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Sirtuins as regulators of metabolism and healthspan
Open accessAbstract
Since the beginning of the century, the mammalian sirtuin protein family (comprising SIRT1-SIRT7) has received much attention for its regulatory role, mainly in metabolism and ageing. Sirtuins act in different cellular compartments: they deacetylate histones and several transcriptional regulators in the nucleus, but also specific proteins in other cellular compartments, such as in the cytoplasm and in mitochondria. As a consequence, sirtuins regulate fat and glucose metabolism in response to physiological changes in energy levels, thereby acting as crucial regulators of the network that controls energy homeostasis and as such determines healthspan.
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“Regarding mammals, several studies have shown that several of the seven mammalian sirtuins can delay various parameters of aging in mice (Houtkooper et al., 2012; Sebastian et al., 2012).”
From The Hallmarks of Aging (2013) · cites this paper as Houtkooper et al., 2012
In the citing paper
“sirtuins can regulate gene expression by deacetylating histone and non-histone substrates, and this activity depends on a cofactor linked to the cellular energy status, NAD+ (nicotinamide adenine dinucleotide) (Houtkooper et al., 2012).”
From The Aging Epigenome (2016) · cites this paper as Houtkooper et al., 2012
In the citing paper
“The SIRT family of NAD+-dependent deacylases, comprising seven members that vary in tissue specificity, subcellular localization, enzymatic activity, and targets, mediates metabolic flexibility in animal models (42).”
From Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease (2018) · cites this paper as [42]
In the citing paper
“Nicotinamide mononucleotide conversion to NAD+ activates SIRT1 and improves glucose homeostasis in mice (42).”
From Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease (2018) · cites this paper as [42]
In the citing paper
“SIRT3, which is localized in the mitochondrial matrix, targets many proteins involved in metabolic homeostasis, including OXPHOS subunits (42).”
From Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease (2018) · cites this paper as [42]
In the citing paper
“SIRT1 controls the activity of transcription factors and cofactors such as p53, MEF2, FOXO, and PGC1α, which govern mitochondrial biogenesis and activity and lipid and glucose metabolism (42).”
From Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease (2018) · cites this paper as [42]
In the citing paper
“This is due to changes in the balances between acetylation and deacetylation rates, for instance involving the mitochondrial NAD+-dependent deacetylase SIRT3 (Houtkooper et al, 2012).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Houtkooper et al, 2012
In the citing paper
“Indeed, different situations of energy restriction, including fasting and exercise, increase NAD+ levels and trigger SIRT1/PGC-1α-dependent mitochondrial adaptation (Lin et al, 2000; Houtkooper et al, 2012).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Houtkooper et al, 2012
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1 retracted
RETRACTED: Metabolic regulation of SIRT1 transcription via a HIC1:CtBP corepressor complex
Zhang, Q., Wang, S.-Y., Fleuriel, C., Leprince, D., Rocheleau, J. V., Piston, D. W., & Goodman, R. H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610590104 · Cited by 171
RetractedSREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver
Horton, J. D., Goldstein, J. L., & Brown, M. S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15593 · Cited by 4,794
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
SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver
Horton, J. D., Goldstein, J. L., & Brown, M. S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215593 · Cited by 4,092
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
Self-citationmTOR: from growth signal integration to cancer, diabetes and ageing
Zoncu, R., Efeyan, A., & Sabatini, D. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3025 · Cited by 3,941
Kim, J.-W., Tchernyshyov, I., Semenza, G. L., & Dang, C. V. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.002 · Cited by 3,905
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
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
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
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Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648
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Buck, M. D., O’Sullivan, D., Geltink, R. I. K., Curtis, J. D., Chang, C., Sanin, D. E., Qiu, J., Kretz, O., Braas, D., van der Windt, G. J. W., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.035 · Cited by 1,491
Acetyl coenzyme A: a central metabolite and second messenger
Pietrocola, F., Galluzzi, L., Bravo-San Pedro, J. M., Madeo, F., & Kroemer, G. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.014 · Cited by 1,378
The growing landscape of lysine acetylation links metabolism and cell signalling
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Senescence and aging: Causes, consequences, and therapeutic avenues
McHugh, D., & Gil, J. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201708092 · Cited by 1,233
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
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
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Audia, J. E., & Campbell, R. M. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a019521 · Cited by 1,060
Kauppinen, A., Suuronen, T., Ojala, J. O., Kaarniranta, K., & Salminen, A. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.06.007 · Cited by 1,016
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Kawano, Y., & Cohen, D. E. (2013) · Journal of Gastroenterology · doi:10.1007/s00535-013-0758-5 · Cited by 1,009
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Shi, L., & Tu, B. P. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.02.003 · Cited by 903
“The dependency of sirtuins on NAD+ have led to the hypothesis that their activity could be regulated by fluctuations in NAD+ concentrations [63,64].”
BackgroundMetabolic control of autophagy
Galluzzi, L., Pietrocola, F., Levine, B., & Kroemer, G. (2014) · Cell · doi:10.1016/j.cell.2014.11.006 · Cited by 855
Slowing ageing by design: the rise of NAD+ and sirtuin-activating compounds
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Reprogramming of glucose, fatty acid and amino acid metabolism for cancer progression
Li, Z., & Zhang, H. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2070-4 · Cited by 840
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Singh, C. K., Chhabra, G., Ndiaye, M. A., Garcia‐Peterson, L. M., Mack, N. J., & Ahmad, N. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7290 · Cited by 820
Senescence and aging: the critical roles of p53
Rufini, A., Tucci, P., Celardo, I., & Melino, G. (2013) · Oncogene · doi:10.1038/onc.2012.640 · Cited by 798
Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease
Smith, R. L., Soeters, M. R., Wüst, R. C. I., & Houtkooper, R. H. (2018) · Endocrine Reviews · doi:10.1210/er.2017-00211 · Cited by 787
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Green, C. L., Lamming, D. W., & Fontana, L. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00411-4 · Cited by 714
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Galluzzi, L., Kepp, O., Heiden, M. G. V., & Kroemer, G. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4145 · Cited by 731
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Mottamal, M., Zheng, S., Huang, T. L., & Wang, G. (2015) · Molecules · doi:10.3390/molecules20033898 · Cited by 698
Metabolites as regulators of insulin sensitivity and metabolism
Yang, Q., Vijayakumar, A., & Kahn, B. B. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0044-8 · Cited by 698
The effects of aging in the hippocampus and cognitive decline
Bettio, L. E. B., Rajendran, L., & Gil‐Mohapel, J. (2017) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2017.04.030 · Cited by 700
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NAD+ homeostasis in health and disease
Katsyuba, E., Romani, M., Hofer, D., & Auwerx, J. (2020) · Nature Metabolism · doi:10.1038/s42255-019-0161-5 · Cited by 627
Self-citationMitochondria in health, disease, and aging
Harrington, J. S., Ryter, S. W., Plataki, M. E., Price, D. R., & Choi, A. M. K. (2023) · Physiological Reviews · doi:10.1152/physrev.00058.2021 · Cited by 641
Ryall, J. G., Dell’Orso, S., Derfoul, A., Juan, A., Zare, H., Feng, X., Clermont, D., Koulnis, M., Gutierrez-Cruz, G., Fulco, M., et al. (2015) · Cell Stem Cell · doi:10.1016/j.stem.2014.12.004 · Cited by 575
Simcox, J. A., & McClain, D. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.02.007 · Cited by 545
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Bloom, S. I., Islam, M. T., Lesniewski, L. A., & Donato, A. J. (2022) · Nature Reviews Cardiology · doi:10.1038/s41569-022-00739-0 · Cited by 521
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Hwang, J.-W., Yao, H., Caito, S., Sundar, I. K., & Rahman, I. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.03.015 · Cited by 503
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Booth, L. N., & Brunet, A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.013 · Cited by 499
Pearce, E. J., & Everts, B. (2014) · Nature reviews. Immunology · doi:10.1038/nri3771 · Cited by 500
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Grabowska, W., Sikora, E., & Bielak-Zmijewska, A. (2017) · Biogerontology · doi:10.1007/s10522-017-9685-9 · Cited by 470
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Dai, H., Sinclair, D. A., Ellis, J. L., & Steegborn, C. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.03.004 · Cited by 463
“SIRT1, 6, and 7 are primarily nuclear, SIRT3, 4, and 5 are mitochondrial, and SIRT2 is primarily cytosolic (Houtkooper et al., 2012).”
BackgroundCrosstalk between Oxidative Stress and SIRT1: Impact on the Aging Process
Salminen, A., Kaarniranta, K., & Kauppinen, A. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14023834 · Cited by 464
Jeong, S. M., Xiao, C., Finley, L. W. S., Lahusen, T., Souza, A. L., Pierce, K., Li, Y.-H., Wang, X., Laurent, G., German, N. J., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.02.024 · Cited by 445
Protective effects of sirtuins in cardiovascular diseases: from bench to bedside
Winnik, S., Auwerx, J., Sinclair, D. A., & Matter, C. M. (2015) · European Heart Journal · doi:10.1093/eurheartj/ehv290 · Cited by 422
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Liu, H., Wang, S., Wang, J., Guo, X., Song, Y., Fu, K., Gao, Z., Liu, D., He, W., & Yang, L. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02141-x · Cited by 484
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Katsyuba, E., Mottis, A., Ziętak, M., Franco, F., van der Velpen, V., Gariani, K., Ryu, D., Cialabrini, L., Matilainen, O., Liscio, P., et al. (2018) · Nature · doi:10.1038/s41586-018-0645-6 · Cited by 447
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Gaffney, D. O., Jennings, E. Q., Anderson, C. C., Marentette, J., Shi, T., Oxvig, A.-M. S., Streeter, M. D., Johannsen, M., Spiegel, D. A., Chapman, E., et al. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.11.005 · Cited by 430
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Koo, S. (2013) · Clinical and Molecular Hepatology · doi:10.3350/cmh.2013.19.3.210 · Cited by 421
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Gut, P., & Verdin, E. M. (2013) · Nature · doi:10.1038/nature12752 · Cited by 431
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Laurent, G., German, N. J., Saha, A. K., de Boer, V. C. J., Davies, M. N., Koves, T. R., Dephoure, N., Fischer, F. F., Boanca, G., Vaitheesvaran, B., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.05.012 · Cited by 399
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Che, R., Yuan, Y., Huang, S., & Zhang, A. (2013) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00571.2013 · Cited by 399
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Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383
Self-citationSeven sirtuins for seven deadly diseases ofaging
Morris, B. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.525 · Cited by 386
NRK1 controls nicotinamide mononucleotide and nicotinamide riboside metabolism in mammalian cells
Ratajczak, J., Joffraud, M., Trammell, S. A. J., Ras, R., Canela, N., Boutant, M., Kulkarni, S. S., Rodrigues, M., Redpath, P., Migaud, M. E., et al. (2016) · Nature Communications · doi:10.1038/ncomms13103 · Cited by 378
Self-citationTafani, M., Sansone, L., Limana, F., Arcangeli, T., Santis, E. D., Polese, M., Fini, M., & Russo, M. A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3907147 · Cited by 379
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Cerutti, R., Pirinen, E., Lamperti, C., Marchet, S., Sauve, A. A., Li, W., Leoni, V., Schon, E. A., Dantzer, F., Auwerx, J., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.001 · Cited by 343
Self-citationTraumatic Brain Injury: Oxidative Stress and Neuroprotection
Cornelius, C., Crupi, R., Calabrese, V., Graziano, A., Milone, P., Pennisi, G., Radak, Z. O., Calabrese, E. J., & Cuzzocrea, S. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4981 · Cited by 355
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Zhang, Y., Sowers, J. R., & Ren, J. (2018) · Nature Reviews Endocrinology · doi:10.1038/s41574-018-0009-1 · Cited by 338
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
Self-citationEndo, H., Niioka, M., Kobayashi, N., Tanaka, M., & Watanabe, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063388 · Cited by 339
Ren, B., Zhang, Y., Liu, S., Cheng, X., Yang, X. C., Cui, X., Zhao, X., Zhao, H., Hao, M., Li, M., et al. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15725 · Cited by 333
Protein acetylation in metabolism – metabolites and cofactors
Menzies, K. J., Zhang, H., Katsyuba, E., & Auwerx, J. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.181 · Cited by 331
Self-citationThe metabolic fate of acetate in cancer
Schug, Z. T., Vande Voorde, J., & Gottlieb, E. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.87 · Cited by 331
Little Fish, Big Data: Zebrafish as a Model for Cardiovascular and Metabolic Disease
Gut, P., Reischauer, S., Stainier, D. Y. R., & Arnaout, R. (2017) · Physiological Reviews · doi:10.1152/physrev.00038.2016 · Cited by 339
SIRT4 is a lysine deacylase that controls leucine metabolism and insulin secretion
Anderson, K. A., Huynh, F. K., Fisher-Wellman, K., Stuart, J. D., Peterson, B. S., Douros, J. D., Wagner, G. R., Thompson, J. W., Madsen, A. S., Green, M. F., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.03.003 · Cited by 326
“Conversely, ablation or inhibition of sirtuins accelerates the onset of several aging phenotypes (Houtkooper et al., 2012).”
BackgroundBao, X., Wang, Y., Li, X., Li, X.-M., Liu, Z., Yang, T., Wong, C. F., Zhang, J., Hao, Q., & Li, X. D. (2014) · eLife · doi:10.7554/elife.02999 · Cited by 324
Kim, J. K., Noh, J. H., Jung, K. H., Eun, J. W., Bae, H. J., Kim, M. G., Chang, Y. G., Shen, Q., Park, W. S., Lee, J. Y., et al. (2012) · Hepatology · doi:10.1002/hep.26101 · Cited by 323
Wang, C., Wu, S., Wu, Y., & Wei, Y. (2013) · Experimental Biology and Medicine · doi:10.1177/1535370213493069 · Cited by 321
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Hirschey, M. D., DeBerardinis, R. J., Diehl, A. M., Drew, J. E., Frezza, C., Green, M. F., Jones, L. W., Ko, Y. H., Le, A., Lea, M. A., et al. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.10.002 · Cited by 316
Eight Kinetically Stable but Thermodynamically Activated Molecules that Power Cell Metabolism
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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 308
Tatone, C., Emidio, G. D., Barbonetti, A., Carta, G., Luciano, A. M., Falone, S., & Amicarelli, F. (2018) · Human Reproduction Update · doi:10.1093/humupd/dmy003 · Cited by 296
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Masri, S., Rigor, P., Cervantes, M., Ceglia, N., Sebastian, C., Xiao, C., Roqueta-Rivera, M., Deng, C., Osborne, T. F., Mostoslavsky, R., et al. (2014) · Cell · doi:10.1016/j.cell.2014.06.050 · Cited by 292
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Phan, A. T., Goldrath, A. W., & Glass, C. K. (2017) · Immunity · doi:10.1016/j.immuni.2017.04.016 · Cited by 296
Ippolito, L., Morandi, A., Taddei, M. L., Parri, M., Comito, G., Iscaro, A., Raspollini, M. R., Magherini, F., Rapizzi, E., Masquelier, J., et al. (2019) · Oncogene · doi:10.1038/s41388-019-0805-7 · Cited by 290
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Shin, J., He, M., Liu, Y., Paredes, S., Villanova, L., Brown, K., Qiu, X., Nabavi, N., Mohrin, M., Wojnoonski, K., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.007 · Cited by 287
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Gano, L. B., Patel, M., & Rho, J. M. (2014) · Journal of Lipid Research · doi:10.1194/jlr.r048975 · Cited by 291
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Jing, H., & Lin, H. (2015) · Chemical Reviews · doi:10.1021/cr500457h · Cited by 276
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Yaku, K., Okabe, K., & Nakagawa, T. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.05.006 · Cited by 269
Huang, K., Huang, J., Xie, X., Wang, S., Chen, C., Shen, X., Liu, P., & Huang, H. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.029 · Cited by 269
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Eskandarian, H. A., Impens, F., Nahori, M., Soubigou, G., Coppée, J., Cossart, P., & Hamon, M. A. (2013) · Science · doi:10.1126/science.1238858 · Cited by 268
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He, W., Newman, J. C., Wang, M. Z., Ho, L., & Verdin, E. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.07.004 · Cited by 262
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Pillai, V. B., Sundaresan, N. R., & Gupta, M. P. (2014) · Circulation Research · doi:10.1161/circresaha.113.300536 · Cited by 262
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Ryu, D., Jo, Y. S., Sasso, G. L., Stein, S., Zhang, H., Perino, A., Lee, J. U., Zeviani, M., Romand, R., Hottiger, M. O., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.08.001 · Cited by 267
Self-citationPatel, V. B., Mori, J., McLean, B. A., Basu, R., Das, S. K., Ramprasath, T., Parajuli, N., Penninger, J. M., Grant, M. B., Lopaschuk, G. D., et al. (2015) · Diabetes · doi:10.2337/db15-0399 · Cited by 260
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Pirinen, E., Cantó, C., Jo, Y. S., Morato, L., Zhang, H., Menzies, K. J., Williams, E. G., Mouchiroud, L., Moullan, N., Hagberg, C., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.002 · Cited by 254
“The sirtuin enzymes have emerged as critical regulators of mitochondrial and oxidative metabolism (Houtkooper et al., 2012).”
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Pissios, P. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.02.004 · Cited by 259
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Gomes, P., Outeiro, T. F., & Cavadas, C. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.08.001 · Cited by 259
Autophagy in diabetic kidney disease: regulation, pathological role and therapeutic potential
Yang, D., Livingston, M. J., Liu, Z., Dong, G., Zhang, M., Chen, J.-K., & Dong, Z. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2639-1 · Cited by 252
Metadata
- Authors
- Houtkooper, R. H., Pirinen, E., & Auwerx, J.
- Affiliations
- École Polytechnique Fédérale de Lausanne (CH)
- University of Eastern Finland (FI)
- Corresponding author
- Auwerx, Johan
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2012-03-07
- Volume
- 13
- Issue
- 4
- Pages
- 225-238
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC4872805
- OpenAlex
- W2028178274
- Cited by
- 2,008
- References
- 160
- Citations by year
- 2026: 109 · 2025: 114 · 2024: 137 · 2023: 147 · 2022: 132 · 2021: 159 · 2020: 169 · 2019: 140 · 2018: 175 · 2017: 145 · 2016: 122 · 2015: 144 · 2014: 126 · 2013: 131 · 2012: 57
- FWCI
- 12.11
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Pure Amsterdam UMC (publishedVersion)
- PubMed Central (acceptedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (125487, 124713)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- sirtuins, histone deacetylation, energy homeostasis, glucose metabolism, lipid metabolism, healthspan, aging, transcriptional regulation
- MeSH terms
- Resveratrol, Insulin Secretion, Aging, Animals, Energy Metabolism, Multigene Family, Glucose, Histones, Homeostasis, Humans, Insulin, Longevity, NAD, Phylogeny, Protein Processing, Post-Translational, Stilbenes, Sirtuins, Lipid Metabolism
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