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 5,800 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 941 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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. A., et al. (2011) · Science · doi:10.1126/science.1198973 · Cited by 586 · see citing works

Organization of the human myostatin gene and expression in healthy men and HIV-infected men with muscle wasting

Gonzalez-Cadavid, N. F., Taylor, W. E., Yarasheski, K., Sinha-Hikim, I., Ma, K., Ezzat, S., Shen, R., Lalani, R., Asa, S., Mamita, M., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14938 · Cited by 571 · see citing works

Suppression of body fat accumulation in myostatin-deficient mice

McPherron, A. C., & Lee, S.-J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0213562 · Cited by 505 · see citing works

Inhibition 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 503 · see citing works

Myostatin induces cachexia by activating the ubiquitin proteolytic system through an NF‐κB‐independent, FoxO1‐dependent mechanism

McFarlane, C., Plummer, E., Thomas, M., Hennebry, A., Ashby, M. G., Ling, N., Smith, H., Sharma, M., & Kambadur, R. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20757 · Cited by 480 · see citing works

The transforming growth factor-β superfamily of receptors

de Caestecker, M. (2004) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2003.10.004 · Cited by 464 · see citing works

Activation of latent myostatin by the BMP-1/tolloid family of metalloproteinases

Wolfman, N. M., McPherron, A. C., Pappano, W. N., Davies, M. V., Song, K., Tomkinson, K. N., Wright, J. F., Zhao, L., Sebald, S. M., Greenspan, D. S., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2534946100 · Cited by 454 · see citing works

The Myostatin Propeptide and the Follistatin-related Gene Are Inhibitory Binding Proteins of Myostatin in Normal Serum

Hill, J. J., Davies, M. V., Pearson, A. A., Wang, J. H., Hewick, R. M., Wolfman, N. M., & Qiu, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206379200 · Cited by 444 · see citing works

Lack of myostatin results in excessive muscle growth but impaired force generation

Amthor, H., Macharia, R., Navarrete, R., Schuelke, M., Brown, S., Otto, A., Voït, T., Francesco Muntoni, A., Vrbovà, G., Partridge, T. A., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604893104 · Cited by 425 · see citing works

Myostatin inhibits cell proliferation and protein synthesis in C2C12 muscle cells

Taylor, W. E., Bhasin, S., Artaza, J., Byhower, F., Azam, M., Willard, D. H., Kull, F. C., & González-Cadavid, N. F. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.280.2.e221 · Cited by 410 · see citing works

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

Guo, T., Jou, W., Chanturiya, T., Portas, J., Gavrilova, O., & McPherron, A. C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004937 · Cited by 402 · see citing works

Signaling pathways perturbing muscle mass.

Glass, D. J. (2010) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e32833862df · Cited by 359 · see citing works

Functional and morphological recovery of dystrophic muscles in mice treated with deacetylase inhibitors

Minetti, G., Colussi, C., Adami, R., Serra, C., Mozzetta, C., Parente, V., Fortuni, S., Straino, S., Sampaolesi, M., Padova, M. D., et al. (2006) · Nature Medicine · doi:10.1038/nm1479 · Cited by 341 · see citing works

Increased secretion and expression of myostatin in skeletal muscle from extremely obese women

Hittel, D. S., Berggren, J. R., Shearer, J., Boyle, K., & Houmard, J. A. (2009) · Diabetes · doi:10.2337/db08-0943 · Cited by 324 · see citing works

Serum myostatin-immunoreactive protein is increased in 60-92 year old women and men with muscle wasting.

Yarasheski, K. E., Bhasin, S., Sinha‐Hikim, I., Pak-Loduca, J., & González-Cadavid, N. F. (2002) · PubMed · Cited by 293 · see citing works

Human Sarcopenia Reveals an Increase in SOCS-3 and Myostatin and a Reduced Efficiency of Akt Phosphorylation

Léger, B., Derave, W., Bock, K. D., Hespel, P., & Russell, A. P. (2008) · Rejuvenation Research · doi:10.1089/rej.2007.0588 · Cited by 274 · see citing works

Myostatin and the control of skeletal muscle mass

Lee, S., & McPherron, A. C. (1999) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(99)00004-0 · Cited by 273 · see citing works

Myostatin decreases with aerobic exercise and associates with insulin resistance

HITTEL, D. S., AXELSON, M., SARNA, N., SHEARER, J., HUFFMAN, K. M., & KRAUS, W. E. (2010) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3181e0b9a8 · Cited by 271 · see citing works

Structure of the ternary signaling complex of a TGF-β superfamily member

Allendorph, G. P., Vale, W., & Choe, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602558103 · Cited by 247 · see citing works

Deacetylase Inhibitors Increase Muscle Cell Size by Promoting Myoblast Recruitment and Fusion through Induction of Follistatin

Iezzi, S., Padova, M. D., Serra, C., Caretti, G., Simone, C., Maklan, E., Minetti, G., Zhao, P., Hoffman, E. P., Puri, P., et al. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00107-8 · Cited by 238 · see citing works

Genetic deletion of myostatin from the heart prevents skeletal muscle atrophy in heart failure

Heineke, J., Auger-Messier, M., Xu, J., Sargent, M., York, A., Welle, S., & Molkentin, J. D. (2010) · Circulation · doi:10.1161/circulationaha.109.882068 · Cited by 238 · see citing works

Acute inhibition of myostatin-family proteins preserves skeletal muscle in mouse models of cancer cachexia

Klimek, M. B., Aydogdu, T., Link, M., Pons, M., Koniaris, L. G., & Zimmers, T. A. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.12.123 · Cited by 229 · see citing works

Secreted proteins from adipose tissue and skeletal muscle – adipokines, myokines and adipose/muscle cross-talk

Trayhurn, P., Drevon, C. A., & Eckel, J. (2011) · Archives of Physiology and Biochemistry · doi:10.3109/13813455.2010.535835 · Cited by 214 · see citing works

The role of cytokines in cancer cachexia

Argilés, J. M. A., Busquets, S., Toledo, M., & López-Soriano, F. J. (2009) · Current Opinion in Supportive and Palliative Care · doi:10.1097/spc.0b013e3283311d09 · Cited by 211 · see citing works

Myostatin modulates adipogenesis to generate adipocytes with favorable metabolic effects

Feldman, B. J., Streeper, R. S., Farese, R. V., & Yamamoto, K. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607501103 · Cited by 210 · see citing works

Myostatin Inhibits Myogenesis and Promotes Adipogenesis in C3H 10T(1/2) Mesenchymal Multipotent Cells

Artaza, J. N., Bhasin, S., Magee, T. R., Reisz‐Porszasz, S., Shen, R., Groome, N. P., Fareez, M. M., & González-Cadavid, N. F. (2005) · Endocrinology · doi:10.1210/en.2005-0362 · Cited by 207 · see citing works

Myostatin (GDF-8) as a key factor linking muscle mass and bone structure.

Elkasrawy, M., & Hamrick, M. W. (2010) · PubMed · Cited by 203 · see citing works

Exercise induces a marked increase in plasma follistatin: Evidence that follistatin is a contraction-induced hepatokine

Hansen, J., Brandt, C., Nielsen, A. R., Hojman, P., Whitham, M., Febbraio, M. A., Pedersen, B. K., & Plomgaard, P. (2011) · Endocrinology · doi:10.1210/en.2010-0868 · Cited by 200 · see citing works

Inhibition of myostatin with emphasis on follistatin as a therapy for muscle disease

Rodino‐Klapac, L. R., Haidet, A. M., Kota, J., Handy, C., Kaspar, B. K., & Mendell, J. R. (2009) · Muscle & Nerve · doi:10.1002/mus.21244 · Cited by 194 · see citing works

Cross-talk between skeletal muscle and adipose tissue: A link with obesity?

Argilés, J. M. A., López‐Soriano, J., Almendro, V., Busquets, S., & López-Soriano, F. J. (2004) · Medicinal Research Reviews · doi:10.1002/med.20010 · Cited by 194 · see citing works

Inhibition of myostatin protects against diet-induced obesity by enhancing fatty acid oxidation and promoting a brown adipose phenotype in mice

Zhang, C., McFarlane, C., Lokireddy, S., Masuda, S., Ge, X., Gluckman, P. D., Sharma, M., & Kambadur, R. (2012) · Diabetologia · doi:10.1007/s00125-011-2304-4 · Cited by 192 · see citing works

Transgenic expression of myostatin propeptide prevents diet-induced obesity and insulin resistance

Zhao, B., Wall, R. J., & Yang, J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.09.044 · Cited by 186 · see citing works

TNF Can Directly Induce the Expression of Ubiquitin-Dependent Proteolytic System in Rat Soleus Muscles

Llovera, M., Garcia‐Martínez, C., Agell, N., López-Soriano, F. J., & Argilés, J. M. A. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.5827 · Cited by 184 · see citing works

Myostatin, activin receptor IIb, and follistatin-like-3 gene expression are altered in adipose tissue and skeletal muscle of obese mice

Allen, D. L., Cleary, A. S., Speaker, K. J., Lindsay, S. F., Uyenishi, J., Reed, J. M., Madden, M. C., & Mehan, R. S. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00798.2007 · Cited by 183 · see citing works

Muscle myostatin signalling is enhanced in experimental cancer cachexia

Costelli, P., Muscaritoli, M., Bonetto, A., Penna, F., Reffo, P., Bossola, M., Bonelli, G., Doglietto, G. B., Baccino, F. M., & Fanelli, F. R. (2008) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2008.01970.x · Cited by 181 · see citing works

Anticachectic Effects of Formoterol

Busquets, S., Figueras, M. T., Fuster, G., Almendro, V., Moore‐Carrasco, R., Ametller, E., Argilés, J. M. A., & López-Soriano, F. J. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0425 · Cited by 167 · see citing works

Increased muscle ubiquitin mRNA levels in gastric cancer patients.

Bossola, M., Muscaritoli, M., Costelli, P., Bellantone, R., Pacelli, F., Busquets, S., Argilès, J., López-Soriano, F., Civello, I. M., Baccino, F., et al. (2001) · American Journal of Physiology. Regulatory Integrative and Comparative Physiology · doi:10.1152/ajpregu.2001.280.5.r1518 · Cited by 164 · see citing works

Ectopic Expression of Myostatin Induces Atrophy of Adult Skeletal Muscle by Decreasing Muscle Gene Expression

Durieux, A., Amirouche, A., Banzet, S., Koulmann, N., Bonnefoy, R., Pasdeloup, M., Mouret, C., Bigard, X. A., Peinnequin, A., & Freyssenet, D. G. (2007) · Endocrinology · doi:10.1210/en.2006-1500 · Cited by 162 · see citing works

The myostatin gene: physiology and pharmacological relevance

Joulia-Ekaza, D., & Cabello, G. (2007) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2006.11.011 · Cited by 160 · see citing works

Myostatin-deficient mice exhibit reduced insulin resistance through activating the AMP-activated protein kinase signalling pathway

Zhang, C., McFarlane, C., Lokireddy, S., Bonala, S., Ge, X., Masuda, S., Gluckman, P. D., Sharma, M., & Kambadur, R. (2011) · Diabetologia · doi:10.1007/s00125-011-2079-7 · Cited by 158 · see citing works

Myostatin Propeptide Gene Delivery by Adeno-Associated Virus Serotype 8 Vectors Enhances Muscle Growth and Ameliorates Dystrophic Phenotypes in mdx Mice

Qiao, C., Li, J., Jiang, J., Zhu, X., Wang, B., Li, J., & Xiao, X. (2008) · Human Gene Therapy · doi:10.1089/hum.2007.159 · Cited by 157 · see citing works

Identification of a Novel Pool of Extracellular Pro-myostatin in Skeletal Muscle

Anderson, S. B., Goldberg, A. L., & Whitman, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706678200 · Cited by 150 · see citing works

The effects of a soluble activin type IIB receptor on obesity and insulin sensitivity

Akpan, I., Goncalves, M. D., Dhir, R., Yin, X., Pistilli, E. E., Bogdanovich, S., Khurana, T. S., Ucran, J., Lachey, J., & Ahima, R. S. (2009) · International Journal of Obesity · doi:10.1038/ijo.2009.162 · Cited by 140 · see citing works

Exercise training leads to a reduction of elevated myostatin levels in patients with chronic heart failure

Lenk, K., Erbs, S., Höllriegel, R., Beck, E. B., Linke, A. H.-P., Gielen, S., Winkler, S. M., Sandri, M., Hambrecht, R., Schuler, G. C., et al. (2011) · European Journal of Preventive Cardiology · doi:10.1177/1741826711402735 · Cited by 140 · see citing works

Prolonged absence of myostatin reduces sarcopenia

Siriett, V., Platt, L., Salerno, M. S., Ling, N., Kambadur, R., & Sharma, M. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20778 · Cited by 139 · see citing works

The Regulation and Action of Myostatin as a Negative Regulator of Muscle Development during Avian Embryogenesis

Amthor, H., Huang, R., McKinnell, I. W., Christ, B., Kambadur, R., Sharma, M., & Patel, K. (2002) · Developmental Biology · doi:10.1006/dbio.2002.0812 · Cited by 138 · see citing works

Impact of Exercise Training on Myostatin Expression in the Myocardium and Skeletal Muscle in a Chronic Heart Failure Model

Lenk, K., Schur, R., Linke, A., Erbs, S., Matsumoto, Y., Adams, V., & Schuler, G. C. (2009) · European Journal of Heart Failure · doi:10.1093/eurjhf/hfp020 · Cited by 136 · see citing works

Skeletal Muscle Hypertrophy and Muscle Myostatin Reduction After Resistive Training in Stroke Survivors

Ryan, A. S., Ivey, F. M., Prior, S. J., Li, G., & Hafer‐Macko, C. E. (2010) · Stroke · doi:10.1161/strokeaha.110.602441 · Cited by 131 · see citing works

Myostatin from the heart: local and systemic actions in cardiac failure and muscle wasting

Breitbart, A., Auger‐Messier, M., Molkentin, J. D., & Heineke, J. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00200.2011 · Cited by 131 · see citing works

Decorin enhances the proliferation and differentiation of myogenic cells through suppressing myostatin activity

Kishioka, Y., Thomas, M., Wakamatsu, J., Hattori, A., Sharma, M., Kambadur, R., & Nishimura, T. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21371 · Cited by 130 · see citing works

Transcriptional profiling of myostatin‐knockout mice implicates Wnt signaling in postnatal skeletal muscle growth and hypertrophy

Steelman, C. A., Recknor, J. C., Nettleton, D. S., & Reecy, J. M. (2006) · The FASEB Journal · doi:10.1096/fj.05-5125fje · Cited by 129 · see citing works

Recent advances in the biology and therapy of muscle wasting

Glass, D. J., & Roubenoff, R. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05809.x · Cited by 127 · see citing works

Antibody‐directed myostatin inhibition in 21‐mo‐old mice reveals novel roles for myostatin signaling in skeletal muscle structure and function

Murphy, K. T., Koopman, R., Naim, T., Léger, B., Trieu, J., Ibebunjo, C., & Lynch, G. S. (2010) · The FASEB Journal · doi:10.1096/fj.10-159608 · Cited by 124 · see citing works

Muscular atrophy of caveolin-3–deficient mice is rescued by myostatin inhibition

Ohsawa, Y., Hagiwara, H., Nakatani, M., Yasue, A., Moriyama, K., Murakami, T., Tsuchida, K., Noji, S., & Sunada, Y. (2006) · Journal of Clinical Investigation · doi:10.1172/jci28520 · Cited by 120 · see citing works

Genetic Analysis of the Role of Proteolysis in the Activation of Latent Myostatin

Lee, S.-J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001628 · Cited by 113 · see citing works

Regulation of myostatin signaling by c-Jun N-terminal kinase in C2C12 cells

Huang, Z., Chen, D., Zhang, K., Yu, B., Chen, X., & Meng, J. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.07.002 · Cited by 104 · see citing works

Structure to function: muscle failure in critically ill patients

Puthucheary, Z., Montgomery, H., Moxham, J., Harridge, S. D. R., & Hart, N. (2010) · The Journal of Physiology · doi:10.1113/jphysiol.2010.197632 · Cited by 103 · see citing works

Changes in Muscle Myostatin Expression in Obese Subjects after Weight Loss

Milan, G., Nora, E. D., Pilon, C., Pagano, C., Granzotto, M., Manco, M., Mingrone, G., & Vettor, R. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-032047 · Cited by 100 · see citing works

Myostatin Up-Regulation Is Associated with the Skeletal Muscle Response to Hypoxic Stimuli

Hayot, M., Rodriguez, J., Vernus, B., Carnac, G., Jean, E., Allen, D., Goret, L., Obert, P., Candau, R., & Bonnieu, A. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.09.008 · Cited by 98 · see citing works

Myostatin antisense RNA-mediated muscle growth in normal and cancer cachexia mice

Cm, L., Yang, Z., Liu, C.-W., Wang, R., Tien, P., Dale, R., & Sun, L.-Q. (2007) · Gene Therapy · doi:10.1038/sj.gt.3303016 · Cited by 98 · see citing works

Systemic inflammation correlates with increased expression of skeletal muscle ubiquitin but not uncoupling proteins in cancer cachexia

Dejong, C. H. C., Busquets, S., Moses, A. G. W., Schrauwen, P., Ross, J. A., Argilés, J. M. A., & Fearon, K. C. H. (2005) · Oncology Reports · doi:10.3892/or.14.1.257 · Cited by 90 · see citing works

Atrophy and hypertrophy signalling in the diaphragm of patients with COPD

Testelmans, D., Crul, T., Maes, K., Agten, A., Crombach, M., Decramer, M., & Gayan‐Ramirez, G. (2009) · European Respiratory Journal · doi:10.1183/09031936.00091108 · Cited by 87 · see citing works

Targeting myostatin for therapies against muscle-wasting disorders.

Tsuchida, K. (2008) · PubMed · Cited by 84 · see citing works

Myostatin in Muscle Growth and Repair

Sharma, M., Langley, B. C., Bass, J. J., & Kambadur, R. (2001) · Exercise and Sport Sciences Reviews · doi:10.1097/00003677-200110000-00004 · Cited by 84 · see citing works

Changes in Myostatin Signaling in Non-Weight-Losing Cancer Patients

Aversa, Z., Bonetto, A., Penna, F., Costelli, P., Rienzo, G. D., Lacitignola, A., Baccino, F. M., Ziparo, V., Mercantini, P., Fanelli, F. R., et al. (2011) · Annals of Surgical Oncology · doi:10.1245/s10434-011-1720-5 · Cited by 83 · see citing works

Combination of Myostatin Pathway Interference and Dystrophin Rescue Enhances Tetanic and Specific Force in Dystrophic mdx Mice

Dumonceaux, J., Marie, S., Beley, C., Trollet, C., Vignaud, A., Ferry, A., Butler-Browne, G. S., & Garcı́a, L. (2010) · Molecular Therapy · doi:10.1038/mt.2009.322 · Cited by 79 · see citing works

Effect of RNA oligonucleotide targeting Foxo-1 on muscle growth in normal and cancer cachexia mice

Cm, L., Yang, Z., Liu, C.-W., Wang, R., Tien, P., Dale, R., & Sun, L.-Q. (2007) · Cancer Gene Therapy · doi:10.1038/sj.cgt.7701091 · Cited by 78 · see citing works

Myostatin blockade improves function but not histopathology in a murine model of limb‐girdle muscular dystrophy 2C

Bogdanovich, S., McNally, E. M., & Khurana, T. S. (2007) · Muscle & Nerve · doi:10.1002/mus.20920 · Cited by 74 · see citing works

The Effect of Glutamine on Prevention of Glucocorticoid-Induced Skeletal Muscle Atrophy Is Associated with Myostatin Suppression

Salehian, B., Mahabadi, V., Bilas, J., Taylor, W. E., & Ma, K. (2006) · Metabolism · doi:10.1016/j.metabol.2006.05.009 · Cited by 69 · see citing works

Deacetylase Inhibitors Modulate the Myostatin/Follistatin Axis without Improving Cachexia in Tumor-Bearing Mice

Bonetto, A., Penna, F., Minero, V. G., Reffo, P., Bonelli, G., Baccino, F. M., & Costelli, P. (2009) · Current Cancer Drug Targets · doi:10.2174/156800909789057015 · Cited by 69 · see citing works

Systemic Myostatin Inhibition via Liver-Targeted Gene Transfer in Normal and Dystrophic Mice

Morine, K., Bish, L. T., Pendrak, K., Sleeper, M. M., Barton, E. R., & Sweeney, H. L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009176 · Cited by 64 · see citing works

Upregulation of myostatin gene expression in streptozotocin-induced type 1 diabetes mice is attenuated by insulin

Chen, Y., Cao, L., Ye, J., & Zhu, D. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.07.129 · Cited by 63 · see citing works

Role of Follistatin in Promoting Adipogenesis in Women

Flanagan, J. N., Linder, K., Mejhert, N., Dungner, E., Wåhlén, K., Decaunes, P., Rydén, M., Björklund, P., Arver, S., Bhasin, S., et al. (2009) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2008-2005 · Cited by 63 · see citing works

Sprinting without myostatin: a genetic determinant of athletic prowess

Lee, S. (2007) · Trends in Genetics · doi:10.1016/j.tig.2007.08.008 · Cited by 61 · see citing works

Mechanisms to explain wasting of muscle and fat in cancer cachexia

Argilés, J. M. A., López-Soriano, F. J., & Busquets, S. (2007) · Current Opinion in Supportive and Palliative Care · doi:10.1097/spc.0b013e3282f34738 · Cited by 57 · see citing works

Inhibiting Myostatin with Follistatin Improves the Success of Myoblast Transplantation in Dystrophic Mice

Benabdallah, B., Bouchentouf, M., Rousseau, J., Bigey, P., Michaud, A., Chapdelaine, P., Scherman, D., & Tremblay, J. P. (2008) · Cell Transplantation · doi:10.3727/096368908784153913 · Cited by 51 · see citing works

Quadriceps Myostatin Expression in COPD

D-C. Man, W., Natanek, S. A., Riddoch-Contreras, J., Lewis, A., Marsh, G. S., Kemp, P. R., & Polkey, M. I. (2010) · European Respiratory Journal · doi:10.1183/09031936.00032510 · Cited by 48 · see citing works

Myostatin regulates preadipocyte differentiation and lipid metabolism of adipocyte via ERK1/2

Li, F., Yang, H., Duan, Y., & Yin, Y. (2011) · Cell Biology International · doi:10.1042/cbi20110112 · Cited by 47 · see citing works

Glutamine prevents myostatin hyperexpression and protein hypercatabolism induced in C2C12 myotubes by tumor necrosis factor-α

Bonetto, A., Penna, F., Minero, V. G., Reffo, P., Costamagna, D., Bonelli, G., Baccino, F. M., & Costelli, P. (2010) · Amino Acids · doi:10.1007/s00726-010-0683-3 · Cited by 43 · see citing works

Blocking the Myostatin Signal With a Dominant Negative Receptor Improves the Success of Human Myoblast Transplantation in Dystrophic Mice

Fakhfakh, R., Michaud, A., & Tremblay, J. P. (2010) · Molecular Therapy · doi:10.1038/mt.2010.171 · Cited by 42 · see citing works

Enhanced muscle by myostatin propeptide increases adipose tissue adiponectin, PPAR-α, and PPAR-γ expressions

Suzuki, S., Zhao, B., & Yang, J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.02.092 · Cited by 36 · see citing works

Follistatin-derived peptide expression in muscle decreases adipose tissue mass and prevents hepatic steatosis

Nakatani, M., Kokubo, M., Ohsawa, Y., Sunada, Y., & Tsuchida, K. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00430.2010 · Cited by 34 · see citing works

Interaction between myostatin and extracellular matrix components

Miura, T., Kishioka, Y., Wakamatsu, J., Hattori, A., & Nishimura, T. (2009) · Animal Science Journal · doi:10.1111/j.1740-0929.2009.00700.x · Cited by 33 · see citing works

Identification of NF-kappaB responsive elements in follistatin related gene (FLRG) promoter

Bartholin, L., Guindon, S., Martel, S., Corbo, L., & Rimokh, R. (2007) · Gene · doi:10.1016/j.gene.2007.02.007 · Cited by 24 · see citing works

Towards a fluorescent chemoreceptive lipid membrane-based optode

Krull, U. J. (1988) · Talanta · doi:10.1016/0039-9140(88)80051-1 · Cited by 19 · see citing works

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 · see citing works

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 1,518 · see citing works

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 · see citing works

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 375 · see citing works

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 305 · see citing works

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 · see citing works

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 243 · see citing works

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 · see citing works

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 · see citing works

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 151 · see citing works

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 · see citing works

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 139 · see citing works

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 117 · see citing works

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 · see citing works

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 · see citing works

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 90 · see citing works

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 · see citing works

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 · see citing works

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

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 · see citing works

Hormones and Muscle Atrophy.

Martín, A., Priego, T., & López-Calderón, A. (2018) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-13-1435-3_9 · Cited by 68 · see citing works

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 · see citing works

Cancer-Mediated Muscle Cachexia: Etiology and Clinical Management

Siff, T., Parajuli, P., Razzaque, M., & Atfi, A. (2021) · Trends in endocrinology and metabolism · doi:10.1016/j.tem.2021.03.007 · Cited by 62 · see citing works

Advances in research on pharmacotherapy of sarcopenia

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

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 63 · see citing works

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 · see citing works

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 57 · see citing works

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 · see citing works

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 56 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 47 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 44 · see citing works

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 · see citing works

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 · see citing works

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 39 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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

Miao, C.-X., Lv, Y.-Y., Zhang, W., Chai, X., Feng, L.-X., Fang, Y., Liu, X., & Zhang, X.-W. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00915 · Cited by 35 · see citing works

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 35 · see citing works

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 33 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 30 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 30 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 24 · see citing works

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 · see citing works

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 · see citing works

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 23 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 17 · see citing works

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 16 · see citing works

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 16 · see citing works

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 · see citing works

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 16 · see citing works

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 · see citing works

“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 13 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 13 · see citing works

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 · see citing works

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 · see citing works

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 11 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 8 · see citing works

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 8 · see citing works

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 · see citing works

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

Patalong-Wójcik, M., Golara, A., Zając, K., Sokołowska, A., Kozłowski, M., Tołoczko‐Grabarek, A., Krzyścin, M., Brodowska, A., Janiec, A., Myszka, A., et al. (2023) · Biomedicines · doi:10.3390/biomedicines11061574 · Cited by 7 · see citing works

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

Berstein, L. M., Евгеньевна, П. Т., & Vasilyev, D. A. (2017) · Obesity and metabolism · doi:10.14341/omet2017135-40 · Cited by 6 · see citing works

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 · see citing works

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 6 · see citing works

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

Bonnet, M., Kaspric, N., Vonnahme, K. A., Viala, D., Chambon, C., & Picard, B. B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124375 · Cited by 5 · see citing works

Editorial: The Fall of Mechanogrowth Factor?

Rotwein, P. S. (2014) · Molecular Endocrinology · doi:10.1210/me.2013-1411 · Cited by 5 · see citing works

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 · see citing works

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 · see citing works

Role of myostatin in metabolism

González-Cadavid, N. F., & Bhasin, S. (2004) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/01.mco.0000134365.99523.7f · Cited by 88 · see citing works

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

Guo, T., Jou, W., Chanturiya, T., Portas, J., Gavrilova, O., & McPherron, A. C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004937 · Cited by 402 · see citing works

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

Elkina, Y., von Haehling, S., Anker, S. D., & Springer, J. (2011) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0035-5 · Cited by 349 · see citing works

Myostatin: Basic biology to clinical application

Esposito, P. B., Picciotto, D., Battaglia, Y., Costigliolo, F., Viazzi, F. C., & Verzola, D. (2022) · Advances in clinical chemistry · doi:10.1016/bs.acc.2021.09.006 · Cited by 70 · see citing works