Sirt1 and the Mitochondria

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

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

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

Multiple Wearable Sensors in Parkinson and Huntington Disease Individuals: A Pilot Study in Clinic and at Home

Adams, J., Dinesh, K., Xiong, M., Tarolli, C. G., Sharma, S., Sheth, N., Aranyosi, A. J., Zhu, W. Y., Goldenthal, S. B., Biglan, K., et al. (2017) · Digital Biomarkers · doi:10.1159/000479018 · Cited by 3,190

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

Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase

Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., & Mayo, M. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600244 · Cited by 2,750

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

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

HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption

Papandreou, I., Cairns, R. A., Fontana, L., Lim, A. L., & Denko, N. C. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.01.012 · Cited by 2,267

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

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

Huntington's disease: from molecular pathogenesis to clinical treatment

Ross, C. A., & Tabrizi, S. J. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70245-3 · Cited by 1,816

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

SIRT1 is required for AMPK activation and the beneficial effects of resveratrol on mitochondrial function

Price, N. L., Gomes, A. P., Ling, A. J. Y., Duarte, F. V., Martin-Montalvo, A., North, B. J., Agarwal, B., Ye, L., Ramadori, G., Teodoro, J. S., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.003 · Cited by 1,602

Extrachromosomal rDNA circles—a cause of aging in yeast

Sinclair, D. A., & Guarente, L. (1997) · Cell · doi:10.1016/s0092-8674(00)80493-6 · Cited by 1,500

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

Resveratrol Ameliorates Aging-Related Metabolic Phenotypes by Inhibiting cAMP Phosphodiesterases

Park, S. J., Ahmad, F., Philp, A., Baar, K., Williams, T., Luo, H., Ke, H., Rehmann, H., Taussig, R., Brown, A. L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.01.017 · Cited by 1,370

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

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

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

Haigis, M. C., & Guarente, L. P. (2006) · Genes & Development · doi:10.1101/gad.1467506 · Cited by 1,295

Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC‐1α

Gerhart‐Hines, Z., Rodgers, J. T., Bare, O., Lerin, C., Kim, S., Mostoslavsky, R., Alt, F. W., Wu, Z., & Puigserver, P. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601633 · Cited by 1,294

The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men

Yang, X., & Seto, E. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2346 · Cited by 1,277

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

Calorie restriction promotes mitochondrial biogenesis by inducing the expression of eNOS

Nisoli, E., Tonello, C., Cardile, A., Cozzi, V., Bracale, R., Tedesco, L., Falcone, S., Valerio, A., Cantoni, O., Clementi, E., et al. (2005) · Science · doi:10.1126/science.1117728 · Cited by 1,107 · cited 3×

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

Mitochondrial dynamics and inheritance during cell division, development and disease

Mishra, P., & Chan, D. C. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3877 · Cited by 1,076

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

AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation

Zong, H., Ren, J. M., Young, L. H., Pypaert, M., Mu, J., Birnbaum, M. J., & Shulman, G. I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252625599 · Cited by 1,036

Transcriptional Repression of PGC-1α by Mutant Huntingtin Leads to Mitochondrial Dysfunction and Neurodegeneration

Cui, L., Jeong, H., Borovecki, F., Parkhurst, C. N., Tanese, N., & Krainc, D. (2006) · Cell · doi:10.1016/j.cell.2006.09.015 · Cited by 1,012

PARIS (ZNF746) Repression of PGC-1α Contributes to Neurodegeneration in Parkinson's Disease

Shin, J.-H., Ko, H. S., Kang, H., Lee, Y., Lee, Y.-I., Pletinkova, O., Troconso, J. C., Dawson, V. L., & Dawson, T. M. (2011) · Cell · doi:10.1016/j.cell.2011.02.010 · Cited by 953

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

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

50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond

Verdin, E. M., & Ott, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3931 · Cited by 905

PGC-1 α, A Potential Therapeutic Target for Early Intervention in Parkinson’s Disease

Zheng, B., Liao, Z., Locascio, J. J., Lesniak, K. A., Roderick, S. S., Watt, M. L., Eklund, A. C., Zhang‐James, Y., Kim, P. D., Hauser, M. A., et al. (2010) · Science Translational Medicine · doi:10.1126/scitranslmed.3001059 · Cited by 868

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

SIRT1 Modulation of the Acetylation Status, Cytosolic Localization, and Activity of LKB1

Lan, F., Cacicedo, J. M., Ruderman, N., & Ido, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805711200 · Cited by 825

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

Calorie Restriction Increases Muscle Mitochondrial Biogenesis in Healthy Humans

Civitarese, A. E., Carling, S., Heilbronn, L. K., Hulver, M. H., Ukropcova, B., Deutsch, W. A., Smith, S. R., & Ravussin, E. (2007) · PLoS Medicine · doi:10.1371/journal.pmed.0040076 · Cited by 790

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

SIRT1 Regulates Hepatocyte Lipid Metabolism through Activating AMP-activated Protein Kinase

Hou, X., Xu, S., Maitland-Toolan, K. A., Sato, K., Jiang, B., Ido, Y., Lan, F., Walsh, K., Wierzbicki, M., Verbeuren, T. J., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802187200 · Cited by 778

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

Substrate-specific activation of sirtuins by resveratrol

Kaeberlein, M., McDonagh, T., Heltweg, B., Hixon, J., Westman, E. A., Caldwell, S. D., Napper, A., Curtis, R., DiStefano, P. S., Fields, S., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500655200 · Cited by 745

Resveratrol stimulates AMP kinase activity in neurons

Dasgupta, B., & Milbrandt, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610068104 · Cited by 723

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

Defective Mitophagy in XPA via PARP-1 Hyperactivation and NAD+/SIRT1 Reduction

Fang, E. F., Scheibye-Knudsen, M., Brace, L. E., Kassahun, H., SenGupta, T., Nilsen, H., Mitchell, J. R., Croteau, D. L., & Bohr, V. A. (2014) · Cell · doi:10.1016/j.cell.2014.03.026 · Cited by 711

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

FOXO transcription factors: key regulators of cellular quality control

Webb, A. E., & Brunet, A. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.02.003 · Cited by 649

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

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

PGC1α and mitochondrial metabolism – emerging concepts and relevance in ageing and neurodegenerative disorders

Austin, S., & St‐Pierre, J. (2012) · Journal of Cell Science · doi:10.1242/jcs.113662 · Cited by 617

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

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

PINK1/Parkin-mediated mitophagy in mammalian cells

Eiyama, A., & Okamoto, K. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.01.002 · Cited by 603

Evidence for a common mechanism of SIRT1 regulation by allosteric activators

Hubbard, B. P., Gomes, A. P., Dai, H., Li, J., Case, A. W., Considine, T., Riera, T. V., Lee, J. E., E, S. Y., Lamming, D. W., et al. (2013) · Science · doi:10.1126/science.1231097 · Cited by 561

Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1- O- acetyl-ADP-ribose

Tanner, K. G., Landry, J. W., Sternglanz, R., & Denu, J. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250422697 · Cited by 557

Aging-associated reductions in AMP-activated protein kinase activity and mitochondrial biogenesis

Reznick, R. M., Zong, H., Li, J., Morino, K., Moore, I. K., Yu, H. J., Liu, Z.-X., Dong, J., Mustard, K. J., Hawley, S. A., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.01.008 · Cited by 555

Activation of AMP-Activated Protein Kinase Reduces Hyperglycemia-Induced Mitochondrial Reactive Oxygen Species Production and Promotes Mitochondrial Biogenesis in Human Umbilical Vein Endothelial Cells

Kukidome, D., Nishikawa, T., Sonoda, K., Imoto, K., Fujisawa, K., Yano, M., Motoshima, H., Taguchi, T., Matsumura, T., & Araki, E. (2006) · Diabetes · doi:10.2337/diabetes.55.01.06.db05-0943 · Cited by 504

Akt/PKB regulates hepatic metabolism by directly inhibiting PGC-1α transcription coactivator

Li, X., Monks, B., Ge, Q., & Birnbaum, M. J. (2007) · Nature · doi:10.1038/nature05861 · Cited by 487

Mitochondrial transcription factor A regulates mitochondrial transcription initiation, DNA packaging, and genome copy number

Campbell, C. T., Kolesar, J. E., & Kaufman, B. A. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.03.002 · Cited by 477

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

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

SIRT1 Negatively Regulates the Mammalian Target of Rapamycin

Ghosh, H. S., McBurney, M., & Robbins, P. D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009199 · Cited by 397

Caloric restriction, SIRT1 and longevity

Cantó, C., & Auwerx, J. (2009) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2009.03.008 · Cited by 395

Epigenetic control of rDNA loci in response to intracellular energy status

Murayama, A., Ohmori, K., Fujimura, A., Minami, H., Yasuzawa-Tanaka, K., Kuroda, T., Oie, S., Daitoku, H., Okuwaki, M., Nagata, K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.03.030 · Cited by 394

The role of AMP‐activated protein kinase in mitochondrial biogenesis

Reznick, R. M., & Shulman, G. I. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.109512 · Cited by 375

SIRT1 Regulates Apoptosis and Nanog Expression in Mouse Embryonic Stem Cells by Controlling p53 Subcellular Localization

Han, M., Song, E.-K., Guo, Y., Ou, X., Mantel, C., & Broxmeyer, H. E. (2008) · Cell stem cell · doi:10.1016/j.stem.2008.01.002 · Cited by 374

Sensing of energy and nutrients by AMP-activated protein kinase

Hardie, D. G. (2011) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.110.001925 · Cited by 372

Acetylation-Deacetylation of the Transcription Factor Nrf2 (Nuclear Factor Erythroid 2-related Factor 2) Regulates Its Transcriptional Activity and Nucleocytoplasmic Localization

Kawai, Y., Garduño, L., Theodore, M., Yang, J., & Arinze, I. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.208173 · Cited by 362

Peroxisome Proliferator-activated Receptor γ Co-activator 1α (PGC-1α) and Sirtuin 1 (SIRT1) Reside in Mitochondria

Aquilano, K., Vigilanza, P., Baldelli, S., Pagliei, B., Rotilio, G., & Ciriolo, M. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.070169 · Cited by 347

SIRT1 Positively Regulates Autophagy and Mitochondria Function in Embryonic Stem Cells Under Oxidative Stress

Ou, X., Lee, M. R., Huang, X., Messina‐Graham, S., & Broxmeyer, H. E. (2014) · Stem Cells · doi:10.1002/stem.1641 · Cited by 338

SirT1 Regulation of Antioxidant Genes Is Dependent on the Formation of a FoxO3a/PGC-1α Complex

Olmos, Y., Sánchez-Gómez, F. J., Wild, B., García-Quintáns, N., Cabezudo, S., Lamas, S., & Monsalve, M. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4713 · Cited by 328

FOXO3a regulates reactive oxygen metabolism by inhibiting mitochondrial gene expression

Ferber, E. C., Peck, B., Delpuech, O., Bell, G. P., East, P., & Schulze, A. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.179 · Cited by 320

Transgenic expression and activation of PGC-1α protect dopaminergic neurons in the MPTP mouse model of Parkinson’s disease

Mudò, G., Mäkelä, J., Liberto, V. D., Tselykh, T. V., Olivieri, M., Piepponen, P. T., Eriksson, O., Mälkiä, A., Bonomo, A., Kairisalo, M., et al. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0850-z · Cited by 305

SIRT1 Promotes Proliferation and Prevents Senescence Through Targeting LKB1 in Primary Porcine Aortic Endothelial Cells

Zu, Y., Liu, L., Lee, M. Y. K., Xu, C., Liang, Y., Man, R. Y., Vanhoutte, P. M., & Wang, Y. (2010) · Circulation Research · doi:10.1161/circresaha.109.215483 · Cited by 303

Mitochondrial DNA nucleoid structure

Bogenhagen, D. F. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.11.005 · Cited by 290

SIRT3 interacts with the daf-16 homolog FOXO3a in the Mitochondria, as well as increases FOXO3a Dependent Gene expression

Jacobs, K. M., Pennington, J. D., Bisht, K. S., Aykin‐Burns, N., Kim, H., Mishra, M. V., Sun, L., Nguyen, P., Ahn, B., Leclerc, J., et al. (2008) · International Journal of Biological Sciences · doi:10.7150/ijbs.4.291 · Cited by 285

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

Anderson, R. M., Barger, J. L., Edwards, M. G., Braun, K. H., O’Connor, C. E., Prolla, T. A., & Weindruch, R. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2007.00357.x · Cited by 283 · cited 1×

Nicotinamide-induced Mitophagy

Jang, S., Kang, H. T., & Hwang, E. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.363747 · Cited by 264

The SIRT1 activator resveratrol protects SK‐N‐BE cells from oxidative stress and against toxicity caused by α‐synuclein or amyloid‐β (1‐42) peptide

Albani, D., Polito, L., Batelli, S., Mauro, S. D., Fracasso, C., Martelli, G., Colombo, L., Manzoni, C., Salmona, M., Caccia, S., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06228.x · Cited by 263

p38 Mitogen-activated Protein Kinase Activates Peroxisome Proliferator-activated Receptor α

Barger, P. M., Browning, A. C., Garner, A. N., & Kelly, D. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105945200 · Cited by 260

Effects of Resveratrol and SIRT1 on PGC-1α Activity and Mitochondrial Biogenesis: A Reevaluation

Higashida, K., Kim, S. H., Jung, S. R., Asaka, M., Holloszy, J. O., & Han, D.-H. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001603 · Cited by 237

SIRT1 Controls the Transcription of the Peroxisome Proliferator-activated Receptor-γ Co-activator-1α (PGC-1α) Gene in Skeletal Muscle through the PGC-1α Autoregulatory Loop and Interaction with MyoD

Amat, R., Planavila, A., Chen, S. L., Iglesias, R., Giralt, M., & Villarroya, F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.022749 · Cited by 224

Sirtuins, Aging, and MetabolismPreprint

Guarente, L. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010629 · Cited by 213

Structural Identification of 2′- and 3′-O-Acetyl-ADP-ribose as Novel Metabolites Derived from the Sir2 Family of β-NAD+-dependent Histone/Protein Deacetylases

Jackson, M. D., & Denu, J. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200671200 · Cited by 212

Protective effects and mechanisms of sirtuins in the nervous system

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Deacetylation of cortactin by SIRT1 promotes cell migration

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Nutrient-dependent regulation of PGC-1α's acetylation state and metabolic function through the enzymatic activities of Sirt1/GCN5

Dominy, J. E., Lee, Y., Gerhart‐Hines, Z., & Puigserver, P. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.11.023 · Cited by 199

Sirtuins' modulation of autophagy

Ng, F., & Tang, B. L. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24399 · Cited by 198

Cytoplasm‐localized SIRT1 enhances apoptosis

Jin, Q., Yan, T., Ge, X., Sun, C., Shi, X., & Zhai, Q. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21091 · Cited by 197

PPAR control: it's SIRTainly as easy as PGC

Sugden, M. C., Caton, P., & Holness, M. J. (2009) · Journal of Endocrinology · doi:10.1677/joe-09-0359 · Cited by 196

SIRT1 in the brain—connections with aging-associated disorders and lifespan

Ng, F. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00064 · Cited by 192

Gain-of-function R225Q Mutation in AMP-activated Protein Kinase γ3 Subunit Increases Mitochondrial Biogenesis in Glycolytic Skeletal Muscle

Garcia-Roves, P. M., Osler, M. E., Holmström, M. H., & Zierath, J. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805078200 · Cited by 190

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

Resveratrol Inhibits mTOR Signaling by Promoting the Interaction between mTOR and DEPTOR

Liu, M., Wilk, S. A., Wang, A., Zhou, L., Wang, R.-H., Ogawa, W., Deng, C., Dong, L., & Liu, F. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.169284 · Cited by 181

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

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

Maintaining Ancient Organelles

Vega, R. B., Horton, J. L., & Kelly, D. P. (2015) · Circulation Research · doi:10.1161/circresaha.116.305420 · Cited by 147

Does calorie restriction induce mitochondrial biogenesis? A reevaluation

Hancock, C. R., Han, D., Higashida, K., Kim, S. H., & Holloszy, J. O. (2011) · The FASEB Journal · doi:10.1096/fj.10-170415 · Cited by 131

SNCA (α-synuclein)-induced toxicity in yeast cells is dependent on Sir2-mediated mitophagy

Sampaio‐Marques, B., Felgueiras, C., Silva, A., Rodrigues, M. L., Tenreiro, S., Franssens, V., Reichert, A. S., Outeiro, T. F., Winderickx, J., & Ludovico, P. (2012) · Autophagy · doi:10.4161/auto.21275 · Cited by 128

Nicotinamide enhances mitochondria quality through autophagy activation in human cells

Kang, H. T., & Hwang, E. S. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00487.x · Cited by 128

Aberrant Cytoplasm Localization and Protein Stability of SIRT1 is Regulated by PI3K/IGF-1R Signaling in Human Cancer Cells

Byles, V., Chmilewski, L. K., Wang, J., Zhu, L., Forman, L. W., Faller, D. V., & Dai, Y. (2010) · International Journal of Biological Sciences · doi:10.7150/ijbs.6.599 · Cited by 125

Mitochondrial quality control: Easy come, easy go

Stotland, A. B., & Gottlieb, R. A. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.041 · Cited by 123

Nicotinamide improves motor deficits and upregulates PGC-1α and BDNF gene expression in a mouse model of Huntington's disease

Hathorn, T., Snyder-Keller, A., & Messer, A. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.08.017 · Cited by 123

PGC-1α at the intersection of bioenergetics regulation and neuron function: From Huntington's disease to Parkinson's disease and beyond

Tsunemi, T., & Spada, A. R. L. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.10.004 · Cited by 119

Mitochondrial defect and PGC-1α dysfunction in parkin-associated familial Parkinson's disease

Pacelli, C., Rasmo, D. D., Signorile, A., Grattagliano, I., Tullio, G. D., D’Orazio, A., Nico, B., Comi, G. P., Ronchi, D., Ferranini, E., et al. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.12.022 · Cited by 119

Effect of exercise intensity and AICAR on isoform-specific expressions of murine skeletal muscle PGC-1α mRNA: a role of β2-adrenergic receptor activation

Tadaishi, M., Miura, S., Kai, Y., Kawasaki, E., Koshinaka, K., Kawanaka, K., Nagata, J., Oishi, Y., & Ezaki, O. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00400.2010 · Cited by 109

Cross-talk between Sirtuin and Mammalian Target of Rapamycin Complex 1 (mTORC1) Signaling in the Regulation of S6 Kinase 1 (S6K1) Phosphorylation

Hong, S., Zhao, B., Lombard, D. B., Fingar, D. C., & Inoki, K. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.520734 · Cited by 101

PGC-1α is required for AICAR-induced expression of GLUT4 and mitochondrial proteins in mouse skeletal muscle

Leick, L., Fentz, J., Biensø, R. S., Knudsen, J. G., Jeppesen, J. F., Kiens, B., Wojtaszewski, J. F. P., & Pilegaard, H. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00648.2009 · Cited by 101

Nuclear SIRT1 activity, but not protein content, regulates mitochondrial biogenesis in rat and human skeletal muscle

Gurd, B. J., Yoshida, Y., McFarlan, J. T., Holloway, G. P., Moyes, C. D., Heigenhauser, G. J. F., Spriet, L. L., & Bonen, A. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00417.2010 · Cited by 101

Autophagy machinery in the context of mammalian mitophagy

Yoshii, S. R., & Mizushima, N. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.01.013 · Cited by 96

The deacetylase enzyme SIRT1 is not associated with oxidative capacity in rat heart and skeletal muscle and its overexpression reduces mitochondrial biogenesis

Gurd, B. J., Yoshida, Y., Lally, J., Holloway, G. P., & Bonen, A. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.168096 · Cited by 94

Sirtuin1 and autophagy protect cells from fluoride-induced cell stress

Suzuki, M., & Bartlett, J. D. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.11.023 · Cited by 87

The spatiotemporal regulation of the Keap1–Nrf2 pathway and its importance in cellular bioenergetics

Dinkova‐Kostova, A. T., Baird, L., Holmström, K. M., Meyer, C. J., & Abramov, A. Y. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150003 · Cited by 86

Linking sirtuins, IGF-I signaling, and starvation

Longo, V. D. (2008) · Experimental Gerontology · doi:10.1016/j.exger.2008.06.005 · Cited by 85

The genetics of Parkinson's disease

Mullin, S., & Schapira, A. H. V. (2015) · British Medical Bulletin · doi:10.1093/bmb/ldv022 · Cited by 81

Silent Information Regulator 2 (Sir2) and Forkhead Box O (FOXO) Complement Mitochondrial Dysfunction and Dopaminergic Neuron Loss in Drosophila PTEN-induced Kinase 1 (PINK1) Null Mutant

Koh, H., Kim, H., Kim, M. J., Park, J., Lee, H.-J., & Chung, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.337907 · Cited by 68

The Role of PGC-1α in the Pathogenesis of Neurodegenerative Disorders

Ròna-Vörös, K., & Weydt, P. (2010) · Current Drug Targets · doi:10.2174/1389450111007011262 · Cited by 66

Extranuclear Localization of SIRT1 and PGC-1α: An Insight into Possible Roles in Diseases Associated with Mitochondrial Dysfunction

Aquilano, K., Baldelli, S., Pagliei, B., & Ciriolo, M. R. (2012) · Current Molecular Medicine · doi:10.2174/156652413804486241 · Cited by 64

SIRT1, neuronal cell survival and the insulin/IGF-1 aging paradox

Tang, B. L. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.02.001 · Cited by 58

PGC‐1α: overexpression exacerbates β‐amyloid and tau deposition in a transgenic mouse model of Alzheimer's disease

Dumont, M., Stack, C., Elipenahli, C., Jainuddin, S., Launay, N., Gerges, M., Starkova, N. N., Starkov, A. A., Calingasan, N. Y., Tampellini, D., et al. (2014) · The FASEB Journal · doi:10.1096/fj.13-236331 · Cited by 51

PPARGC1A/PGC-1α, TFEB and enhanced proteostasis in Huntington disease

Spada, A. R. L. (2012) · Autophagy · doi:10.4161/auto.21862 · Cited by 50

Tumor Necrosis Factor Receptor-associated Protein 1 (TRAP1) Mutation and TRAP1 Inhibitor Gamitrinib-triphenylphosphonium (G-TPP) Induce a Forkhead Box O (FOXO)-dependent Cell Protective Signal from Mitochondria

Kim, H., Yang, J., Kim, M. J., Choi, S., Chung, J.-R., Kim, J., Yoo, Y. H., Chung, J., & Koh, H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.656934 · Cited by 40

Sirt1’s Complex Roles in Neuroprotection

Tang, B. L. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9414-2 · Cited by 37

Reduced expression of peroxisome-proliferator activated receptor gamma coactivator-1α enhances α-synuclein oligomerization and down regulates AKT/GSK3β signaling pathway in human neuronal cells that inducibly express α-synuclein

Ebrahim, A. S., Ko, L., & Yen, S.-H. C. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.02.034 · Cited by 34

Foxo3a targets mitochondria during guanosine 5′-triphosphate guided erythroid differentiation

Meshkini, A., & Yazdanparast, R. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.06.023 · Cited by 10

Extranuclear Localization of SIRT1 and PGC-1α: An Insight into Possible Roles in Diseases Associated with Mitochondrial Dysfunction

Aquilano, K., Baldelli, S., Pagliei, B., & Ciriolo, M. R. (2012) · Current Molecular Medicine · doi:10.2174/1566524011307010140 · Cited by 8

Mitochondrial Dysfunction and Oxidative Stress in Alzheimer’s Disease

Misrani, A., Tabassum, S., & Yang, L. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.617588 · Cited by 654

PGC-1 α , Inflammation, and Oxidative Stress: An Integrative View in Metabolism

Rius‐Pérez, S., Torres-Cuevas, I., Millán, I., Ortega, Á., & Pérez, S. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/1452696 · Cited by 671

Biological Activities of Stilbenoids

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NAD+ improves cognitive function and reduces neuroinflammation by ameliorating mitochondrial damage and decreasing ROS production in chronic cerebral hypoperfusion models through Sirt1/PGC-1α pathway

Zhao, Y., Zhang, J., Zheng, Y., Zhang, Y., Zhang, X. J., Wang, H., Du, Y., Guan, J., Wang, X., & Fu, J. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02250-8 · Cited by 362

The Role of Autophagy and Mitophagy in Bone Metabolic Disorders

Wang, S., Deng, Z., Ma, Y., Jin, J., Qi, F., Li, S., Liu, C., Lyu, F., & Zheng, Q. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.46627 · Cited by 333

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

The deacetylase enzyme SIRT1 is not associated with oxidative capacity in rat heart and skeletal muscle and its overexpression reduces mitochondrial biogenesis

Gurd, B. J., Yoshida, Y., Lally, J., Holloway, G. P., & Bonen, A. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.168096 · Cited by 94

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

Regulation of SIRT1 in aging: Roles in mitochondrial function and biogenesis

Cruzat, V. F. (2022) · Figshare · doi:10.25905/21555243

Relationship between Sirt1 expression and mitochondrial proteins during conditions of chronic muscle use and disuse

Chabi, B., Adhihetty, P. J., O′Leary, M. F. N., Menzies, K. J., & Hood, D. A. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91451.2008 · Cited by 64