Myostatin: more than just a regulator of muscle mass

Definition and classification of cancer cachexia: an international consensus

Fearon, K., Strasser, F., Anker, S. D., Bosaeus, I. G., Bruera, E. D., Fainsinger, R. L., Jatoi, A., Loprinzi, C. L., Macdonald, N., Mantovani, G., et al. (2011) · The Lancet Oncology · doi:10.1016/s1470-2045(10)70218-7 · Cited by 6,020

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

Cachexia: a new definition.

Evans, W., Morley, J., Argilés, J., Bales, C., Baracos, V., Guttridge, D., Jatoi, A., Kalantar-zadeh, K., Lochs, H., Mantovani, G., et al. (2008) · Clinical Nutrition · doi:10.1016/j.clnu.2008.06.013 · Cited by 2,341

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

Reversal of Cancer Cachexia and Muscle Wasting by ActRIIB Antagonism Leads to Prolonged Survival

Zhou, X., Wang, J. L., Lu, J., Song, Y., Kwak, K. S., Jiao, Q., Rosenfeld, R., Chen, Q., Boone, T. C., Simonet, W. S., et al. (2010) · Cell · doi:10.1016/j.cell.2010.07.011 · Cited by 960

Myostatin Inhibits Myoblast Differentiation by Down-regulating MyoD Expression

Langley, B. C., Thomas, M., Bishop, A., Sharma, M., Gilmour, S., & Kambadur, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204291200 · Cited by 910

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

Functional 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

Adipose Triglyceride Lipase Contributes to Cancer-Associated Cachexia

Das, S. K., Eder, S., Schauer, S., Diwoky, C., Temmel, H., Guertl, B., Gorkiewicz, G., Tamilarasan, K. P., Kumari, P., Trauner, M., et al. (2011) · Science · doi:10.1126/science.1198973 · Cited by 594

Cancer cachexia: understanding the molecular basis

Argilés, J. M. A., Busquets, S., Stemmler, B., & López-Soriano, F. J. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3829 · Cited by 1,567

Physical Exercise-Induced Myokines and Muscle-Adipose Tissue Crosstalk: A Review of Current Knowledge and the Implications for Health and Metabolic Diseases

Leal, L. G., Lopes, M. A., & Batista, M. L. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01307 · Cited by 382

Cancer cachexia and its pathophysiology: links with sarcopenia, anorexia and asthenia

da Silva, S. P., Santos, J., Silva, M. P. C. E., da Costa, R. M. G., & Medeiros, R. (2020) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12528 · Cited by 392

Inter-tissue communication in cancer cachexia

Argilés, J. M. A., Stemmler, B., López-Soriano, F. J., & Busquets, S. (2018) · Nature Reviews Endocrinology · doi:10.1038/s41574-018-0123-0 · Cited by 317

Myostatin Knockout Drives Browning of White Adipose Tissue through Activating the AMPK-PGC1α-Fndc5 Pathway in Muscle

Shan, T., Liang, X., Bi, P., & Kuang, S. (2013) · The FASEB Journal · doi:10.1096/fj.12-225755 · Cited by 301

Molecular Mechanisms of Inflammation in Sarcopenia: Diagnosis and Therapeutic Update

Jiménez-Gutiérrez, G. E., Martínez-Gómez, L. E., Martínez-Armenta, C., Pineda, C., Martínez‐Nava, G. A., & López-Reyes, A. G. (2022) · Cells · doi:10.3390/cells11152359 · Cited by 245

Inter‐organ communication: a gatekeeper for metabolic health

Castillo‐Armengol, J., Fajas, L., & Lopez‐Mejia, I. C. (2019) · The EMBO Reports · doi:10.15252/embr.201947903 · Cited by 178

Sarcopenic obesity: molecular clues to a better understanding of its pathogenesis?

Kob, R., Bollheimer, L. C., Bertsch, T., Fellner, C., Djukic, M., Sieber, C. C., & Fischer, B. E. (2015) · Biogerontology · doi:10.1007/s10522-014-9539-7 · Cited by 151

Myostatin inhibitors as therapies for muscle wasting associated with cancer and other disorders

Smith, R. C., & Lin, B. K. (2013) · Current Opinion in Supportive and Palliative Care · doi:10.1097/spc.0000000000000013 · Cited by 161

Sarcopenic obesity: how do we treat it?

Bouchonville, M. F., & Villareal, D. T. (2013) · Current Opinion in Endocrinology, Diabetes & Obesity · doi:10.1097/01.med.0000433071.11466.7f · Cited by 141

Myokines and Resistance Training: A Narrative Review

Zunner, B. E. M., Wachsmuth, N. B., Eckstein, M. L., Scherl, L., Schierbauer, J., Haupt, S., Stumpf, C., Reusch, L., & Moser, O. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073501 · Cited by 146

Cachexia-associated adipose tissue morphological rearrangement in gastrointestinal cancer patients

Júnior, M. L. B., Henriques, F. D. S., das Neves, R. X., Oliván, M., de Matos‐Neto, E. M., de Alcântara, P. S. M., Maximiano, L. F., Otoch, J. P., Alves, M. J., & Seelaender, M. C. L. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12037 · Cited by 116

Molecular pathways leading to loss of skeletal muscle mass in cancer cachexia – can findings from animal models be translated to humans?

Mueller, T. C., Bachmann, J., Prokopchuk, O., Friess, H., & Martignoni, M. E. (2016) · BMC Cancer · doi:10.1186/s12885-016-2121-8 · Cited by 95

Effect of bimagrumab on thigh muscle volume and composition in men with casting‐induced atrophy

Rooks, D. S., Laurent, D., Praestgaard, J., Rasmussen, S., Bartlett, M., & Tankó, L. B. (2017) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12205 · Cited by 90

Management of Cancer Cachexia: Attempting to Develop New Pharmacological Agents for New Effective Therapeutic Options

Marceca, G. P., Londhe, P., & Calore, F. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00298 · Cited by 92

The Role of Systemic Inflammation in Cancer‐Associated Muscle Wasting and Rationale for Exercise as a Therapeutic Intervention

Cole, C. L., Kleckner, I. R., Jatoi, A., Schwarz, E. M., & Dunne, R. F. (2018) · JCSM Clinical Reports · doi:10.17987/jcsm-cr.v3i2.65 · Cited by 84

Myostatin – The Holy Grail for Muscle, Bone, and Fat?

Buehring, B., & Binkley, N. (2013) · Current Osteoporosis Reports · doi:10.1007/s11914-013-0160-5 · Cited by 79

Untitled work

Harper (2016) · doi:10.1161/circresaha.116.307962 · Cited by 74

Mediators of cachexia in cancer patients

Argilés, J. M. A., López-Soriano, F. J., & Busquets, S. (2019) · Nutrition · doi:10.1016/j.nut.2019.03.012 · Cited by 75

Hormones and Muscle Atrophy

Martı́n, A. I., Priego, T., & López‐Calderón, A. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-1435-3_9 · Cited by 84

The Use of Platelet-Rich and Platelet-Poor Plasma to Enhance Differentiation of Skeletal Myoblasts: Implications for the Use of Autologous Blood Products for Muscle Regeneration

Miroshnychenko, O., Chang, W., & Dragoo, J. L. (2016) · The American Journal of Sports Medicine · doi:10.1177/0363546516677547 · Cited by 70

Cancer-Mediated Muscle Cachexia: Etiology and Clinical Management

Siff, T. E., Parajuli, P., Razzaque, M. S., & Atfi, A. (2021) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2021.03.007 · Cited by 73

Advances in research on pharmacotherapy of sarcopenia

Feike, Y., Liu, Z., & Chen, W. (2021) · Aging Medicine · doi:10.1002/agm2.12168 · Cited by 67

Irisin mRNA and circulating levels in relation to other myokines in healthy and morbidly obese humans

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

First-in-Human Phase I Study of the Activin A Inhibitor, STM 434, in Patients with Granulosa Cell Ovarian Cancer and Other Advanced Solid Tumors

Tao, J. J., Cangemi, N. A., Makker, V., Cadoo, K. A., Liu, J. F., Rasco, D. W., Navarro, W. H., Haqq, C. M., & Hyman, D. M. (2019) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-19-1065 · Cited by 60

Myostatin inhibitors as pharmacological treatment for muscle wasting and muscular dystrophy

Saitoh, M., Ishida, J., Ebner, N., Anker, S. D., Springer, J., & von Haehling, S. (2017) · JCSM Clinical Reports · doi:10.17987/jcsm-cr.v2i1.37 · Cited by 60

Pharmacological prospects in the treatment of Duchenne muscular dystrophy

Rüegg, U. T. (2013) · Current Opinion in Neurology · doi:10.1097/wco.0b013e328364fbaf · Cited by 56

Duchenne muscular dystrophy: an updated review of common available therapies

Salmaninejad, A., Valilou, S. F., Bayat, H., Ebadi, N., Daraei, A., Yousefi, M., Nesaei, A., & Mojarrad, M. (2018) · International Journal of Neuroscience · doi:10.1080/00207454.2018.1430694 · Cited by 59

Myostatin — From the Mighty Mouse to cardiovascular disease and cachexia

Dschietzig, T. B. (2014) · Clinica Chimica Acta · doi:10.1016/j.cca.2014.03.021 · Cited by 55

MSTN Attenuates Cardiac Hypertrophy through Inhibition of Excessive Cardiac Autophagy by Blocking AMPK /mTOR and miR-128/PPARγ/NF-κB

Qi, H., Ren, J., Ba, L., Song, C., Zhang, Q., Cao, Y., Shi, P., Fu, B., Liu, Y., & Sun, H. (2019) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2019.12.003 · Cited by 54

Low-intensity pulsed ultrasound prevents muscle atrophy induced by type 1 diabetes in rats

Tang, L., Li, N., Jian, W., Kang, Y., Yin, B., Sun, S., Guo, J., Sun, L., & Ta, D. (2017) · Skeletal Muscle · doi:10.1186/s13395-017-0145-7 · Cited by 50

The Pathway to Cancer Cachexia: MicroRNA-Regulated Networks in Muscle Wasting Based on Integrative Meta-Analysis

Freire, P. P., Fernández, G. J., Cury, S. S., de Moraes, D., Oliveira, J. S., de Oliveira, G., Dal‐Pai‐Silva, M., Reis, P. P., & Carvalho, R. F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081962 · Cited by 45

Growth differentiation factor 8 down-regulates pentraxin 3 in human granulosa cells

Chang, H., Fang, L., Cheng, J., Klausen, C., Sun, Y., & Leung, P. C. K. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.01.036 · Cited by 45

Muscle wasting in osteoarthritis model induced by anterior cruciate ligament transection

Silva, J. M. D. S., Alabarse, P. V. G., Teixeira, V. D. O. N., Freitas, E. C., de Oliveira, F. H., Chakr, R. M. D. S., & Xavier, R. M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0196682 · Cited by 45

Compensatory anabolic signaling in the sarcopenia of experimental chronic arthritis

Little, R. D., Prieto‐Potín, I., Pérez-Baos, S., Villalvilla, A., Gratal, P., Cicuttini, F., Largo, R., & Herrero‐Beaumont, G. (2017) · Scientific Reports · doi:10.1038/s41598-017-06581-6 · Cited by 44

Interaction of Fibromodulin and Myostatin to Regulate Skeletal Muscle Aging: An Opposite Regulation in Muscle Aging, Diabetes, and Intracellular Lipid Accumulation

Lee, E. J., Ahmad, S. S., Lim, J. H., Ahmad, K., Shaikh, S., Lee, Y., Park, S. J., Jin, J., Lee, Y., & Choi, I. (2021) · Cells · doi:10.3390/cells10082083 · Cited by 46

Endurance training prevents TWEAK but not myostatin-mediated cardiac remodelling in cancer cachexia

Padrão, A. I., Moreira‐Gonçalves, D., Oliveira, P. A., Teixeira, C., Faustino‐Rocha, A. I., Helguero, L. A., Vitorino, R. M. P., Santos, L. L., Amado, F. M. L., Duarte, J. A., et al. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.12.026 · Cited by 43

The myokine Fibcd1 is an endogenous determinant of myofiber size and mitigates cancer-induced myofiber atrophy

Graça, F. A., Rai, M., Hunt, L. C., Stephan, A., Wang, Y., Gordon, B., Wang, R., Quarato, G., Xu, B., Fan, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30120-1 · Cited by 41

Establishment and phenotypic analysis of an Mstn knockout rat

Gu, H., Cao, Y., Qiu, B., Zhou, Z., Deng, R., Chen, Z., Li, R., Li, X., Wei, Q., Xia, X., et al. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.06.030 · Cited by 40

Parallel comparative proteomics and phosphoproteomics reveal that cattle myostatin regulates phosphorylation of key enzymes in glycogen metabolism and glycolysis pathway

Yang, S., Li, X., Liu, X., Ding, X., Xin, X., Jin, C., Zhang, S., Li, G., & Guo, H. (2018) · Oncotarget · doi:10.18632/oncotarget.24250 · Cited by 39

Effects of dapagliflozin on the serum levels of fibroblast growth factor 21 and myokines and muscle mass in Japanese patients with type 2 diabetes: A randomized, controlled trial

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

Proteomics insights into the effects of MSTN on muscle glucose and lipid metabolism in genetically edited cattle

Xin, X., Yang, S., Li, X., Liu, X., Zhang, L.-L., Ding, X., Zhang, S., Li, G., & Guo, H. (2019) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2019.113237 · Cited by 37

Pyrrolidine Dithiocarbamate (PDTC) Attenuates Cancer Cachexia by Affecting Muscle Atrophy and Fat Lipolysis

Miao, C., Lv, Y., Zhang, W., Chai, X., Feng, L., Fang, Y., Liu, X., & Zhang, X. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00915 · Cited by 37

New insight of obesity-associated NAFLD: Dysregulated “crosstalk” between multi-organ and the liver?

Wang, Y., Wu, L.-L., Qi, X.-Y., Wang, Y.-Y., Liao, Z., Liu, J., & Xiao, X. (2022) · Genes & Diseases · doi:10.1016/j.gendis.2021.12.013 · Cited by 36

Implication of diet and exercise on the management of age‐related sarcopenic obesity in Asians

Kim, Y. J., Moon, S., Yu, J. M., & Chung, H. S. (2022) · Geriatrics and gerontology international/Geriatrics & gerontology international · doi:10.1111/ggi.14442 · Cited by 36

The Use of Platelet-Rich and Platelet-Poor Plasma to Enhance Differentiation of Skeletal Myoblasts

Dragoo, J. L. (2016) · Orthopaedic Journal of Sports Medicine · doi:10.1177/2325967116s00150 · Cited by 34

Role of serum myostatin in the association between hyperinsulinemia and muscle atrophy in Japanese obese patients

Tanaka, M., Masuda, S., Yamakage, H., Inoue, T., Ohue‐Kitano, R., Yokota, S., Kusakabe, T., Wada, H., Sanada, K., Ishii, K., et al. (2018) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2018.05.041 · Cited by 32

Myostatin knockout induces apoptosis in human cervical cancer cells via elevated reactive oxygen species generation

Han, Y.-Q., Ming, S., Wu, H.-T., Zeng, L., Ba, G., Li, J., Lu, W., Han, J., Du, Q., Sun, M., et al. (2018) · Redox Biology · doi:10.1016/j.redox.2018.09.009 · Cited by 32

The Role of Adipocytokines in Atherogenesis and Atheroprogression

Carbone, F., Mach, F., & Montecucco, F. (2015) · Current Drug Targets · doi:10.2174/1389450115666141109213439 · Cited by 31

The 2015 ESPEN Sir David Cuthbertson lecture: Inflammation as the driving force of muscle wasting in cancer

Argilés, J. M. A. (2016) · Clinical Nutrition · doi:10.1016/j.clnu.2016.05.010 · Cited by 31

Non-coding RNAs and exercise: pathophysiological role and clinical application in the cardiovascular system

Gomes, C. P. C., de Gonzalo‐Calvo, D., Toro, R., Fernandes, T. M., Theisen, D., Wang, D., Devaux, Y., & on behalf of the Cardiolinc™ network (2018) · Clinical Science · doi:10.1042/cs20171463 · Cited by 31

Hepatocyte Growth Factor and Satellite Cell Activation

Anderson, J. E. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-27511-6_1 · Cited by 30

Exercise Training as Therapeutic Approach in Cancer Cachexia: A Review of Potential Anti-inflammatory Effect on Muscle Wasting

Leal, L. G., Lopes, M. A., Peres, S. B., & Júnior, M. L. B. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2020.570170 · Cited by 30

Cancer cachexia, a clinical challenge

Argilés, J. M. A., Busquets, S., & López-Soriano, F. J. (2019) · Current Opinion in Oncology · doi:10.1097/cco.0000000000000517 · Cited by 28

Molecular basis and therapeutic potential of myostatin on bone formation and metabolism in orthopedic disease

Cui, Y., Yi, Q., Sun, W., Huang, D., Zhang, H., Duan, L., Shang, H., Wang, D., & Xiong, J. (2020) · BioFactors · doi:10.1002/biof.1675 · Cited by 30

Sarcopenia in chronic kidney disease: from bench to bedside

Kim, D. W., & Song, S. H. (2023) · The Korean Journal of Internal Medicine · doi:10.3904/kjim.2022.338 · Cited by 32

Poor maternal nutrition during gestation alters the expression of genes involved in muscle development and metabolism in lambs1

Hoffman, M. L., Peck, K. N., Wegrzyn, J., Reed, S. A., Zinn, S. A., & Govoni, K. E. (2016) · Journal of Animal Science · doi:10.2527/jas.2016-0570 · Cited by 28

Growth Differentiation Factor-8 (GDF8)/Myostatin Is a Predictor of Troponin I Peak and a Marker of Clinical Severity after Acute Myocardial Infarction

Méloux, A., Rochette, L., Maza, M., Bichât, F., Tribouillard, L., Cottin, Y., Zeller, M., & Vergely, C. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm9010116 · Cited by 27

Nitric oxide treatment attenuates muscle atrophy during hind limb suspension in mice

Anderson, J. E., Zhu, A., & Mizuno, T. M. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.12.021 · Cited by 25

In ovo L‐arginine supplementation stimulates myoblast differentiation but negatively affects muscle development of broiler chicken after hatching

Li, Y., Wang, Y., Willems, E., Willemsen, H., Franssens, L., Buyse, J., Decuypere, E., & Everaert, N. (2015) · Journal of Animal Physiology and Animal Nutrition · doi:10.1111/jpn.12299 · Cited by 25

Mutation in myostatin 3′UTR promotes C2C12 myoblast proliferation and differentiation by blocking the translation of MSTN

Ge, L., Dong, X., Gong, X., Kang, J., Zhang, Y., & Quan, F. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.03.043 · Cited by 25

Hallmarks of Appetite: A Comprehensive Review of Hunger, Appetite, Satiation, and Satiety

Garutti, M., Sirico, M., Noto, C., Foffano, L., Hopkins, M., & Puglisi, F. (2025) · Current Obesity Reports · doi:10.1007/s13679-024-00604-w · Cited by 30

The role of extracellular vesicles in skeletal muscle wasting

Zhang, X., Zhao, Y., & Yan, W. (2023) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13364 · Cited by 24

Effects of aerobic training, resistance training, or both on circulating irisin and myostatin in untrained women

Shabani, R., & Izaddoust, F. (2018) · Acta Gymnica · doi:10.5507/ag.2018.007 · Cited by 23

New insights about the putative role of myokines in the context of cardiac rehabilitation and secondary cardiovascular prevention

Raimondo, D. D., Miceli, G., Musiari, G., Tuttolomondo, M., & Pinto, A. V. (2017) · Annals of Translational Medicine · doi:10.21037/atm.2017.07.30 · Cited by 24

IL-15 expression increased in response to treadmill running and inhibited endoplasmic reticulum stress in skeletal muscle in rats

Yang, H., Luo, L.-J., Chen, W.-J., Zhao, L., Tang, C., Qi, Y., & Zhang, J. (2014) · Endocrine · doi:10.1007/s12020-014-0233-y · Cited by 22

Single nucleotide polymorphisms in the upstream regulatory region alter the expression of myostatin

Hu, W., Chen, S., Zhang, R., & Lin, Y. (2013) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-013-9621-5 · Cited by 22

Treatment to Improve Nutrition and Functional Capacity Evaluation in Liver Transplant Candidates

Dasarathy, S. (2014) · Current Treatment Options in Gastroenterology · doi:10.1007/s11938-014-0016-9 · Cited by 22

Epigenetics of cancer-associated muscle catabolism

Carr, R. M., Enriquez-Hesles, E., Olson, R. L., Jatoi, A., Doles, J. D., & Fernández-Zapico, M. E. (2017) · Epigenomics · doi:10.2217/epi-2017-0058 · Cited by 18

Bimagrumab: an investigational human monoclonal antibody against activin type II receptors for treating obesity

Kaur, M., & Misra, S. (2024) · Journal of Basic and Clinical Physiology and Pharmacology · doi:10.1515/jbcpp-2024-0065 · Cited by 17

Featured characteristics and pivotal roles of satellite cells in skeletal muscle regeneration

Song, T., & Sadayappan, S. (2019) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-019-09553-7 · Cited by 20

Histone Deacetylases as Modulators of the Crosstalk Between Skeletal Muscle and Other Organs

Renzini, A., D’Onghia, M., Coletti, D., & Moresi, V. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.706003 · Cited by 15

Nutritional Considerations in Preventing Muscle Atrophy

Creţoiu, S. M., & Zugravu, C. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-1435-3_23 · Cited by 17

Myostatin site‐directed mutation and simultaneous PPARγ site‐directed knockin in bovine genome

Ge, L., Kang, J., Dong, X., Luan, D., Su, G., Li, G., Zhang, Y., & Quan, F. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.30017 · Cited by 15

“Bioelectrical impedance analysis in managing sarcopenic obesity in NAFLD”

Hanna, D. J., Jamieson, S. T., Lee, C. S., Pluskota, C. A., Bressler, N., Benotti, P. N., Khurana, S., Rolston, D. D. K., & Still, C. D. (2021) · Obesity Science & Practice · doi:10.1002/osp4.509 · Cited by 14

Major determinants of circulating myostatin in polycystic ovary syndrome

Arpacı, H. (2018) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2018.7080 · Cited by 14

Myostatin inhibition promotes fast fibre hypertrophy but causes loss of AMP‐activated protein kinase signalling and poor exercise tolerance in a model of limb‐girdle muscular dystrophy R1/2A

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

Effect of quercetin on muscle growth and antioxidant status of the dark sleeper Odontobutis potamophila

Zhu, C., Liu, G., Gu, X., Yin, J., Xia, A., Han, M., Zhang, T., & Jiang, Q. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.938526 · Cited by 14

Effect of eccentric contraction on satellite cell activation in human vastus lateralis muscle

Imaoka, Y., Kawai, M., Mori, F., & Miyata, H. (2015) · The Journal of Physiological Sciences · doi:10.1007/s12576-015-0385-4 · Cited by 14

Targeting Unique Epitopes on Highly Similar Proteins GDF-11 and GDF-8 with Modified DNA Aptamers

Ochsner, U. A., Green, L. S., Rice, T., Olivas, E., Janjić, N., & Katilius, E. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00760 · Cited by 14

Integrated data mining of transcriptomic and proteomic datasets to predict the secretome of adipose tissue and muscle in ruminants

Bonnet, M., Tournayre, J., & Cassar‐Malek, I. (2016) · Molecular BioSystems · doi:10.1039/c6mb00224b · Cited by 12

Myostatin, a profibrotic factor and the main inhibitor of striated muscle mass, is present in the penile and vascular smooth muscle

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's marvels: From muscle regulator to diverse implications in health and disease

Sharma, S., & Patil, A. (2024) · Cell Biochemistry and Function · doi:10.1002/cbf.4106 · Cited by 12

Telmisartan versus metformin in downregulating myostatin gene expression and enhancing insulin sensitivity in the skeletal muscles of type 2 diabetic rat model

Tammam, A. A.-E., Rizg, W. Y., Boushra, A. F., Alhelf, M., Alissa, M., Soliman, G. F., Ouais, G. N., Hosny, K. M., Alkhalidi, H. M., & Elebiary, A. M. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1228525 · Cited by 10

Irisin and Myostatin Levels in Patients with Graves' Disease

Yalçın, M. M., Aktürk, M., Tohma, Y., Cerit, E. T., Altınova, A. E., Arslan, E., Yetkin, İ., & Törüner, F. B. (2016) · Archives of Medical Research · doi:10.1016/j.arcmed.2016.11.002 · Cited by 10

Inhibition of activin receptor 2 signalling ameliorates metabolic dysfunction–associated steatotic liver disease in western diet/L-NAME induced cardiometabolic disease

Swan, J., Szabó, Z., Peters, J., Kummu, O., Kemppi, A., Rahtu‐Korpela, L., Konzack, A., Hakkola, J., Pasternack, A. H., Ritvos, O., et al. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116683 · Cited by 9

Changes to daily feed intake during the laying period alters embryonicMSTNandMYOGgene expression in genetically fat and lean lines of chickens

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

Donor and recipient plasma follistatin levels are associated with acute GvHD in Blood and Marrow Transplant Clinical Trials Network 0402

Turcotte, L. M., DeFor, T. E., Newell, L. F., Cutler, C. S., Verneris, M. R., Wu, J., Howard, A., MacMillan, M. L., Antin, J. H., Vercellotti, G. M., et al. (2017) · Bone Marrow Transplantation · doi:10.1038/bmt.2017.236 · Cited by 8

Impact of Disease Severity and Disease-Modifying Therapies on Myostatin Levels in SMA Patients

Mackels, L., Mariot, V., Buscemi, L., Servais, L., & Dumonceaux, J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168763 · Cited by 8

MERG1A Protein Abundance Increases in the Atrophied Skeletal Muscle of Denervated Mice, But Does Not Affect NFκB Activity

Anderson, L. B., Ravara, B., Hameed, S., Latour, C. D., Latour, S. M., Graham, V. M., Hashmi, M. N., Cobb, B. A., Dethrow, N. M., Urazaev, A. K., et al. (2021) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlab062 · Cited by 10

Serum Myostatin and Follistatin Levels in Patients With Dermatomyositis and Polymyositis

de Sordi, C. M., dos Reis-Neto, E. T., Keppeke, G. D., Shinjo, S. K., & Sato, E. I. (2021) · JCR Journal of Clinical Rheumatology · doi:10.1097/rhu.0000000000001806 · Cited by 12

The Effects of Dietary Supplements, Nutraceutical Agents, and Physical Exercise on Myostatin Levels: Hope or Hype?

Santos, H. O., Cerqueira, H. S. C., & Tinsley, G. M. (2022) · Metabolites · doi:10.3390/metabo12111146 · Cited by 8

Influence of Muscle Mass and Strength on Bone Mineralisation with Consideration of Sclerostin Concentration

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Adipokines, myokines and cytokines in endometrial cancer patients: relations to obesity phenotype of excessive body mass and features of the tumor

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Serum myostatin level is associated with myocardial scar burden by SPECT myocardial perfusion imaging

Chiang, J., Lin, L., Wu, C., Hwang, J., Yang, W., & Wu, Y. (2022) · Clinica Chimica Acta · doi:10.1016/j.cca.2022.09.024 · Cited by 6

Sarcopenia in chronic obstructive pulmonary disease: mechanisms, diagnosis, and management strategies

Khan, M. H., Fatima, M., Adnan, A. B., Jawaid, A., Hassan, S. M., Talal, M., Rahim, S., Mughal, Z. U. N., Patel, A. O., & Singh, A. K. (2025) · Annals of Medicine and Surgery · doi:10.1097/ms9.0000000000003584 · Cited by 9

Prediction of the Secretome and the Surfaceome: A Strategy to Decipher the Crosstalk between Adipose Tissue and Muscle during Fetal Growth

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Editorial: The Fall of Mechanogrowth Factor?

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Mecanismos moleculares associados í hipertrofia e hipotrofia muscular: relação com a prática do exercício físico

Lima, W. P. (2017) · Revista Brasileira de Fisiologia do Exercício · doi:10.33233/rbfe.v16i2.972 · Cited by 3

Comprendre le développement des muscles et des tissus adipeux : un préalable pour maîtriser les qualités des carcasses et des produits des animaux d’élevage

Bonnet, M., Louveau, I., Cassar‐Malek, I., Lefaucheur, L., & Rescan, P. (2020) · INRAE Productions Animales · doi:10.20870/productions-animales.2015.28.2.3021 · Cited by 3

Role of myostatin in metabolism

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Myostatin inhibition in muscle, but not adipose tissue, decreases fat mass and improves insulin sensitivity

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DOI 10.1007/s13539-011-0035-5 REVIEW The role of myostatin in muscle wasting: an overview

Elkina, Y., von Haehling, S., Anker, S. D., Springer, J., Elkina, Y., von Haehling, S., Anker, S. D., Springer, J., Elkina, Y., Haehling, S., et al. (2011)

The role of myostatin in muscle wasting: an overview

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Myostatin: Basic biology to clinical application

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