Sirtuins as regulators of metabolism and healthspan

Resveratrol improves health and survival of mice on a high-calorie diet

Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290 · see citing works

SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver

Horton, J. D., Goldstein, J. L., & Brown, M. S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15593 · Cited by 4,285 · see citing works

SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver

Horton, J. D., Goldstein, J. L., & Brown, M. S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215593 · Cited by 4,092 · see citing works

Resveratrol Improves Mitochondrial Function and Protects against Metabolic Disease by Activating SIRT1 and PGC-1α

Lagouge, M., Argmann, C., Gerhart-Hines, Z., Meziane, H., Lerin, C., Daussin, F., Messadeq, N., Milne, J., Lambert, P., Elliott, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.11.013 · Cited by 4,057 · see citing works

mTOR: from growth signal integration to cancer, diabetes and ageing

Zoncu, R., Efeyan, A., & Sabatini, D. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3025 · Cited by 3,941 · see citing works

HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia

Kim, J.-W., Tchernyshyov, I., Semenza, G. L., & Dang, C. V. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.002 · Cited by 3,905 · see citing works

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

Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1

Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160 · see citing works

Extending Healthy Life Span—From Yeast to Humans

Fontana, L., Partridge, L., & Longo, V. D. (2010) · Science · doi:10.1126/science.1172539 · Cited by 3,023 · 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

AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α

Jäger, S., Handschin, C., St.-Pierre, J., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705070104 · Cited by 2,491 · 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

Mammalian Sirtuins: Biological Insights and Disease Relevance

Haigis, M. C., & Sinclair, D. A. (2010) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092250 · Cited by 2,085 · see citing works

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

Poly(ADP-ribose): novel functions for an old molecule

Schreiber, V., Dantzer, F., Amé, J., & de MURCIA, G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1963 · Cited by 1,917 · see citing works

Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes

Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707 · 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

Genomic Instability and Aging-like Phenotype in the Absence of Mammalian SIRT6

Mostoslavsky, R., Chua, K. F., Lombard, D. B., Pang, W. W., Fischer, M. R., Gellon, L., Liu, P., Mostoslavsky, G., Franco, S., Murphy, M. M., et al. (2006) · Cell · doi:10.1016/j.cell.2005.11.044 · Cited by 1,637 · 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

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

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

Sir2 mediates longevity in the fly through a pathway related to calorie restriction

Rogina, B., & Helfand, S. L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404184101 · Cited by 1,361 · see citing works

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

Nicotinamide Mononucleotide, a Key NAD+ Intermediate, Treats the Pathophysiology of Diet- and Age-Induced Diabetes in Mice

Yoshino, J., Mills, K. F., Yoon, M. J., & Imai, S.-I. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.014 · Cited by 1,340 · see citing works

Calorie Restriction-like Effects of 30 Days of Resveratrol Supplementation on Energy Metabolism and Metabolic Profile in Obese Humans

Timmers, S., Konings, E., Bilet, L., Houtkooper, R. H., van de Weijer, T., Goossens, G. H., Hoeks, J., van der Krieken, S., Ryu, D., Kersten, S., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.10.002 · Cited by 1,320 · 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

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

Regulation of pgc-1α, a nodal regulator of mitochondrial biogenesis

Fernandez-Marcos, P. J., & Auwerx, J. (2011) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.110.001917 · Cited by 1,237 · 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

Molecular and metabolic mechanisms of insulin resistance and β-cell failure in type 2 diabetes

Muoio, D. M., & Newgard, C. B. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2327 · Cited by 1,177 · 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

Resveratrol delays age-related deterioration and mimics transcriptional aspects of dietary restriction without extending life span

Pearson, K. J., Baur, J. A., Lewis, K. N., Peshkin, L., Price, N. L., Labinskyy, N., Swindell, W. R., Kamara, D., Minor, R. K., Perez, E., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.06.011 · Cited by 1,162 · see citing works

Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction

Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150 · 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

Peroxisome Proliferator-Activated Receptor γ Coactivator 1 Coactivators, Energy Homeostasis, and Metabolism

Handschin, C., & Spiegelman, B. M. (2006) · Endocrine Reviews · doi:10.1210/er.2006-0037 · Cited by 1,090 · 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

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

Sirt1 protects against high-fat diet-induced metabolic damage

Pfluger, P. T., Herranz, D., Velasco-Miguel, S., Serrano, M., & Tschöp, M. H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802917105 · Cited by 932 · see citing works

Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle

Cantó, C., Jiang, L. Q., Deshmukh, A. S., Mataki, C., Coste, A., Lagouge, M., Zierath, J. R., & Auwerx, J. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.02.006 · Cited by 921 · see citing works

SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1

Pacholec, M., Bleasdale, J. E., Chrunyk, B., Cunningham, D., Flynn, D., Garofalo, R. S., Griffith, D., Griffor, M., Loulakis, P., Pabst, B., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.088682 · Cited by 915 · see citing works

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

Houtkooper, R. H., Cantó, C., Wanders, R. J., & Auwerx, J. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0026 · Cited by 899 · see citing works

PARP-1 inhibition increases mitochondrial metabolism through SIRT1 activation

Bai, P., Cantó, C., Oudart, H., Brunyánszki, A., Cen, Y., Thomas, C., Yamamoto, H., Huber, A., Kiss, B., Houtkooper, R. H., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.004 · Cited by 837 · see citing works

The PARP Side of the Nucleus: Molecular Actions, Physiological Outcomes, and Clinical Targets

Krishnakumar, R., & Kraus, W. L. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.017 · Cited by 836 · see citing works

SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome

Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.019 · Cited by 787 · 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

Nucleocytoplasmic Shuttling of the NAD+-dependent Histone Deacetylase SIRT1*

Tanno, M., Sakamoto, J., Miura, T., Shimamoto, K., & Horio, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609554200 · Cited by 784 · see citing works

SIRT3 Opposes Reprogramming of Cancer Cell Metabolism through HIF1α Destabilization

Finley, L. W. S., Carracedo, A., Lee, J., Souza, A., Egia, A., Zhang, J., Teruya-Feldstein, J., Moreira, P. I., Cardoso, S. M., Clish, C. B., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.02.014 · Cited by 782 · see citing works

Use of Cells Expressing γ Subunit Variants to Identify Diverse Mechanisms of AMPK Activation

Hawley, S. A., Ross, F. A., Chevtzoff, C., Green, K. A., Evans, A., Fogarty, S., Towler, M. C., Brown, L. J., Ogunbayo, O. A., Evans, A. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.04.001 · Cited by 773 · 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

The first identification of lysine malonylation substrates and its regulatory enzyme

Peng, C., Lu, Z., Xie, Z., Cheng, Z., Chen, Y., Tan, M., Luo, H., Zhang, Y., He, W., Yang, K., et al. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.012658 · Cited by 751 · see citing works

Discoveries of Nicotinamide Riboside as a Nutrient and Conserved NRK Genes Establish a Preiss-Handler Independent Route to NAD+ in Fungi and Humans

Bieganowski, P., & Brenner, C. (2004) · Cell · doi:10.1016/s0092-8674(04)00416-7 · Cited by 750 · 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 transgenic mice show phenotypes resembling calorie restriction

Bordone, L., Cohen, D., Robinson, A., Motta, M. C., Van Veen, E., Czopik, A., Steele, A. D., Crowe, H., Marmor, S., Luo, J., et al. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00335.x · Cited by 722 · see citing works

Specific SIRT1 Activation Mimics Low Energy Levels and Protects against Diet-Induced Metabolic Disorders by Enhancing Fat Oxidation

Feige, J. N., Lagouge, M., Canto, C., Strehle, A., Houten, S. M., Milne, J. C., Lambert, P. D., Mataki, C., Elliott, P. J., & Auwerx, J. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.017 · Cited by 719 · 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

Nutrient Availability Regulates SIRT1 Through a Forkhead-Dependent Pathway

Nemoto, S., Fergusson, M. M., & Finkel, T. (2004) · Science · doi:10.1126/science.1101731 · Cited by 671 · 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

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

Verdin, E., Hirschey, M. D., Finley, L. W. S., & Haigis, M. C. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.003 · Cited by 661 · see citing works

Tumor Suppressor HIC1 Directly Regulates SIRT1 to Modulate p53-Dependent DNA-Damage Responses

Chen, W., Wang, D. H., Yen, R.-W. C., Luo, J., Gu, W. J., & Baylin, S. B. (2005) · Cell · doi:10.1016/j.cell.2005.08.011 · Cited by 649 · see citing works

AMP-activated protein kinase-deficient mice are resistant to the metabolic effects of resveratrol

Um, J.-H., Park, S.-J., Kang, H., Yang, S., Foretz, M., McBurney, M. W., Kim, M. K., Viollet, B., & Chung, J. H. (2010) · Diabetes · doi:10.2337/db09-0482 · Cited by 647 · 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

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 630 · 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 & Development · doi:10.1101/gad.1399706 · Cited by 629 · see citing works

Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila

Burnett, C., Valentini, S., Cabreiro, F., Goss, M., Somogyvári, M., Piper, M. D., Hoddinott, M., Sutphin, G. L., Leko, V., McElwee, J. J., et al. (2011) · Nature · doi:10.1038/nature10296 · Cited by 624 · see citing works

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

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

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

Tissue-specific regulation of SIRT1 by calorie restriction

Chen, D., Bruno, J., Easlon, E., Lin, S.-J., Cheng, H.-L., Alt, F. W., & Guarente, L. (2008) · Genes & Development · doi:10.1101/gad.1650608 · Cited by 567 · see citing works

A fasting inducible switch modulates gluconeogenesis via activator/coactivator exchange

Liu, Y., Dentin, R., Chen, D., Hedrick, S. A., Ravnskjær, K., Schenk, S., Milne, J. C., Meyers, D. J., Cole, P., Yates, J. R., et al. (2008) · Nature · doi:10.1038/nature07349 · Cited by 556 · see citing works

Nuclear Trapping of the Forkhead Transcription Factor FoxO1 via Sirt-dependent Deacetylation Promotes Expression of Glucogenetic Genes*

Frescas, D., Valenti, L. N., & Accili, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412357200 · Cited by 554 · see citing works

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 549 · see citing works

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*

Ponugoti, B., Kim, D.-H., Xiao, Z., Smith, Z., Miao, J., Zang, M., Wu, S.-Y., Chiang, C., Veenstra, T. D., & Kemper, J. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.122978 · Cited by 545 · 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

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 · see citing works

Untitled work

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

Sirtuins, Aging, and Medicine

Guarente, L. (2011) · New England Journal of Medicine · doi:10.1056/nejmra1100831 · Cited by 510 · see citing works

DBC1 is a negative regulator of SIRT1

Kim, J., Chen, J., & Lou, Z. (2008) · Nature · doi:10.1038/nature06500 · Cited by 503 · see citing works

SIRT2 Regulates Adipocyte Differentiation through FoxO1 Acetylation/Deacetylation

Jing, E., Gesta, S., & Kahn, C. R. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.07.003 · Cited by 490 · see citing works

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

Palacios, O. M., Carmona, J. J., Michan, S., Chen, K. Y., Manabe, Y., III, J. L. W., Goodyear, L. J., & Tong, Q. (2009) · Aging · doi:10.18632/aging.100075 · Cited by 487 · 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

Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production

Jing, E., Emanuelli, B., Hirschey, M. D., Boucher, J., Lee, K. Y., Lombard, D., Verdin, E. M., & Kahn, C. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111308108 · Cited by 469 · see citing works

Negative regulation of the deacetylase SIRT1 by DBC1

Zhao, W., Kruse, J.-P., Tang, Y., Jung, S. Y., Qin, J., & Gu, W. J. (2008) · Nature · doi:10.1038/nature06515 · Cited by 464 · see citing works

Inhibition of mitochondrial proton F0F1‐ATPase/ATP synthase by polyphenolic phytochemicals

Zheng, J., & Ramirez, V. D. (2000) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0703397 · Cited by 453 · see citing works

GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1α

Lerin, C., Rodgers, J. T., Kalume, D. E., Kim, S.-H., Pandey, A., & Puigserver, P. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.04.013 · Cited by 443 · see citing works

Effects of resveratrol on lifespan in Drosophila melanogaster and Caenorhabditis elegans

Bass, T. M., Weinkove, D., Houthoofd, K., Gems, D., & Partridge, L. (2007) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.07.007 · Cited by 435 · 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

Resveratrol is not a direct activator of SIRT1 enzyme activity

Beher, D., Wu, J., Cumine, S., Kim, K. W., Lu, S., Atangan, L., & Wang, M. (2009) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2009.00901.x · Cited by 426 · see citing works

Sirtuins — novel therapeutic targets to treat age-associated diseases

Lavu, S., Boss, O., Elliott, P. J., & Lambert, P. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2665 · Cited by 425 · see citing works

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

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

AMP-activated protein kinase and its downstream transcriptional pathways

Cantó, C., & Auwerx, J. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0454-z · Cited by 421 · see citing works

Genetic control of de novo lipogenesis: role in diet-induced obesity

Strable, M. S., & Ntambi, J. M. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409231003667500 · Cited by 415 · 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

Active Regulator of SIRT1 Cooperates with SIRT1 and Facilitates Suppression of p53 Activity

Kim, E.-J., Kho, J.-H., Kang, M., & Um, S. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.08.030 · Cited by 389 · see citing works

Metabolomic Analysis of Livers and Serum from High-Fat Diet Induced Obese Mice

Kim, H.-J., Kim, J. H., Noh, S., Hur, H. J., Sung, M. J., Hwang, J.-T., Park, J. H., Yang, H. J., Kim, M.-S., Kwon, D. Y., et al. (2011) · Journal of Proteome Research · doi:10.1021/pr100892r · Cited by 376 · see citing works

Resveratrol alleviates alcoholic fatty liver in mice

Ajmo, J. M., Liang, X., Rogers, C. Q., Pennock, B., & You, M. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90358.2008 · Cited by 370 · see citing works

Efficient Transcriptional Silencing in Saccharomyces cerevisiae Requires a Heterochromatin Histone Acetylation Pattern

Braunstein, M., Sobel, R. E., Allis, C. D., Turner, B. M., & Broach, J. R. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.8.4349 · Cited by 367 · see citing works

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

Conserved role of SIRT1 orthologs in fasting-dependent inhibition of the lipid/cholesterol regulator SREBPPreprint

Walker, A. K., Yang, F., Jiang, K., Ji, J., Watts, J. L., Purushotham, A., Boss, O., Hirsch, M. L., Ribich, S. A., Smith, J. J., et al. (2010) · Genes & Development · doi:10.1101/gad.1901210 · Cited by 352 · see citing works

The Cellular Fate of Glucose and Its Relevance in Type 2 Diabetes

Bouché, C., Serdy, S., Kahn, C. R., & Goldfine, A. B. (2004) · Endocrine Reviews · doi:10.1210/er.2003-0026 · Cited by 348 · 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 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress

Yang, Y., Fu, W., Chen, J., Olashaw, N., Zhang, X. M., Nicosia, S. V., Bhalla, K. N., & Bai, W. (2007) · Nature Cell Biology · doi:10.1038/ncb1645 · Cited by 324 · see citing works

SIRT4 Regulates Fatty Acid Oxidation and Mitochondrial Gene Expression in Liver and Muscle Cells

Nasrin, N., Wu, X.-P., Fortier, E., Feng, Y., Bare, O., Chen, S., Ren, X., Wu, Z., Streeper, R. S., & Bordone, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.124164 · Cited by 323 · see citing works

The secretory function of adipocytes in the physiology of white adipose tissue

Wang, P., Mariman, E., Renes, J., & Keijer, J. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21386 · Cited by 318 · 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 315 · see citing works

Splicing regulates NAD metabolite binding to histone macroH2A

Kustatscher, G., Hothorn, M., Pugieux, C., Scheffzek, K., & Ladurner, A. G. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb956 · Cited by 300 · see citing works

Hepatic overexpression of SIRT1 in mice attenuates endoplasmic reticulum stress and insulin resistance in the liver

Li, Y., Xu, S., Giles, A. J., Nakamura, K., Lee, J. W., Hou, X., Dönmez, G., Li, J., Luo, Z., Walsh, K., et al. (2011) · The FASEB Journal · doi:10.1096/fj.10-173492 · Cited by 298 · see citing works

SRT1720 improves survival and healthspan of obese mice

Minor, R. K., Baur, J. A., Gomes, A. P., Ward, T. M., Csiszár, A., Mercken, E. M., Abdelmohsen, K., Shin, Y., Cantó, C., Scheibye‐Knudsen, M., et al. (2011) · Scientific Reports · doi:10.1038/srep00070 · Cited by 297 · see citing works

Regulatory enzymes of mitochondrial β‐oxidation as targets for treatment of the metabolic syndrome

Schreurs, M., Kuipers, F., & van der Leij, F. R. (2009) · Obesity Reviews · doi:10.1111/j.1467-789x.2009.00642.x · Cited by 295 · see citing works

Sirtuin 1 in lipid metabolism and obesity

Schug, T. T., & Li, X. (2011) · Annals of Medicine · doi:10.3109/07853890.2010.547211 · Cited by 292 · see citing works

Phosphorylation Regulates SIRT1 Function

Sasaki, T., Maier, B., Koclega, K. D., Chruszcz, M., Gluba, W., Stukenberg, P. T., Minor, W., & Scrable, H. J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0004020 · Cited by 290 · 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

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

NCoR1 Is a Conserved Physiological Modulator of Muscle Mass and Oxidative Function

Yamamoto, H., Williams, E. G., Mouchiroud, L., Cantó, C., Fan, W., Downes, M., Héligon, C., Barish, G. D., Desvergne, B., Evans, R. M., et al. (2011) · Cell · doi:10.1016/j.cell.2011.10.017 · Cited by 261 · 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 Pathway Involving Farnesoid X Receptor and Small Heterodimer Partner Positively Regulates Hepatic Sirtuin 1 Levels via MicroRNA-34a Inhibition

Lee, J., Padhye, A., Sharma, A., Song, G., Miao, J., Mo, Y.-Y., Wang, L., & Kemper, J. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.094524 · Cited by 259 · see citing works

SIRT1: recent lessons from mouse models

Herranz, D., & Serrano, M. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2962 · Cited by 256 · see citing works

PARP-2 Regulates SIRT1 Expression and Whole-Body Energy Expenditure

Bai, P., Cantó, C., Brunyánszki, A., Huber, A., Szántó, M., Cen, Y., Yamamoto, H., Houten, S. M., Kiss, B., Oudart, H., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.013 · Cited by 250 · see citing works

The enzyme CD38 (a NAD glycohydrolase, EC 3.2.2.5) is necessary for the development of diet‐induced obesity

Barbosa, M. T., Soares, S. M., Novak, C. M., Sinclair, D. A., Levine, J. A., Aksoy, P., & Chini, E. N. (2007) · The FASEB Journal · doi:10.1096/fj.07-8290com · Cited by 249 · see citing works

DYRK1A and DYRK3 Promote Cell Survival through Phosphorylation and Activation of SIRT1

Guo, X., Williams, J. G., Schug, T. T., & Li, X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.102574 · Cited by 237 · see citing works

Mitochondrial sirtuins

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

PPARγ in human and mouse physiology

Heikkinen, S., Auwerx, J. H., & Argmann, C. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2007.03.006 · Cited by 222 · see citing works

Lack of SIRT1 (Mammalian Sirtuin 1) Activity Leads to Liver Steatosis in the SIRT1+/− Mice: A Role of Lipid Mobilization and Inflammation

Xu, F. L., Gao, Z., Zhang, J., Rivera, C. A., Yin, J., Weng, J., & Ye, J. (2010) · Endocrinology · doi:10.1210/en.2009-1013 · Cited by 221 · see citing works

SIRT1 is regulated by a PPARγ–SIRT1 negative feedback loop associated with senescence

Han, L., Zhou, R., Niu, J., McNutt, M. A., Wang, P., & Tong, T. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq609 · Cited by 218 · see citing works

Metabolic networks of longevity

Houtkooper, R. H., Williams, R. W., & Auwerx, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.029 · Cited by 217 · see citing works

A SIRT1-LSD1 Corepressor Complex Regulates Notch Target Gene Expression and Development

Mulligan, P., Yang, F., Stefano, L. D., Ji, J., Ouyang, J., Nishikawa, J. L., Toiber, D., Kulkarni, M., Wang, Q., Najafi-Shoushtari, S. H., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.020 · Cited by 211 · see citing works

Peroxisome Proliferator-activated Receptor-γ Coactivator-1α Controls Transcription of the Sirt3 Gene, an Essential Component of the Thermogenic Brown Adipocyte Phenotype

Giralt, A., Hondares, E., Villena, J. A., Ribas, F., Díaz-Delfín, J., Giralt, M., Iglesias, R., & Villarroya, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.202390 · Cited by 210 · see citing works

The genetic ablation of SRC-3 protects against obesity and improves insulin sensitivity by reducing the acetylation of PGC-1α

Coste, A., Louet, J.-F., Lagouge, M., Lerin, C., Antal, M. C., Meziane, H., Schoonjans, K., Puigserver, P., O'Malley, B. W., & Auwerx, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808207105 · Cited by 205 · see citing works

Transcriptional targets of sirtuins in the coordination of mammalian physiology

Feige, J. N., & Auwerx, J. H. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.012 · Cited by 202 · see citing works

Sirt1 enhances skeletal muscle insulin sensitivity in mice during caloric restriction

Schenk, S., McCurdy, C. E., Philp, A., Chen, M. Z., Holliday, M. J., Bandyopadhyay, G. K., Osborn, O., Baar, K., & Olefsky, J. M. (2011) · Journal of Clinical Investigation · doi:10.1172/jci58554 · Cited by 197 · 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

Deleted in breast cancer–1 regulates SIRT1 activity and contributes to high-fat diet–induced liver steatosis in mice

Escande, C., Chini, C. C. S., Nin, V., Dykhouse, K. M., Novak, C. M., Levine, J. A., van Deursen, J., Gores, G. J., Chen, J., Lou, Z., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci39319 · Cited by 186 · see citing works

Sirtuin 1 (SIRT1) Deacetylase Activity Is Not Required for Mitochondrial Biogenesis or Peroxisome Proliferator-activated Receptor-γ Coactivator-1α (PGC-1α) Deacetylation following Endurance Exercise

Philp, A., Chen, A., Lan, D., Meyer, G. A., Murphy, A. N., Knapp, A. E., Olfert, I. M., McCurdy, C. E., Marcotte, G. R., Hogan, M. C., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.261685 · Cited by 184 · see citing works

Neural sirtuin 6 (Sirt6) ablation attenuates somatic growth and causes obesity

Schwer, B., Schumacher, B., Lombard, D. B., Xiao, C., Kurtev, M. V., Gao, J., Schneider, J. I., Chai, H., Bronson, R. T., Tsai, L., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016306107 · Cited by 176 · 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

CREB and ChREBP oppositely regulate SIRT1 expression in response to energy availability

Noriega, L. G., Feige, J. N., Cantó, C., Yamamoto, H., Yu, J., Herman, M. A., Mataki, C., Kahn, B. B., & Auwerx, J. H. (2011) · EMBO Reports · doi:10.1038/embor.2011.151 · Cited by 172 · see citing works

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

Yamazaki, Y., Usui, I., Kanatani, Y., Matsuya, Y., Tsuneyama, K., Fujisaka, S., Bukhari, A., Suzuki, H., Senda, S., Imanishi, S., et al. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90997.2008 · Cited by 164 · see citing works

Fasting promotes the expression of SIRT1, an NAD+-dependent protein deacetylase, via activation of PPARα in mice

Hayashida, S., Arimoto, A., Kuramoto, Y., Kozako, T., Honda, S., Shimeno, H., & Soeda, S. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0391-z · Cited by 137 · see citing works

Liver Steatosis and Increased ChREBP Expression in Mice Carrying a Liver Specific SIRT1 Null Mutation under a Normal Feeding Condition

Wang, R., Li, C., & Deng, C. (2010) · International Journal of Biological Sciences · doi:10.7150/ijbs.6.682 · Cited by 121 · see citing works

Function and metabolism of sirtuin metabolite O-acetyl-ADP-ribose

Tong, L., & Denu, J. M. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.02.007 · Cited by 115 · see citing works

Sir2 and calorie restriction in yeast: A skeptical perspective

Kaeberlein, M. R., & Powers, R. W. (2007) · Ageing Research Reviews · doi:10.1016/j.arr.2007.04.001 · Cited by 108 · see citing works

SIRT1 mRNA expression may be associated with energy expenditure and insulin sensitivity

Rutanen, J., Yaluri, N., Modi, S., Pihlajamäki, J., Vänttinen, M., Itkonen, P., Kainulainen, S., Yamamoto, H., Lagouge, M., Sinclair, D. A., et al. (2010) · Diabetes · doi:10.2337/db09-1191 · Cited by 104 · see citing works

The Management of Nicotinamide and Nicotinic Acid in the Mouse

Collins, P. B., & Chaykin, S. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45675-5 · Cited by 102 · see citing works

PPAR.BETA./.DELTA. regulates the human SIRT1 gene transcription via Sp1

Okazaki, M., Iwasaki, Y., Nishiyama, M., Taguchi, T., Tsugita, M., Nakayama, S., Kambayashi, M., Hashimoto, K., & Terada, Y. (2010) · Endocrine Journal · doi:10.1507/endocrj.k10e-004 · Cited by 97 · see citing works

Fine Tuning Our Cellular Factories: Sirtuins in Mitochondrial Biology

Zhong, L., & Mostoslavsky, R. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.05.004 · Cited by 90 · see citing works

Sirtuin 1 (SIRT1) sequence variation is not associated with exceptional human longevity

Flachsbart, F., CROUCHER, P., Nikolaus, S., Hampe, J., CORDES, C., SCHREIBER, S., & Nebel, A. (2005) · Experimental Gerontology · doi:10.1016/j.exger.2005.09.008 · Cited by 79 · see citing works

Exposure to resveratrol triggers pharmacological correction of fatty acid utilization in human fatty acid oxidation-deficient fibroblasts

Bastin, J., Costa, A. L., & Djouadi, F. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr089 · Cited by 72 · see citing works

Peroxisome Proliferator-Activated Receptor γ Coactivator-1α, as a Transcription Amplifier, Is Not Essential for Basal and Hormone-Induced Phosphoenolpyruvate Carboxykinase Gene Expression

Herzog, B., Hall, R. K., Wang, X. L., Waltner-Law, M. E., & Granner, D. K. (2004) · Molecular Endocrinology · doi:10.1210/me.2003-0384 · Cited by 44 · see citing works

Effects of aging on cardiac and skeletal muscle AMPK activity: basal activity, allosteric activation, and response to in vivo hypoxemia in mice

Gonzalez, A. A., Kumar, R., Mulligan, J. D., Davis, A. J., & Saupe, K. W. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00409.2004 · Cited by 43 · see citing works

Design, synthesis and biological characterization of novel inhibitors of CD38

Dong, M., Si, Y.-Q., Sun, S.-Y., Pu, X., Yang, Z.-J., Zhang, L., Zhang, L., Leung, F. P., Lam, C. M. C., Kwong, A. K., et al. (2011) · Organic & Biomolecular Chemistry · doi:10.1039/c0ob00768d · Cited by 37 · see citing works

What's in a dream?

James, A. N. (2011) · Nature · doi:10.1038/nj7364-1 · Cited by 9 · see citing works

The Hallmarks of Aging

López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982 · see citing works

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

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

Mitochondrial Dynamics Controls T Cell Fate through Metabolic Programming

Buck, M. D., O’Sullivan, D., Geltink, R. I. K., Curtis, J. D., Chang, C., Sanin, D. E., Qiu, J., Kretz, O., Braas, D., van der Windt, G. J. W., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.035 · Cited by 1,444 · see citing works

Acetyl Coenzyme A: A Central Metabolite and Second Messenger

Pietrocola, F., Galluzzi, L., Pedro, J. M. B., Madeo, F., & Kroemer, G. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.014 · Cited by 1,349 · see citing works

The growing landscape of lysine acetylation links metabolism and cell signalling

Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3841 · Cited by 1,324 · see citing works

Senescence and aging: Causes, consequences, and therapeutic avenues

McHugh, D., & Gil, J. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201708092 · Cited by 1,233 · see citing works

Functions and mechanisms of non-histone protein acetylation

Narita, T., Weinert, B. T., & Choudhary, C. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0081-3 · Cited by 1,232 · see citing works

The NAD+/Sirtuin Pathway Modulates Longevity through Activation of Mitochondrial UPR and FOXO Signaling

Mouchiroud, L., Houtkooper, R. H., Moullan, N., Katsyuba, E., Ryu, D., Cantó, C., Mottis, A., Jo, Y.-S., Viswanathan, M., Schoonjans, K., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.016 · Cited by 1,210 · see citing works

Histone Modifications and CancerPreprint

Audia, J. E., & Campbell, R. M. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a019521 · Cited by 1,024 · 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

Mechanisms of hepatic triglyceride accumulation in non-alcoholic fatty liver disease

Kawano, Y., & Cohen, D. E. (2013) · Journal of Gastroenterology · doi:10.1007/s00535-013-0758-5 · Cited by 968 · see citing works

Ketone bodies as signaling metabolites

Newman, J. C., & Verdin, E. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.09.002 · Cited by 966 · see citing works

Acetyl-CoA and the regulation of metabolism: mechanisms and consequences

Shi, L., & Tu, B. P. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.02.003 · Cited by 903 · see citing works

Metabolic control of autophagy

Galluzzi, L., Pietrocola, F., Levine, B., & Kroemer, G. (2014) · Cell · doi:10.1016/j.cell.2014.11.006 · Cited by 855 · see citing works

Slowing ageing by design: the rise of NAD+ and sirtuin-activating compounds

Bonkowski, M. S., & Sinclair, D. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.93 · Cited by 834 · see citing works

Reprogramming of glucose, fatty acid and amino acid metabolism for cancer progression

Li, Z., & Zhang, H. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2070-4 · Cited by 829 · see citing works

The Role of Sirtuins in Antioxidant and Redox Signaling

Singh, C. K., Chhabra, G., Ndiaye, M. A., Garcia‐Peterson, L. M., Mack, N. J., & Ahmad, N. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7290 · Cited by 812 · see citing works

Senescence and aging: the critical roles of p53

Rufini, A., Tucci, P., Celardo, I., & Melino, G. (2013) · Oncogene · doi:10.1038/onc.2012.640 · Cited by 798 · see citing works

Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease

Smith, R. L., Soeters, M. R., Wüst, R. C. I., & Houtkooper, R. H. (2018) · Endocrine Reviews · doi:10.1210/er.2017-00211 · Cited by 787 · see citing works

Lactate as a fulcrum of metabolism

Brooks, G. A. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101454 · Cited by 724 · see citing works

Molecular mechanisms of dietary restriction promoting health and longevity

Green, C. L., Lamming, D. W., & Fontana, L. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00411-4 · Cited by 714 · see citing works

Metabolic targets for cancer therapy

Galluzzi, L., Kepp, O., Heiden, M. G. V., & Kroemer, G. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4145 · Cited by 705 · see citing works

Histone Deacetylase Inhibitors in Clinical Studies as Templates for New Anticancer Agents

Mottamal, M., Zheng, S., Huang, T. L., & Wang, G. (2015) · Molecules · doi:10.3390/molecules20033898 · Cited by 687 · see citing works

Metabolites as regulators of insulin sensitivity and metabolism

Yang, Q., Vijayakumar, A., & Kahn, B. B. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0044-8 · Cited by 681 · see citing works

The effects of aging in the hippocampus and cognitive decline

Bettio, L. E. B., Rajendran, L., & Gil‐Mohapel, J. (2017) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2017.04.030 · Cited by 654 · see citing works

Telomeres: history, health, and hallmarks of aging

Chakravarti, D., LaBella, K. A., & DePinho, R. A. (2021) · Cell · doi:10.1016/j.cell.2020.12.028 · Cited by 637 · see citing works

NAD+ homeostasis in health and disease

Katsyuba, E., Romani, M., Hofer, D., & Auwerx, J. (2020) · Nature Metabolism · doi:10.1038/s42255-019-0161-5 · Cited by 627 · see citing works

Mitochondria in health, disease, and aging

Harrington, J. S., Ryter, S. W., Plataki, M. E., Price, D. R., & Choi, A. M. K. (2023) · Physiological Reviews · doi:10.1152/physrev.00058.2021 · Cited by 622 · see citing works

The NAD+-Dependent SIRT1 Deacetylase Translates a Metabolic Switch into Regulatory Epigenetics in Skeletal Muscle Stem Cells

Ryall, J. G., Dell’Orso, S., Derfoul, A., Juan, A., Zare, H., Feng, X., Clermont, D., Koulnis, M., Gutierrez-Cruz, G., Fulco, M., et al. (2015) · Cell Stem Cell · doi:10.1016/j.stem.2014.12.004 · Cited by 575 · see citing works

Iron and diabetes risk

Simcox, J. A., & McClain, D. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.02.007 · Cited by 545 · see citing works

Molecular and physiological manifestations and measurement of aging in humans

Khan, S. S., Singer, B. D., & Vaughan, D. E. (2017) · Aging Cell · doi:10.1111/acel.12601 · Cited by 530 · see citing works

A two-way street: reciprocal regulation of metabolism and signalling

Wellen, K. E., & Thompson, C. B. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3305 · Cited by 528 · see citing works

Mechanisms and consequences of endothelial cell senescence

Bloom, S. I., Islam, M. T., Lesniewski, L. A., & Donato, A. J. (2022) · Nature Reviews Cardiology · doi:10.1038/s41569-022-00739-0 · Cited by 512 · see citing works

Redox regulation of SIRT1 in inflammation and cellular senescence

Hwang, J.-W., Yao, H., Caito, S., Sundar, I. K., & Rahman, I. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.03.015 · Cited by 503 · see citing works

The multifaceted functions of sirtuins in cancer

Chalkiadaki, A., & Guarente, L. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3985 · Cited by 501 · see citing works

Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies

Jiang, H., Zhang, X., Chen, X., Aramsangtienchai, P., Tong, Z., & Lin, H. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00750 · Cited by 501 · see citing works

The Aging Epigenome

Booth, L. N., & Brunet, A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.013 · Cited by 499 · see citing works

Dendritic cell metabolism

Pearce, E. J., & Everts, B. (2014) · Nature reviews. Immunology · doi:10.1038/nri3771 · Cited by 482 · 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

Sirtuin activators and inhibitors: Promises, achievements, and challenges

Dai, H., Sinclair, D. A., Ellis, J. L., & Steegborn, C. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.03.004 · Cited by 463 · see citing works

Crosstalk between Oxidative Stress and SIRT1: Impact on the Aging Process

Salminen, A., Kaarniranta, K., & Kauppinen, A. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14023834 · Cited by 457 · 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

Protective effects of sirtuins in cardiovascular diseases: from bench to bedside

Winnik, S. H., Auwerx, J. H., Sinclair, D. A., & Matter, C. M. (2015) · European Heart Journal · doi:10.1093/eurheartj/ehv290 · Cited by 443 · see citing works

Energy metabolism in health and diseases

Liu, H., Wang, S., Wang, J., Guo, X., Song, Y., Fu, K., Gao, Z., Liu, D., He, W., & Yang, L. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02141-x · Cited by 438 · see citing works

De novo NAD+ synthesis enhances mitochondrial function and improves health

Katsyuba, E., Mottis, A., Ziętak, M., Franco, F., van der Velpen, V., Gariani, K., Ryu, D., Cialabrini, L., Matilainen, O., Liscio, P., et al. (2018) · Nature · doi:10.1038/s41586-018-0645-6 · Cited by 436 · see citing works

Non-enzymatic Lysine Lactoylation of Glycolytic Enzymes

Gaffney, D. O., Jennings, E. Q., Anderson, C. C., Marentette, J., Shi, T., Oxvig, A.-M. S., Streeter, M. D., Johannsen, M., Spiegel, D. A., Chapman, E., et al. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.11.005 · Cited by 430 · see citing works

Nonalcoholic fatty liver disease: molecular mechanisms for the hepatic steatosis

Koo, S. (2013) · Clinical and Molecular Hepatology · doi:10.3350/cmh.2013.19.3.210 · Cited by 421 · see citing works

The nexus of chromatin regulation and intermediary metabolism

Gut, P., & Verdin, E. M. (2013) · Nature · doi:10.1038/nature12752 · Cited by 419 · see citing works

Metabolic control of epigenetics in cancer

Kinnaird, A. S., Zhao, S., Wellen, K. E., & Michelakis, E. D. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.82 · Cited by 419 · see citing works

Mitochondria as central regulators of neural stem cell fate and cognitive function

Khacho, M., Harris, R., & Slack, R. S. (2018) · Nature reviews. Neuroscience · doi:10.1038/s41583-018-0091-3 · Cited by 396 · see citing works

SIRT4 Coordinates the Balance between Lipid Synthesis and Catabolism by Repressing Malonyl CoA Decarboxylase

Laurent, G., German, N. J., Saha, A. K., de Boer, V. C. J., Davies, M. N., Koves, T. R., Dephoure, N., Fischer, F. F., Boanca, G., Vaitheesvaran, B., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.05.012 · Cited by 394 · see citing works

Mitochondrial dysfunction in the pathophysiology of renal diseases

Che, R., Yuan, Y., Huang, S., & Zhang, A. (2013) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00571.2013 · Cited by 393 · see citing works

Pharmacological approaches to restore mitochondrial function

Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383 · see citing works

Seven sirtuins for seven deadly diseases ofaging

Morris, B. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.525 · Cited by 380 · see citing works

NRK1 controls nicotinamide mononucleotide and nicotinamide riboside metabolism in mammalian cells

Ratajczak, J., Joffraud, M., Trammell, S. A. J., Ras, R., Canela, N., Boutant, M., Kulkarni, S. S., Rodrigues, M., Redpath, P., Migaud, M. E., et al. (2016) · Nature Communications · doi:10.1038/ncomms13103 · Cited by 378 · see citing works

The Interplay of Reactive Oxygen Species, Hypoxia, Inflammation, and Sirtuins in Cancer Initiation and Progression

Tafani, M., Sansone, L., Limana, F., Arcangeli, T., Santis, E. D., Polese, M., Fini, M., & Russo, M. A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3907147 · Cited by 371 · see citing works

Mitochondria and Epigenetics – Crosstalk in Homeostasis and Stress

Matilainen, O., Quirós, P. M., & Auwerx, J. H. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.02.004 · Cited by 368 · see citing works

Mitophagy in neurodegeneration and aging

Fivenson, E. M., Lautrup, S., Sun, N., Scheibye-Knudsen, M., Stevnsner, T., Nilsen, H., Bohr, V. A., & Fang, E. F. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.02.007 · Cited by 364 · see citing works

Circadian Reprogramming in the Liver Identifies Metabolic Pathways of Aging

Sato, S., Solanas, G., Peixoto, F. O., Bee, L., Symeonidi, A., Schmidt, M. S., Brenner, C., Masri, S., Benitah, S. A., & Sassone‐Corsi, P. (2017) · Cell · doi:10.1016/j.cell.2017.07.042 · Cited by 359 · see citing works

The Roles of Histone Deacetylases and Their Inhibitors in Cancer Therapy

Guo, L., Tian, Y., & Zhu, W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.576946 · Cited by 358 · see citing works

The Link Between Angiogenesis and Endothelial Metabolism

Potente, M., & Carmeliet, P. (2016) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105134 · Cited by 353 · see citing works

A high-fat diet and NAD(+) activate Sirt1 to rescue premature aging in Cockayne syndrome

Scheibye-Knudsen, M., Mitchell, S. J., Fang, E. F., Iyama, T., Ward, T., Wang, J., Dunn, C. A., Singh, N., Veith, S., Hasan-Olive, M. M., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.10.005 · Cited by 352 · see citing works

NAD+-Dependent Activation of Sirt1 Corrects the Phenotype in a Mouse Model of Mitochondrial Disease

Cerutti, R., Pirinen, E., Lamperti, C., Marchet, S., Sauve, A. A., Li, W., Leoni, V., Schon, E. A., Dantzer, F., Auwerx, J., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.001 · Cited by 343 · see citing works

Traumatic Brain Injury: Oxidative Stress and Neuroprotection

Cornelius, C., Crupi, R., Calabrese, V., Graziano, A., Milone, P., Pennisi, G., Radak, Z. O., Calabrese, E. J., & Cuzzocrea, S. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4981 · Cited by 343 · see citing works

Targeting autophagy in obesity: from pathophysiology to management

Zhang, Y., Sowers, J. R., & Ren, J. (2018) · Nature Reviews Endocrinology · doi:10.1038/s41574-018-0009-1 · Cited by 338 · see citing works

Repairing mitochondrial dysfunction in disease

Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337 · see citing works

Butyrate-Producing Probiotics Reduce Nonalcoholic Fatty Liver Disease Progression in Rats: New Insight into the Probiotics for the Gut-Liver Axis

Endo, H., Niioka, M., Kobayashi, N., Tanaka, M., & Watanabe, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063388 · Cited by 335 · see citing works

Curcumin alleviates oxidative stress and inhibits apoptosis in diabetic cardiomyopathy via Sirt1‐Foxo1 and PI3K‐Akt signalling pathways

Ren, B., Zhang, Y., Liu, S., Cheng, X., Yang, X. C., Cui, X., Zhao, X., Zhao, H., Hao, M., Li, M., et al. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15725 · Cited by 333 · see citing works

Protein acetylation in metabolism – metabolites and cofactors

Menzies, K. J., Zhang, H., Katsyuba, E., & Auwerx, J. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.181 · Cited by 331 · see citing works

The metabolic fate of acetate in cancer

Schug, Z. T., Vande Voorde, J., & Gottlieb, E. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.87 · Cited by 331 · see citing works

Little Fish, Big Data: Zebrafish as a Model for Cardiovascular and Metabolic Disease

Gut, P., Reischauer, S., Stainier, D. Y. R., & Arnaout, R. (2017) · Physiological Reviews · doi:10.1152/physrev.00038.2016 · Cited by 327 · see citing works

SIRT4 is a lysine deacylase that controls leucine metabolism and insulin secretion

Anderson, K. A., Huynh, F. K., Fisher-Wellman, K., Stuart, J. D., Peterson, B. S., Douros, J. D., Wagner, G. R., Thompson, J. W., Madsen, A. S., Green, M. F., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.03.003 · Cited by 326 · see citing works

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

Bao, X., Wang, Y., Li, X., Li, X.-M., Liu, Z., Yang, T., Wong, C. F., Zhang, J., Hao, Q., & Li, X. D. (2014) · eLife · doi:10.7554/elife.02999 · Cited by 324 · 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

Oxidative stress response elicited by mitochondrial dysfunction: Implication in the pathophysiology of aging

Wang, C., Wu, S., Wu, Y., & Wei, Y. (2013) · Experimental Biology and Medicine · doi:10.1177/1535370213493069 · Cited by 315 · see citing works

Connecting Mitochondria, Metabolism, and Stem Cell Fate

Wanet, A., Arnould, T., Najimi, M., & Renard, P. (2015) · Stem Cells and Development · doi:10.1089/scd.2015.0117 · Cited by 310 · see citing works

Dysregulated metabolism contributes to oncogenesis

Hirschey, M. D., DeBerardinis, R. J., Diehl, A. M., Drew, J. E., Frezza, C., Green, M. F., Jones, L. W., Ko, Y. H., Le, A., Lea, M. A., et al. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.10.002 · Cited by 306 · see citing works

Eight Kinetically Stable but Thermodynamically Activated Molecules that Power Cell Metabolism

Walsh, C. T., Tu, B. P., & Tang, Y. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00510 · Cited by 302 · see citing works

Targeting mitochondria for cardiovascular disorders: therapeutic potential and obstacles

Bonora, M., Wieckowski, M. R., Sinclair, D. A., Kroemer, G., Pinton, P., & Galluzzi, L. (2018) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0074-0 · Cited by 299 · see citing works

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

Tatone, C., Emidio, G. D., Barbonetti, A., Carta, G., Luciano, A. M., Falone, S., & Amicarelli, F. (2018) · Human Reproduction Update · doi:10.1093/humupd/dmy003 · Cited by 294 · see citing works

Resveratrol and Its Human Metabolites—Effects on Metabolic Health and Obesity

Springer, M., & Moco, S. (2019) · Nutrients · doi:10.3390/nu11010143 · Cited by 293 · see citing works

Partitioning Circadian Transcription by SIRT6 Leads to Segregated Control of Cellular Metabolism

Masri, S., Rigor, P., Cervantes, M., Ceglia, N., Sebastian, C., Xiao, C., Roqueta-Rivera, M., Deng, C., Osborne, T. F., Mostoslavsky, R., et al. (2014) · Cell · doi:10.1016/j.cell.2014.06.050 · Cited by 292 · see citing works

Metabolic and Epigenetic Coordination of T Cell and Macrophage Immunity

Phan, A. T., Goldrath, A. W., & Glass, C. K. (2017) · Immunity · doi:10.1016/j.immuni.2017.04.016 · Cited by 291 · see citing works

Cancer-associated fibroblasts promote prostate cancer malignancy via metabolic rewiring and mitochondrial transfer

Ippolito, L., Morandi, A., Taddei, M. L., Parri, M., Comito, G., Iscaro, A., Raspollini, M. R., Magherini, F., Rapizzi, E., Masquelier, J., et al. (2019) · Oncogene · doi:10.1038/s41388-019-0805-7 · Cited by 290 · 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

Ketogenic diets, mitochondria, and neurological diseases

Gano, L. B., Patel, M., & Rho, J. M. (2014) · Journal of Lipid Research · doi:10.1194/jlr.r048975 · Cited by 279 · see citing works

Sirtuins in Epigenetic Regulation

Jing, H., & Lin, H. (2015) · Chemical Reviews · doi:10.1021/cr500457h · Cited by 271 · see citing works

NAD metabolism: Implications in aging and longevity

Yaku, K., Okabe, K., & Nakagawa, T. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.05.006 · Cited by 269 · see citing works

Sirt1 resists advanced glycation end products-induced expressions of fibronectin and TGF-β1 by activating the Nrf2/ARE pathway in glomerular mesangial cells

Huang, K., Huang, J., Xie, X., Wang, S., Chen, C., Shen, X., Liu, P., & Huang, H. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.029 · Cited by 269 · 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

Mitochondrial sirtuins: regulators of protein acylation and metabolism

He, W., Newman, J. C., Wang, M. Z., Ho, L., & Verdin, E. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.07.004 · Cited by 262 · see citing works

NAD + Metabolism in Cardiac Health, Aging, and Disease

Abdellatif, M., Sedej, S., & Kroemer, G. (2021) · Circulation · doi:10.1161/circulationaha.121.056589 · Cited by 262 · see citing works

Regulation of Akt Signaling by Sirtuins

Pillai, V. B., Sundaresan, N. R., & Gupta, M. P. (2014) · Circulation Research · doi:10.1161/circresaha.113.300536 · 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

ACE2 Deficiency Worsens Epicardial Adipose Tissue Inflammation and Cardiac Dysfunction in Response to Diet-Induced Obesity

Patel, V. B., Mori, J., McLean, B. A., Basu, R., Das, S. K., Ramprasath, T., Parajuli, N., Penninger, J. M., Grant, M. B., Lopaschuk, G. D., et al. (2015) · Diabetes · doi:10.2337/db15-0399 · Cited by 257 · see citing works

Sirtuins, Cell Senescence, and Vascular Aging

Kida, Y., & Goligorsky, M. S. (2015) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2015.11.022 · Cited by 255 · see citing works

Pharmacological Inhibition of poly(ADP-ribose) polymerases improves fitness and mitochondrial function in skeletal muscle

Pirinen, E., Cantó, C., Jo, Y. S., Morato, L., Zhang, H., Menzies, K. J., Williams, E. G., Mouchiroud, L., Moullan, N., Hagberg, C., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.002 · Cited by 254 · see citing works

Nicotinamide N -Methyltransferase: More Than a Vitamin B3 Clearance Enzyme

Pissios, P. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.02.004 · Cited by 254 · see citing works

Emerging Role of Sirtuin 2 in the Regulation of Mammalian Metabolism

Gomes, P., Outeiro, T. F., & Cavadas, C. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.08.001 · Cited by 253 · see citing works

Autophagy in diabetic kidney disease: regulation, pathological role and therapeutic potential

Yang, D., Livingston, M. J., Liu, Z., Dong, G., Zhang, M., Chen, J.-K., & Dong, Z. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2639-1 · Cited by 252 · 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

Sirtuins and their role as physiological modulators of metabolism

Sygitowicz, G., & Sitkiewicz, D. (2020) · Postępy Higieny i Medycyny Doświadczalnej · doi:10.5604/01.3001.0014.5247 · Cited by 4 · see citing works

Sirtuins and energy homeostasis

Nehra, B., Kasnia, R., Demiwal, S., Suthar, S., & Debnath, B. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-45380-9.00018-3

Sirtuins: The ‘ <i>magnificent seven</i> ’, function, metabolism and longevity

Dali‐Youcef, N., Lagouge, M., Froelich, S., Koehl, C., Schoonjans, K., & Auwerx, J. (2007) · Annals of Medicine · doi:10.1080/07853890701408194 · Cited by 402 · see citing works

Sirtuins in glucose and lipid metabolism

Ye, X., Li, M., Hou, T., Gao, T., Zhu, W., & Yang, Y. (2016) · Oncotarget · doi:10.18632/oncotarget.12157 · Cited by 215 · see citing works