Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size

Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216

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

Identification of ubiquitin ligases required for skeletal muscle atrophy.

Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521

Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.

Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012

Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo

Bodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752

Double muscling in cattle due to mutations in the myostatin gene

McPherron, A. C., & Lee, S.-J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12457 · Cited by 2,039

The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors.

Stitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00211-4 · Cited by 1,964

Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy

Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A., & Goldberg, A. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251541198 · Cited by 1,774

Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways

Rommel, C., Bodine, S. C., Clarke, B. A., Rossman, R., Nunez, L., Stitt, T. N., Yancopoulos, G. D., & Glass, D. J. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1009 · Cited by 1,583

Rapid Disuse Atrophy of Diaphragm Fibers in Mechanically Ventilated Humans

Levine, S., Nguyen, T., Taylor, N. E., Friscia, M. E., Budak, M. T., Rothenberg, P., Zhu, J., Sachdeva, R., Sonnad, S. S., Kaiser, L. R., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa070447 · Cited by 1,580

Current understanding of sarcopenia: possible candidates modulating muscle mass

Sakuma, K., Aoi, W., & Yamaguchi, A. (2014) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-014-1527-x · Cited by 133

HIF-1-driven skeletal muscle adaptations to chronic hypoxia: molecular insights into muscle physiology

Favier, F. B., Britto, F. A., Freyssenet, D. G., Bigard, X. A., & Benoit, H. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2025-9 · Cited by 135

Cisplatin-Induced Skeletal Muscle Dysfunction: Mechanisms and Counteracting Therapeutic Strategies

Conte, E., Bresciani, E., Rizzi, L., Cappellari, O., Luca, A. D., Torsello, A., & Liantonio, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041242 · Cited by 136

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 130

Molecular effects of exercise training in patients with cardiovascular disease: focus on skeletal muscle, endothelium, and myocardium

Adams, V., Reich, B., Uhlemann, M., & Niebauer, J. (2017) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00470.2016 · Cited by 131

Mitochondrial dysfunction and skeletal muscle atrophy: Causes, mechanisms, and treatment strategies

Kubat, G. B., Bouhamida, E., Ülger, Ö., Türkel, İ., Pedriali, G., Ramaccini, D., Ekinci, Ö., Özerkliğ, B., Atalay, Ö., Patergnani, S., et al. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.07.003 · Cited by 134

LARGE glycans on dystroglycan function as a tunable matrix scaffold to prevent dystrophy

Goddeeris, M. M., Wu, B., Venzke, D. P., Yoshida‐Moriguchi, T., Saito, F., Matsumura, K., Moore, S. A., & Campbell, K. P. (2013) · Nature · doi:10.1038/nature12605 · Cited by 125

Blockade of the Activin Receptor IIB Activates Functional Brown Adipogenesis and Thermogenesis by Inducing Mitochondrial Oxidative Metabolism

Fournier, B., Murray, B., Gutzwiller, S., Marcaletti, S., Marcellin, D., Bergling, S., Brachat, S., Persohn, E., Pierrel, E., Bombard, F., et al. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06575-11 · Cited by 130

Identification of atrogin-1-targeted proteins during the myostatin-induced skeletal muscle wasting

Lokireddy, S., Wijesoma, I. W., Sze, S. K., McFarlane, C., Kambadur, R., & Sharma, M. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00402.2011 · Cited by 135

Metabolic Functions of Myostatin and GDF11

McPherron, A. C. (2010) · Immunology Endocrine & Metabolic Agents - Medicinal Chemistry · doi:10.2174/187152210793663810 · Cited by 128

Myostatin signaling regulates Akt activity via the regulation of miR-486 expression

Hitachi, K., Nakatani, M., & Tsuchida, K. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.12.003 · Cited by 127

Advances in cancer cachexia: Intersection between affected organs, mediators, and pharmacological interventions

Siddiqui, J. A., Pothuraju, R., Jain, M., Batra, S. K., & Nasser, M. W. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188359 · Cited by 126

Sarcopenia in Inflammatory Bowel Disease: A Narrative Overview

Dhaliwal, A., Quinlan, J. I., Overthrow, K., Greig, C. A., Lord, J. M., Armstrong, M. J., & Cooper, S. C. (2021) · Nutrients · doi:10.3390/nu13020656 · Cited by 129

Molecular Adaptations to Aerobic Exercise Training in Skeletal Muscle of Older Women

Konopka, A. R., Douglass, M. D., Kaminsky, L. A., Jemioło, B., Trappe, T. A., Trappe, S. W., & Harber, M. P. (2010) · The Journals of Gerontology Series A · doi:10.1093/gerona/glq109 · Cited by 134

Myostatin inhibition induces muscle fibre hypertrophy prior to satellite cell activation

Wang, Q., & McPherron, A. C. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2011.226001 · Cited by 128

Myostatin promotes the wasting of human myoblast cultures through promoting ubiquitin-proteasome pathway-mediated loss of sarcomeric proteins

Lokireddy, S., Mouly, V., Butler-Browne, G. S., Gluckman, P. D., Sharma, M., Kambadur, R., & McFarlane, C. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00114.2011 · Cited by 126

Regulation of mTORC1 by growth factors, energy status, amino acids and mechanical stimuli at a glance

Bond, P. (2016) · Journal of the International Society of Sports Nutrition · doi:10.1186/s12970-016-0118-y · Cited by 121

JNK regulates muscle remodeling via myostatin/SMAD inhibition

Lessard, S. J., MacDonald, T. L., Pathak, P., Han, M. S., Coffey, V. G., Edge, J., Rivas, D. A., Hirshman, M. F., Davis, R. J., & Goodyear, L. J. (2018) · Nature Communications · doi:10.1038/s41467-018-05439-3 · Cited by 119

Forum on bone and skeletal muscle interactions: Summary of the proceedings of an ASBMR workshop

Bonewald, L. F., Kiel, D. P., Clemens, T. L., Esser, K. A., ORWOLL, E. S., O’Keefe, R. J., & Fielding, R. A. (2013) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.1980 · Cited by 119

Mammalian Target of Rapamycin (mTOR) Signaling Network in Skeletal Myogenesis

Ge, Y., & Chen, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.406942 · Cited by 121

Myostatin: Expanding horizons

Sharma, M., McFarlane, C., Kambadur, R., Kukreti, H., Bonala, S., & Srinivasan, S. (2015) · IUBMB Life · doi:10.1002/iub.1392 · Cited by 120

Engineered skeletal muscles for disease modeling and drug discovery

Wang, J., Khodabukus, A., Rao, L., VanDusen, K. W., Abutaleb, N. O., & Bursac, N. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.119416 · Cited by 125

Cancer stem cells and cell size: A causal link?

Li, Q., Rycaj, K., Chen, X., & Tang, D. G. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.07.002 · Cited by 119

Sarcopenia in chronic liver disease: mechanisms and countermeasures

Allen, S., Quinlan, J. I., Dhaliwal, A., Armstrong, M. J., Elsharkawy, A. M., Greig, C. A., Lord, J. M., Lavery, G. G., & Breen, L. (2020) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00373.2020 · Cited by 129

Metabolic benefits of resistance training and fast glycolytic skeletal muscle

LeBrasseur, N. K., Walsh, K. X., & Arany, Z. P. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00512.2010 · Cited by 123

Supraphysiological levels of GDF11 induce striated muscle atrophy

Hammers, D. W., Merscham‐Banda, M., Hsiao, J. Y., Engst, S., Hartman, J. J., & Sweeney, H. L. (2017) · EMBO Molecular Medicine · doi:10.15252/emmm.201607231 · Cited by 120

Structural basis for potency differences between GDF8 and GDF11

Walker, R. G., Czepnik, M., Goebel, E. J., McCoy, J. C., Vujić, A., Cho, M., Oh, J., Aykul, S., Walton, K. L., Schang, G., et al. (2017) · BMC Biology · doi:10.1186/s12915-017-0350-1 · Cited by 115

Biomarkers of cancer cachexia

Loumaye, A., & Thissen, J. (2017) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2017.07.011 · Cited by 112

Molecular genetic studies of gene identification for sarcopenia

Tan, L., Liu, S., Lei, S., Papasian, C. J., & Deng, H. (2011) · Human Genetics · doi:10.1007/s00439-011-1040-7 · Cited by 115

Molecular Mechanisms and Treatment Options for Muscle Wasting Diseases

Rüegg, M. A., & Glass, D. J. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010510-100537 · Cited by 114

Connecting Myokines and Metabolism

Ahima, R. S., & Park, H. K. (2015) · Endocrinology and Metabolism · doi:10.3803/enm.2015.30.3.235 · Cited by 111

The Molecular Basis for Load-Induced Skeletal Muscle Hypertrophy

Marcotte, G. R., West, D. W. D., & Baar, K. (2014) · Calcified Tissue International · doi:10.1007/s00223-014-9925-9 · Cited by 123

Minireview: New Molecular Mediators of Glucocorticoid Receptor Activity in Metabolic Tissues

Patel, R., Williams‐Dautovich, J., & Cummins, C. L. (2014) · Molecular Endocrinology · doi:10.1210/me.2014-1062 · Cited by 113

Out of Control: The Role of the Ubiquitin Proteasome System in Skeletal Muscle during Inflammation

Haberecht-Müller, S., Krüger, E., & Fielitz, J. (2021) · Biomolecules · doi:10.3390/biom11091327 · Cited by 108

Mechanisms regulating muscle mass during disuse atrophy and rehabilitation in humans

Marimuthu, K., Murton, A. J., & Greenhaff, P. L. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00962.2010 · Cited by 107

TAK-1/p38/nNFκB signaling inhibits myoblast differentiation by increasing levels of Activin A

Trendelenburg, A. U., Meyer, A. S., Jacobi, C., Feige, J. N., & Glass, D. J. (2012) · Skeletal Muscle · doi:10.1186/2044-5040-2-3 · Cited by 106

Molecular pathways: cachexia signaling-A targeted approach to cancer treatment

Miyamoto, Y., Hanna, D. L., Zhang, W., Baba, H., & Lenz, H.-J. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-0495 · Cited by 111

Novel events in the molecular regulation of muscle mass in critically ill patients

Constantin, D., McCullough, J., Mahajan, R. P., & Greenhaff, P. L. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.206193 · Cited by 105

The therapeutic potential of IGF-I in skeletal muscle repair

Song, Y., Song, J. L., Delafontaine, P., & Godard, M. P. (2013) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.03.004 · Cited by 102

Muscle protein synthesis, mTORC1/MAPK/Hippo signaling, and capillary density are altered by blocking of myostatin and activins

Hulmi, J. J., Oliveira, B. M. S., Silvennoinen, M., Hoogaars, W. M. H., Ma, H., Pierre, P., Pasternack, A. H., Kainulainen, H., & Ritvos, O. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00389.2012 · Cited by 102

Understanding of sarcopenia: from definition to therapeutic strategies

Kim, J. W., Kim, R., Choi, H., Lee, S., & Bae, G. (2021) · Archives of Pharmacal Research · doi:10.1007/s12272-021-01349-z · Cited by 103

Smad7 gene delivery prevents muscle wasting associated with cancer cachexia in mice

Winbanks, C. E., Murphy, K. T., Bernardo, B. C., Qian, H., Liu, Y., Sepulveda, P. V., Beyer, C., Hagg, A., Thomson, R. E., Chen, J. L., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aac4976 · Cited by 95

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

Mechanisms involved in the enhancement of mammalian target of rapamycin signalling and hypertrophy in skeletal muscle of myostatin‐deficient mice

Lipina, C., Kendall, H., McPherron, A. C., Taylor, P. M., & Hundal, H. S. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.04.039 · Cited by 98

Androgen-mediated regulation of skeletal muscle protein balance

Rossetti, M. L., Steiner, J. L., & Gordon, B. S. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.02.031 · Cited by 95

Blocking extracellular activation of myostatin as a strategy for treating muscle wasting

Pirruccello, M., Jackson, J., Wawersik, S., Webster, M. T., Salta, L., Long, K. K., McConaughy, W., Capili, A. D., Boston, C., Carven, G. J., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-20524-9 · Cited by 101

Muscle Wasting Diseases: Novel Targets and Treatments

Furrer, R., & Handschin, C. (2018) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010818-021041 · Cited by 94

Murine models of atrophy, cachexia, and sarcopenia in skeletal muscle

Romanick, M. A., Thompson, L. V., & Brown‐Borg, H. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.03.011 · Cited by 104

Emerging role of myostatin and its inhibition in the setting of chronic kidney disease

Verzola, D., Barisione, C., Picciotto, D., Garibotto, G., & Koppe, L. (2018) · Kidney International · doi:10.1016/j.kint.2018.10.010 · Cited by 95

The methyltransferase SMYD3 mediates the recruitment of transcriptional cofactors at the myostatin and c-Met genes and regulates skeletal muscle atrophyPreprint

Proserpio, V., Fittipaldi, R., Ryall, J. G., Sartorelli, V., & Caretti, G. (2013) · Genes & Development · doi:10.1101/gad.217240.113 · Cited by 99

The Role of IGF-1 Signaling in Skeletal Muscle Atrophy

Timmer, L. T., Hoogaars, W. M. H., & Jaspers, R. T. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-1435-3_6 · Cited by 90

Activin signal promotes cancer progression and is involved in cachexia in a subset of pancreatic cancer

Togashi, Y., Kogita, A., Sakamoto, H., Hayashi, H., Terashima, M., Velasco, M. A. D., Sakai, K., Fujita, Y., Tomida, S., Kitano, M., et al. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.10.037 · Cited by 89

Extracellular Regulation of Myostatin: A Molecular Rheostat for Muscle Mass

Lee, S. (2010) · Immunology Endocrine & Metabolic Agents - Medicinal Chemistry · doi:10.2174/187152210793663748 · Cited by 88

Revisiting the paradigm of myostatin in vertebrates: Insights from fishes

Gabillard, J., Biga, P. R., Rescan, P., & Seiliez, I. (2013) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2013.08.012 · Cited by 87

Lipopolysaccharide inhibits myogenic differentiation of C2C12 myoblasts through the Toll-like receptor 4-nuclear factor-κB signaling pathway and myoblast-derived tumor necrosis factor-α

Ono, Y., & Sakamoto, K. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182040 · Cited by 89

Supraphysiologic Administration of GDF11 Induces Cachexia in Part by Upregulating GDF15

Jones, J. E., Cadena, S. M., Gong, C., Wang, X., Chen, Z., Wang, S. X., Vickers, C., Chen, H., Lach‐Trifilieff, E., Hadcock, J. R., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.01.044 · Cited by 87

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

Modelling in vivo skeletal muscle ageing in vitro using three‐dimensional bioengineered constructs

Sharples, A. P., Player, D. J., Martin, N. R. W., Mudera, V., Stewart, C. E., & Lewis, M. P. (2012) · Aging Cell · doi:10.1111/j.1474-9726.2012.00869.x · Cited by 84

Signalling and the control of skeletal muscle size

Otto, A., & Patel, K. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.04.009 · Cited by 84

Swimming-induced exercise promotes hypertrophy and vascularization of fast skeletal muscle fibres and activation of myogenic and angiogenic transcriptional programs in adult zebrafish

Palstra, A. P., Rovira, M., Rizo‐Roca, D., Torrella, J. R., Spaink, H. P., & Planas, J. V. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-1136 · Cited by 88

β2-Adrenergic agonists and the treatment of skeletal muscle wasting disorders

Joassard, O. R., Durieux, A., & Freyssenet, D. G. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.06.025 · Cited by 85

Altered REDD1, myostatin, and Akt/mTOR/FoxO/MAPK signaling in streptozotocin-induced diabetic muscle atrophy

Hulmi, J. J., Silvennoinen, M., Lehti, M., Kivelä, R., & Kainulainen, H. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00398.2011 · Cited by 81

TGF-β Blockade Reduces Mortality and Metabolic Changes in a Validated Murine Model of Pancreatic Cancer Cachexia

Greco, S. H., Tomkötter, L., Vahle, A., Rokosh, R. S., Avanzi, A., Mahmood, S. K., Deutsch, M., Alothman, S., Alqunaibit, D., Ochi, A., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0132786 · Cited by 84

Depletion of CD206+ M2-like macrophages induces fibro-adipogenic progenitors activation and muscle regeneration

Nawaz, A., Bilal, M., Fujisaka, S., Kado, T., Aslam, M. R., Ahmed, S., Okabe, K., Igarashi, Y., Watanabe, Y., Kuwano, T., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34191-y · Cited by 81

microRNAs: Modulators of the underlying pathophysiology of sarcopenia?

Brown, D. M., & Goljanek‐Whysall, K. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.08.007 · Cited by 77

Muscle disuse atrophy is not accompanied by changes in skeletal muscle satellite cell content

Snijders, T., Wall, B. T., Dirks, M. L., Senden, J. M., Hartgens, F., Dolmans, J., Losen, M. H., Verdijk, L. B., & van Loon, L. J. C. (2013) · Clinical Science · doi:10.1042/cs20130295 · Cited by 82

Myostatin inhibits myosatellite cell proliferation and consequently activates differentiation: evidence for endocrine-regulated transcript processing

Garikipati, D. K., & Rodgers, B. D. (2012) · Journal of Endocrinology · doi:10.1530/joe-12-0260 · Cited by 78

Decreased specific force and power production of muscle fibers from myostatin-deficient mice are associated with a suppression of protein degradation

Mendias, C. L., Kayupov, E., Bradley, J. R., Brooks, S. V., & Claflin, D. R. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00126.2011 · Cited by 77

The TGF-β Signalling Network in Muscle Development, Adaptation and Disease

Chen, J. L., Colgan, T. D., Walton, K. L., Gregorevic, P., & Harrison, C. A. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-27511-6_5 · Cited by 78

Untitled work

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

Aerobic exercise + weight loss decreases skeletal muscle myostatin expression and improves insulin sensitivity in older adults

Ryan, A. S., Li, G., Blumenthal, J. B., & Ortmeyer, H. K. (2013) · Obesity · doi:10.1002/oby.20216 · Cited by 74

An Image Analysis Method for the Precise Selection and Quantitation of Fluorescently Labeled Cellular Constituents

Agley, C. C., Velloso, C. P., Lazarus, N. R., & Harridge, S. D. R. (2012) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155412442897 · Cited by 73

Muscle cell‐derived cytokines in skeletal muscle regeneration

Waldemer, R. J., Kim, D., & Chen, J. (2022) · FEBS Journal · doi:10.1111/febs.16372 · Cited by 79

Vitamin D Signaling in Myogenesis: Potential for Treatment of Sarcopenia

Wagatsuma, A., & Sakuma, K. (2014) · BioMed Research International · doi:10.1155/2014/121254 · Cited by 73

Enhanced Development of Skeletal Myotubes from Porcine Induced Pluripotent Stem Cells

Genovese, N. J., Domeier, T. L., Telugu, B. P. V. L., & Roberts, R. M. (2017) · Scientific Reports · doi:10.1038/srep41833 · Cited by 75

Skeletal Muscle in ALS: An Unappreciated Therapeutic Opportunity?

Scaricamazza, S., Salvatori, I., Ferri, A., & Valle, C. (2021) · Cells · doi:10.3390/cells10030525 · Cited by 70

Proteotoxicity: An underappreciated pathology in cardiac disease

Sandri, M., & Robbins, J. M. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.12.015 · Cited by 73

Akt deficiency attenuates muscle size and function but not the response to ActRIIB inhibition

Goncalves, M. D., Pistilli, E. E., Balduzzi, A., Birnbaum, M. J., Lachey, J., Khurana, T. S., & Ahima, R. S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012707 · Cited by 69

Optimizing Skeletal Muscle Anabolic Response to Resistance Training in Aging

Endo, Y., Nourmahnad, A., & Sinha, I. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00874 · Cited by 77

The Intriguing Regulators of Muscle Mass in Sarcopenia and Muscular Dystrophy

Sakuma, K., Aoi, W., & Yamaguchi, A. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00230 · Cited by 70

Muscle Hyperplasia in Japanese Quail by Single Amino Acid Deletion in MSTN Propeptide

Lee, J., Kim, D., & Lee, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041504 · Cited by 71

Iron Metabolism of the Skeletal Muscle and Neurodegeneration

Hałoń, M., Borkowska, A., Herman-Antosiewicz, A., & Antosiewicz, J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00165 · Cited by 73

Advances in research on pharmacotherapy of sarcopenia

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

Myostatin inhibits proliferation but not differentiation of trout myoblasts

Seiliez, I., Sabin, N., & Gabillard, J. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.12.011 · Cited by 68

Myostatin Promotes Interleukin-1β Expression in Rheumatoid Arthritis Synovial Fibroblasts through Inhibition of miR-21-5p

Hu, S., Chang, A., Huang, C., Tsai, C., Lin, C., & Tang, C. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01747 · Cited by 68

Specific targeting of TGF-β family ligands demonstrates distinct roles in the regulation of muscle mass in health and disease

Chen, J. L., Walton, K. L., Hagg, A., Colgan, T. D., Johnson, K., Qian, H., Gregorevic, P., & Harrison, C. A. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620013114 · Cited by 116

If my muscle could talk: Myokines as a biomarker of frailty

Coelho‐Júnior, H. J., Picca, A., Calvani, R., Uchida, M. C., & Marzetti, E. (2019) · Experimental Gerontology · doi:10.1016/j.exger.2019.110715 · Cited by 71

Wnt4 activates the canonical β-catenin pathway and regulates negatively myostatin: functional implication in myogenesis

Bernardi, H., Gay, S., Fédon, Y., Vernus, B., Bonnieu, A., & Bacou, F. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00214.2010 · Cited by 67

GDF15/GFRAL Pathway as a Metabolic Signature for Cachexia in Patients with Cancer

Ahmed, D. S., Isnard, S., Lin, J. C.-Y., Routy, B., & Routy, J. (2020) · Journal of Cancer · doi:10.7150/jca.50376 · Cited by 71

Impaired regeneration: A role for the muscle microenvironment in cancer cachexia

Talbert, E. E., & Guttridge, D. C. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.09.009 · Cited by 71

Denervation atrophy is independent from Akt and mTOR activation and is not rescued by myostatin inhibition

MacDonald, E. M., Andrés‐Mateos, E., Mejías, R., Simmers, J. L., Mi, R., Park, J.-S., Ying, S., Höke, A., Lee, S., & Cohn, R. D. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.014126 · Cited by 67

Muscle cell communication in development and repair

Demonbreun, A. R., & McNally, E. M. (2017) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2017.03.008 · Cited by 64

Reduction of ribosome biogenesis with activation of the mTOR pathway in denervated atrophic muscle

Machida, M., Takeda, K., Yokono, H., IKEMUNE, S., Taniguchi, Y., Kiyosawa, H., & Takemasa, T. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22871 · Cited by 64

SMAD3 augments FoxO3-induced MuRF-1 promoter activity in a DNA-binding-dependent manner

Bollinger, L. M., Witczak, C. A., Houmard, J. A., & Brault, J. J. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00391.2013 · Cited by 67

Smad2/3 Proteins Are Required for Immobilization-induced Skeletal Muscle Atrophy

Tando, T., Hirayama, A., Furukawa, M., Sato, Y., Kobayashi, T., Funayama, A., Kanaji, A., Wu, H., Watanabe, R., Morita, M., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.680579 · Cited by 70

Regulation of Muscle Growth in Early Postnatal Life in a Swine Model

Rudar, M., Fiorotto, M. L., & Davis, T. A. (2018) · Annual Review of Animal Biosciences · doi:10.1146/annurev-animal-020518-115130 · Cited by 69

TGFβ signalling acts as a molecular brake of myoblast fusion

Melendez, J., Sieiro, D., Salgado, D., Morin, V., Dejardin, M.-J., Zhou, C., Mullen, A. C., & Marcelle, C. (2021) · Nature Communications · doi:10.1038/s41467-020-20290-1 · Cited by 66

The role of mechanobiology in progression of rotator cuff muscle atrophy and degeneration

Gibbons, M. C., Singh, A., Engler, A. J., & Ward, S. R. (2017) · Journal of Orthopaedic Research® · doi:10.1002/jor.23662 · Cited by 63

Electrical pulse stimulation: an in vitro exercise model for the induction of human skeletal muscle cell hypertrophy. A proof‐of‐concept study

Tarum, J., Folkesson, M., Atherton, P. J., & Kadi, F. (2017) · Experimental Physiology · doi:10.1113/ep086581 · Cited by 68

Down-Regulation of Akt/Mammalian Target of Rapamycin Signaling Pathway in Response to Myostatin Overexpression in Skeletal Muscle

Amirouche, A., Durieux, A., Banzet, S., Koulmann, N., Bonnefoy, R., Mouret, C., Bigard, X. A., Peinnequin, A., & Freyssenet, D. G. (2008) · Endocrinology · doi:10.1210/en.2008-0959 · Cited by 301

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

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

Myostatin and muscle fiber size. Focus on “Smad2 and 3 transcription factors control muscle mass in adulthood” and “Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size”

Welle, S. L. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00154.2009 · Cited by 32

Extracellular Signal–Regulated Kinase 1/2 Mitogen-Activated Protein Kinase Pathway Is Involved in Myostatin-Regulated Differentiation Repression

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 152