., Urpí-Sardà, M., Zamora‐Ros, R., Sun, K., Cherubini, A., Bandinelli, S., & Andrés‐Lacueva, C. (2014) · JAMA Internal Medicine · doi:10.1001/jamainternmed.2014.1582 · Cited by 168 · see citing works

Early combination therapy for the treatment of type 2 diabetes mellitus: systematic review and meta‐analysis

Phung, O. J., Sobieraj, D. M., Engel, S. S., & Rajpathak, S. N. (2013) · Diabetes Obesity and Metabolism · doi:10.1111/dom.12233 · Cited by 164 · see citing works

Evidence for a Trade‐Off between Survival and Fitness Caused by Resveratrol Treatment of Caenorhabditis elegans

Gruber, J., Tang, S. Y., & Halliwell, B. B. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1395.059 · Cited by 163 · see citing works

CD73 Protein as a Source of Extracellular Precursors for Sustained NAD+ Biosynthesis in FK866-treated Tumor Cells

Grozio, A., Sociali, G., Sturla, L., Caffa, I., Soncini, D., Salis, A., Raffaelli, N., De Flora, A., Nencioni, A., & Bruzzone, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.470435 · Cited by 158 · see citing works

Inhibition of mammalian S6 kinase by resveratrol suppresses autophagy

Armour, S. M., Baur, J. A., Hsieh, S. N., Land-Bracha, A., Thomas, S. Μ., & Sinclair, D. A. (2009) · Aging · doi:10.18632/aging.100056 · Cited by 156 · see citing works

A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol

Sajish, M., & SCHIMMEL, P. R. (2014) · Nature · doi:10.1038/nature14028 · Cited by 152 · see citing works

SIRT1 Modulating Compounds from High-Throughput Screening as Anti-Inflammatory and Insulin-Sensitizing Agents

Nayagam, V. M., Wang, X., Tan, Y. C., Poulsen, A., Goh, K. C., Ng, T., Wang, H., Song, H. Y., Ni, B., Entzeroth, M., et al. (2006) · SLAS DISCOVERY · doi:10.1177/1087057106294710 · Cited by 150 · see citing works

The Sirt1 activator SRT3025 provides atheroprotection in Apoe−/− mice by reducing hepatic Pcsk9 secretion and enhancing Ldlr expression

Miranda, M. X., van Tits, L. J., Lohmann, C., Arsiwala, T., Winnik, S. H., Tailleux, A., Stein, S. M. A., Gomes, A. P., Suri, V., Ellis, J. L., et al. (2014) · European Heart Journal · doi:10.1093/eurheartj/ehu095 · Cited by 150 · see citing works

Resveratrol activates duodenal Sirt1 to reverse insulin resistance in rats through a neuronal network

Côté, C. D., Rasmussen, B. A., Duca, F. A., Zadeh‐Tahmasebi, M., Baur, J. A., Daljeet, M., Breen, D. M., Filippi, B., & Lam, T. K. T. (2015) · Nature Medicine · doi:10.1038/nm.3821 · Cited by 148 · see citing works

A Pilot Randomized, Placebo Controlled, Double Blind Phase I Trial of the Novel SIRT1 Activator SRT2104 in Elderly Volunteers

Libri, V., Brown, A., Gambarota, G., Haddad, J., Shields, G. S., Dawes, H., Pinato, D. J., Hoffman, E., Elliot, P. J., Vlasuk, G. P., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051395 · Cited by 145 · see citing works

The caloric restriction paradigm: Implications for healthy human aging

Anderson, R. M., & Weindruch, R. H. (2012) · American Journal of Human Biology · doi:10.1002/ajhb.22243 · Cited by 144 · see citing works

Discovery, synthesis, and biological evaluation of thiazoloquin(az)olin(on)es as potent CD38 inhibitors

Haffner, C. D., Becherer, J. D., Boros, E. E., Cadilla, R., Carpenter, T., Cowan, D., Deaton, D. N., Guo, Y., Harrington, W., Henke, B. R., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm502009h · Cited by 137 · see citing works

SirT1-null mice develop tumors at normal rates but are poorly protected by resveratrol

Boily, G., He, X. H., Pearce, B., Jardine, K. E., & McBurney, M. W. (2009) · Oncogene · doi:10.1038/onc.2009.147 · Cited by 136 · see citing works

Resveratrol Prevents β-Cell Dedifferentiation in Nonhuman Primates Given a High-Fat/High-Sugar Diet

Fiori, J. L., Shin, Y., Kim, W., Krzysik-Walker, S. M., González‐Mariscal, I., Carlson, O. D., Sanghvi, M., Moaddel, R., Farhang, K., Gadkaree, S. K., et al. (2013) · Diabetes · doi:10.2337/db13-0266 · Cited by 136 · see citing works

Gene expression profiling of aging in multiple mouse strains: identification of aging biomarkers and impact of dietary antioxidants

Park, S., Kim, K., Page, G. P., Allison, D. B., Weindruch, R., & Prolla, T. A. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00496.x · Cited by 134 · see citing works

Pharmacokinetics and tolerability of SRT 2104, a first‐in‐class small molecule activator of SIRT 1, after single and repeated oral administration in man

Hoffmann, E. C., Wald, J., Lavu, S., Roberts, J., Beaumont, C., Haddad, J., Elliott, P. J., Westphal, C. H., & Jacobson, E. W. (2012) · British Journal of Clinical Pharmacology · doi:10.1111/j.1365-2125.2012.04340.x · Cited by 133 · see citing works

A dietary regimen of caloric restriction or pharmacological activation of SIRT1 to delay the onset of neurodegeneration

Gräff, J., Kahn, M., Samiei, A., Gao, J., Ota, K. T., Rei, D., & Tsai, L.-H. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.5657-12.2013 · Cited by 124 · see citing works

SIRT6 rescues the age related decline in base excision repair in a PARP1-dependent manner

Xu, Z., Zhang, L., Zhang, W., Du, M., Zhang, H., Jiang, Y., Xu, X., Meter, M. V., Seluanov, A., Gorbunova, V. A., et al. (2015) · Cell Cycle · doi:10.4161/15384101.2014.980641 · Cited by 118 · see citing works

Sirt1 activation by resveratrol is substrate sequence-selective

Lakshminarasimhan, M., Rauh, D., Schutkowski, M., & Steegborn, C. (2013) · Aging · doi:10.18632/aging.100542 · Cited by 117 · see citing works

The Evolutionarily Conserved Longevity Determinants HCF-1 and SIR-2.1/SIRT1 Collaborate to Regulate DAF-16/FOXO

Rizki, G., Iwata, T., Li, J., Riedel, C. G., Picard, C. L., Jan, M., Murphy, C. T., & Lee, S. S. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002235 · Cited by 116 · see citing works

The lifespan extension effects of resveratrol are conserved in the honey bee and may be driven by a mechanism related to caloric restriction

Rascón, B., Hubbard, B. P., Sinclair, D. A., & Amdam, G. V. (2012) · Aging · doi:10.18632/aging.100474 · Cited by 116 · see citing works

Molecular mechanisms of yeast aging

Sinclair, D. A., Mills, K. D., & Guarente, L. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01188-8 · Cited by 115 · see citing works

Sirtuin‐independent effects of nicotinamide on lifespan extension from calorie restriction in yeast

Tsuchiya, M., Dang, N., Kerr, E. O., Hu, D., Steffen, K. K., Oakes, J. A., Kennedy, B. K., & Kaeberlein, M. R. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00240.x · Cited by 115 · see citing works

dSir2 in the Adult Fat Body, but Not in Muscles, Regulates Life Span in a Diet-Dependent Manner

Banerjee, K. K., Ayyub, C., Syed, Z. A., Mandot, V., Prasad, N. G., & Kolthur‐Seetharam, U. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.11.013 · Cited by 113 · see citing works

A novel assay for replicative lifespan in

Jarolim, S., Millen, J. I., Heeren, G., Laun, P., Goldfarb, D. S., & Breitenbach, M. (2004) · FEMS Yeast Research · doi:10.1016/j.femsyr.2004.06.015 · Cited by 104 · see citing works

A Randomized, Placebo-Controlled Study of SRT2104, a SIRT1 Activator, in Patients with Moderate to Severe Psoriasis

Krueger, J. G., Suárez‐Fariñas, M., Cueto, I., Khatcherian, A., Matheson, R. T., Parish, L. C., Leonardi, C. L., Shortino, D., Gupta, A., Haddad, J., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0142081 · Cited by 104 · see citing works

Increased expression of Drosophila Sir 2 extends life span in a dose-dependent manner

Whitaker, R., Faulkner, S., Miyokawa, R., Burhenn, L., Henriksen, M., Wood, J. G., & Helfand, S. L. (2013) · Aging · doi:10.18632/aging.100599 · Cited by 103 · see citing works

Resveratrol sensitizes melanomas to TRAIL through modulation of antiapoptotic gene expression

Ivanov, V. N., Partridge, M. A., Johnson, G. E., Huang, S. X. L., Zhou, H., & Hei, T. K. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.12.012 · Cited by 98 · see citing works

dSir2 and Dmp53 interact to mediate aspects of CR-dependent life span extension in D. melanogaster

Bauer, J. H., Morris, S. N. S., Chang, C.-Y., Flatt, T., Wood, J. G., & Helfand, S. L. (2008) · Aging · doi:10.18632/aging.100001 · Cited by 97 · see citing works

The high-resolution crystal structure of periplasmic<i>Haemophilus influenzae</i>NAD nucleotidase reveals a novel enzymatic function of human CD73 related to NAD metabolism

Garavaglia, S., Bruzzone, S., Cassani, C., Canella, L., Allegrone, G., Sturla, L., Mannino, E., Millo, E., De Flora, A., & Rizzi, M. (2012) · Biochemical Journal · doi:10.1042/bj20111263 · Cited by 94 · see citing works

Cardiovascular Effects of a Novel SIRT1 Activator, SRT2104, in Otherwise Healthy Cigarette Smokers

Venkatasubramanian, S., Noh, R. M., Daga, S., Langrish, J. P., Joshi, N. V., Mills, N. L., Hoffmann, E. C., Jacobson, E. W., Vlasuk, G. P., Waterhouse, B. R., et al. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.113.000042 · Cited by 92 · see citing works

Dietary restriction involves NAD +‐dependent mechanisms and a shift toward oxidative metabolism

Moroz, N., Carmona, J. J., Anderson, E. N., Hart, A. C., Sinclair, D. A., & Blackwell, T. K. (2014) · Aging Cell · doi:10.1111/acel.12273 · Cited by 90 · see citing works

Short-term consumption of a resveratrol-containing nutraceutical mixture mimics gene expression of long-term caloric restriction in mouse heart

Barger, J. L., Kayo, T., Pugh, T. D., Prolla, T. A., & Weindruch, R. H. (2008) · Experimental Gerontology · doi:10.1016/j.exger.2008.06.013 · Cited by 89 · see citing works

Resveratrol and the Pharmacology of Aging: A New Vertebrate Model to Validate an Old Molecule

Valenzano, D. R., & Cellerino, A. (2006) · Cell Cycle · doi:10.4161/cc.5.10.2739 · Cited by 85 · see citing works

Optimizing Dietary Restriction for Genetic Epistasis Analysis and Gene Discovery in C. elegans

Mair, W. B., Panowski, S. H., Shaw, R. J., & Dillin, A. G. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004535 · Cited by 85 · see citing works

Linking sirtuins, IGF-I signaling, and starvation

Longo, V. D. (2008) · Experimental Gerontology · doi:10.1016/j.exger.2008.06.005 · Cited by 84 · see citing works

The Drosophila melanogaster sir2+ Gene Is Nonessential and Has Only Minor Effects on Position-Effect Variegation

Åström, S. U., Cline, T. W., & Rine, J. (2003) · Genetics · doi:10.1093/genetics/163.3.931 · Cited by 83 · see citing works

NAD+ metabolite levels as a function of vitamins and calorie restriction: evidence for different mechanisms of longevity

Evans, C., Bogan, K. L., Song, P., Burant, C. F., Kennedy, R. T., & Brenner, C. (2010) · BMC Chemical Biology · doi:10.1186/1472-6769-10-2 · Cited by 81 · see citing works

Overexpression of Sir2 in the adult fat body is sufficient to extend lifespan of male and female Drosophila

Hoffmann, J., Romey, R., Fink, C., Yong, L., & Roeder, T. (2013) · Aging · doi:10.18632/aging.100553 · Cited by 81 · see citing works

Effects of resveratrol on longevity, cognitive ability and aging-related histological markers in the annual fish Nothobranchius guentheri

Yu, X., & Li, G. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.08.009 · Cited by 78 · see citing works

The N-Terminal Domain of SIRT1 Is a Positive Regulator of Endogenous SIRT1-Dependent Deacetylation and Transcriptional Outputs

Ghisays, F., Brace, C. S., Yackly, S. M., Kwon, H. J., Mills, K. F., Kashentseva, E. A., Dmitriev, I. P., Curiel, D. T., Imai, S., & Ellenberger, T. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.02.036 · Cited by 77 · see citing works

Locus specificity determinants in the multifunctional yeast silencing protein Sir2

Cuperus, G., Shafaatian, R., & Shore, D. (2000) · The EMBO Journal · doi:10.1093/emboj/19.11.2641 · Cited by 75 · see citing works

Natural genetic variation in yeast longevityPreprint

Stumpferl, S. W., Brand, S. E., Jiang, J. C., Korona, B., Tiwari, A., Dai, J., Seo, J., & Jazwinski, S. M. (2012) · Genome Research · doi:10.1101/gr.136549.111 · Cited by 73 · see citing works

SnapShot: Sirtuins, NAD, and Aging

Nakagawa, T., & Guarente, L. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.06.001 · Cited by 71 · see citing works

A Drosophila Homologue of Sir2 Modifies Position-Effect Variegation but Does Not Affect Life Span

Newman, B., Lundblad, J. R., Chen, Y., & Smolik, S. M. (2002) · Genetics · doi:10.1093/genetics/162.4.1675 · Cited by 66 · see citing works

The joint action on healthy life years (JA: EHLEIS)

the JA: EHLEIS team, Robine, J., Cambois, E., Nusselder, W. J., Jeune, B., Oyen, H. J. V., & Jagger, C. (2013) · Archives of Public Health · doi:10.1186/0778-7367-71-2 · Cited by 65 · see citing works

Molgramostim to treat SS-sickle cell leg ulcers

Pieters, R., Rojer, R. A., Saleh, A. W., Saleh, A. E. C., & Duits, A. (1995) · The Lancet · doi:10.1016/s0140-6736(95)90629-0 · Cited by 64 · see citing works

Resveratrol Attenuates Oxidative Stress and Extends Life Span in the Annual Fish Nothobranchius guentheri

Liu, T., Qi, H., Ma, L., Liu, Z., Fu, H., Zhu, W., Song, T., Yang, B., & Li, G. (2015) · Rejuvenation Research · doi:10.1089/rej.2014.1618 · Cited by 60 · see citing works

Anti-ageing pill pushed as bona fide drug

Hayden, E. C. (2015) · Nature · doi:10.1038/522265a · Cited by 58 · see citing works

Characterization of Nuclear Sirtuins: Molecular Mechanisms and Physiological Relevance

Toiber, D., Sebastián, C., & Mostoslavsky, R. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_9 · Cited by 55 · see citing works

The Caenorhabditis elegans nicotinamidase PNC-1 enhances survival

van der Horst, A., Schavemaker, J. M., Berkel, W. P.-V., & Burgering, B. M. T. (2007) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.01.004 · Cited by 54 · see citing works

Differential Effects of Resveratrol and SRT1720 on Lifespan of AdultCaenorhabditis elegans

Zarse, K., Schmeisser, S., Birringer, M., Falk, E., Schmoll, D., & Ristow, M. (2010) · Hormone and Metabolic Research · doi:10.1055/s-0030-1265225 · Cited by 43 · see citing works

Resveratrol extends lifespan and preserves glia but not neurons of the Nothobranchius guentheri optic tectum

Genade, T., & Lang, D. M. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.11.013 · Cited by 40 · see citing works

dSir2 mediates the increased spontaneous physical activity in flies on calorie restriction

Parashar, V., & Rogina, B. (2009) · Aging · doi:10.18632/aging.100061 · Cited by 38 · see citing works

Expression and localization of Werner syndrome protein is modulated by SIRT1 and PML

Vaitiekunaite, R., Butkiewicz, D., Krześniak, M., Przybyłek, M., Gryc, A., Śnietura, M., Benedyk‐Machaczka, M., Harris, C. C., & Rusin, M. (2007) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.09.004 · Cited by 36 · see citing works

Calorie Restriction-Mediated Replicative Lifespan Extension in Yeast Is Non-Cell Autonomous

Mei, S.-C., & Brenner, C. (2015) · PLoS Biology · doi:10.1371/journal.pbio.1002048 · Cited by 22 · see citing works

Potent SIRT1 Enzyme-stimulating and Anti-glycation Activities of Polymethoxyflavonoids from Kaempferia parviflora

Nakata, A., Koike, Y., Matsui, H., Shimada, T., Aburada, M., & Yang, J. (2014) · Natural Product Communications · doi:10.1177/1934578x1400900918 · Cited by 20 · see citing works

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

From discoveries in ageing research to therapeutics for healthy ageing

Campisi, J., Kapahi, P., Lithgow, G. J., Melov, S., Newman, J. C., & Verdin, E. (2019) · Nature · doi:10.1038/s41586-019-1365-2 · Cited by 1,389 · see citing works

Functions and mechanisms of non-histone protein acetylation

Narita, T., Weinert, B. T., & Choudhary, C. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0081-3 · Cited by 1,232 · see citing works

The effects of polyphenols and other bioactives on human health

Fraga, C. G., Croft, K. D., Kennedy, D. O., & Tomás-Barberán, F. A. (2019) · Food & Function · doi:10.1039/c8fo01997e · Cited by 1,150 · see citing works

Why does COVID-19 disproportionately affect older people?

Mueller, A. L., McNamara, M. S., & Sinclair, D. A. (2020) · Aging · doi:10.18632/aging.103344 · Cited by 1,128 · see citing works

Modulation of cellular processes by histone and non-histone protein acetylation

Shvedunova, M., & Akhtar, A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00441-y · Cited by 975 · 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

NAD+ in Brain Aging and Neurodegenerative Disorders

Lautrup, S., Sinclair, D. A., Mattson, M. P., & Fang, E. F. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.09.001 · Cited by 790 · see citing works

Regulation of SIRT1 and Its Roles in Inflammation

Yang, Y., Liu, Y., Wang, Y., Chao, Y., Zhang, J., Jia, Y., Tie, J., & Hu, D. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.831168 · Cited by 721 · see citing works

The metabolic roots of senescence: mechanisms and opportunities for intervention

Wiley, C. D., & Campisi, J. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00483-8 · Cited by 691 · see citing works

Epigenetic regulation of aging: implications for interventions of aging and diseases

Kang, W., Liu, H., Hu, Q., Wang, L., Liu, J., Zheng, Z., Zhang, W., Ren, J., Zhu, F., & Liu, G. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01211-8 · Cited by 694 · 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

Meta-hallmarks of aging and cancer

López-Otín, C., Pietrocola, F., Roiz-Valle, D., Galluzzi, L., & Kroemer, G. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2022.11.001 · Cited by 529 · see citing works

NAD+ metabolism, stemness, the immune response, and cancer

Navas, L. E., & Carnero, A. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00354-w · Cited by 529 · see citing works

Immunosenescence: a key player in cancer development

Lian, J., Yue, Y., Yu, W., & Zhang, Y. (2020) · Journal of Hematology &amp; Oncology · doi:10.1186/s13045-020-00986-z · Cited by 510 · 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

Sirtuins and NAD + in the Development and Treatment of Metabolic and Cardiovascular Diseases

Kane, A. E., & Sinclair, D. A. (2018) · Circulation Research · doi:10.1161/circresaha.118.312498 · Cited by 490 · see citing works

NAD ⁺ supplementation normalizes key Alzheimer’s features and DNA damage responses in a new AD mouse model with introduced DNA repair deficiency

Hou, Y., Lautrup, S., Cordonnier, S., Wang, Y., Croteau, D. L., Zavala, E., Zhang, Y., Moritoh, K., O’Connell, J. F., Baptiste, B. A., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718819115 · Cited by 472 · see citing works

Sirtuins, a promising target in slowing down the ageing process

Grabowska, W., Sikora, E., & Bielak-Zmijewska, A. (2017) · Biogerontology · doi:10.1007/s10522-017-9685-9 · Cited by 470 · see citing works

Sirtuin activators and inhibitors: Promises, achievements, and challenges

Dai, H., Sinclair, D. A., Ellis, J. L., & Steegborn, C. (2018) · Pharmacology &amp; Therapeutics · doi:10.1016/j.pharmthera.2018.03.004 · Cited by 463 · see citing works

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 438 · see citing works

The landscape of aging

Cai, Y., Song, W., Li, J., Jing, Y., Liang, C., Zhang, L., Zhang, X., Zhang, W., Liu, B., An, Y., et al. (2022) · Science China Life Sciences · doi:10.1007/s11427-022-2161-3 · Cited by 436 · see citing works

Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury

Rungratanawanich, W., Qu, Y., Wang, X., Essa, M. M., & Song, B.-J. (2021) · Experimental &amp; Molecular Medicine · doi:10.1038/s12276-021-00561-7 · Cited by 411 · see citing works

Inflammation, epigenetics, and metabolism converge to cell senescence and ageing: the regulation and intervention

Zhu, X., Chen, Z., Shen, W., Huang, G., Sedivy, J. M., Wang, H., & Ju, Z. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00646-9 · Cited by 410 · see citing works

DNA damage and repair in age-related inflammation

Zhao, Y., Simon, M. A., Seluanov, A., & Gorbunova, V. A. (2022) · Nature reviews. Immunology · doi:10.1038/s41577-022-00751-y · Cited by 393 · see citing works

De 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

Mitophagy in neurodegeneration and aging

Fivenson, E. M., Lautrup, S., Sun, N., Scheibye-Knudsen, M., Stevnsner, T., Nilsen, H., Bohr, V. A., & Fang, E. F. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.02.007 · Cited by 364 · see citing works

Mitochondria and Epigenetics – Crosstalk in Homeostasis and Stress

Matilainen, O., Quirós, P. M., & Auwerx, J. H. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.02.004 · Cited by 368 · see citing works

The Roles of Histone Deacetylases and Their Inhibitors in Cancer Therapy

Guo, L., Tian, Y., & Zhu, W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.576946 · Cited by 358 · see citing works

Sirtuins in Renal Health and Disease

Morigi, M., Perico, L., & Benigni, A. (2018) · Journal of the American Society of Nephrology · doi:10.1681/asn.2017111218 · Cited by 359 · see citing works

Amelioration of Alzheimer’s disease pathology by mitophagy inducers identified via machine learning and a cross-species workflow

Xie, C., Zhuang, X., Niu, Z., Ai, R., Lautrup, S., Zheng, S., Jiang, Y., Han, R., Gupta, T. S., Cao, S., et al. (2022) · Nature Biomedical Engineering · doi:10.1038/s41551-021-00819-5 · Cited by 347 · see citing works

SIRT2 Acts as a Cardioprotective Deacetylase in Pathological Cardiac Hypertrophy

Tang, X., Chen, X., Wang, N.-Y., Wang, X., Liang, S., Zheng, W., Lu, Y., Zhao, X., Hao, D., Zhang, Z., et al. (2017) · Circulation · doi:10.1161/circulationaha.117.028728 · Cited by 342 · see citing works

Mitochondrial Dysfunction, Oxidative Stress, Neuroinflammation, and Metabolic Alterations in the Progression of Alzheimer's Disease: A Meta-Analysis of In Vivo Magnetic Resonance Spectroscopy Studies

Song, T., Song, X., Zhu, C., Patrick, R., Skurla, M., Santangelo, I., Green, M., Harper, D., Ren, B., Forester, B. P., et al. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101503 · Cited by 346 · see citing works

Repairing mitochondrial dysfunction in disease

Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337 · see citing works

Nicotinamide Mononucleotide Supplementation Reverses the Declining Quality of Maternally Aged Oocytes

Miao, Y., Cui, Z., Gao, Q., Rui, R., & Xiong, B. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107987 · Cited by 312 · see citing works

Targeting mitochondria for cardiovascular disorders: therapeutic potential and obstacles

Bonora, M., Wieckowski, M. R., Sinclair, D. A., Kroemer, G., Pinton, P., & Galluzzi, L. (2018) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0074-0 · Cited by 299 · see citing works

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 288 · see citing works

Effects of hydrogen sulfide on mitochondrial function and cellular bioenergetics

Paul, B. D., Snyder, S. H., & Kashfi, K. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101772 · Cited by 283 · see citing works

Niacin in the Central Nervous System: An Update of Biological Aspects and Clinical Applications

Gasperi, V., Sibilano, M., Savini, I., & Catani, M. V. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20040974 · Cited by 282 · see citing works

Drosophila as a model for ageing

Piper, M. D. W., & Partridge, L. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.09.016 · Cited by 273 · see citing works

Lysine acetyltransferases and lysine deacetylases as targets for cardiovascular disease

Li, P., Ge, J., & Li, H. (2020) · Nature Reviews Cardiology · doi:10.1038/s41569-019-0235-9 · Cited by 269 · see citing works

SIRT6: Novel Mechanisms and Links to Aging and Disease

Tasselli, L., Zheng, W., & Chua, K. F. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2016.10.002 · Cited by 267 · see citing works

Plant Polyphenols, More than Just Simple Natural Antioxidants: Oxidative Stress, Aging and Age-Related Diseases

Hano, C., & Tungmunnithum, D. (2020) · Medicines · doi:10.3390/medicines7050026 · Cited by 259 · see citing works

The role of nutrition in inflammaging

Giosia, P. D., Stamerra, C. A., Giorgini, P., Jamialahamdi, T., Butler, A. E., & Sahebkar, A. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101596 · Cited by 250 · see citing works

Mitochondrial sirtuins, metabolism, and aging

Ji, Z., Liu, G., & Qu, J. T. (2021) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2021.11.005 · Cited by 246 · see citing works

Stilbene-based natural compounds as promising drug candidates against COVID-19

Wahedi, H. M., Ahmad, S., & Abbasi, S. W. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1762743 · Cited by 243 · see citing works

Key proteins and pathways that regulate lifespan

Pan, H., & Finkel, T. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r116.771915 · Cited by 218 · see citing works

Aging - Oxidative stress, antioxidants and computational modeling

Warraich, U.-E.-A., Hussain, F., & Kayani, H. U. R. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e04107 · Cited by 212 · see citing works

Increase in blood–brain barrier leakage in healthy, older adults

Verheggen, I. C. M., de Jong, J. J. A., van Boxtel, M. P. J., Gronenschild, E. H. B. M., Palm, W. M., Postma, A. A., Jansen, J. F. A., Verhey, F. R. J., & Backes, W. H. (2020) · GeroScience · doi:10.1007/s11357-020-00211-2 · Cited by 205 · see citing works

Gut stem cell aging is driven by mTORC1 via a p38 MAPK-p53 pathway

He, D. N., Wu, H., Xiang, J., Ruan, X., Peng, P., Ruan, Y., Chen, Y., Wang, Y., Yu, Q., Zhang, H., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-13911-x · Cited by 196 · see citing works

Sirtuin 3-dependent mitochondrial redox homeostasis protects against AGEs-induced intervertebral disc degeneration

Song, Y., Li, S., Geng, W., Luo, R., Liu, W., Tu, J., Wang, K., Kang, L., Yin, H., Wu, X., et al. (2018) · Redox Biology · doi:10.1016/j.redox.2018.09.006 · Cited by 192 · see citing works

A conserved NAD + binding pocket that regulates protein-protein interactions during aging

Li, J., Bonkowski, M. S., Moniot, S., Zhang, D., Hubbard, B. P., Ling, A. J. Y., Rajman, L. A., Qin, B., Lou, Z., Gorbunova, V. A., et al. (2017) · Science · doi:10.1126/science.aad8242 · Cited by 188 · see citing works

Metabolic landscape in cardiac aging: insights into molecular biology and therapeutic implications

Xie, S., Xu, S., Deng, W., & Tang, Q. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01378-8 · Cited by 185 · see citing works

Repeat dose NRPT (nicotinamide riboside and pterostilbene) increases NAD(+) levels in humans safely and sustainably: a randomized, double-blind, placebo-controlled study

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

The Good, the Bad, and the Ugly of ROS: New Insights on Aging and Aging‐Related Diseases from Eukaryotic and Prokaryotic Model Organisms

Santos, A. L., Sinha, S., & Lindner, A. B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1941285 · Cited by 168 · see citing works

Coronavirus (Covid-19) sepsis: revisiting mitochondrial dysfunction in pathogenesis, aging, inflammation, and mortality

Shenoy, S. (2020) · Inflammation Research · doi:10.1007/s00011-020-01389-z · Cited by 171 · see citing works

The multifaceted benefits of walking for healthy aging: from Blue Zones to molecular mechanisms

Ungvari, Z., Fazekas-Pongor, V., Csiszar, A., & Kunutsor, S. (2023) · GeroScience · doi:10.1007/s11357-023-00873-8 · Cited by 161 · see citing works

Systematic review and analysis of human proteomics aging studies unveils a novel proteomic aging clock and identifies key processes that change with age

Johnson, A. A., Shokhirev, M. N., Wyss-Coray, T., & Lehallier, B. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101070 · Cited by 166 · see citing works

The metabolomics of human aging: Advances, challenges, and opportunities

Panyard, D. J., Yu, B., & Snyder, M. P. (2022) · Science Advances · doi:10.1126/sciadv.add6155 · Cited by 155 · see citing works

Turning back time with emerging rejuvenation strategies

Mahmoudi, S., Xu, L., & Brunet, A. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0206-0 · Cited by 163 · see citing works

Nicotinamide riboside supplementation alters body composition and skeletal muscle acetylcarnitine concentrations in healthy obese humans

Remie, C. M., Roumans, K. H., Moonen, M. P., Connell, N. J., Havekes, B., Mevenkamp, J., Lindeboom, L., de Wit, V. H., van de Weijer, T., Aarts, S. A., et al. (2020) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/nqaa072 · Cited by 160 · see citing works

Impact of Yoga and Meditation on Cellular Aging in Apparently Healthy Individuals: A Prospective, Open‐Label Single‐Arm Exploratory Study

Tolahunase, M., Sagar, R., & Dada, R. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/7928981 · Cited by 164 · see citing works

NLRP3 inflammasome activation in inflammaging

Latz, E., & Duewell, P. (2018) · Seminars in Immunology · doi:10.1016/j.smim.2018.09.001 · Cited by 174 · see citing works

Mediterranean diet and inflammaging within the hormesis paradigm

Martucci, M., Ostan, R., Biondi, F., Bellavista, E., Fabbri, C., Bertarelli, C., Salvioli, S., Capri, M., Franceschi, C., & Santoro, A. (2017) · Nutrition Reviews · doi:10.1093/nutrit/nux013 · Cited by 160 · see citing works

New insight into dyslipidemia‐induced cellular senescence in atherosclerosis

Xiang, Q., Tian, F., Xu, J. R., Du, X., Zhang, S., & Liu, L. (2022) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12866 · Cited by 164 · see citing works

Sirtuins and intervertebral disc degeneration: Roles in inflammation, oxidative stress, and mitochondrial function

Zhang, G., Deng, Y.-J., Xie, Q.-Q., Ren, E., Ma, Z., He, X., Gao, Y., & Kang, X. (2020) · Clinica Chimica Acta · doi:10.1016/j.cca.2020.04.016 · Cited by 157 · see citing works

SIRT6 in Aging, Metabolism, Inflammation and Cardiovascular Diseases

Guo, Z., Li, P., Ge, J., & Li, H. (2022) · Aging and Disease · doi:10.14336/ad.2022.0413 · Cited by 160 · see citing works

The crosstalk between Sirt1 and Keap1/Nrf2/ARE anti-oxidative pathway forms a positive feedback loop to inhibit FN and TGF-β1 expressions in rat glomerular mesangial cells

Huang, K., Gao, X., & Wei, W. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.09.042 · Cited by 155 · see citing works

SIRT1 activation attenuates cardiac fibrosis by endothelial-to-mesenchymal transition

Liu, Z., Zhang, Y., Wang, X., Fan, X., Zhang, Y., Li, X., Gong, Y., & Han, L. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109227 · Cited by 154 · see citing works

Mitochondria initiate and regulate sarcopenia

Alway, S. E., Mohamed, J. S., & Myers, M. J. (2017) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000101 · Cited by 153 · see citing works

Aging and Caloric Restriction Research: A Biological Perspective with Translational Potential

Balasubramanian, P., Howell, P. R., & Anderson, R. M. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.06.015 · Cited by 148 · see citing works

Mechanisms and disease implications of sirtuin-mediated autophagic regulation

Lee, I. H. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0302-7 · Cited by 147 · see citing works

Immunosenescence: signaling pathways, diseases and therapeutic targets

Fu, Y., Wang, B., Alu, A., Hong, W., Hong, L., He, X., Shi, H., Cheng, P., & Yang, X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02371-z · Cited by 157 · see citing works

AMP-Activated Protein Kinase Regulation of the NLRP3 Inflammasome during Aging

Cordero, M. D., Williams, M. R., & Ryffel, B. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.10.009 · Cited by 147 · see citing works

Nicotinamide riboside does not alter mitochondrial respiration, content or morphology in skeletal muscle from obese and insulin‐resistant men

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

Possible Adverse Effects of High-Dose Nicotinamide: Mechanisms and Safety Assessment

Hwang, E., & Song, S. (2020) · Biomolecules · doi:10.3390/biom10050687 · Cited by 144 · see citing works

The landscape of transcription errors in eukaryotic cells

Goût, J.-F., Li, W., Fritsch, C., Li, A., Haroon, S., Singh, L. N., Ding, H., Fazelinia, H., Smith, Z., Seeholzer, S. H., et al. (2017) · Science Advances · doi:10.1126/sciadv.1701484 · Cited by 143 · see citing works

Sirtuins and Insulin Resistance

Zhou, S., Tang, X., & Chen, H. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00748 · Cited by 143 · see citing works

Discovery of cryptic allosteric sites using reversed allosteric communication by a combined computational and experimental strategy

Ni, D., Wei, J., He, X., Rehman, A. U., Li, X., Qiu, Y., Pu, J., Lu, S., & Zhang, J. (2020) · Chemical Science · doi:10.1039/d0sc05131d · Cited by 137 · see citing works

The flavonoid 4,4′-dimethoxychalcone promotes autophagy-dependent longevity across species

Carmona‐Gutiérrez, D., Zimmermann, A., Kainz, K., Pietrocola, F., Chen, G., Maglioni, S., Schiavi, A., Nah, J., Mertel, S., Beuschel, C. B., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-08555-w · Cited by 137 · see citing works

Melatonin attenuates acute kidney ischemia/reperfusion injury in diabetic rats by activation of the SIRT1/Nrf2/HO-1 signaling pathway

Shi, S., Lei, S., Tang, C., Wang, K., & Xia, Z. (2019) · Bioscience Reports · doi:10.1042/bsr20181614 · Cited by 135 · see citing works

Semisynthetic biosensors for mapping cellular concentrations of nicotinamide adenine dinucleotides

Sallin, O., Reymond, L., Gondrand, C., Raith, F., Koch, B., & Johnsson, K. (2018) · eLife · doi:10.7554/elife.32638 · Cited by 135 · see citing works

Nicotinamide mononucleotide (NMN) treatment attenuates oxidative stress and rescues angiogenic capacity in aged cerebromicrovascular endothelial cells: a potential mechanism for the prevention of vascular cognitive impairment

Kiss, T., Balasubramanian, P., Valcarcel‐Ares, M. N., Tarantini, S., Yabluchanskiy, A., Csípő, T., Lipécz, Á., Reglődi, D., Zhang, X. A., Bari, F., et al. (2019) · GeroScience · doi:10.1007/s11357-019-00074-2 · Cited by 134 · see citing works

Targeting Mitochondrial Impairment in Parkinson's Disease: Challenges and Opportunities

Prasuhn, J., Davis, R. L., & Kumar, K. R. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.615461 · Cited by 134 · see citing works

Sirtuins and FoxOs in osteoporosis and osteoarthritis

Almeida, M., & Porter, R. M. (2019) · Bone · doi:10.1016/j.bone.2019.01.018 · Cited by 129 · see citing works

Exosomal LncRNA–NEAT1 derived from MIF-treated mesenchymal stem cells protected against doxorubicin-induced cardiac senescence through sponging miR-221-3p

Zhuang, L., Xia, W., Chen, D., Ye, Y., Hu, T., Li, S., & Hou, M. (2020) · Journal of Nanobiotechnology · doi:10.1186/s12951-020-00716-0 · Cited by 123 · see citing works

Metformin Is a Direct SIRT1-Activating Compound: Computational Modeling and Experimental Validation

Cuyàs, E., Verdura, S., Llorach-Parés, L., Fernández-Arroyo, S., Joven, J., Martin-Castillo, B., Bosch-Barrera, J., Brunet, J., Nonell-Canals, A., Sanchez-Martinez, M., et al. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00657 · Cited by 122 · see citing works

Mitochondrial Regulation of Stem Cells in Bone Homeostasis

Zheng, C., Sui, B., Qiu, X., Hu, C., & Jin, Y. J. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.04.008 · Cited by 121 · see citing works

The road ahead for health and lifespan interventions

Gonzalez-Freire, M., Diaz-Ruiz, A., Hauser, D., Martinez-Romero, J., Ferrucci, L., Bernier, M., & de Cabo, R. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101037 · Cited by 118 · see citing works

From molecular promise to preclinical results: HDAC inhibitors in the race for healthy aging drugs

McIntyre, R. L., Daniels, E. G., Molenaars, M., Houtkooper, R. H., & Janssens, G. E. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201809854 · Cited by 115 · see citing works

Illuminating NAD+ Metabolism in Live Cells and In Vivo Using a Genetically Encoded Fluorescent Sensor

Zou, Y., Wang, A., Huang, L. Z., Zhu, X., Hu, Q., Zhang, Y., Chen, X., Li, F., Wang, Q., Wang, H., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.02.017 · Cited by 116 · see citing works

Interplay between TRAP1 and Sirtuin-3 Modulates Mitochondrial Respiration and Oxidative Stress to Maintain Stemness of Glioma Stem Cells

Park, H.-K., Hong, J.-H., Oh, Y. T., Kim, S. S., Yin, J., Lee, A., Chae, Y. C., Kim, J. H., Park, S., Park, C.-K., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-2558 · Cited by 116 · see citing works

Role of epigenetic regulation in myocardial ischemia/reperfusion injury

Wang, K., Li, Y., Qiang, T., Chen, J., & Wang, X. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105743 · Cited by 115 · see citing works

Evidence for Biological Age Acceleration and Telomere Shortening in COVID-19 Survivors

Mongelli, A., Barbi, V., Zamperla, M. G., Atlante, S., Forleo, L., Nesta, M., Massetti, M., Pontecorvi, A., Nanni, S., Farsetti, A., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116151 · Cited by 113 · see citing works

Sirtuins, resveratrol and the intertwining cellular pathways connecting them

Ungurianu, A., Zanfirescu, A., & Margina, D. M. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101936 · Cited by 113 · see citing works

Caloric Restriction Mimetics in Nutrition and Clinical Trials

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

The chemistry of the vitamin B3 metabolome

Makarov, M. V., Trammell, S. A. J., & Migaud, M. E. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180420 · Cited by 111 · see citing works

Mitophagy in health and disease. Molecular mechanisms, regulatory pathways, and therapeutic implications

D'Arcy, M. (2024) · APOPTOSIS · doi:10.1007/s10495-024-01977-y · Cited by 113 · see citing works

Acute nicotinamide riboside supplementation improves redox homeostasis and exercise performance in old individuals: a double-blind cross-over study

Dolopikou, C. F., Kourtzidis, I. A., Margaritelis, N. V., Vrabas, I. S., Koidou, E., Kyparos, A., Theodorou, A. A., Paschalis, V., & Nikolaidis, M. G. (2019) · European Journal of Nutrition · doi:10.1007/s00394-019-01919-4 · Cited by 104 · see citing works

Sirtuin Activators

Kane, A. E., & Sinclair, D. A. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.62135-9

Sirtuin Activation by Small Molecules

Massudi, H., Wu, L. E., & Sinclair, D. A. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_12 · Cited by 4 · see citing works

Small molecule SIRT1 activators for the treatment of aging and age-related diseases

Hubbard, B. P., & Sinclair, D. A. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.12.004 · Cited by 572 · see citing works

Antiaging Strategies Based on Sirtuin Activation

Garg, G., & Singh, S. (2023) · Springer eBooks · doi:10.1007/978-981-19-7443-4_14 · Cited by 1 · see citing works

The Role of Mammalian Sirtuins in the Regulation of Metabolism, Aging, and Longevity

Satoh, A., Stein, L. R., & Imai, S. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_7 · Cited by 171 · see citing works