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

Oxidants, oxidative stress and the biology of ageing

Finkel, T., & Holbrook, N. J. (2000) · Nature · doi:10.1038/35041687 · Cited by 9,413

Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1

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

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Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase

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

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hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase

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

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

Negative Control of p53 by Sir2α Promotes Cell Survival under Stress

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Peroxisome Proliferator-Activated Receptor-γ Coactivator 1α (PGC-1α): Transcriptional Coactivator and Metabolic Regulator

Puigserver, P., & Spiegelman, B. M. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0012 · Cited by 2,076

Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase

Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., Kessler, B., Howitz, K. T., Gorospe, M., de Cabo, R., & Sinclair, D. A. (2004) · Science · doi:10.1126/science.1099196 · Cited by 1,924

Small molecule activators of SIRT1 replicate signaling pathways triggered by calorie restriction in vivo

Smith, J. J., Kenney, R. D., Gagne, D. J., Frushour, B. P., Ladd, W., Galonek, H. L., Israelian, K., Song, J., Razvadauskaite, G., Lynch, A. V., et al. (2009) · BMC Systems Biology · doi:10.1186/1752-0509-3-31 · Cited by 186

Protective effects and mechanisms of sirtuins in the nervous system

Zhang, F., Wang, S., Gan, L., Vosler, P. S., Gao, Y., Zigmond, M. J., & Chen, J. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.09.001 · Cited by 211

Understanding the role of histone deacetylase and their inhibitors in neurodegenerative disorders: current targets and future perspective

Kumar, V., Kundu, S., Singh, A., & Singh, S. (2022) · Current Neuropharmacology · doi:10.2174/1570159x19666210609160017 · Cited by 210

Oleic acid stimulates complete oxidation of fatty acids through protein kinase A-dependent activation of SIRT1-PGC1α complex

Lim, J.-H., Gerhart-Hines, Z., Dominy, J. E., Lee, Y., Kim, S., Tabata, M., Xiang, Y. K., & Puigserver, P. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.415729 · Cited by 212

Protective Role of SIRT1 in Diabetic Vascular Dysfunction

Orimo, M., Minamino, T., Miyauchi, H., Tateno, K., Okada, S., Moriya, J., & Komuro, I. (2009) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.109.185694 · Cited by 209

Crystal Structures of Human SIRT3 Displaying Substrate-induced Conformational Changes

Jin, L., Wei, W., Jiang, Y., Peng, H., Cai, J., Mao, C., Dai, H., Choy, W., Bemis, J. E., Jirousek, M. R., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014928 · Cited by 211

Isoflavones Promote Mitochondrial Biogenesis

Rasbach, K. A., & Schnellmann, R. G. (2008) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.134882 · Cited by 202

Cellular Senescence, Vascular Disease, and Aging

Kovacic, J. C., Moreno, P., Hachinski, V., Nabel, E. G., & Fuster, V. (2011) · Circulation · doi:10.1161/circulationaha.110.007021 · Cited by 209

Calories and carcinogenesis: lessons learned from 30 years of calorie restriction research

Hursting, S. D., Smith, S. M., Lashinger, L. M., Harvey, A. E., & Perkins, S. N. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp280 · Cited by 209

Quantitative Acetylome Analysis Reveals the Roles of SIRT1 in Regulating Diverse Substrates and Cellular Pathways

Chen, Y., Zhao, W., Yang, J. S., Cheng, Z., Luo, H., Lu, Z., Tan, M., Gu, W. J., & Zhao, Y. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.019547 · Cited by 204

Mitochondria in Neurodegeneration

Lezi, E., & Swerdlow, R. H. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_12 · Cited by 213

Sirtuins, Aging, and MetabolismPreprint

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

Regulation of Cartilage-specific Gene Expression in Human Chondrocytes by SirT1 and Nicotinamide Phosphoribosyltransferase

Dvir‐Ginzberg, M., Gagarina, V., Lee, E. J., & Hall, D. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803196200 · Cited by 204

Deposition of 5-Methylcytosine on Enhancer RNAs Enables the Coactivator Function of PGC-1α

Aguiló, F., Li, S., Balasubramaniyan, N., Sancho, A., Benko, S., Zhang, F., Vashisht, A. A., Rengasamy, M., Andino, B., Chen, C., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.043 · Cited by 205

Nutritional Ketosis and Mitohormesis: Potential Implications for Mitochondrial Function and Human Health

Miller, V. J., Villamena, F. A., & Volek, J. S. (2018) · Journal of Nutrition and Metabolism · doi:10.1155/2018/5157645 · Cited by 205

Multi-regulatory network of ROS: the interconnection of ROS, PGC-1 alpha, and AMPK-SIRT1 during exercise.

Thirupathi, A., & de Souza, C. T. (2017) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-017-0576-y · Cited by 198

Oxidative Stress in Ischemia/Reperfusion Injuries following Acute Ischemic Stroke

Jurcău, A., & Ardelean, A. I. (2022) · Biomedicines · doi:10.3390/biomedicines10030574 · Cited by 204

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

Sirtuins' modulation of autophagy

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

Transcription factors and coactivators controlling nutrient and hormonal regulation of hepatic gluconeogenesis

Jitrapakdee, S. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.10.001 · Cited by 202

SIRT1 and SIRT2 Activity Control in Neurodegenerative Diseases

Manjula, R., Anuja, K., & Alcain, F. J. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.585821 · Cited by 197

Mitochondrial Hormesis and Diabetic Complications

Sharma, K. (2015) · Diabetes · doi:10.2337/db14-0874 · Cited by 194

NAD+/NADH and skeletal muscle mitochondrial adaptations to exercise

White, A. T., & Schenk, S. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00054.2012 · Cited by 199

Reversible acetylation of PGC-1: connecting energy sensors and effectors to guarantee metabolic flexibility

Jeninga, E. H., Schoonjans, K., & Auwerx, J. H. (2010) · Oncogene · doi:10.1038/onc.2010.206 · Cited by 197

Targeting Mitochondrial Biogenesis with Polyphenol Compounds

Chodari, L., Aytemir, M. D., Vahedi, P., Alipour, M., Vahed, S. Z., Khatibi, S. M. H., Ahmadian, E., Ardalan, M., & Eftekhari, A. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/4946711 · Cited by 200

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

Genetics of Aging in Caenorhabditis elegans

Antebi, A. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030129 · Cited by 190

The Role of PGC1α in Cancer Metabolism and its Therapeutic Implications

Tan, Z., Luo, X., Xiao, L., Tang, M., Bode, A. M., Dong, Z., & Cao, Y. (2016) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-15-0621 · Cited by 198

MicroRNA Regulation of SIRT1

Yamakuchi, M. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00068 · Cited by 196

Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity

Gao, Z., Zhang, J., Kheterpal, I., Kennedy, N., Davis, R. J., & Ye, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.228874 · Cited by 187

SCFCdc4 acts antagonistically to the PGC-1α transcriptional coactivator by targeting it for ubiquitin-mediated proteolysisPreprint

Olson, B. L., Hock, M. B., Ekholm‐Reed, S., Wohlschlegel, J. A., Dev, K. K., Kralli, A., & Reed, S. I. (2008) · Genes & Development · doi:10.1101/gad.1624208 · Cited by 189

Browsing the oldest antioxidant enzyme: catalase and its multiple regulation in cancer

Galasso, M., Gambino, S., Romanelli, M. G., Donadelli, M., & Scupoli, M. T. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.06.010 · Cited by 184

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

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 190

Resveratrol and Neurodegenerative Diseases: Activation of SIRT1 as the Potential Pathway towards Neuroprotection

Pallàs, M., Casadesús, G., Smith, M. A., Coto‐Montes, A. M., Pelegrı́, C., Vilaplana, J., & Camins, A. (2009) · Current Neurovascular Research · doi:10.2174/156720209787466019 · Cited by 184

Regulatory circuits controlling white versus brown adipocyte differentiation

Hansen, J. B., & Kristiansen, K. (2006) · Biochemical Journal · doi:10.1042/bj20060402 · Cited by 178

Cytoplasmic and Mitochondrial NADPH-Coupled Redox Systems in the Regulation of Aging

Bradshaw, P. C. (2019) · Nutrients · doi:10.3390/nu11030504 · Cited by 178

Redox regulation of mitochondrial biogenesis

Piantadosi, C. A., & Suliman, H. B. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.014 · Cited by 183

SIRT1 and AMPK in regulating mammalian senescence: A critical review and a working model

Wang, Y., Liang, Y. Q., & Vanhoutte, P. M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.11.047 · Cited by 178

Opposing Effects of Sirtuins on Neuronal Survival: SIRT1-Mediated Neuroprotection Is Independent of Its Deacetylase Activity

Pfister, J. A., Ma, C., Morrison, B. E., & D’Mello, S. R. (2008) · PLoS ONE · doi:10.1371/journal.pone.0004090 · Cited by 178

Is Mitochondrial Dysfunction a Common Root of Noncommunicable Chronic Diseases?

Díaz‐Vegas, A., Sánchez-Aguilera, P., Krycer, J. R., Morales, P. E., Monsalves‐Álvarez, M., Cifuentes, M., Rothermel, B. A., & Lavandero, S. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnaa005 · Cited by 179

The expression of SIRT1 in nonalcoholic fatty liver disease induced by high‐fat diet in rats

Deng, X., Chen, L., & Li, N. (2007) · Liver International · doi:10.1111/j.1478-3231.2007.01497.x · Cited by 179

Disruption of Sirt1 in chondrocytes causes accelerated progression of osteoarthritis under mechanical stress and during ageing in mice

Matsuzaki, T., Matsushita, T., Takayama, K., Matsumoto, T., Nishida, K., Kuroda, R., & Kurosaka, M. (2013) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2012-202620 · Cited by 178

Exercise training attenuates aging-associated mitochondrial dysfunction in rat skeletal muscle: Role of PGC-1α

Kang, C., Chung, E., Diffee, G., & Ji, L. L. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.08.004 · Cited by 174

Sirtuins: Molecular Traffic Lights in the Crossroad of Oxidative Stress, Chromatin Remodeling, and Transcription

Rajendran, R., Garva, R., Krstic–Demonacos, M., & Demonacos, C. (2011) · BioMed Research International · doi:10.1155/2011/368276 · Cited by 180

Exercise-induced hormesis and skeletal muscle health

Ji, L. L., Kang, C., & Zhang, Y. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.02.025 · Cited by 182

The role of sirtuins in aging and age-related diseases

Wątroba, M., & Szukiewicz, D. (2015) · Advances in Medical Sciences · doi:10.1016/j.advms.2015.09.003 · Cited by 190

Role of mitochondrial homeostasis and dynamics in Alzheimer's disease

Selfridge, J. E., E, L., Lu, J., & Swerdlow, R. H. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.057 · Cited by 175

Paths of Convergence: Sirtuins in Aging and Neurodegeneration

Gan, L., & Mucke, L. (2008) · Neuron · doi:10.1016/j.neuron.2008.03.015 · Cited by 173

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

Chen, L., Qin, Y. H., Liu, B., Gao, M. Q., Li, A., Li, X., & Gong, G. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.871357 · Cited by 186

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

The Direct Involvement of SirT1 in Insulin-induced Insulin Receptor Substrate-2 Tyrosine Phosphorylation

Zhang, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706644200 · Cited by 175

High Levels of SIRT1 Expression as a Protective Mechanism Against Disease-Related Conditions

Elibol, B., & Kilic, U. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00614 · Cited by 171

Accelerated recovery of renal mitochondrial and tubule homeostasis with SIRT1/PGC-1α activation following ischemia–reperfusion injury

Funk, J. A., & Schnellmann, R. G. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.09.026 · Cited by 174

Mitochondrial NAD + /NADH Redox State and Diabetic Cardiomyopathy

Berthiaume, J. M., Kurdys, J., Muntean, D. M., & Rosca, M. G. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7415 · Cited by 169

SIRT1 stimulation by polyphenols is affected by their stability and metabolism

de Boer, V. C. J., de Goffau, M. C., Arts, I. C. W., Hollman, P. C. H., & Keijer, J. (2006) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2006.02.007 · Cited by 168

The emerging role of alternative splicing in senescence and aging

Deschênes, M., & Chabot, B. (2017) · Aging Cell · doi:10.1111/acel.12646 · Cited by 172

Sirtuin 1-mediated Effects of Exercise and Resveratrol on Mitochondrial Biogenesis

Menzies, K. J., Singh, K., Saleem, A., & Hood, D. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.431155 · Cited by 171

Gallic Acid Regulates Body Weight and Glucose Homeostasis Through AMPK Activation

Doan, K. V., Ko, C. M., Kinyua, A. W., Yang, D. J., Choi, Y., Oh, I. Y., Nguyen, N. M., Ko, A., Choi, J. W., Jeong, Y., et al. (2014) · Endocrinology · doi:10.1210/en.2014-1354 · Cited by 171

Clock Genes and Clock-Controlled Genes in the Regulation of Metabolic Rhythms

Mazzoccoli, G., Pazienza, V., & Vinciguerra, M. (2012) · Chronobiology International · doi:10.3109/07420528.2012.658127 · Cited by 173

Nuclear Perilipin 5 integrates lipid droplet lipolysis with PGC-1α/SIRT1-dependent transcriptional regulation of mitochondrial function

Gallardo-Montejano, V. I., Saxena, G., Kusminski, C. M., Yang, C., McAfee, J. L., Hahner, L., Hoch, K. M., Dubinsky, W. P., Narkar, V. A., & Bickel, P. E. (2016) · Nature Communications · doi:10.1038/ncomms12723 · Cited by 167

Signaling pathway cross talk in Alzheimer’s disease

Godoy, J. A., Ríos, J. A., Zolezzi, J. M., Braidy, N., & Inestrosa, N. C. (2014) · Cell Communication and Signaling · doi:10.1186/1478-811x-12-23 · Cited by 165

Mitochondrial Dysfunction in Diabetic Neuropathy: a Series of Unfortunate Metabolic Events

Fernyhough, P. (2015) · Current Diabetes Reports · doi:10.1007/s11892-015-0671-9 · Cited by 173

PGC-1α in aging and anti-aging interventions

Anderson, R., & Prolla, T. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.04.005 · Cited by 162

MicroRNA‐146b promotes adipogenesis by suppressing the SIRT1‐FOXO1 cascade

Ahn, J., Lee, H., Jung, C. H., Jeon, T. I., & Ha, T. Y. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201302647 · Cited by 166

Unravelling the mechanisms regulating muscle mitochondrial biogenesis

Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159

Shift Work or Food Intake during the Rest Phase Promotes Metabolic Disruption and Desynchrony of Liver Genes in Male Rats

Salgado‐Delgado, R., Saderi, N., Basualdo, M. D. C., Guerrero‐Vargas, N. N., Escobar, C., & Buijs, R. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060052 · Cited by 164

Sirtuin 1 inhibition delays cyst formation in autosomal-dominant polycystic kidney disease

Zhou, X., Fan, L. X., Sweeney, W. E., Denu, J. M., Avner, E. D., & Li, X. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64401 · Cited by 158

Activation of peroxisome proliferator-activated receptor-γ coactivator 1α ameliorates mitochondrial dysfunction and protects podocytes from aldosterone-induced injury

Yuan, Y., Huang, S., Wang, W., Wang, Y., Zhang, P., Zhu, C., Ding, G., Liu, B., Yang, T., & Zhang, A. (2012) · Kidney International · doi:10.1038/ki.2012.188 · Cited by 159

SIRT1/PGC-1α Signaling Promotes Mitochondrial Functional Recovery and Reduces Apoptosis after Intracerebral Hemorrhage in Rats

Zhou, Y., Wang, S., Li, Y., Yu, S., & Zhao, Y. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00443 · Cited by 161

Brain SIRT1 Mediates Metabolic Homeostasis and Neuroprotection

Xu, J., Jackson, C. W., Khoury, N., Escobar, I., & Pérez‐Pinzón, M. A. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00702 · Cited by 158

Asiatic acid, a pentacyclic triterpene in Centella asiatica, attenuates glutamate-induced cognitive deficits in mice and apoptosis in SH-SY5Y cells

Xu, M.-F., Xiong, Y.-Y., Liu, J.-K., Qian, J.-J., Zhu, L., & Gao, J. (2012) · Acta Pharmacologica Sinica · doi:10.1038/aps.2012.3 · Cited by 156

Resveratrol Induces Brain Resilience Against Alzheimer Neurodegeneration Through Proteostasis Enhancement

Corpas, R., Griñán‐Ferré, C., Rodrı́guez-Farré, E., Pallàs, M., & Sanfeliu, C. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1157-y · Cited by 164

Sirtuin Functions in Female Fertility: Possible Role in Oxidative Stress and Aging

Tatone, C., Emidio, G. D., Vitti, M., Carlo, M. D., Santini, S. J., D’Alessandro, A. M., Falone, S., & Amicarelli, F. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/659687 · Cited by 157

Inhibition of SIRT1 Impairs the Accumulation and Transcriptional Activity of HIF-1α Protein under Hypoxic Conditions

Laemmle, A., Lechleiter, A., Roh, V., Schwarz, C., Portmann, S., Furer, C., Keogh, A., Tschan, M. P., Candinas, D., Vorburger, S. A., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033433 · Cited by 156

Age-Associated declines in mitochondrial biogenesis and protein quality control factors are minimized by exercise training

Koltai, E., Hart, N., Taylor, A. W., Goto, S., Ngo, J. K., Davies, K. J. A., & Radak, Z. (2012) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00337.2011 · Cited by 152

SRT1720 Induces Mitochondrial Biogenesis and Rescues Mitochondrial Function after Oxidant Injury in Renal Proximal Tubule Cells

Funk, J. A., Odejinmi, S. I., & Schnellmann, R. G. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.109.161992 · Cited by 156

A potent and selective Sirtuin 1 inhibitor alleviates pathology in multiple animal and cell models of Huntington's disease

Smith, M. R., Syed, A., Lukácsovich, T., Purcell, J., Barbaro, B. A., Worthge, S. A., Wei, S. R., Pollio, G., Magnoni, L., Scali, C., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu010 · Cited by 152

The Effects of Resveratrol on Inflammation and Oxidative Stress in a Rat Model of Chronic Obstructive Pulmonary Disease

Wang, X., Li, T., Li, J., Miao, S.-Y., & Xiao, X. (2017) · Molecules · doi:10.3390/molecules22091529 · Cited by 151

Cardioprotection of CAPE-oNO2 against myocardial ischemia/reperfusion induced ROS generation via regulating the SIRT1/eNOS/NF-κB pathway in vivo and in vitro

Li, D., Wang, X., Huang, Q., Li, S., Zhou, Y. L., & Li, Z. (2017) · Redox Biology · doi:10.1016/j.redox.2017.11.023 · Cited by 152

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

Dusabimana, T., Kim, S. R., Kim, H. J., Park, S. W., & Kim, H. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0245-z · Cited by 151

Neuronal protection by sirtuins in Alzheimer's disease

Anekonda, T. S., & Reddy, P. H. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03492.x · Cited by 152

Alternative mRNA Splicing Produces a Novel Biologically Active Short Isoform of PGC-1α

Zhang, Y., Huypens, P., Adamson, A. W., Chang, J. S., Henagan, T. M., Boudreau, A., Lenard, N. R., Burk, D. H., Klein, J. C., Perwitz, N., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.037556 · Cited by 152

Mitochondria and PGC-1α in Aging and Age-Associated Diseases

Wenz, T. (2011) · Journal of Aging Research · doi:10.4061/2011/810619 · Cited by 152

Janus‐faced role of SIRT1 in tumorigenesis

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MicroRNA-149 Inhibits PARP-2 and Promotes Mitochondrial Biogenesis via SIRT-1/PGC-1α Network in Skeletal Muscle

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Interplay between oxidative stress, SIRT1, reproductive and metabolic functions

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Biological and Potential Therapeutic Roles of Sirtuin Deacetylases

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Deacetylation of the retinoblastoma tumour suppressor protein by SIRT1

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SIRT1: Regulator of p53 Deacetylation

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The caloric restriction paradigm: Implications for healthy human aging

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Hepatic lipid metabolism and non-alcoholic fatty liver disease in aging

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Mechanism-Based Inhibition of Sir2 Deacetylases by Thioacetyl-Lysine Peptide

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Reactive Oxygen Species–Mediated Mitochondria-to-Nucleus Signaling: A Key to Aging and Radical-Caused Diseases

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Salmonella Typhimurium disrupts Sirt1/AMPK checkpoint control of mTOR to impair autophagy

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Sirtuins and Insulin Resistance

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Mitochondrial gene expression and increased oxidative metabolism: Role in increased lifespan of fat-specific insulin receptor knock-out mice

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Emerging beneficial roles of sirtuins in heart failure

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PGC-1α: a potent transcriptional cofactor involved in the pathogenesis of type 2 diabetes

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Sirt1 and the Mitochondria

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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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Identification of cofactor network, including SIRT1 and SRC-3, which converges on energy expenditure through PGC-1α

Lagouge, M. (2008) · Serveur des thèses de l'Université de Strasbourg (University of Strasbourg)

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

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Metabolic adaptations through the PGC‐1α and SIRT1 pathways

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