The role of sirtuins in cellular homeostasis

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

Sirtuins as regulators of metabolism and healthspan

Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008

NAD+ Metabolism and the Control of Energy Homeostasis: A Balancing Act between Mitochondria and the Nucleus

Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648

Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase

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

Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins

Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409

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

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

SIRT1 and other sirtuins in metabolism

Chang, H.-C., & Guarente, L. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.12.001 · Cited by 1,157

The sirtuin SIRT6 regulates lifespan in male mice

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

The many faces of insulin-like peptide signalling in the brain

Fernandez, A. M., & Torres-Alemán, I. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3209 · Cited by 872

Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes

Pandey, R. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf660 · Cited by 783

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

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

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

SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation

Barber, M. F., Michishita-Kioi, E., Xi, Y., Tasselli, L., Kioi, M., Moqtaderi, Z., Tennen, R. I., Paredes, S., Young, N. L., Chen, K., et al. (2012) · Nature · doi:10.1038/nature11043 · Cited by 635

Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS

Chen, Y., Zhang, J., Lin, Y., Lei, Q., Guan, K., Zhao, S., & Xiong, Y. (2011) · The EMBO Reports · doi:10.1038/embor.2011.65 · Cited by 572

Mouse Sir2 Homolog SIRT6 Is a Nuclear ADP-ribosyltransferase

Liszt, G., Ford, E., Kurtev, M., & Guarente, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413296200 · Cited by 548

Identification of a Class of Small Molecule Inhibitors of the Sirtuin Family of NAD-dependent Deacetylases by Phenotypic Screening

Grozinger, C. M., Chao, E. D., Blackwell, H. E., Moazed, D., & Schreiber, S. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106779200 · Cited by 533

Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity

Mathias, R. A., Greco, T. M., Oberstein, A., Budayeva, H. G., Chakrabarti, R., Rowland, E. A., Kang, Y., Shenk, T., & Cristea, I. M. (2014) · Cell · doi:10.1016/j.cell.2014.11.046 · Cited by 430

Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation

Hirschey, M. D., & Zhao, Y. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r114.046664 · Cited by 429

SIRT1 and SIRT2: emerging targets in neurodegeneration

Dönmez, G., & Outeiro, T. F. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201302451 · Cited by 419

Structure of the histone deacetylase SIRT2.

Finnin, M. S., Donigian, J. R., & Pavletich, N. P. (2001) · Nature Structural Biology · doi:10.1038/89668 · Cited by 376

Chromatin and beyond: the multitasking roles for SIRT6

Kugel, S., & Mostoslavsky, R. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.12.002 · Cited by 374

SIRT1 and energy metabolism

Li, X. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gms108 · Cited by 360

The Dual Role of Sirtuins in Cancer

Bosch‐Presegué, L., & Vaquero, A. (2011) · Genes & Cancer · doi:10.1177/1947601911417862 · Cited by 337

Identification of ‘erasers’ for lysine crotonylated histone marks using a chemical proteomics approach

Bao, 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

Histone Deacetylase Genes in Arabidopsis Development

Hollender, C. A., & Liu, Z. (2008) · Journal of Integrative Plant Biology · doi:10.1111/j.1744-7909.2008.00704.x · Cited by 301

A SIRT7-Dependent Acetylation Switch of GABPβ1 Controls Mitochondrial Function

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

Structural basis for sirtuin function: What we know and what we don't

Sanders, B. D., Jackson, B. A., & Marmorstein, R. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.09.009 · Cited by 254

Mitochondrial Metabolism, Sirtuins, and AgingPreprint

Sack, M. N., & Finkel, T. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013102 · Cited by 242

Sirtuin/Sir2 Phylogeny, Evolutionary Considerations and Structural Conservation

Greiss, S., & Gartner, A. (2009) · Molecules and Cells · doi:10.1007/s10059-009-0169-x · Cited by 217

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

Feldman, J. L., Dittenhafer‐Reed, K. E., Kudo, N., Thelen, J. N., Ito, A., Yoshida, M., & Denu, J. M. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00150 · Cited by 191

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

Sirtuins and Disease: The Road Ahead

Carafa, V., Nebbioso, A., & Altucci, L. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00004 · Cited by 177

Histone Deacetylases

Parbin, S., Kar, S., Shilpi, A., Sengupta, D., Deb, M., Rath, S. K., & Patra, S. K. (2013) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155413506582 · Cited by 174

Histone deacetylases and their functions in plants

Ma, X., Lv, S., Zhang, C., & Yang, C. (2013) · Plant Cell Reports · doi:10.1007/s00299-013-1393-6 · Cited by 170

Sirt6 Regulates Tnf-Alpha Secretion Through Hydrolysis of Long-Chain Fatty Acyl Lysine

Jiang, H. X., Khan, S., Wang, Y., Charron, G., He, B., Sebastián, C., Du, J., Kim, R., Ge, E. J., Mostoslavsky, R., et al. (2013) · Nature · doi:10.2210/pdb3zg6/pdb · Cited by 169

Structural Basis for Sirtuin Activity and Inhibition

Yuan, H., & Marmorstein, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.372300 · Cited by 167

Mitochondrial Sirtuins and Their Relationships with Metabolic Disease and Cancer

Kumar, S., & Lombard, D. B. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6213 · Cited by 160

Sirtuin-7 Inhibits the Activity of Hypoxia-inducible Factors

Hubbi, M. E., Hu, H., Gupta, K., Gilkes, D. M., & Semenza, G. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.476903 · Cited by 154

Arabidopsis Putative Deacetylase AtSRT2 Regulates Basal Defense by Suppressing PAD4, EDS5 and SID2 Expression

Wang, C., Gao, F., Wu, J., Dai, J., Wei, C., & Li, Y. (2010) · Plant and Cell Physiology · doi:10.1093/pcp/pcq087 · Cited by 150

The chemical biology of sirtuins

Chen, B., Zang, W., Wang, J., Huang, Y., He, Y., Yan, L., Liu, J., & Zheng, W. (2015) · Chemical Society Reviews · doi:10.1039/c4cs00373j · Cited by 146

Regulation of Sirtuin Function by Posttranslational Modifications

Flick, F., & Lüscher, B. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00029 · Cited by 144

SIRT2 as a Therapeutic Target for Age-Related Disorders

de Oliveira, R. M., Sarkander, J., Kazantsev, A. G., & Outeiro, T. F. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00082 · Cited by 141

The Sirtuin-2 Inhibitor AK7 Is Neuroprotective in Models of Parkinson’s Disease but Not Amyotrophic Lateral Sclerosis and Cerebral Ischemia

Chen, X., Wales, P., Quinti, L., Zuo, F., Moniot, S., Hérisson, F., Rauf, N. A., Wang, H., Silverman, R. B., Ayata, C., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0116919 · Cited by 138

Epigenetic effects of natural polyphenols: A focus on SIRT1‐mediated mechanisms

Owona, V. B. A., Ebrahimi, A., & Schluesener, H. J. (2013) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201300195 · Cited by 126

Sirtuins: NAD+-dependent deacetylase mechanism and regulation

Sauve, A. A., & Youn, D. Y. (2012) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.10.003 · Cited by 126

Sirtuin 7 Plays a Role in Ribosome Biogenesis and Protein Synthesis

Tsai, Y.-C., Greco, T. M., & Cristea, I. M. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.031377 · Cited by 125

Potential Modulation of Sirtuins by Oxidative Stress

Santos, L., Escande, C., & Denicola, A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9831825 · Cited by 120

The conserved role of sirtuins in chromatin regulation

Vaquero, A. (2009) · The International Journal of Developmental Biology · doi:10.1387/ijdb.082675av · Cited by 119

The Arabidopsis Class II Sirtuin Is a Lysine Deacetylase and Interacts with Mitochondrial Energy Metabolism

König, A., Hartl, M., Pham, P. A., Laxa, M., Boersema, P. J., Orwat, A., Kalitventseva, I., Plöchinger, M., Braun, H., Leister, D., et al. (2014) · PLANT PHYSIOLOGY · doi:10.1104/pp.113.232496 · Cited by 116

Mitochondrial sirtuins: Emerging roles in metabolic regulations, energy homeostasis and diseases

Parihar, P., Solanki, I., Mansuri, M. L., & Parihar, M. S. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.12.004 · Cited by 114

A small molecule Inauhzin inhibits SIRT1 activity and suppresses tumour growth through activation of p53

Zhang, Q., Zeng, S. X., Zhang, Y., Zhang, Y.-W., Ding, D., Ye, Q.-Z., Meroueh, S. O., & Lu, H. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201100211 · Cited by 110

Analysis of histone acetyltransferase and deacetylase families of Vitis vinifera

Aquea, F., Timmermann, T., & Arce‐Johnson, P. (2010) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2009.12.009 · Cited by 93

Identification and characterization of histone deacetylases in tomato (Solanum lycopersicum)

Zhao, L., Lu, J., Zhang, J., Wu, P.-Y., Yang, S., & Wu, K. (2015) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00760 · Cited by 88

Genetic and chemical analyses of the action mechanisms of sirtinol in Arabidopsis

Dai, X., Hayashi, K., Nozaki, H., Cheng, Y., & Zhao, Y. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500185102 · Cited by 84

SIRT3 and SIRT4 are mitochondrial tumor suppressor proteins that connect mitochondrial metabolism and carcinogenesis

Zhu, Y., Yan, Y., Principe, D. R., Zou, X., Vassilopoulos, A., & Gius, D. R. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-15 · Cited by 77

Sirtinol Treatment Reduces Inflammation in Human Dermal Microvascular Endothelial Cells

Orecchia, A., Scarponi, C., Felice, F. D., Cesarini, E., Avitabile, S., Mai, A., Mauro, M. L., Sirri, V., Zambruno, G., Albanesi, C., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024307 · Cited by 75

Histone Acylation beyond Acetylation: Terra Incognita in Chromatin Biology.

Rousseaux, S., & Khochbin, S. (2015) · PubMed · doi:10.22074/cellj.2015.506 · Cited by 74

Integrative Chemical Biology Approaches for Identification and Characterization of “Erasers” for Fatty‐Acid‐Acylated Lysine Residues within Proteins

Liu, Z., Yang, T., Li, X., Peng, T., Hang, H. C., & Li, X. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201408763 · Cited by 63

The Rice NAD+-Dependent Histone Deacetylase OsSRT1 Targets Preferentially to Stress- and Metabolism-Related Genes and Transposable Elements

Zhong, X., Zhang, H., Zhao, Y. J., Sun, Q., Hu, Y., Peng, H., & Zhou, D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066807 · Cited by 62

Synthesis and biological characterisation of sirtuin inhibitors based on the tenovins

McCarthy, A. R., Pirrie, L., Hollick, J. J., Ronseaux, S., Campbell, J., Higgins, M., Staples, O. D., Tran, F., Slawin, A. M. Z., Laı́n, S., et al. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2012.01.001 · Cited by 62

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

Sirtuin 1 activator SRT 2104 protects Huntington's disease mice

Jiang, M., Zheng, J., Peng, Q., Hou, Z., Zhang, J., Mori, S., Ellis, J. L., Vlasuk, G. P., Fries, H. E., Suri, V., et al. (2014) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.135 · Cited by 54

The sirtuins: Markers of metabolic health

Covington, J. D., & Bajpeyi, S. (2015) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201500340 · Cited by 51

Catalysis and Mechanistic Insights into Sirtuin Activation

Dittenhafer‐Reed, K. E., Feldman, J. L., & Denu, J. M. (2010) · ChemBioChem · doi:10.1002/cbic.201000434 · Cited by 36

Sirtuin Modulators

Mahajan, S. S., Leko, V., Simon, J. A., & Bedalov, A. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_11 · Cited by 32

Spontaneous Electrical Activity of Cultured Interstitial Cells of Cajal from Mouse Urinary Bladder

Kim, S., Jeong, H., Jang, S., Wu, M.-J., Park, J. K., Jiao, H.-Y., Jun, J. Y., & Park, J.-S. (2013) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2013.17.6.531 · Cited by 28

SIRT7 an emerging sirtuin: deciphering newer roles.

Kim, W., & Kim, J. (2013) · PubMed · Cited by 27

Identification of benzofuran-3-yl(phenyl)methanones as novel SIRT1 inhibitors: Binding mode, inhibitory mechanism and biological action

Wu, J., Li, Y., Chen, K., Jiang, H., Xu, M., & Liu, D. (2012) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2012.12.026 · Cited by 21

Characterization and differential expression analysis of complete coding sequences of Vitis vinifera L. sirtuin genes

Cucurachi, M., Busconi, M., Morreale, G., Zanetti, A., Bavaresco, L., & Fogher, C. (2012) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2012.02.017 · Cited by 20

Mitochondria 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

SIRT1 Activation by Natural Phytochemicals: An Overview

Iside, C., Scafuro, M., Nebbioso, A., & Altucci, L. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01225 · Cited by 328

Sirtuins in gamete biology and reproductive physiology: emerging roles and therapeutic potential in female and male infertility

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

A Critical Review of the Evidence That Metformin Is a Putative Anti-Aging Drug That Enhances Healthspan and Extends Lifespan

Mohammed, I., Hollenberg, M. D., Ding, H., & Triggle, C. R. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.718942 · Cited by 278

Sirtuins and Their Roles in Brain Aging and Neurodegenerative Disorders

Jęśko, H. M., Wencel, P. L., Strosznajder, R. P., & Strosznajder, J. B. (2016) · Neurochemical Research · doi:10.1007/s11064-016-2110-y · Cited by 264

The Role of Sirtuins in the Control of Metabolic Homeostasis

Yu, J., & Auwerx, J. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.04952.x · Cited by 145

Characterization of Nuclear Sirtuins: Molecular Mechanisms and Physiological Relevance

Toiber, D., Sebastián, C., & Mostoslavsky, R. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_9 · Cited by 57

Function of SIRT1 in physiology

Kong, X., Wang, R., Liu, X., Zhu, L., Shao, D., Chang, Y., & Fang, F. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909070013 · Cited by 28

Sirtuin Functions in Health and Disease

Yamamoto, H., Schoonjans, K., & Auwerx, J. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0079 · Cited by 480

Pharmacological manipulations of CNS sirtuins: Potential effects on metabolic homeostasis

Ramadori, G., & Coppari, R. (2010) · Pharmacological Research · doi:10.1016/j.phrs.2010.02.002 · Cited by 8