Sirtuins at the Service of Healthy Longevity

On the origin of cancer cells

Warburg, O. (1956) · Science · doi:10.1126/science.123.3191.309 · Cited by 13,425 · see citing works

How mitochondria produce reactive oxygen species

Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works

Ischemia and reperfusion—from mechanism to translation

Eltzschig, H. K., & Eckle, T. D. L. G. (2011) · Nature Medicine · doi:10.1038/nm.2507 · Cited by 3,389 · see citing works

Apoptosis, oncosis, and necrosis. An overview of cell death.

Majno, G., & Joris, I. (1995) · PubMed · Cited by 3,328 · see citing works

Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase

Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239 · 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

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

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

Sirtuins in mammals: insights into their biological function

Michán, S., & Sinclair, D. A. (2007) · Biochemical Journal · doi:10.1042/bj20070140 · Cited by 1,750 · 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

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

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

A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis

Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., Deng, C.-X., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803790105 · Cited by 1,291 · see citing works

Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation

Lombard, D. B., Alt, F. W., Cheng, H.-L., Bunkenborg, J., Streeper, R. S., Mostoslavsky, R., Kim, J., Yancopoulos, G., Valenzuela, D., Murphy, A., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01636-07 · Cited by 1,216 · see citing works

Sirt1 Regulates Aging and Resistance to Oxidative Stress in the Heart

Alcendor, R. R., Gao, S., Zhai, P., Zablocki, D., Holle, E., Yu, X., Tian, B., Wagner, T., Vatner, S. F., & Sadoshima, J. (2007) · Circulation Research · doi:10.1161/01.res.0000267723.65696.4a · Cited by 1,147 · see citing works

SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin

Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L. A., Barrett, J. C., et al. (2008) · Nature · doi:10.1038/nature06736 · Cited by 1,111 · see citing works

Role of Mitochondrial Dysfunction in Insulin Resistance

Kim, J.-A., Wei, Y., & Sowers, J. R. (2008) · Circulation Research · doi:10.1161/circresaha.107.165472 · Cited by 1,103 · see citing works

SIRT6 Links Histone H3 Lysine 9 Deacetylation to NF-κB-Dependent Gene Expression and Organismal Life Span

Kawahara, T. L. A., Michishita, E., Adler, A. S., Damian, M., Berber, E., Lin, M., McCord, R. A., Ongaigui, K. C. L., Boxer, L. D., Chang, H. Y., et al. (2009) · Cell · doi:10.1016/j.cell.2008.10.052 · Cited by 1,090 · see citing works

NAD(H) and NADP(H) Redox Couples and Cellular Energy Metabolism

Xiao, W., Wang, R., Handy, D. E., & Loscalzo, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7216 · Cited by 1,062 · see citing works

Calorie restriction, SIRT1 and metabolism: understanding longevity

Bordone, L., & Guarente, L. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1616 · Cited by 1,021 · see citing works

Antagonistic crosstalk between NF-κB and SIRT1 in the regulation of inflammation and metabolic disorders

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 · see citing works

Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice

Sundaresan, N. R., Gupta, M., Gene, K., Rajamohan, S. B., Isbatan, A., & Gupta, M. P. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39162 · Cited by 996 · see citing works

Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949 · see citing works

Hypothalamic programming of systemic ageing involving IKK-β, NF-κB and GnRH

Zhang, G., Li, J., Purkayastha, S., Tang, Y., Zhang, H., Yin, Y., Li, B., Liu, G., & Cai, D. (2013) · Nature · doi:10.1038/nature12143 · Cited by 834 · see citing works

Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF‐κB

Chen, L., Mu, Y., & Greene, W. C. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf660 · Cited by 827 · see citing works

SIRT1 Improves Insulin Sensitivity under Insulin-Resistant Conditions by Repressing PTP1B

Sun, C., Zhang, F., Ge, X., Yan, T., Chen, X., Shi, X., & Zhai, Q. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.08.014 · Cited by 766 · 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 747 · see citing works

Sir2 links chromatin silencing, metabolism, and agingPreprint

Guarente, L. (2000) · Genes & Development · doi:10.1101/gad.14.9.1021 · Cited by 718 · see citing works

Sirt1 Regulates Insulin Secretion by Repressing UCP2 in Pancreatic β Cells

Bordone, L., Motta, M. C., Picard, F., Robinson, A., Jhala, U. S., Apfeld, J., McDonagh, T., Lemieux, M., McBurney, M., Szilvasi, A., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0040031 · Cited by 715 · see citing works

SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine

Jiang, H., Khan, S., Wang, Y., Charron, G., He, B., Sebastian, C., Du, J., Kim, R., Ge, E., Mostoslavsky, R., et al. (2013) · Nature · doi:10.1038/nature12038 · Cited by 697 · see citing works

SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosisPreprint

Vaquero, A., Scher, M. B., Lee, D. H., Sutton, A., Cheng, H.-L., Alt, F. W., Serrano, L., Sternglanz, R., & Reinberg, D. (2006) · Genes & Development · doi:10.1101/gad.1412706 · Cited by 670 · see citing works

Calorie restriction enhances cell adaptation to hypoxia through Sirt1-dependent mitochondrial autophagy in mouse aged kidney

Kume, S., Uzu, T., Horiike, K., Chin-Kanasaki, M., Isshiki, K., Araki, S.-I., Sugimoto, T., Haneda, M., Kashiwagi, A., & Koya, D. (2010) · Journal of Clinical Investigation · doi:10.1172/jci41376 · Cited by 640 · 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

Transcription Factor HIF-1 Is a Necessary Mediator of the Pasteur Effect in Mammalian Cells

Seagroves, T. N., Ryan, H. E., Lu, H., Wouters, B. G., Knapp, M., Thibault, P., Laderoute, K. R., & Johnson, R. S. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.10.3436-3444.2001 · Cited by 634 · 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

Sirt1 improves healthy ageing and protects from metabolic syndrome-associated cancer

Herranz, D., Muñoz-Martin, M., Cañamero, M., Mulero, F., Martinez-Pastor, B., Fernandez-Capetillo, O., & Serrano, M. (2010) · Nature Communications · doi:10.1038/ncomms1001 · Cited by 612 · see citing works

Silent Information Regulator 1 Protects the Heart From Ischemia/Reperfusion

Hsu, C., Zhai, P., Yamamoto, T., Maejima, Y., Matsushima, S., Hariharan, N., Shao, D., Takagi, H., Oka, S., & Sadoshima, J. (2010) · Circulation · doi:10.1161/circulationaha.110.958033 · Cited by 561 · see citing works

SIRT1 Deacetylates and Inhibits SREBP-1C Activity in Regulation of Hepatic Lipid Metabolism*

Ponugoti, B., Kim, D.-H., Xiao, Z., Smith, Z., Miao, J., Zang, M., Wu, S.-Y., Chiang, C., Veenstra, T. D., & Kemper, J. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.122978 · Cited by 542 · see citing works

Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy

Hafner, A. V., Dai, J., Gomes, A. P., Xiao, C., Palmeira, C. M., Rosenzweig, A., & Sinclair, D. A. (2010) · Aging · doi:10.18632/aging.100252 · Cited by 542 · see citing works

SIRT3 Is a Stress-Responsive Deacetylase in Cardiomyocytes That Protects Cells from Stress-Mediated Cell Death by Deacetylation of Ku70

Sundaresan, N. R., Samant, S. A., Pillai, V. B., Rajamohan, S. B., & Gupta, M. P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00426-08 · Cited by 542 · see citing works

SIRT2 Maintains Genome Integrity and Suppresses Tumorigenesis through Regulating APC/C Activity

Kim, H., Vassilopoulos, A., Wang, R.-H., Lahusen, T. J., Xiao, Z., Xu, X., Li, C., Veenstra, T. D., Li, B., Yu, H., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.09.004 · Cited by 536 · see citing works

Cardiac Actions Of Angiotensin II: Role Of An Intracardiac Renin-Angiotensin System

Baker, K. M., Booz, G. W., & Dostal, D. E. (1992) · Annual Review of Physiology · doi:10.1146/annurev.ph.54.030192.001303 · Cited by 516 · see citing works

Untitled work

(2010) · doi:10.1016/j.cmet.2010.06.009 · Cited by 512 · see citing works

A mitochondrial UPR-mediated metabolic checkpoint regulates hematopoietic stem cell aging

Mohrin, M., Shin, J., Liu, Y., Brown, K., Luo, H., Xi, Y., Haynes, C. M., & Chen, D. (2015) · Science · doi:10.1126/science.aaa2361 · Cited by 490 · see citing works

Disruption of the Ang II type 1 receptor promotes longevity in mice

Benigni, A., Corna, D., Zoja, C., Sonzogni, A., Latini, R., Salio, M., Conti, S., Rottoli, D., Longaretti, L., Cassis, P., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci36703 · Cited by 486 · see citing works

The sirtuin SIRT6 blocks IGF-Akt signaling and development of cardiac hypertrophy by targeting c-Jun

Sundaresan, N. R., Vasudevan, P., Zhong, L., Kim, G. H., Samant, S. A., Parekh, V., Pillai, V. B., Veeranna, R. P., Gupta, M., Jeevanandam, V., et al. (2012) · Nature Medicine · doi:10.1038/nm.2961 · Cited by 477 · see citing works

SIRT4 Has Tumor-Suppressive Activity and Regulates the Cellular Metabolic Response to DNA Damage by Inhibiting Mitochondrial Glutamine Metabolism

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 · see citing works

mTOR as a central regulator of lifespan and aging

Papadopoli, D. J., Boulay, K., Kazak, L., Pollak, M., Mallette, F. A., Topisirović, I., & Hulea, L. (2019) · F1000Research · doi:10.12688/f1000research.17196.1 · Cited by 443 · see citing works

SIRT3 Reverses Aging-Associated Degeneration

Brown, K., Xie, S., Qiu, X., Mohrin, M., Shin, J., Liu, Y., Zhang, D., Scadden, D. T., & Chen, D. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.005 · Cited by 436 · see citing works

Tyrosine Dephosphorylation and Deactivation of Insulin Receptor Substrate-1 by Protein-tyrosine Phosphatase 1B

Goldstein, B. J., Bittner-Kowalczyk, A., White, M. F., & Harbeck, M. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4283 · Cited by 423 · see citing works

Regulation of Insulin Secretion by SIRT4, a Mitochondrial ADP-ribosyltransferase

Ahuja, N., Schwer, B., Carobbio, S., Waltregny, D., North, B. J., Castronovo, V., Maechler, P., & Verdin, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705488200 · Cited by 422 · 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

DNA resection in eukaryotes: deciding how to fix the break

Huertas, P. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1710 · Cited by 398 · see citing works

Ten years of NAD-dependent SIR2 family deacetylases: implications for metabolic diseases

Imai, S., & Guarente, L. (2010) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.02.003 · Cited by 394 · see citing works

Gadd45 in Stress Signaling, Cell Cycle Control, and Apoptosis

Salvador, J. M., Brown-Clay, J. D., & Fornace, A. J. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-8289-5_1 · Cited by 391 · see citing works

The role of sirtuins in cardiac disease

Matsushima, S., & Sadoshima, J. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00053.2015 · Cited by 390 · see citing works

Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6

Michishita, E., McCord, R. A., Boxer, L. D., Barber, M. F., Hong, T., Gozani, O., & Chua, K. F. (2009) · Cell Cycle · doi:10.4161/cc.8.16.9367 · Cited by 384 · see citing works

SIRT2 regulates NF-κB-dependent gene expression through deacetylation of p65 Lys310

Rothgiesser, K., Erener, S., Waibel, S., Lüscher, B., & Hottiger, M. O. (2010) · Journal of Cell Science · doi:10.1242/jcs.073783 · Cited by 377 · see citing works

Regulation of FOXOs and p53 by SIRT1 Modulators under Oxidative Stress

Hori, Y. S., Kuno, A., Hosoda, R., & Horio, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073875 · Cited by 361 · see citing works

SIRT1 Deacetylation and Repression of p300 Involves Lysine Residues 1020/1024 within the Cell Cycle Regulatory Domain 1

Bouras, T., Fu, M., Sauve, A. A., Wang, F., Quong, A. A., Perkins, N. D., Hay, R. T., Gu, W. J., & Pestell, R. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m408748200 · Cited by 354 · see citing works

Therapeutic effect of Sirtuin 3 on ameliorating nonalcoholic fatty liver disease: The role of the ERK-CREB pathway and Bnip3-mediated mitophagy

Li, R., Xin, T., Li, D., Wang, C., Zhu, H., & Zhou, H. (2018) · Redox Biology · doi:10.1016/j.redox.2018.07.011 · Cited by 353 · see citing works

Caloric Restriction in Humans: Impact on Physiological, Psychological, and Behavioral Outcomes

Redman, L. M., & Ravussin, É. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3253 · Cited by 346 · see citing works

The Deacetylase SIRT1 Promotes Membrane Localization and Activation of Akt and PDK1 During Tumorigenesis and Cardiac Hypertrophy

Sundaresan, N. R., Pillai, V. B., Wolfgeher, D., Samant, S. A., Vasudevan, P., Parekh, V., Raghuraman, H., Cunningham, J. M., Gupta, M., & Gupta, M. P. (2011) · Science Signaling · doi:10.1126/scisignal.2001465 · Cited by 345 · see citing works

Neuroprotective role of Sirt1 in mammalian models of Huntington's disease through activation of multiple Sirt1 targets

Jiang, M., Wang, J., Fu, J., Du, L., Jeong, H., West, T., Xiang, L., Peng, Q., Hou, Z., Cai, H., et al. (2011) · Nature Medicine · doi:10.1038/nm.2558 · Cited by 344 · see citing works

Sirt6 deficiency exacerbates podocyte injury and proteinuria through targeting Notch signaling

Liu, M., Liang, K., Zhen, J., Zhou, M., Wang, X., Wang, Z., Wei, X., Zhang, Y., Sun, Y., Zhou, Z., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00498-4 · Cited by 343 · see citing works

Pathways and Subcellular Compartmentation of NAD Biosynthesis in Human Cells

Nikiforov, A., Dölle, C., Niere, M., & Ziegler, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213298 · Cited by 326 · see citing works

Sirtuin7 oncogenic potential in human hepatocellular carcinoma and its regulation by the tumor suppressors MiR-125a-5p and MiR-125b

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 322 · see citing works

Protein Tyrosine Phosphatase 1B Interacts With the Activated Insulin Receptor

Seely, B. L., Staubs, P. A., Reichart, D. R., Berhanu, P., Milarski, K. L., Saltiel, A. R., Kusari, J., & Olefsky, J. M. (1996) · Diabetes · doi:10.2337/diab.45.10.1379 · Cited by 319 · see citing works

Sirt1 activation protects the mouse renal medulla from oxidative injury

He, W., Wang, Y., Zhang, M., Li, Y., Davis, L. S., Fan, H. X., Yang, H., Fogo, A. B., Zent, R., Harris, R. C., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci41563 · Cited by 316 · see citing works

Brain SIRT1: Anatomical Distribution and Regulation by Energy Availability

Ramadori, G., Lee, C. E., Bookout, A. L., Lee, S., Williams, K. W., Anderson, J. G., Elmquist, J. K., & Coppari, R. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.3257-08.2008 · Cited by 311 · see citing works

Nicotinamide Mononucleotide, an Intermediate of NAD+ Synthesis, Protects the Heart from Ischemia and Reperfusion

Yamamoto, T., Byun, J., Zhai, P., Ikeda, Y., Oka, S., & Sadoshima, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098972 · Cited by 305 · see citing works

SIRT1 Promotes Cell Survival under Stress by Deacetylation-Dependent Deactivation of Poly(ADP-Ribose) Polymerase 1

Rajamohan, S. B., Pillai, V. B., Gupta, M., Sundaresan, N. R., Birukov, K. G., Samant, S. A., Hottiger, M. O., & Gupta, M. P. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00121-09 · Cited by 303 · see citing works

TGF-β1/Smads and miR-21 in Renal Fibrosis and Inflammation

Łoboda, A., Sobczak, M., Józkowicz, A., & Dulak, J. (2016) · Mediators of Inflammation · doi:10.1155/2016/8319283 · Cited by 298 · see citing works

Teaching the fundamentals of electron transfer reactions in mitochondria and the production and detection of reactive oxygen species

Mailloux, R. J. (2015) · Redox Biology · doi:10.1016/j.redox.2015.02.001 · Cited by 292 · see citing works

The type III histone deacetylase Sirt1 is essential for maintenance of T cell tolerance in mice

Zhang, J., Lee, S., Shannon, S., Gao, B., Chen, W., Chen, A., Divekar, R. D., McBurney, M. W., Braley‐Mullen, H., Zaghouani, H., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38902 · Cited by 289 · see citing works

Identification of a cellularly active SIRT6 allosteric activator

Huang, Z., Zhao, J., Deng, W., Chen, Y., Shang, J., Song, K., Zhang, L., Wang, C., Lu, S., Yang, X., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0150-0 · Cited by 277 · see citing works

SIRT7 promotes genome integrity and modulates non‐homologous end joining DNA repair

Vázquez, B. N., Thackray, J. K., Simonet, N. G., Kane‐Goldsmith, N., Martínez‐Redondo, P., Nguyen, T. T. T., Bunting, S. F., Vaquero, A., Tischfield, J. A., & Serrano, L. (2016) · The EMBO Journal · doi:10.15252/embj.201593499 · Cited by 276 · see citing works

The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic stability

Yang, B., Zwaans, B. M. M., Eckersdorff, M., & Lombard, D. B. (2009) · Cell Cycle · doi:10.4161/cc.8.16.9329 · Cited by 254 · see citing works

Nicotinamide Mononucleotide, an NAD+ Precursor, Rescues Age-Associated Susceptibility to AKI in a Sirtuin 1–Dependent Manner

Guan, Y., Wang, S.-R., Huang, X.-Z., Xie, Q.-H., Xu, Y.-Y., Shang, D., & Hao, C.-M. (2017) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016040385 · Cited by 238 · see citing works

SIRT1 Inhibits Transforming Growth Factor β-Induced Apoptosis in Glomerular Mesangial Cells via Smad7 Deacetylation

Kume, S., Haneda, M., Kanasaki, K., Sugimoto, T., Araki, S., Isshiki, K., Isono, M., Uzu, T., Guarente, L., Kashiwagi, A., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605904200 · Cited by 231 · see citing works

Mitochondrial sirtuins

Huang, J.-Y., Hirschey, M. D., Shimazu, T., Ho, L., & Verdin, E. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.12.021 · Cited by 231 · see citing works

SIRT1 Deacetylase in POMC Neurons Is Required for Homeostatic Defenses against Diet-Induced Obesity

Ramadori, G., Fujikawa, T., Fukuda, M., Anderson, J. G., Morgan, D. A., Mostoslavsky, R., Stuart, R. C., Perelló, M., Vianna, C. R., Nillni, E. A., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.05.010 · Cited by 226 · see citing works

SIRT1 Suppresses the Epithelial-to-Mesenchymal Transition in Cancer Metastasis and Organ Fibrosis

Šimić, P., Williams, E. O., Bell, E. L., Gong, J., Bonkowski, M. S., & Guarente, L. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.03.019 · Cited by 221 · see citing works

SIRT1 protects the heart from ER stress-induced cell death through eIF2α deacetylation

Prola, A., Silva, J. P. D., Guilbert, A., Lecru, L., Piquereau, J., Ribeiro, M., Matéo, P., Gressette, M., Fortin, D., Boursier, C., et al. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.138 · Cited by 216 · see citing works

Dietary Restriction Ameliorates Diabetic Nephropathy through Anti-Inflammatory Effects and Regulation of the Autophagy via Restoration of Sirt1 in Diabetic Wistar Fatty (<i>fa/fa</i>) Rats: A Model of Type 2 Diabetes

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SIRT3 deficiency exacerbates ischemia-reperfusion injury: implication for aged hearts

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SIRT3 Blocks Aging-Associated Tissue Fibrosis in Mice by Deacetylating and Activating Glycogen Synthase Kinase 3β

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Resveratrol Inhibits Renal Fibrosis in the Obstructed Kidney

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SIRT3 Is a Mitochondrial Tumor Suppressor: A Scientific Tale That Connects Aberrant Cellular ROS, the Warburg Effect, and Carcinogenesis

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The role of JNK in the development of hepatocellular carcinomaPreprint

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Markers of mitochondrial biogenesis and metabolism are lower in overweight and obese insulin-resistant subjects.

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SIRT1 activation by resveratrol ameliorates cisplatin-induced renal injury through deacetylation of p53

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Silent information regulator 2 (SIRT1) attenuates oxidative stress-induced mesangial cell apoptosis via p53 deacetylation

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Sirtuin 6 (SIRT6) rescues the decline of homologous recombination repair during replicative senescence

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The Direct Involvement of SirT1 in Insulin-induced Insulin Receptor Substrate-2 Tyrosine Phosphorylation

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Treatment with SRT1720, a SIRT1 activator, ameliorates fatty liver with reduced expression of lipogenic enzymes in MSG mice

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SIRT6 is required for maintenance of telomere position effect in human cells

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Mitochondrial Stress-Initiated Aberrant Activation of the NLRP3 Inflammasome Regulates the Functional Deterioration of Hematopoietic Stem Cell Aging

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PGC-1α Protects from Notch-Induced Kidney Fibrosis Development

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Aging-like Phenotype and Defective Lineage Specification in SIRT1-Deleted Hematopoietic Stem and Progenitor Cells

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Alteration of Forkhead Box O (Foxo4) Acetylation Mediates Apoptosis of Podocytes in Diabetes Mellitus

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The complement system in ischemia–reperfusion injuries

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Functional Interplay between Acetylation and Methylation of the RelA Subunit of NF-κB

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SIRT1 modulates MAPK pathways in ischemic–reperfused cardiomyocytes

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Sirtuin 3 regulates Foxo3a-mediated antioxidant pathway in microglia

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SIRT6 Controls Hematopoietic Stem Cell Homeostasis through Epigenetic Regulation of Wnt Signaling

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Sirtuin 3 Deficiency Accelerates Hypertensive Cardiac Remodeling by Impairing Angiogenesis

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The epigenetic regulator SIRT6 protects the liver from alcohol-induced tissue injury by reducing oxidative stress in mice

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Sirtuin 1 Regulates Hepatitis B Virus Transcription and Replication by Targeting Transcription Factor AP-1

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Inhibition of myocardial reperfusion injury by ischemic postconditioning requires sirtuin 3-mediated deacetylation of cyclophilin D

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The Effects of Calorie Restriction on Autophagy: Role on Aging Intervention

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Endothelial Sirtuin 1 Deficiency Perpetrates Nephrosclerosis through Downregulation of Matrix Metalloproteinase-14

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Protective effects of sirtuin 3 in a murine model of sepsis-induced acute kidney injury

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SIRT6 Overexpression Potentiates Apoptosis Evasion in Hepatocellular Carcinoma via BCL2-Associated X Protein–Dependent Apoptotic Pathway

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Calorie restriction-induced SIRT6 activation delays aging by suppressing NF-κB signaling

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Sirt1 ablation promotes stress-induced loss of epigenetic and genomic hematopoietic stem and progenitor cell maintenance

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SIRT2 Regulates LPS-Induced Renal Tubular CXCL2 and CCL2 Expression

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SIRT1 deficiency compromises mouse embryonic stem cell hematopoietic differentiation, and embryonic and adult hematopoiesis in the mouse

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Increase in Angiotensin II Type 1 Receptor Expression Immediately After Ischemia-Reperfusion in Isolated Rat Hearts

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The Sirt1 activator, SRT1720, attenuates renal fibrosis by inhibiting CTGF and oxidative stress

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SIRT6 Promotes Hepatic Beta-Oxidation via Activation of PPARα

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Regulation of chromatin structure by poly(ADP-ribosyl)ation

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Reduction in podocyte SIRT1 accelerates kidney injury in aging mice

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Melatonin Effects on Non-Alcoholic Fatty Liver Disease Are Related to MicroRNA-34a-5p/Sirt1 Axis and Autophagy

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SIRT1 antagonizes liver fibrosis by blocking hepatic stellate cell activation in mice

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SIRT1 regulates metabolism and leukemogenic potential in CML stem cells

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SIRT6 Protects Against Liver Fibrosis by Deacetylation and Suppression of SMAD3 in Hepatic Stellate Cells

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SIRT7 regulates hepatocellular carcinoma response to therapy by altering the p53-dependent cell death pathway

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Sirtuin 3 Activation by Honokiol Decreases Unilateral Ureteral Obstruction-Induced Renal Inflammation and Fibrosis via Regulation of Mitochondrial Dynamics and the Renal NF-κB-TGF-β1/Smad Signaling Pathway

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Mitochondrial Sirtuins in cardiometabolic diseases

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The deacetylase sirtuin 6 protects against kidney fibrosis by epigenetically blocking β-catenin target gene expression

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SIRT6, a protein with many faces

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Association of Sirtuin 1 (SIRT1) Gene SNPs and Transcript Expression Levels With Severe Obesity

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SIRT5 promotes cell proliferation and invasion in hepatocellular carcinoma by targeting E2F1

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Sirtuin‐1/Mitochondrial Ribosomal Protein S5 Axis Enhances the Metabolic Flexibility of Liver Cancer Stem Cells

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Role of complement and perspectives for intervention in ischemia-reperfusion damage

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Endothelial sirtuin 1 inactivation enhances capillary rarefaction and fibrosis following kidney injury through Notch activation

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SIRT4 silencing in tumor-associated macrophages promotes HCC development via PPARδ signalling-mediated alternative activation of macrophages

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Ampelopsin attenuates carbon tetrachloride-induced mouse liver fibrosis and hepatic stellate cell activation associated with the SIRT1/TGF-β1/Smad3 and autophagy pathway

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Sirtuin 1 Activation Reduces Transforming Growth Factor-β1–Induced Fibrogenesis and Affords Organ Protection in a Model of Progressive, Experimental Kidney and Associated Cardiac Disease

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AGK2, A SIRT2 Inhibitor, Inhibits Hepatitis B Virus Replication In Vitro And In Vivo

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Interplay between SIRT1 and hepatitis B virus X protein in the activation of viral transcription

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NAD-dependent histone deacetylase, SIRT1, plays essential roles in the maintenance of hematopoietic stem cells

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SIRT1 in the Development and Treatment of Hepatocellular Carcinoma

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NMNAT3 is involved in the protective effect of SIRT3 in Ang II-induced cardiac hypertrophy

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Systemic DNA Damage Response and Metabolic Syndrome as a Premalignant State

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Protein tyrosine phosphatase 1B interacts with the activated insulin receptor

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Losartan Protects the Heart Against Ischemia Reperfusion Injury: Sirtuin3 Involvement

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Hepatic stellate cell-specific deletion of SIRT1 exacerbates liver fibrosis in mice

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Sirtuin 6 promotes transforming growth factor‐β1/H 2 O 2 / HOC l‐mediated enhancement of hepatocellular carcinoma cell tumorigenicity by suppressing cellular senescence

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HBx-elevated SIRT2 promotes HBV replication and hepatocarcinogenesis

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miR-200a controls hepatic stellate cell activation and fibrosis via SIRT1/Notch1 signal pathway

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MicroRNA-141 Targets Sirt1 and Inhibits Autophagy to Reduce HBV Replication

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SIRT3-KLF15 signaling ameliorates kidney injury induced by hypertension

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Ginkgetin aglycone ameliorates LPS-induced acute kidney injury by activating SIRT1 via inhibiting the NF-κB signaling pathway

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Effect of renin–angiotensin system on senescence

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Forkhead box-O transcription factor: critical conductors of cancer's fate

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Anti-Fibrotic Effect of Losartan, an Angiotensin II Receptor Blocker, Is Mediated through Inhibition of ER Stress via Up-Regulation of SIRT1, Followed by Induction of HO-1 and Thioredoxin

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SIRT1 upregulation protects against liver injury induced by a HFD through inhibiting CD36 and the NF‑κB pathway in mouse kupffer cells

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Sirt6 regulates dendritic cell differentiation, maturation, and function

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Regulation of unfolded protein response in hematopoietic stem cells

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SIRT3 expression in hepatocellular carcinoma and its impact on proliferation and invasion of hepatoma cells

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MiR-9a-5p regulates proliferation and migration of hepatic stellate cells under pressure through inhibition of Sirt1

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Sirtuins in Hematological Aging and Malignancy

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Protective role of AGK2 on thioacetamide-induced acute liver failure in mice

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SIRT1 mediates the role of RNA-binding protein QKI 5 in the synthesis of triglycerides in non-alcoholic fatty liver disease mice via the PPARα/FoxO1 signaling pathway

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Regulation of Adaptive Immune Cells by Sirtuins

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SIRT6 Inhibitor, OSS_128167 Restricts Hepatitis B Virus Transcription and Replication Through Targeting Transcription Factor Peroxisome Proliferator-Activated Receptors α

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Sirtuin2 enhances the tumoricidal function of liver natural killer cells in a mouse hepatocellular carcinoma model

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SIRT3 as a Regulator of Non-alcoholic Fatty Liver Disease

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Palmitate induces cardiomyocyte death via inositol requiring enzyme-1 (IRE1)-mediated signaling independent of X-box binding protein 1 (XBP1)

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γ-Mangostin alleviates liver fibrosis through Sirtuin 3-superoxide-high mobility group box 1 signaling axis

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SIRT3 functions as a tumor suppressor in hepatocellular carcinoma

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Downregulation of angiotensin type 1 receptor and nuclear factor-κB by sirtuin 1 contributes to renoprotection in unilateral ureteral obstruction

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The Role of Sirtuin 3 in Radiation-Induced Long-Term Persistent Liver Injury

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Role of sirtuins in liver diseases

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SIRT1 activators promote p65 deacetylation and suppress TNFa stimulated NF‐kB activation

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Connecting the Dots: Linking Sirtuins and AMPK in Metabolism and Aging

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Science and the search for meaning The Meaning of Human Existence Edward O. Wilson Liveright, 2014. 208 pp.

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Sirtuins in hematopoiesis and blood malignancies

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Sirtuins in the biology of aging

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Targeting sirtuins to modulate energy metabolism in heart disease

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Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging

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Chrononutrition—When We Eat Is of the Essence in Tackling Obesity

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The impact of aging and oxidative stress in metabolic and nervous system disorders: programmed cell death and molecular signal transduction crosstalk

Maiese, K. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1273570 · Cited by 47 · see citing works

Why Is Longevity Still a Scientific Mystery? Sirtuins—Past, Present and Future

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Cellular Metabolism: A Fundamental Component of Degeneration in the Nervous System

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Improving the effectiveness of anti-aging modalities by using the constrained disorder principle-based management algorithms

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A nutrigeroscience approach: Dietary macronutrients and cellular senescence

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SIRT2 inhibition protects against cardiac hypertrophy and ischemic injury

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Cognitive Impairment in Multiple Sclerosis

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The Metabolic Basis for Nervous System Dysfunction in Alzheimer’s Disease, Parkinson’s Disease, and Huntington’s Disease

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Cornerstone Cellular Pathways for Metabolic Disorders and Diabetes Mellitus: Non-Coding RNAs, Wnt Signaling, and AMPK

Maiese, K. (2023) · Cells · doi:10.3390/cells12222595 · Cited by 29 · see citing works

Pathophysiology of vascular ageing and the effect of novel cardio‐renal protective medications in preventing progression of chronic kidney disease in people living with diabetes

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Ergothioneine, where are we now?

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The Role of Sirtuin-1 (SIRT1) in the Physiology and Pathophysiology of the Human Placenta

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PPARα in the Epigenetic Driver Seat of NAFLD: New Therapeutic Opportunities for Epigenetic Drugs?

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Novel Thiazole-Based SIRT2 Inhibitors Discovered via Molecular Modelling Studies and Enzymatic Assays

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Sirtuins and Gut Microbiota: Dynamics in Health and a Journey from Metabolic Dysfunction to Hepatocellular Carcinoma

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Vitamin D, Cellular Senescence and Chronic Kidney Diseases: What Is Missing in the Equation?

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Epigenetic aging of mammalian gametes

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Astragalin from Thesium chinense: A Novel Anti-Aging and Antioxidant Agent Targeting IGFR/CD38/Sirtuins

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Ginsenoside Rb1 improves intestinal aging via regulating the expression of sirtuins in the intestinal epithelium and modulating the gut microbiota of mice

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Cardiac Acetylation in Metabolic Diseases

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Chronobiotic and cytoprotective activity of melatonin in the cardiovascular system. Doses matter

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Melatonin as a Chronobiotic and Cytoprotector in Non-communicable Diseases: More than an Antioxidant

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Distinctive Gene Expression Profiles and Biological Responses of Skin Fibroblasts to Nicotinamide Mononucleotide: Implications for Longevity Effects on Skin

Kang, S., Park, J.-W., Cho, E., Kim, D., Ye, S., Jeong, E. T., Jun, S., & Kang, N. G. (2025) · Biomedicines · doi:10.3390/biomedicines13102395 · Cited by 13 · see citing works

Nutraceuticals, Social Interaction, and Psychophysiological Influence on Pet Health and Well-Being: Focus on Dogs and Cats

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p63 affects distinct metabolic pathways during keratinocyte senescence, evaluated by metabolomic profile and gene expression analysis

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Evolution, mechanism and limits of dietary restriction induced health benefits & longevity

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The Antiaging and Antioxidative Effects of a Combination of Resveratrol and High‐Intensity Interval Training on the Frontal Lobe in Aged Rats: The Role of SIRTS 4, SIRTS 5, SOD1, and SOD2

Mehrabi, A., Nouri, R., Gaeini, A. A., Amirazodi, M., Mehrtash, M., Esfahlani, M. A., Bahrami, M., Bejeshk, M. A., & Rajizadeh, M. A. (2025) · Oxidative Medicine and Cellular Longevity · doi:10.1155/omcl/8251896 · Cited by 9 · see citing works

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Cardiovascular and nonalcoholic fatty liver disease: Sharing common ground through SIRT1 pathways

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Ribose-induced advanced glycation end products reduce the lifespan in Drosophila melanogaster by changing the redox state and down-regulating the Sirtuin genes

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Pyroptosis, Apoptosis, and Autophagy: Critical Players of Inflammation and Cell Demise in the Nervous System

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Human Umbilical Cord Mesenchymal-Stem-Cell-Derived Extracellular Vesicles Reduce Skin Inflammation In Vitro

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Mitochondrial Function in Neurons and Glia in Health and Its Alteration in Parkinson's Disease: A Review

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The Implications of Telomere Length: Advanced Aging, Cell Senescence, MRI Phenotypes, Stem Cells and Alzheimer’s Disease

Maiese, K. (2023) · Current Neurovascular Research · doi:10.2174/1567202620666230510150337 · Cited by 7 · see citing works

Obesity, the other pandemic: linking diet and carcinogenesis by epigenetic mechanisms

Izquierdo‐Torres, E., Hernández‐Oliveras, A., Lozano-Arriaga, D., & Zarain‐Herzberg, Á. (2022) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2022.109092 · Cited by 7 · see citing works

Rodent Models of D-Galactose Induction of Accelerated Aging: A Platform for Exploring Kidney Aging Mechanisms and Anti-Kidney Aging Strategies

Niu, S., Azzouz, R. S., & Yan, L. (2026) · Cells · doi:10.3390/cells15090766 · Cited by 5 · see citing works

Insights into Reproductive Immunology and Placental Pathology

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Intense Caloric Restriction from Birth Protects the Heart Against Ischemia/Reperfusion Injury and Reduces Reactive Oxygen Species in Ovariectomized Rats

Cantuária, V. L., Rodrigues, C. M., Dias, I. R., Ottone, V. D. O., Costa, B. O., Godinho, L. F., Silva, G., Schetino, M. A. A., Rocha-Vieira, E., Dias-Peixoto, M. F., et al. (2025) · Antioxidants · doi:10.3390/antiox14020169 · Cited by 4 · see citing works

Clinical studies with drugs and biologics aimed at slowing or reversing normal aging processes—emerging results and future perspectives

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Nutrient-Sensing Pathways: Gatekeepers of Longevity

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Does Selection for Longevity in Acheta domesticus Involve Sirtuin Activity Modulation and Differential Response to Activators (Resveratrol and Nanodiamonds)?

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Melatonin as a Chronobiotic and Cytoprotector in Healthy Aging

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Influence of a diet with potential geroprotectors on blood biochemistry and aging-associated markers in domestic cats: a pilot study

Protopopov, V. A., Sekunov, A. V., Toropova, T. V., Георгиевна, Б. И., Burganova, D. N., Milaev, V. B., Sharafislamova, M. B., Pozdeev, S. V., & Moskalev, A. (2025) · Biogerontology · doi:10.1007/s10522-025-10293-0 · Cited by 2 · see citing works

Circadian Rhythm, Clock Genes, and Stroke

Maiese, K. (2024) · Current Neurovascular Research · doi:10.2174/1567202622999241028121817 · Cited by 1 · see citing works

NAD+ and Its Precursors for Health and Longevity

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Dietary strategies to counter obesity-accelerated aging: Enhancing health-span and longevity

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Natural Bioactive Compounds Targeting Key Hallmarks of Aging: Functional Food Potential of Spermidine, Fisetin, Berberine, and Urolithin A

Rzeski, W., & Rzeska, W. (2026) · Nutrients · doi:10.3390/nu18152511 · Cited by 1 · see citing works

Oxidative stress, aging, metabolism, SIRT1, and the gut microbiota: the neurocardiac basis of cognitive loss

Maiese, K. (2026) · Medical Gas Research · doi:10.4103/mgr.medgasres-d-26-00073 · Cited by 2 · see citing works

SCA® Slows the Decline of Functional Parameters Associated with Senescence in Skin Cells

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Az idősödés során jellemző genetikai és epigenetikai változások és a gammopátiák progressziója •

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Sirtuins and the Twelve Hallmarks of Ageing: A Framework for Understanding Ageing Processes and Targeted Intervention

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Mitigating Oxidative Stress and Inflammation: The Protective Role of β-lapachone in Kidney Disease

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Sarcopenic obesity: prospects of mitochondrial transplantation to combat metabolic deterioration in aging

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Application of melatonin in long COVID and noncommunicable diseases

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Sirtuins, Autophagy, and Brain Longevity

Bisht, S., Jaiswal, V., & Prakash, S. (2025) · Nutritional neurosciences · doi:10.1007/978-981-95-2790-8_11

Stress and neurodegeneration: mechanistic insights and therapeutic opportunities for preserving brain resilience

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Diapause and aging: Two opposing yet intertwined biological phenomena

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Transcriptional Control of Hepatocellular Carcinoma Cells Aggressiveness by AAV2/8-Mediated Delivery of Human Centenarian-Associated SIRT6 N308K/A313S

Vittal, M., Liorni, N., Kazaili, A., Leire, E., Akhtar, R., Mazza, T., & Vinciguerra, M. (2026) · Cancers · doi:10.3390/cancers18050812

Involvement of eIF2 in cardiomyocytes response to endoplasmic reticulum stress

PERALTA, C. C. (2023) · doi:10.70675/09c9192ez0534z46d9za72cze056e66291cb

Translational perspectives in drug discovery

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Mechanistic intersections of empagliflozin and nebivolol in aging-associated redox and inflammatory pathways

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Sirtuins and Aging

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Sirtuins as Mediator of the Anti-Ageing Effects of Calorie Restriction in Skeletal and Cardiac Muscle

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