Cited by 364Peroxisome Proliferator-Activated ReceptorsAdipose Tissue and MetabolismMetabolism, Diabetes, and Cancer

The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.

PPARγ coactivator 1β/ERR ligand 1 is an ERR protein ligand, whose expression induces a high-energy expenditure and antagonizes obesity.

Open access

Kamei, Yasutomi, Ohizumi, Hiroshi, Fujitani, Yasushi, Nemoto, Tomoyuki, Tanaka, Toshiya, Takahashi, Nobuyuki, Kawada, Teruo, Miyoshi, Masamitsu, Ezaki, Osamu, Kakizuka, Akira·2003·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.2135217100PMC PMC218766

Open this paper in CoChat — free account

Abstract

A well balanced body energy budget controlled by limitation of calorie uptake and/or increment of energy expenditure, which is typically achieved by proper physical exercise, is most effective against obesity and diabetes mellitus. Recently, peroxisome proliferator-activated receptor (PPAR) gamma, a member of the nuclear receptor, and its cofactors have been shown to be involved in lipid metabolism and in the control of energy expenditure. Here we show that PPARgamma coactivator 1 (PGC-1) beta functions as ERRL1 (for ERR ligand 1), which can bind and activate orphan ERRs (estrogen receptor-related receptors) in vitro. Consistently, PGC-1beta/ERRL1 transgenic mice exhibit increased expression of the medium-chain acyl CoA dehydrogenase, a known ERR target and a pivotal enzyme of mitochondrial beta-oxidation in skeletal muscle. As a result, the PGC-1beta/ERRL1 mice show a state similar to an athlete; namely, the mice are hyperphagic and of elevated energy expenditure and are resistant to obesity induced by a high-fat diet or by a genetic abnormality. These results demonstrate that PGC-1beta/ERRL1 can function as a protein ligand of ERR, and that its level contributes to the control of energy balance in vivo, and provide a strategy for developing novel antiobesity drugs.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1073/pnas.2135217100

Cites

26 of 26 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The nuclear receptor superfamily: the second decade
Mangelsdorf, D. J., Thummel, C., Beato, M., Herrlich, P., Schütz, G., Umesono, K., Blumberg, B., Kastner, P., Mark, M., Chambon, P., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90199-x · Cited by 6,964
Efficient selection for high-expression transfectants with a novel eukaryotic vector
Niwa, H., Yamamura, K., & Miyazaki, J. (1991) · Gene · doi:10.1016/0378-1119(91)90434-d · Cited by 5,135
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
Stimulation of adipogenesis in fibroblasts by PPARγ2, a lipid-activated transcription factor
Tontonoz, P., Hu, E., & Spiegelman, B. M. (1994) · Cell · doi:10.1016/0092-8674(94)90006-x · Cited by 3,564
The coregulator exchange in transcriptional functions of nuclear receptors
Glass, C. K., & Rosenfeld, M. G. (2000) · Genes & Development · doi:10.1101/gad.14.2.121 · Cited by 2,233
A CBP Integrator Complex Mediates Transcriptional Activation and AP-1 Inhibition by Nuclear Receptors
Kamei, Y., Xu, L., Heinzel, T., Torchia, J., Kurokawa, R., Gloss, B., Lin, S.-C., Heyman, R. A., Rose, D. W., Glass, C. K., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81118-6 · Cited by 2,150
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
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
Identification of a new class of steroid hormone receptors
Giguère, V., Yang, N., Segui, P., & Evans, R. M. (1988) · Nature · doi:10.1038/331091a0 · Cited by 867
Obesity in the new millennium
Friedman, J. M. (2000) · Nature · doi:10.1038/35007504 · Cited by 709

Flagged first, then by citations

Show all 26 references

Research works printed but not linked: 1

Maxwell, G. M., Nobbs, S. & Bates, D. J. (1987) Am. J. Physiol. 253, E264-E270.3115113

Sorted by citations

Items 101–200 of 364

Identification and Structure−Activity Relationship of Phenolic Acyl Hydrazones as Selective Agonists for the Estrogen-Related Orphan Nuclear Receptors ERRβ and ERRγ
Zuercher, W. J., Gaillard, S. L., Orband‐Miller, L. A., Chao, E. Y. H., Shearer, B. G., Jones, D. G., Miller, A. B., Collins, J. L., McDonnell, D. P., & Willson, T. M. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm050161j · Cited by 104
Molecular determinants for the polarization of macrophage and osteoclast
Yang, D., & Wan, Y. (2019) · Seminars in Immunopathology · doi:10.1007/s00281-019-00754-3 · Cited by 104
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 102
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 106
Human skeletal muscle fibre type variations correlate with PPARα, PPARδ and PGC‐1α mRNA
Kramer, D., Ahlsén, M., Norrbom, J., Jansson, E., Hjeltnes, N., Gustafsson, T. P., & Krook, A. (2006) · Acta Physiologica · doi:10.1111/j.1748-1716.2006.01620.x · Cited by 101
Estrogen-Related Receptor Alpha: An Under-Appreciated Potential Target for the Treatment of Metabolic Diseases
Tripathi, M., Yen, P. M., & Singh, B. K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051645 · Cited by 98
Structure-guided synthesis of tamoxifen analogs with improved selectivity for the orphan ERRγ
Chao, E. Y. H., Collins, J. L., Gaillard, S. L., Miller, A. B., Wang, L., Orband‐Miller, L. A., Nolte, R. T., McDonnell, D. P., Willson, T. M., & Zuercher, W. J. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.11.030 · Cited by 97
PGC-1α Induces Human RPE Oxidative Metabolism and Antioxidant Capacity
Iacovelli, J., Rowe, G. C., Khadka, A., Diaz‐Aguilar, D., Spencer, C., Arany, Z. P., & Saint‐Geniez, M. (2016) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.15-17758 · Cited by 100
Health Promotion Effects of Soy Isoflavones
Nakai, S., Fujita, M., & Kamei, Y. (2020) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.66.502 · Cited by 98
Role of the PGC-1 family in the metabolic adaptation of goldfish to diet and temperature
LeMoine, C. M. R., Genge, C. E., & Moyes, C. D. (2008) · Journal of Experimental Biology · doi:10.1242/jeb.014951 · Cited by 95
Ncoa3 functions as an essential Esrrb coactivator to sustain embryonic stem cell self-renewal and reprogrammingPreprint
Percharde, M., Lavial, F., Ng, J.-H., Kumar, V., Tomaz, R. A., Martin, N., Yeo, J.-C., Gil, J., Prabhakar, S., Ng, H., et al. (2012) · Genes & Development · doi:10.1101/gad.195545.112 · Cited by 97
ERRα as a Bridge Between Transcription and Function: Role in Liver Metabolism and Disease
Xia, H., Dufour, C. R., & Giguère, V. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00206 · Cited by 98
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 95
The E3 ligase synoviolin controls body weight and mitochondrial biogenesis through negative regulation of PGC‐1β
Fujita, H., Yagishita, N., Aratani, S., Saito‐Fujita, T., Morota, S., Yamano, Y., Hansson, M. J., Inazu, M., Kokuba, H., Sudo, K., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201489897 · Cited by 92
Mitochondrial oxidative injury: a key player in nonalcoholic fatty liver disease
Dornas, W., & Schuppan, D. (2020) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00121.2020 · Cited by 89
Orphan nuclear receptor estrogen-related receptor-β suppresses in vitro and in vivo growth of prostate cancer cells via p21WAF1/CIP1 induction and as a potential therapeutic target in prostate cancer
Yu, S., Wong, Y. C., Wang, X. H., Ling, M. T., Ng, C., Chen, S., & Chan, F. L. (2007) · Oncogene · doi:10.1038/sj.onc.1210986 · Cited by 88
Estrogen-related Receptor α Is a Repressor of Phosphoenolpyruvate Carboxykinase Gene Transcription
Herzog, B., Cardenas, J., Hall, R. K., Villena, J. A., Budge, P. J., Giguère, V., Granner, D. K., & Kralli, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509276200 · Cited by 93
Rosiglitazone-Induced Mitochondrial Biogenesis in White Adipose Tissue Is Independent of Peroxisome Proliferator-Activated Receptor γ Coactivator-1α
Pardo, R., Enguix, N., Lasheras, J., Felíu, J. E., Kralli, A., & Villena, J. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026989 · Cited by 86
Potential Use of Gene Transfer in Athletic Performance Enhancement
Baoutina, A., Alexander, I. E., Rasko, J. E. J., & Emslie, K. R. (2007) · Molecular Therapy · doi:10.1038/sj.mt.6300278 · Cited by 84
The Role of PGC-1α/UCP2 Signaling in the Beneficial Effects of Physical Exercise on the Brain
Bristot, V. J. D. O., Alves, A. C. D. B., Cardoso, L. R., Scheffer, D. D. L., & Aguiar, A. S. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00292 · Cited by 86
ATP Maintenance via Two Types of ATP Regulators Mitigates Pathological Phenotypes in Mouse Models of Parkinson's Disease
Nakano, M., Imamura, H., Sasaoka, N., Yamamoto, M., Uemura, N., Shudo, T., Fuchigami, T., Takahashi, R., & Kakizuka, A. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.07.024 · Cited by 76
Regulation of SREBP1c Gene Expression in Skeletal Muscle: Role of Retinoid X Receptor/Liver X Receptor and Forkhead-O1 Transcription Factor
Kamei, Y., Miura, S., Suganami, T., Akaike, F., Kanai, S., Sugita, S., Katsumata, A., Aburatani, H., Unterman, T. G., Ezaki, O., et al. (2008) · Endocrinology · doi:10.1210/en.2007-1461 · Cited by 82
Regulation of Hepatic ApoC3 Expression by PGC-1β Mediates Hypolipidemic Effect of Nicotinic Acid
Hernandez, C., Molusky, M. M., Li, Y., Li, S., & Lin, J. D. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.09.001 · Cited by 79
Molecular Pathways: The Metabolic Regulator Estrogen-Related Receptor α as a Therapeutic Target in Cancer
Chang, C., & McDonnell, D. P. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-3221 · Cited by 80
Estrogen-related receptor α modulates the expression of adipogenesis-related genes during adipocyte differentiation
Ijichi, N., Ikeda, K., Horie‐Inoue, K., Yagi, K., Okazaki, Y., & Inoue, S. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.209 · Cited by 77
The transcriptional coregulator PGC-1β controls mitochondrial function and anti-oxidant defence in skeletal muscles
Ramamoorthy, T. G., LAVERNY, G., Schlagowski, A.-I., Zoll, J., Messaddeq, N., Bornert, J., Panza, S., Ferry, A., Gény, B., & METZGER, D. (2015) · Nature Communications · doi:10.1038/ncomms10210 · Cited by 82
Mitochondrial network remodeling: an important feature of myogenesis and skeletal muscle regeneration
Rahman, F. A., & Quadrilatero, J. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03807-9 · Cited by 77
Effect of nitric oxide synthase inhibition on mitochondrial biogenesis in rat skeletal muscle
Wadley, G. D., & McConell, G. K. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00549.2006 · Cited by 73
Peroxisome proliferator-activated receptor-γ coactivator-1 and insulin resistance: acute effect of fatty acids
Hoeks, J., Hesselink, M. K. C., Russell, A. P., Mensink, M., Saris, W. H. M., Mensink, R. P., & Schrauwen, P. (2006) · Diabetologia · doi:10.1007/s00125-006-0369-2 · Cited by 74
Mitochondrial development and the influence of its dysfunction during rat adipocyte differentiation
Lu, R., Ji, H., Chang, Z.-G., Shang-Shun, S. U., & Yang, G.-S. (2009) · Molecular Biology Reports · doi:10.1007/s11033-009-9695-z · Cited by 72
Obesity and polymorphisms in genes regulating human adipose tissue
Dahlman, I. A., & Arner, P. (2007) · International Journal of Obesity · doi:10.1038/sj.ijo.0803657 · Cited by 71
The nuclear bile acid receptor FXR is activated by PGC-1α in a ligand-dependent manner
Kanaya, E. N., Shiraki, T., & Jingami, H. (2004) · Biochemical Journal · doi:10.1042/bj20040432 · Cited by 70
Sex dimorphism in cardiac pathophysiology: experimental findings, hormonal mechanisms, and molecular mechanisms.
Du, X.-J., Fang, L., & Kiriazis, H. (2006) · Pharmacology and Therapeutics · doi:10.1016/j.pharmthera.2005.10.016 · Cited by 75
Physiological Genomics Identifies Estrogen-Related Receptor α as a Regulator of Renal Sodium and Potassium Homeostasis and the Renin-Angiotensin Pathway
Tremblay, A., Dufour, C. R., Ghahremani, M., Reudelhuber, T. L., & Giguère, V. (2009) · Molecular Endocrinology · doi:10.1210/me.2009-0254 · Cited by 68
Absence of Estrogen Receptor-Related-α Increases Osteoblastic Differentiation and Cancellous Bone Mineral Density
Delhon, I., Gutzwiller, S., Morvan, F., Rangwala, S. M., Wyder, L., Evans, G. L., Studer, A., Kneissel, M., & Fournier, B. (2009) · Endocrinology · doi:10.1210/en.2009-0121 · Cited by 67
Alterations in the mitochondrial regulatory pathways constituted by the nuclear co-factors PGC-1α or PGC-1β and mitofusin 2 in skeletal muscle in type 2 diabetes
Antonio Zorzano, A., Hernández‐Álvarez, M. I., Palacín, M., & Mingrone, G. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.017 · Cited by 69
Ovariectomy in Mice Decreases Lipid Metabolism-Related Gene Expression in Adipose Tissue and Skeletal Muscle with Increased Body Fat
Kamei, Y., SUZUKI, M. T., Miyazaki, H., Tsuboyama-Kasaoka, N., Wu, J., Ishimi, Y., & Ezaki, O. (2005) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.51.110 · Cited by 68
Structural determination of estrogen-related receptor γ in the presence of phenol derivative compounds
Abad, M. C., Askari, H. B., O’Neill, J., Klinger, A. L., Milligan, C. M., Lewandowski, F. A., Springer, B. A., Spurlino, J. C., & Rentzeperis, D. (2007) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2007.06.006 · Cited by 63
Fatty acids regulate perilipin5 in muscle by activating PPARδ
Bindesb⊘ll, C., Berg, O., Arntsen, B. M., Nebb, H. I., & Dalen, K. T. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m038992 · Cited by 65
RIP140 Expression Is Stimulated by Estrogen-related Receptor α during Adipogenesis
Nichol, D., Christian, M., Steel, J. H., White, R., & Parker, M. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604803200 · Cited by 61
Thermogenic and metabolic antiobesity drugs: rationale and opportunities
Clapham, J. C., & Arch, J. R. S. (2007) · Diabetes, Obesity and Metabolism · doi:10.1111/j.1463-1326.2006.00608.x · Cited by 60
Dual modulation of both lipid oxidation and synthesis by peroxisome proliferator‐activated receptor‐γ coactivator‐1α and ‐1β in cultured myotubes
Espinoza, D., Boros, L. G., Crunkhorn, S., Gami, H., & Patti, M. (2009) · The FASEB Journal · doi:10.1096/fj.09-133728 · Cited by 60
ERRs and cancers: Effects on metabolism and on proliferation and migration capacities
Bianco, S., Sailland, J., & Vanacker, J.-M. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2011.03.014 · Cited by 59
Role of Nuclear Receptors in Central Nervous System Development and Associated Diseases
Maria, A. A., Moreno-Ramos, O. A., & Haider, N. B. (2015) · Journal of Experimental Neuroscience · doi:10.4137/jen.s25480 · Cited by 63
Definition of the Molecular Basis for Estrogen Receptor-Related Receptor-α-Cofactor Interactions
Gaillard, S. L., Dwyer, M. A., & McDonnell, D. P. (2006) · Molecular Endocrinology · doi:10.1210/me.2006-0179 · Cited by 57
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
Binding of bisphenol A and acrylamide to BSA and DNA: Insights into the comparative interactions of harmful chemicals with functional biomacromolecules
Zhang, Y., Zhang, X., Fei, X., Wang, S.-L., & Gao, H. (2010) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2010.06.131 · Cited by 57
Road to exercise mimetics: targeting nuclear receptors in skeletal muscle
Fan, W., Atkins, A. R., Yu, R. T., Downes, M., & Evans, R. M. (2013) · Journal of Molecular Endocrinology · doi:10.1530/jme-13-0258 · Cited by 57
Estrogen-related receptor α regulates skeletal myocyte differentiation via modulation of the ERK MAP kinase pathway
Murray, J., & Huss, J. M. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00033.2011 · Cited by 55
Estrogen-Related Receptors Mediate the Adaptive Response of Brown Adipose Tissue to Adrenergic Stimulation
Brown, E. L., Hazen, B. C., Eury, E., Wattez, J.-S., Gantner, M. L., Albert, V., Chau, S., Sánchez-Alavez, M., Conti, B., & Kralli, A. (2018) · iScience · doi:10.1016/j.isci.2018.03.005 · Cited by 60
Evidence of an association between genetic variation of the coactivator PGC-1β and obesity
Andersen, G., Wegner, L., Yanagisawa, K., Rose, C. S., Lin, J. D., Glümer, C., Drivsholm, T., Borch-Johnsen, K., Jørgensen, T., Hansen, T. F., et al. (2005) · Journal of Medical Genetics · doi:10.1136/jmg.2004.026278 · Cited by 57
Insight on Transcriptional Regulation of the Energy Sensing AMPK and Biosynthetic mTOR Pathway Genes
Sukumaran, A., Choi, K., & Dasgupta, B. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00671 · Cited by 62
Functional crosstalk of PGC-1 coactivators and inflammation in skeletal muscle pathophysiology
Eisele, P. S., & Handschin, C. (2013) · Seminars in Immunopathology · doi:10.1007/s00281-013-0406-4 · Cited by 54
The genetics of human performance
Kim, D. S., Wheeler, M. T., & Ashley, E. A. (2021) · Nature Reviews Genetics · doi:10.1038/s41576-021-00400-5 · Cited by 53
Aging, senescence and mitochondria: the PGC-1/ERR axis
Vernier, M., & Giguère, V. (2020) · Journal of Molecular Endocrinology · doi:10.1530/jme-20-0196 · Cited by 52
Impaired myogenesis in estrogen‐related receptor γ (ERRγ)‐deficient skeletal myocytes due to oxidative stress
Murray, J., Auwerx, J. H., & Huss, J. M. (2012) · The FASEB Journal · doi:10.1096/fj.12-212290 · Cited by 56
Modulation of adipogenesis-related gene expression by estrogen-related receptor γ during adipocytic differentiation
Kubo, M., Ijichi, N., Ikeda, K., Horie‐Inoue, K., Takeda, S., & Inoue, S. (2008) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.08.012 · Cited by 51
VAPB/ALS8 MSP Ligands Regulate Striated Muscle Energy Metabolism Critical for Adult Survival in Caenorhabditis elegans
Han, S. M., Oussini, H. E., Scekic‐Zahirovic, J., Vibbert, J., Cottee, P. A., PRASAIN, J. K., Bellen, H. J., Dupuis, L., & Miller, M. A. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003738 · Cited by 51
Mice lacking PGC-1β in adipose tissues reveal a dissociation between mitochondrial dysfunction and insulin resistance
Enguix, N., Pardo, R., González-Vicens, A., López-Álvarez, V. M., Simó, R., Kralli, A., & Villena, J. A. (2013) · Molecular Metabolism · doi:10.1016/j.molmet.2013.05.004 · Cited by 51
The Asymmetric Binding of PGC-1α to the ERRα and ERRγ Nuclear Receptor Homodimers Involves a Similar Recognition Mechanism
Takács, M., Petoukhov, M. V., Atkinson, R. A., Roblin, P., Ogi, F.-X., Demeler, B., Potier, N., Chebaro, Y., Dejaegere, A. P., Svergun, D. I., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067810 · Cited by 49
Interactions between the consumption of a high-fat diet and fasting in the regulation of fatty acid oxidation enzyme gene expression: an evaluation of potential mechanisms
Frier, B. C., Jacobs, R. L., & Wright, D. C. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00367.2010 · Cited by 50
STAT3 Targets ERR-α to Promote Epithelial–Mesenchymal Transition, Migration, and Invasion in Triple-Negative Breast Cancer Cells
Ma, J., Qi, J., Lin, S., Zhang, C., Liu, F.-Y., Xie, W., & Li, X. (2019) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-18-1194 · Cited by 49
Soluble factors derived from tumor mammary cell lines induce a stromal mammary adipose reversion in human and mice adipose cells. Possible role of TGF-β1 and TNF-α
Guerrero, J., Tobar, N., Cáceres, M., Espinoza, L., Escobar, P., Dotor, J., Smith, P. C., & Martı́nez, J. (2009) · Breast Cancer Research and Treatment · doi:10.1007/s10549-009-0491-1 · Cited by 49
Interplay between estrogen-related receptor alpha (ERRα) and gamma (ERRγ) on the regulation of ERRα gene expression
Zhang, Z., & Teng, C. T. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2006.11.002 · Cited by 49
Estrogen receptor related beta is expressed in human endometrium throughout the normal menstrual cycle
Bombail, V., Macpherson, S., Critchley, H., & Saunders, P. T. K. (2008) · Human Reproduction · doi:10.1093/humrep/den298 · Cited by 49
Nuclear receptors and their relevance to diseases related to lipid metabolism
Berkenstam, A. L., & Gustafsson, J.-Å. (2005) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2005.01.003 · Cited by 49
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 49
Genetic Ablation of the c-Cbl Ubiquitin Ligase Domain Results in Increased Energy Expenditure and Improved Insulin Action
Molero, J. C., Turner, N. A., Thien, C. B. F., Langdon, W. Y., James, D. E., & Cooney, G. J. (2006) · Diabetes · doi:10.2337/db06-0955 · Cited by 47
Cardiac maturation
Sakamoto, T., & Kelly, D. P. (2023) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2023.12.008 · Cited by 50
Retinoid-related orphan receptor γ regulates several genes that control metabolism in skeletal muscle cells: links to modulation of reactive oxygen species production
Raichur, S., Lau, P., Staels, B., & Muscat, G. E. O. (2007) · Journal of Molecular Endocrinology · doi:10.1677/jme.1.00010 · Cited by 48
Characterization of a Novel Small Molecule Subtype Specific Estrogen-Related Receptor α Antagonist in MCF-7 Breast Cancer Cells
Chisamore, M. J., Cunningham, M. E. A., Flores, O. A., Wilkinson, H. A., & Chen, J. D. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005624 · Cited by 45
Vitamin D Attenuates FOXO1-Target Atrophy Gene Expression in C2C12 Muscle Cells
Hirose, Y., Onishi, T., Miura, S., Hatazawa, Y., & Kamei, Y. (2018) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.64.229 · Cited by 43
Adopting New Orphans into the Family of Metabolic Regulators
Hummasti, S., & Tontonoz, P. (2008) · Molecular Endocrinology · doi:10.1210/me.2007-0566 · Cited by 45
Organotin compounds cause structure-dependent induction of progesterone in human choriocarcinoma Jar cells
Hiromori, Y., Yui, H., Nishikawa, J., Nagase, H., & Nakanishi, T. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.10.010 · Cited by 41
Bcl3 Interacts Cooperatively with Peroxisome Proliferator-Activated Receptor Gamma (PPARγ) Coactivator 1α To Coactivate Nuclear Receptors Estrogen-Related Receptor α and PPARα
Yang, J., Williams, R. S., & Kelly, D. P. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01669-08 · Cited by 41
Identification of a New Type of Covalent PPARγ Agonist using a Ligand-Linking Strategy
Ohtera, A., Miyamae, Y., Yoshida, K., Maejima, K., Akita, T., Kakizuka, A., Irie, K., Masuda, S., Kambe, T., & Nagao, M. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00628 · Cited by 42
Clocking In, Working Out: Circadian Regulation of Exercise Physiology
Duglan, D., & Lamia, K. A. (2019) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2019.04.003 · Cited by 43
Estrogen Receptor α (ERα) and Estrogen Related Receptor α (ERRα) are both transcriptional regulators of the Runx2-I isoform
Kammerer, M., Gutzwiller, S., Stauffer, D., Delhon, I., Seltenmeyer, Y., & Fournier, B. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.01.024 · Cited by 39
Complementary Roles of Estrogen-Related Receptors in Brown Adipocyte Thermogenic Function
Gantner, M. L., Hazen, B. C., Eury, E., Brown, E. L., & Kralli, A. (2016) · Endocrinology · doi:10.1210/en.2016-1767 · Cited by 43
PGC-1α regulates alanine metabolism in muscle cells
Hatazawa, Y., Qian, K., Gong, D., & Kamei, Y. (2018) · PLoS ONE · doi:10.1371/journal.pone.0190904 · Cited by 38
An ERRβ/γ agonist modulates GRα expression, and glucocorticoid responsive gene expression in skeletal muscle cells
Wang, S.-C., Myers, S., Dooms, C., Capon, R. J., & Muscat, G. E. O. (2009) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.07.012 · Cited by 38
Aging-Associated Changes in Physical Performance and Energy Metabolism in the Senescence-Accelerated Mouse
Haramizu, S., Ota, N., Hase, T., & Murase, T. (2011) · The Journals of Gerontology Series A · doi:10.1093/gerona/glr037 · Cited by 39
A Bacterial Biosensor of Endocrine Modulators
Σκρέτας, Γ., & Wood, D. W. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.04.009 · Cited by 38
The Estrogen-Related Receptor α Inverse Agonist XCT 790 Is a Nanomolar Mitochondrial Uncoupler
Eskiocak, B., Ali, A., & White, M. A. (2014) · Biochemistry · doi:10.1021/bi500737n · Cited by 37
Dynamic epigenetic responses to muscle contraction.
Rasmussen, M., Zierath, J., & Barrès, R. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.03.003 · Cited by 39
Orphan nuclear receptors: therapeutic opportunities in skeletal muscle
Smith, A. G., & Muscat, G. E. O. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00476.2005 · Cited by 37
PGC-1β and ChREBP partner to cooperatively regulate hepatic lipogenesis in a glucose concentration-dependent manner
Chambers, K. T., Chen, Z., Lai, L., Leone, T. C., Towle, H. C., Kralli, A., Crawford, P. A., & Finck, B. N. (2013) · Molecular Metabolism · doi:10.1016/j.molmet.2013.05.001 · Cited by 36
Adipose tissue failure and mitochondria as a possible target for improvement by bioactive food components
Keijer, J., & van Schothorst, E. M. (2008) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e3282f39f95 · Cited by 36
Absence of RIP140 Reveals a Pathway Regulating glut4-Dependent Glucose Uptake in Oxidative Skeletal Muscle through UCP1-Mediated Activation of AMPK
Fritah, A., Steel, J. H., Parker, N., Nikolopoulou, E., Christian, M., Carling, D., & Parker, M. G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032520 · Cited by 37
Network analysis reveals a causal role of mitochondrial gene activity in atherosclerotic lesion formation
Vilne, B., Skogsberg, J., Asl, H. F., Talukdar, H. A., Kessler, T., Björkegren, J., & Schunkert, H. (2017) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2017.10.019 · Cited by 36
Genes and pathophysiology of type 2 diabetes: more than just the Randle cycle all over again
Shuldiner, A. R., & McLenithan, J. C. (2004) · Journal of Clinical Investigation · doi:10.1172/jci23586 · Cited by 36
Peri‐implantation lethality in mice lacking the PGC‐1‐related coactivator protein
He, X., Sun, C., Wang, F., Shan, A., Guo, T., Gu, W., Cui, B., & Ning, G. (2012) · Developmental Dynamics · doi:10.1002/dvdy.23769 · Cited by 36
Indazole-based ligands for estrogen-related receptor α as potential anti-diabetic agents
Patch, R. J., Huang, H., Patel, S., Cheung, W. S., Xu, G., Zhao, B., Beauchamp, D. A., Rentzeperis, D., Geisler, J. G., Askari, H. B., et al. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.07.015 · Cited by 36
Sex-Specific Differences in Type 2 Diabetes Mellitus and Dyslipidemia Therapy: PPAR Agonists
Benz, V., Kintscher, U., & Foryst‐Ludwig, A. (2012) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-30726-3_18 · Cited by 32
PGC-1ss Down-Regulation Is Associated With Reduced ERR Activity and MCAD Expression in Skeletal Muscle of Senescence-Accelerated Mice
Rodríguez‐Calvo, R., Jové, M., Coll, T., Camins, A., Sanchez, R. M., Alegret, M., Merlos, M., Pallàs, M., Laguna, J. C., & Vázquez‐Carrera, M. (2006) · The Journals of Gerontology Series A · doi:10.1093/gerona/61.8.773 · Cited by 34
Transcriptional co-activator peroxisome proliferator-activated receptor (PPAR)γ co-activator-1β is involved in the regulation of glucose-stimulated insulin secretion in INS-1E cells
Oberkofler, H., Hafner, M., Felder, T. K., Krempler, F., & Patsch, W. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0425-0 · Cited by 33
PGC-1α and PGC-1β Increase Protein Synthesis via ERRα in C2C12 Myotubes
Brown, E. L., Foletta, V. C., Wright, C. R., Sepulveda, P. V., Konstantopoulos, N., Sanigorski, A. J., Gatta, P. A. D., Cameron‐Smith, D., Kralli, A., & Russell, A. P. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01336 · Cited by 33
Proteome Modulation in H9c2 Cardiac Cells by microRNAs miR-378 and miR-378
Mallat, Y., Tritsch, E., Ladouce, R., Winter, D. L., Friguet, B., Li, Z., & Mericskay, M. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.030569 · Cited by 38
Insulin receptor sensitizer, dicholine succinate, prevents both Toll-like receptor 4 (TLR4) upregulation and affective changes induced by a high-cholesterol diet in mice
Strekalova, T. V., Costa-Nunes, J. P., Veniaminova, E. A., Kubatiev, A. A., Lesch, K., Chekhonin, V. P., Evans, M. C., & Steinbusch, H. W. M. (2016) · Journal of Affective Disorders · doi:10.1016/j.jad.2016.02.045 · Cited by 33
Nuclear receptor ERRα and coactivator PGC-1β are effectors of IFN-γ-induced host defensePreprint
Sonoda, J., Laganière, J., Mehl, I. R., Barish, G. D., Chong, L.-W., Li, X., Scheffler, I. E., Mock, D. C., Bataille, A. R., Robert, F., et al. (2007) · Genes & Development · doi:10.1101/gad.1553007 · Cited by 218

Authors: Kamei, Y., Ohizumi, H., Fujitani, Y., Nemoto, T., Tanaka, T., Takahashi, N., Kawada, T., Miyoshi, M., Ezaki, O., & Kakizuka, A.
Affiliations: Kyoto University (JP)
Corresponding author: Kakizuka, Akira
ORCID: Kamei, Yasutomi
Tanaka, Toshiya
Takahashi, Nobuyuki
Kawada, Teruo
Ezaki, Osamu
Kakizuka, Akira
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2003-10-06
Volume: 100
Issue: 21
Pages: 12378-12383
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.2135217100
PMC: PMC218766
OpenAlex: W1965989272
Cited by: 357
References: 26
Citations by year: 2026: 3 · 2025: 8 · 2024: 11 · 2023: 8 · 2022: 6 · 2021: 12 · 2020: 11 · 2019: 12 · 2018: 14 · 2017: 10 · 2016: 9 · 2015: 16 · 2014: 11 · 2013: 15 · 2012: 16
FWCI: 8.04
Type: journal article
Language: en
Open access: green
europepmc.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords: PGC-1β, orphan nuclear receptor, protein ligands, energy expenditure, obesity resistance, high-fat diet, medium-chain acyl-CoA dehydrogenase, mitochondrial beta-oxidation, skeletal muscle, hyperphagia, energy balance, anti-obesity drugs
MeSH terms: ERRalpha Estrogen-Related Receptor, Amino Acid Sequence, Animals, Base Sequence, DNA, Energy Metabolism, Ligands, Mice, Transgenic, Molecular Sequence Data, Obesity, Receptors, Estrogen, Recombinant Proteins, Transcription Factors, Gene Expression, Receptors, Cytoplasmic and Nuclear, Mice

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

PPARγ coactivator 1β/ERR ligand 1 is an ERR protein ligand, whose expression induces a high-energy expenditure and antagonizes obesity.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks