Myostatin and its Regulation: A Comprehensive Review of Myostatin Inhibiting Strategies
Open accessAbstract
Myostatin (MSTN) is a well-reported negative regulator of muscle growth and a member of the transforming growth factor (TGF) family. MSTN has important functions in skeletal muscle (SM), and its crucial involvement in several disorders has made it an important therapeutic target. Several strategies based on the use of natural compounds to inhibitory peptides are being used to inhibit the activity of MSTN. This review delivers an overview of the current state of knowledge about SM and myogenesis with particular emphasis on the structural characteristics and regulatory functions of MSTN during myogenesis and its involvements in various muscle related disorders. In addition, we review the diverse approaches used to inhibit the activity of MSTN, especially in silico approaches to the screening of natural compounds and the design of novel short peptides derived from proteins that typically interact with MSTN.
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
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In human skeletal muscle, resistance training primarily activates mechanical stress-sensitive pathways; tension sensed by integrins and focal adhesion kinase leads to JNK phosphorylation, and JNK phosphorylates Smad2/3 and inhibits nuclear translocation, downregulating MSTN expression.
“In human skeletal muscle, resistance training primarily activates mechanical stress-sensitive pathways. The tension generated during muscle contraction is sensed by integrins and focal adhesion kinase (FAK), leading to JNK phosphorylation. JNK directly phosphorylates Smad2/3 and inhibits their nuclear translocation, thereby downregulating MSTN expression [55].”
From Exercise-Induced Myokines in Obesity-Related Metabolic Disorders and Cardiovascular Protection: A Narrative Review (2026) · cites this paper as [55]
Split into 2 atoms — 0 confirmed, 0 partially supported, 1 disputed, 0 misattributed, 1 unverifiable. Expand the claim to see per-atom verdicts.
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredThe molecular mechanisms underlying resistance training-induced myostatin suppression involve inhibition of the classical SMAD pathway and modulation of non-SMAD pathways such as MAPK/ERK, p38, JNK, and Akt phosphorylation.
“The molecular mechanisms underlying resistance training-induced MSTN suppression involve multiple signaling pathways, including inhibition of the classical SMAD pathway and modulation of non-SMAD pathways such as MAPK/ERK, p38, JNK, and Akt phosphorylation [55].”
From Exercise-Induced Myokines in Obesity-Related Metabolic Disorders and Cardiovascular Protection: A Narrative Review (2026) · cites this paper as [55]
The Signaling Pathways section describes Smad and non-Smad myostatin signaling, including JNK/ERK, p38 MAPK, and Akt phosphorylation. The Smad-Mediated Pathways subsection also associates inhibition of myostatin–Smad signaling with muscle hypertrophy. These passages do not establish that resistance training suppresses myostatin through those pathways. (LLM, conf=0.87)
Experimental — accuracy not yet measuredMyostatin exerts its effects by binding to activin receptor type IIB, leading to phosphorylation of SMAD2/3 and subsequent inhibition of myogenic gene transcription.
“MSTN exerts its effects by binding to activin receptor type IIB (ActRIIB), leading to phosphorylation of SMAD2/3 and subsequent inhibition of myogenic gene transcription [55].”
From Exercise-Induced Myokines in Obesity-Related Metabolic Disorders and Cardiovascular Protection: A Narrative Review (2026) · cites this paper as [55]
The Signaling Pathways figure says MSTN binds the ACVRIIB–ALK4/5 complex and triggers Smad2/3 phosphorylation. The Smad-Mediated Pathways section says this signaling inhibits myoblast differentiation, but the copy does not specifically say that phosphorylated Smad2/3 inhibits myogenic gene transcription; it describes transcriptional alterations more generally. (LLM, conf=0.82)
Experimental — accuracy not yet measuredMyostatin is also expressed in adipose tissue and has been implicated in metabolic regulation and cardiovascular pathology.
“Beyond its canonical role in muscle, MSTN is also expressed in adipose tissue and has been implicated in metabolic regulation and cardiovascular pathology.”
From Exercise-Induced Myokines in Obesity-Related Metabolic Disorders and Cardiovascular Protection: A Narrative Review (2026) · cites this paper as [55]
The ‘Diabetes and Obesity’ section implicates MSTN in metabolic regulation, including insulin sensitivity and obesity. The copy does not establish that MSTN itself is expressed in adipose tissue: the ‘MSTN Receptor Proteins’ section says its receptor is distributed there, while a reference title mentions adipose-tissue gene expression. Its cardiovascular references concern myokines generally or an inhibitor, not a role for MSTN in cardiovascular pathology. No page numbers are provided in the copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredMyostatin levels rise with increasing obesity and correlate with insulin resistance, whereas Metrnl levels may progressively decrease as obesity worsens.
“Closely related is obesity severity: myostatin levels have been shown to rise with increasing obesity and to correlate with insulin resistance [55], whereas Metrnl levels may progressively decrease as obesity worsens [68].”
From Exercise-Induced Myokines in Obesity-Related Metabolic Disorders and Cardiovascular Protection: A Narrative Review (2026) · cites this paper as [55]
The “Diabetes and Obesity” section (page unavailable) reports higher myostatin secretion in obese insulin-resistant subjects, high expression in morbidly obese patients, and an inverse relationship between myostatin expression and insulin sensitivity. It does not establish that myostatin levels rise progressively as obesity severity increases. The Metrnl clause is attributed to a different citation and is not part of this verdict. (LLM, conf=0.84)
Experimental — accuracy not yet measured
Myostatin is a member of the transforming growth factor-beta superfamily, primarily expressed in skeletal muscle, and functions as a key negative regulator of muscle growth and development.
“Myostatin (MSTN), also known as growth differentiation factor 8 (GDF-8), is a member of the transforming growth factor-beta (TGF-β) superfamily. It is primarily expressed in skeletal muscle and functions as a key negative regulator of muscle growth and development [55].”
From Exercise-Induced Myokines in Obesity-Related Metabolic Disorders and Cardiovascular Protection: A Narrative Review (2026) · cites this paper as [55]
Exercise downregulates myostatin expression, with the magnitude of reduction depending on exercise mode, duration, and intensity.
“Exercise downregulates MSTN expression, with the magnitude of reduction depending on exercise mode, duration, and intensity.”
From Exercise-Induced Myokines in Obesity-Related Metabolic Disorders and Cardiovascular Protection: A Narrative Review (2026) · cites this paper as [55]
The Myokines section says exercise regulates myokine secretion, but does not say that it downregulates MSTN expression. A References entry names a study on reduced myostatin with aerobic exercise; the passages found do not address whether the reduction depends on exercise mode, duration, or intensity (pages unavailable). (LLM, conf=0.70)
Experimental — accuracy not yet measuredMechanistic insights from cell and animal studies suggest that when muscle is subjected to mechanical stress, it can downregulate myostatin expression via pathways such as JNK-mediated phosphorylation of transcription factor Smad2.
“Mechanistic insights from cell and animal studies suggest that when muscle is subjected to mechanical stress, it can downregulate MSTN expression via pathways such as JNK-mediated phosphorylation of transcription factor Smad2 [55,57].”
From Exercise-Induced Myokines in Obesity-Related Metabolic Disorders and Cardiovascular Protection: A Narrative Review (2026) · cites this paper as [55]
The Signaling Pathways sections describe MSTN activating JNK in C2C12 cells and signaling through Smad2/3, but do not say that mechanical stress downregulates MSTN expression or that JNK phosphorylates Smad2 in that process. Searches for mechanical loading, exercise-induced downregulation, and JNK-mediated Smad2 phosphorylation found no passage establishing the claimed mechanism. Page numbers were unavailable in our copy. (LLM, conf=0.74)
Experimental — accuracy not yet measuredResistance training activates JNK/Smad pathways to inhibit MSTN expression.
“Resistance training, through its characteristic mechanical load, efficiently activates JNK/Smad pathways to inhibit MSTN expression [55].”
From Exercise-Induced Myokines in Obesity-Related Metabolic Disorders and Cardiovascular Protection: A Narrative Review (2026) · cites this paper as [55]
The Signaling Pathways sections describe MSTN activating JNK and Smad signaling, but do not say that resistance training or mechanical load activates those pathways to inhibit MSTN expression. A search for “resistance training” found it only in a reference title, not in a passage establishing the claimed mechanism. Our copy therefore does not verify the relationship attributed to this review. (LLM, conf=0.76)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · cited 1× · see citing works
“The advancement in the field of 3-dimensional structure predictions of proteins and PPI includes the recent discovery of AlphaFold (Jumper et al., 2021) and AlphaFold2 (Bryant et al., 2022).”
BackgroundTrott, O., & Olson, A. J. (2010) · Journal of Computational Chemistry · doi:10.1002/jcc.21334 · Cited by 38,412 · 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
Muscles, exercise and obesity: skeletal muscle as a secretory organ
Pedersen, B. K., & Febbraio, M. A. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2012.49 · Cited by 2,909 · see citing works
Principles of protein-protein interactions
Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684 · see citing works
Skeletal muscle: A brief review of structure and function
Frontera, W. R., & Ochala, J. (2015) · Calcified Tissue International · doi:10.1007/s00223-014-9915-y · Cited by 1,758 · see citing works
Regulation 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 · see citing works
Synthetic therapeutic peptides: science and market
Vlieghe, P., Lisowski, V., Martínez, J., & Khrestchatisky, M. (2009) · Drug Discovery Today · doi:10.1016/j.drudis.2009.10.009 · Cited by 1,487 · see citing works
Vilar, S., Cozza, G., & Moro, S. (2008) · Current Topics in Medicinal Chemistry · doi:10.2174/156802608786786624 · Cited by 1,200 · see citing works
Improved prediction of protein-protein interactions using AlphaFold2
Bryant, P., Pozzati, G., & Elofsson, A. (2021) · doi:10.1101/2021.09.15.460468 · Cited by 1,025 · 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
Mechanisms of muscle atrophy and hypertrophy: implications in health and disease
Sartori, R., Romanello, V., & Sandri, M. (2021) · Nature Communications · doi:10.1038/s41467-020-20123-1 · Cited by 940 · see citing works
Muscle satellite cells adopt divergent fates
Zammit, P. S., Golding, J. P., Nagata, Y., Hudon, V., Partridge, T. A., & Beauchamp, J. R. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200312007 · Cited by 924 · see citing works
Lu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891 · see citing works
Interleukin-6 Is an Essential Regulator of Satellite Cell-Mediated Skeletal Muscle Hypertrophy
Serrano, A. L., Baeza-Raja, B., Perdiguero, E., Jardí, M., & Muñoz-Cánoves, P. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.011 · Cited by 873 · see citing works
Interleukin‐6 myokine signaling in skeletal muscle: a double‐edged sword?
Muñoz‐Cánoves, P., Scheele, C., Pedersen, B. K., & Serrano, A. L. (2013) · The FEBS Journal · doi:10.1111/febs.12338 · Cited by 774 · see citing works
The circuitry of a master switch: Myod and the regulation of skeletal muscle gene transcription
Tapscott, S. J. (2005) · Development · doi:10.1242/dev.01874 · Cited by 766 · cited 1× · see citing works
“…by Myf5, drives cells to the myogenic lineage, and MYOG seems to work downstream of Myf5 and MyoD, and it is necessary for the establishment of the myogenic lineage as well as terminal differentiation of myoblasts (Lindon et al., 1998; Tapscott, 2005; Londhe and Davie, 2011; Ganassi et al., 2020).”
BackgroundSatellite Cells and Skeletal Muscle Regeneration
Dumont, N. A., Bentzinger, C. F., Sincennes, M., & Rudnicki, M. A. (2015) · Comprehensive Physiology · doi:10.1002/cphy.c140068 · Cited by 719 · see citing works
Skeletal Muscle Regulates Metabolism via Interorgan Crosstalk: Roles in Health and Disease
Argilés, J. M., Campos, N., Lopez-Pedrosa, J. M., Rueda, R., & Rodriguez-Mañas, L. (2016) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2016.04.019 · Cited by 581 · see citing works
Pharmacology of Schisandra chinensis Bail.: An overview of Russian research and uses in medicine
Panossian, A. G., & Wikman, G. (2008) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2008.04.020 · Cited by 527 · see citing works
Niche Regulation of Muscle Satellite Cell Self-Renewal and Differentiation
Kuang, S., Gillespie, M. A., & Rudnicki, M. A. (2008) · Cell Stem Cell · doi:10.1016/j.stem.2007.12.012 · Cited by 507 · see citing works
Satellite-cell pool size does matter: Defining the myogenic potency of aging skeletal muscle
Shefer, G., de Mark, D. P. V., Richardson, J. B., & Yablonka‐Reuveni, Z. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.02.022 · Cited by 506 · see citing works
Exercise Promotes Healthy Aging of Skeletal Muscle
Cartee, G. D., Hepple, R. T., Bamman, M. M., & Zierath, J. R. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.007 · Cited by 483 · see citing works
A phase I/IItrial of MYO‐029 in adult subjects with muscular dystrophy
Wagner, K. R., Fleckenstein, J. L., Amato, A. A., Barohn, R. J., Bushby, K., Escolar, D. M., Flanigan, K. M., Pestronk, A., Tawil, R., Wolfe, G. I., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21338 · Cited by 481 · see citing works
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
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
Phospholipid spherules (liposomes) as a model for biological membranes
Sessa, G., & Weissmann, G. (1968) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)43097-4 · Cited by 446 · see citing works
Regulation of muscle mass by growth hormone and IGF‐I
Velloso, C. P. (2008) · British Journal of Pharmacology · doi:10.1038/bjp.2008.153 · Cited by 444 · cited 1× · see citing works
“As a result of stimulation of insulin-like growth factor-1 (IGF-1) production via the liver JAKSTAT pathway, GH stimulates muscle fiber hypertrophy by enhancing the synthesis of proteins associated with MSC proliferation (Velloso, 2008).”
BackgroundHill, 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
Vieira, D., & Gamarra, L. (2016) · International Journal of Nanomedicine · doi:10.2147/ijn.s117210 · Cited by 427 · see citing works
Computer Aided Drug Design: Success and Limitations
Baig, M. H., Ahmad, K., Roy, S., Ashraf, J. M., Adil, M., Siddiqui, M. H., Khan, S. A., Kamal, M. A., Provazník, I., & Choi, I. (2016) · Current Pharmaceutical Design · doi:10.2174/1381612822666151125000550 · Cited by 426 · see citing works
Self-citationLack 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
Elabd, C., Cousin, W., Upadhyayula, P., Chen, R. Y., Chooljian, M. S., Li, J., Kung, S., Jiang, K. P., & Conboy, I. M. (2014) · Nature Communications · doi:10.1038/ncomms5082 · Cited by 411 · see citing works
Prevalence, incidence and clinical impact of cachexia: facts and numbers—update 2014
von Haehling, S., & Anker, S. D. (2014) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-014-0164-8 · Cited by 394 · see citing works
Myostatin antibody (LY2495655) in older weak fallers: a proof-of-concept, randomised, phase 2 trial
Becker, C., Lord, S. R., Studenski, S. A., Warden, S. J., Fielding, R. A., Recknor, C. P., Hochberg, M., Ferrari, S., Blain, H., Binder, E. F., et al. (2015) · The Lancet Diabetes & Endocrinology · doi:10.1016/s2213-8587(15)00298-3 · Cited by 381 · see citing works
Determinants of Muscle and Bone Aging
Curtis, E., Litwic, A., Cooper, C., & Dennison, E. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.25001 · Cited by 375 · see citing works
Molecular and cellular mechanisms of skeletal muscle atrophy: an update
Fanzani, A., Conraads, V. M., Penna, F., & Martinet, W. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-012-0074-6 · Cited by 372 · see citing works
Sulforaphane inhibits histone deacetylase in vivo and suppresses tumorigenesis in Apc min mice
Myzak, M. C., Dashwood, W. M., Orner, G. A., Ho, E., & Dashwood, R. H. (2006) · The FASEB Journal · doi:10.1096/fj.05-4785fje · Cited by 344 · 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
The Homeostatic Force of Ghrelin
Yanagi, S., Sato, T., Kangawa, K., & Nakazato, M. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.02.008 · Cited by 324 · see citing works
Motor cortex disinhibition of the unaffected hemisphere after acute stroke
Liepert, J., Hamzei, F., & Weiller, C. (2000) · Muscle & Nerve · doi:10.1002/1097-4598(200011)23:11 · Cited by 294 · see citing works
Yarasheski, K. E., Bhasin, S., Sinha‐Hikim, I., Pak-Loduca, J., & González-Cadavid, N. F. (2002) · PubMed · Cited by 293 · see citing works
Extracellular matrix: an important regulator of cell functions and skeletal muscle development
Zhang, W., Liu, Y., & Zhang, H. (2021) · Cell & Bioscience · doi:10.1186/s13578-021-00579-4 · Cited by 289 · see citing works
Catechins: Sources, extraction and encapsulation: A review
Gadkari, P. V., & Balaraman, M. (2013) · Food and Bioproducts Processing · doi:10.1016/j.fbp.2013.12.004 · Cited by 282 · see citing works
Regulation of Muscle Mass by Follistatin and Activins
Lee, S.-J., Lee, Y.-S., Zimmers, T. A., Soleimani, A., Matzuk, M. M., Tsuchida, K., Cohn, R. D., & Barton, E. R. (2010) · Molecular Endocrinology · doi:10.1210/me.2010-0127 · 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
The Light and Dark Sides of Virtual Screening: What Is There to Know?
Gimeno, A., Ojeda, M. J., Tomas‐Hernández, S., Cereto‐Massagué, A., Beltrán‐Debón, R., Mulero, M., Pujadas, G., & Garcı́a-Vallvé, S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20061375 · Cited by 270 · see citing works
Tries, R. S., Chen, T., Vies, M. V. D., Tomkinson, K. N., Pearson, A. A., Shakey, Q., & Wolfman, N. M. (2001) · Growth Factors · doi:10.3109/08977190109029114 · Cited by 265 · see citing works
Allen, D. L., & Unterman, T. G. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00542.2005 · Cited by 264 · see citing works
Ji, S., Li, Z., Song, W., Wang, Y., Liang, W., Li, K., Tang, S., Wang, Q., Qiao, X., Zhou, D., et al. (2016) · Journal of Natural Products · doi:10.1021/acs.jnatprod.5b00877 · Cited by 242 · see citing works
Campbell, C., McMillan, H. J., Mah, J. K., Tarnopolsky, M. A., Selby, K. A., McClure, T., Wilson, D. M., Sherman, M. L., Escolar, D. M., & Attie, K. M. (2016) · Muscle & Nerve · doi:10.1002/mus.25268 · Cited by 240 · see citing works
Myostatin Inhibits IGF-I-Induced Myotube Hypertrophy through Akt
Morissette, M. R., Cook, S. A., Buranasombati, C., Rosenberg, M. A., & Rosenzweig, A. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00043.2009 · Cited by 231 · see citing works
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
Quinn, L. S., Anderson, B. G., Drivdahl, R. H., Alvarez, B., & Argilés, J. M. (2002) · Experimental Cell Research · doi:10.1006/excr.2002.5624 · Cited by 226 · see citing works
Hill, J. J., Qiu, Y., Hewick, R. M., & Wolfman, N. M. (2003) · Molecular Endocrinology · doi:10.1210/me.2002-0366 · Cited by 225 · see citing works
Winbanks, C. E., Weeks, K. L., Thomson, R. E., Sepulveda, P. V., Beyer, C., Qian, H., Chen, J. L., Allen, J. M., Lancaster, G. I., Febbraio, M. A., et al. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201109091 · Cited by 218 · see citing works
Prerigor and postrigor changes in tenderness of ovine longissimus muscle2
WHEELER, T. L., & Koohmaraie, M. (1994) · Journal of Animal Science · doi:10.2527/1994.7251232x · Cited by 215 · see citing works
Role of Activin A and Myostatin in Human Cancer Cachexia
Loumaye, A., de Barsy, M., Nachit, M., Lause, P., Frateur, L., Maanen, A. G. V., Tréfois, P., Gruson, D., & Thissen, J. (2015) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2014-4318 · Cited by 212 · see citing works
Cancer-induced muscle wasting: latest findings in prevention and treatment
Aversa, Z., Costelli, P., & Muscaritoli, M. (2017) · Therapeutic Advances in Medical Oncology · doi:10.1177/1758834017698643 · Cited by 212 · see citing works
Cancer cachexia: Diagnosis, assessment, and treatment
Sadeghi, M. A., Keshavarz‐Fathi, M., Baracos, V. E., Arends, J., Mahmoudi, M., & Rezaei, N. (2018) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2018.05.006 · Cited by 212 · see citing works
Expression and function of myostatin in obesity, diabetes, and exercise adaptation
ALLEN, D. L., HITTEL, D. S., & MCPHERRON, A. C. (2011) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3182178bb4 · Cited by 207 · see citing works
Joulia-Ekaza, D., & Cabello, G. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.04.012 · Cited by 207 · see citing works
Collins, C. A., & Morgan, J. E. (2003) · International Journal of Experimental Pathology · doi:10.1046/j.1365-2613.2003.00354.x · Cited by 202 · see citing works
Chen, J., Splenser, A. E., Guillory, B., Luo, J., Mendiratta, M., Belinova, B., Halder, T., Zhang, G., Li, Y., & Garcia, J. M. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12023 · Cited by 201 · see citing works
QUINN, L., STRAITBODEY, L., ANDERSON, B., ARGILES, J., & HAVEL, P. (2005) · Cell Biology International · doi:10.1016/j.cellbi.2005.02.005 · Cited by 199 · see citing works
Investigating Protein–Peptide Interactions Using the Schrödinger Computational Suite
Bhachoo, J., & Beuming, T. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6798-8_14 · Cited by 195 · cited 1× · see citing works
“For VS, licensed software such as Molecular Operating Environment (MOE) (Vilar et al., 2008), and the GLIDE module in Schrodinger (Bhachoo and Beuming, 2017) as well as open access tools such as Autodock Vina (Trott and Olson, 2010), are commonly used.”
MethodExtracellular matrix regulation in the muscle satellite cell niche
Thomas, K. A., Engler, A. J., & Meyer, G. A. (2014) · Connective Tissue Research · doi:10.3109/03008207.2014.947369 · Cited by 194 · see citing works
Myostatin and Sarcopenia: Opportunities and Challenges - A Mini-Review
White, T. A., & LeBrasseur, N. K. (2014) · Gerontology · doi:10.1159/000356740 · Cited by 191 · see citing works
Qian, L., Tang, M., Yang, J., Wang, Q., Cai, C., Jiang, S., Li, H., Jiang, K., Gao, P., Ma, D., et al. (2015) · Scientific Reports · doi:10.1038/srep14435 · Cited by 190 · see citing works
Activin A more prominently regulates muscle mass in primates than does GDF8
Latres, E., Mastaitis, J., Fury, W., Miloscio, L., Trejos, J., Pangilinan, J., Okamoto, H., Cavino, K., Na, E., Papatheodorou, A., et al. (2017) · Nature Communications · doi:10.1038/ncomms15153 · Cited by 185 · see citing works
Camporez, J.-P. G., Petersen, M. C., Abudukadier, A., Moreira, G. V., Jurczak, M. J., Friedman, G., Haqq, C. M., Petersen, K. F., & Shulman, G. I. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1525795113 · Cited by 184 · see citing works
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
The central role of myostatin in skeletal muscle and whole body homeostasis
Elliott, B., Renshaw, D. W., Getting, S. J., & Mackenzie, R. (2012) · Acta Physiologica · doi:10.1111/j.1748-1716.2012.02423.x · Cited by 183 · see citing works
Interleukin-15 antagonizes muscle protein waste in tumour-bearing rats
Carbó, N., López‐Soriano, J., Costelli, P., Busquets, S., Alvarez, B., Baccino, F. M., Quinn, L. S., López-Soriano, F. J., & Argilés, J. M. A. (2000) · British Journal of Cancer · doi:10.1054/bjoc.2000.1299 · Cited by 181 · 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
Expression of myostatin pro domain results in muscular transgenic mice
Yang, J., Ratovitski, T., Brady, J. P., Solomon, M. B., Wells, K. D., & Wall, R. J. (2001) · Molecular Reproduction and Development · doi:10.1002/mrd.1097 · Cited by 177 · see citing works
Skeletal muscle atrophy: Potential therapeutic agents and their mechanisms of action
Dutt, V., Gupta, S. K., Dabur, R., Injeti, E. R., & Mittal, A. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.05.010 · Cited by 174 · see citing works
The role of TGF‐β1 during skeletal muscle regeneration
Delaney, K., Kasprzycka, P., Ciemerych, M. A., & Zimowska, M. (2016) · Cell Biology International · doi:10.1002/cbin.10725 · Cited by 168 · see citing works
The extracellular matrix dimension of skeletal muscle development
Thorsteinsdóttir, S., Deries, M., Cachaço, A. S., & Bajanca, F. (2011) · Developmental Biology · doi:10.1016/j.ydbio.2011.03.015 · Cited by 167 · see citing works
Myostatin signals through Pax7 to regulate satellite cell self-renewal
McFarlane, C., Hennebry, A., Thomas, M., Plummer, E., Ling, N., Sharma, M., & Kambadur, R. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.09.012 · Cited by 165 · see citing works
Myostatin is associated with age‐related human muscle stem cell dysfunction
McKay, B. R., Ogborn, D. I., Bellamy, L. M., Tarnopolsky, M. A., & Parise, G. (2012) · The FASEB Journal · doi:10.1096/fj.11-198663 · Cited by 164 · see citing works
Laminin-211 in skeletal muscle function
Holmberg, J., & Durbeej, M. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.22618 · Cited by 161 · see citing works
Myostatin as a Biomarker of Muscle Wasting and other Pathologies-State of the Art and Knowledge Gaps
Bączek, J., Silkiewicz, M., & Wojszel, Z. B. (2020) · Nutrients · doi:10.3390/nu12082401 · Cited by 159 · see citing works
Regulation of Myostatin on the Growth and Development of Skeletal Muscle
Chen, M., Zhao, Y.-P., Zhao, Y., Deng, S., & Yu, K. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.785712 · Cited by 158 · see citing works
Wilkes, J. J., Lloyd, D. J., & Gekakis, N. (2009) · Diabetes · doi:10.2337/db08-0245 · Cited by 156 · see citing works
LIF is a contraction-induced myokine stimulating human myocyte proliferation
Broholm, C., Laye, M. J., Brandt, C., Vadalasetty, R., Pilegaard, H., Pedersen, B. K., & Scheele, C. C. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01399.2010 · Cited by 155 · see citing works
Regulation of GDF-8 signaling by the p38 MAPK
Philip, B., Lu, Z., & Gao, Y. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2004.08.003 · Cited by 153 · see citing works
Myogenin is an essential regulator of adult myofibre growth and muscle stem cell homeostasis
Ganassi, M., Badodi, S., Wanders, K., Zammit, P. S., & Hughes, S. M. (2020) · eLife · doi:10.7554/elife.60445 · Cited by 152 · see citing works
Myostatin: A novel insight into its role in metabolism, signal pathways, and expression regulation
Huang, Z., Chen, X., & Chen, D. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.05.003 · Cited by 149 · see citing works
Yang, W. Z., Chen, Y., Zhang, Y., Wang, X., Yang, N., & Zhu, D. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3060 · Cited by 144 · see citing works
Latres, E., Pangilinan, J., Miloscio, L., Bauerlein, R., Na, E., Potocky, T. B., Huang, Y., Eckersdorff, M., Rafique, A., Mastaitis, J., et al. (2015) · Skeletal Muscle · doi:10.1186/s13395-015-0060-8 · Cited by 143 · see citing works
Hot spot-based design of small-molecule inhibitors for protein–protein interactions
Guo, W., Wisniewski, J. A., & Ji, H. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.03.095 · Cited by 142 · see citing works
Smad3 Induces Atrogin-1, Inhibits mTOR and Protein Synthesis, and Promotes Muscle Atrophy In Vivo
Goodman, C. A., McNally, R. M., Hoffmann, F. M., & Hornberger, T. A. (2013) · Molecular Endocrinology · doi:10.1210/me.2013-1194 · Cited by 141 · see citing works
Busquets, S., Toledo, M., Orpí, M., Massa, D., Porta, M. M., Capdevila, E., Padilla, N., Frailis, V., López-Soriano, F. J., Han, H. Q., et al. (2011) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0049-z · Cited by 141 · see citing works
Sarcopenia and cachexia: the adaptations of negative regulators of skeletal muscle mass
Sakuma, K., & Yamaguchi, A. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0052-4 · Cited by 137 · see citing works
Bergen, H. R., Farr, J. N., Vanderboom, P. M., Atkinson, E. J., White, T. A., Singh, R. J., Khosla, S., & LeBrasseur, N. K. (2015) · Skeletal Muscle · doi:10.1186/s13395-015-0047-5 · Cited by 137 · see citing works
Protein breakdown in cancer cachexia
Sandri, M. (2016) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2015.11.002 · Cited by 134 · cited 1× · see citing works
“In preclinical investigations of cancer cachexia, excessive proteolysis, particularly via autophagy and the ubiquitinproteasome system, and low protein synthesis in SM have been documented (Sandri, 2016).”
BackgroundKishioka, 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
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
Williams, A. J., Ekins, S., & Tkachenko, V. (2012) · Drug Discovery Today · doi:10.1016/j.drudis.2012.02.013 · Cited by 126 · see citing works
Cell Cycle–regulated Expression of the Muscle Determination Factor Myf5 in Proliferating Myoblasts
Lindon, C., Montarras, D., & Pinset, C. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.1.111 · Cited by 122 · see citing works
Myostatin Gene Inactivation Prevents Skeletal Muscle Wasting in Cancer
Gallot, Y. S., Durieux, A., Castells, J., Desgeorges, M. M., Vernus, B., Plantureux, L., Rémond, D., Jahnke, V. E., Lefai, É., Dardevet, D. P., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0057 · Cited by 117 · see citing works
Consitt, L. A., & Clark, B. C. (2018) · The Journal of Frailty & Aging · doi:10.14283/jfa.2017.33 · Cited by 115 · see citing works
Effects of (−)-epicatechin on molecular modulators of skeletal muscle growth and differentiation
Gutiérrez-Salmeán, G., Ciaraldi, T. P., Nogueira, L., Barboza, J., Taub, P. R., Hogan, M. C., Henry, R. R., Meaney, E., Villarreal, F. J., Ceballos, G. M., et al. (2013) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2013.09.007 · Cited by 113 · see citing works
Sulforaphane prevents age‐associated cardiac and muscular dysfunction through Nrf2 signaling
Bose, C., Alves, I., Singh, P., Palade, P., Carvalho, E., Børsheim, E., Jun, S., Cheema, A. K., Boerma, M., Awasthi, S., et al. (2020) · Aging Cell · doi:10.1111/acel.13261 · Cited by 111 · see citing works
Hoene, M., Runge, H., Häring, H. U., Schleicher, E. D., & Weigert, C. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00025.2012 · Cited by 110 · see citing works
Physiological roles for butyrylcholinesterase: A BChE-ghrelin axis
Brimijoin, S., Chen, V. P., Pang, Y., Geng, L., & Gao, Y. (2016) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2016.02.013 · Cited by 110 · see citing works
LY2495655, an antimyostatin antibody, in pancreatic cancer: a randomized, phase 2 trial
Golan, T., Geva, R., Richards, D., Madhusudan, S., Lin, B. K., Wang, H. T., Walgren, R. A., & Stemmer, S. M. (2018) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12331 · Cited by 109 · see citing works
The Human Experience With Ghrelin Administration
Garin, M. C., Burns, C. M., Kaul, S., & Cappola, A. R. (2013) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2012-4247 · Cited by 107 · see citing works
Use of Peptides for the Management of Alzheimer’s Disease: Diagnosis and Inhibition
Baig, M. H., Ahmad, K., Rabbani, G., & Choi, I. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00021 · Cited by 107 · see citing works
Self-citationRatkevičius, A., Joyson, A., Selmer, I.-S., Dhanani, T., Grierson, C., Tommasi, A. M., DeVries, A., Rauchhaus, P., Crowther, D. J., Alesci, S., et al. (2011) · The Journals of Gerontology Series A · doi:10.1093/gerona/glr025 · Cited by 104 · 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
Myostatin in the Pathophysiology of Skeletal Muscle
Bonnieu, A., Carnac, G., & Vernus, B. (2007) · Current Genomics · doi:10.2174/138920207783591672 · Cited by 103 · see citing works
Quinn, L. S., Anderson, B. G., Conner, J. D., & Wolden-Hanson, T. (2013) · Endocrinology · doi:10.1210/en.2012-1773 · Cited by 102 · see citing works
Andre, M. S., Johnson, M. C., Bansal, P. N., Wellen, J. W., Robertson, A. W., Opsahl, A., Burch, P. M., Bialek, P., Morris, C. A., & Owens, J. M. (2017) · Skeletal Muscle · doi:10.1186/s13395-017-0141-y · Cited by 101 · see citing works
Regulation of GDF-11 and myostatin activity by GASP-1 and GASP-2
Lee, Y., & Lee, S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1309907110 · Cited by 99 · cited 1× · see citing works
“Growth and Differentiation Factor-Associated Serum Protein Growth and differentiation factor-associated serum protein-1 and -2 (GASP-1 and GASP-2) also importantly regulate the biological activity of MSTN (Lee and Lee, 2013).”
BackgroundLeukaemia inhibitory factor - an exercise-induced myokine
Broholm, C., & Pedersen, B. K. (2026) · PubMed · doi:10.22029/eir.2010.1652 · Cited by 97 · see citing works
Alshehri, B., D’Souza, D. G., Lee, J. Y., Petratos, S., & Richardson, S. J. (2015) · Journal of Neuroendocrinology · doi:10.1111/jne.12271 · Cited by 94 · see citing works
Peng, L., Lee, W., Liu, L., Lin, M., & Chen, L. (2018) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12302 · Cited by 93 · see citing works
Serum Myostatin is Upregulated in Obesity and Correlates with Insulin Resistance in Humans
Amor, M., Itariu, B. K., Moreno-Viedma, V., Keindl, M., Jürets, A., Prager, G., Langer, F., Grablowitz, V., Zeyda, M., & Stulnig, T. M. (2019) · Experimental and Clinical Endocrinology & Diabetes · doi:10.1055/a-0641-5546 · Cited by 93 · see citing works
Ghrelin and cardiovascular diseases
Kishimoto, I., Tokudome, T., Hosoda, H., Miyazato, M., & Kangawa, K. (2011) · Journal of Cardiology · doi:10.1016/j.jjcc.2011.11.002 · Cited by 89 · see citing works
da Costa, K. S., do Nascimento, L. D., Lima, A. H., Damasceno, V., Nahum, C., Braga, R. C., & Lameira, J. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.662688 · Cited by 88 · 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
Mafi, F., Biglari, S., Afousi, A. G., & Gaeini, A. A. (2018) · Journal of Aging and Physical Activity · doi:10.1123/japa.2017-0389 · Cited by 87 · see citing works
Structure of Myostatin·Follistatin-like 3
Cash, J. N., Angerman, E. B., Kattamuri, C., Nolan, K., Zhao, H., Sidis, Y., Keutmann, H. T., & Thompson, T. B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.270801 · Cited by 86 · see citing works
Myostatin Inhibitors: Panacea or Predicament for Musculoskeletal Disorders?
Suh, J., & Lee, Y. (2020) · Journal of Bone Metabolism · doi:10.11005/jbm.2020.27.3.151 · Cited by 86 · 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
Lee, E. J., Jan, A. T., Baig, M. H., Ashraf, J. M., Nahm, S., Kim, Y., Park, S., & Choi, I. (2016) · The FASEB Journal · doi:10.1096/fj.201500133r · Cited by 83 · see citing works
Self-citationHatakeyama, S., Summermatter, S., Jourdain, M., Melly, S., Minetti, G., & Lach‐Trifilieff, E. (2016) · Skeletal Muscle · doi:10.1186/s13395-016-0098-2 · Cited by 82 · see citing works
Sequential association of myogenic regulatory factors and E proteins at muscle-specific genes
Londhe, P., & Davie, J. K. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-14 · Cited by 79 · see citing works
The administration of Fructus Schisandrae attenuates dexamethasone-induced muscle atrophy in mice
Kim, J. W., Ku, S., Han, M. H., Kim, K. Y., Kim, S. G., Kim, G., Hwang, H. J., Kim, B. W., Kim, C. M., & Choi, Y. H. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2200 · Cited by 77 · see citing works
Yu, R., Chen, J., Xu, J., Cao, J., Wang, Y., Thomas, S. S., & Hu, Z. (2016) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12162 · Cited by 73 · see citing works
Induction of Acute Skeletal Muscle Regeneration by Cardiotoxin Injection
Guardiola, O., Andolfi, G., Tirone, M., Iavarone, F., Brunelli, S., & Minchiotti, G. (2017) · Journal of Visualized Experiments · doi:10.3791/54515 · Cited by 73 · see citing works
Structure of the human myostatin precursor and determinants of growth factor latency
Cotton, T. R., Fischer, G., Wang, X., McCoy, J. C., Czepnik, M., Thompson, T. B., & Hyvönen, M. (2018) · The EMBO Journal · doi:10.15252/embj.201797883 · Cited by 71 · see citing works
Liu, M., Qin, J., Hao, Y., Liu, M., Luo, J., Luo, T., & Wei, L. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/782497 · Cited by 70 · see citing works
Baig, M. H., Jan, A. T., Rabbani, G., Ahmad, K., Ashraf, J. M., Kim, T., Min, H., Lee, Y., Cho, W., Yeul, J., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-06067-5 · Cited by 70 · see citing works
Self-citationBonetto, 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
Sulforaphane causes a major epigenetic repression of myostatin in porcine satellite cells
Fan, H., Zhang, R., Tesfaye, D., Tholen, E., Looft, C., Hoelker, M., Schellander, K., & Çınar, M. U. (2012) · Epigenetics · doi:10.4161/epi.22609 · Cited by 66 · see citing works
Multifaceted Interweaving Between Extracellular Matrix, Insulin Resistance, and Skeletal Muscle
Ahmad, K., Lee, E. J., Moon, J. S., Park, S., & Choi, I. (2018) · Cells · doi:10.3390/cells7100148 · Cited by 65 · see citing works
Self-citationLocally acting ACE‐083 increases muscle volume in healthy volunteers
Glasser, C. E., Gartner, M. R., Wilson, D. M., Miller, B., Sherman, M. L., & Attie, K. M. (2018) · Muscle & Nerve · doi:10.1002/mus.26113 · Cited by 63 · see citing works
Villoutreix, B. O., Bastard, K., Spérandio, O., Fåhræus, R., Poyet, J., Calvo, F. M., Deprez, B. P., & Miteva, M. A. (2008) · Current Pharmaceutical Biotechnology · doi:10.2174/138920108783955218 · Cited by 62 · see citing works
Myokines as possible therapeutic targets in cancer cachexia
Manole, E., Ceafalan, L. C., Popescu, B. O., Dumitru, C., & Bastian, A. E. (2018) · Journal of Immunology Research · doi:10.1155/2018/8260742 · Cited by 60 · see citing works
Cross-Talk Between Extracellular Matrix and Skeletal Muscle: Implications for Myopathies
Ahmad, K., Shaikh, S., Ahmad, S. S., Lee, E. J., & Choi, I. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00142 · Cited by 60 · see citing works
Self-citationLiu, X., Bauman, W. A., & Cardozo, C. P. (2018) · Physiological Reports · doi:10.14814/phy2.13837 · Cited by 59 · see citing works
Salade, L., Wauthoz, N., Deleu, M., Vermeersch, M., Vriese, C. D., Amighi, K., & Goole, J. (2017) · International Journal of Nanomedicine · doi:10.2147/ijn.s147650 · Cited by 56 · see citing works
Dermatopontin in Skeletal Muscle Extracellular Matrix Regulates Myogenesis
Kim, T., Ahmad, K., Shaikh, S., Jan, A. T., Seo, M.-G., Lee, E. J., & Choi, I. (2019) · Cells · doi:10.3390/cells8040332 · Cited by 56 · see citing works
Self-citationRegeneration of Skeletal Muscle After Eccentric Injury
Dueweke, J. J., Awan, T. M., & Mendias, C. L. (2016) · Journal of Sport Rehabilitation · doi:10.1123/jsr.2016-0107 · Cited by 55 · see citing works
STAT3 induces muscle stem cell differentiation by interaction with myoD
Yang, Y., Xu, Y., Li, W., Wang, G., Song, Y., Yang, G., Han, X., Du, Z., Sun, L., & Ma, K. (2009) · Cytokine · doi:10.1016/j.cyto.2008.12.015 · Cited by 54 · see citing works
Inhibition of the myostatin/Smad signaling pathway by short decorin-derived peptides
Shafey, N. E., Guesnon, M., Simon, F., Deprez, E., Cosette, J., Stockholm, D., Scherman, D., Bigey, P., & Kichler, A. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.01.019 · Cited by 54 · see citing works
Loop diuretics affect skeletal myoblast differentiation and exercise-induced muscle hypertrophy
Mandai, S., Furukawa, S., Kodaka, M., Hata, Y., Mori, T., Nomura, N., Ando, F., Mori, Y., Takahashi, D., Yoshizaki, Y., et al. (2017) · Scientific Reports · doi:10.1038/srep46369 · Cited by 53 · see citing works
Lee, E. J., Jan, A. T., Baig, M. H., Ahmad, K., Malik, A., Rabbani, G., Kim, T., Lee, I., Lee, Y., Park, S., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700665r · Cited by 53 · see citing works
Self-citationAhmad, S., Jan, A. T., Baig, M. H., Lee, E. J., & Choi, I. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.12.011 · Cited by 50 · see citing works
Self-citationAhmad, K., Choi, I., & Lee, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113845 · Cited by 49 · see citing works
Self-citationBianchi, A., Mozzetta, C., Pegoli, G., Lucini, F., Valsoni, S., Rosti, V., Petrini, C., Cortesi, A., Gregoretti, F., Antonelli, L., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci128161 · Cited by 47 · see citing works
The histone deacetylase SIRT6 blocks myostatin expression and development of muscle atrophy
Samant, S. A., Kanwal, A., Pillai, V. B., Bao, R., & Gupta, M. P. (2017) · Scientific Reports · doi:10.1038/s41598-017-10838-5 · Cited by 46 · see citing works
Pashirova, T. N., Sapunova, А. S., Lukashenko, S. S., Burilova, E. A., Lubina, A. P., Shaihutdinova, Z. M., Gerasimova, T. P., Коваленко, В. И., Voloshina, A. D., Souto, E. B., et al. (2019) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2019.118953 · Cited by 46 · see citing works
Similar sequences but dissimilar biological functions of GDF11 and myostatin
Suh, J., & Lee, Y. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-00516-4 · Cited by 46 · see citing works
Lee, E. J., Shaikh, S., Ahmad, K., Ahmad, S., Lim, J., Park, S., Yang, H., Cho, W.-K., Park, S.-J., Lee, Y.-H., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020876 · Cited by 46 · see citing works
Self-citationDeBoer, M. D. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.02.012 · Cited by 44 · cited 1× · see citing works
“Ghrelin is largely produced in gastric oxyntic mucosa (DeBoer, 2011), and ghrelin treatment reduces proinflammatory cytokine release in cachexia patients (Kishimoto et al., 2012).”
BackgroundLee, 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
Self-citationIntracellular and extracellular control of activin function by novel regulatory molecules
Tsuchida, K., Matsuzaki, T., Yamakawa, N., Liu, Z. H., & Sugino, H. (2001) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(01)00522-6 · Cited by 42 · see citing works
Tsuchida, K. (2008) · PubMed Central · Cited by 42 · see citing works
Nishimura, T., FUTAMI, E., TANEICHI, A., Mori, T., & Hattori, A. (2002) · Cells Tissues Organs · doi:10.1159/000063713 · Cited by 41 · see citing works
Computational methods-guided design of modulators targeting protein-protein interactions (PPIs)
Qiu, Y., Li, X., He, X., Pu, J., Zhang, J., & Lu, S. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112764 · Cited by 41 · see citing works
Quinn, L. S., Anderson, B. G., Conner, J. D., Wolden-Hanson, T., & Marcell, T. J. (2014) · Endocrinology · doi:10.1210/en.2013-1645 · Cited by 40 · see citing works
Gastric cancer does not affect the expression of atrophy-related genes in human skeletal muscle
D’Orlando, C., Marzetti, E., François, S., Lorenzi, M., Conti, V., Stasio, E. D., Rosa, F., Brunelli, S., Doglietto, G. B., Pacelli, F., et al. (2013) · Muscle & Nerve · doi:10.1002/mus.23945 · Cited by 38 · 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
Ubiquitous Gasp1 overexpression in mice leads mainly to a hypermuscular phenotype
Monestier, O., Brun, C. E., Heu, K., Passet, B., Malhouroux, M. M., Magnol, L., Vilotte, J., & Blanquet, V. (2012) · BMC Genomics · doi:10.1186/1471-2164-13-541 · Cited by 32 · see citing works
Fu, J., Huang, L., Zhang, H., Yang, S., & Chen, S. (2013) · Journal of Asian Natural Products Research · doi:10.1080/10286020.2013.778832 · Cited by 30 · see citing works
Sarcopenia and Predictors of Skeletal Muscle Mass in Elderly Men With and Without Obesity
Stoever, K., Heber, A., Eichberg, S., & Brixius, K. (2017) · Gerontology and Geriatric Medicine · doi:10.1177/2333721417713637 · Cited by 28 · see citing works
Tauer, J. T., & Rauch, F. (2019) · Bone · doi:10.1016/j.bone.2019.115036 · Cited by 28 · see citing works
Takayama, K., Rentier, C., Asari, T., Nakamura, A., Saga, Y., Shimada, T., Nirasawa, K., Sasaki, E., Muguruma, K., Taguchi, A., et al. (2017) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.7b00168 · Cited by 24 · see citing works
Howick, K., Alam, R. M., Chruścicka, B., Kandil, D., Fitzpatrick, D., Ryan, A. M., Cryan, J. F., Schellekens, H., & Griffin, B. T. (2017) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2017.11.051 · Cited by 23 · see citing works
Hulmi, J. J., Nissinen, T. A., Penna, F., & Bonetto, A. (2021) · Cells · doi:10.3390/cells10030516 · Cited by 23 · see citing works
Lee, E. J., Shaikh, S., Choi, D., Ahmad, K., Baig, M. H., Lim, J. H., Lee, Y., Park, S. J., Kim, Y., Park, S., et al. (2019) · Cells · doi:10.3390/cells8121565 · Cited by 21 · see citing works
Self-citationNanomolar Protein–Protein Interaction Monitoring with a Label-Free Protein-Probe Technique
Valtonen, S., Vuorinen, E., Kariniemi, T., Eskonen, V., Quesne, J. P. C. L., Bushell, M., Härmä, H., & Kopra, K. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c02823 · Cited by 20 · see citing works
Meeting the meat: delineating the molecular machinery of muscle development
Jan, A. T., Lee, E. J., Ahmad, S., & Choi, I. (2016) · Journal of Animal Science and Technology · doi:10.1186/s40781-016-0100-x · Cited by 19 · see citing works
Self-citationOzawa, 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 19 · see citing works
Liu, Y., Lehar, A., Rydzik, R., Chandok, H., Lee, Y., Youngstrom, D. W., George, J., Matzuk, M. M., Germain‐Lee, E. L., & Lee, S. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2111401118 · Cited by 19 · see citing works
Lee, E. J., Kamli, M. R., Pokharel, S., Malik, A., Tareq, K. M. A., Bhat, A. R., Park, H.-B., Lee, Y. S., Kim, S. H., Yang, B., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079780 · Cited by 15 · cited 1× · see citing works
“Growth and Differentiation Factor-Associated Serum Protein Growth and differentiation factor-associated serum protein-1 and -2 (GASP-1 and GASP-2) also importantly regulate the biological activity of MSTN (Lee and Lee, 2013).”
BackgroundSelf-citationHedayati, M., Nozhat, Z., & Hannani, M. (2016) · Asian Pacific Journal of Cancer Prevention · doi:10.7314/apjcp.2016.17.s3.119 · Cited by 13 · see citing works
Lee, S.-J. (2012) · Muscle · doi:10.1016/b978-0-12-381510-1.00079-x · Cited by 8 · cited 1× · see citing works
“In adults, MSTN is secreted by SM, circulates in the blood, and inhibits muscle fiber growth (Lee, 2012).”
BackgroundOzawa, T., Miyazono, K., & Morikawa, M. (2021) · STAR Protocols · doi:10.1016/j.xpro.2021.100839 · Cited by 4 · see citing works
Flagged first, then by citations
1 of the 184 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Liu, D., Wang, S., Liu, S., Wang, Q., Che, X., & Wu, G. (2024) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2024.101270 · Cited by 134 · see citing works
Espino-González, E., Dalbram, E., Mounier, R., Gondin, J., Farup, J., Jessen, N., & Treebak, J. T. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2024.02.014 · Cited by 132 · see citing works
Sarcopenia and Diabetes: A Detrimental Liaison of Advancing Age
Lisco, G., Disoteo, O., Tullio, A. D., Geronimo, V. D., Giagulli, V. A., Monzani, F., Jirillo, E., Cozzi, R. C., Guastamacchia, E., Pergola, G. D., et al. (2023) · Nutrients · doi:10.3390/nu16010063 · Cited by 109 · see citing works
“Suppressing the adenosine monophosphate-activate protein kinase (AMPK)–mammalian target of rapamycin (mTOR) pathway by the TGF-β -small mother against decapentaplegic (Smad) signaling results in impaired muscle synthesis and muscle atrophy [66,67].”
BackgroundDowling, P., Gargan, S., Swandulla, D., & Ohlendieck, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032415 · Cited by 95 · see citing works
Ahmad, S. S., Chun, H. J., Ahmad, K., Shaikh, S., Lim, J. H., Ali, S. M., Han, S. S., Hur, S. J., Sohn, J., Lee, E. J., et al. (2022) · Journal of Animal Science and Technology · doi:10.5187/jast.2022.e114 · Cited by 78 · see citing works
“The negative effect of myostatin (MSTN) was found to be compensated by the positive effect of IGF-1 during myogenesis [85].”
BackgroundInfluentialSelf-citationPathogenesis, Intervention, and Current Status of Drug Development for Sarcopenia: A Review
Jang, J. Y., Kim, D.-H., & Kim, N. D. (2023) · Biomedicines · doi:10.3390/biomedicines11061635 · Cited by 60 · see citing works
Sarcopenia and Cardiogeriatrics: The Links Between Skeletal Muscle Decline and Cardiovascular Aging
Anagnostou, D., Theodorakis, N., Hitas, C., Kreouzi, M., Pantos, I., Vamvakou, G. D., & Nikolaou, M. (2025) · Nutrients · doi:10.3390/nu17020282 · Cited by 51 · see citing works
Livshits, G., & Kalinkovich, A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102267 · Cited by 42 · see citing works
Sarcopenic Obesity: Involvement of Oxidative Stress and Beneficial Role of Antioxidant Flavonoids
Jung, U. J. (2023) · Antioxidants · doi:10.3390/antiox12051063 · Cited by 41 · see citing works
Alzheimer’s Disease: Understanding Motor Impairments
Andrade-Guerrero, J., Martínez-Orozco, H., Villegas-Rojas, M. M., Santiago-Balmaseda, A., Delgado-Minjares, K. M., Pérez‐Segura, I., Baéz-Cortés, M. T., Toro-Colín, M. A. D., Guerra‐Crespo, M., Arias-Carrión, Ó., et al. (2024) · Brain Sciences · doi:10.3390/brainsci14111054 · Cited by 47 · see citing works
Shaikh, S., Ahmad, K., Lim, J. H., Ahmad, S. S., Lee, E. J., & Choi, I. (2024) · Archives of Pharmacal Research · doi:10.1007/s12272-024-01522-0 · Cited by 32 · see citing works
“The focus has been on natural compounds that enhance skeletal muscle growth and recovery, particularly in conditions such as muscle atrophy, age-related muscle decline, and metabolic disorders like diabetes (Baig et al. 2017, 2022; Ali et al. 2023).”
Self-citationRanasinghe, T., Seo, Y., Park, H., Choe, S., & Cha, S. (2024) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2024.136215 · Cited by 28 · see citing works
Kanai, M., Ganbaatar, B., Endo, I., Ohnishi, Y., Teramachi, J., Tenshin, H., Higa, Y., Hiasa, M., Mitsui, Y., Hara, T., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25115715 · Cited by 27 · see citing works
“It has been reported that myostatin inhibits myoblast differentiation and muscle protein synthesis by downreg-Int ulating MyoD1 and myogenin expression [16,17].”
BackgroundLicochalcone A and B enhance muscle proliferation and differentiation by regulating Myostatin
Ahmad, K., Lee, E. J., Ali, S. M., Han, K. S., Hur, S. J., Lim, J. H., & Choi, I. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.155350 · Cited by 26 · see citing works
Self-citationTaldefgrobep Alfa and the Phase 3 RESILIENT Trial in Spinal Muscular Atrophy
Servais, L., Lair, L. L., Connolly, A. M., Byrne, B. J., Chen, K. S., Coric, V., Qureshi, I., Durham, S., Campbell, D. J., Maclaine, G. D. H., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910273 · Cited by 26 · see citing works
Chen, M., Zhao, Y. M., Yu, K., Zhang, X., Zhang, X., Wu, S., Liu, Z., Yuan, Y.-M., Guo, X.-F., Qi, S., et al. (2023) · eLife · doi:10.7554/elife.86827 · Cited by 25 · see citing works
“Due to its role in promoting muscle atrophy and cachexia, MSTN has been recognized as a promising therapeutic target to offset the loss of muscle mass ( Lee, 2021 ; Baig et al., 2022 ; Wijaya et al., 2022 ).”
BackgroundPazokian, F., Amani-Shalamzari, S., & Rajabi, H. (2022) · European Review of Aging and Physical Activity · doi:10.1186/s11556-022-00303-2 · Cited by 22 · see citing works
“and suppresses muscle growth signaling pathways, protein synthesis, satellite cell activation, and negatively regulates myogenic differentiation and myofiber hypertrophy [8, 9].”
BackgroundSaadat, Y. R., Abbasi, A., Hejazian, S. S., Hekmatshoar, Y., Ardalan, M., Farnood, F., & Vahed, S. Z. (2025) · BMC Nephrology · doi:10.1186/s12882-025-04057-8 · Cited by 24 · see citing works
“Various studies have shown that myo-statin loss-of-function mutations in both human and animal studies all lead to significant increases in muscle mass [179].”
Ahmad, K., Shaikh, S., Lim, J. H., Ahmad, S. S., Chun, H. J., Lee, E. J., & Choi, I. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115642 · Cited by 25 · see citing works
Self-citationNguyen, T. T., Dao, T., Nguyen, H. T., Park, J.-H., Jeong, S.-J., Kim, S., Jo, Y., Thieu, N. T. H., Zhao, J., Ding, F., et al. (2026) · Endocrinology and Metabolism · doi:10.3803/enm.2025.2656 · Cited by 23 · see citing works
“Consequently, the myostatin/activin axis represents a major therapeutic target, and multiple strategies to inhibit this pathway have been tested in efforts to combat sarcopenia [66,67].”
Therapeutic Applications of Ginseng Natural Compounds for Health Management
Ahmad, S. S., Ahmad, K., Hwang, Y. C., Lee, E. J., & Choi, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417290 · Cited by 18 · see citing works
“Myostatin is a well-known inhibitor of muscle development [68].”
BackgroundSelf-citationÖZDEMİR, K., & Demir, Y. (2026) · Tissue and Cell · doi:10.1016/j.tice.2026.103406 · Cited by 17 · see citing works
Knapp, M., Supruniuk, E., & Górski, J. (2023) · Biomolecules · doi:10.3390/biom13121777 · Cited by 17 · see citing works
“This leads to the activation of the Smad 2 and 3 transcription factors (the canonical Smad pathway), which inhibits protein synthesis and activates protein degradation [6–8].”
BackgroundMascarella, M. A., Ferdus, J., Vendra, V., Sridharan, S., Sultanem, K., Tsien, C. I., Shenouda, G., Bouganim, N., Esfahani, K., Richardson, K., et al. (2024) · Head & Neck · doi:10.1002/hed.27688 · Cited by 15 · see citing works
“15,30,37 Several animal studies have shown that myostatin inhibition was associated with increased muscle mass and tumor regression.”
BackgroundTimofte, D. V., Tudor, R. C., Mocanu, V., & Labusca, L. S. (2024) · Nutrients · doi:10.3390/nu16234231 · Cited by 15 · see citing works
Potential Vitamin E Signaling Mediators in Skeletal Muscle
Meacci, E., Chirco, A., & Garcia‐Gil, M. (2024) · Antioxidants · doi:10.3390/antiox13111383 · Cited by 15 · 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
“114,115 MIPs MIPs play pivotal roles in controlling MSTN activity and promoting muscle growth.”
Zhong, C., Zeng, X., Yi, X., Yang, Y., Hu, J., Yin, R., & Chen, X. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47030158 · Cited by 11 · see citing works
Agrifoglio, O., Görs, S., Sciascia, Q. L., Li, Z., Albrecht, E., Achilles, S., Statz, M., Bastian, M., Lindner, T., Gauß, K. F., et al. (2025) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13737 · Cited by 10 · see citing works
“…sham-operated animals, mice with BDL had significantly or tended to have higher mRNA levels of genes associated with atrophy and protein degradation [23] (Tripartite Motif Containing 63 ( Trim63 ), Fbox protein32 ( Fbxo32 ), and Ubiquitin B) and the muscle growth inhibitor Myostatin ( Mstn ) [24].”
Wen, J., Ansari, U., Shehabat, M., Ansari, Z., Syed, B., Razick, A. A., Razick, D., Akhtar, M., & Frezza, E. (2025) · Journal of Diabetes · doi:10.1111/1753-0407.70119 · Cited by 10 · see citing works
“Preliminary mice studies with GLP-1 RAs found that muscle biopsy results demonstrated decreased muscle atrophy and inflammation, improved muscle vasculature, and increased preservation of mitochondria [1].”
InfluentialAhmadi-Harchegani, F., Tobin, R. A., Degan, C., Naveed, A., Guglieri, M., Jiménez-Requena, A., de Vries, S. I., Szigyarto, C. A., Spitali, P., Tsonaka, R., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-23758-6 · Cited by 9 · see citing works
Michiue, K., Takayama, K., Taniguchi, A., Hayashi, Y., & Kogure, K. (2023) · Pharmaceuticals · doi:10.3390/ph16030397 · Cited by 9 · see citing works
“33-fold) upon intramuscular injection of MID-35 [20], though it should be noted that the dose of MID-35 for ItP (75 nmol) was higher than that for intramuscular injection (30 nmol).”
BackgroundA perspective on muscle phenotyping in musculoskeletal research
Foessl, I., Ackert‐Bicknell, C. L., Kague, É., Laskou, F., Jakob, F. J., Karasik, D., Obermayer-Pietsch, B. M., Alonso, N., Bjørnerem, Å., Brandi, M. L., et al. (2024) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2024.01.004 · Cited by 8 · see citing works
Potential Biomarkers of Resilience to Microgravity Hazards in Astronauts
Minoretti, P., Fontana, G. A., Lavdas, K., & D’Acquino, D. (2024) · Cureus · doi:10.7759/cureus.57173 · Cited by 8 · see citing works
“Myostatin, a member of the transforming growth factor-β superfamily, is a negative regulator of skeletal muscle mass [15].”
Ambroszkiewicz, J., Gajewska, J., Szamotulska, K., Rowicka, G., Klemarczyk, W., Strucińska, M., & Chełchowska, M. (2024) · Nutrients · doi:10.3390/nu16132009 · Cited by 8 · see citing works
Molecular markers associated with growth, meat, and carcass traits in sheep: a review
Begenova, A., Bissengaliyev, R., Kulmagambetov, T., Nurgulsim, K., Bekenova, A., Otepova, G., & Akhatayeva, Z. (2025) · Animal Biotechnology · doi:10.1080/10495398.2025.2526458 · Cited by 8 · see citing works
“35 The findings by Boman et al. 36 indicated that the c.960delG mutation in the MSTN gene significantly affects meat and fat characteristics more than the c.2360G > A mutation, which is consistent with the latter’s role in reducing myostatin protein levels to about one-third due to translational…”
Nguyen, V.-L., Lee, K.-B., & Moon, Y. J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157060 · Cited by 10 · see citing works
“Several studies have revealed vital pathways and modulators that could be related to myostatin: ERK1/2 cascade, Wnt pathways, TGF-β 1, and IGF-1 [55].”
InfluentialMyostatin 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 · see citing works
“Myostatin exerts its effects primarily through binding to the activin receptor type IIB (ActRIIB), in complex with type I receptors ALK4 or ALK5, leading to SMAD2/3 phosphorylation and transcriptional regulation of target genes, as demonstrated in cellular and in vivo models [22–25].”
McNeish, B. L., Miljkovic, I., Zhu, X., Cawthon, P. M., Newman, A. B., Goodpaster, B. H., Yaffe, K. S., & Rosano, C. (2023) · The Journals of Gerontology Series A · doi:10.1093/gerona/glad132 · Cited by 7 · see citing works
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 · see citing works
“Modifying myostatin activity mainly results in enhanced muscle development and reduced intramuscular fat accumulation (Baig et al. 2022).”
Shaikh, S., Ahmad, K., Lim, J. H., Ahmad, S. S., Lee, E. J., & Choi, I. (2025) · Pharmaceuticals · doi:10.3390/ph18091407 · Cited by 6 · see citing works
“MSTN inhibition is promising as a sarcopenia treatment, with the potential to improve SM performance [107,108].”
Self-citationSamali, S. A., Hosseini, S. F., Mohammadi, Y., Sadri, F., & Rezaei, Z. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-11390-6 · Cited by 6 · see citing works
“Importantly, myostatin activity is endogenously regulated by several natural antagonists, including follistatin, GASP-1, and decorin, which bind myostatin and prevent its interaction with receptors [8].”
Dave, A., Park, E., Piya, S., & Pezzuto, J. M. (2025) · Foods · doi:10.3390/foods14040695 · Cited by 7 · see citing works
“Serpina1d increases with exercise [63], may play a role in muscle contraction [64], and promotes muscle hypertrophy due to inhibiting the negative regulator of muscle growth, myostatin [65].”
Díaz‐Castro, J., Reyes-Olavarría, D., Toledano, J. M., Puche-Juárez, M., Garcia-Vega, J. E., Ochoa, J. J., & Moreno‐Fernández, J. (2024) · Clinical Nutrition · doi:10.1016/j.clnu.2024.02.024 · Cited by 6 · see citing works
Akhter, A., Sheikh, A. M., Yoshino, J., Kanda, T., Nagai, A., Matsuo, M., & Yano, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26073098 · Cited by 5 · see citing works
“MSTN, scientifically recognized as Growth Differentiation Factor-8 (GDF-8), restricts the potential of skeletal muscle growth, which induces protein breakdown and skeletal muscle loss by activating the ubiquitin– proteasome pathway [17,18].”
Klf9 Loss of Function Protects Against Glucocorticoids Induced Skeletal Muscle Wasting
Zhang, Y., Hao, J., Feng, Y.-Y., Qiu, T., Wu, J., Zhou, X., Fan, H., & Chang, Y. (2025) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.70020 · Cited by 5 · see citing works
“Mstn decreases protein synthesis by inhibiting the AKT/mTOR signalling pathway and inducing muscle atrophy by activating the transcription of atrophy-related genes, including MAFbx and MuRF1 [11–13].”
Skeletal muscle dysfunction in COPD: miRNAs, myokines and exercise
Maniscalco, M., Fuschillo, S., Ambrosino, P., Candia, C., Domenico, A. D., Lombardi, C., Motta, A., & Ambrosino, N. (2026) · ERJ Open Research · doi:10.1183/23120541.00887-2025 · Cited by 5 · see citing works
Wu, Y., Yang, L., Du, Y., Su, Y., Zhao, C., Lu, L., Cai, J., Wang, D., & Zhou, L. (2024) · Aquaculture Reports · doi:10.1016/j.aqrep.2024.101926 · Cited by 5 · see citing works
Lee, H., & Lim, Y. (2025) · Nutrients · doi:10.3390/nu17223615 · Cited by 4 · see citing works
“Myostatin, a member of the TGF-β superfamily, is a well-established negative regulator of skeletal muscle growth and regeneration [54].”
Roles of natural products on myokines expression and secretion in skeletal muscle atrophy.
Liu, Z.-Y., Ye, X.-M., Li, N., Shang, J.-M., Du, G.-H., & Yang, X.-Y. (2024) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2024.114550 · Cited by 5 · see citing works
Role of Myostatin in Rheumatoid Arthritis: A Review of the Clinical Impact
González-Ponce, F., Ramírez-Villafaña, M., Gómez-Ramírez, E. E., Saldaña-Cruz, A. M., Gallardo-Moya, S. G., Rodriguez-Jimenez, N. A., Jacobo-Cuevas, H., Nava-Valdivia, C. A., Avalos-Salgado, F. A., Totsuka-Sutto, S. E., et al. (2024) · Diagnostics · doi:10.3390/diagnostics14111085 · Cited by 4 · see citing works
“To date, various mechanisms have been described by which myostatin can negatively regulate muscle growth, which can be, in turn, blocked by physical exercise, as well as mechanisms by which myostatin can affect bone integrity [46].”
BackgroundTomaszewska, E., Wojtysiak, D., Grzegorzewska, A. K., Świątkiewicz, M., Donaldson, J., Arciszewski, M. B., Dresler, S., Puzio, I., Szymańczyk, S., Dobrowolski, P., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168735 · Cited by 4 · see citing works
“OT and MNST are sarcopenic indicators, and the obtained results are consistent with other data [94–98].”
ResultAmbroszkiewicz, J., Chełchowska, M., Mazur, J., Rowicka, G., Klemarczyk, W., Strucińska, M., & Gajewska, J. (2025) · Nutrients · doi:10.3390/nu17050834 · Cited by 4 · see citing works
Kang, M. J., Hwang, S. H., Park, C. H., Moon, J. W., Kim, D. W., Bae, S. E., Kim, J. H., Nam, J. M., Kim, S. J., Bang, J., et al. (2025) · Experimental Cell Research · doi:10.1016/j.yexcr.2025.114577 · Cited by 4 · see citing works
Self-citationLee, E. J., Shaikh, S., Lee, J. H., Hur, S. J., & Choi, I. (2025) · Scientific Reports · doi:10.1038/s41598-025-98386-1 · Cited by 4 · see citing works
Self-citationMicroRNA-33 inhibition ameliorates muscular dystrophy by enhancing skeletal muscle regeneration
Sowa, N., Horie, T., Ide, Y., Baba, O., Kora, K., Yoshida, T., Nakamura, Y., Matsumura, S., Matsushita, K., Imanaka, M., et al. (2025) · EMBO Molecular Medicine · doi:10.1038/s44321-025-00273-9 · Cited by 4 · see citing works
“FST inhibits the function of other members of the TGF-β superfamily, including myostatin, a negative regulator of muscle development and growth that induces muscle atrophy-related genes, such as MuRF1 and Atrogin1 , through the Smad signaling pathway (Baig et al, 2022).”
Studying Myostatin as a Diagnostic Indicator in Sera of Iraqi Women with Metabolic Syndrome
Assaf, R. H., & Farhan, L. O. (2023) · Baghdad Science Journal · doi:10.21123/bsj.2023.8180 · Cited by 3 · see citing works
Zhang, Y., & Qiu, Y. (2026) · Sports · doi:10.3390/sports14050212 · Cited by 3 · see citing works
“Mechanistic insights from cell and animal studies suggest that when muscle is subjected to mechanical stress, it can downregulate MSTN expression via pathways such as JNK-mediated phosphorylation of transcription factor Smad2 [55,57].”
InfluentialCircular RNAs and their emerging roles in muscular immune-related diseases
Urzi, F., Srpčič, A., & Lakota, K. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1675567 · Cited by 3 · see citing works
Manjutha, S., Elayadeth‐Meethal, M., Abraham, B. L., Muhasin Asaf, V. N., Murugan, S. S., & Radhika, G. (2023) · Animal Biotechnology · doi:10.1080/10495398.2023.2189916 · Cited by 3 · see citing works
Quan, B., Liu, X., Li, Z.-Y., Han, S., Cui, Q., Chang, S.-Y., Lv, S., Yin, X., & Liang, S. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.111673 · Cited by 3 · see citing works
Serum Myostatin among Excessive Drinkers
Martín‐González, C., Pérez‐Hernández, O., Rodríguez, A. G., Abreu-González, P., Toledo, P. O., Fernández-Rodríguez, C. M., Alvisa-Negrín, J. C., Martı́nez-Riera, A., & González‐Reimers, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032981 · Cited by 4 · see citing works
“Only men were included given the marked differences in body composition among men and women and the possibly different relationship between myostatin and muscle mass among men and women [53].”
BackgroundMogiłko, N., & Małgorzewicz, S. (2025) · Biomolecules · doi:10.3390/biom15050703 · Cited by 3 · see citing works
“Myostatin also has therapeutic applications in muscle-related diseases, such as muscular dystrophy, where inhibiting myostatin may help build muscle mass. Additionally, manipulating myostatin levels may prove beneficial in treating sarcopenia in older individuals [15].”
Investigation of snails transmitting parasitic diseases in Yunnan Province.
Yuan-xiao, C., Zhang, W., Ming, T., Chen, Y., WenLin, W., & Naiguang, Z. (2009) · Journal of Pathogen Biology · Cited by 3 · see citing works
From aging to space: A comparative biology of skeletal muscle degeneration
Qaisar, R. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.168058 · Cited by 2 · see citing works
Ayers-Creech, W. A., Steiner, J. L., Laskin, G. R., & Gordon, B. S. (2025) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2025.112704 · Cited by 2 · see citing works
Ahmad, K., Ahmad, S. S., & Choi, I. (2026) · Scientific Reports · doi:10.1038/s41598-026-39066-6 · Cited by 2 · see citing works
Self-citationStein, M. J., Baurecht, H., Bohmann, P., Córdova, R., Ferrari, P., Fervers, B., Friedenreich, C. M., Gunter, M. J., Peruchet‐Noray, L., Wu, D., et al. (2026) · Communications Medicine · doi:10.1038/s43856-026-01514-9 · Cited by 2 · see citing works
“MVPA was strongly inversely associated with the proteins LEP, MSTN, and TGFBR2, and strongly positively associated with COMP, ITGAM, and MYOM3 (Fig.”
Transglutaminase-catalyzed covalent anti-myostatin peptide depots
Hamm, P., Beckmann, D., Worschech, R., Braun, A. C., Gutmann, M., Korb‐Pap, A., Lühmann, T. C., Pap, T., & Meinel, L. (2024) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2024.114462 · Cited by 2 · see citing works
Khalıl, F., shehata, N., Ibrahim, M. A., Nady, S., Emeash, H. H., & Abdelghany, A. K. (2024) · Beni-Suef University Journal of Basic and Applied Sciences · doi:10.1186/s43088-024-00575-w · Cited by 2 · see citing works
“The myostatin gene ( MSTN ) is a muscle regulator that contributes to the development of the highest muscular mass [23].”
Marulanda-Díaz, N., Estrada, A., Milán, A. F., Narváez-Sánchez, R., Calderón, J. C., & Giraldo, N. A. G. (2025) · Nutrition · doi:10.1016/j.nut.2025.112767 · Cited by 2 · see citing works
Identification and Validation of Genus/Species-Specific Short InDels in Dairy Ruminants
Cosenza, G., Fulgione, A., Albarella, S., Ciotola, F., Peretti, V., Gallo, D., & Pauciullo, A. (2025) · BMC Veterinary Research · doi:10.1186/s12917-025-04694-z · Cited by 2 · see citing works
“Mutations at this locus result in muscular hypertrophy and reduced fat, a phenomenon observed in ‘double muscled’ breeds of cattle and in several livestock and model species [44, 45].”
Cord Blood as a Trophic-Growth Additive for Culture Work
Goncharov, A., Shupletsova, V., Gazatova, N. D., Melashchenko, O., Yurova, K., & Litvinova, L. S. (2024) · Cell and Tissue Biology · doi:10.1134/s1990519x24700299
“Myostatin factor has a broad regulatory effect on muscle tissue cells (Baig et al., 2022; Esposito et al., 2022; Venugopal et al., 2022).”
Yang, H., Zheng, Y., Yu, T., Wu, B., Liu, Z., Liu, S., Sun, X., & Zhou, L. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142308 · Cited by 1 · see citing works
Targeting myostatin in cancer cachexia: Exploring the potential of MSTN gene therapy
Penumarthi, K. (2025) · Scholarly review . · doi:10.70121/001c.139049 · Cited by 1 · see citing works
Zhang, L., Li, P., Wang, X., Kong, M., Wu, W., & Zheng, W. (2025) · Animals · doi:10.3390/ani15233387 · Cited by 1 · see citing works
“Consistent with findings from MSTN editing studies in cattle, pigs, goats, and other livestock, these results confirm the cross-species conservation of MSTN as a negative regulator of skeletal muscle growth [19,20].”
Molecular Regulation of Growth in Aquaculture: From Genes to Sustainable Production
Șerban, D. A., Barbacariu, C.-A., Ivancia, M., & Creangă, Ș. (2025) · Life · doi:10.3390/life15121831 · Cited by 1 · see citing works
“The growth hormone (GH)-insulin-like growth factor (IGF) axis functions as the central endocrine system controlling body size development [7,8], while the transforming growth factor-β (TGF-β ) superfamily, particularly myostatin, acts as the primary negative regulator limiting muscle growth [9,10].”
PDMD: A Comprehensive Repository of Plants Reported for Skeletal Muscle-related Ailments
Gupta, A., & Chawla, S. (2026) · Current Drug Targets · doi:10.2174/0113894501435270251129220150 · Cited by 1 · see citing works
Xu, X.-Q., Wang, Y.-R., Guo, D.-D., Zhou, Y., Long, J.-Y., & Liu, Z.-Y. (2026) · Poultry Science · doi:10.1016/j.psj.2026.106511 · Cited by 1 · see citing works
Rahaman, K. A., Kim, M.-J., Jung, Y.-N., Kang, S.-K., & Han, H.-S. (2026) · Bioactive Materials · doi:10.1016/j.bioactmat.2026.01.035 · Cited by 1 · see citing works
Bhatt, S. P., Khurana, A., Pandey, S., & Misra, A. (2026) · Frontiers in Endocrinology · doi:10.3389/fendo.2026.1740628 · Cited by 1 · see citing works
Mohammad, H., CHATTERJEE, R. N., Jammula, S. P., Kumboju, C., Vadlapally, H., Ramidi, A., Rajashree, A., Yousuf, F., Tetarwal, D. P., Anuradha, C., et al. (2026) · The Nucleus · doi:10.1007/s13237-026-00676-0 · Cited by 1 · see citing works
Exercise Intensity and Circulating Exerkine Responses: A Narrative Review of Selected Molecules
Zhao, Y., Wang, T., Zhang, X., Wang, W., Fu, Y., Laher, I., & Li, S. (2026) · Biomolecules · doi:10.3390/biom16060852 · Cited by 1 · see citing works
“MSTN suppresses myocyte growth and regeneration by inhibiting satellite cell proliferation and differentiation, thereby limiting skeletal muscle mass [57,58].”
Targeting Myostatin for Sustainable Meat Production: Insights From Multiple Species
Santomassimo, C., Perini, F., Colombi, D., Bettini, S., Trombetta, M. F., Pasquini, M., Ceccobelli, S., Haruna, I. L., Patel, K., & Lasagna, E. (2026) · Animal Genetics · doi:10.1002/age.70149 · Cited by 1 · see citing works
“MSTN negatively regulates myogenesis through autocrine and paracrine signalling mediated by activin type II-A and II-B receptors (Baig et al. 2022; Chen et al. 2021).”
Epis, R., Rovetta, G., Ferrari, G., Bonfanti, C., Careccia, G., & Messina, G. (2026) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.70333 · Cited by 1 · see citing works
“Among them, the blockage of myostatin (Mstn) [65], a myokine that negatively regulates muscle growth, has been largely investigated [66].”
孙玲淑, Zhao, P., Fan, X., Puig-Ribera, A. M., & Solé‐Casals, J. (2026) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2026.2734595 · Cited by 1 · see citing works
Incomplete Immunization and Chronic Energy Deficiency (CED) as Risk Factors for Stunting in Toddlers
Firdausi, A. H., & Dasuki, M. S. (2023) · Disease Prevention and Public Health Journal (DPPHJ) · doi:10.12928/dpphj.v17i2.8468 · Cited by 1 · see citing works
“KEK in pregnant women is influenced by several conditions including mother's knowledge, food diversity, energy intake, and protein intake [24].”
Jelić, I. M., Štoković, N., Ivanjko, N., Pecina, M. M., Kufner, V., Bordukalo-Nikšić, T., & Vukičević, S. (2024) · International Orthopaedics · doi:10.1007/s00264-024-06389-w · Cited by 1 · see citing works
“GDF8 (myostatin) is a negative regulator of muscle growth, and its inhibition could counteract the muscle atrophy seen in MDC1A [ 58 ].”
Furalyov, V. A., Kukes, V. G., Амырхановна, Г. А., Parfenova, O. K., Sidorov, N. G., & Kurkin, R. V. (2022) · Current Bioactive Compounds · doi:10.2174/1573407219666221122122346 · Cited by 1 · see citing works
Chen, M., Zhao, Y. M., Xu, X.-L., Zhang, X., Zhang, J.-L., Wu, S., Liu, Z., Yuan, Y., Guo, X., Qi, S., et al. (2023) · eLife · doi:10.7554/elife.86827.1 · Cited by 1 · see citing works
Polymorphisms of the myostatin gene in animals (overreview)
Klimanova, E. A., Alexandrova, D. A., & Kochnev, N. N. (2024) · Bulletin of NSAU (Novosibirsk State Agrarian University) · doi:10.31677/2072-6724-2024-71-2-209-219
Chen, M., Zhao, Y. M., Xu, X.-L., Zhang, X., Zhang, J., Wu, S., Liu, Z., Yuan, Y., Guo, X., Qi, S., et al. (2024) · eLife · doi:10.7554/elife.86827.2
Umbilical blood as a trophic-growth supplement for cultural work
Goncharov, A., Shupletsova, V., Gazatova, N. D., Melashchenko, O., Yurova, K., & Litvinova, L. S. (2024) · Tsitologiya · doi:10.31857/s0041377124020019
Kartika, R. W., Sidharta, V. M., Djuartina, T., Sartika, C. R., & Timotius, K. H. (2024) · Annals of African Medicine · doi:10.4103/aam.aam_205_23
Stein, M. J., Baurecht, H., Bohmann, P., Córdova, R., Ferrari, P., Fervers, B., Friedenreich, C. M., Gunter, M. J., Peruchet‐Noray, L., Wu, D., et al. (2025) · medRxiv · doi:10.1101/2025.03.26.25324689
Exploring the Myostatin Activation Pathway: A Promising Target for Treating Muscle Atrophy
Quintanilha, D. B., & Santos, H. F. D. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c00639
Koczulla, A. R., Boeselt, T., Zoellner, A. S., Gloeckl, R., Kroll, D., Jarosch, I., Schneeberger, T., Held, J., & Janciauskiene, S. M. (2025) · Respiratory Medicine and Research · doi:10.1016/j.resmer.2025.101193
González-Ponce, F., Gámez-Nava, J. I., Jacobo-Cuevas, H., Ponce-Guarneros, J. M., Valdivia-Tangarife, E. R., Nava-Valdivia, C. A., Rodriguez-Jimenez, N. A., Ramírez-Villafaña, M., Gómez-Ramírez, E. E., González-Vázquez, S. A., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26178232
Lutski, M., Karni‐Efrati, Z., Zucker, I., & Frankenthal, D. (2025) · European Geriatric Medicine · doi:10.1007/s41999-025-01297-7
Simoes, D. C. M., Kritikaki, E., Terzis, G. D., & Vogiatzis, I. (2025) · Cells · doi:10.3390/cells14211656
“Furthermore, we assessed the expression of MSTN , whose protein levels are known to negatively regulate muscle growth and size [20].”
- Authors
- Baig, M. H., Ahmad, K., Moon, J. S., Park, S.-Y., Ho Lim, J., Chun, H. J., Qadri, A. F., Hwang, Y. C., Jan, A. T., Ahmad, S. S., Ali, S., Shaikh, S., Lee, E. J., & Choi, I.
- Affiliations
- Yonsei University (KR)
- Yeungnam University (KR)
- Yeungnam University College (KR)
- Baba Ghulam Shah Badshah University (IN)
- Corresponding author
- Lee, Eun Ju
- Choi, Inho
- ORCID
- Venue
- Frontiers in Physiology
- Publisher
- Frontiers Media SA
- Published
- 2022-06-23
- Volume
- 13
- Pages
- 876078-876078
- ISSN
- 1664-042X (ISSN-L)
- PMC
- PMC9259834
- OpenAlex
- W4283320528
- Cited by
- 135
- References
- 184
- Citations by year
- 2026: 48 · 2025: 38 · 2024: 30 · 2023: 15 · 2022: 3
- FWCI
- 2.24
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Physiology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- YUHSpace (Yonsei University Medical Library) (submittedVersion, cc-by-nc-nd)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Research Foundation of Korea (2020R1A6A1A03044512 NRF-2021R1A2C2004177 2019R1C1C1006542)
- Korea Institute of Planning and Evaluation for Technology in Food, Agriculture and Forestry (321026-05)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac Fibrosis and Remodeling
- Keywords
- myostatin, skeletal muscle, myogenesis, muscle growth regulation, TGF-beta superfamily, myostatin inhibitors, natural compounds, peptide inhibitors, virtual screening, protein-peptide interactions
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
