The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Myostatin Knockout Drives Browning of White Adipose Tissue through Activating the AMPK-PGC1α-Fndc5 Pathway in Muscle
Open accessAbstract
Myostatin (Mstn) is predominantly expressed in skeletal muscles and plays important roles in regulating muscle growth and development, as well as fat deposition. Mstn-knockout (Mstn(-/-)) mice exhibit increased muscle mass due to both hypertrophy and hyperplasia, and leaner body composition due to reduced fat mass. Here, we show that white adipose tissue (WAT) of Mstn(-/-) develops characteristics of brown adipose tissue (BAT) with dramatically increased expression of BAT signature genes, including Ucp1 and Pgc1α, and beige adipocyte markers Tmem26 and CD137. Strikingly, the observed browning phenotype is non-cell autonomous and is instead driven by the newly defined myokine irisin (Fndc5) secreted from Mstn(-/-) skeletal muscle. Within the muscle, Mstn(-/-) leads to increased expression of AMPK and its phosphorylation, which subsequently activates PGC1α and Fndc5. Together, our study defines a paradigm of muscle-fat crosstalk mediated by Fndc5, which is up-regulated and secreted from muscle to induce beige cell markers and the browning of WAT in Mstn(-/-) mice. These results suggest that targeting muscle Mstn and its downstream signaling represents a therapeutic approach to treat obesity and type 2 diabetes.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“It contributes to the induction of PGC-1α, FNDC5, and irisin in SkM [27,49,133].”
In the citing paper
“Secreted FNDC5 then promotes the browning of WAT, establishing muscle–fat crosstalk that enhances energy expenditure and improves metabolic profiles [70].”
From Exercise-Induced Muscle–Fat Crosstalk: Molecular Mediators and Their Pharmacological Modulation for the Maintenance of Metabolic Flexibility in Aging (2025) · cites this paper as [70]
In the citing paper
“which in turn was due to the presence of the browning phenotype in the WAT, mainly because of an increase in the expression of irisin (Shan et al., 2013).”
From Physical Exercise-Induced Myokines and Muscle-Adipose Tissue Crosstalk: A Review of Current Knowledge and the Implications for Health and Metabolic Diseases (2018) · cites this paper as Shan et al., 2013
In the citing paper
“On the other hand, knockout animals for myostatin presented not only an increase in muscle mass but also an improvement in composition due to a reduction of fat mass”
From Physical Exercise-Induced Myokines and Muscle-Adipose Tissue Crosstalk: A Review of Current Knowledge and the Implications for Health and Metabolic Diseases (2018) · cites this paper as Shan et al., 2013
In the citing paper
“Importantly, the inhibition of myostatin signaling increases PGC1α and mitochondrial biogenesis 145, while mice deficient for myostatin show an improved metabolic phenotype and a resistance to HFD 146, 147.”
From Inter‐organ communication: a gatekeeper for metabolic health (2019) · cites this paper as [147]
Citations
Cites
Brown Adipose Tissue: Function and Physiological Significance
CANNON, B., & NEDERGAARD, J. (2004) · Physiological Reviews · doi:10.1152/physrev.00015.2003 · Cited by 6,433
A PGC1-α-dependent myokine that drives brown-fat-like development of white fat and thermogenesis
Boström, P., Wu, J., Jedrychowski, M. P., Korde, A., Ye, L., Lo, J. C., Rasbach, K. A., Boström, E. A., Choi, J. H., Long, J. Z., et al. (2012) · Nature · doi:10.1038/nature10777 · Cited by 4,810
Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013
Beige Adipocytes Are a Distinct Type of Thermogenic Fat Cell in Mouse and Human
Wu, J., Boström, P., Sparks, L. M., Li, Y., Choi, J. H., Giang, A.-H., Khandekar, M. J., Virtanen, K. A., Nuutila, P., Schaart, G., et al. (2012) · Cell · doi:10.1016/j.cell.2012.05.016 · Cited by 3,406
FGF21 regulates PGC-1α and browning of white adipose tissues in adaptive thermogenesis
Fisher, F. M., Kleiner, S., Douris, N., Fox, E. C., Mepani, R. J., Verdeguer, F., Wu, J., Kharitonenkov, A., Flier, J. S., Maratos-Flier, E., et al. (2012) · Genes & Development · doi:10.1101/gad.177857.111 · Cited by 1,478
Prdm16 determines the thermogenic program of subcutaneous white adipose tissue in mice
Seale, P., Conroe, H. M., Estall, J. L., Kajimura, S., Frontini, A., Ishibashi, J., Cohen, P., Cinti, S., & Spiegelman, B. M. (2010) · Journal of Clinical Investigation · doi:10.1172/jci44271 · Cited by 1,273
New role of bone morphogenetic protein 7 in brown adipogenesis and energy expenditure
Tseng, Y.-H., Kokkotou, E., Schulz, T. J., Huang, T. L., Winnay, J. N., Taniguchi, C. M., Tran, T. T., Suzuki, R., Espinoza, D. O., Yamamoto, Y., et al. (2008) · Nature · doi:10.1038/nature07221 · Cited by 1,099
Myostatin, a Negative Regulator of Muscle Growth, Functions by Inhibiting Myoblast Proliferation
Thomas, M., Langley, B., Berry, C., Sharma, M., Kirk, S., Bass, J., & Kambadur, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004356200 · Cited by 1,014
Brown Remodeling of White Adipose Tissue by SirT1-Dependent Deacetylation of Pparγ
Qiang, L., Wang, L., Kon, N., Zhao, W., Lee, S., Zhang, Y., ROSENBAUM, M. S., Zhao, Y., Gu, W. J., Farmer, S. R., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.027 · Cited by 816
Myostatin negatively regulates satellite cell activation and self-renewal
McCroskery, S., Thomas, M., Maxwell, L., Sharma, M., & Kambadur, R. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207056 · Cited by 784
Research works printed but not linked: 1
- Tsurutani Y., 2009, Myostatin (MSTN) inhibits adipogenesis and high‐fat induced obesity via smad3: a possibility of crosstalk between muscle and adipose tissue, Diabetes, 58, A436
Cited by
Sorted by citations
Items 101–200 of 300
Bone and muscle crosstalk in ageing and disease
Kirk, B., Lombardi, G., & Duque, G. (2025) · Nature Reviews Endocrinology · doi:10.1038/s41574-025-01088-x · Cited by 89
Feraco, A., Gorini, S., Armani, A., Camajani, E., Rizzo, M., & Caprio, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179327 · Cited by 78
The role of sex, adiposity, and gonadectomy in the regulation of irisin secretion
Zügel, M., Qiu, S., Laszlo, R., Bosnyák, E., Weigt, C., Müller, D. R., Diel, P. R., Steinacker, J. M., & Schümann, U. (2016) · Endocrine · doi:10.1007/s12020-016-0913-x · Cited by 76
Irisin prevents dexamethasone-induced atrophy in C2C12 myotubes
Chang, J. S., & Kong, I. D. (2020) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-020-02367-4 · Cited by 74
Canosa, L. F., & Bertucci, J. I. (2020) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2020.111029 · Cited by 72
Regulation of brown adipocyte metabolism by myostatin/follistatin signaling
Singh, R., Braga, M., & Pervin, S. (2014) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2014.00060 · Cited by 71
Irisin in obesity and type 2 diabetes
Højlund, K., & Boström, P. (2013) · Journal of Diabetes and its Complications · doi:10.1016/j.jdiacomp.2013.04.002 · Cited by 76
Wang, Q., Sun, J., Liu, M., Zhou, Y., Zhang, L., & Li, Y. (2021) · Biomolecules · doi:10.3390/biom11121757 · Cited by 77
Zhou, X., Chen, J., Chen, J., Wu, W.-C., Wang, X., & Wang, Y. (2015) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2015.08.014 · Cited by 69
Lkb1 Is Indispensable for Skeletal Muscle Development, Regeneration, and Satellite Cell Homeostasis
Shan, T., Zhang, P., Liang, X., Bi, P., Yue, F., & Kuang, S. (2014) · Stem Cells · doi:10.1002/stem.1788 · Cited by 74
Huerta, A. E., Prieto-Hontoria, P. L., Fernández‐Galilea, M., Sáinź, N., Cuervo, M., Martínez, J. A., & Moreno-Aliaga, M. J. (2015) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-015-0400-5 · Cited by 70
Li, A.-N., Chen, J.-J., Li, Q.-Q., Zeng, G.-Y., Chen, Q.-Y., Chen, J.-L., Liao, Z.-M., Jin, P., Wang, K.-S., & Yang, Z.-C. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.01.023 · Cited by 69
Myostatin signals through miR-34a to regulate Fndc5 expression and browning of white adipocytes
Ge, X., Sathiakumar, D., Lua, B.-N., Kukreti, H., Lee, M., & McFarlane, C. (2016) · International Journal of Obesity · doi:10.1038/ijo.2016.110 · Cited by 67
Taming the Flames: Targeting White Adipose Tissue Browning in Hypermetabolic Conditions
Abdullahi, A., & Jeschke, M. G. (2017) · Endocrine Reviews · doi:10.1210/er.2017-00163 · Cited by 68
Wetzlich, B., Nyakundi, B. B., & Yang, J. (2024) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-024-05120-y · Cited by 74
Vamvini, M. T., Aronis, K. N., Panagiotou, G., Huh, J. Y., Chamberland, J. P., Brinkoetter, M. T., Petrou, M., Christophi, C. A., Kales, S. N., Christiani, D. C., et al. (2013) · European Journal of Endocrinology · doi:10.1530/eje-13-0276 · Cited by 65
Skeletal muscle as a therapeutic target for delaying type 1 diabetic complications
Coleman, S. K. (2015) · World Journal of Diabetes · doi:10.4239/wjd.v6.i17.1323 · Cited by 67
Gao, S., Li, F., Li, H., Yi, H., Liu, Y., & Chen, Y. (2016) · PLoS ONE · doi:10.1371/journal.pone.0147480 · Cited by 63
Role of Irisin on the bone–muscle functional unit
Colaianni, G., & Grano, M. (2015) · BoneKEy Reports · doi:10.1038/bonekey.2015.134 · Cited by 58
Bonfante, I. L. P., Chacon‐Mikahil, M. P. T., Brunelli, D. T., Gáspari, A. F., Duft, R. G., Lopes, W. A., Bonganha, V., Libardi, C. A., & Cavaglieri, C. R. (2017) · European Journal of Sport Science · doi:10.1080/17461391.2017.1296025 · Cited by 60
Nonmuscle Tissues Contribution to Cancer Cachexia
Argilés, J. M. A., Stemmler, B., López-Soriano, F. J., & Busquets, S. (2015) · Mediators of Inflammation · doi:10.1155/2015/182872 · Cited by 59
Liu, X., Bauman, W. A., & Cardozo, C. P. (2018) · Physiological Reports · doi:10.14814/phy2.13837 · Cited by 61
Yano, N., Zhang, L., Wei, D., Dubielecka, P. M., Lei, W., Zhuang, S., Zhu, P., Qin, G., Liu, P. Y., Chin, Y. E., et al. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00219.2019 · Cited by 59
The weight of nutrients: kynurenine metabolites in obesity and exercise
Dadvar, S., Ferreira, D. M. S., Červenka, I., & Ruas, J. L. (2018) · Journal of Internal Medicine · doi:10.1111/joim.12830 · Cited by 59
Nong, Q., Wang, L., Zhou, Y., Sun, Y., Chen, W., Xie, J., Zhu, X., & Shan, T. (2020) · Animals · doi:10.3390/ani10091543 · Cited by 57
FNDC5: A novel player in metabolism and metabolic syndrome.
Cao, R. Y., Zheng, H., Redfearn, D., & Yang, J. (2019) · Biochimie · doi:10.1016/j.biochi.2019.01.001 · Cited by 49
Fan, L., Xu, H., Yang, R., Zang, Y., Chen, J., & Qin, H. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b02191 · Cited by 57
Caria, A. C. I., Nonaka, C. K. V., Cavalcante, B. R. R., Sousa, R. A. L. D., Aras, R., & Souza, B. S. D. F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144977 · Cited by 57
Qi, G., Zhou, Y., Zhang, X., Yu, J., Li, X., Cao, X., Wu, C., & Guo, P. (2018) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2018.10.004 · Cited by 54
Singh, R., Braga, M., Reddy, S. T., Lee, S.-J., Parveen, M., Grijalva, V., Vergnes, L., & Pervin, S. (2017) · Endocrinology · doi:10.1210/en.2016-1607 · Cited by 54
Imran, K. M., Rahman, N., Yoon, D., Jeon, M., Lee, B., & Kim, Y. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2017.08.001 · Cited by 54
Regulation of angiopoietin-like protein 4 production during and after exercise
Norheim, F., Hjorth, M., Langleite, T. M., Lee, S., Holen, T., Bindesbøll, C., Stadheim, H. K., Gulseth, H. L., Birkeland, K. I., Kielland, A., et al. (2014) · Physiological Reports · doi:10.14814/phy2.12109 · Cited by 53
Magnolol promotes thermogenesis and attenuates oxidative stress in 3T3-L1 adipocytes
Parray, H. A., Lone, J. B., Park, J. P., Choi, J. W., & Yun, J. W. (2018) · Nutrition · doi:10.1016/j.nut.2018.01.017 · Cited by 54
Current Evidence of the Role of the Myokine Irisin in Cancer
Tsiani, E., Tsakiridis, N., Kouvelioti, R., Jaglanian, A., & Klentrou, P. (2021) · Cancers · doi:10.3390/cancers13112628 · Cited by 52
High Serum Irisin Level as an Independent Predictor of Diabetes Mellitus
Huh, J. H., Ahn, S. V., Choi, J. H., Koh, S. B., & Chung, C. H. (2016) · Medicine · doi:10.1097/md.0000000000003742 · Cited by 51
Rao, Y., Yu, H., Gao, L., Lu, Y., Zhao, X. D., Liu, H., Gu, L., Ye, J., & Huang, Z. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13855 · Cited by 51
Liu, W., Shan, T., Yang, X., Liang, S., Zhang, P., Liu, Y., Liu, X., & Kuang, S. (2013) · Journal of Cell Science · doi:10.1242/jcs.124321 · Cited by 50
Sarcopenia and cachexia: molecular mechanisms and therapeutic interventions
Wang, T., Zhou, D., & Hong, Z. (2025) · MedComm · doi:10.1002/mco2.70030 · Cited by 46
Cai, C., Qian, L., Jiang, S., Sun, Y., Wang, Q., Ma, D., Xiao, G., Li, B., Xie, S., Gao, T., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.16822 · Cited by 51
Whole Body Vibration: A Valid Alternative Strategy to Exercise?
Bonanni, R., Cariati, I., Romagnoli, C., D’Arcangelo, G., Annino, G., & Tancredi, V. (2022) · Journal of Functional Morphology and Kinesiology · doi:10.3390/jfmk7040099 · Cited by 48
Neonatal vitamin A injection promotes cattle muscle growth and increases oxidative muscle fibers
Wang, B., Nie, W., Fu, X., de Avila, J. M., Ma, Y., Zhu, M. J., Maquivar, M., Parish, S. M., Busboom, J. R., Nelson, M. L., et al. (2018) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-018-0296-3 · Cited by 50
Myostatin/Activin Receptor Ligands in Muscle and the Development Status of Attenuating Drugs
Rodgers, B. D., & Ward, C. W. (2022) · Endocrine Reviews · doi:10.1210/endrev/bnab030 · Cited by 111
Irisin treatment improves healing of dystrophic skeletal muscle
Reza, M. M., Sim, C. M., Subramaniyam, N., Ge, X., Sharma, M., Kambadur, R., & McFarlane, C. (2017) · Oncotarget · doi:10.18632/oncotarget.21636 · Cited by 45
Komolka, K., Albrecht, E., Schering, L., Brenmoehl, J., Hoeflich, A., & Maak, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0088060 · Cited by 44
Breaking BAT: can browning create a better white?
Warner, A., & Mittag, J. (2015) · Journal of Endocrinology · doi:10.1530/joe-15-0408 · Cited by 45
Pervin, S., Reddy, S. T., & Singh, R. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.653179 · Cited by 42
Zamboni, M. M., Mazzali, G., Brunelli, A., Saatchi, T., Urbani, S., Giani, A., Rossi, A. P., Zoico, E., & Fantin, F. (2022) · Cells · doi:10.3390/cells11213361 · Cited by 47
Impact of exercise on muscle and nonmuscle organs
Boström, P., Graham, E. L., Georgiadi, A., & Ma, X. (2013) · IUBMB Life · doi:10.1002/iub.1209 · Cited by 50
IMB0901 inhibits muscle atrophy induced by cancer cachexia through MSTN signaling pathway
Liu, D., Qiao, X., Ge, Z., Shang, Y., Li, Y., Wang, W., Chen, M., Si, S., & Chen, S. (2019) · Skeletal Muscle · doi:10.1186/s13395-019-0193-2 · Cited by 42
Muscle-Bone Crosstalk in Chronic Obstructive Pulmonary Disease
Zhang, L., & Sun, Y. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.724911 · Cited by 42
Tero-Vescan, A., Degens, H., Matsakas, A., Ștefănescu, R., Ősz, B. E., & Slevin, M. (2025) · Pharmaceuticals · doi:10.3390/ph18081222 · Cited by 44
Effects of a Phosphodiesterase inhibitor on the Browning of Adipose Tissue in Mice
Seo, D. H., Shin, E., Lee, Y., Park, S., Nam, K. T., Kim, J. W., & Soo, B. (2022) · Biomedicines · doi:10.3390/biomedicines10081852 · Cited by 41
Cornish, S. M., Bugera, E. M., Duhamel, T. A., Peeler, J. D., & Anderson, J. E. (2020) · European Journal of Applied Physiology · doi:10.1007/s00421-020-04337-1 · Cited by 43
Brown and beige adipose tissues: phenotype and metabolic potential in mice and men
Chechi, K., Lichtenbelt, W. D. V. M., & Richard, D. (2017) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00021.2017 · Cited by 40
Muscle-Bone Crosstalk in Chronic Kidney Disease: The Potential Modulatory Effects of Exercise
Leal, D. V., Ferreira, A., Watson, E. L., Wilund, K. R., & Viana, J. L. (2021) · Calcified Tissue International · doi:10.1007/s00223-020-00782-4 · Cited by 40
Tao, B., Tan, J., Chen, L., Xu, Y., Liao, X., Li, Y., Chen, J., Song, Y., & Hu, W. (2021) · Aquaculture · doi:10.1016/j.aquaculture.2021.737097 · Cited by 40
Shero, J. A., Lindholm, M. E., Sandri, M. F., & Stanford, K. I. (2025) · Circulation Research · doi:10.1161/circresaha.124.325614 · Cited by 45
Yamakage, H., Tanaka, M., Inoue, T., Odori, S., Kusakabe, T., & Satoh‐Asahara, N. (2019) · Journal of Diabetes Investigation · doi:10.1111/jdi.13179 · Cited by 39
Liu, L., Zhang, T., Hu, J., Ma, R., He, B., Wang, M., & Wang, Y. (2019) · Obesity Surgery · doi:10.1007/s11695-019-04295-4 · Cited by 40
Beige Adipocyte as the Flame of White Adipose Tissue: Regulation of Browning and Impact of Obesity
Altınova, A. E. (2021) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgab921 · Cited by 39
Lkb1 Deletion Promotes Ectopic Lipid Accumulation in Muscle Progenitor Cells and Mature Muscles
Shan, T., Zhang, P., Bi, P., & Kuang, S. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24831 · Cited by 37
Serum irisin and myostatin levels after 2 weeks of high-altitude climbing
Śliwicka, E., Cisoń, T., Kasprzak, Z., Nowak, A., & Pilaczyńska-Szczȩśniak, Ł. (2017) · PLoS ONE · doi:10.1371/journal.pone.0181259 · Cited by 36
Mammalian target of rapamycin is essential for cardiomyocyte survival and heart development in mice
Zhang, P., Shan, T., Liang, X., Deng, C., & Kuang, S. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.08.046 · Cited by 35
Irisin regulates cardiac physiology in zebrafish
Sundarrajan, L., Yeung, C., Hahn, L., Weber, L. P., & Unniappan, S. (2017) · PLoS ONE · doi:10.1371/journal.pone.0181461 · Cited by 35
Muscle fiber-type conversion in the transgenic pigs with overexpression of PGC1α gene in muscle
Fei, Y., Zhang, L., Bu, G., Xiong, Y., & Zuo, B. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.113 · Cited by 35
AMP-activated protein kinase is required for the anti-adipogenic effects of alpha-linolenic acid
Zhou, X., Wu, W.-C., Chen, J., Wang, X., & Wang, Y. (2015) · Nutrition & Metabolism · doi:10.1186/s12986-015-0006-5 · Cited by 34
The Heating Microenvironment: Intercellular Cross Talk Within Thermogenic Adipose Tissue
Knights, A. J., Wu, J., & Tseng, Y. (2020) · Diabetes · doi:10.2337/db20-0303 · Cited by 35
Do Bariatric Surgeries Enhance Brown/Beige Adipose Tissue Thermogenesis?
Hankir, M. K., & Seyfried, F. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00275 · Cited by 34
Myostatin inhibition therapy for insulin-deficient type 1 diabetes
Coleman, S. K., Rebalka, I. A., D’Souza, D. M., Deodhare, N., Desjardins, E. M., & Hawke, T. J. (2016) · Scientific Reports · doi:10.1038/srep32495 · Cited by 34
Abdul-Rahman, O., Kristóf, E., Doan‐Xuan, Q., Vida, A., Nagy, L., Horváth, A., Simon, J., Maros, T., Szentkirályi, I., Palotás, L., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0157644 · Cited by 32
Exercise‐Induced cytokines, diet, and inflammation and their role in adipose tissue metabolism
Al‐Ibraheem, A. M. T., Hameed, A. A. Z., Marsool, M. D. M., Jain, H., Prajjwal, P., Khazmi, I., Nazzal, R., Al-Najati, H. M. H., Al‐Zuhairi, B. H. Y. K., Razzaq, M., et al. (2024) · Health Science Reports · doi:10.1002/hsr2.70034 · Cited by 33
Pauly, M., Chabi, B., Favier, F. B., Vanterpool, F., Matecki, S., Fouret, G., Bonafos, B., Vernus, B., Feillet‐Coudray, C., Coudray, C., et al. (2014) · The Journals of Gerontology Series A · doi:10.1093/gerona/glu147 · Cited by 29
Myostatin Attenuation In Vivo Reduces Adiposity, but Activates Adipogenesis
Li, N., Yang, Q., Walker, R. G., Thompson, T. B., Du, ., & Rodgers, B. D. (2015) · Endocrinology · doi:10.1210/en.2015-1546 · Cited by 29
From Exercise to Cognitive Performance: Role of Irisin
Pesce, M., Fratta, I. L., Paolucci, T., Grilli, A., Patruno, A., Agostini, F., Bernetti, A., Mangone, M., Paoloni, M., Invernizzi, M., et al. (2021) · Applied Sciences · doi:10.3390/app11157120 · Cited by 29
Rabiee, F., Forouzanfar, M., Zadegan, F. G., Tanhaei, S., Ghaedi, K., Motovali-Bashi, M., Baharvand, H., & Nasr‐Esfahani, M. H. (2014) · Gene · doi:10.1016/j.gene.2014.08.045 · Cited by 29
Irisin promotes the browning of white adipocytes tissue by AMPKα1 signaling pathway
Luo, X., Li, J., Zhang, H., Wang, Y., Shi, H., Ge, Y., Yu, X., Wang, H., & Dong, Y. (2022) · Research in Veterinary Science · doi:10.1016/j.rvsc.2022.08.025 · Cited by 25
The key role of myostatin b in somatic growth in fishes derived from distant hybridization
Liu, Q., Duan, L., Li, B., Zhang, X., Liu, F., Yu, J., Shu, Y., Hu, F., Lin, J., Xiong, X., et al. (2024) · Science China Life Sciences · doi:10.1007/s11427-023-2487-8 · Cited by 26
Eilers, W., Chambers, D. J., Cleasby, M. E., & Foster, K. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00185.2019 · Cited by 29
Molecular pathways regulating the formation of brown‐like adipocytes in white adipose tissue
Fu, J., Li, Z., Zhang, H., Mao, Y., Wang, A., Wang, X., Zou, Z., & Zhang, X. (2014) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.2600 · Cited by 29
Li, H., Zhang, C., Liu, J., Xie, W., Xu, W., Liang, F., Huang, K., & He, X. (2019) · PLoS ONE · doi:10.1371/journal.pone.0220310 · Cited by 26
The Controversial Role of Irisin in Clinical Management of Coronary Heart Disease
Ou-Yang, W.-L., Guo, B., Xu, F., Lin, X., Li, F., Shan, S., Wu, F., Wang, Y., Zheng, M.-H., Xu, Q.-S., et al. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.678309 · Cited by 25
Cariati, I., Bonanni, R., Pallone, G., Romagnoli, C., Rinaldi, A. M., Annino, G., D’Arcangelo, G., & Tancredi, V. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810388 · Cited by 25
Kim, S., Park, D., LEE, S.-H., Kwak, H., & Kang, J. (2023) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000003136 · Cited by 25
Fighting obesity: When muscle meets fat
Yang, X., Bi, P., & Kuang, S. (2014) · Adipocyte · doi:10.4161/21623945.2014.964075 · Cited by 25
Bubak, M. P., Heesch, M., Shute, R. J., Dinan, N. E., Laursen, T. L., Salle, D. T. L., & Slivka, D. R. (2017) · International journal of exercise science · doi:10.70252/xkmw8211 · Cited by 24
Irisin Serum Levels and Skeletal Muscle Assessment in a Cohort of Charcot-Marie-Tooth Patients
Colaianni, G., Oranger, A., Dicarlo, M., Lovero, R., Storlino, G., Pignataro, P., Fontana, A., Serio, F. D., Ingravallo, A., Caputo, G., et al. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.886243 · Cited by 25
Serum myostatin levels are associated with abdominal aortic calcification in dialysis patients
Lee, S. M., Kim, S. E., Lee, J. Y., Jeong, H. J., Son, Y. K., & An, W. S. (2019) · Kidney Research and Clinical Practice · doi:10.23876/j.krcp.19.019 · Cited by 23
Myostatin inhibits porcine intramuscular preadipocyte differentiation in vitro
Sun, W. X., Dodson, M. V., Jiang, Z., Yu, S., Chu, W., & Chen, J. (2015) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2015.10.005 · Cited by 23
Wang, H., Guo, S., Gao, H., Ding, J., Li, H., Kong, X., Zhang, S., He, M., Feng, Y., Wu, W., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci178303 · Cited by 22
Vita, F., Gangemi, S., Pioggia, G., Trimarchi, F., & Mauro, D. D. (2022) · Medicina · doi:10.3390/medicina58060767 · Cited by 20
Zhou, S., Qian, B., Wang, L., Zhang, C., Hogan, M. V., & Li, H. (2018) · Muscle & Nerve · doi:10.1002/mus.26195 · Cited by 22
Zhang, L., Li, C., Xiong, J., Chang, C. H., & Sun, Y. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.929926 · Cited by 22
Skeletal muscle AMPK is essential for the maintenance of FNDC5 expression
Lally, J., Ford, R. J., Johar, J., Crane, J. D., Kemp, B. E., & Steinberg, G. R. (2015) · Physiological Reports · doi:10.14814/phy2.12343 · Cited by 21
Role and Functions of Irisin: A Perspective on Recent Developments and Neurodegenerative Diseases
Minuti, A., Raffaele, I., Scuruchi, M., Lui, M., Muscarà, C., & Calabrò, M. (2025) · Antioxidants · doi:10.3390/antiox14050554 · Cited by 27
Zhang, Y., Wang, L., Kang, H., Lin, C.-Y. J., & Fan, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076551 · Cited by 21
Zheng, Y., Ni, Y., Pang, Y., Gong, Y., Yang, H., Ding, W., & Yang, H. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1132342 · Cited by 20
Tsukamoto, M., Wang, K., Tasaki, T., Murata, Y., Okada, Y., Yamanaka, Y., Nakamura, E., Yamada, S., Izumi, H., Zhou, Q., et al. (2018) · Bone · doi:10.1016/j.bone.2018.10.009 · Cited by 20
Maternal inheritance of circulating irisin in humans
Al‐Daghri, N. M., Al-Attas, O. S., Alokail, M. S., Alkharfy, K. M., Yousef, M., Vinodson, B., Amer, O. E., Alnaami, A. M., Sabico, S., Tripathi, G., et al. (2014) · Clinical Science · doi:10.1042/cs20130426 · Cited by 18
Natural constituents from food sources: potential therapeutic agents against muscle wasting
Shen, S., Yu, H., Gan, L., Yang, Y., & Lin, L. (2019) · Food & Function · doi:10.1039/c9fo00912d · Cited by 20
Endocrine Mechanisms Connecting Exercise to Brown Adipose Tissue Metabolism: a Human Perspective
Méndez-Gutiérrez, A., Osuna‐Prieto, F. J., Aguilera, C. M., Ruiz, J. R., & Sánchez‐Delgado, G. (2020) · Current Diabetes Reports · doi:10.1007/s11892-020-01319-7 · Cited by 17
Metadata
- Authors
- Shan, T., Liang, X., Bi, P., & Kuang, S.
- Affiliations
- Purdue University West Lafayette (US)
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2013-01-29
- Volume
- 27
- Issue
- 5
- Pages
- 1981-1989
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- PMC
- PMC3633817
- OpenAlex
- W2124205424
- Cited by
- 301
- References
- 49
- Citations by year
- 2026: 6 · 2025: 15 · 2024: 15 · 2023: 16 · 2022: 30 · 2021: 28 · 2020: 20 · 2019: 26 · 2018: 19 · 2017: 26 · 2016: 21 · 2015: 30 · 2014: 31 · 2013: 18
- FWCI
- 23.21
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The FASEB Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Muscular Dystrophy Association
- National Institutes of Health
- U.S. Department of Agriculture
- Topics
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Keywords
- myostatin, white adipose tissue browning, brown adipose tissue, AMPK, PGC-1α, FNDC5, irisin, beige adipocytes, skeletal muscle, non-cell-autonomous signaling, obesity, type 2 diabetes, UCP1, 4-1BB
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Adenylate Kinase, Animals, Adipose Tissue, Brown, Fibronectins, Transcription Factors, Trans-Activators, Up-Regulation, Mice, Knockout, Muscle, Skeletal, Mice, Adipose Tissue, White, Myostatin
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