The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
Abstract
In diverse organisms, calorie restriction slows the pace of ageing and increases maximum lifespan. In the budding yeast Saccharomyces cerevisiae, calorie restriction extends lifespan by increasing the activity of Sir2 (ref. 1), a member of the conserved sirtuin family of NAD(+)-dependent protein deacetylases. Included in this family are SIR-2.1, a Caenorhabditis elegans enzyme that regulates lifespan, and SIRT1, a human deacetylase that promotes cell survival by negatively regulating the p53 tumour suppressor. Here we report the discovery of three classes of small molecules that activate sirtuins. We show that the potent activator resveratrol, a polyphenol found in red wine, lowers the Michaelis constant of SIRT1 for both the acetylated substrate and NAD(+), and increases cell survival by stimulating SIRT1-dependent deacetylation of p53. In yeast, resveratrol mimics calorie restriction by stimulating Sir2, increasing DNA stability and extending lifespan by 70%. We discuss possible evolutionary origins of this phenomenon and suggest new lines of research into the therapeutic use of sirtuin activators.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Resveratrol, a natural polyphenolic compound present in various dietary components such as mulberries, peanuts, grapes and red wine, was identified as the most potent activator of SIRT1 (Howitz et al., 2003).”
From Calorie Restriction-like Effects of 30 Days of Resveratrol Supplementation on Energy Metabolism and Metabolic Profile in Obese Humans (2011) · cites this paper as Howitz et al., 2003
In the citing paper
“Experiments in animal models have shown that resveratrol significantly reduces body weight [14].”
From The Role of Resveratrol Administration in Human Obesity (2021) · cites this paper as [14]
In the citing paper
“SIRT-1 is a human deacetylase that negatively regulates the p53 tumor suppressor gene, thus it promotes cell survival [14].”
From The Role of Resveratrol Administration in Human Obesity (2021) · cites this paper as [14]
In the citing paper
“an intervention capable of extending life span in many different organisms from yeast to mammals (Cohen et al., 2004; Howitz et al., 2003; Lin et al., 2000; Rogina and Helfand, 2004; Wood et al., 2004”
From DNA Repair, Genome Stability, and Aging (2005) · cites this paper as Howitz et al., 2003
In the citing paper
“resveratrol, a plant polyphenol commonly found in red wine that extends lifespan in yeast, worms and flies [143, 144].”
From PGC-1α in aging and anti-aging interventions (2009) · cites this paper as [143]
In the citing paper
“Indeed, this polyphenol has been reported to activate the AMPK and SIRT1 (Howitz et al., 2003; Hawley et al., 2010)”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Howitz et al., 2003
In the citing paper
“Resveratrol prolongs the life of flies (Bauer et al., 2004), worms (Baur and Sinclair, 2006), and the replicative lifespan of yeast (Howitz et al., 2003), but not yeast’s chronological lifespan (our unpublished observations).”
From The Search for Antiaging Interventions: From Elixirs to Fasting Regimens (2014) · cites this paper as Howitz et al., 2003
In the citing paper
“Resveratrol, an ingredient in red wines, is a polyphenolic SIRT1 activator that, like calorie restriction, has anti-aging effects in lower organisms (22, 143, 331), reduces signs of aging in mice (248), and extends survival (22).”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [143]
Citations
Cites
ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.
Monod, J., Wyman, J., & Changeux, J. (1965) · Journal of Molecular Biology · doi:10.1016/s0022-2836(65)80285-6 · Cited by 7,681
Cancer chemopreventive activity of resveratrol, a natural product derived from grapes
Jang, M., Cai, L., Udeani, G. O., Slowing, K. V., Thomas, C. F., Beecher, C. W. W., Fong, H. H. S., Farnsworth, N. R., Kinghorn, A. D., Mehta, R. G., et al. (1997) · Science · doi:10.1126/science.275.5297.218 · Cited by 4,935 · cited 1×
“The most potent activator was resveratrol (3,5,4′-trihydroxystilbene), a polyphenol found in red wine that is associated with a surprising number of health benefits, most notably the mitigation of age-related diseases, including neurodegeneration, carcinogenesis and atherosclerosi”
BackgroundMiddleton, E., Kandaswami, C., & Theoharides, T. C. (2000) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01472-8 · Cited by 4,882
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
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
Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253 · cited 1×
“Together, these findings add to the body of evidence that yeast ageing is caused by genomic instabilit”
BackgroundNegative 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
Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775
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 1,603
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
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Items 801–900 of 1,038
He, X., Wang, Y., Zhu, J., Orloff, M. S., & Eng, C. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.11.012 · Cited by 114
Sirt1 Mediates Hyperbaric Oxygen Preconditioning-Induced Ischemic Tolerance in Rat Brain
Yan, W., Fang, Z., Yang, Q., Dong, H., Lü, Y., Lei, C., & Xiong, L. (2013) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2012.179 · Cited by 116
Resveratrol inhibits insulin responses in a SirT1-independent pathway
Zhang, J. (2006) · Biochemical Journal · doi:10.1042/bj20050977 · Cited by 115
Joven, J., Micol, V., Segura‐Carretero, A., Alonso‐Villaverde, C., Menéndez, J. A., & for the Bioactive Food Components, P. (2013) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2011.621772 · Cited by 115
Plant-derived epigenetic modulators for cancer treatment and prevention
Schnekenburger, M., Dicato, M. A., & Diederich, M. F. (2014) · Biotechnology Advances · doi:10.1016/j.biotechadv.2014.03.009 · Cited by 117
Nutrition and Healthy Ageing: Calorie Restriction or Polyphenol-Rich “MediterrAsian” Diet?
Pallauf, K., Giller, K., Huebbe, P., & Rimbach, G. H. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/707421 · Cited by 116
Renoprotective approaches and strategies in acute kidney injury
Yuan, Y., Song, M., Liu, Y., Liu, H., Sun, L., Peng, Y., Liu, F., Venkatachalam, M. A., & Dong, Z. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.03.015 · Cited by 115
Current Perspective in the Discovery of Anti-aging Agents from Natural Products
Ding, A., Zheng, S., Huang, X., Xing, T.-K., Wu, G.-S., Sun, H., Qi, S., & Luo, H. (2017) · Natural Products and Bioprospecting · doi:10.1007/s13659-017-0135-9 · Cited by 115
Maugeri, A., Barchitta, M., Mazzone, M. G., Giuliano, F., Basile, G., & Agodi, A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19072118 · Cited by 119
Key Signaling Pathways in Aging and Potential Interventions for Healthy Aging
Yu, M., Zhang, H., Wang, B. Z., Zhang, Y., Zheng, X., Shao, B., Zhuge, Q., & Jin, K. (2021) · Cells · doi:10.3390/cells10030660 · Cited by 117
The trifecta of aging in Caenorhabditis elegans
Wolff, S., & Dillin, A. G. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.06.054 · Cited by 115
Risitano, R., Currò, M., Cirmi, S., Ferlazzo, N., Campiglia, P., Caccamo, D., Ientile, R., & Navarra, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107431 · Cited by 113
Peptide Switch Is Essential for Sirt1 Deacetylase Activity
Kang, H., Suh, J., Jung, Y., Jung, J., Kim, M. K., & Chung, J. H. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.038 · Cited by 117
Adiponectin: A Key Adipokine in Alcoholic Fatty Liver
You, M., & Rogers, C. Q. (2009) · Experimental Biology and Medicine · doi:10.3181/0902-mr-61 · Cited by 113
Finding a Target for Resveratrol
Tennen, R. I., Michishita-Kioi, E., & Chua, K. F. (2012) · Cell · doi:10.1016/j.cell.2012.01.032 · Cited by 113
A comparative study of anti-aging properties and mechanism: resveratrol and caloric restriction
Li, J., Zhang, C.-X., Liu, Y., Chen, K., & Chen, G. (2017) · Oncotarget · doi:10.18632/oncotarget.20084 · Cited by 117
Sebori, R., Kuno, A., Hosoda, R., Hayashi, T., & Horio, Y. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9179270 · Cited by 114
Iakovou, E., & Kourti, M. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.827900 · Cited by 119
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 114
Dong, W., Li, N., Gao, D., Zhen, H., Zhang, X., & Li, F. (2008) · Journal of Vascular Surgery · doi:10.1016/j.jvs.2008.04.007 · Cited by 113
Synthesis of methylated resveratrol and analogues by Heck reactions in organic and aqueous solvents
Botella, L., & Nájera, C. (2004) · Tetrahedron · doi:10.1016/j.tet.2004.04.076 · Cited by 113
Tang, B. L., & Chua, C. E. L. (2007) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2007.02.001 · Cited by 114
Nampt/PBEF/Visfatin: A regulator of mammalian health and longevity?
Yang, H., Lavu, S., & Sinclair, D. A. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.06.003 · Cited by 113
Self-citationLan, F., Weikel, K., Cacicedo, J., & Ido, Y. (2017) · Nutrients · doi:10.3390/nu9070751 · Cited by 112
Regulation of the Telomerase Reverse Transcriptase Subunit through Epigenetic Mechanisms
Lewis, K. A., & Tollefsbol, T. O. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00083 · Cited by 112
Resveratrol serves as a protein-substrate interaction stabilizer in human SIRT1 activation
Hou, X., Rooklin, D. W., Fang, H., & Zhang, Y. (2016) · Scientific Reports · doi:10.1038/srep38186 · Cited by 117
Wang, X., Gao, Y., Tian, N., Wang, T., Shi, Y., Xu, J., & Wu, B. (2019) · Scientific Reports · doi:10.1038/s41598-018-36911-1 · Cited by 112
Doré, S. (2005) · Neurosignals · doi:10.1159/000085386 · Cited by 113
Grape and wine biotechnology: Challenges, opportunities and potential benefits
Pretorius, I. S., & Høj, P. B. (2005) · Australian Journal of Grape and Wine Research · doi:10.1111/j.1755-0238.2005.tb00281.x · Cited by 112
Dietary Interventions to Extend Life Span and Health Span Based on Calorie Restriction
Minor, R. K., Allard, J. S., Younts, C. M., Ward, T. M., & de Cabo, R. (2010) · The Journals of Gerontology Series A · doi:10.1093/gerona/glq042 · Cited by 113
Lee, H. R., Shin, H. K., Park, S. Y., Kim, H. Y., Lee, W. S., Rhim, B. Y., Hong, K. W., & Kim, C. D. (2014) · Journal of Neuroscience Research · doi:10.1002/jnr.23421 · Cited by 114
Challenges of Translating Basic Research Into Therapeutics: Resveratrol as an Example
Smoliga, J. M., Vang, O., & Baur, J. A. (2011) · The Journals of Gerontology Series A · doi:10.1093/gerona/glr062 · Cited by 113
Molecular insights into the premature aging disease progeria
Vidak, S., & Foisner, R. (2016) · Histochemistry and Cell Biology · doi:10.1007/s00418-016-1411-1 · Cited by 115
Changes in kynurenine pathway metabolism in the brain, liver and kidney of aged female Wistar rats
Braidy, N., Guillemin, G. J., Mansour, H., Chan‐Ling, T., & Grant, R. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08366.x · Cited by 111
Chow, S., Hshu, Y.-C., Wang, J., & Chen, J. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00881.2006 · Cited by 111
Aging and induced senescence as factors in the pathogenesis of lung emphysema
Karrasch, S., Holz, O., & Jörres, R. A. (2008) · Respiratory Medicine · doi:10.1016/j.rmed.2008.04.013 · Cited by 114
Flavonoids: Antioxidant Compounds for Plant Defence... and for a Healthy Human Diet
Vicente, Ó., & Boşcaiu, M. (2017) · Notulae Botanicae Horti Agrobotanici Cluj-Napoca · doi:10.15835/nbha46110992 · Cited by 112
Hadley, E. C., Lakatta, E. G., Morrison‐Bogorad, M., Warner, H. R., & Hodes, R. J. (2005) · Cell · doi:10.1016/j.cell.2005.01.030 · Cited by 111
Metabolic effects of resveratrol: Addressing the controversies
Bitterman, J. L., & Chung, J. H. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1808-8 · Cited by 109
Cunha-Santos, J., Duarte-Neves, J., Carmona, V., Guarente, L., Pereira de Almeida, L., & Cavadas, C. (2016) · Nature Communications · doi:10.1038/ncomms11445 · Cited by 109
Exploring the therapeutic space around NAD+
Houtkooper, R. H., & Auwerx, J. H. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201207019 · Cited by 113
Pflanzliche Polyphenole: chemische Eigenschaften, biologische Aktivität und Synthese
Quideau, S., Deffieux, D., Douat, C., & Pouységu, L. (2011) · Angewandte Chemie · doi:10.1002/ange.201000044 · Cited by 109
Kou, X., Liu, X., Chen, X., Li, J., Yang, X., Fan, J., Yang, Y., & Chen, N. (2016) · Oncotarget · doi:10.18632/oncotarget.12811 · Cited by 109
The role of SIRT1 in ocular aging
Mimura, T., Kaji, Y., Noma, H., Funatsu, H., & Okamoto, S. (2013) · Experimental Eye Research · doi:10.1016/j.exer.2013.07.017 · Cited by 114
Sirtuin-1 regulation of mammalian metabolism
Gillum, M. P., Erion, D. M., & Shulman, G. I. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.09.005 · Cited by 110
Oxidative Stress in Mesenchymal Stem Cell Senescence: Regulation by Coding and Noncoding RNAs
Vono, R., Jover, E., Spinetti, G., & Madeddu, P. R. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7294 · Cited by 112
Su, J.-L., Yang, C., Zhao, M., Kuo, M., & Yen, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702452200 · Cited by 110
Roles of SIRT1 in the acute and restorative phases following induction of inflammation
Zhang, Z., Lowry, S. F., Guarente, L., & Haimovich, B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.174482 · Cited by 92
Age-related hearing loss: Is it a preventable condition?
Bielefeld, E. C., Tanaka, C., Chen, G., & Henderson, D. (2009) · Hearing Research · doi:10.1016/j.heares.2009.09.001 · Cited by 110
Sir2 and calorie restriction in yeast: A skeptical perspective
Kaeberlein, M. R., & Powers, R. W. (2007) · Ageing Research Reviews · doi:10.1016/j.arr.2007.04.001 · Cited by 109
Significance of Resveratrol in Clinical Management of Chronic Diseases
Wahab, A., Gao, K., Jia, C., Zhang, F., Tian, G., Murtaza, G., & Chen, J. (2017) · Molecules · doi:10.3390/molecules22081329 · Cited by 113
Design and synthesis of compounds that extend yeast replicative lifespan
Yang, H., Baur, J. A., Chen, A. Y., Miller, C. M., & Sinclair, D. A. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00259.x · Cited by 108
Self-citationLi, Y., Wang, P., Yang, X., Wang, W., Zhang, J., He, Y., Zhang, W. K., Jing, T., Wang, B., & Lin, R. (2016) · Molecular Immunology · doi:10.1016/j.molimm.2016.07.018 · Cited by 107
Geroprotectors: A Unified Concept and Screening Approaches
Moskalev, A., Chernyagina, E., Kudryavtseva, A. V., & Shaposhnikov, M. V. (2017) · Aging and Disease · doi:10.14336/ad.2016.1022 · Cited by 110
Epigenetic Regulation of NRF2/KEAP1 by Phytochemicals
Bhattacharjee, S., & Dashwood, R. H. (2020) · Antioxidants · doi:10.3390/antiox9090865 · Cited by 107
Antiaging agents: safe interventions to slow aging and healthy life span extension
Liu, J. (2022) · Natural Products and Bioprospecting · doi:10.1007/s13659-022-00339-y · Cited by 112
Sin, T. K., Tam, B. T., Yung, B. Y., Yip, S. P., Chan, L., Wong, S. C. C., Ying, M. T. C., Rudd, J. A., & Siu, P. M. (2015) · The Journal of Physiology · doi:10.1113/jphysiol.2014.270101 · Cited by 107
Role and possible mechanisms of Sirt1 in depression
Lu, G., Li, J., Zhang, H., Zhao, X., Yan, L.-J., & Yang, X. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/8596903 · Cited by 106
AMP-Activated Protein Kinase and Metabolic Control
Viollet, B., & Andréelli, F. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-17214-4_13 · Cited by 113
Lucas, J., Hsieh, T., Halicka, H. D., Darżynkiewicz, Z., & WU, J. M. (2018) · International Journal of Oncology · doi:10.3892/ijo.2018.4512 · Cited by 106
Emerging senolytic agents derived from natural products
Li, W., Qin, L., Feng, R., Hu, G., Sun, H., He, Y., & Zhang, R. (2019) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2019.05.001 · Cited by 106
Mechanisms of aging and potential role of selected polyphenols in extending healthspan
Russo, G. L., Spagnuolo, C., Russo, M., Tedesco, I., Moccia, S., & Cervellera, C. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.113719 · Cited by 108
Zhang, K., Huang, J., Wang, D., Wan, X., & Wang, Y. (2024) · Frontiers in Nutrition · doi:10.3389/fnut.2024.1371401 · Cited by 106
mTOR, AMPK, and Sirt1: Key Players in Metabolic Stress Management
Cetrullo, S., D’Adamo, S., Tantini, B., Borzı̀, R. M., & Flamigni, F. (2015) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukaryotgeneexpr.2015012975 · Cited by 109
Fancd2 −/− mice have hematopoietic defects that can be partially corrected by resveratrol
Zhang, Q., Loza, L. I. M., Eaton, L., Duncan, A. W., Goldman, D. C., Anur, P., Watanabe‐Smith, K., Rathbun, R. K., Fleming, W., Bagby, G. C., et al. (2010) · Blood · doi:10.1182/blood-2010-04-278226 · Cited by 109
Autophagy in ageing and ageing-associated diseases
He, L., Lu, J., & Yue, Z. (2013) · Acta Pharmacologica Sinica · doi:10.1038/aps.2012.188 · Cited by 107
Molecular biology of pyridine nucleotide and nicotine biosynthesis
Katoh, A. (2004) · Frontiers in bioscience · doi:10.2741/1350 · Cited by 106
Barrajón‐Catalán, E., Herranz‐López, M., Joven, J., Segura‐Carretero, A., Alonso‐Villaverde, C., Menéndez, J. A., & Micol, V. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-07320-0_11 · Cited by 106
Pharmacological modulation of circadian rhythms by synthetic activators of the deacetylase SIRT1
Bellet, M. M., Nakahata, Y., Boudjelal, M., Watts, E. F., Mossakowska, D. E., Edwards, K. A., Cervantes, M., Astarita, G., Loh, C., Ellis, J. L., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1214266110 · Cited by 110
Biological/Chemopreventive Activity of Stilbenes and their Effect on Colon Cancer
Rimando, A. M., & Suh, N. (2008) · Planta Medica · doi:10.1055/s-0028-1088301 · Cited by 108
Soy Isoflavones—Phytoestrogens and What Else?
Barnes, S. (2004) · Journal of Nutrition · doi:10.1093/jn/134.5.1225s · Cited by 106
Deacetylation of Nonhistone Proteins by HDACs and the Implications in Cancer
Peng, L., & Seto, E. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_3 · Cited by 107
Epigenomics of leukemia: from mechanisms to therapeutic applications
Florean, C., Schnekenburger, M., Grandjenette, C., Dicato, M. A., & Diederich, M. F. (2011) · Epigenomics · doi:10.2217/epi.11.73 · Cited by 107
Human Sirtuin Regulators: The “Success” Stories
Curry, A. M., White, D. S., Donu, D., & Cen, Y. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.752117 · Cited by 107
Acetaminophen-induced liver injury: Molecular mechanism and treatments from natural products
Liao, J., Lu, Q., Li, Z., Li, J., Zhao, Q., & Li, J. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1122632 · Cited by 111
Sirt1 protects the heart from aging and stress
Hsu, C., Odewale, I., Alcendor, R. R., & Sadoshima, J. (2008) · Biological Chemistry · doi:10.1515/bc.2008.032 · Cited by 108
Sirtuin-1 (SIRT1) Is Required for Promoting Chondrogenic Differentiation of Mesenchymal Stem Cells
Buhrmann, C., Busch, F., Shayan, P., & Shakibaei, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.568790 · Cited by 107
Beneficial Effects of Resveratrol on Atherosclerosis
Fan, E., Zhang, L., Jiang, S., & Bai, Y. (2008) · Journal of Medicinal Food · doi:10.1089/jmf.2007.0091 · Cited by 104
Self-citationZhu, W., Chen, S., Li, Z., Zhao, X., Li, W., Sun, Y., Zhang, Z., Ling, W., & Feng, X. (2014) · Nutrition & Metabolism · doi:10.1186/1743-7075-11-35 · Cited by 104
Molecular signaling mechanisms behind polyphenol-induced bone anabolism
Torre, E. (2017) · Phytochemistry Reviews · doi:10.1007/s11101-017-9529-x · Cited by 105
Liu, X., Chen, A., Liang, Q., Yang, X., Dong, Q., Fu, M., Wang, S., Li, Y., Ye, Y., Lan, Z., et al. (2021) · Aging Cell · doi:10.1111/acel.13377 · Cited by 104
Compounds that confer thermal stress resistance and extended lifespan
Benedetti, M. G., Foster, A. L., Vantipalli, M. C., White, M. P., Sampayo, J. N., Gill, M. S., Olsen, A., & Lithgow, G. J. (2008) · Experimental Gerontology · doi:10.1016/j.exger.2008.08.049 · Cited by 108
Glycolytic inhibition as a strategy for developing calorie restriction mimetics
Ingram, D. K., & Roth, G. S. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.12.001 · Cited by 104
Delipidating effect of resveratrol metabolites in 3 T 3‐L 1 adipocytes
Lasa, A., Churruca, I., Eseberri, I., Andrés‐Lacueva, C., & Portillo, M. P. (2012) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201100772 · Cited by 103
Diversity of Polyphenol Action in Caenorhabditis elegans: Between Toxicity and Longevity
Saul, N., Pietsch, K., Stürzenbaum, S. R., Menzel, R., & Steinberg, C. E. W. (2011) · Journal of Natural Products · doi:10.1021/np200011a · Cited by 103
Kang, W., Hong, H. J., Guan, J., Kim, D. G., Yang, E.-J., Koh, G., Park, D.-B., Han, C. H., Lee, Y. J., & Lee, D.-H. (2011) · Metabolism · doi:10.1016/j.metabol.2011.08.003 · Cited by 104
Immunometabolic rewiring of tubular epithelial cells in kidney disease
van der Rijt, S., Leemans, J. C., Florquin, S., Houtkooper, R. H., & Tammaro, A. (2022) · Nature Reviews Nephrology · doi:10.1038/s41581-022-00592-x · Cited by 105
Induction of stilbenes in grapes by UV-C: Comparison of different subspecies of Vitis
Guerrero, R. F., Puertas, B., Fernández‐Marín, M. I., Palma, M., & Cantos‐Villar, E. (2009) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2009.10.005 · Cited by 103
Nijhout, H. F. (2003) · Development · doi:10.1242/dev.00902 · Cited by 103
Speakman, J. R., & Król, E. (2010) · Integrative and Comparative Biology · doi:10.1093/icb/icq049 · Cited by 106
Liao, Z.-Y., Chen, J.-L., Xiao, M.-H., Sun, Y., Zhao, Y.-X., Pu, D., Lv, A.-K., Wang, M.-L., Zhou, J., Zhu, S.-Y., et al. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.08.032 · Cited by 102
Pollack, R. M., Barzilai, N., Anghel, V., Kulkarni, A. S., Golden, A., Broin, P. Ó., Sinclair, D. A., Bonkowski, M. S., Coleville, A. J., Powell, D. S., et al. (2017) · The Journals of Gerontology Series A · doi:10.1093/gerona/glx041 · Cited by 103
Self-citationPhytochemicals as Prebiotics and Biological Stress Inducers
Martel, J., Ojcius, D. M., Ko, Y., & Young, J. D. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.02.008 · Cited by 103
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
From Resveratrol to Its Derivatives: New Sources of Natural Antioxidant
He, S., & Yan, X. (2013) · Current Medicinal Chemistry · doi:10.2174/092986713805288941 · Cited by 103
Lanzillotta, A., Pignataro, G., Branca, C., Cuomo, O., Sarnico, I., Benarese, M., Annunziato, L., Spano, P., & Pizzi, M. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.08.018 · Cited by 102
Yang, C., Chen, Y., Chi, P., Lin, C., & Hsiao, L. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.03.003 · Cited by 103
Chemical and structural biology of protein lysine deacetylases
Yoshida, M., Kudo, N., Kosono, S., & Ito, A. (2017) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.93.019 · Cited by 109
Zhao, P., & Saltiel, A. R. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.011356 · Cited by 106
Resveratrol-Based Nanoformulations as an Emerging Therapeutic Strategy for Cancer
Sharifi‐Rad, J., Quispe, C., Mukazhanova, Z., Knut, E., Turgumbayeva, A., Kipchakbayeva, A., Seitimova, G. A., Mahomoodally, M. F., Lobine, D., Koay, A. C. C., et al. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.649395 · Cited by 102
Metadata
- Authors
- 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., Scherer, B., & Sinclair, D. A.
- Affiliations
- Harvard University (US)
- Corresponding author
- Sinclair, David A.
- Venue
- Nature
- Published
- 2003-08-24
- Volume
- 425
- Issue
- 6954
- Pages
- 191-196
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2088381487
- Cited by
- 3,796
- References
- 30
- Citations by year
- 2026: 77 · 2025: 73 · 2024: 117 · 2023: 99 · 2022: 133 · 2021: 159 · 2020: 159 · 2019: 158 · 2018: 181 · 2017: 189 · 2016: 198 · 2015: 215 · 2014: 227 · 2013: 267 · 2012: 253
- FWCI
- 51.56
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institute on Aging (R37AG028730, P01AG027916, R01AG028730, R01AG019719, R01AG019972, R13AG033466)
- National Institute of General Medical Sciences (R01GM068072)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- sirtuins, Sir2, SIRT1, resveratrol, caloric restriction, lifespan extension, aging, Sir2p, p53 deacetylation, NAD+-dependent deacetylase, DNA stability, Saccharomyces cerevisiae, small molecule activators
- MeSH terms
- Resveratrol, Acetylation, Catalysis, Cell Line, Cell Survival, Flavonoids, Histone Deacetylases, Humans, Kinetics, Longevity, Phenols, Polymers, Recombination, Genetic, Saccharomyces cerevisiae, Stilbenes, Wine, Tumor Suppressor Protein p53, Cellular Senescence, Caloric Restriction, Sirtuins, Silent Information Regulator Proteins, Saccharomyces cerevisiae, Sirtuin 1, Sirtuin 2, Polyphenols
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
