The DOI matches its Crossref record; 49 of the 51 references it cites were found in a registry or an index.
Myostatin Inhibition in Muscle, but Not Adipose Tissue, Decreases Fat Mass and Improves Insulin Sensitivity
Open accessAbstract
Myostatin (Mstn) is a secreted growth factor expressed in skeletal muscle and adipose tissue that negatively regulates skeletal muscle mass. Mstn(-/-) mice have a dramatic increase in muscle mass, reduction in fat mass, and resistance to diet-induced and genetic obesity. To determine how Mstn deletion causes reduced adiposity and resistance to obesity, we analyzed substrate utilization and insulin sensitivity in Mstn(-/-) mice fed a standard chow. Despite reduced lipid oxidation in skeletal muscle, Mstn(-/-) mice had no change in the rate of whole body lipid oxidation. In contrast, Mstn(-/-) mice had increased glucose utilization and insulin sensitivity as measured by indirect calorimetry, glucose and insulin tolerance tests, and hyperinsulinemic-euglycemic clamp. To determine whether these metabolic effects were due primarily to the loss of myostatin signaling in muscle or adipose tissue, we compared two transgenic mouse lines carrying a dominant negative activin IIB receptor expressed specifically in adipocytes or skeletal muscle. We found that inhibition of myostatin signaling in adipose tissue had no effect on body composition, weight gain, or glucose and insulin tolerance in mice fed a standard diet or a high-fat diet. In contrast, inhibition of myostatin signaling in skeletal muscle, like Mstn deletion, resulted in increased lean mass, decreased fat mass, improved glucose metabolism on standard and high-fat diets, and resistance to diet-induced obesity. Our results demonstrate that Mstn(-/-) mice have an increase in insulin sensitivity and glucose uptake, and that the reduction in adipose tissue mass in Mstn(-/-) mice is an indirect result of metabolic changes in skeletal muscle. These data suggest that increasing muscle mass by administration of myostatin antagonists may be a promising therapeutic target for treating patients with obesity or diabetes.
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?
The cited source doesn’t support the claim as written.
In the citing paper
“Its importance in this tissue is related to the maintenance of adipose mass and greater sensitivity to insulin (Hamrick et al., 2006; Guo et al., 2009).”
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 Guo et al., 2009
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Evidence that myostatin needs to act on skeletal muscle to cause fat loss comes from a study where the knock out myostatin receptor in adipose tissue had no effect on body composition, weight gain, or glucose and insulin tolerance in mice fed a standard or high-fat diet [181].”
From Effects of Skeletal Muscle Hypertrophy on Fat Mass and Glucose Homeostasis in Humans and Animals: A Narrative Review with Systematic Literature Search (2025) · cites this paper as [181]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“For example, the stimulation of skeletal muscle hypertrophy by expressing constitutively active Akt1 [22] only within muscle, or by knocking down the myostatin (i.e., activin IIB) receptor only in muscle [181], demonstrates that muscle hypertrophy is sufficient to cause fat loss and improve glucose homeostasis as secondary effects.”
From Effects of Skeletal Muscle Hypertrophy on Fat Mass and Glucose Homeostasis in Humans and Animals: A Narrative Review with Systematic Literature Search (2025) · cites this paper as [181]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“It also exerts a significant regulatory influence on adipose tissue function, energy metabolism, and systemic energy homeostasis [62].”
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 [62]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“However, myostatin is not exclusively secreted by SkM tissue, with studies indicating that AT also secretes this protein.”
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 Guo et al., 2009
Experimental — accuracy not yet measured
In the citing paper
“Adipocyte-specific expression of a dominant negative form of Acvr2b did not induce any changes in body composition, suggesting that changes in fat mass are not directly due to loss of ActRII signaling in adipose tissue [26].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [26]
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
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
Self-citationRegulation of myostatin activity and muscle growth
Lee, S.-J., & McPherron, A. C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151270098 · Cited by 1,616
Self-citationFolland, J. P., & Williams, A. G. (2007) · Sports Medicine · doi:10.2165/00007256-200737020-00004 · Cited by 1,347
Musarò, A., McCullagh, K., Paul, A., Houghton, L., Dobrowolny, G., Molinaro, M., Barton, E. R., L Sweeney, H., & Rosenthal, N. (2001) · Nature Genetics · doi:10.1038/84839 · Cited by 1,137
Physical Activity/Exercise and Type 2 Diabetes
Sigal, R. J., Kenny, G. P., Wasserman, D. H., Castaneda-Sceppa, C., & White, R. D. (2006) · Diabetes Care · doi:10.2337/dc06-9910 · Cited by 949
Induction of Cachexia in Mice by Systemically Administered Myostatin
Zimmers, T. A., Davies, M. V., Koniaris, L. G., Haynes, P. A., Esquela‐Kerscher, A., Tomkinson, K. N., McPherron, A. C., Wolfman, N. M., & Lee, S. (2002) · Science · doi:10.1126/science.1069525 · Cited by 908
Self-citationFunctional improvement of dystrophic muscle by myostatin blockade
Bogdanovich, S., Krag, T. O. B., Barton, E. R., Morris, L. D., Whittemore, L.-A., Ahima, R. S., & Khurana, T. S. (2002) · Nature · doi:10.1038/nature01154 · Cited by 831
REGULATION OF MUSCLE MASS BY MYOSTATIN
Lee, S.-J. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.012103.135836 · Cited by 819
Life without white fat: a transgenic mousePreprint
Moitra, J., Mason, M. M., Olive, M., Krylov, D. Y., Gavrilova, O., Marcus‐Samuels, B., Feigenbaum, L., Lee, E., Aoyama, T., Eckhaus, M., et al. (1998) · Genes & Development · doi:10.1101/gad.12.20.3168 · Cited by 776
Self-citationInhibition of myostatin in adult mice increases skeletal muscle mass and strength
Whittemore, L.-A., Song, K., Li, X., Aghajanian, J. D., Davies, M. V., Girgenrath, S., Hill, J. J., Jalenak, M., Kelley, P. E., Knight, A., et al. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02953-4 · Cited by 512
Flagged first, then by citations
2 of the 51 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 201–300 of 400
Jaworska, J., Rodziewicz-Flis, E. A., Kortas, J. A., Flis, M., Micielska, K., Babińska, A., Laskowski, R., Lombardi, G., & Ziemann, E. (2020) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph17155496 · Cited by 19
Omosule, C. L., Gremminger, V. L., AGUILLARD, A., Jeong, Y., Harrelson, E. N., Miloscio, L., Mastaitis, J. W., Rafique, A., Kleiner, S., Pfeiffer, F. M., et al. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.4223 · Cited by 21
Ozawa, T., Morikawa, M., Morishita, Y., Ogikubo, K., Itoh, F., Koinuma, D., Nygren, P., & Miyazono, K. (2021) · iScience · doi:10.1016/j.isci.2021.102488 · Cited by 20
Myostatin Knockout Regulates Bile Acid Metabolism by Promoting Bile Acid Synthesis in Cattle
Wu, D., Gu, M., Wei, Z., Bai, C., Su, G., Liu, X., Zhao, Y., Yang, L., & Li, G. (2022) · Animals · doi:10.3390/ani12020205 · Cited by 19
Key factors involved in obesity development
Wang, Z., Yuan, D., Duan, Y., Li, S., & Hou, S. (2017) · Eating and Weight Disorders - Studies on Anorexia Bulimia and Obesity · doi:10.1007/s40519-017-0428-3 · Cited by 19
Peiris, H. N., Ponnampalam, A. P., Osepchook, C. C., Mitchell, M. D., & Green, M. P. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00673.2009 · Cited by 19
Omosule, C. L., Joseph, D., Weiler, B., Gremminger, V. L., Silvey, S., Jeong, Y., Rafique, A., Krueger, P., Kleiner, S., & Phillips, C. L. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.4529 · Cited by 18
Zhang, F., Deng, B., Wen, J., Chen, K., Liu, W., Ye, S., Huang, H., Jiang, S., & Xiong, Y. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.01.120 · Cited by 18
Dias, A., de Nonohay, U., & Blessmann, G. (2012) · Arquivos rio-grandenses de medicina · Cited by 18
Havers, T., Held, S., Schönfelder, M., Geisler, S., & Wackerhage, H. (2025) · Sports Medicine · doi:10.1007/s40279-025-02263-w · Cited by 19
“This idea was formulated by the group of Alexandra McPherron, who found that myostatin knock out-induced muscle hypertrophy results in fat loss and improved glucose homeostasis in mice [181].”
InfluentialLeardini-Tristao, M., Charles, A.-L., Lejay, A., Pizzimenti, M., Meyer, A., Estato, V., Tibiriçá, E., Andres, E., & Geny, B. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8050653 · Cited by 17
del Pino, L. M., Urrutia, O., Arana, A., Alfonso, L., Mendizabal, J. A., & Soret, B. (2020) · animal · doi:10.1017/s1751731120000051 · Cited by 17
Variants in the Myostatin Gene and Physical Performance Phenotype of Elite Athletes
Ginevičienė, V., Jakaitienė, A., Pranckevičienė, E., Milašius, K., & Utkus, A. (2021) · Genes · doi:10.3390/genes12050757 · Cited by 18
Rodríguez‐Fdez, S., Lorenzo‐Martín, L. F., Fabbiano, S., Menacho-Márquez, M., Sauzeau, V., Dosil, M., & Bustelo, X. R. (2021) · Biology · doi:10.3390/biology10090857 · Cited by 17
Vasyukova, O. V., Kasyanova, Y. V., Okorokov, P. L., & Bezlepkina, O. B. (2021) · Problems of Endocrinology · doi:10.14341/probl12779 · Cited by 18
Wilhelmsen, A., Stephens, F. B., Bennett, A. J., Karagounis, L. G., Jones, S. W., & Tsintzas, K. (2023) · GeroScience · doi:10.1007/s11357-023-00956-6 · Cited by 17
Brown, M., Ungerleider, N., Bonomi, L. M., Andrzejewski, D., Burnside, A., & Schneyer, A. L. (2014) · Islets · doi:10.1080/19382014.2015.1017226 · Cited by 17
Collins‐Hooper, H., Sartori, R., Giallourou, N., Matsakas, A., Mitchell, R., Makarenkova, H. P., Flasskamp, H., Macharia, R., Ray, S., Swann, J. R., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0120524 · Cited by 17
Perry, C. A., Van Guilder, G. P., & Butterick, T. A. (2022) · BMC Nutrition · doi:10.1186/s40795-022-00516-9 · Cited by 16
Price, S. R., & Wang, X. H. (2025) · Kidney Research and Clinical Practice · doi:10.23876/j.krcp.24.214 · Cited by 18
Functional genomics applications and therapeutic implications in sarcopenia
Melouane, A., Ghanemi, A., Yoshioka, M., & St‐Amand, J. (2019) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2019.04.003 · Cited by 16
Gu, M., Zhou, X., Zhu, L., Gao, Y., Gao, L., Bai, C., Yang, L., & Li, G. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.774185 · Cited by 16
Kärst, S., Strucken, E. M., Schmitt, A. O., Weyrich, A., de Villena, F. P., Yang, H., & Brockmann, G. A. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-16 · Cited by 16
Ma, Y., Li, X., Zhang, H., Ou, Y., Zhang, Z., Li, S., Wu, F., Sheng, Z., & Liao, E. (2016) · Endocrine Research · doi:10.3109/07435800.2015.1044609 · Cited by 16
Pei, Y., Song, Y., Zheng, F., Li, H., Mu, Y., Rehman, S. U., Liu, Q., & Li, K. (2022) · Foods · doi:10.3390/foods11091286 · Cited by 15
Davey, J. R., Estévez, E., Thomson, R. E., Whitham, M., Watt, K. I., Hagg, A., Qian, H., Henstridge, D. C., Ludlow, H., Hedger, M. P., et al. (2020) · The FASEB Journal · doi:10.1096/fj.201802059rrr · Cited by 16
Myostatin serum levels in children with type 1 diabetes mellitus
Efthymiadou, A., Vasilakis, I.-A., Giannakopoulos, A., & Chrysis, D. (2021) · HORMONES · doi:10.1007/s42000-021-00317-y · Cited by 16
Tang, L. V., Liu, C., Wang, X.-D., Luo, K., Zhang, D., Chi, A., Zhang, J., & Sun, L. (2014) · Biotechnology Letters · doi:10.1007/s10529-014-1617-z · Cited by 15
Kocsis, T., Trencsényi, G., Szabó, K., Baán, J. A., Müller, G., Mendler, L., Garai, I., Reinauer, H., Deak, F., László, A., et al. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00216.2016 · Cited by 16
The effect of myostatin silencing by lentiviral-mediated RNA interference on goat fetal fibroblasts
Lü, J., Wei, C., Zhang, X., Xu, L., Zhang, S., Liu, J., Cao, J., Zhao, F., Zhang, L., Li, B., et al. (2013) · Molecular Biology Reports · doi:10.1007/s11033-013-2494-6 · Cited by 14
Different regulation role of myostatin in differentiating pig ADSCs and MSCs into adipocytes
Deng, B., Wen, J., Ding, Y., Peng, J., & Jiang, S. (2011) · Cell Biochemistry and Function · doi:10.1002/cbf.1828 · Cited by 14
Kramerova, I. A., Marinov, M., Owens, J. M., Lee, S., Becerra, D., & Spencer, M. J. (2020) · The Journal of Physiology · doi:10.1113/jp279943 · Cited by 14
Exercise alters myostatin protein expression in sedentary and exercised streptozotocin-diabetic rats
Dibai, D. B., Bueno, P., Nonaka, K. O., Selistre-de-Araújo, H. S., & Leal, A. M. O. (2015) · Archives of Endocrinology and Metabolism · doi:10.1590/2359-3997000000028 · Cited by 16
Post-exercise changes in myostatin and actRIIB expression in obese insulin-resistant rats
Bueno, P. G., Bassi, D., Contrera, D. G., Carnielli, H. M., Silva, R. N., Nonaka, K. O., Selistre-de-Araújo, H. S., & Leal, A. M. O. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.04.006 · Cited by 13
Follistatin and follistatin-like 3 in metabolic disorders
Bielka, W., Przezak, A., & Pawlik, A. (2023) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2023.106785 · Cited by 15
Zhao, L., Xu, L., Yang, Y., He, Q., Liu, Q., Luo, J., Luo, W., Zhang, X., Yan, T., & Yang, S. Y. (2022) · Aquaculture · doi:10.1016/j.aquaculture.2022.738850 · Cited by 13
Myostatin as a plausible biomarker for early stage of sarcopenic obesity
Ishibashi, C., Nakanishi, K., Nishida, M., Shinomiya, H., Shinzawa, M., Kanayama, D., Yamamoto, R., Kudo, T., Nagatomo, I., & Yamauchi‐Takihara, K. (2024) · Scientific Reports · doi:10.1038/s41598-024-79534-5 · Cited by 14
Effects triggered in the periphery by acupuncture
Lund, I., & Lundeberg, T. (2015) · Acupuncture and Related Therapies · doi:10.1016/j.arthe.2015.08.002 · Cited by 13
Hao, R.-H., Yang, T.-L., Rong, Y., Yao, S., Dong, S.-S., Chen, H., & Guo, Y. (2017) · International Journal of Obesity · doi:10.1038/ijo.2017.283 · Cited by 13
Pan, S., Zhang, L., Liu, Z., & Hua, X. (2021) · Journal of Animal Science · doi:10.1093/jas/skab287 · Cited by 13
Takahashi, H., Sato, K., Yamaguchi, T., Miyake, M., Watanabe, H., Nagasawa, Y., Kitagawa, E., Terada, S., Urakawa, M., Rose, M. T., et al. (2014) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2014.01.007 · Cited by 14
Kuang, L., Xie, X., Zhang, X., Lei, M., Li, C., Ren, Y., Zheng, J., Guo, Z., Zhang, C., Yang, C., et al. (2014) · Animal Biotechnology · doi:10.1080/10495398.2013.865639 · Cited by 13
Li, Y., Fan, G., Liu, Y., Yao, W., Albrecht, E., Zhao, R., & Yang, X. (2021) · Research in Veterinary Science · doi:10.1016/j.rvsc.2021.03.017 · Cited by 13
Dybus, A., Proskura, W. S., Sadkowski, S., & Pawlina, E. (2013) · Veterinární Medicína · doi:10.17221/6654-vetmed · Cited by 13
Impact of muscle mass on blood glucose level
Taha, M., Alnaam, Y., Al-Maqati, T. N., Musallam, L. A., Altalib, G., Alowfi, D., & Haider, N. (2021) · Journal of Basic and Clinical Physiology and Pharmacology · doi:10.1515/jbcpp-2021-0316 · Cited by 14
Tankó, L. B., Goldhahn, J., Varela, A., Lesage, E., Smith, S. Y., Pilling, A. M., & Chivers, S. (2016) · Calcified Tissue International · doi:10.1007/s00223-016-0148-0 · Cited by 12
Alterations in Adiposity and Glucose Homeostasis in Adult Gasp-1 Overexpressing Mice
Pèrié, L., Parenté, A., Baraige, F., Magnol, L., & Blanquet, V. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000485878 · Cited by 13
Takao, N., Kurose, S., Miyauchi, T., Onishi, K., Tamanoi, A., Tsuyuguchi, R., Fujii, A., Yoshiuchi, S., Takahashi, K., Tsutsumi, H., et al. (2021) · BMC Endocrine Disorders · doi:10.1186/s12902-021-00808-4 · Cited by 13
Kovanecz, I., Masouminia, M., Gelfand, R., Vernet, D. A., Rajfer, J., & González-Cadavid, N. F. (2017) · International Journal of Impotence Research · doi:10.1038/ijir.2017.22 · Cited by 12
Myostatin in the placentae of pregnancies complicated with gestational diabetes mellitus
Peiris, H. N., Lappas, M., Georgiou, H. M., Vaswani, K., Salomón, C., Rice, G. E., & Mitchell, M. D. (2014) · Placenta · doi:10.1016/j.placenta.2014.11.006 · Cited by 12
Gelatinases impart susceptibility to high-fat diet-induced obesity in mice
Biga, P. R., Froehlich, J. M., Greenlee, K. J., Galt, N. J., Meyer, B. M., & Christensen, D. J. (2013) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2012.12.005 · Cited by 12
Murakami, Y., Andô, M., Kishimoto, K., Ohama, M., Uemura, Y., Tani, R., Akazawa, A., Matsumiya, K., Sato, K., & Kinoshita, M. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e32242 · Cited by 11
Ontogenetic and in silico models of spatial‐packing in the hypermuscular mouse skull
Jeffery, N. S., Sarver, D. C., & Mendias, C. L. (2021) · Journal of Anatomy · doi:10.1111/joa.13393 · Cited by 11
Possible Mechanisms Linking Obesity, Steroidogenesis, and Skeletal Muscle Dysfunction
Sheptulina, A. F., Antyukh, K. Y., Kiselev, A. R., Mitkovskaya, N. P., & Drapkina, O. M. (2023) · Life · doi:10.3390/life13061415 · Cited by 11
Peiris, H. N., Ashman, K., Vaswani, K., Kvaskoff, D., Rice, G. E., & Mitchell, M. D. (2014) · Journal of Proteome Research · doi:10.1021/pr5004642 · Cited by 10
Myostatin dysfunction does not protect from fasting-induced loss of muscle mass in mice.
Fokin, A., Minderis, P., Venckūnas, T., Lionikas, A., Kvedaras, M., & Ratkevičius, A. (2019) · PubMed Central · Cited by 11
Kvedaras, M., Minderis, P., Krusnauskas, R., Lionikas, A., & Ratkevičius, A. (2019) · Experimental Gerontology · doi:10.1016/j.exger.2019.110751 · Cited by 12
Endocranial and masticatory muscle volumes in myostatin-deficient mice
Jeffery, N. S., & Mendias, C. L. (2014) · Royal Society Open Science · doi:10.1098/rsos.140187 · Cited by 11
Modeling Energy Dynamics in Mice with Skeletal Muscle Hypertrophy Fed High Calorie Diets
Bond, N. D., Guo, J., Hall, K. D., & McPherron, A. C. (2016) · International Journal of Biological Sciences · doi:10.7150/ijbs.13525 · Cited by 10
Self-citationSun, T., Meng, X.-Z., Li, Y., Zhang, H., He, R., He, R., Liu, T., Lv, W., Xu, X., Shen, Y., et al. (2025) · Aquaculture · doi:10.1016/j.aquaculture.2025.743355 · Cited by 10
Gaweł, E., Hall, B., Siatkowski, S., Grabowska, A., & Zwierzchowska, A. (2024) · Nutrients · doi:10.3390/nu16030355 · Cited by 14
Zheng, Y., Lin, Y. Q., Yu, Y., Xu, Y., & Jin, S. (2011) · Czech Journal of Animal Science · doi:10.17221/4417-cjas · Cited by 10
Sarcopenia in the setting of nonalcoholic fatty liver
Arrese, M. A., Cabello‐Verrugio, C., Arab, J. P., Francisco Barrera, M., Baudrand, R. F., Guarda, F. J., Gul, I., & Cabrera, D. (2022) · Metabolism and Target Organ Damage · doi:10.20517/mtod.2021.16 · Cited by 10
Lian, J., Walker, R. G., D’Amico, A., Vujić, A., Mills, M. J., Messemer, K. A., Mendello, K. R., Goldstein, J. M., Leacock, K. A., Epp, S., et al. (2023) · Life Science Alliance · doi:10.26508/lsa.202201662 · Cited by 12
Bauman, W. A., & Cardozo, C. P. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-415853-5.00047-9 · Cited by 11
Xing, H. J., Wang, Z. Y., Zhong, B., Ying, S. J., Nie, H., Zhou, Z. R., Fan, Y. X., & Wang, F. (2014) · Genetics and Molecular Research · doi:10.4238/2014.july.24.4 · Cited by 11
Baumgartner, M., Lischka, J., Schanzer, A., de Gier, C., Walleczek, N.-K., Greber-Platzer, S., & Zeyda, M. (2022) · Nutrients · doi:10.3390/nu14102133 · Cited by 9
Lin, X., Yan, M., Yu, W., Ma, Y., Zhang, L., Wei, W., & Chen, J. (2021) · Animal Science Journal · doi:10.1111/asj.13544 · Cited by 9
Dichtel, L. E., Kimball, A., Bollinger, B., Scarff, G., Gerweck, A. V., Bredella, M. A., & Haines, M. S. (2024) · Physiological Reports · doi:10.14814/phy2.16169 · Cited by 9
The Dual Role of Myokines in Fatigue Associated with Inflammatory Joint Diseases
Chmielewski, G., Kuna, J., Jaśkiewicz, Ł., Knapik, M., Mikiewicz, M., Majewski, M. S., & Krajewska–Włodarczyk, M. (2025) · Journal of Inflammation Research · doi:10.2147/jir.s545914 · Cited by 9
Li, A., Zhou, Z., Li, D., Sha, P.-R., Hu, H., Lin, Y.-Q., Yue, B.-L., Li, J., & Xiong, Y. (2025) · Cells · doi:10.3390/cells14241954 · Cited by 10
Li, F., Shan, A. S., Hu, J., Zheng, Y.-L., Xu, L., & Chen, Z. H. (2013) · British Poultry Science · doi:10.1080/00071668.2013.853868 · Cited by 9
Tavoian, D., Arnold, W. D., Mort, S. C., & Lacalle, S. D. (2019) · PLoS ONE · doi:10.1371/journal.pone.0225283 · Cited by 11
Halmos, T., & Suba, I. (2014) · Orvosi Hetilap · doi:10.1556/oh.2014.29959 · Cited by 9
Li, M., Tang, X., You, W., Wang, Y., Chen, Y., Liu, Y., Yuan, H., Gao, C., Chen, X., Xiao, Z., et al. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.06.011 · Cited by 9
Myokines in Acromegaly: An Altered Irisin Profile
Mizera, Ł., Halupczok-Żyła, J., Kolačkov, K., Zembska, A., Grzegrzółka, J., Jędrzejuk, D., Bolanowski, M., & Daroszewski, J. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.728734 · Cited by 9
Chen, T., Li, Z., Zhang, Y., Feng, F., Wang, X., Wang, X., & Shen, Q. W. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.01.075 · Cited by 9
Physical activity, exercise and non-communicable diseases
Archer, E., & Blair, S. N. (2012) · doi:10.24804/ree.14.1 · Cited by 10
Concordant and divergent strategies to improve postprandial glucose and lipid metabolism
Edinburgh, R. M., Betts, J. A., Burns, S. F., & Gonzalez, J. T. (2017) · Nutrition Bulletin · doi:10.1111/nbu.12259 · Cited by 10
Turning fat into muscle: can this be an alternative to anti‐obesity drugs such as semaglutide?
Wackerhage, H., Hinrichs, A., Wolf, E., & Hrabě de Angelis, M. (2024) · The Journal of Physiology · doi:10.1113/jp286430 · Cited by 8
Myokines and interorgan crosstalk: bridging exercise to health promotion and disease prevention
Ha, J., Sung, S., & Kim, H. (2025) · Annals of Pediatric Endocrinology & Metabolism · doi:10.6065/apem.2448218.109 · Cited by 10
Saremi, A., & Parastesh, M. (2019) · International Journal of Diabetes and Metabolism · doi:10.1159/000497712 · Cited by 8
Skeletal muscle growth to combat diabetes and obesity: the potential role of muscle‐secreted factors
Sammut, M. J., Thorne, B. R., & Melling, C. W. J. (2025) · Obesity · doi:10.1002/oby.24223 · Cited by 8
Myostatin in Obesity: A Molecular Link Between Metabolic Dysfunction and Musculotendinous Remodeling
Cesanelli, L., Minderis, P., Fokin, A., Ratkevičius, A., Satkunskienė, D., & Degens, H. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27020967 · Cited by 7
Fat, muscle, and anti-obesity medications in cardiovascular disease prevention
Khan, M. S., Dawood, M. H., Handelsman, Y., Anker, S. D., Coats, A. J. S., Green, J. B., & Butler, J. (2026) · European Heart Journal · doi:10.1093/eurheartj/ehag201 · Cited by 9
Myostatin (GDF-8) as a therapeutic target for the prevention of osteoporotic fractures
Hamrick, M. W. (2010) · IBMS BoneKEy · doi:10.1138/20100423 · Cited by 7
Elashry, M. I., Eldaey, A., Glenske, K., Matsakas, A., Wenisch, S., Arnhold, S., & Patel, K. (2019) · Journal of Anatomy · doi:10.1111/joa.13025 · Cited by 7
Omosule, C. L., Joseph, D., Weiler, B., Gremminger, V. L., Silvey, S., Lafaver, B. N., Jeong, Y., Kleiner, S., & Phillips, C. L. (2023) · JBMR Plus · doi:10.1002/jbm4.10753 · Cited by 7
Pedro, A. E., Torrecilhas, J. A., Torres, R. D. N. S., Ramírez-Zamudio, G. D., Baldassini, W. A., Chardulo, L. A. L., Curi, R. A., Russo, G. H., Napolitano, J. A., Tinoco, G. L. B., et al. (2023) · Metabolites · doi:10.3390/metabo13091028 · Cited by 7
Kim, J. H., Kim, J. H., Sutikno, L. A., Lee, S. B., Jin, D., Hong, Y., Kim, Y. S., & Jin, H. (2019) · PLoS ONE · doi:10.1371/journal.pone.0215298 · Cited by 7
Kim, J. H., Kim, J., Jang, J., Jang, J., Jin, D., Kim, Y., & Jin, H. (2021) · Molecules · doi:10.3390/molecules26092676 · Cited by 7
Jang, J., Kim, Y., Song, T., Park, S., Kim, H., Koh, J., Cho, Y., Park, S., Sadayappan, S., Kwak, H., et al. (2024) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13519 · Cited by 8
Exploring myostatin’s role and potential applications in fisheries and aquaculture: a review
Priyanka, P., Kashyap, S., Umesh, Verma, K., Singh, M., & Yadav, N. (2024) · Aquaculture International · doi:10.1007/s10499-024-01700-3 · Cited by 6
Samali, S. A., Hosseini, S. F., Mohammadi, Y., Sadri, F., & Rezaei, Z. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-11390-6 · Cited by 9
Kowalik, S., Wiśniewska, A., Kędzierski, W., & Janczarek, I. (2020) · Animals · doi:10.3390/ani10122268 · Cited by 7
Zhang, Y., Tang, Z.-Y., Liu, Z., Shen, J., Feng, H., & Xue, L. (2021) · Aquaculture · doi:10.1016/j.aquaculture.2021.736795 · Cited by 6
Zhu, Z., Ali, A., Wang, J., Qi, S., Hua, Z., Ren, H., Zhang, L., Gu, H., Molenaar, A. J., Babar, M. E., et al. (2022) · Adipocyte · doi:10.1080/21623945.2022.2065715 · Cited by 6
Kits for RNA Extraction, Isolation, and Purification
Johnson, M. (2012) · Materials and Methods · doi:10.13070/mm.en.2.201 · Cited by 6
Viscera Characteristics of MSTN-Edited Heterozygous Pigs
Pei, Y., Fan, Z., Song, Y., Chen, C., Mu, Y., Li, B., Zheng, F., Li, H., & Li, K. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.764965 · Cited by 6
Senescent adipocytes as potential effectors of muscle cells dysfunction: An in vitro model
Zoico, E., Saatchi, T., Nori, N., Mazzali, G., Rizzatti, V., Pizzi, E., Fantin, F., Giani, A., Urbani, S., & Zamboni, M. M. (2023) · Experimental Gerontology · doi:10.1016/j.exger.2023.112233 · Cited by 5
Metadata
- Authors
- Guo, T., Jou, W., Chanturiya, T., Portas, J., Gavrilova, O., & McPherron, A. C.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- McPherron, Alexandra C.
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2009-03-19
- Volume
- 4
- Issue
- 3
- Pages
- e4937
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC2654157
- OpenAlex
- W2028966038
- Cited by
- 402
- References
- 51
- Citations by year
- 2026: 17 · 2025: 18 · 2024: 20 · 2023: 17 · 2022: 27 · 2021: 31 · 2020: 23 · 2019: 25 · 2018: 15 · 2017: 23 · 2016: 17 · 2015: 28 · 2014: 27 · 2013: 29 · 2012: 27
- FWCI
- 11.40
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, public-domain)
- PubMed Central (publishedVersion, public-domain)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Funders
- Johns Hopkins University
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases
- Topics
- 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
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- myostatin, Mstn knockout mice, skeletal muscle, adipose tissue, fat mass, insulin sensitivity, glucose metabolism, lipid oxidation, diet-induced obesity, obesity resistance, muscle mass, high-fat diet, diabetes treatment
- MeSH terms
- Adipose Tissue, Animals, Diet, Dietary Fats, Glucose, Humans, Insulin, Insulin Resistance, Male, Mice, Inbred C57BL, Oxidation-Reduction, Glucose Clamp Technique, Signal Transduction, Mice, Knockout, Muscle, Skeletal, Lipid Metabolism, Proto-Oncogene Proteins c-akt, Mice, 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
