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 accessAbstract
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.
Overview
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
Cites
Statistics
Verification
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?
In the citing paper
“In addition, PGC-1␣ and PGC-1 coactivate different nuclear receptors (272).”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [272]
In the citing paper
“Taken together, these studies suggest that modest overexpression of PGC-1␣ (261, 262) and transgenic overexpression of PGC-1 (271, 272) increase oxidative metabolism and insulin sensitivity.”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [272]
In the citing paper
“Consistent with these findings, whole-body transgenic overexpression of PGC-1 resulted in increased oxidative metabolism, protection from obesity induced by high-fat diet or hyperphagia, and enhanced insulin sensitivity (272).”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [272]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
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
Friedman, J. M. (2000) · Nature · doi:10.1038/35007504 · Cited by 709
Research works printed but not linked: 1
- Maxwell, G. M., Nobbs, S. & Bates, D. J. (1987) Am. J. Physiol. 253, E264-E270.3115113
Cited by
Sorted by citations
Items 301–364 of 364
Wan, Y. (2010) · Cited by 3
Sugimoto, T., Sakamaki, C., Kimura, T., Eguchi, T., Miura, S., & Kamei, Y. (2024) · Scientific Reports · doi:10.1038/s41598-024-52198-x · Cited by 3
Good, D. J. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-285-4_71 · Cited by 3
Role of FKBP51 and FKBP52 in glucocorticoid receptor regulated metabolism
Warrier, M. (2008) · OhioLink ETD Center (Ohio Library and Information Network) · Cited by 3
Cold exposure induces the constitutively active thermogenic receptor, GPR3, via ERRα and ERRγ
Johansen, O. S., McIntyre, R. L., Rahbani, J. F., Zhang, Q., Scholtes, C., Lagarde, D., Billon, C., Côté, I., Delgado-Martin, M., Tandio, D., et al. (2025) · Molecular Metabolism · doi:10.1016/j.molmet.2025.102277 · Cited by 3
Structural Pharmacology of Estrogen-Related Receptors
Zhao, P., Fang, H., Elgendy, B., & Hegazy, L. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.5c00661 · Cited by 2
Estrogen-Related Receptors and Breast Cancer: A Mini Review
Therkildsen, C., & Richard-Fiardo, P. (2011) · InTech eBooks · doi:10.5772/20623 · Cited by 2
Rodents as genetic models of obesity
Imai, Y., & Ahima, R. S. (2005) · Drug Discovery Today Disease Models · doi:10.1016/j.ddmod.2005.08.005 · Cited by 2
Vitamin D Activates Various Gene Expressions, Including Lipid Metabolism, in C2C12 Cells
Mizutani, S., Oyabu, M., YAMAMOTO, A., Uchitomi, R., SUGIMOTO, T., & Kamei, Y. (2022) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.68.65 · Cited by 2
Kamei, Y., Hatazawa, Y., Yoshimura, R., & Miura, S. (2015) · doi:10.11648/j.bs.20150101.12 · Cited by 2
Skeletal Muscle Formation, Regeneration, and Recovery from Injury
Myers, C. M. (2024) · Springer eBooks · doi:10.1007/978-3-031-47065-3_7 · Cited by 1
Influencing energy expenditure and substrate utilisation
Clapham, J. C., & Arch, J. R. S. (2008) · Birkhäuser Basel eBooks · doi:10.1007/978-3-7643-7425-9_8 · Cited by 1
Muscle-Specific PPAR β/δ Agonism May Provide Synergistic Benefits with Life Style Modifications
Erol, A. (2007) · PPAR Research · doi:10.1155/2007/30578 · Cited by 1
Thermogenesis and the Metabolic Syndrome
Bonet, M. L., Picó, C., & Palou, A. (2005) · Elsevier eBooks · doi:10.1016/b978-84-8174-892-5.50017-6 · Cited by 2
Role of PPARγ in adipocyte recruitment and thermogenesis
Nora, E. D., Gray, S. L., & Vidal‐Puig, A. (2007) · Expert Review of Endocrinology & Metabolism · doi:10.1586/17446651.2.5.641 · Cited by 1
Huang, M. N., Prasad, R. B., Coral, D., Hjort, L., Minja, D. T. R., Mulder, H., Franks, P. W., & Kalamajski, S. (2024) · Diabetes · doi:10.2337/db23-0531 · Cited by 3
Sato, T., Morita, A., Watanabe, Y., Naito, Y., Kawaji, H., Nakagawa, T., Hamaguchi, H., Manabe, Y., FUJII, N. L., Ogo, N., et al. (2025) · The Journal of Physiological Sciences · doi:10.1016/j.jphyss.2025.100012 · Cited by 1
ESTROGEN RECEPTORS IN SKELETAL MUSCLE
Wiik, A. (2008) · Figshare · Cited by 4
Bezuidenhout, N. (2011) · SUNScholar (Stellenbosch University) · Cited by 1
The regulation of metabolic gene expression in humans
Tisdale, P. B. (2011) · Nottingham ePrints (University of Nottingham)
Liu, Y. (2013) · RMIT Research Repository (RMIT University Library) · doi:10.25439/rmt.27332901
THE FUNCTION OF NR3B AND NR4A ORPHAN NUCLEAR RECEPTORS IN OSTEOBLASTS
Rajalin, A.-M. (2011) · Työväentutkimus Vuosikirja
To Divide or Not to Divide; MicroRNAs and Small Compounds as Modulators of Mitosis
Mäki-Jouppila, J. H. (2015) · UTUPub (University of Turku)
Beyond the scale: understanding mechanisms of weight gain and obesity in diabetes
Goldfine, A. B. (2005) · Current Opinion in Endocrinology & Diabetes · doi:10.1097/01.med.0000158151.47287.95
ESRRA (estrogen-related receptor alpha)
Stein, K. R., & Dp, M. (2011) · Atlas of Genetics and Cytogenetics in Oncology and Haematology · doi:10.4267/2042/44776
EFFECTS OF EXERCISE TRAINING ON BRAIN BIOENERGETICS: LACTATE AS A KEY MEDIATOR
Lezi, E. (2013) · KU ScholarWorks (University of Kansas)
Sylvain-Drolet, G. (2011) · eScholarship@McGill (McGill) · doi:10.82308/43435
mouse skeletal muscle Identification of the circadian transcriptome in adult
Barber, B. K., Miller, B. H., Walker, J. R., McCarthy, J., Andrews, J. L., McDearmon, E. L., Kenneth, S. K., Harfmann, B. D., Schroder, E. A., & Esser, K. A. (2015)
Silveira, M. A. D. (2015) · Americanae (AECID Library)
CONTROL TRANSCRIPCIONAL I AL·LOSTÈRIC DEL GEN CARNITINA PALMITOÏLTRANSFERASA 1B (CPT1B)
de Farmàcia, F., de Bioquímica, D., & Molecular, I. B. (2006)
Yeo, J. C. (2015) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/62942
Nuclear Receptor Coactivators Co-ordinate Metabolic Responses to Hormonal and Environmental Stimuli
Evans, R. M., Downes, M., Nofsinger, R. R., Sonoda, J., & Yu, R. T. (2008) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789812819178_0018
Adipose Drug Targets for Obesity Treatment
Giacobino, J., Lehr, L., & Boss, O. (2007) · CRC Press eBooks · doi:10.1201/9781420005479.pt4
Regulation of Bone Resorption by PPARγ
Wei, W., & Wan, Y. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-415784-2.00010-5
Good, D. J. (2008)
HEK293A Cells Memorize a Brief Cold Exposure via a PPARα-Mediated Positive-Feedback Mechanism
Alfaqaan, S. (2019) · Kyoto University Research Information Repository (Kyoto University) · doi:10.14989/doctor.k21977
Seneviratne, A. M. P. B., Lidagoster, S., Valbuena-Castor, S., Lashley, K., Saha, S., Alimova, A., & Kreitzer, G. E. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.08.515201
Mechanism of Gene Regulation in Skeletal Muscle Function
Kamei, Y. (2022) · Nippon Eiyo Shokuryo Gakkaishi · doi:10.4327/jsnfs.75.267
Ma, Y., Cai, G., Chen, J., Yang, X. Q., Hua, G., Han, D., Li, X., Feng, D., & Deng, X. (2024) · Figshare · doi:10.6084/m9.figshare.25017760
PGC1α in Skeletal Muscle Mediates Anti-Obesity Effects of Soy Isoflavones
SUGIMOTO, T., KIMURA, T., Oyabu, M., Uchitomi, R., Nakai, S., & Kamei, Y. (2024) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.70.434
Kato, M., Sato, T., Fuchino, H., KAWAKAMI, H., Yoshimatsu, K., IIJIMA, K., HIRAOKA, S., Kun, T. A. N. G., Manabe, Y., FUJII, N. L., et al. (2025) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.71.256
Ma, Y., Cai, G., Chen, J., Yang, X., Hua, G., Han, D., Li, X., Feng, D., & Deng, X. (2024) · Figshare · doi:10.6084/m9.figshare.26668812
Ma, Y., Cai, G., Chen, J., Yang, X., Hua, G., Han, D., Li, X., Feng, D., & Deng, X. (2024) · Figshare · doi:10.6084/m9.figshare.26668815
Ma, Y., Cai, G., Chen, J., Yang, X., Hua, G., Han, D., Li, X., Feng, D., & Deng, X. (2024) · Figshare · doi:10.6084/m9.figshare.25017946
Ma, Y., Cai, G., Chen, J., Yang, X., Hua, G., Han, D., Li, X., Feng, D., & Deng, X. (2024) · Figshare · doi:10.6084/m9.figshare.26668809
Dahan, A., Ifrah, S., Yarmolinsky, L., Khalfin, B., Fleisher‐Berkovich, S., & Ben‐Shabat, S. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27052507
Role of PGC-1β and TIF2 co-regulators in mouse skeletal muscle function
Ramamoorthy, T. G. (2013) · theses.fr (ABES) · doi:10.70675/e05002c4z4806z4363z90b1z0e406b6c0e4c
The role of serotoninergic neurons in amyotrophic lateral sclerosis
Oussini, H. E. (2016) · theses.fr (ABES) · doi:10.70675/2431e8ddzd4e4z4710z81dcz14100daa6294
Conditional truncation of the FUS protein in mice : a new animal model of the ALS/FTD continuum
Scekic‐Zahirovic, J. (2016) · theses.fr (ABES) · doi:10.70675/6bed4f95z0a05z438fz937ez33f29f11923d
Kaminski, L. (2018) · theses.fr (ABES) · doi:10.70675/7f6ae88bz4f3cz49d3zafcdz8682254b2be3
Etude des isoformes du gène PGC-1a dans le développement musculaire chez le bovin
Bamba‐Funck, J. (2018) · theses.fr (ABES) · doi:10.70675/ffb388c0z6084z4cf4z83bez9c767829ded2
Wang, D., Hu, Q., Li, K., Jia, Q., Lin, H., Zhao, J. Y., Jiao, H., & Wang, X. (2026) · Poultry Science · doi:10.1016/j.psj.2026.107352
Wu, J., Liu, D., Xu, H., Zeng, L., Lin, P., Zhao, P., & Shen, G. (2026) · PLoS Genetics · doi:10.1371/journal.pgen.1012339
BindingDB (2020) · UC San Diego · doi:10.7270/q2w098f7
NR1L: A NOVEL NUCLEAR RECEPTOR GROUP ACTIVATED BY JUVENILE HORMONE ANALOGS
Li, Y. (2011) · TigerPrints (Clemson University)
Metadata
- 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
- 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
- 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