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

Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase

Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510

AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity

Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300

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

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 2,690

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

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

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

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

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

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

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

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

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 1,603

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

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 1,497

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

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

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

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

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

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

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 1,366

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

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 1,362

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

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

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

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

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

Acetylation: a regulatory modification to rival phosphorylation?

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

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 1,135

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

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

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

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

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

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

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

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

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

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 1,006

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 1,003

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

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

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 971

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

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

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 940

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

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

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

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

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

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

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

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

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

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

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

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

Sir2 links chromatin silencing, metabolism, and agingPreprint

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

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

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

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

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

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

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 704

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

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

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

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 659

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 649

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 646

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 638

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

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 & Development · doi:10.1101/gad.1399706 · Cited by 629

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

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

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

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

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

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

Fulco, M., Schiltz, R. L., Iezzi, S., King, M. T., Zhao, P., Kashiwaya, Y., Hoffman, E. P., Veech, R. L., & Sartorelli, V. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00226-0 · Cited by 591

The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth.

Firestein, R., Blander, G., Michan, S., Oberdoerffer, P., Ogino, S., Campbell, J., Bhimavarapu, A., Luikenhuis, S., de Cabo, R., Fuchs, C., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002020 · Cited by 588

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 588

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

Csibi, A., Fendt, S.-M., Li, C., Poulogiannis, G., Choo, A. Y., Chapski, D. J., Jeong, S. M., Dempsey, J. M., Parkhitko, A., Morrison, T., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.023 · Cited by 586

Silent Information Regulator 1 Protects the Heart From Ischemia/Reperfusion

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

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

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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 553

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

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

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

Schlicker, C., Gertz, M., Papatheodorou, P., Kachholz, B., Becker, C. F. W., & Steegborn, C. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.048 · Cited by 531

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

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 506

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

Scher, M. B., Vaquero, A., & Reinberg, D. (2007) · Genes & Development · doi:10.1101/gad.1527307 · Cited by 489

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

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 478

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

Rodgers, J. T., & Puigserver, P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702509104 · Cited by 466

SIRT3 deacetylates FOXO3 to protect mitochondria against oxidative damage

Tseng, A. H.-H., Shieh, S.-S., & Wang, D. L. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.002 · Cited by 458

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 456

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 453

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 452

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

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

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

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

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

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

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

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 424

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 424

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 404

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

Berdichevsky, A., Viswanathan, M., Horvitz, H. R., & Guarente, L. (2006) · Cell · doi:10.1016/j.cell.2006.04.036 · Cited by 402

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 402

Myosin isoenzyme changes in several models of rat cardiac hypertrophy.

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Nampt: linking NAD biology, metabolism and cancer

Garten, A., Petzold-Quinque, S., Körner, A., Imai, S., & Kieß, W. (2008) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2008.10.004 · Cited by 399

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 396

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

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 390

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

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 381

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

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

Dasuri, K., Zhang, L., & Keller, J. N. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.016 · Cited by 371

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

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

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

Rothgiesser, K. M., Erener, S., Waibel, S., Lüscher, B., & Hottiger, M. O. (2010) · Journal of Cell Science · doi:10.1242/jcs.073783 · Cited by 345

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

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 341

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

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

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 330

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 329

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 324

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 323

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

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 318

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 315

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 315

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 313

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 309

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

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 303

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 298

Sirtuins at a glance

Nakagawa, T., & Guarente, L. (2011) · Journal of Cell Science · doi:10.1242/jcs.081067 · Cited by 292

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 290

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

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 289

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

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

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

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

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

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

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 275

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

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

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

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

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

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

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 253

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 248

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

SIRT2 induces the checkpoint kinase BubR1 to increase lifespan

North, B. J., Rosenberg, M. A., Jeganathan, K. B., Hafner, A. V., Michan, 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 238

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

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

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

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 230

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 229

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

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 225

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

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

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

Porter, G. A., 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 221

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 218

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

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

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 & Disease · doi:10.1038/cddis.2013.254 · Cited by 205

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

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

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

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 203

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

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 201

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 201

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

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

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

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 185

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., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.510354 · Cited by 181

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 181

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

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. M., Yamamoto, H., Viader, A., North, B. J., Michán, S., Baloh, R. H., Golden, J. P., Schmidt, R. E., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1104969108 · Cited by 175

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 & Redox Signaling · doi:10.1089/ars.2013.5420 · Cited by 173

Vitamin E Protects Against Oxidative Damage and Learning Disability After Mild Traumatic Brain Injury in Rats

Wu, A., Ying, Z., & Gómez‐Pinilla, F. (2009) · Neurorehabilitation and neural repair · doi:10.1177/1545968309348318 · Cited by 171

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

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

Melatonin and inflammation-Story of a double-edged blade

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

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

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

‘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

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

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

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