Sirtuin regulation in aging and injury

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 · see citing works

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 · see citing works

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 · 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

hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase

Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,653 · see citing works

The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms

Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253 · see citing works

Negative Control of p53 by Sir2α Promotes Cell Survival under Stress

Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081 · see citing works

Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ

Picard, F., Kurtev, M. V., Chung, N., Topark‐Ngarm, A., Senawong, T., de Oliveira, R. M., Leid, M. E., McBurney, M. W., & Guarente, L. (2004) · Nature · doi:10.1038/nature02583 · Cited by 1,943 · 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

Sirtuin activators mimic caloric restriction and delay ageing in metazoans

Wood, J. G., Rogina, B., Lavu, S., Howitz, K., Helfand, S. L., Tatar, M., & Sinclair, D. (2004) · Nature · doi:10.1038/nature02789 · Cited by 1,868 · see citing works

Requirement of NAD and <i>SIR2</i> for Life-Span Extension by Calorie Restriction in <i>Saccharomyces cerevisiae</i>

Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775 · see citing works

SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation

Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687 · see citing works

PGC-1α, SIRT1 and AMPK, an energy sensing network that controls energy expenditure

Cantó, C., & Auwerx, J. (2009) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e328328d0a4 · Cited by 1,624 · see citing works

The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase

North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., & Verdin, E. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00038-8 · Cited by 1,542 · see citing works

Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging

Gomes, A. P., Price, N. L., Ling, A. J. Y., Moslehi, J. J., Montgomery, M. K., Rajman, L., White, J. P., Teodoro, J. S., Wrann, C. D., Hubbard, B. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.11.037 · Cited by 1,482 · see citing works

The Sir2 Family of Protein Deacetylases

Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,480 · see citing works

Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis

Gregoretti, I., Lee, Y.-M., & Goodson, H. V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.006 · Cited by 1,456 · see citing works

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 · see citing works

The NAD+-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control

Nakahata, Y., Kaluzova, M., Grimaldi, B., Sahar, S., Hirayama, J., Chen, D., Guarente, L. P., & Sassone-Corsi, P. (2008) · Cell · doi:10.1016/j.cell.2008.07.002 · Cited by 1,427 · see citing works

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 · see citing works

SIRT1 regulates circadian clock gene expression through PER2 deacetylation

Asher, G., Gatfield, D., Stratmann, M., Reinke, H., Dibner, C., Kreppel, F., Mostoslavsky, R., Alt, F. W., & Schibler, U. (2008) · Cell · doi:10.1016/j.cell.2008.06.050 · Cited by 1,376 · see citing works

Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins

Michishita, E., Park, J. Y., Burneskis, J. M., Barrett, J. C., & Horikawa, I. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-01-0033 · Cited by 1,364 · see citing works

Mammalian SIRT1 Represses Forkhead Transcription Factors

Motta, M. C., Divecha, N., Lemieux, M. E., Kamel, C., Chen, D., Gu, W. J., Bultsma, Y., McBurney, M. W., & Guarente, L. (2004) · Cell · doi:10.1016/s0092-8674(04)00126-6 · Cited by 1,351 · see citing works

miR-34a repression of SIRT1 regulates apoptosis

Yamakuchi, M., Ferlito, M., & Lowenstein, C. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801613105 · Cited by 1,344 · see citing works

Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation

Qiu, X., Brown, K., Hirschey, M. D., Verdin, E., & Chen, D. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.015 · Cited by 1,310 · see citing works

Regulation of Yeast Replicative Life Span by TOR and Sch9 in Response to Nutrients

Kaeberlein, M., Powers, R. W., Steffen, K. K., Westman, E. A., Hu, D., Dang, N., Kerr, E. O., Kirkland, K. T., Fields, S., & Kennedy, B. K. (2005) · Science · doi:10.1126/science.1115535 · Cited by 1,293 · 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

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 · see citing works

Acetylation: a regulatory modification to rival phosphorylation?

Kouzarides, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.6.1176 · Cited by 1,155 · see citing works

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 1,138 · see citing works

p53-Mediated Activation of miRNA34 Candidate Tumor-Suppressor Genes

Bommer, G. T., Gerin, I., Feng, Y., Kaczorowski, A. J., Kuick, R. D., Love, R. E., Zhai, Y., Giordano, T. J., Qin, Z. S., Moore, B. B., et al. (2007) · Current Biology · doi:10.1016/j.cub.2007.06.068 · Cited by 1,122 · see citing works

Hepatocyte-Specific Deletion of SIRT1 Alters Fatty Acid Metabolism and Results in Hepatic Steatosis and Inflammation

Purushotham, A., Schug, T. T., Xu, Q., Surapureddi, S., Guo, X., & Li, X. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.02.006 · Cited by 1,112 · 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

Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

Cheng, H.-L., Mostoslavsky, R., Saito, S., Manis, J. P., Gu, Y., Patel, P., Bronson, R., Appella, E., Alt, F. W., & Chua, K. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934713100 · Cited by 1,095 · see citing works

SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis

Kim, D., Nguyen, M. D., Dobbin, M. M., Fischer, A., Sananbenesi, F., Rodgers, J. T., Delalle, I., Baur, J. A., Sui, G., Armour, S. M., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601758 · Cited by 1,074 · see citing works

Increased Nuclear NAD Biosynthesis and SIRT1 Activation Prevent Axonal Degeneration

Araki, T., Sasaki, Y., & Milbrandt, J. (2004) · Science · doi:10.1126/science.1098014 · Cited by 1,060 · see citing works

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 · see citing works

Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration

Lin, S.-J., Kaeberlein, M., Andalis, A. A., Sturtz, L. A., Defossez, P.-A., Culotta, V. C., Fink, G. R., & Guarente, L. (2002) · Nature · doi:10.1038/nature00829 · Cited by 1,057 · see citing works

SIRT1 Functionally Interacts with the Metabolic Regulator and Transcriptional Coactivator PGC-1α

Nemoto, S., Fergusson, M. M., & Finkel, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501485200 · Cited by 1,047 · see citing works

HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention

Yang, X.-J., & Seto, E. (2007) · Oncogene · doi:10.1038/sj.onc.1210599 · Cited by 1,040 · see citing works

Regulation of the Caenorhabditis elegans longevity protein DAF-16 by insulin/IGF-1 and germline signaling

Lin, K., Hsin, H., Libina, N., & Kenyon, C. J. (2001) · Nature Genetics · doi:10.1038/88850 · Cited by 1,027 · see citing works

Inhibition of Silencing and Accelerated Aging by Nicotinamide, a Putative Negative Regulator of Yeast Sir2 and Human SIRT1

Bitterman, K. J., Anderson, R. M., Cohen, H. Y., Latorre-Esteves, M., & Sinclair, D. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205670200 · Cited by 1,002 · 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 1,001 · see citing works

The Histone Deacetylase Sirt6 Regulates Glucose Homeostasis via Hif1α

Zhong, L., D'Urso, A., Toiber, D., Sebastian, C., Henry, R. E., Vadysirisack, D. D., Guimaraes, A., Marinelli, B., Wikstrom, J. D., Nir, T., et al. (2010) · Cell · doi:10.1016/j.cell.2009.12.041 · Cited by 1,001 · 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

The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases

Landry, J., Sutton, A., Tafrov, S. T., Heller, R. C., Stebbins, J., Pillus, L., & Sternglanz, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.110148297 · Cited by 970 · see citing works

The genetics of caloric restriction in Caenorhabditis elegans

Lakowski, B., & Hekimi, S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.22.13091 · Cited by 967 · 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

Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin.

Vaquero, A., Scher, M., Lee, D., Erdjument-Bromage, H., Tempst, P., & Reinberg, D. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.031 · Cited by 916 · see citing works

SIRT1 Promotes Endothelium-Dependent Vascular Relaxation by Activating Endothelial Nitric Oxide Synthase

Mattagajasingh, I., Kim, C.-S., Naqvi, A., Yamamori, T., Hoffman, T. A., Jung, S.-B., DeRicco, J., Kasuno, K., & Irani, K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0704329104 · Cited by 881 · see citing works

SIRT6 Promotes DNA Repair Under Stress by Activating PARP1

Mao, Z., Hine, C., Tian, X., Van Meter, M., Au, M., Vaidya, A., Seluanov, A., & Gorbunova, V. (2011) · Science · doi:10.1126/science.1202723 · Cited by 867 · see citing works

Human SIR2 deacetylates p53 and antagonizes PML/p53‐induced cellular senescence

Langley, E., Pearson, M., Faretta, M., Bauer, U., Frye, R. A., Minucci, S., Pelicci, P. G., & Kouzarides, T. (2002) · The EMBO Journal · doi:10.1093/emboj/21.10.2383 · Cited by 859 · see citing works

Lysine glutarylation is a protein posttranslational modification regulated by SIRT5

Tan, M., Peng, C., Anderson, K. A., Chhoy, P., Xie, Z., Dai, L., Park, J., Chen, Y., Huang, H., Zhang, Y., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.014 · Cited by 844 · see citing works

Characterization of Five Human cDNAs with Homology to the Yeast SIR2 Gene: Sir2-like Proteins (Sirtuins) Metabolize NAD and May Have Protein ADP-Ribosyltransferase Activity

Frye, R. A. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0897 · Cited by 809 · see citing works

Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

Hallows, W. C., Lee, S., & Denu, J. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604392103 · Cited by 792 · see citing works

SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle

Nakagawa, T., Lomb, D. J., Haigis, M. C., & Guarente, L. (2009) · Cell · doi:10.1016/j.cell.2009.02.026 · Cited by 787 · see citing works

Sirtuin 1 Modulates Cellular Responses to Hypoxia by Deacetylating Hypoxia-Inducible Factor 1α

Lim, J.-H., Lee, Y.-M., Chun, Y.-S., Chen, J., Kim, J.-E., & Park, J.-W. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.05.023 · Cited by 758 · see citing works

SIRT1 Protects against Microglia-dependent Amyloid-β Toxicity through Inhibiting NF-κB Signaling

Chen, J., Zhou, Y., Mueller-Steiner, S., Chen, L.-F., Kwon, H., Yi, S., Mucke, L., & Gan, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509329200 · Cited by 740 · see citing works

Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae

Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., & Sinclair, D. A. (2003) · Nature · doi:10.1038/nature01578 · Cited by 736 · 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 734 · 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

A phylogenetically conserved NAD ⁺ -dependent protein deacetylase activity in the Sir2 protein family

Smith, J. S., Brachmann, C. B., Celic, I., Kenna, M. A., Muhammad, S., Starai, V. J., Avalos, J. L., Escalante-Semerena, J. C., Grubmeyer, C., Wolberger, C., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.12.6658 · 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

SIRT3, a Mitochondrial Sirtuin Deacetylase, Regulates Mitochondrial Function and Thermogenesis in Brown Adipocytes

Shi, T., Wang, F., Stieren, E., & Tong, Q. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414670200 · Cited by 712 · see citing works

SIRT5 Regulates the Mitochondrial Lysine Succinylome and Metabolic Networks

Rardin, M. J., He, W., Nishida, Y., Newman, J. C., Carrico, C., Danielson, S. R., Guo, A., Gut, P., Sahu, A. K., Li, B., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.11.013 · Cited by 711 · see citing works

Four Genes Responsible for a Position Effect on Expression From HML and HMR in Saccharomyces cerevisiae

Rine, J., & Herskowitz, I. (1987) · Genetics · doi:10.1093/genetics/116.1.9 · Cited by 711 · see citing works

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

Schwer, B., Bunkenborg, J., Verdin, R. O., Andersen, J. S., & Verdin, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603968103 · Cited by 705 · see citing works

CBP/p300-mediated acetylation of histone H3 on lysine 56

Das, C., Lucia, M. S., Hansen, K. C., & Tyler, J. K. (2009) · Nature · doi:10.1038/nature07861 · Cited by 698 · 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

SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction

Wang, F., Nguyen, M., Qin, F. X.-F., & Tong, Q. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00304.x · Cited by 652 · see citing works

Sirt7 Increases Stress Resistance of Cardiomyocytes and Prevents Apoptosis and Inflammatory Cardiomyopathy in Mice

Vakhrusheva, O., Smolka, C., Gajawada, P., Sawa Kostin, D., Boettger, T., Kubin, T., Braun, T. W., & Bober, E. (2008) · Circulation Research · doi:10.1161/circresaha.107.164558 · Cited by 639 · see citing works

SIRT1 Deacetylates and Positively Regulates the Nuclear Receptor LXR

Li, X., Zhang, S., Blander, G., Tse, J. G., Krieger, M., & Guarente, L. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.032 · Cited by 631 · see citing works

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

Ford, E., Voit, R., Liszt, G., Magin, C., Grummt, I., & Guarente, L. (2006) · Genes &amp; Development · doi:10.1101/gad.1399706 · Cited by 629 · see citing works

Increased dosage of mammalian Sir2 in pancreatic β cells enhances glucose-stimulated insulin secretion in mice

Moynihan, K. A., Grimm, A. A., Plueger, M. M., Bernal‐Mizrachi, E., Ford, E. L., CRAS-MÉNEUR, C. M. H., Permutt, M. A., & Imai, S. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.07.001 · Cited by 628 · see citing works

Ischemic Brain Injury is Mediated by the Activation of Poly(ADP-Ribose)Polymerase

Endres, M., Wang, Z., Namura, S., Waeber, C., & Moskowitz, M. A. (1997) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199711000-00002 · Cited by 622 · see citing works

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 621 · see citing works

Wallerian degeneration of injured axons and synapses is delayed by a Ube4b/Nmnat chimeric gene

Mack, T. G. A., Reiner, M., Beirowski, B., Mi, W., Emanuelli, M., Wagner, D., Thomson, D., Gillingwater, T., Court, F., Conforti, L., et al. (2001) · Nature Neuroscience · doi:10.1038/nn770 · Cited by 611 · see citing works

The Mammalian SIR2α Protein Has a Role in Embryogenesis and Gametogenesis

McBurney, M. W., Yang, X., Jardine, K., Hixon, M., Boekelheide, K., Webb, J. R., Lansdorp, P. M., & Lemieux, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.38-54.2003 · Cited by 611 · see citing works

The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability.Preprint

Brachmann, C. B., Sherman, J. M., Devine, S. E., Cameron, E. E., Pillus, L., & Boeke, J. D. (1995) · Genes & Development · doi:10.1101/gad.9.23.2888 · Cited by 605 · see citing works

The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide–dependent deacetylase

Schwer, B., North, B. J., Frye, R. A., Ott, M., & Verdin, E. M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200205057 · Cited by 599 · see citing works

The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth.

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The mTORC1 Pathway Stimulates Glutamine Metabolism and Cell Proliferation by Repressing SIRT4

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Sir2 Regulates Skeletal Muscle Differentiation as a Potential Sensor of the Redox State

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Downregulation of MiR-199a Derepresses Hypoxia-Inducible Factor-1α and Sirtuin 1 and Recapitulates Hypoxia Preconditioning in Cardiac Myocytes

Rane, S., He, M., Sayed, D. H., Vashistha, H., Malhotra, A., Sadoshima, J., Vatner, D. E., Vatner, S. F., & Abdellatif, M. (2009) · Circulation Research · doi:10.1161/circresaha.108.193102 · Cited by 578 · see citing works

Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine

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Silent Information Regulator 1 Protects the Heart From Ischemia/Reperfusion

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Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1

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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 · see citing works

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

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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

FOXO4 Is Acetylated upon Peroxide Stress and Deacetylated by the Longevity Protein hSir2

van der Horst, A., Tertoolen, L. G. J., Smits, L. M. M., Frye, R. A., Medema, R. H., & Burgering, B. M. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401138200 · Cited by 541 · see citing works

Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5

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SIRT1, an antiinflammatory and antiaging protein, is decreased in lungs of patients with chronic obstructive pulmonary disease

Rajendrasozhan, S., Yang, S.-R., Kinnula, V. L., & Rahman, I. (2008) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200708-1269oc · Cited by 520 · see citing works

Untitled work

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Role for Human SIRT2 NAD-Dependent Deacetylase Activity in Control of Mitotic Exit in the Cell Cycle

Dryden, S. C., Nahhas, F. A., Nowak, J. E., Goustin, A. S., & Tainsky, M. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.9.3173-3185.2003 · Cited by 500 · see citing works

SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production

Shimazu, T., Hirschey, M. D., Hua, L., Dittenhafer-Reed, K. E., Schwer, B., Lombard, D. B., Li, Y., Bunkenborg, J., Alt, F. W., Denu, J. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.003 · Cited by 484 · see citing works

SirT3 is a nuclear NAD + -dependent histone deacetylase that translocates to the mitochondria upon cellular stressPreprint

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Regulation of Hypoxia-Inducible Factor 2α Signaling by the Stress-Responsive Deacetylase Sirtuin 1

Dioum, E. M., Chen, R., Alexander, M. S., Zhang, Q., Hogg, R. T., Gerard, R. D., & Garcia, J. A. (2009) · Science · doi:10.1126/science.1169956 · Cited by 470 · see citing works

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

Van Meter, M., Kashyap, M., Rezazadeh, S., Geneva, A. J., Morello, T. D., Seluanov, A., & Gorbunova, V. (2014) · Nature Communications · doi:10.1038/ncomms6011 · Cited by 455 · see citing works

Honokiol blocks and reverses cardiac hypertrophy in mice by activating mitochondrial Sirt3

Pillai, V. B., Samant, S. A., Sundaresan, N. R., Raghuraman, H., Kim, G. H., Bonner, M. Y., Arbiser, J. L., Walker, D. I., Jones, D. P., Gius, D. R., et al. (2015) · Nature Communications · doi:10.1038/ncomms7656 · Cited by 448 · see citing works

SIRT3 Deacetylates and Activates OPA1 To Regulate Mitochondrial Dynamics during Stress

Samant, S. A., Zhang, H. J., Hong, Z., Pillai, V. B., Sundaresan, N. R., Wolfgeher, D., Archer, S. L., Chan, D. C., & Gupta, M. P. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01483-13 · Cited by 446 · see citing works

SIRT3 Protein Deacetylates Isocitrate Dehydrogenase 2 (IDH2) and Regulates Mitochondrial Redox Status

Yu, W., Dittenhafer‐Reed, K. E., & Denu, J. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.355206 · Cited by 445 · 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

SIRT3 deacetylates FOXO3 to protect mitochondria against oxidative damage.

Tseng, A. H., Shieh, S., & Wang, D. (2013) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2013.05.002 · Cited by 445 · see citing works

Sir2-Independent Life Span Extension by Calorie Restriction in Yeast

Kaeberlein, M., Kirkland, K. T., Fields, S., & Kennedy, B. K. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020296 · Cited by 441 · see citing works

SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production

Bell, E. L., Emerling, B. M., Ricoult, S. J. H., & Guarente, L. (2011) · Oncogene · doi:10.1038/onc.2011.37 · Cited by 440 · see citing works

SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation.

Vaquero, A., Scher, M., Erdjument-Bromage, H., Tempst, P., Serrano, L., & Reinberg, D. (2007) · Nature · doi:10.1038/nature06268 · Cited by 439 · see citing works

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

Cantó, C., & Auwerx, J. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.003905 · Cited by 433 · see citing works

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 · see citing works

Exogenous NAD Blocks Cardiac Hypertrophic Response via Activation of the SIRT3-LKB1-AMP-activated Kinase Pathway

Pillai, V. B., Sundaresan, N. R., Kim, G. H., Gupta, M., Rajamohan, S. B., Pillai, J. B., Samant, S. A., Ravindra, P. A., Isbatan, A., & Gupta, M. P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.077271 · Cited by 420 · see citing works

Acetylation Regulates Gluconeogenesis by Promoting PEPCK1 Degradation via Recruiting the UBR5 Ubiquitin Ligase

Jiang, W., Wang, S., Xiao, M., Lin, Y., Zhou, L., Lei, Q., Xiong, Y., Guan, K., & Zhao, S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.028 · Cited by 415 · see citing works

Myosin isoenzyme changes in several models of rat cardiac hypertrophy.

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Nampt: linking NAD biology, metabolism and cancer

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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

C. elegans SIR-2.1 Interacts with 14-3-3 Proteins to Activate DAF-16 and Extend Life Span

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Poly(ADP-ribose) Polymerase-1-dependent Cardiac Myocyte Cell Death during Heart Failure Is Mediated by NAD+ Depletion and Reduced Sir2α Deacetylase Activity

Pillai, J. B., Isbatan, A., Imai, S., & Gupta, M. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506162200 · Cited by 391 · see citing works

An Enzymatic Activity in the Yeast Sir2 Protein that Is Essential for Gene Silencing

Tanny, J. C., Dowd, G. J., Huang, J., Hilz, H., & Moazed, D. (1999) · Cell · doi:10.1016/s0092-8674(00)81671-2 · Cited by 391 · see citing works

Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction

Hallows, W. C., Yu, W., Smith, B. C., Devires, M. K., Ellinger, J. J., Someya, S., Shortreed, M. R., Prolla, T., Markley, J. L., Smith, L. M., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.01.002 · Cited by 389 · see citing works

Sir2 Blocks Extreme Life-Span Extension

Fabrizio, P., Gattazzo, C., Battistella, L., Wei, M., Cheng, C., McGrew, K., & Longo, V. D. (2005) · Cell · doi:10.1016/j.cell.2005.08.042 · Cited by 388 · see citing works

Acetylation-dependent regulation of endothelial Notch signalling by the SIRT1 deacetylase

Guarani, V., Deflorian, G., Franco, C. A., Krüger, M., Phng, L., Bentley, K., Toussaint, L., Dequiedt, F., Mostoslavsky, R., Schmidt, M. H. H., et al. (2011) · Nature · doi:10.1038/nature09917 · Cited by 385 · 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

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 · see citing works

Resveratrol pretreatment protects rat brain from cerebral ischemic damage via a sirtuin 1–uncoupling protein 2 pathway

Della‐Morte, D., Dave, K. R., DeFazio, R. A., Bao, Y. C., Raval, A. P., & Pérez‐Pinzón, M. A. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.01.017 · Cited by 375 · see citing works

Oxidative stress, neurodegeneration, and the balance of protein degradation and protein synthesis

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Chromatin and beyond: the multitasking roles for SIRT6

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Succinate Dehydrogenase Is a Direct Target of Sirtuin 3 Deacetylase Activity

Finley, L. W. S., Haas, W., Desquiret‐Dumas, V., Wallace, D. C., Procaccio, V., Gygi, S. P., & Haigis, M. C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023295 · Cited by 364 · see citing works

SIRT1 promotes DNA repair activity and deacetylation of Ku70

Jeong, J., Juhn, K., Lee, H., Kim, S. H., Min, B.-H., Lee, K., Cho, M., Park, G. H., & Lee, K.-H. (2007) · Experimental & Molecular Medicine · doi:10.1038/emm.2007.2 · Cited by 356 · see citing works

Resveratrol Improves Oxidative Stress and Protects Against Diabetic Nephropathy Through Normalization of Mn-SOD Dysfunction in AMPK/SIRT1-Independent Pathway

Kitada, M., Kume, S., Imaizumi, N., & Koya, D. (2011) · Diabetes · doi:10.2337/db10-0386 · Cited by 345 · see citing works

FXR Acetylation Is Normally Dynamically Regulated by p300 and SIRT1 but Constitutively Elevated in Metabolic Disease States

Kemper, J. K., Xiao, Z., Ponugoti, B., Miao, J., Fang, S., Kanamaluru, D., Tsang, S., Wu, S.-Y., Chiang, C.-M., & Veenstra, T. D. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.09.009 · Cited by 332 · see citing works

SirT1 inhibition reduces IGF-I/IRS-2/Ras/ERK1/2 signaling and protects neurons

Li, Y., Xu, W., McBurney, M. W., & Longo, V. D. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.05.004 · Cited by 331 · see citing works

SIRT1 Regulates HIV Transcription via Tat Deacetylation

Pagans, S., Pedal, A., North, B. J., Kaehlcke, K., Marshall, B. L., Dorr, A., Hetzer‐Egger, C., Henklein, P., Frye, R. A., McBurney, M. W., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030041 · Cited by 330 · see citing works

Crystal Structure of a SIR2 Homolog–NAD Complex

Min, J., Landry, J. W., Sternglanz, R., & Xu, R.-M. (2001) · Cell · doi:10.1016/s0092-8674(01)00317-8 · Cited by 326 · see citing works

Myeloid Deletion of SIRT1 Induces Inflammatory Signaling in Response to Environmental Stress

Schug, T. T., Xu, Q., Gao, H., Peres-da-Silva, A., Draper, D. W., Fessler, M. B., Purushotham, A., & Li, X. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00657-10 · Cited by 324 · 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

Induction of autophagy contributes to the neuroprotection of nicotinamide phosphoribosyltransferase in cerebral ischemia

Wang, P., Guan, Y., Du, H., Zhai, Q., Su, D., & Miao, C. (2012) · Autophagy · doi:10.4161/auto.8.1.18274 · Cited by 319 · see citing works

Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress#

Wang, Y., Zhou, L., Zhao, Y., Wang, S., Chen, L.-L., Liu, L., Ling, Z., Hu, F., Sun, Y.-P., Zhang, J., et al. (2014) · The EMBO Journal · doi:10.1002/embj.201387224 · Cited by 318 · 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

Resveratrol prevents renal lipotoxicity and inhibits mesangial cell glucotoxicity in a manner dependent on the AMPK–SIRT1–PGC1α axis in db/db mice

Kim, M. Y., Lim, J. H., Youn, H. H., Hong, Y. A., Yang, K. S., Park, H., Chung, S., Koh, S. H., Shin, S. J., Choi, B. S., et al. (2012) · Diabetologia · doi:10.1007/s00125-012-2747-2 · Cited by 313 · see citing works

Hepatic Sirt1 deficiency in mice impairs mTorc2/Akt signaling and results in hyperglycemia, oxidative damage, and insulin resistance

Wang, R.-H., Kim, H., Xiao, C., Xu, X., Gavrilova, O., & Deng, C. (2011) · Journal of Clinical Investigation · doi:10.1172/jci46243 · Cited by 311 · see citing works

MSN2 and MSN4 Link Calorie Restriction and TOR to Sirtuin-Mediated Lifespan Extension in Saccharomyces cerevisiae

Medvedik, O., Lamming, D. W., Kim, K. D., & Sinclair, D. A. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050261 · Cited by 308 · 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

Silent Information Regulator 2α, a Longevity Factor and Class III Histone Deacetylase, Is an Essential Endogenous Apoptosis Inhibitor in Cardiac Myocytes

Alcendor, R. R., Kirshenbaum, L. A., Imai, S., Vatner, S. F., & Sadoshima, J. (2004) · Circulation Research · doi:10.1161/01.res.0000147557.75257.ff · Cited by 302 · see citing works

The Deacetylase Sirt6 Activates the Acetyltransferase GCN5 and Suppresses Hepatic Gluconeogenesis

Dominy, J. E., Lee, Y., Jedrychowski, M. P., Chim, H., Jurczak, M. J., Camporez, J. P., Ruan, H., Feldman, J., Pierce, K. A., Mostoslavsky, R., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.030 · Cited by 296 · see citing works

NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs

Vaquero, A., Sternglanz, R., & Reinberg, D. (2007) · Oncogene · doi:10.1038/sj.onc.1210617 · Cited by 291 · see citing works

Sirtuins at a glance

Nakagawa, T., & Guarente, L. (2011) · Journal of Cell Science · doi:10.1242/jcs.081067 · Cited by 289 · see citing works

The Interaction of Alba, a Conserved Archaeal Chromatin Protein, with Sir2 and Its Regulation by Acetylation

Bell, S. D., Botting, C. H., Wardleworth, B. N., Jackson, S. P., & White, M. F. (2002) · Science · doi:10.1126/science.1070506 · Cited by 289 · see citing works

SIRT2 Suppresses Adipocyte Differentiation by Deacetylating FOXO1 and Enhancing FOXO1's Repressive Interaction with PPARγ

Wang, F., & Tong, Q. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-06-0647 · Cited by 289 · see citing works

Nicotinamide phosphoribosyltransferase protects against ischemic stroke through SIRT1‐dependent adenosine monophosphate–activated kinase pathway

Wang, P., Xu, T., Guan, Y., Tian, W., Viollet, B., Rui, Y., Zhai, Q., Su, D., & Miao, C. (2011) · Annals of Neurology · doi:10.1002/ana.22236 · Cited by 288 · see citing works

SIRT7 represses Myc activity to suppress ER stress and prevent fatty liver disease

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 · see citing works

Nicotinamide Phosphoribosyltransferase Regulates Cell Survival Through NAD + Synthesis in Cardiac Myocytes

Hsu, C., Oka, S., Shao, D., Hariharan, N., & Sadoshima, J. (2009) · Circulation Research · doi:10.1161/circresaha.109.203703 · Cited by 284 · see citing works

Sirt3 regulates metabolic flexibility of skeletal muscle through reversible enzymatic deacetylation

Jing, E., O’Neill, B. T., Rardin, M. J., Kleinridders, A., Ilkeyeva, O. R., Ussar, S., Bain, J. R., Lee, K. Y., Verdin, E. M., Newgard, C. B., et al. (2013) · Diabetes · doi:10.2337/db12-1650 · Cited by 283 · see citing works

MAR1—A REGULATOR OF THE HM a AND HMα LOCI IN SACCHAROMYCES CEREVISIAE

Klar, A. J. S., Fogel, S., & Macleod, K. (1979) · Genetics · doi:10.1093/genetics/93.1.37 · Cited by 278 · see citing works

SIRT5 desuccinylates and activates SOD1 to eliminate ROS

Lin, Z., Xu, H.-B., Wang, J., Lin, Q., Ruan, Z., Liu, F., Wang, J., Huang, H., & Chen, X. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.10.033 · Cited by 276 · see citing works

Longevity Regulation by Drosophila Rpd3 Deacetylase and Caloric Restriction

Rogina, B., Helfand, S. L., & Frankel, S. A. (2002) · Science · doi:10.1126/science.1078986 · Cited by 276 · see citing works

JNK1 Phosphorylates SIRT1 and Promotes Its Enzymatic Activity

Nasrin, N., Kaushik, V. K., Fortier, E., Wall, D., Pearson, K. J., de Cabo, R., & Bordone, L. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008414 · Cited by 271 · see citing works

A Role for SIRT2-Dependent Histone H3K18 Deacetylation in Bacterial Infection

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 · see citing works

Regulation of MEF2 by Histone Deacetylase 4- and SIRT1 Deacetylase-Mediated Lysine Modifications

Zhao, X., Sternsdorf, T., Bolger, T. A., Evans, R. M., & Yao, T.-P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.19.8456-8464.2005 · Cited by 264 · see citing works

Assembly of the SIR Complex and Its Regulation by O-Acetyl-ADP-Ribose, a Product of NAD-Dependent Histone Deacetylation

Liou, G., Tanny, J. C., Kruger, R. G., Walz, T., & Moazed, D. (2005) · Cell · doi:10.1016/j.cell.2005.03.035 · Cited by 260 · see citing works

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 258 · see citing works

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 248 · see citing works

SIRT2 induces the checkpoint kinase BubR1 to increase lifespan

North, B. J., Rosenberg, M. A., Jeganathan, K. B., Hafner, A. V., Michán, S., Dai, J., Baker, D. J., Cen, Y., Wu, L. E., Sauve, A. A., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201386907 · Cited by 243 · see citing works

Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product

Tanny, J. C., & Moazed, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.2.415 · Cited by 242 · see citing works

Dual control of mitochondrial biogenesis by sirtuin 1 and sirtuin 3

Brenmoehl, J., & Hoeflich, A. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.04.002 · Cited by 240 · see citing works

Resveratrol Mimics Ischemic Preconditioning in the Brain

Raval, A. P., Dave, K. R., & Pérez‐Pinzón, M. A. (2006) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600262 · Cited by 239 · see citing works

Progressive loss of SIRT1 with cell cycle withdrawal

Sasaki, T., Maier, B., Bartke, A., & Scrable, H. J. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00235.x · Cited by 235 · see citing works

Hormonal Control of Androgen Receptor Function through SIRT1

Fu, M., Liu, M., Sauve, A. A., Jiao, X., Zhang, X., Wu, X., Powell, M. J., Yang, T., Gu, W. J., Avantaggiati, M. L., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00289-06 · Cited by 234 · see citing works

Silent Information Regulator 1 Protects the Brain Against Cerebral Ischemic Damage

Hernández‐Jiménez, M., Hurtado, O., Cuartero, M. I., Ballesteros, I., Moraga, A., Pradillo, J. M., McBurney, M. W., Lizasoaín, I., & Moro, M. Á. (2013) · Stroke · doi:10.1161/strokeaha.113.001715 · Cited by 234 · see citing works

HST2 Mediates SIR2 -Independent Life-Span Extension by Calorie Restriction

Lamming, D. W., Latorre‐Esteves, M., Medvedik, O., Wong, S. N., Tsang, F. A., Wang, C., Lin, S.-J., & Sinclair, D. A. (2005) · Science · doi:10.1126/science.1113611 · Cited by 227 · see citing works

Repression of RNA Polymerase I upon Stress Is Caused by Inhibition of RNA-Dependent Deacetylation of PAF53 by SIRT7

Chen, S., Seiler, J., Santiago-Reichelt, M., Felbel, K., Grummt, I., & Voit, R. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.10.010 · Cited by 224 · see citing works

SIRT3‐dependent GOT2 acetylation status affects the malate–aspartate NADH shuttle activity and pancreatic tumor growth

Yang, H., Zhou, L., Shi, Q., Zhao, Y., Lin, H., Zhang, M., Zhao, S., Yang, Y. A., Ling, Z., Guan, K., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201591041 · Cited by 224 · see citing works

Kidney-specific Overexpression of Sirt1 Protects against Acute Kidney Injury by Retaining Peroxisome Function

Hasegawa, K., Wakino, S., Yoshioka, K., Tatematsu, S., Hara, Y., Minakuchi, H., Sueyasu, K., Washida, N., Tokuyama, H., Tzukerman, M., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.067728 · Cited by 223 · see citing works

SIRT1 Regulates UV-Induced DNA Repair through Deacetylating XPA

Fan, W., & Luo, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.006 · Cited by 223 · see citing works

SIRT1 Deacetylates the DNA Methyltransferase 1 (DNMT1) Protein and Alters Its Activities

Peng, L., Yuan, Z., Ling, H., Fukasawa, K., Robertson, K. D., Olashaw, N., Koomen, J. M., Chen, J., Lane, W. S., & Seto, E. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.06147-11 · Cited by 222 · see citing works

SIRT7 Controls Hepatic Lipid Metabolism by Regulating the Ubiquitin-Proteasome Pathway

Yoshizawa, T., Karim, M. F., Sato, Y., Senokuchi, T., Miyata, K., Fukuda, T., Go, C., Tasaki, M., Uchimura, K., Kadomatsu, T., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.006 · Cited by 217 · see citing works

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

Porter, G. A., Jr., Urciuoli, W. R., Brookes, P. S., & Nadtochiy, S. M. (2014) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00027.2014 · Cited by 212 · see citing works

Protection by tetrahydroxystilbene glucoside against cerebral ischemia: involvement of JNK, SIRT1, and NF-κB pathways and inhibition of intracellular ROS/RNS generation

Wang, T., Gu, J. F., Wu, P., Wang, F., Xiong, Z., Yang, Y., Wu, W., Dong, L.-D., & Chen, J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.02.027 · Cited by 208 · see citing works

Resveratrol regulates mitochondrial reactive oxygen species homeostasis through Sirt3 signaling pathway in human vascular endothelial cells

Zhou, X., Chen, M., Zeng, X., Yang, J., Deng, H., Yi, L., & Mt, M. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.530 · Cited by 208 · see citing works

Interaction of Sirt3 with OGG1 contributes to repair of mitochondrial DNA and protects from apoptotic cell death under oxidative stress

Cheng, Y., Ren, X., Gowda, A. S., Shan, Y., Zhang, L., Yuan, Y.-S., Patel, R., Wu, H., Huber-Keener, K., Yang, J. W., et al. (2013) · Cell Death &amp; Disease · doi:10.1038/cddis.2013.254 · Cited by 205 · see citing works

Deacetylation of cortactin by SIRT1 promotes cell migration

Zhang, Y., Zhang, M., Dong, H., Yong, S., Li, X., Olashaw, N., Kruk, P. A., Cheng, J., Bai, W., Chen, J., et al. (2008) · Oncogene · doi:10.1038/onc.2008.388 · Cited by 205 · see citing works

An acetylome peptide microarray reveals specificities and deacetylation substrates for all human sirtuin isoforms

Rauh, D., Fischer, F. F., Gertz, M., Lakshminarasimhan, M., Bergbrede, T., Aladini, F., Kambach, C., Becker, C. F. W., Zerweck, J., Schutkowski, M., et al. (2013) · Nature Communications · doi:10.1038/ncomms3327 · Cited by 204 · see citing works

Oral Resveratrol Reduces Neuronal Damage in a Model of Multiple Sclerosis

Shindler, K. S., Ventura, E. S., Dutt, M., Elliott, P. J., Fitzgerald, D. C., & Rostami, A. M. (2010) · Journal of Neuro-Ophthalmology · doi:10.1097/wno.0b013e3181f7f833 · Cited by 203 · see citing works

NBS1 and its functional role in the DNA damage response

Kobayashi, J., Antoccia, A., Tauchi, H., Matsuura, S., & Komatsu, K. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.03.023 · Cited by 202 · see citing works

Mechanism of Cardioprotection by Early Ischemic Preconditioning

Yang, X., Cohen, M. V., & Downey, J. M. (2010) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-010-6236-x · Cited by 201 · see citing works

Regulation of Glycolytic Enzyme Phosphoglycerate Mutase-1 by Sirt1 Protein-mediated Deacetylation

Hallows, W. C., Yu, W., & Denu, J. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.317404 · Cited by 200 · see citing works

Functional Proteomics Establishes the Interaction of SIRT7 with Chromatin Remodeling Complexes and Expands Its Role in Regulation of RNA Polymerase I Transcription

Tsai, Y.-C., Greco, T. M., Boonmee, A., Miteva, Y., & Cristea, I. M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.a111.015156 · Cited by 198 · 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 &amp; Redox Signaling · doi:10.1089/ars.2013.5482 · Cited by 194 · see citing works

Nicotinamide Clearance by Pnc1 Directly Regulates Sir2-Mediated Silencing and Longevity

Gallo, C. M., Smith, D. L., & Smith, J. S. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.1301-1312.2004 · Cited by 193 · see citing works

Regulation of Caenorhabditis elegans lifespan by sir-2.1 transgenes

Viswanathan, M., & Guarente, L. (2011) · Nature · doi:10.1038/nature10440 · Cited by 191 · see citing works

Regulation of SIRT6 protein levels by nutrient availability

Kanfi, Y., Shalman, R., Peshti, V., Pilosof, S. N., Gozlan, Y. M., Pearson, K. J., Lerrer, B., Moazed, D., Marine, J., de Cabo, R., et al. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.01.019 · Cited by 187 · see citing works

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

Kim, D. H., Jung, Y. J., Lee, J. E., Lee, A. S., Kang, K. P., Lee, S., Park, S. K., Han, M., Lee, S. Y., Ramkumar, K. M., et al. (2011) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00258.2010 · Cited by 180 · see citing works

Sirtuin 3 (SIRT3) Protein Regulates Long-chain Acyl-CoA Dehydrogenase by Deacetylating Conserved Lysines Near the Active Site

Bharathi, S. S., Zhang, Y., Mohsen, A.-W. A., Uppala, R., Balasubramani, M., Schreiber, E. M., Uechi, G. T., Beck, M. E., Rardin, M. J., Vockley, J. E., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.510354 · Cited by 179 · see citing works

Omega-3 Fatty Acids Supplementation Restores Mechanisms that Maintain Brain Homeostasis in Traumatic Brain Injury

Wu, A., Ying, Z., & Gómez‐Pinilla, F. (2007) · Journal of Neurotrauma · doi:10.1089/neu.2007.0313 · Cited by 178 · see citing works

Regulation of WRN Protein Cellular Localization and Enzymatic Activities by SIRT1-mediated Deacetylation

Li, K., Casta, A., Wang, R., Lozada, E., Fan, W., Kane, S. E., Ge, Q., Gu, W. J., Orren, D. K., & Luo, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709707200 · Cited by 177 · see citing works

Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through polarity protein Par-3/atypical protein kinase C (aPKC) signaling

Beirowski, B., Gustin, J. A., Armour, S., Yamamoto, H., Viader, A., North, B., Michán, S., Baloh, R., Golden, J., Schmidt, R., et al. (2011) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1104969108 · Cited by 175 · see citing works

SIRT3 Deacetylates ATP Synthase F ₁ Complex Proteins in Response to Nutrient- and Exercise-Induced Stress

Vassilopoulos, A., Pennington, J. D., Andresson, T., Rees, D. M., Bosley, A. D., Fearnley, I. M., Ham, A., Flynn, C. R., Hill, S., Rose, K. L., et al. (2014) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2013.5420 · Cited by 173 · see citing works

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

Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638 · see citing works

Sirtuins, a promising target in slowing down the ageing process

Grabowska, W., Sikora, E., & Bielak-Zmijewska, A. (2017) · Biogerontology · doi:10.1007/s10522-017-9685-9 · Cited by 470 · see citing works

Melatonin and inflammation-Story of a double-edged blade

Hardeland, R. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12525 · Cited by 455 · see citing works

Aging, melatonin, and the pro- and anti-inflammatory networks

Hardeland, R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20051223 · Cited by 337 · see citing works

‘Adipaging’: ageing and obesity share biological hallmarks related to a dysfunctional adipose tissue

Pérez, L. M., Pareja‐Galeano, H., Sanchis‐Gomar, F., Emanuele, E., Lucia, A., & Gálvez, B. G. (2016) · The Journal of Physiology · doi:10.1113/jp271691 · Cited by 215 · see citing works

Mitochondria initiate and regulate sarcopenia

Alway, S. E., Mohamed, J. S., & Myers, M. J. (2017) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000101 · Cited by 153 · see citing works

HDAC inhibitors: A new promising drug class in anti-aging research

Pasyukova, E. G., & Vaiserman, A. M. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.08.008 · Cited by 99 · see citing works

Could sirtuin activities modify ALS onset and progression?

Tang, B. L. (2017) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0452-2 · Cited by 24 · see citing works

USP7 deubiquitinates and stabilizes SIRT1.

Song, N., Cao, C., Tian, S., Long, M., & Liu, L. (2020) · The Anatomical Record · doi:10.1002/ar.24252 · Cited by 19 · see citing works

A comprehensive review on modulation of <scp>SIRT1</scp> signaling pathways in the immune system of <scp>COVID</scp> ‐19 patients by phytotherapeutic melatonin and epigallocatechin‐3‐gallate

Chattree, V., Singh, K., Singh, K., Goel, A., Maity, A., & Lone, A. (2022) · Journal of Food Biochemistry · doi:10.1111/jfbc.14259 · Cited by 19 · see citing works

Effects of Sirtuins on Female Reproductivity and Oocyte Quality: Traditional Review

ŞEN, E., Dalçık, H., & Dalçık, C. (2022) · Turkiye Klinikleri Journal of Medical Sciences · doi:10.5336/medsci.2021-86890 · Cited by 1 · see citing works

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

Resveratrol Induced Premature Senescence Is Associated with DNA Damage Mediated SIRT1 and SIRT2 Down-Regulation

Kilic Eren, M., Kilincli, A., & Eren, Ö. (2015) · PLOS ONE · doi:10.1371/journal.pone.0124837 · Cited by 68 · see citing works

Faculty Opinions recommendation of The role of sirtuins in antioxidant and redox signaling.

Ji, L. L. (2021) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.731078139.793582081

Faculty Opinions recommendation of The sirtuin SIRT6 regulates lifespan in male mice.

Conley, K. E., & Padowski, J. M. (2012) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.14256976.15768104