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Mammalian sirtuins—emerging roles in physiology, aging, and calorie restriction

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Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation

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

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Sirt1 Regulates Aging and Resistance to Oxidative Stress in the Heart

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

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

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SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways

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The secret life of NAD+: an old metabolite controlling new metabolic signaling pathways

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Calorie Restriction Increases Muscle Mitochondrial Biogenesis in Healthy Humans

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SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle

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Sirt1 and the Mitochondria

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Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2

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Multiple roles of HDAC inhibition in neurodegenerative conditions

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Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling

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Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription

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Redox regulation of mitochondrial function

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Redox regulation of SIRT1 in inflammation and cellular senescence

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Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1α in skeletal muscle

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Sirtuin Functions in Health and Disease

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Sirtuins as potential targets for metabolic syndrome

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

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Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity

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Targeting Sirtuin 1 to Improve Metabolism: All You Need Is NAD+?

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

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Epigenetic control of rDNA loci in response to intracellular energy status

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The Role of SIRT1 on DNA Damage Response and Epigenetic Alterations in Cancer

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Manganese Superoxide Dismutase: Guardian of the Powerhouse

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SIRT6 stabilizes DNA-dependent protein kinase at chromatin for DNA double-strand break repair

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Dynamic regulation of PGC‐1α localization and turnover implicates mitochondrial adaptation in calorie restriction and the stress response

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Sirtuin-3 (SIRT3), a novel potential therapeutic target for oral cancer

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Sirtuin 3 deficiency is associated with inhibited mitochondrial function and pulmonary arterial hypertension in rodents and humans

Paulin, R., Dromparis, P., Sutendra, G., Gurtu, V., Zervopoulos, S., Bowers, L., Haromy, A., Webster, L., Provencher, S., Bonnet, S., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.08.011 · Cited by 214 · see citing works

Protective effects and mechanisms of sirtuins in the nervous system

Zhang, F., Wang, S., Gan, L., Vosler, P. S., Gao, Y., Zigmond, M. J., & Chen, J. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.09.001 · Cited by 211 · see citing works

The coordination of nuclear and mitochondrial communication during aging and calorie restriction

Finley, L. W. S., & Haigis, M. C. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.03.003 · Cited by 207 · see citing works

Sirtuin 6 Expression and Inflammatory Activity in Diabetic Atherosclerotic Plaques: Effects of Incretin Treatment

Balestrieri, M. L., Rizzo, M. R., Barbieri, M., Paolisso, P., D’Onofrio, N., Giovane, A., Siniscalchi, M., Minicucci, F., Sardu, C., D’Andrea, D., et al. (2015) · Diabetes · doi:10.2337/db14-1149 · Cited by 196 · see citing works

Regulation of MnSOD Enzymatic Activity by Sirt3 Connects the Mitochondrial Acetylome Signaling Networks to Aging and Carcinogenesis

Tao, R., Vassilopoulos, A., Parisiadou, L., Yan, Y., & Gius, D. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5482 · Cited by 194 · see citing works

SIRT3 regulates mitochondrial protein acetylation and intermediary metabolism

Hirschey, M. D., Shimazu, T., Huang, J. Y., Schwer, B., & Verdin, E. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010850 · Cited by 180 · see citing works

Efficient Demyristoylase Activity of SIRT2 Revealed by Kinetic and Structural Studies

Teng, Y.-B., Jing, H., Aramsangtienchai, P., He, B., Khan, S., Hu, J., Lin, H., & Hao, Q. (2015) · Scientific Reports · doi:10.1038/srep08529 · Cited by 184 · see citing works

Deacetylation of PGC-1α by SIRT1: importance for skeletal muscle function and exercise-induced mitochondrial biogenesis

Gurd, B. J. (2011) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h11-070 · Cited by 171 · see citing works

NAD⁺metabolism and oxidative stress: the golden nucleotide on a crown of thorns

Massudi, H., Grant, R., Guillemin, G. J., & Braidy, N. (2012) · Redox Report · doi:10.1179/1351000212y.0000000001 · Cited by 158 · see citing works

Insulin‐like growth factor‐1 regulates the <scp>SIRT</scp> 1‐p53 pathway in cellular senescence

Tran, D., Bergholz, J., Zhang, H., He, H., Wang, Y., Zhang, Y., Li, Q., Kirkland, J. L., & Xiao, Z. (2014) · Aging Cell · doi:10.1111/acel.12219 · Cited by 161 · see citing works

Histone deacetylases (HDACs) and brain function

Volmar, C.-H., & Wahlestedt, C. (2015) · Neuroepigenetics · doi:10.1016/j.nepig.2014.10.002 · Cited by 151 · see citing works

Lysine-Directed Post-translational Modifications of Tau Protein in Alzheimer's Disease and Related Tauopathies

Kontaxi, C., Piccardo, P., & Gill, A. C. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00056 · Cited by 138 · see citing works

NAD(+)-SIRT1 control of H3K4 trimethylation through circadian deacetylation of MLL1

Aguilar-Arnal, L., Katada, S., Orozco-Solis, R., & Sassone-Corsi, P. (2015) · Nature Structural &amp; Molecular Biology · doi:10.1038/nsmb.2990 · Cited by 117 · see citing works

Caloric restriction blocks neuropathology and motor deficits in Machado-Joseph disease mouse models through SIRT1 pathway

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 · see citing works

The seven faces of SIRT7

Blank, M. F., & Grummt, I. (2017) · Transcription · doi:10.1080/21541264.2016.1276658 · Cited by 111 · see citing works

Distinct regulation of mitochondrial localization and stability of two human Sirt5 isoforms: Regulation of two human SIRT5 isoforms

Matsushita, N., Yonashiro, R., Ogata, Y., Sugiura, A., Nagashima, S., Fukuda, T., Inatome, R., & Yanagi, S. (2011) · Genes to Cells · doi:10.1111/j.1365-2443.2010.01475.x · Cited by 106 · see citing works

SIRT1 Acts as a Nutrient-sensitive Growth Suppressor and Its Loss Is Associated with Increased AMPK and Telomerase Activity

Narala, S. R., Allsopp, R. C., Wells, T. B., Zhang, G., Prasad, P., Coussens, M. J., Rossi, D. J., Weissman, I. L., & Vaziri, H. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-09-0965 · Cited by 106 · see citing works

Nicotinamide extends replicative lifespan of human cells

Kang, H. T., Lee, H. I., & Hwang, E. S. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00234.x · Cited by 105 · see citing works

HDAC8 cooperates with SMAD3/4 complex to suppress SIRT7 and promote cell survival and migration

Tang, X., Li, G., Su, F., Cai, Y., Shi, L., Meng, Y., Liu, Z., Sun, J., Wang, M., Qian, M., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa039 · Cited by 91 · see citing works

Quantification of lysine acetylation and succinylation stoichiometry in proteins using mass spectrometric data-independent acquisitions (SWATH)

Meyer, J. G., D’Souza, A. K., Sorensen, D. J., Rardin, M. J., Wolfe, A. J., Gibson, B. W., & Schilling, B. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1476-z · Cited by 79 · see citing works

The role of altered protein acetylation in neurodegenerative disease

Kabir, F., Atkinson, R., Cook, A. L., Phipps, A. J., & King, A. E. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1025473 · Cited by 75 · see citing works

SIRT5 deficiency suppresses mitochondrial ATP production and promotes AMPK activation in response to energy stress

Zhang, M., Wu, J., Sun, R., Tao, X., Wang, X., Kang, Q., Wang, H., Zhang, L., Liu, P., Zhang, J., et al. (2019) · PLOS ONE · doi:10.1371/journal.pone.0211796 · Cited by 72 · see citing works

Alcohol alters hepatic FoxO1, p53, and mitochondrial SIRT5 deacetylation function

Lieber, C. S., Leo, M. A., Wang, X., & DeCarli, L. M. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.06.006 · Cited by 71 · see citing works

Protein deacetylation by sirtuins: delineating a post-translational regulatory program responsive to nutrient and redox stressors

Bao, J., & Sack, M. N. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0402-y · Cited by 67 · see citing works

Differential sirtuin expression patterns in amyotrophic lateral sclerosis (ALS) postmortem tissue: neuroprotective or neurotoxic properties of sirtuins in ALS?

Körner, S., Böselt, S., Thau, N., Rath, K. J., Dengler, R., & Petri, S. (2013) · Neurodegenerative Diseases · doi:10.1159/000338048 · Cited by 64 · see citing works

Interplay between protein acetylation and ubiquitination controls MCL1 protein stability

Shimizu, K., Gi, M., Suzuki, S., North, B. J., Watahiki, A., Fukumoto, S., Asara, J. M., Tokunaga, F., Wei, W., & Inuzuka, H. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109988 · Cited by 62 · see citing works

Ethanol intoxication increases hepatic N-lysyl protein acetylation

Picklo, M. J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.09.039 · Cited by 60 · see citing works

Chapter 8 Acetylation of Mitochondrial Proteins

Hirschey, M. D., Shimazu, T., Huang, J., & Verdin, E. (2009) · Methods in Enzymology · doi:10.1016/s0076-6879(09)05008-3 · Cited by 55 · see citing works

SIRT5 deacetylates and activates urate oxidase in liver mitochondria of mice

Nakamura, Y., Ogura, M., Ogura, K., Tanaka, D., & Inagaki, N. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.10.009 · Cited by 55 · see citing works

Sirtuins, nuclear hormone receptor acetylation and transcriptional regulation

Whittle, J. R., Powell, M. J., Popov, V. M., Shirley, L. A., Wang, C., & Pestell, R. G. (2007) · Trends in Endocrinology &amp; Metabolism · doi:10.1016/j.tem.2007.07.007 · Cited by 51 · see citing works

SIRT7 activates p53 by enhancing PCAF-mediated MDM2 degradation to arrest the cell cycle

Lu, Y.-F., Xu, X.-P., Lu, X.-P., Zhu, Q., Liu, G., Bao, Y.-T., Wen, H., Li, Y.-L., Gu, W., & Zhu, W.-G. (2020) · Oncogene · doi:10.1038/s41388-020-1305-5 · Cited by 40 · see citing works

Comparison of sirtuin 3 levels in ALS and Huntington's disease-differential effects in human tissue samples vs. transgenic mouse models

Buck, E., Bayer, H., Lindenberg, K. S., Hanselmann, J., Pasquarelli, N., Ludolph, A. C., Weydt, P., & Witting, A. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00156 · Cited by 36 · see citing works

Leptin induces SIRT1 expression through activation of NF-E2-related factor 2: implications for obesity-associated colon carcinogenesis

Song, N.-Y., Lee, Y.-H., Na, H.-K., Baek, J.-H., & Surh, Y.-J. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.02.001 · Cited by 36 · see citing works

Glycyrrhizin mitigates inflammatory bone loss and promotes expression of senescence-protective sirtuins in an aging mouse model of periprosthetic osteolysis

Yamada, C., Ho, A., Akkaoui, J., Garcia, C., Duarte, C., & Movila, A. (2021) · Biomedicine &amp; Pharmacotherapy · doi:10.1016/j.biopha.2021.111503 · Cited by 33 · see citing works

SIRT7 regulates NUCKS1 chromatin binding to elicit metabolic and inflammatory gene expression in senescence and liver aging

Tran, K. A., Gilbert, M., Vazquez, B. N., Ianni, A., Garcia, B. A., Vaquero, A., & Berger, S. L. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.05.025 · Cited by 15 · see citing works

High calorie diet background alters the expression of sirtuins in the testes of mice under caloric restriction

Maldonado, M., Chen, J., Duan, H., Huang, T., Jiang, G., & Zhong, Y. (2021) · Translational Medicine of Aging · doi:10.1016/j.tma.2021.02.001 · Cited by 11 · see citing works

Sirtuins as Potential Drug Targets for Metabolic Diseases

Tong, Q. (2011) · doi:10.1002/9780470910016.ch15

Effect of Nutritional Stress on the Expression of Sirtuin Gene Family

Zhang, X., Ameer, F. S., Crane, J., et al. (2020) · Innovation in Aging · doi:10.1093/geroni/igaa057.407

Molecular Dynamics Simulation Reveals New Pocket for the Design of Novel Amino Acid Coupled Sirt1 Selective Inhibitor

Singh, M., Srivastava, M., Purushotham, N., et al. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2019.11.1239 · Cited by 3 · see citing works

Biochemical and structural studies on the mitochondrial Sirtuins 4 and 5

Pannek, M. (2018) · EPub Bayreuth (University of Bayreuth)

Shedding light on structure, function and regulation of human sirtuins: a comprehensive review

Sharma, A. B., Mahur, P., Muthukumaran, J., Singh, A. K., & Jain, M. (2022) · 3 Biotech · doi:10.1007/s13205-022-03455-1 · Cited by 58 · see citing works