PGC-1 coactivators: inducible regulators of energy metabolism in health and disease

PGC-1α-responsive genes involved in oxidative phosphorylation are coordinately downregulated in human diabetes

Mootha, V. K., Lindgren, C. M., Eriksson, K.-F., Subramanian, A., Sihag, S., Lehar, J., Puigserver, P., Carlsson, E., Ridderstråle, M., Laurila, E., et al. (2003) · Nature Genetics · doi:10.1038/ng1180 · Cited by 10,197

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

Transcriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres

Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546

Insulin-regulated hepatic gluconeogenesis through FOXO1–PGC-1α interaction

Puigserver, P., Rhee, J., Donovan, J., Walkey, C. J., Yoon, J. C., Oriente, F., Kitamura, Y., Altomonte, J., Dong, H., Accili, D., et al. (2003) · Nature · doi:10.1038/nature01667 · Cited by 1,487

Peroxisome-Proliferator-Activated Receptor δ Activates Fat Metabolism to Prevent Obesity

Wang, Y.-X., Lee, C.-H., Tiep, S., Yu, R. T., Ham, J., Kang, H., & Evans, R. M. (2003) · Cell · doi:10.1016/s0092-8674(03)00269-1 · Cited by 1,296

Peroxisome proliferator–activated receptor γ coactivator-1 promotes cardiac mitochondrial biogenesis

Lehman, J. J., Barger, P. M., Kovacs, A., Saffitz, J. E., Medeiros, D. M., & Kelly, D. P. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10268 · Cited by 1,285

Defects in Adaptive Energy Metabolism with CNS-Linked Hyperactivity in PGC-1α Null Mice

Lin, J., Wu, P.-H., Tarr, P. T., Lindenberg, K. S., St-Pierre, J., Zhang, C.-Y., Mootha, V. K., Jäger, S., Vianna, C. R., Reznick, R. M., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.013 · Cited by 1,162

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

Adaptations of skeletal muscle to exercise: rapid increase in the transcriptional coactivator PGC-1

Baar, K., Wende, A. R., Jones, T. E., Marison, M., Nolte, L. A., Chen, M., Kelly, D. P., & Holloszy, J. O. (2002) · The FASEB Journal · doi:10.1096/fj.02-0367com · Cited by 1,020

PGC-1α Deficiency Causes Multi-System Energy Metabolic Derangements: Muscle Dysfunction, Abnormal Weight Control and Hepatic Steatosis

Leone, T. C., Lehman, J. J., Finck, B. N., Schaeffer, P. J., Wende, A. R., Boudina, S., Courtois, M., Wozniak, D. F., Sambandam, N., Bernal-Mizrachi, C., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030101 · Cited by 951

Adipocyte dysfunctions linking obesity to insulin resistance and type 2 diabetes.

Guilherme, A., Virbasius, J. V., Puri, V., & Czech, M. P. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2391 · Cited by 2,292

Transcriptional paradigms in mammalian mitochondrial biogenesis and function

Scarpulla, R. C. (2008) · Physiological Reviews · doi:10.1152/physrev.00025.2007 · Cited by 1,666

mTOR controls mitochondrial oxidative function through a YY1–PGC-1α transcriptional complex

Cunningham, J. T., Rodgers, J. T., Arlow, D. H., Vazquez, F., Mootha, V. K., & Puigserver, P. (2007) · Nature · doi:10.1038/nature06322 · Cited by 1,488

Exercise induces hippocampal BDNF through a PGC-1α/FNDC5 pathway

Wrann, C. D., White, J. P., Salogiannnis, J., Laznik-Bogoslavski, D., Wu, J., Ma, D., Lin, J. D., Greenberg, M. E., & Spiegelman, B. M. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.09.008 · Cited by 1,440

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

Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network

Scarpulla, R. C. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.09.019 · Cited by 1,281

Role of Mitochondrial Dysfunction in Insulin Resistance

Kim, J.-A., Wei, Y., & Sowers, J. R. (2008) · Circulation Research · doi:10.1161/circresaha.107.165472 · Cited by 1,103

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

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

TFEB controls cellular lipid metabolism through a starvation-induced autoregulatory loop

Settembre, C., De Cegli, R., Mansueto, G., Saha, P. K., Vetrini, F., Visvikis, O., Huynh, T., Carissimo, A., Palmer, D., Jürgen Klisch, T., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2718 · Cited by 1,022

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

The emerging role of Nrf2 in mitochondrial function

Dinkova-Kostova, A. T., & Abramov, A. Y. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.04.036 · Cited by 983

PGC-1α protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription

Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607795103 · Cited by 974

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

The Tumor Microenvironment Represses T Cell Mitochondrial Biogenesis to Drive Intratumoral T Cell Metabolic Insufficiency and Dysfunction

Scharping, N. E., Menk, A. V., Moreci, R. S., Whetstone, R. D., Dadey, R. E., Watkins, S. C., Ferris, R. L., & Delgoffe, G. M. (2016) · Immunity · doi:10.1016/j.immuni.2016.07.009 · Cited by 848

Oncogenic BRAF Regulates Oxidative Metabolism via PGC1α and MITF

Haq, R., Shoag, J., Andreu-Perez, P., Yokoyama, S., Edelman, H., Rowe, G. C., Frederick, D. T., Hurley, A. D., Nellore, A., Kung, A. L., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.02.003 · Cited by 818

Transcriptional integration of mitochondrial biogenesis

Scarpulla, R. C., Vega, R. B., & Kelly, D. P. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.06.006 · Cited by 798

The Molecular Bases of Training Adaptation

Coffey, V. G., & Hawley, J. A. (2007) · Sports Medicine · doi:10.2165/00007256-200737090-00001 · Cited by 756

Sirtuin 3, a New Target of PGC-1α, Plays an Important Role in the Suppression of ROS and Mitochondrial Biogenesis

Kong, X., Wang, R., Xue, Y., Liu, X., Zhang, H., Chen, Y., Fang, F., & Chang, Y. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011707 · Cited by 718

FGF21 induces PGC-1α and regulates carbohydrate and fatty acid metabolism during the adaptive starvation response

Potthoff, M. J., Inagaki, T., Satapati, S., Ding, X., He, T., Goetz, R., Mohammadi, M., Finck, B. N., Mangelsdorf, D. J., Kliewer, S. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904187106 · Cited by 704

The Redox Code

Jones, D. P., & Sies, H. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6247 · Cited by 647

Endurance Exercise as a Countermeasure for Aging

Lanza, I. R., Short, D. K., Short, K. R., Raghavakaimal, S., Basu, R., Joyner, M. J., McConnell, J. P., & Nair, K. S. (2008) · Diabetes · doi:10.2337/db08-0349 · Cited by 582

PGC-1α Is a Master Regulator of Mitochondrial Lifecycle and ROS Stress Response

Abu Shelbayeh, O., Arroum, T., Morris, S., & Busch, K. B. (2023) · Antioxidants · doi:10.3390/antiox12051075 · Cited by 552

PINK1 and Parkin mitochondrial quality control: a source of regional vulnerability in Parkinson’s disease

Ge, P., Dawson, V. L., & Dawson, T. M. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00367-7 · Cited by 496

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

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

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

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

Common Inherited Variation in Mitochondrial Genes Is Not Enriched for Associations with Type 2 Diabetes or Related Glycemic Traits

Segrè, A. V., DIAGRAM Consortium, MAGIC investigators, Groop, L., Mootha, V. K., Daly, M. J., & Altshuler, D. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001058 · Cited by 463

FGF15/19 Regulates Hepatic Glucose Metabolism by Inhibiting the CREB-PGC-1α Pathway

Potthoff, M. J., Boney-Montoya, J., Choi, M., He, T., Sunny, N. E., Satapati, S., Suino-Powell, K., Xu, H. E., Gerard, R. D., Finck, B. N., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.019 · Cited by 431

Oleate Reverses Palmitate-induced Insulin Resistance and Inflammation in Skeletal Muscle Cells

Coll, T., Eyre, E., Rodríguez-Calvo, R., Palomer, X., Sánchez, R. M., Merlos, M., Laguna, J. C., & Vázquez-Carrera, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708700200 · Cited by 347

Muscle as a “Mediator” of Systemic Metabolism

Baskin, K. K., Winders, B. R., & Olson, E. N. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2014.12.021 · Cited by 333

Transcriptional coactivators PGC-1α and PGC-lβ control overlapping programs required for perinatal maturation of the heart

Lai, L., Leone, T. C., Zechner, C., Schaeffer, P. J., Kelly, S. M., Flanagan, D. P., Medeiros, D. M., Kovacs, A., & Kelly, D. P. (2008) · Genes & Development · doi:10.1101/gad.1661708 · Cited by 326

Transcriptional coregulators in the control of energy homeostasis

Feige, J. N., & Auwerx, J. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.04.001 · Cited by 325

Role of PGC-1α Signaling in Skeletal Muscle Health and Disease

Kang, C., & Li Ji, L. (2012) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2012.06738.x · Cited by 291

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

Caloric Restriction and Aging: Studies in Mice and Monkeys

Anderson, R. M., Shanmuganayagam, D., & Weindruch, R. (2009) · Toxicologic Pathology · doi:10.1177/0192623308329476 · Cited by 276

Total Skeletal Muscle PGC-1 Deficiency Uncouples Mitochondrial Derangements from Fiber Type Determination and Insulin Sensitivity

Zechner, C., Lai, L., Zechner, J. F., Geng, T., Yan, Z., Rumsey, J. W., Collia, D., Chen, Z., Wozniak, D. F., Leone, T. C., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.008 · Cited by 274

Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1 and causes obesity and defective thermogenesis in mice

Quirós, P. M., Ramsay, A. J., Sala, D., Fernández‐Vizarra, E., Rodríguez, F., Peinado, J. R., Fernández‐García, M. S., Vega, J. A., Enríquez, J. A., Zorzano, A., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.70 · Cited by 269

PGC-1β controls mitochondrial metabolism to modulate circadian activity, adaptive thermogenesis, and hepatic steatosis

Sonoda, J., Mehl, I. R., Chong, L.-W., Nofsinger, R. R., & Evans, R. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611623104 · Cited by 266

A role for the transcriptional coactivator PGC-1α in muscle refueling.

Wende, A. R., Schaeffer, P. J., Parker, G. J., Zechner, C., Han, D.-H., Chen, M. M., Hancock, C. R., Lehman, J. J., Huss, J. M., McClain, D. A., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707006200 · Cited by 257

ERRα: a metabolic function for the oldest orphan

Villena, J. A., & Kralli, A. (2008) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2008.07.005 · Cited by 252

Insulin resistance induced by physical inactivity is associated with multiple transcriptional changes in skeletal muscle in young men

Alibegovic, A. C., Sonne, M. P., Højbjerre, L., Bork-Jensen, J., Jacobsen, S., Nilsson, E., Færch, K., Hiscock, N., Mortensen, B., Friedrichsen, M., et al. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00590.2009 · Cited by 247

CD36 Deficiency Rescues Lipotoxic Cardiomyopathy

Yang, J., Sambandam, N., Han, X., Gross, R. W., Courtois, M., Kovacs, A., Febbraio, M., Finck, B. N., & Kelly, D. P. (2007) · Circulation Research · doi:10.1161/01.res.0000264104.25265.b6 · Cited by 246

PGC-1α Regulates Expression of Myocardial Mitochondrial Antioxidants and Myocardial Oxidative Stress After Chronic Systolic Overload

Lu, Z., Xu, X., Hu, X., Fassett, J., Zhu, G., Tao, Y., Li, J., Huang, Y., Zhang, P., Zhao, B., et al. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2940 · Cited by 215

Integrative regulation of physiology by histone deacetylase 3

Emmett, M. J., & Lazar, M. A. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0076-0 · Cited by 202

The coordination of nuclear and mitochondrial communication during aging and calorie restriction

Finley, L. W. S., & Haigis, M. C. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.03.003 · Cited by 207

Chronic lymphocytic leukemia cells impair mitochondrial fitness in CD8+ T cells and impede CAR T-cell efficacy

van Bruggen, J. A. C., Martens, A. W. J., Fraietta, J. A., Hofland, T., Tonino, S. H., Eldering, E., Levin, M.-D., Siska, P. J., Endstra, S., Rathmell, J. C., et al. (2019) · Blood · doi:10.1182/blood.2018885863 · Cited by 187

Mitochondrial abnormalities in temporal lobe of autistic brain

Tang, G., Gutierrez Rios, P., Kuo, S.-H., Akman, H. O., Rosoklija, G., Tanji, K., Dwork, A., Schon, E. A., DiMauro, S., Goldman, J., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.01.006 · Cited by 194

Chemical Hybridization of Glucagon and Thyroid Hormone Optimizes Therapeutic Impact for Metabolic Disease

Finan, B., Clemmensen, C., Zhu, Z., Stemmer, K., Gauthier, K., Müller, L., De Angelis, M., Moreth, K., Neff, F., Perez-Tilve, D., et al. (2016) · Cell · doi:10.1016/j.cell.2016.09.014 · Cited by 191

Macrophage mitochondrial energy status regulates cholesterol efflux and is enhanced by anti-miR33 in atherosclerosis

Karunakaran, D., Thrush, A. B., Nguyen, M.-A., Richards, L., Geoffrion, M., Singaravelu, R., Ramphos, E., Shangari, P., Ouimet, M., Pezacki, J. P., et al. (2015) · Circulation Research · doi:10.1161/circresaha.117.305624 · Cited by 188

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

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

Vitamin C and E supplementation prevents some of the cellular adaptations to endurance-training in humans

Morrison, D., Hughes, J., Della Gatta, P. A., Mason, S., Lamon, S., Russell, A. P., & Wadley, G. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.10.412 · Cited by 171

The transcriptional coactivator PGC-1α is essential for maximal and efficient cardiac mitochondrial fatty acid oxidation and lipid homeostasis

Lehman, J. J., Boudina, S., Banke, N. H., Sambandam, N., Han, X., Young, D. M., Leone, T. C., Gross, R. W., Lewandowski, E. D., Abel, E. D., et al. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00081.2008 · Cited by 158

Skeletal Muscle Mitochondria in the Elderly: Effects of Physical Fitness and Exercise Training

Broskey, N. T., Greggio, C., Boss, A., Boutant, M., Dwyer, A., Schlueter, L., Hans, D., Gremion, G., Kreis, R., Boesch, C., et al. (2014) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2013-3983 · Cited by 157

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

Time course of high-fat diet-induced reductions in adipose tissue mitochondrial proteins: potential mechanisms and the relationship to glucose intolerance

Sutherland, L. N., Capozzi, L. C., Turchinsky, N. J., Bell, R. C., & Wright, D. C. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90408.2008 · Cited by 147

Nuclear receptors as therapeutic targets in cholestatic liver diseases

Zollner, G., & Trauner, M. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2008.00030.x · Cited by 146

Aging-induced alterations in gene transcripts and functional activity of mitochondrial oxidative phosphorylation complexes in the heart

Preston, C. C., Oberlin, A. S., Holmuhamedov, E. L., Gupta, A., Sagar, S., Syed, R. H. K., Siddiqui, S. A., Raghavakaimal, S., Terzic, A., & Jahangir, A. (2008) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2008.02.010 · Cited by 136

Mitochondrial Dysfunction in Type 2 Diabetes and Obesity

Højlund, K., Mogensen, M., Sahlin, K., & Beck-Nielsen, H. (2008) · Endocrinology and Metabolism Clinics of North America · doi:10.1016/j.ecl.2008.06.006 · Cited by 135

Deep undepleted human serum proteome profiling toward biomarker discovery for Alzheimer’s disease

Dey, K. K., Wang, H., Niu, M., Bai, B., Wang, X., Li, Y., Cho, J.-H., Tan, H., Mishra, A., High, A. A., et al. (2019) · Clinical Proteomics · doi:10.1186/s12014-019-9237-1 · Cited by 135

Methionine restriction effects on mitochondrial biogenesis and aerobic capacity in white adipose tissue, liver, and skeletal muscle of F344 rats

Perrone, C. E., Mattocks, D. A. L., Jarvis-Morar, M., Plummer, J. D., & Orentreich, N. (2010) · Metabolism · doi:10.1016/j.metabol.2009.10.023 · Cited by 136

Suppression of the aging-associated decline in physical performance by a combination of resveratrol intake and habitual exercise in senescence-accelerated mice

Murase, T., Haramizu, S., Ota, N., & Hase, T. (2009) · Biogerontology · doi:10.1007/s10522-008-9177-z · Cited by 125

Lysosomal adaptation: how the lysosome responds to external cues

Settembre, C., & Ballabio, A. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016907 · Cited by 126

Beneficial role of bitter melon supplementation in obesity and related complications in metabolic syndrome

Alam, M. A., Uddin, R., Subhan, N., Rahman, M. M., Jain, P., & Reza, H. M. (2015) · Journal of Lipids · doi:10.1155/2015/496169 · Cited by 123

CD36-dependent Regulation of Muscle FoxO1 and PDK4 in the PPARδ/β-mediated Adaptation to Metabolic Stress

Nahlé, Z., Hsieh, M., Pietka, T., Coburn, C. T., Grimaldi, P. A., Zhang, M. Q., Das, D., & Abumrad, N. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706478200 · Cited by 122

PPARδ, but not PPARα, activates PGC-1α gene transcription in muscle

Hondares, E., Pineda-Torra, I., Iglesias, R., Staels, B., Villarroya, F., & Giralt, M. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.01.092 · Cited by 120

The role of PGC‐1 coactivators in aging skeletal muscle and heart

Dillon, L. M., Rebelo, A. P., & Moraes, C. T. (2012) · IUBMB Life · doi:10.1002/iub.608 · Cited by 116

Loss of Pgc-1α expression in aging mouse muscle potentiates glucose intolerance and systemic inflammation

Sczelecki, S., Besse-Patin, A., Abboud, A., Kleiner, S., Laznik-Bogoslavski, D., Wrann, C. D., Ruas, J. L., Haibe-Kains, B., & Estall, J. L. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00578.2013 · Cited by 108

Peroxisome Proliferator-Activated Receptor δ Is an Essential Transcriptional Regulator for Mitochondrial Protection and Biogenesis in Adult Heart

Wang, P., Liu, J., Li, Y., Wu, S., Luo, J., Yang, H., Subbiah, R., Chatham, J., Zhelyabovska, O., & Yang, Q. (2010) · Circulation Research · doi:10.1161/circresaha.109.206185 · Cited by 110

SGK1 inhibition in glia ameliorates pathologies and symptoms in Parkinson disease animal models

Kwon, O., Song, J., Yang, Y., Kim, S., Kim, J. Y., Seok, M., Hwang, I., Yu, J., Karmacharya, J., Maeng, H., et al. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202013076 · Cited by 110

The biology of PGC-1α and its therapeutic potential

Handschin, C. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2009.03.006 · Cited by 108

Mitochondrial signaling, TOR, and life span

Schieke, S. M., & Finkel, T. (2006) · Biological Chemistry · doi:10.1515/bc.2006.170 · Cited by 106

Cognitive Decline, Dementia, Alzheimer’s Disease and Presbycusis: Examination of the Possible Molecular Mechanism

Shen, Y., Ye, B., Chen, P., Wang, Q., Fan, C., Shu, Y., & Xiang, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00394 · Cited by 105

The Transcriptional Coactivator Peroxisome Proliferator–Activated Receptor (PPAR)γ Coactivator-1α and the Nuclear Receptor PPARα Control the Expression of Glycerol Kinase and Metabolism Genes Independently of PPARγ Activation in Human White Adipocytes

Mazzucotelli, A., Viguerie, N., Tiraby, C., Annicotte, J.-S., Mairal, A., Klimcakova, E., Lepin, E., Delmar, P., Dejean, S., Tavernier, G., et al. (2007) · Diabetes · doi:10.2337/db06-1465 · Cited by 90

Delayed treatment with fenofibrate protects against high-fat diet-induced kidney injury in mice: the possible role of AMPK autophagy

Sohn, M., Kim, K., Uddin, M. J., Lee, G., Hwang, I., Kang, H., Kim, H., Lee, J. H., & Ha, H. (2017) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00596.2015 · Cited by 80

Eicosapentaenoic acid improves hepatic steatosis independent of PPARα activation through inhibition of SREBP-1 maturation in mice

Tanaka, N., Zhang, X., Sugiyama, E., Kono, H., Horiuchi, A., Nakajima, T., Kanbe, H., Tanaka, E., Gonzalez, F. J., & Aoyama, T. (2010) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.07.031 · Cited by 78

Role of PGC-1α in sarcopenia: Etiology and potential intervention—A mini-review

Ji, L. L., & Kang, C. (2015) · Gerontology · doi:10.1159/000365947 · Cited by 77

mTORC1 and mTORC2 differentially promote natural killer cell development

Yang, C., Tsaih, S.-W., Lemke, A., Flister, M. J., Thakar, M. S., & Malarkannan, S. (2018) · eLife · doi:10.7554/elife.35619 · Cited by 77

PGC-1 is a male-specific disease modifier of human and experimental amyotrophic lateral sclerosis

Eschbach, J., Schwalenstocker, B., Soyal, S. M., Bayer, H., Wiesner, D., Akimoto, C., Nilsson, A.-C., Birve, A., Meyer, T., Dupuis, L., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt202 · Cited by 75

Mitochondrial dysfunction in the skeletal muscle of a mouse model of Rett syndrome (RTT): implications for the disease phenotype

Gold, W. A., Williamson, S. L., Kaur, S., Hargreaves, I. P., Land, J. M., Pelka, G. J., Tam, P. P. L., & Christodoulou, J. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.02.012 · Cited by 73

Central leptin action improves skeletal muscle AKT, AMPK, and PGC1α activation by hypothalamic PI3K-dependent mechanism

Roman, E. A. F. R., Reis, D., Romanatto, T., Maimoni, D., Ferreira, E. A., Santos, G. A., Torsoni, A. S., Velloso, L. A., & Torsoni, M. A. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.08.007 · Cited by 71

PGC-1α and Myokines in the Aging Muscle – A Mini-Review

Arnold, A.-S., Egger, A., & Handschin, C. (2011) · Gerontology · doi:10.1159/000281883 · Cited by 65

The master energy homeostasis regulator PGC-1α exhibits an mRNA nuclear export function

Mihaylov, S. R., Castelli, L. M., Lin, Y.-H., Gül, A., Soni, N., Hastings, C., Flynn, H. R., Păun, O., Dickman, M. J., Snijders, A. P., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41304-8 · Cited by 63

Fiber Type Conversion by PGC-1α Activates Lysosomal and Autophagosomal Biogenesis in Both Unaffected and Pompe Skeletal Muscle

Takikita, S., Schreiner, C., Baum, R., Xie, T., Ralston, E., Plotz, P. H., & Raben, N. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015239 · Cited by 60

Inorganic Nitrate Mimics Exercise-Stimulated Muscular Fiber-Type Switching and Myokine and γ-Aminobutyric Acid Release

Roberts, L. D., Ashmore, T., McNally, B. D., Murfitt, S. A., Fernandez, B. O., Feelisch, M., Lindsay, R., Siervo, M., Williams, E. A., Murray, A. J., et al. (2017) · Diabetes · doi:10.2337/db16-0843 · Cited by 57

PGC-1β is downregulated by training in human skeletal muscle: no effect of training twice every second day vs. once daily on expression of the PGC-1 family

Mortensen, O. H., Plomgaard, P., Fischer, C. P., Hansen, A. K., Pilegaard, H., & Pedersen, B. K. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00575.2007 · Cited by 56

Two weekly sessions of combined aerobic and resistance exercise are sufficient to provide beneficial effects in subjects with Type 2 diabetes mellitus and metabolic syndrome

Fatone, C., Guescini, M., Balducci, S., Battistoni, S., Settequattrini, A., Pippi, R., Stocchi, L., Mantuano, M., Stocchi, V., & De Feo, P. (2010) · Journal of Endocrinological Investigation · doi:10.1007/bf03346630 · Cited by 54

Transcriptional regulation of the human hepatic lipase (LIPC) gene promoter

Rufibach, L. E., Duncan, S. A., Battle, M., & Deeb, S. S. (2006) · Journal of Lipid Research · doi:10.1194/jlr.m600082-jlr200 · Cited by 52

Myricanol mitigates lipid accumulation in 3T3-L1 adipocytes and high fat diet-fed zebrafish via activating AMP-activated protein kinase

Shen, S., Liao, Q., Feng, Y., Liu, J., Pan, R., Lee, S. M.-Y., & Lin, L. (2019) · Food Chemistry · doi:10.1016/j.foodchem.2018.07.117 · Cited by 51

Insulin Regulation of Hepatic Lipid Homeostasis

Uehara, K., Santoleri, D., Whitlock, A. E. G., & Titchenell, P. M. (2023) · Comprehensive Physiology · doi:10.1002/cphy.c220015 · Cited by 49

Transcriptional network analysis in muscle reveals AP-1 as a partner of PGC-1α in the regulation of the hypoxic gene program

Baresic, M., Salatino, S., Kupr, B., van Nimwegen, E., & Handschin, C. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01710-13 · Cited by 40

A novel chemical uncoupler ameliorates obesity and related phenotypes in mice with diet-induced obesity by modulating energy expenditure and food intake

Fu, Y.-Y., Zhang, M., Turner, N., Zhang, L.-N., Dong, T.-C., Gu, M., Leslie, S. J., Li, J.-Y., Nan, F.-J., & Li, J. (2013) · Diabetologia · doi:10.1007/s00125-013-2987-9 · Cited by 35

A Role for Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1α in Nucleus Accumbens Neuron Subtypes in Cocaine Action

Chandra, R., Engeln, M., Francis, T. C., Konkalmatt, P., Patel, D., & Lobo, M. K. (2017) · Biological Psychiatry · doi:10.1016/j.biopsych.2016.10.024 · Cited by 35

Role and treatment of mitochondrial DNA-related mitochondrial dysfunction in sporadic neurodegenerative diseases

H. Swerdlow, R. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211798072535 · Cited by 35

Potential Roles of Glucagon-Like Peptide-1 and Its Analogues in Dementia Targeting Impaired Insulin Secretion and Neurodegeneration

Mehan, S., Bhalla, S., Siddiqui, E. M., Sharma, N., Shandilya, A., & Khan, A. (2022) · Degenerative Neurological and Neuromuscular Disease · doi:10.2147/dnnd.s247153 · Cited by 29

The Implications of Noncoding RNAs in the Evolution and Progression of Nonalcoholic Fatty Liver Disease (NAFLD)-Related HCC

Rusu, I., Pirlog, R., Chiroi, P., Nutu, A., Puia, V. R., Fetti, A. C., Rusu, D. R., Berindan-Neagoe, I., & Al Hajjar, N. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012370 · Cited by 27

Myobolites: muscle-derived metabolites with paracrine and systemic effects

Ibrahim, A., Neinast, M., & Arany, Z. P. (2017) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2017.03.007 · Cited by 22

Targeting skeletal muscle mitochondrial health in obesity

Pileggi, C. A., Hooks, B. G., McPherson, R., Dent, R. R. M., & Harper, M.-E. (2022) · Clinical Science · doi:10.1042/cs20210506 · Cited by 21

Sweet Mitochondria: A Shortcut to Alzheimer’s Disease

Moreira, P. I. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170931 · Cited by 20