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 · 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

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

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 · 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

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 · 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

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 · 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

Sirtuin activators mimic caloric restriction and delay ageing in metazoans

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

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 1,751 · see citing works

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 · see citing works

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 · see citing works

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

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

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

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

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

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

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

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 1,352 · see citing works

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 · see citing works

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 · see citing works

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 1,239 · 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

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 · see citing works

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

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

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

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

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 1,038 · see citing works

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 · see citing works

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 · see citing works

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 · 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

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 876 · see citing works

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 854 · 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

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 · see citing works

Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

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

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 · 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

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 · 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

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 · see citing works

Sirt1 Extends Life Span and Delays Aging in Mice through the Regulation of Nk2 Homeobox 1 in the DMH and LH

Satoh, A., Brace, C. S., Rensing, N., Cliften, P. F., Wozniak, D. F., Herzog, E. D., Yamada, K. A., & Imai, S. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.07.013 · Cited by 734 · see citing works

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 · 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

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 · 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

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

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

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 620 · see citing works

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., Yen, E. S., Lamming, D. W., et al. (2013) · Science · doi:10.1126/science.1231097 · Cited by 618 · 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

The Mammalian SIR2α Protein Has a Role in Embryogenesis and Gametogenesis

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

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 606 · see citing works

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

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

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 458 · see citing works

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

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

The SIRT1 Activator SRT1720 Extends Lifespan and Improves Health of Mice Fed a Standard Diet

Mitchell, S. J., Martín‐Montalvo, A., Mercken, E. M., Palacios, H. H., Ward, T. M., Abulwerdi, G. A., Minor, R. K., Vlasuk, G. P., Ellis, J. L., Sinclair, D. A., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.01.031 · Cited by 399 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 371 · see citing works

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 368 · see citing works

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 355 · see citing works

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 · see citing works

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 336 · see citing works

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 320 · see citing works

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

Mudó, G., Mäkelä, J., Liberto, V. D., Tselykh, T. V., Olivieri, M., Piepponen, P., Eriksson, O., Mälkiä, A., Bonomo, A., Kairisalo, M., et al. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0850-z · Cited by 315 · see citing works

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 307 · see citing works

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 · see citing works

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 · see citing works

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× · see citing works

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

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

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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

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

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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

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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

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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

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Cytoplasm‐localized SIRT1 enhances apoptosis

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

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PPAR control: it's SIRTainly as easy as PGC

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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

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

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

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Maintaining Ancient Organelles

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Does calorie restriction induce mitochondrial biogenesis? A reevaluation

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Nicotinamide enhances mitochondria quality through autophagy activation in human cells

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

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

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

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

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Mitochondrial quality control: Easy come, easy go

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

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

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

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

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

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

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Autophagy machinery in the context of mammalian mitophagy

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Sirtuin1 and autophagy protect cells from fluoride-induced cell stress

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

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Linking sirtuins, IGF-I signaling, and starvation

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The genetics of Parkinson's disease

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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

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

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

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

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

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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

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Sirt1’s Complex Roles in Neuroprotection

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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

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

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Mitochondrial Dysfunction and Oxidative Stress in Alzheimer’s Disease

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

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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

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The Role of Autophagy and Mitophagy in Bone Metabolic Disorders

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Mitochondrial dysfunction in neurodegenerative diseases and the potential countermeasure

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Sirtuins and Their Roles in Brain Aging and Neurodegenerative Disorders

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Mechanisms Leading to Differential Hypoxia-Inducible Factor Signaling in the Diabetic Kidney: Modulation by SGLT2 Inhibitors and Hypoxia Mimetics

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The pleiotropic neuroprotective effects of resveratrol in cognitive decline and Alzheimer’s disease pathology: From antioxidant to epigenetic therapy

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Mesenchymal stem cell secretome for regenerative medicine: Where do we stand?

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Mitochondria as an important target of metformin: The mechanism of action, toxic and side effects, and new therapeutic applications

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SIRT1 and SIRT2 Activity Control in Neurodegenerative Diseases

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Hepatic stellate cell senescence in liver fibrosis: Characteristics, mechanisms and perspectives

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PGC-1α-Mediated Mitochondrial Quality Control: Molecular Mechanisms and Implications for Heart Failure

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Energy Metabolism Decline in the Aging Brain—Pathogenesis of Neurodegenerative Disorders

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Deregulated mitochondrial microRNAs in Alzheimer's disease: Focus on synapse and mitochondria

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Brain SIRT1 Mediates Metabolic Homeostasis and Neuroprotection

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Resveratrol Induces Brain Resilience Against Alzheimer Neurodegeneration Through Proteostasis Enhancement

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Unraveling the AMPK-SIRT1-FOXO Pathway: The In-Depth Analysis and Breakthrough Prospects of Oxidative Stress-Induced Diseases

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Idiopathic Pulmonary Fibrosis: Aging, Mitochondrial Dysfunction, and Cellular Bioenergetics

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Nobiletin ameliorates hepatic ischemia and reperfusion injury through the activation of SIRT-1/FOXO3a-mediated autophagy and mitochondrial biogenesis

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Protective Effects of Curcumin in Cardiovascular Diseases—Impact on Oxidative Stress and Mitochondria

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Sirt1: A Guardian of the Development of Diabetic Retinopathy

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SIRT1 in forebrain excitatory neurons produces sexually dimorphic effects on depression-related behaviors and modulates neuronal excitability and synaptic transmission in the medial prefrontal cortex

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Oxidative Stress, Neuroinflammation and Mitochondria in the Pathophysiology of Amyotrophic Lateral Sclerosis

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Sepsis is associated with mitochondrial DNA damage and a reduced mitochondrial mass in the kidney of patients with sepsis-AKI

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PGC-1α affects skeletal muscle and adipose tissue development by regulating mitochondrial biogenesis

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Pharmacological advances in mitochondrial therapy

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Ameliorating Mitochondrial Dysfunction of Neurons by Biomimetic Targeting Nanoparticles Mediated Mitochondrial Biogenesis to Boost the Therapy of Parkinson's Disease

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Modulation of miR-34a/SIRT1 signaling protects cochlear hair cells against oxidative stress and delays age-related hearing loss through coordinated regulation of mitophagy and mitochondrial biogenesis

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MicroRNAs: pioneering regulators in Alzheimer’s disease pathogenesis, diagnosis, and therapy

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Pyrroloquinoline quinone promotes mitochondrial biogenesis in rotenone-induced Parkinson’s disease model via AMPK activation

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Phosphodiesterase Inhibitors for Alzheimer’s Disease: A Systematic Review of Clinical Trials and Epidemiology with a Mechanistic Rationale

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Mitochondria, Telomeres and Telomerase Subunits

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Ramadan diurnal intermittent fasting modulates SOD2, TFAM, Nrf2, and sirtuins (SIRT1, SIRT3) gene expressions in subjects with overweight and obesity

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Autophagy-dependent and -independent modulation of oxidative and organellar stress in the diabetic heart by glucose-lowering drugs

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Sirtuins, resveratrol and the intertwining cellular pathways connecting them

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