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

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

Intrinsic aerobic capacity correlates with greater inherent mitochondrial oxidative and H2O2emission capacities without major shifts in myosin heavy chain isoform

Seifert, E. L., Bastianelli, M., Aguer, C., Moffat, C., Estey, C., Koch, L. G., Britton, S. L., & Harper, M. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01475.2011 · Cited by 31

On the Intractability of Estrogen-Related Receptor α as a Target for Activation by Small Molecules

Hyatt, S. M., Lockamy, E. L., Stein, R. A., McDonnell, D. P., Miller, A. B., Orband‐Miller, L. A., Willson, T. M., & Zuercher, W. J. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm7012387 · Cited by 30

The pro-inflammatory cytokine IL6 suppresses mitochondrial function via the gp130-JAK1/STAT1/3-HIF1α/ERRα axis

Xu, J., Wakai, M., Xiong, K., Yang, Y., Prabakaran, A., Wu, S. P., Ahrens, D., Molina‐Portela, M. D. P., Ni, M., Bai, Y., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115403 · Cited by 35

Transcriptional Regulation of ROS Homeostasis by the ERR Subfamily of Nuclear Receptors

Scholtes, C., & Giguère, V. (2021) · Antioxidants · doi:10.3390/antiox10030437 · Cited by 33

Loss of skeletal muscle estrogen-related receptors leads to severe exercise intolerance

Wattez, J.-S., Eury, E., Hazen, B. C., Wade, A. K., Chau, S., Ou, S., Russell, A. P., Cho, Y., & Kralli, A. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101670 · Cited by 29

Alteration of mitochondrial oxidative capacity during porcine preadipocyte differentiation and in response to leptin.

Luo, G.-F., Yu, T.-Y., Wen, X.-H., Li, Y., & Yang, G.-S. (2007) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-007-9587-2 · Cited by 28

Effect of sitagliptin on energy metabolism and brown adipose tissue in overweight individuals with prediabetes: a randomised placebo-controlled trial

Nahon, K. J., Doornink, F., Straat, M. E., Botani, K., Martínez‐Téllez, B., Abreu-Vieira, G., van Klinken, J. B., Voortman, G. J., Friesema, E. C. H., Ruiz, J. R., et al. (2018) · Diabetologia · doi:10.1007/s00125-018-4716-x · Cited by 28

The PGC-1/ERR network and its role in precision oncology

Vitto, H. D., Bode, A. M., & Dong, Z. (2019) · npj Precision Oncology · doi:10.1038/s41698-019-0081-6 · Cited by 30

Inhibition of Estrogen-Related Receptor α Blocks Liver Steatosis and Steatohepatitis and Attenuates Triglyceride Biosynthesis

Chen, C.-Y., Li, Y., Zeng, N., He, L., Zhang, X., Tu, T., Tang, Q., Alba, M. M., Mir, S., Stiles, E. X., et al. (2021) · American Journal Of Pathology · doi:10.1016/j.ajpath.2021.04.007 · Cited by 31

Age effect on myocellular remodeling: Response to exercise and nutrition in humans

Irving, B. A., Robinson, M. M., & Nair, K. S. (2011) · Ageing Research Reviews · doi:10.1016/j.arr.2011.11.001 · Cited by 31

Suppressing the activity of ERRα in 3T3‐L1 adipocytes reduces mitochondrial biogenesis but enhances glycolysis and basal glucose uptake

Nie, Y., & Wong, C. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00382.x · Cited by 28

Estrogen‐related receptor α is involved in angiogenesis and skeletal muscle revascularization in hindlimb ischemia

Sopariwala, D. H., Likhite, N., Pei, G., Haroon, F., Lin, L. D., Yadav, V., Zhao, Z., & Narkar, V. A. (2021) · The FASEB Journal · doi:10.1096/fj.202001794rr · Cited by 27

Prenatally Induced Changes in Muscle Structure and Metabolic Function Facilitate Exercise-Induced Obesity Prevention

Huber, K., Miles-Chan, J. L., Norman, A. M., Thompson, N. M., Davison, M., & Breier, B. H. (2009) · Endocrinology · doi:10.1210/en.2009-0125 · Cited by 27

Estrogen-related receptor alpha (ERRα) is a key regulator of intestinal homeostasis and protects against colitis

Tran, A., Scholtes, C., Songane, M., Champagne, C., Galarneau, L., Levasseur, M.-P., Fodil, N., Dufour, C. R., Giguère, V., & Saleh, M. (2021) · Scientific Reports · doi:10.1038/s41598-021-94499-5 · Cited by 27

Acute exercise induces biphasic increase in respiratory mRNA in skeletal muscle

Ikeda, S., Kizaki, T., Haga, S., Ohno, H., & Takemasa, T. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.01.095 · Cited by 26

Estrogen related receptor α-induced adipogenesis is PGC-1β-dependent

Ju, D., He, J., Zhao, L., Zheng, X., & Yang, G. (2011) · Molecular Biology Reports · doi:10.1007/s11033-011-1104-8 · Cited by 26

Troglitazone is an estrogen-related receptor α and γ inverse agonist

Wang, Y., Fang, F., & Wong, C. (2010) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.03.013 · Cited by 26

Excess of miRNA-378a-5p perturbs mitotic fidelity and correlates with breast cancer tumourigenesis in vivo

Winsel, S., Mäki-Jouppila, J. H., Tambe, M., Aure, M. R. R., Pruikkonen, S., Salmela, A.-L., Halonen, T., Leivonen, S., Kallio, L., Børresen-Dale, A.-L., et al. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.524 · Cited by 25

Coactivators PGC-1β and SRC-1 Interact Functionally to Promote the Agonist Activity of the Selective Estrogen Receptor Modulator Tamoxifen

Kressler, D., Hock, M. B., & Kralli, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705596200 · Cited by 26

Development of Novel Cell Lines for High-Throughput Screening to Detect Estrogen-Related Receptor Alpha Modulators

Teng, C. T., Hsieh, J., Zhao, J., Huang, R., Xia, M., Martin, N. P., Gao, X., Dixon, D., Auerbach, S. S., Witt, K. L., et al. (2017) · SLAS DISCOVERY · doi:10.1177/2472555216689772 · Cited by 25

Pharmacogenomics of Chemically Distinct Classes of Keap1-Nrf2 Activators Identify Common and Unique Gene, Protein, and Pathway Responses In Vivo

Wible, R. S., Tran, Q. T., Fathima, S., Sutter, T. R., Kensler, T. W., & Sutter, T. R. (2018) · Molecular Pharmacology · doi:10.1124/mol.117.110262 · Cited by 24

Kaempferol inhibits cancer cell growth by antagonizing estrogen‐related receptor α and γ activities

Wang, H., Gao, M., & Wang, J. (2013) · Cell Biology International · doi:10.1002/cbin.10152 · Cited by 24

Loss of Estrogen-Related Receptor Alpha Facilitates Angiogenesis in Endothelial Cells

Likhite, N., Yadav, V., Milliman, E. J., Sopariwala, D. H., Lorca, S., Narayana, N. P., Sheth, M., Reineke, E. L., Giguère, V., & Narkar, V. A. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00411-18 · Cited by 24

Increased fat oxidation and regulation of metabolic genes with ultraendurance exercise

Helge, J. W., Rehrer, N. J., Pilegaard, H., Manning, P. J., Lucas, S. J. E., GERRARD, D. F., & Cotter, J. D. (2007) · Acta Physiologica · doi:10.1111/j.1748-1716.2007.01709.x · Cited by 24

spargel, the PGC-1α homologue, in models of Parkinson disease in Drosophila melanogaster

Merzetti, E. M., & Staveley, B. E. (2015) · BMC Neuroscience · doi:10.1186/s12868-015-0210-2 · Cited by 23

Morphology, mitochondrial development and adipogenic-related genes expression during adipocytes differentiation in grass carp (Ctenopharyngodon idellus)

Pin, L., Ji, H., Li, C., Chen, L., & Du, Z. (2015) · 中国科学通报：英文版 · doi:10.1007/s11434-015-0833-9 · Cited by 22

Chlorinated biphenyls effect on estrogen-related receptor expression, steroid secretion, mitochondria ultrastructure but not on mitochondrial membrane potential in Leydig cells

Milon, A., Opydo‐Chanek, M., Tworzydlo, W., Galas, J. F., Pardyak, L., Kamińska, A., Ptak, A., & Kotula‐Balak, M. (2017) · Cell and Tissue Research · doi:10.1007/s00441-017-2596-x · Cited by 21

Identification of Compounds That Inhibit Estrogen-Related Receptor Alpha Signaling Using High-Throughput Screening Assays

Lynch, C., Zhao, J., Sakamuru, S., Zhang, L., Huang, R., Witt, K. L., Merrick, B. A., Teng, C. T., & Xia, M. (2019) · Molecules · doi:10.3390/molecules24050841 · Cited by 21

Two target gene activation pathways for orphan ERR nuclear receptors

Nakadai, T., Shimada, M., Ito, K., Cevher, M. A., Chu, C.-S., Kumegawa, K., Maruyama, R., Malik, S., & Roeder, R. G. (2023) · Cell Research · doi:10.1038/s41422-022-00774-z · Cited by 21

Impact of the peroxisome proliferator activated receptor-γ coactivator-1β (PGC-1β) Ala203Pro polymorphism on in vivo metabolism, PGC-1β expression and fibre type composition in human skeletal muscle

Ling, C., Wegner, L., Andersen, G., Almgren, P.-E., Hansen, T. F., Pedersen, O. B., Groop, L., Vaag, A. A., & Poulsen, P. (2007) · Diabetologia · doi:10.1007/s00125-007-0729-6 · Cited by 21

PGC-1: a key regulator in bone homeostasis

Chen, H., Fan, W., He, H., & Huang, F. P. (2021) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-021-01263-w · Cited by 20

Simulated microgravity attenuates myogenesis and contractile function of 3D engineered skeletal muscle tissues

Ren, Z., Ahn, E. H., Do, M., Mair, D. B., Monemianesfahani, A., Lee, P. H. U., & Kim, D. (2024) · npj Microgravity · doi:10.1038/s41526-024-00353-z · Cited by 20

ERRγ Is Not Required for Skeletal Development but Is a RUNX2-Dependent Negative Regulator of Postnatal Bone Formation in Male Mice

Cardelli, M., & Aubin, J. E. (2014) · PLoS ONE · doi:10.1371/journal.pone.0109592 · Cited by 20

Structural Insights into the Specificity of Ligand Binding and Coactivator Assembly by Estrogen-Related Receptor β

Yao, B., Zhang, S., Wei, Y., Tian, S., Zhou, L., Jin, L., He, Y., Xie, W., & Li, Y. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.08.007 · Cited by 20

Troglitazone induces cytotoxicity in part by promoting the degradation of peroxisome proliferator‐activated receptor γ co‐activator‐1α protein

Liao, X., Wang, Y., & Wong, C. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.00900.x · Cited by 20

Molecular dynamics of the ERRγ ligand-binding domain bound with agonist and inverse agonist

Sasidharan, S., Radhakrishnan, K., Lee, J.-Y., Saudagar, P., Gosu, V., & Shin, D. (2023) · PLoS ONE · doi:10.1371/journal.pone.0283364 · Cited by 19

PGC-1α coactivates estrogen-related receptor-α to induce the expression of glucokinase

Zhu, L., Liu, Y., Cui, A., Шао, Д., Liang, J., Liu, X., Chen, Y., Gupta, N., Fang, F., & Chang, Y. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00633.2009 · Cited by 20

Combined transcriptome and metabolome analysis reveals breed-specific regulatory mechanisms in Dorper and Tan sheep

Ma, Y., Cai, G., Chen, J., Yang, X., Hua, G., Han, D., Li, X., Feng, D., & Deng, X. (2024) · BMC Genomics · doi:10.1186/s12864-023-09870-9 · Cited by 18

Identification of small molecule estrogen‐related receptor α–specific antagonists and homology modeling to predict the molecular determinants as the basis for selectivity over ERRβ and ERRγ

Chisamore, M. J., Mosley, R. T., Cai, S., Birzin, E. T., O’Donnell, G. T., Zuck, P. D., Flores, O. A., Schaeffer, J. M., Rohrer, S. P., Chen, J. D., et al. (2008) · Drug Development Research · doi:10.1002/ddr.20246 · Cited by 17

Genistein, daidzein, and resveratrols stimulate PGC-1β-mediated gene expression

Uchitomi, R., Nakai, S., Matsuda, R., Onishi, T., Miura, S., Hatazawa, Y., & Kamei, Y. (2018) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2018.11.009 · Cited by 18

Small-Angle X-ray Scattering Studies on Structures of an Estrogen-Related Receptor α Ligand Binding Domain and Its Complexes with Ligands and Coactivators

Jin, K. S., Park, J. K., Yoon, J., Rho, Y., Kim, J., Kim, E. E., & Ree, M. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp800120r · Cited by 18

Heterogeneity of adipose tissue-resident macrophages-beyond M1/M2 paradigm

Nawaz, A., Fujisaka, S., Kado, T., Jeelani, I., & Tobe, K. (2023) · Diabetology International · doi:10.1007/s13340-023-00624-2 · Cited by 19

Role of Esrrg in the fibrate-mediated regulation of lipid metabolism genes in human ApoA-I transgenic mice

Sanoudou, D., Duka, A., Drosatos, K., Hayes, K. C., & Zannis, V. I. (2009) · The Pharmacogenomics Journal · doi:10.1038/tpj.2009.51 · Cited by 17

Development of a stable cell line with an intact PGC-1α/ERRα axis for screening environmental chemicals

Teng, C. T., Beames, B., Merrick, B. A., Martin, N. P., Romeo, C., & Jetten, A. M. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.01.033 · Cited by 17

Impact of FMR1 Premutation on Neurobehavior and Bioenergetics in Young Monozygotic Twins

Napoli, E., Schneider, A., Hagerman, R. J., Song, G., Wong, S., Tassone, F., & Giulivi, C. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00338 · Cited by 16

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 17

Nuclear Receptor Coactivator PNRC2 Regulates Energy Expenditure and Adiposity

Zhou, D., Shen, R., Ye, J. J., Li, Y., Tsark, W. M. K., Isbell, D., Tso, P., & Chen, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703234200 · Cited by 16

Deletion of the transcriptional coactivator PGC1α in skeletal muscles is associated with reduced expression of genes related to oxidative muscle function

Hatazawa, Y., Minami, K., Yoshimura, R., Onishi, T., Manio, M. C. C., Inoue, K., Sawada, N., Suzuki, O., Miura, S., & Kamei, Y. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.133 · Cited by 16

Efferent retinal projections visualized by immunohistochemical detection of the estrogen-related receptor beta in the postnatal and adult mouse brain

Real, M. A., Heredia, R., Dávila, J. C., & Guirado, S. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.04.044 · Cited by 16

Putative association of peroxisome proliferator‐activated receptor γ co‐activator 1β (PPARGC1B) polymorphism with Type 2 diabetes mellitus

Park, K. S., Shin, H. D., Park, B. L., Cheong, H. S., Cho, Y., Lee, H. K., Lee, J., Lee, J., Kim, H.-K., Park, C. ‐., et al. (2006) · Diabetic Medicine · doi:10.1111/j.1464-5491.2006.01882.x · Cited by 16

Emerging Roles of COX7RP and Mitochondrial Oxidative Phosphorylation in Breast Cancer

Kamada, S., Takeiwa, T., Ikeda, K., Horie, K., & Inoue, S. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.717881 · Cited by 16

Responsive oligochitosan nano-vesicles with ursodeoxycholic acid and exenatide for NAFLD synergistic therapy via SIRT1

Xie, P., Peng, Y., & Qiu, L. (2022) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2022.119388 · Cited by 17

Molecular Mechanisms for Age-Associated Mitochondrial Deficiency in Skeletal Muscle

Wagatsuma, A., & Sakuma, K. (2012) · Journal of Aging Research · doi:10.1155/2012/768304 · Cited by 15

Molecular cloning and functional study of rat estrogen receptor-related receptor γ in rat prostatic cells

Lui, K., Huang, Y., Choi, H., Yu, S., Wong, K., Chen, S., & Chan, F. L. (2006) · The Prostate · doi:10.1002/pros.20429 · Cited by 15

The orphan nuclear receptors, estrogen receptor-related receptors: their role as new biomarkers in gynecological cancer.

Sun, P., Wei, L., Denkert, C., Lichtenegger, W., & Sehouli, J. (2006) · PubMed · Cited by 15

Altered Hepatic and Muscle Substrate Utilization Provoked by GLUT4 Ablation

Ranalletta, M., Jiang, H., Li, J., Tsao, T., Stenbit, A. E., Yokoyama, M., Katz, E. B., & Charron, M. J. (2005) · Diabetes · doi:10.2337/diabetes.54.4.935 · Cited by 15

Antimitotic activity of DY131 and the estrogen-related receptor beta 2 (ERRβ2) splice variant in breast cancer

Heckler, M. M., Zeleke, T. Z., Divekar, S. D., Fernandez, A. I., Tiek, D. M., Woodrick, J., Farzanegan, A., Roy, R., Üren, A., Mueller, S. C., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9719 · Cited by 14

Control of skeletal muscle metabolic properties by the nuclear receptor corepressor RIP140This 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.

Fritah, A. (2009) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h09-026 · Cited by 13

Adipose targets for obesity drug development

Boss, O., & Bergenhem, N. C. H. (2006) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.10.1.119 · Cited by 12

The 2.3 Genotype of ESRRA23 of the ERRα Gene Is Associated with a Higher BMI Than the 2.2 Genotype

Kamei, Y., Lwin, H., Saito, K., Yokoyama, T., Yoshiike, N., Ezaki, O., & Tanaka, H. (2005) · Obesity Research · doi:10.1038/oby.2005.225 · Cited by 13

Early Mitochondrial Adaptations in Skeletal Muscle to Obesity and Obesity Resistance Differentially Regulated by High-Fat Diet

Sun, J., Huang, T., Qi, Z., You, S., Dong, J., Zhang, C., Qin, L., Zhou, Y., & Ding, S. (2017) · Experimental and Clinical Endocrinology & Diabetes · doi:10.1055/s-0043-104634 · Cited by 12

Estrogen-related Receptor Signaling in Skeletal Muscle Fitness

Sopariwala, D. H., Nguyen, H., & Narkar, V. A. (2023) · International Journal of Sports Medicine · doi:10.1055/a-2035-8192 · Cited by 13

The estrogen-related receptors (ERRs): potential targets against bone loss

Zhang, L., Wong, J., & Vanacker, J.-M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2328-5 · Cited by 12

Antitumor activity of Apocynaceae species used in Amazon traditional medicine

Bastos, M. L. C., Sarmento, R. M., Bahia, M. D. O., Rodrigues, J. D. S., Vale, V. V., Percário, S., & Dolabela, M. F. (2020) · Research Society and Development · doi:10.33448/rsd-v9i10.9241 · Cited by 11

PGC-1β regulates mouse carnitine–acylcarnitine translocase through estrogen-related receptor α

Gacias, M., Pérez‐Martí, A., Pujol‐Vidal, M., Marrero, P. F., Haro, D., & Relat, J. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.06.051 · Cited by 12

Compensatory responses of the insulin signaling pathway restore muscle glucose uptake following long-term denervation

Callahan, Z. J., Oxendine, M., Wheatley, J. L., Menke, C. A., Cassell, E. A., Bartos, A., Geiger, P. C., & Schaeffer, P. J. (2015) · Physiological Reports · doi:10.14814/phy2.12359 · Cited by 11

Comparative Genomic Characterization of Buffalo Fibronectin Type III Domain Proteins: Exploring the Novel Role of FNDC5/Irisin as a Ligand of Gonadal Receptors

Wu, S., Hassan, F., Luo, Y., Fatima, I., Ahmed, I., Ihsan, A., Safdar, W., Liu, Q., & Rehman, S. U. (2021) · Biology · doi:10.3390/biology10111207 · Cited by 11

Development of a Novel PPARγ Ligand Screening System Using Pinpoint Fluorescence-Probed Protein

Nagai, H., Ebisu, S., Abe, R., Goto, T., Takahashi, N., Hosaka, T., & Kawada, T. (2011) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.100810 · Cited by 11

Diesel Exhaust Particle-Induced Airway Responses are Augmented in Obese Rats

Moon, K., Park, M. K., Leikauf, G. D., Park, C., & Jang, A. (2014) · International Journal of Toxicology · doi:10.1177/1091581813518355 · Cited by 12

Non-canonical hepatic androgen receptor mediates glucagon sensitivity in female mice through the PGC1α/ERRα/mitochondria axis

Chen, J., Wu, Y., Hao, W., You, J. E., & Wu, L. (2025) · Cell Reports · doi:10.1016/j.celrep.2024.115188 · Cited by 10

ESRRB plays a crucial role in the promotion of porcine cell reprograming

Yang, F., Ren, Y., Li, H., & Wang, H. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26063 · Cited by 10

PGC‐1β Modulates the Expression of Genes Involved in Mitochondrial Function and Adipogenesis During Preadipocyte Differentiation

Ji, H. L., Lu, R., Chang, Z., Su, S., & Yang, G. (2011) · Reproduction in Domestic Animals · doi:10.1111/j.1439-0531.2011.01894.x · Cited by 11

Sex differences in mitochondrial gene expression during viral myocarditis

Florio, D. N. D., Weigel, G. J., Gorelov, D. J., McCabe, E. J., Beetler, D. J., Shapiro, K. A., Bruno, K. A., Chekuri, I., Jain, A., Whelan, E. R., et al. (2024) · Biology of Sex Differences · doi:10.1186/s13293-024-00678-0 · Cited by 10

Genetic effect of single‐nucleotide polymorphisms in the PPARGC1B gene on airway hyperreactivity in asthmatic patients

Lee, S. ‐., Jang, A., Park, S. W., Park, J. ‐., Kim, Y. K., Uh, S., Kim, Y., Chung, I. Y., Park, B. L., Shin, H. D., et al. (2011) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2011.03801.x · Cited by 8

Estrogen-related receptor alpha: an orphan finds a family

Ochnik, A. M., & Yee, D. (2012) · Breast Cancer Research · doi:10.1186/bcr3124 · Cited by 9

Metabolomic analysis on blood of transgenic mice overexpressing PGC-1α in skeletal muscle

Sugimoto, T., Uchitomi, R., Hatazawa, Y., Miura, S., & Kamei, Y. (2021) · Bioscience Biotechnology and Biochemistry · doi:10.1093/bbb/zbaa059 · Cited by 8

Transcriptional ERRγ2-mediated activation is regulated by sentrin-specific proteases

Hentschke, M., Süsens, U., & Borgmeyer, U. (2008) · Biochemical Journal · doi:10.1042/bj20081556 · Cited by 8

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Ouyang, X., Zhu, X., Wang, L., Zheng, X., & Wang, J. (2023) · Apidologie · doi:10.1007/s13592-023-01042-8 · Cited by 6

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Palou, A., Bonet, M. L., Serra, F. A., & Picó, C. (2010) · Springer eBooks · doi:10.1007/978-1-4419-6039-9_15 · Cited by 5

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Foryst‐Ludwig, A., Clemenz, M., Hohmann, S., Hartge, M., Sprang, C., Frost, N., Krikov, M., Bhanot, S., Barros, R. P. A., Morani, A., et al. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000108 · Cited by 291

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Huss, J. M. (2002)

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