Overexpression of peroxisome proliferator-activated receptor γ coactivator-1α down-regulates GLUT4 mRNA in skeletal muscles.

Molecular cloning: A laboratory manual

Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684 · see citing works

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

Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139 · see citing works

A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis

Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864 · see citing works

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 · see citing works

Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1

Yoon, J. C., Puigserver, P., Chen, G., Donovan, J., Wu, Z., Rhee, J., Adelmant, G., Stafford, J., Kahn, C. R., Granner, D. K., et al. (2001) · Nature · doi:10.1038/35093050 · Cited by 1,821 · see citing works

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 · see citing works

The Coactivator PGC-1 Cooperates with Peroxisome Proliferator-Activated Receptor α in Transcriptional Control of Nuclear Genes Encoding Mitochondrial Fatty Acid Oxidation Enzymes

Vega, R. B., Huss, J. M., & Kelly, D. P. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.5.1868-1876.2000 · Cited by 1,195 · see citing works

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 · see citing works

Walking Compared With Vigorous Physical Activity and Risk of Type 2 Diabetes in Women: A Prospective Study

Hu, F. B., Sigal, R. J., Rich-Edwards, J. W., Colditz, G. A., Solomon, C. G., Willett, W. C., Speizer, F. E., & Manson, J. E. (1999) · JAMA · doi:10.1001/jama.282.15.1433 · Cited by 914 · see citing works

Activation of the human mitochondrial transcriptionfactor A gene by nuclear respiratory factors: a potential regulatory linkbetween nuclear and mitochondrial gene expression in organellebiogenesis.

Virbasius, J. V., & Scarpulla, R. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.4.1309 · Cited by 819 · see citing works

Restoration of insulin-sensitive glucose transporter (GLUT4) gene expression in muscle cells by the transcriptional coactivator PGC-1

Michael, L. F., Wu, Z., Cheatham, R. B., Puigserver, P., Adelmant, G., Lehman, J. J., Kelly, D. P., & Spiegelman, B. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.061035098 · Cited by 663 · see citing works

NRF-1: a trans-activator of nuclear-encoded respiratory genes in animal cells.

Evans, M. J., & Scarpulla, R. C. (1990) · Genes & Development · doi:10.1101/gad.4.6.1023 · Cited by 417 · see citing works

Fish Oil Feeding Decreases Mature Sterol Regulatory Element-binding Protein 1 (SREBP-1) by Down-regulation of SREBP-1c mRNA in Mouse Liver

Kim, H.-J., Takahashi, M., & Ezaki, O. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25892 · Cited by 377 · see citing works

31P nuclear magnetic resonance measurements of muscle glucose-6-phosphate. Evidence for reduced insulin-dependent muscle glucose transport or phosphorylation activity in non-insulin-dependent diabetes mellitus.

Rothman, D. L., Shulman, R. G., & Shulman, G. I. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115686 · Cited by 325 · see citing works

Evidence from transgenic mice that glucose transport is rate-limiting for glycogen deposition and glycolysis in skeletal muscle

Ren, J., Marshall, B. A., Gulve, E. A., Gao, J., Johnson, D. W., Holloszy, J. O., & Mueckler, M. M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85395-4 · Cited by 274 · see citing works

cDNA Cloning and mRNA Analysis of PGC-1 in Epitrochlearis Muscle in Swimming-Exercised Rats

Goto, M., Terada, S., Kato, M., Katoh, M., Yokozeki, T., Tabata, I., & Shimokawa, T. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3134 · Cited by 258 · see citing works

Myocyte Enhancer Factor 2 (MEF2)-Binding Site Is Required forGLUT4 Gene Expression in Transgenic Mice

Thai, M. V., Guruswamy, S., Cao, K. T., Pessin, J. E., & Olson, A. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14285 · Cited by 201 · see citing works

Human Peroxisome Proliferator Activated Receptor Gamma Coactivator 1 (PPARGC1) Gene: cDNA Sequence, Genomic Organization, Chromosomal Localization, and Tissue Expression

Esterbauer, H., Oberkofler, H., Krempler, F., & Patsch, W. (1999) · Genomics · doi:10.1006/geno.1999.5977 · Cited by 201 · see citing works

PPARs: Transcription Factors Controlling Lipid and Lipoprotein Metabolism

Bocher, V., Pineda‐Torra, I., Fruchart, J., & Staels, B. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb04258.x · Cited by 178 · see citing works

Quantitative analysis of the human alpha-skeletal actin gene in transgenic mice.

Brennan, K., & Hardeman, E. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54211-3 · Cited by 169 · see citing works

A forkhead transcription factor FKHR up‐regulates lipoprotein lipase expression in skeletal muscle

Kamei, Y., Mizukami, J., Miura, S., SUZUKI, M. T., Takahashi, N., Kawada, T., Taniguchi, T., & Ezaki, O. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00062-0 · Cited by 136 · see citing works

Up-regulation of SREBP-1c and lipogenic genes in skeletal muscles after exercise training

Ikeda, S., Miyazaki, H., Nakatani, T., Kai, Y., Kamei, Y., Miura, S., Tsuboyama-Kasaoka, N., & Ezaki, O. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00883-5 · Cited by 92 · see citing works

NMR studies of muscle glycogen synthesis in insulin-resistant offspring of parents with non-insulin-dependent diabetes mellitus immediately after glycogen-depleting exercise.

Price, T. B., Perseghin, G., Dulęba, A. J., Chen, W., Chase, J. R., Rothman, D. L., Shulman, R. G., & Shulman, G. I. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.11.5329 · Cited by 77 · see citing works

Exercise-Induced Transcription of the Muscle Glucose Transporter (GLUT 4) Gene

MacLean, P. S., Zheng, D., Jones, J. P., Olson, A. L., & Dohm, G. L. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6654 · Cited by 77 · see citing works

Role of Leptin in Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 Expression1

Kakuma, T., Wang, Z.-W., Pan, W., Unger, R. H., & Zhou, Y.-T. (2000) · Endocrinology · doi:10.1210/endo.141.12.7804 · Cited by 76 · see citing works

Regulatory Elements in the Insulin-Responsive Glucose Transporter (GLUT4) Gene

Ezaki, O. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7587 · Cited by 71 · see citing works

Nuclear respiratory factors and the pathways of nuclear-mitochondrial interaction.

Scarpulla, R. (1996) · Trends in cardiovascular medicine · doi:10.1016/1050-1738(95)00129-8 · Cited by 70 · see citing works

Localization of Exercise- and Denervation-Responsive Elements in the Mouse GLUT4 Gene

Tsunoda, N., Maruyama, K., Cooke, D. W., Lane, D. M., & Ezaki, O. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.2031 · Cited by 34 · see citing works

Fiber Types in Mammalian Skeletal Muscles

Schiaffino, S., & Reggiani, C. (2011) · Physiological Reviews · doi:10.1152/physrev.00031.2010 · Cited by 3,022 · see citing works

PGC-1α: a key regulator of energy metabolism

Liang, H., & Ward, W. F. (2006) · AJP Advances in Physiology Education · doi:10.1152/advan.00052.2006 · Cited by 1,250 · see citing works

The Critical Role of Metabolic Pathways in Aging

Barzilai, N., Huffman, D. M., Muzumdar, R. H., & Bartke, A. (2012) · Diabetes · doi:10.2337/db11-1300 · Cited by 803 · see citing works

Skeletal Muscle FOXO1 (FKHR) Transgenic Mice Have Less Skeletal Muscle Mass, Down-regulated Type I (Slow Twitch/Red Muscle) Fiber Genes, and Impaired Glycemic Control

Kamei, Y., Miura, S., SUZUKI, M. T., Kai, Y., Mizukami, J., Taniguchi, T., Mochida, K., Tomoko, H. A. T. A., Matsuda, J., Aburatani, H., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400674200 · Cited by 574 · see citing works

The role of mitochondria in the pathogenesis of type 2 diabetes

Patti, M.-E., & Corvera, S. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0027 · Cited by 551 · see citing works

Mitochondrial dysfunction and insulin resistance: an update

Montgomery, M. K., & Turner, N. A. (2014) · Endocrine Connections · doi:10.1530/ec-14-0092 · Cited by 530 · see citing works

PGC-1α regulation by exercise training and its influences on muscle function and insulin sensitivity

Lira, V. A., Benton, C. R., Yan, Z., & Bonen, A. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00755.2009 · Cited by 412 · see citing works

PGC-1α Coactivates PDK4 Gene Expression via the Orphan Nuclear Receptor ERRα: a Mechanism for Transcriptional Control of Muscle Glucose Metabolism

Wende, A. R., Huss, J. M., Schaeffer, P. J., Giguère, V., & Kelly, D. P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.24.10684-10694.2005 · Cited by 354 · see citing works

Multiple environmental and genetic factors influence skeletal muscle PGC-1α and PGC-1β gene expression in twins

Ling, C., Poulsen, P., Carlsson, E., Ridderstråle, M., Almgren, P., Wojtaszewski, J. F. P., Beck‐Nielsen, H., Groop, L., & Vaag, A. A. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200421889 · Cited by 300 · see citing works

Paradoxical effects of increased expression of PGC-1α on muscle mitochondrial function and insulin-stimulated muscle glucose metabolism

Choi, C. S., Befroy, D. E., Codella, R., Kim, S., Reznick, R. M., Hwang, Y.-J., Liu, Z.-X., Lee, H.-Y., Distefano, A., Samuel, V. T., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810339105 · Cited by 279 · see citing works

Metabolic remodelling of the failing heart: the cardiac burn-out syndrome?

VANBILSEN, M., Smeets, P. J. H., Gilde, A. J., & Vandervusse, G. J. (2003) · Cardiovascular Research · doi:10.1016/j.cardiores.2003.11.014 · Cited by 261 · see citing works

Mechanisms Modulating Skeletal Muscle Phenotype

Blaauw, B., Schiaffino, S., & Reggiani, C. (2013) · Comprehensive physiology · doi:10.1002/cphy.c130009 · Cited by 278 · see citing works

Regulation of Skeletal Muscle Function by Amino Acids

Kamei, Y., Hatazawa, Y., Uchitomi, R., Yoshimura, R., & Miura, S. (2020) · Nutrients · doi:10.3390/nu12010261 · Cited by 254 · see citing works

Multiple environmental and genetic factors influence skeletal muscle PGC-1α and PGC-1β gene expression in twins

Ling, C., Poulsen, P., Carlsson, E., Ridderstråle, M., Almgren, P., Wojtaszewski, J., Beck-Nielsen, H., Groop, L., & Vaag, A. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21889 · Cited by 300 · see citing works

Modest PGC-1α Overexpression in Muscle in Vivo Is Sufficient to Increase Insulin Sensitivity and Palmitate Oxidation in Subsarcolemmal, Not Intermyofibrillar, Mitochondria

Benton, C. R., Nickerson, J. G., Lally, J., Han, X.-X., Holloway, G. P., Glatz, J. F. C., Luiken, J. J. F. P., Graham, T. E., Heikkila, J. J., & Bonen, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m704332200 · Cited by 214 · see citing works

Exercise and Myocyte Enhancer Factor 2 Regulation in Human Skeletal Muscle

McGee, S. L., & Hargreaves, M. (2004) · Diabetes · doi:10.2337/diabetes.53.5.1208 · Cited by 205 · see citing works

Muscle metabolism and atrophy: let’s talk about sex

Rosa-Caldwell, M. E., & Greene, N. P. (2019) · Biology of Sex Differences · doi:10.1186/s13293-019-0257-3 · Cited by 202 · see citing works

Protein kinase B/Akt: a nexus of growth factor and cytokine signaling in determining muscle mass

Frost, R. A., & Lang, C. H. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00089.2007 · Cited by 200 · see citing works

Fatty acid metabolism, energy expenditure and insulin resistance in muscle

Turner, N. A., Cooney, G. J., Kraegen, E. W., & Bruce, C. R. (2013) · Journal of Endocrinology · doi:10.1530/joe-13-0397 · Cited by 198 · see citing works

Endurance exercise increases the SIRT1 and peroxisome proliferator-activated receptor γ coactivator-1α protein expressions in rat skeletal muscle

Suwa, M., Nakano, H., Radak, Z. O., & Kumagai, S. (2008) · Metabolism · doi:10.1016/j.metabol.2008.02.017 · Cited by 195 · see citing works

Molecular Mechanisms for the Vicious Cycle between Insulin Resistance and the Inflammatory Response in Obesity

Szukiewicz, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24129818 · Cited by 208 · see citing works

An Increase in Murine Skeletal Muscle Peroxisome Proliferator-Activated Receptor-γ Coactivator-1α (PGC-1α) mRNA in Response to Exercise Is Mediated by β-Adrenergic Receptor Activation

Miura, S., Kawanaka, K., Kai, Y., Tamura, M., Goto, M., Shiuchi, T., Minokoshi, Y., & Ezaki, O. (2007) · Endocrinology · doi:10.1210/en.2006-1646 · Cited by 183 · see citing works

Leucine modulation of mitochondrial mass and oxygen consumption in skeletal muscle cells and adipocytes

Sun, X., & Zemel, M. B. (2009) · Nutrition & Metabolism · doi:10.1186/1743-7075-6-26 · Cited by 166 · see citing works

The Role of Mitochondria in the Pathophysiology of Skeletal Muscle Insulin Resistance

Pagel-Langenickel, I., Bao, J., Pang, L., & Sack, M. N. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0003 · Cited by 154 · see citing works

Isoform-Specific Increases in Murine Skeletal Muscle Peroxisome Proliferator-Activated Receptor-γ Coactivator-1α (PGC-1α) mRNA in Response to β2-Adrenergic Receptor Activation and Exercise

Miura, S., Kai, Y., Kamei, Y., & Ezaki, O. (2008) · Endocrinology · doi:10.1210/en.2008-0466 · Cited by 150 · see citing works

Baf60c drives glycolytic metabolism in the muscle and improves systemic glucose homeostasis through Deptor-mediated Akt activation

Meng, Z.-X., Li, S., Wang, L., Ko, H. J., Lee, Y., Jung, D. Y., Okutsu, M., Yan, Z., Kim, J. K., & Lin, J. D. (2013) · Nature Medicine · doi:10.1038/nm.3144 · Cited by 146 · see citing works

Increased levels of peroxisome proliferator-activated receptor gamma, coactivator 1 alpha (PGC-1α) improve lipid utilisation, insulin signalling and glucose transport in skeletal muscle of lean and insulin-resistant obese Zucker rats

Benton, C. R., Holloway, G. P., Han, X.-X., Yoshida, Y., Snook, L. A., Lally, J., Glatz, J. F. C., Luiken, J. J. F. P., Chabowski, A., & Bonen, A. (2010) · Diabetologia · doi:10.1007/s00125-010-1773-1 · Cited by 143 · see citing works

Artificial selection for high-capacity endurance running is protective against high-fat diet-induced insulin resistance

Noland, R. C., Thyfault, J. P., Henes, S. T., Whitfield, B. R., Woodlief, T., Evans, J. R., Lust, J. A., Britton, S. L., Koch, L. G., Dudek, R. W., et al. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00500.2006 · Cited by 141 · see citing works

Nitric oxide and mitochondrial biogenesis: A key to long-term regulation of cellular metabolism

Clementi, E., & Nisoli, E. (2005) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpb.2005.04.022 · Cited by 136 · see citing works

Regulation of skeletal muscle mitochondrial fatty acid metabolism in lean and obese individuals

Holloway, G. P., Bonen, A., & Spriet, L. L. (2008) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.2008.26717b · Cited by 140 · see citing works

Involvement of PPARγ co-activator-1, nuclear respiratory factors 1 and 2, and PPARα in the adaptive response to endurance exercise

Baar, K. (2004) · Proceedings of The Nutrition Society · doi:10.1079/pns2004334 · Cited by 139 · see citing works

PGC-1α Integrates Insulin Signaling, Mitochondrial Regulation, and Bioenergetic Function in Skeletal Muscle

Pagel-Langenickel, I., Bao, J., Joseph, J. J., Schwartz, D. R., Mantell, B. S., Xu, X., Raghavachari, N., & Sack, M. N. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800842200 · Cited by 124 · see citing works

Inhibition of Endothelial p53 Improves Metabolic Abnormalities Related to Dietary Obesity

Yokoyama, M., Okada, S., Nakagomi, A., Moriya, J., Shimizu, I., Nojima, A., Yoshida, Y., Ichimiya, H., Kamimura, N., Kobayashi, Y., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.046 · Cited by 122 · see citing works

Cellular distribution of glucose and monocarboxylate transporters in human brain white matter and multiple sclerosis lesions

Nijland, P. G., Michailidou, I., Witte, M. E., Mizee, M. R., van der Pol, S. M. A., Hof, B. V. H., Reijerkerk, A., Pellerin, L., van der Valk, P., de Vries, H. E., et al. (2014) · Glia · doi:10.1002/glia.22667 · Cited by 113 · see citing works

Overexpression of peroxisome proliferator-activated receptor γ co-activator-1α leads to muscle atrophy with depletion of ATP.

Miura, S., Tomitsuka, E., Kamei, Y., Yamazaki, T., Kai, Y., Tamura, M., Kita, K., Nishino, I., & Ezaki, O. (2006) · The American Journal of Pathology · doi:10.2353/ajpath.2006.060034 · Cited by 107 · see citing works

Lactate transported by MCT1 plays an active role in promoting mitochondrial biogenesis and enhancing TCA flux in skeletal muscle

Zhang, L., Xin, C., Wang, S., Zhuo, S., Zhu, J., Li, Z., Liu, Y., Yang, L., & Chen, Y. (2024) · Science Advances · doi:10.1126/sciadv.adn4508 · Cited by 103 · see citing works

PGC-1α and PGC-1β have both similar and distinct effects on myofiber switching toward an oxidative phenotype

Mortensen, O. H., Frandsen, L., Schjerling, P., Nishimura, E., & Grunnet, N. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00591.2005 · Cited by 101 · see citing works

PGC-1α-Mediated Branched-Chain Amino Acid Metabolism in the Skeletal Muscle

Hatazawa, Y., Tadaishi, M., Nagaike, Y., Morita, A., Ogawa, Y., Ezaki, O., Takai‐Igarashi, T., Kitaura, Y., Shimomura, Y., Kamei, Y., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091006 · Cited by 101 · see citing works

Coordination of mitochondrial biogenesis by PGC-1α in human skeletal muscle: A re-evaluation

Islam, H., Edgett, B. A., & Gurd, B. J. (2018) · Metabolism · doi:10.1016/j.metabol.2017.11.001 · Cited by 99 · see citing works

PGC-1α increases skeletal muscle lactate uptake by increasing the expression of MCT1 but not MCT2 or MCT4

Benton, C. R., Yoshida, Y., Lally, J., Han, X.-X., Hatta, H., & Bonen, A. (2008) · Physiological Genomics · doi:10.1152/physiolgenomics.90217.2008 · Cited by 97 · see citing works

Complex Haplotypes of the PGC-1α Gene Are Associated With Carbohydrate Metabolism and Type 2 Diabetes

Oberkofler, H., Linnemayr, V., Weitgasser, R., Klein, K., Xie, M., Iglseder, B., Krempler, F., Paulweber, B., & Patsch, W. (2004) · Diabetes · doi:10.2337/diabetes.53.5.1385 · Cited by 96 · see citing works

PGC-1α-mediated regulation of gene expression and metabolism: implications for nutrition and exercise prescriptions

Benton, C. R., Wright, D. C., & Bonen, A. (2008) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h08-074 · Cited by 91 · see citing works

Fine-Tuning of PGC1α Expression Regulates Cardiac Function and Longevity

Zhu, X., Shen, W., Yao, K., Wang, H., Лю, Б., Li, T., Song, L., Diao, D., Mao, G., Huang, P., et al. (2019) · Circulation Research · doi:10.1161/circresaha.119.315529 · Cited by 88 · see citing works

The Implication of PGC-1α on Fatty Acid Transport across Plasma and Mitochondrial Membranes in the Insulin Sensitive Tissues

Supruniuk, E., Mikłosz, A., & Chabowski, A. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00923 · Cited by 83 · see citing works

Local estrogen formation and its regulation in endometriosis

Mori, T., Ito, F., Koshiba, A., Kataoka, H., Takaoka, O., Okimura, H., Khan, K. N., & Kitawaki, J. (2019) · Reproductive Medicine and Biology · doi:10.1002/rmb2.12285 · Cited by 84 · see citing works

Metabolomic Analysis of the Skeletal Muscle of Mice Overexpressing PGC-1α

Hatazawa, Y., Senoo, N., Tadaishi, M., Ogawa, Y., Ezaki, O., Kamei, Y., & Miura, S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0129084 · Cited by 78 · see citing works

PGC-1α-induced improvements in skeletal muscle metabolism and insulin sensitivityThis paper is one of a selection of papers published in this Special Issue, entitled 14th International Biochemistry of Exercise Conference – Muscles as Molecular and Metabolic Machines, and has undergone the Journal’s usual peer review process.

Bonen, A. (2009) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h09-008 · Cited by 70 · see citing works

Rapid decline in MyHC I(β) mRNA expression in rat soleus during hindlimb unloading is associated with AMPK dephosphorylation

Vilchinskaya, N. A., Mochalova, E. P., Nemirovskaya, T. L., Mirzoev, T. M., Turtikova, O. V., & Shenkman, B. S. (2017) · The Journal of Physiology · doi:10.1113/jp275184 · Cited by 63 · see citing works

Mild hyperbaric oxygen: mechanisms and effects

Ishihara, A. (2019) · The Journal of Physiological Sciences · doi:10.1007/s12576-019-00678-5 · Cited by 64 · see citing works

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 · see citing works

Muscle type‐specific response of PGC‐1α and oxidative enzymes during voluntary wheel running in mouse skeletal muscle

Ikeda, S., Kawamoto, H., Kasaoka, K., Hitomi, Y., Kizaki, T., Sankai, Y., Ohno, H., Haga, S., & Takemasa, T. (2006) · Acta Physiologica · doi:10.1111/j.1748-1716.2006.01623.x · Cited by 58 · see citing works

Amelioration of lipid-induced insulin resistance in rat skeletal muscle by overexpression of Pgc-1β involves reductions in long-chain acyl-CoA levels and oxidative stress

Wright, L. E., Brandon, A. E., Hoy, A. J., Forsberg, G.-B., Lelliott, C. J., Reznick, J., Löfgren, L., Oscarsson, J., Strömstedt, M., Cooney, G. J., et al. (2011) · Diabetologia · doi:10.1007/s00125-011-2068-x · Cited by 57 · see citing works

α2-AMPK activity is not essential for an increase in fatty acid oxidation during low-intensity exercise

Miura, S., Kai, Y., Kamei, Y., Bruce, C. R., Kubota, N., Febbraio, M. A., Kadowaki, T., & Ezaki, O. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90690.2008 · Cited by 53 · see citing works

Dietary soya protein intake and exercise training have an additive effect on skeletal muscle fatty acid oxidation enzyme activities and mRNA levels in rats

Morifuji, M., Sanbongi, C., & Sugiura, K. (2006) · British Journal Of Nutrition · doi:10.1079/bjn20061855 · Cited by 48 · see citing works

PGC-1α's relationship with skeletal muscle palmitate oxidation is not present with obesity despite maintained PGC-1α and PGC-1β protein

Holloway, G. P., Perry, C. G. R., Thrush, A. B., Heigenhauser, G. J. F., Dyck, D. J., Bonen, A., & Spriet, L. L. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00726.2007 · Cited by 48 · see citing works

Mitochondrial Inhibitor as a New Class of Insulin Sensitizer

Zhang, Y., & Ye, J. (2012) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2012.06.010 · Cited by 47 · see citing works

Prep1 Deficiency Induces Protection from Diabetes and Increased Insulin Sensitivity through a p160-Mediated Mechanism

Oriente, F., Fernández, L. C., Miele, C., Iovino, S., Mori, S., Diaz, V. M., Troncone, G., Cassese, A., Formisano, P., Blasi, F., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00117-08 · Cited by 47 · see citing works

Mechanisms of disease

Fernyhough, P., & McGavock, J. (2014) · Handbook of clinical neurology · doi:10.1016/b978-0-444-53480-4.00027-8 · Cited by 47 · see citing works

The effect of exercise on epigenetic modifications of PGC1: The impact on type 2 diabetes

dos Santos, J. M., Tewari, S., & Benite‐Ribeiro, S. A. (2014) · Medical Hypotheses · doi:10.1016/j.mehy.2014.03.018 · Cited by 45 · see citing works

Potential role of lipin-1 in exercise-induced mitochondrial biogenesis

Higashida, K., Higuchi, M., & Terada, S. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.07.079 · Cited by 45 · see citing works

PGC-1α and exercise in the control of body weight

Summermatter, S., & Handschin, C. (2012) · International Journal of Obesity · doi:10.1038/ijo.2012.12 · Cited by 45 · see citing works

How is Mitochondrial Biogenesis Affected in Mitochondrial Disease?

Chabi, B., Adhihetty, P. J., Ljubicic, V., & Hood, D. A. (2005) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000177426.68149.83 · Cited by 44 · see citing works

Different contribution of muscle and liver lipid metabolism to endurance capacity and obesity susceptibility of mice

Haramizu, S., Nagasawa, A., Ota, N., Hase, T., Tokimitsu, I., & Murase, T. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90804.2008 · Cited by 43 · see citing works

VLDL and apolipoprotein CIII induce ER stress and inflammation and attenuate insulin signalling via Toll-like receptor 2 in mouse skeletal muscle cells

Botteri, G., Montori-Grau, M., Gumà, A., Pizarro‐Delgado, J., Cedó, L., Escolá‐Gil, J. C., Li, D., Barroso, E., Palomer, X., Kohan, A. B., et al. (2017) · Diabetologia · doi:10.1007/s00125-017-4401-5 · Cited by 42 · see citing works

Transcription Factor Tfe3 Directly Regulates Pgc‐1alpha in Muscle

Salma, N., Song, J. S., Arany, Z. P., & Fisher, D. E. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.24978 · Cited by 41 · see citing works

Fish protein intake induces fast-muscle hypertrophy and reduces liver lipids and serum glucose levels in rats

Kawabata, F., Mizushige, T., Uozumi, K., Hayamizu, K., Han, L., Tsuji, T., & Kishida, T. (2015) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2014.951025 · Cited by 40 · see citing works

Mechanisms Modulating Skeletal Muscle Phenotype

Blaauw, B., Schiaffino, S., & Reggiani, C. (2013) · Comprehensive physiology · doi:10.1002/j.2040-4603.2013.tb00534.x · Cited by 38 · see citing works

Postexercise skeletal muscle signaling responses to moderate- to high-intensity steady-state exercise in the fed or fasted state

Stocks, B., Dent, J. R., Ogden, H. B., Zemp, M., & Philp, A. (2018) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00311.2018 · Cited by 38 · see citing works

Aromatase as a target for treating endometriosis

Mori, T., Ito, F., Koshiba, A., Kataoka, H., Tanaka, Y., Okimura, H., Khan, K. N., & Kitawaki, J. (2018) · Journal of obstetrics and gynaecology research · doi:10.1111/jog.13743 · Cited by 36 · see citing works

Key signalling factors and pathways in the molecular determination of skeletal muscle phenotype

Chang, K. (2007) · animal · doi:10.1017/s1751731107702070 · Cited by 37 · see citing works

DNA Sequence Variants in PPARGC1A, a Gene Encoding a Coactivator of the ω-3 LCPUFA Sensing PPAR-RXR Transcription Complex, Are Associated with NV AMD and AMD-Associated Loci in Genes of Complement and VEGF Signaling Pathways

SanGiovanni, J. P., Chen, J., Sapieha, P. S., Aderman, C. M., Stahl, A., Clemons, T. E., Chew, E. Y., & Smith, L. E. H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053155 · Cited by 34 · see citing works

Improved skeletal muscle Ca2+ regulation in vivo following contractions in mice overexpressing PGC-1α

Eshima, H., Miura, S., Senoo, N., Hatakeyama, K., Poole, D. C., & Kano, Y. (2017) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00032.2017 · Cited by 33 · see citing works

Enhancing healthy aging with small molecules: A mitochondrial perspective

Qin, X., Li, H., Zhao, H., Fang, L., & Wang, X. (2024) · Medicinal Research Reviews · doi:10.1002/med.22034 · Cited by 33 · see citing works

Co-activator binding protein PIMT mediates TNF-α induced insulin resistance in skeletal muscle via the transcriptional down-regulation of MEF2A and GLUT4

Kain, V., Kapadia, B. B., Viswakarma, N., Seshadri, S., Prajapati, B., Jena, P. K., Meda, C. L. T., Subramanian, M., Suraj, S. K., Kumar, S. T., et al. (2015) · Scientific Reports · doi:10.1038/srep15197 · Cited by 31 · see citing works

Supplementing the maternal diet of rats with butyrate enhances mitochondrial biogenesis in the skeletal muscles of weaned offspring

Huang, Y., Gao, S., Guo, J. X., Zhao, R., & Yang, X. (2017) · British Journal Of Nutrition · doi:10.1017/s0007114516004402 · Cited by 28 · see citing works

Altering aspects of mitochondrial quality to improve musculoskeletal outcomes in disuse atrophy

Rosa‐Caldwell, M. E., Lim, S., Haynie, W. S., Jansen, L. T., Westervelt, L. C., Amos, M. G., Washington, T. A., & Greene, N. P. (2020) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00407.2020 · Cited by 28 · see citing works

Regulation of Cardiomyocyte Glut4 Expression by ZAC1

Czubryt, M. P., Lamoureux, L., Ramjiawan, A., Abrenica, B., Jangamreddy, J. R., & Swan, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.097246 · Cited by 24 · see citing works

The effect of previous weight training and concurrent weight training on endurance for functional electrical stimulation cycle ergometry

PETROFSKY, J. S., & Laymon, M. (2004) · European Journal of Applied Physiology · doi:10.1007/s00421-003-1003-3 · Cited by 24 · see citing works

Ablation of Lgr4 enhances energy adaptation in skeletal muscle via activation of Ampk/Sirt1/Pgc1α pathway

Sun, Y., Hong, J., Chen, M., Ke, Y., Zhao, S., Liu, W., Ma, Q., Shi, J., Zou, Y., Ning, T., et al. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.06.066 · Cited by 22 · see citing works

Constitutive PGC-1α overexpression in skeletal muscle does not protect from age-dependent decline in neurogenesis

Karlsson, L., Alvarado, M. N. G., Motalleb, R., Blomgren, K., Börjesson, M., & Kuhn, H. G. (2019) · Scientific Reports · doi:10.1038/s41598-019-48795-w · Cited by 22 · see citing works

Hepatic response to restoration of GLUT4 in skeletal muscle of GLUT4 null mice

Ranalletta, M., Du, X. Q., Seki, Y., Glenn, A. S., Kruse, M., Fiallo, A., Estrada, I. J., Tsao, T., Stenbit, A. E., Katz, E. B., et al. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00628.2006 · Cited by 19 · see citing works

Muscle-derived SDF-1α/CXCL12 modulates endothelial cell proliferation but not exercise training-induced angiogenesis

Yamada, M., Hokazono, C., Tokizawa, K., Marui, S., Iwata, M., Lira, V. A., Suzuki, K., Miura, S., Nagashima, K., & Okutsu, M. (2019) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00155.2019 · Cited by 19 · see citing works

Swim therapy-induced tissue specific metabolic responses in male rats

Moustafa, A., & Arisha, A. H. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118516 · Cited by 19 · see citing works

Correlation between porcinePPARGC1A mRNA expression and its downstream target genes in backfat andlongissimus dorsi muscle

Erkens, T., Vandesompele, J., Zeveren, A. V., & Peelman, L. J. (2009) · Journal of Applied Genetics · doi:10.1007/bf03195694 · Cited by 18 · see citing works

PGC-1α activation: a therapeutic target for type 2 diabetes?

Yuan, D., Xiao, D., Gao, Q., & Zeng, L. (2018) · Eating and Weight Disorders - Studies on Anorexia Bulimia and Obesity · doi:10.1007/s40519-018-0622-y · Cited by 18 · see citing works

SAFB1, an RBMX-binding protein, is a newly identified regulator of hepatic SREBP-1c gene

Omura, Y., Nishio, Y., Takemoto, T., Ikeuchi, C., Sekine, O., Morino, K., Maeno, Y., Obata, T., Ugi, S., Maegawa, H., et al. (2009) · BMB Reports · doi:10.5483/bmbrep.2009.42.4.232 · Cited by 17 · see citing works

Genetic Associations ofPPARGC1Awith Type 2 Diabetes: Differences among Populations with African Origins

Cheema, A. K., Li, T., Liuzzi, J. P., Zarini, G. G., Dorak, M. T., & Huffman, F. G. (2015) · Journal of Diabetes Research · doi:10.1155/2015/921274 · Cited by 18 · see citing works

Overexpression of PGC-1β improves insulin sensitivity and mitochondrial function in 3T3-L1 adipocytes

Gao, C., Guang-ling, L., Liu, S., Chen, X.-H., Ji, C., Zhang, C., Xia, Z., & Guo, X. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-0789-2 · Cited by 16 · see citing works

Control of microvascular P o 2kinetics following onset of muscle contractions: role for AMPK

Kano, Y., Poole, D. C., Sudo, M., Hirachi, T., Miura, S., & Ezaki, O. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00294.2011 · Cited by 16 · see citing works

Metformin prevents LYRM1 -induced insulin resistance in 3T3-L1 adipocytes via a mitochondrial-dependent mechanism

Qin, Z., Zhang, M., Dai, Y., Wang, Y.-M., Zhu, G.-Z., Zhao, Y., Ji, C., Qiu, J., Cao, X.-G., & Guo, X. (2014) · Experimental Biology and Medicine · doi:10.1177/1535370214537746 · Cited by 16 · see citing works

Autophagy activation, not peroxisome proliferator‐activated receptor γ coactivator 1α, may mediate exercise‐induced improvements in glucose handling during diet‐induced obesity

Rosa‐Caldwell, M. E., Brown, J. L., Lee, D. E., Blackwell, T. A., Turner, K. W., Brown, L. A., Perry, R. A., Haynie, W. S., Washington, T. A., & Greene, N. P. (2017) · Experimental Physiology · doi:10.1113/ep086406 · Cited by 16 · see citing works

Exogenous parathyroid hormone attenuates ovariectomy-induced skeletal muscle weakness in vivo

Fujimaki, T., Ando, T., Hata, T., Takayama, Y., Ohba, T., Ichikawa, J., Takiyama, Y., Tatsuno, R., Koyama, K., & Haro, H. (2021) · Bone · doi:10.1016/j.bone.2021.116029 · Cited by 16 · see citing works

Unloading-induced atrophy and decreased oxidative capacity of the soleus muscle in rats are reversed by pre- and postconditioning with mild hyperbaric oxygen

Takemura, A., Roy, R. R., Yoshihara, I., & Ishihara, A. (2017) · Physiological Reports · doi:10.14814/phy2.13353 · Cited by 16 · see citing works

Increased oxidative properties of gastrocnemius in rats fed on a high-protein diet

Nakazato, K., & Song, H. (2007) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2006.12.019 · Cited by 16 · see citing works

Impact of Metabolic disrupting chemicals on redox homeostasis, energy sensors, receptor modulation, and hormone metabolism: A comparative account in Teleost and mammalian model organisms

Mukherjee, U., & Maitra, S. (2023) · Aquaculture and Fisheries · doi:10.1016/j.aaf.2023.05.004 · Cited by 15 · see citing works

Peroxisome proliferator-activated receptor-γ coactivator 1α-mediated pathway as a possible therapeutic target in endometriosis.

Kataoka, H., Mori, T., Okimura, H., Matsushima, H., Ito, F., Koshiba, A., Tanaka, Y., Akiyama, K., Maeda, E., Sugahara, T., et al. (2019) · Human Reproduction · doi:10.1093/humrep/dez067 · Cited by 9 · see citing works

Macrophage migration inhibitory factor promotes expression of GLUT4 glucose transporter through MEF2 and Zac1 in cardiomyocytes

Liang, Y., Yuan, W., Zhu, W., Zhu, J.-N., Lin, Q., Zou, X., Deng, C., Fu, Y., Zheng, X., Yang, M., et al. (2015) · Metabolism · doi:10.1016/j.metabol.2015.09.007 · Cited by 14 · see citing works

Increased Mass of Slow-Type Skeletal Muscles and Depressed Myostatin Gene Expression in Cold-Tolerant Chicks

Ijiri, D., Miura, M., KANAI, Y., & Hirabayashi, M. (2009) · ZOOLOGICAL SCIENCE · doi:10.2108/zsj.26.277 · Cited by 14 · see citing works

GLUT4 expression in 3T3-L1 adipocytes is repressed by proteasome inhibition, but not by inhibition of calpains

Cooke, D. W., & Patel, Y. M. (2005) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2004.12.008 · Cited by 14 · see citing works

The role of FoxO1 and its modulation with small molecules in the development of diabetes mellitus: A review

Nathanael, J., Suardana, P., Vianney, Y. M., & Putra, S. E. D. (2021) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13989 · Cited by 13 · see citing works

Regulation of Mitochondrial Biogenesis and GLUT4 Expression by Exercise

Holloszy, J. O. (2011) · Comprehensive physiology · doi:10.1002/j.2040-4603.2011.tb00346.x · Cited by 14 · see citing works

Regulation by exercise of skeletal muscle content of mitochondria and GLUT4.

Holloszy, J. O. (2008) · PubMed · Cited by 202 · see citing works

PGC-1α-induced improvements in skeletal muscle metabolism and insulin sensitivityThis paper is one of a selection of papers published in this Special Issue, entitled 14th International Biochemistry of Exercise Conference – Muscles as Molecular and Metabolic Machines, and has undergone the Journal’s usual peer review process.

Bonen, A. (2009) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h09-008 · Cited by 70 · see citing works

Peroxisome proliferator-activated receptor γ coactivator 1α expression levels in soleus and EDL muscles after exercise

Macaluso, F., Scalia, F., Damico, D. C. S., Cappello, F., Farina, F., Felice, V. D., & Barone, R. (2018) · Italian Journal of Anatomy and Embryology · doi:10.13128/ijae-11433

Dissociation between PGC-1α and GLUT-4 Expression in Skeletal Muscle of Rats Fed a High-Fat Diet

Higashida, K., Higuchi, M., & Terada, S. (2009) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.55.486 · Cited by 13 · see citing works