The bone morphogenetic protein axis is a positive regulator of skeletal muscle mass
Open accessAbstract
Although the canonical transforming growth factor β signaling pathway represses skeletal muscle growth and promotes muscle wasting, a role in muscle for the parallel bone morphogenetic protein (BMP) signaling pathway has not been defined. We report, for the first time, that the BMP pathway is a positive regulator of muscle mass. Increasing the expression of BMP7 or the activity of BMP receptors in muscles induced hypertrophy that was dependent on Smad1/5-mediated activation of mTOR signaling. In agreement, we observed that BMP signaling is augmented in models of muscle growth. Importantly, stimulation of BMP signaling is essential for conservation of muscle mass after disruption of the neuromuscular junction. Inhibiting the phosphorylation of Smad1/5 exacerbated denervation-induced muscle atrophy via an HDAC4-myogenin–dependent process, whereas increased BMP–Smad1/5 activity protected muscles from denervation-induced wasting. Our studies highlight a novel role for the BMP signaling pathway in promoting muscle growth and inhibiting muscle wasting, which may have significant implications for the development of therapeutics for neuromuscular disorders.
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?
Follistatin-mediated hypertrophy not only blocks myostatin signaling but simultaneously stimulates Smad1/5/8 activation.
“Consistently, follistatin-mediated hypertrophy not only blocks myostatin signaling but simultaneously stimulates Smad1/5/8 activation19,22,23.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [23]
BMP pathway is activated in myostatin knockout and is sufficient, when induced, to promote muscle growth and counteract muscle loss after denervation and in the absence of nutrients.
“BMP pathway is activated in myostatin knockout and is sufficient, when induced, to promote muscle growth and to counteract muscle loss after denervation and in the absence of nutrients [6–8].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [7]
BMP signaling is a positive regulator of muscle mass and is dominant over the myostatin pathway.
“On the other hand, BMP signaling is a positive regulator of muscle mass and is dominant over the myostatin pathway [6, 7].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [7]
Induction of BMP signaling activates Smad1/5/8, which with SMAD4 suppresses MUSA1 and activates mTOR-dependent protein synthesis.
“Induction of BMP signaling activates Smad1/5/8, which, together with SMAD 4, leads to the suppression of the MUSA1 [6] and the activation of mTOR-dependent protein synthesis [7].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [7]
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
Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143 · 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
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 · see citing works
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 · see citing works
Smad transcription factorsPreprint
Massagué, J., Seoane, J., & Wotton, D. (2005) · Genes & Development · doi:10.1101/gad.1350705 · Cited by 2,432 · see citing works
Targets for Cell Cycle Arrest by the Immunosuppressant Rapamycin in Yeast
Heitman, J., Movva, N. R., & Hall, M. N. (1991) · Science · doi:10.1126/science.1715094 · Cited by 2,010 · see citing works
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 · see citing works
Identification of Smad7, a TGFβ-inducible antagonist of TGF-β signalling
Nakao, A., Afrakhte, M., Morn, A., Nakayama, T., Christian, J. L., Heuchel, R. L., Itoh, S., Kawabata, M., Heldin, N., Heldin, C., et al. (1997) · Nature · doi:10.1038/39369 · Cited by 1,796 · see citing works
The Spemann Organizer Signal noggin Binds and Inactivates Bone Morphogenetic Protein 4
Zimmerman, L. B., Jesús-Escobar, J. M. D., & Harland, R. M. (1996) · Cell · doi:10.1016/s0092-8674(00)80133-6 · Cited by 1,639 · 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
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 · see citing works
Hayashi, H., Abdollah, S., Qiu, Y., Cai, J., Xu, Y., Grinnell, B. W., Richardson, M. A., Topper, J. N., Gimbrone, M. A., Wrana, J. L., et al. (1997) · Cell · doi:10.1016/s0092-8674(00)80303-7 · Cited by 1,322 · see citing works
Mutations in <i>myostatin</i> ( <i>GDF8</i> ) in Double-Muscled Belgian Blue and Piedmontese Cattle
Kambadur, R., Sharma, M., Smith, T. P. L., & Bass, J. J. (1997) · Genome Research · doi:10.1101/gr.7.9.910 · Cited by 1,204 · see citing works
Chung, J., Kuo, C. J., Crabtree, G. R., & Blenis, J. (1992) · Cell · doi:10.1016/0092-8674(92)90643-q · Cited by 1,151 · see citing works
Smad6 inhibits signalling by the TGF-β superfamily
Imamura, T., Takase, M., Nishihara, A., Oeda, E., Hanai, J., Kawabata, M., & Miyazono, K. (1997) · Nature · doi:10.1038/39355 · Cited by 1,023 · 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
Functional improvement of dystrophic muscle by myostatin blockade
Bogdanovich, S., Krag, T. O. B., Barton, E. R., Morris, L. D., Whittemore, L.-A., Ahima, R. S., & Khurana, T. S. (2002) · Nature · doi:10.1038/nature01154 · Cited by 831 · see citing works
Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size
Trendelenburg, A. U., Meyer, A., Rohner, D., Boyle, J., Hatakeyama, S., & Glass, D. J. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00105.2009 · Cited by 792 · see citing works
Fischle, W., Dequiedt, F., Hendzel, M. J., Guenther, M. G., Lazar, M. A., Voelter, W., & Verdin, E. (2002) · Molecular Cell · doi:10.1016/s1097-2765(01)00429-4 · Cited by 754 · see citing works
Musarò, A., McCullagh, K. J. A., Naya, F. J., Olson, E. N., & Rosenthal, N. A. (1999) · Nature · doi:10.1038/23060 · Cited by 652 · see citing works
Systemic delivery of genes to striated muscles using adeno-associated viral vectors
Gregorevic, P., Blankinship, M. J., Allen, J. M., Crawford, R. W., Meuse, L., Miller, D. G., Russell, D. W., & Chamberlain, J. S. (2004) · Nature Medicine · doi:10.1038/nm1085 · Cited by 620 · see citing works
Self-citationCohen, S., Brault, J. J., Gygi, S. P., Glass, D. J., Valenzuela, D. M., Gartner, C. A., Latres, E., & Goldberg, A. L. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200901052 · Cited by 584 · see citing works
Rebbapragada, A., Benchabane, H., Wrana, J. L., Celeste, A. J., & Attisano, L. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7230-7242.2003 · Cited by 566 · see citing works
Smad2 and 3 transcription factors control muscle mass in adulthood
Sartori, R., Milan, G., Patron, M., Mammucari, C., Blaauw, B., Abraham, R., & Sandri, M. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00104.2009 · Cited by 517 · see citing works
Latres, E., Amini, A. R., Amini, A. A., Griffiths, J. S., Martin, F. J., Wei, Y., Lin, H. C., Yancopouloš, G., & Glass, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m407517200 · Cited by 514 · see citing works
Rapamycin Attenuates Load-Induced Cardiac Hypertrophy in Mice
Shioi, T., McMullen, J., Tarnavski, O., Converso, K., Sherwood, M., Manning, W., & Izumo, S. (2003) · Circulation · doi:10.1161/01.cir.0000057979.36322.88 · Cited by 482 · see citing works
Self-citationBMP signaling controls muscle mass
Sartori, R., Schirwis, E., Blaauw, B., Bortolanza, S., Zhao, J., Enzo, E., Stantzou, A., Mouisel, E., Toniolo, L., Ferry, A., et al. (2013) · Nature Genetics · doi:10.1038/ng.2772 · Cited by 467 · see citing works
Myogenin and Class II HDACs Control Neurogenic Muscle Atrophy by Inducing E3 Ubiquitin Ligases
Moresi, V., Williams, A. H., Meadows, E., Flynn, J. M., Potthoff, M. J., McAnally, J., Shelton, J. M., Backs, J., Klein, W. H., Richardson, J. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.09.004 · Cited by 445 · see citing works
Lateral and Axial Signals Involved in Avian Somite Patterning: A Role for BMP4
Pourquié, O., Fan, C., Coltey, M., Hirsinger, E., 渡邉, 裕., Bréant, C., Francis‐West, P. H., Brickell, P. M., Tessier‐Lavigne, M., & Douarin, N. M. L. (1996) · Cell · doi:10.1016/s0092-8674(00)81291-x · Cited by 422 · see citing works
Histone deacetylase degradation andMEF2 activation promote the formation of slow-twitch myofibers
Potthoff, M. J., Wu, H., Arnold, M., Shelton, J. M., Backs, J., McAnally, J., Richardson, J. A., Bassel‐Duby, R., & Olson, E. N. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31960 · Cited by 416 · see citing works
McCabe, B. D., Marqués, G., Haghighi, A. P., Fetter, R. D., Crotty, M. L., Haerry, T. E., Goodman, C. S., & O’Connor, M. B. (2003) · Neuron · doi:10.1016/s0896-6273(03)00426-4 · Cited by 390 · see citing works
Quadrupling Muscle Mass in Mice by Targeting TGF-ß Signaling Pathways
Lee, S.-J. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000789 · Cited by 316 · see citing works
Smad6 Is a Smad1/5-induced Smad Inhibitor
Ishida, W., Hamamoto, T., Kusanagi, K., Yagi, K., Kawabata, M., Takehara, K., Sampath, T. K., Kato, M., & Miyazono, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.9.6075 · 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
Ibebunjo, C., Chick, J. M., Kendall, T., Eash, J. K., Li, C., Zhang, Y., Vickers, C., Wu, Z., Clarke, B. A., Shi, J., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01036-12 · Cited by 267 · see citing works
TGF-β Regulates miR-206 and miR-29 to Control Myogenic Differentiation through Regulation of HDAC4
Winbanks, C. E., Wang, B., Beyer, C., Koh, P., White, L. J., Kantharidis, P., & Gregorevic, P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.192625 · Cited by 265 · see citing works
Self-citationPescatori, M., Broccolini, A., Minetti, C., Bertini, E., Bruno, C., D’Amico, A., Bernardini, C., Massimiliano Mirabella, A., Silvestri, G., Giglio, V., et al. (2007) · The FASEB Journal · doi:10.1096/fj.06-7285com · Cited by 243 · see citing works
Holley, S. A., Neul, J. L., Attisano, L., Wrana, J. L., Sasai, Y., O’Connor, M. B., Robertis, E. M. D., & Ferguson, E. L. (1996) · Cell · doi:10.1016/s0092-8674(00)80134-8 · Cited by 239 · see citing works
Cloning of a Second Type of Activin Receptor and Functional Characterization in Xenopus Embryos
Mathews, L. S., Vale, W., & Kintner, C. R. (1992) · Science · doi:10.1126/science.1313188 · Cited by 221 · see citing works
Yamamoto, N., Akiyama, S., Katagiri, T., Namiki, M., Kurokawa, T., & Suda, T. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7325 · Cited by 219 · 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
Self-citationForced expression of dystrophin deletion constructs reveals structure-function correlations.
Rafael, J. A., Cox, G. A., Corrado, K., Jung, D., Campbell, K. P., & Chamberlain, J. S. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.134.1.93 · Cited by 184 · see citing works
The importance of timing differentiation during limb muscle development
Amthor, H., Christ, B., Weil, M., & Patel, K. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70251-9 · Cited by 169 · see citing works
Ball, R. W., Warren-Paquin, M., Tsurudome, K., Liao, E. H., Elazzouzi, F., Cavanagh, C., An, B., Wang, T. T., White, J. H., & Haghighi, A. P. (2010) · Neuron · doi:10.1016/j.neuron.2010.04.011 · Cited by 153 · see citing works
A Single Residue of GDF-5 Defines Binding Specificity to BMP Receptor IB
Nickel, J., Kotzsch, A., Sebald, W., & Mueller, T. D. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.04.015 · Cited by 152 · see citing works
Sako, D., Grinberg, A. V., Liu, J., Davies, M. V., Castonguay, R., Maniatis, S., Andreucci, A. J., Pobre, E. G., Tomkinson, K. N., Monnell, T. E., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.114959 · Cited by 152 · see citing works
Tang, H., Macpherson, P. C. D., Marvin, M. C., Meadows, E., Klein, W. H., Yang, X., & Goldman, D. J. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-07-0759 · Cited by 142 · see citing works
Ochala, J., Gustafson, A., Llano‐Diez, M., Renaud, G., Li, M., Aare, S., Qaisar, R., Banduseela, V. C., Hedström, Y., Tang, X., et al. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2010.202044 · Cited by 139 · see citing works
Self-citationKatagiri, T., Akiyama, S., Namiki, M., Komaki, M., Yamaguchi, A., Rosen, V., Wozney, J. M., Fujisawa‐Sehara, A., & Suda, T. (1997) · Experimental Cell Research · doi:10.1006/excr.1996.3432 · Cited by 139 · see citing works
Amthor, H., Christ, B., Rashid‐Doubell, F., Kemp, C. F., Lang, E., & Patel, K. (2002) · Developmental Biology · doi:10.1006/dbio.2001.0555 · Cited by 136 · see citing works
Townsend, K. L., Suzuki, R., Huang, T. L., Jing, E., Schulz, T. J., Lee, K., Taniguchi, C. M., Espinoza, D. O., McDougall, L. E., Zhang, H., et al. (2012) · The FASEB Journal · doi:10.1096/fj.11-199067 · Cited by 105 · see citing works
Gronroos, E. C., Kingston, I. J., Ramachandran, A., Randall, R. A., Vizán, P., & Hill, C. S. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00231-12 · Cited by 99 · see citing works
Bayat, V., Jaiswal, M., & Bellen, H. J. (2010) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2010.08.014 · Cited by 98 · see citing works
Molecular cloning and binding properties of the human type II activin receptor
Donaldson, C. J., Mathews, L. S., & Vale, W. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91194-u · Cited by 84 · see citing works
Clever, J. L., Sakai, Y., Wang, R. A., & Schneider, D. B. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00388.2009 · Cited by 61 · see citing works
Kalista, S., Schakman, O., Gilson, H., Lause, P., Demeulder, B., Bertrand, L., Pende, M., & Thissen, J. (2011) · Endocrinology · doi:10.1210/en.2011-1687 · Cited by 58 · see citing works
BMPs are mediators in tissue crosstalk of the regenerating musculoskeletal system
Ruschke, K., Hiepen, C., Becker, J., & Knaus, P. I. (2012) · Cell and Tissue Research · doi:10.1007/s00441-011-1283-6 · Cited by 55 · see citing works
Langenfeld, E. M., Kong, Y., & Langenfeld, J. E. (2005) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-05-0124 · Cited by 52 · see citing works
Learning of physiological responses: I. Habituation, sensitization, and classical conditioning.
Dworkin, B. R., & Dworkin, S. (1990) · Behavioral Neuroscience · doi:10.1037//0735-7044.104.2.298 · Cited by 50 · see citing works
Learning of physiological responses: I. Habituation, sensitization, and classical conditioning.
Dworkin, B. R., & Dworkin, S. (1990) · Behavioral Neuroscience · doi:10.1037/0735-7044.104.2.298 · Cited by 49 · see citing works
Suryawan, A., Frank, J. W., Nguyen, H. V., & Davis, T. A. (2006) · Pediatric Research · doi:10.1203/01.pdr.0000196718.47935.6e · Cited by 42 · see citing works
Baroreflexes of the rat. III. Open-loop gain and electroencephalographic arousal
Dworkin, B. R., & Dworkin, S. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00469.2003 · Cited by 35 · see citing works
(2012) · The Medical Journal of Australia · doi:10.5694/mja12.10667 · Cited by 1 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Sarcopenia: Aging-Related Loss of Muscle Mass and Function
Larsson, L., Degens, H., Li, M., Salviati, L., Lee, Y. I., Thompson, W., Kirkland, J. L., & Sandri, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00061.2017 · Cited by 1,797 · see citing works
Self-citationBone Morphogenetic Protein (BMP) signaling in development and human diseases
Wang, R. N., Green, J. J., Wang, Z., Deng, Y., Qiao, M., Peabody, M., Zhang, Q., Ye, J., Yan, Z., Denduluri, S. K., et al. (2014) · Genes & Diseases · doi:10.1016/j.gendis.2014.07.005 · Cited by 1,036 · 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
Bone Morphogenetic ProteinsPreprint
Katagiri, T., & Watabe, T. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021899 · Cited by 533 · see citing works
BMP signaling controls muscle mass
Sartori, R., Schirwis, E., Blaauw, B., Bortolanza, S., Zhao, J., Enzo, E., Stantzou, A., Mouisel, E., Toniolo, L., Ferry, A., et al. (2013) · Nature Genetics · doi:10.1038/ng.2772 · Cited by 467 · see citing works
Mechanisms Regulating Neuromuscular Junction Development and Function and Causes of Muscle Wasting
Tintignac, L. A. J., Brenner, H.-R., & Rüegg, M. A. (2015) · Physiological Reviews · doi:10.1152/physrev.00033.2014 · Cited by 422 · see citing works
DRP1-mediated mitochondrial shape controls calcium homeostasis and muscle mass
Favaro, G., Romanello, V., Varanita, T., Andrea Desbats, M., Morbidoni, V., Tezze, C., Albiero, M., Canato, M., Gherardi, G., De Stefani, D., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10226-9 · Cited by 398 · see citing works
Cancer cachexia: molecular mechanisms and treatment strategies
Setiawan, T., Sari, I. N., Wijaya, Y., Julianto, N. M., Muhammad, J. A., Lee, H.-Y., Ji, H.-O.-C., & Kwon, H. (2023) · Journal of Hematology & Oncology · doi:10.1186/s13045-023-01454-0 · Cited by 300 · see citing works
Bone morphogenetic protein receptor signal transduction in human disease
Gomez‐Puerto, M. C., Iyengar, P. V., de Vinuesa, A. G., ten Dijke, P., & Sánchez‐Duffhues, G. (2018) · The Journal of Pathology · doi:10.1002/path.5170 · Cited by 239 · see citing works
Signaling Pathways That Control Muscle Mass
Vainshtein, A., & Sandri, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134759 · Cited by 213 · see citing works
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
Exercise-Induced Myokines With Therapeutic Potential for Muscle Wasting
Piccirillo, R. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00287 · Cited by 190 · see citing works
Sarcopenia – The search for emerging biomarkers
Kalinkovich, A., & Livshits, G. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.05.001 · Cited by 187 · see citing works
Efficient myotube formation in 3D bioprinted tissue construct by biochemical and topographical cues
Kim, W., Lee, H., Lee, J., Atala, A., Yoo, J. J., Lee, S. J., & Kim, G. H. (2020) · Biomaterials · doi:10.1016/j.biomaterials.2019.119632 · Cited by 185 · see citing works
TGFβ and BMP signaling in skeletal muscle: potential significance for muscle-related disease
Sartori, R., Gregorevic, P., & Sandri, M. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2014.06.002 · Cited by 177 · see citing works
Self-citationMolecular Mechanisms of Skeletal Muscle Hypertrophy
Schiaffino, S., Reggiani, C., Akimoto, T., & Blaauw, B. (2020) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-200568 · Cited by 169 · see citing works
Uezumi, A., Ikemoto‐Uezumi, M., Zhou, H., Kurosawa, T., Yoshimoto, Y., Nakatani, M., Hitachi, K., Yamaguchi, H., Wakatsuki, S., Araki, T., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci139617 · Cited by 166 · see citing works
The Hippo pathway effector YAP is a critical regulator of skeletal muscle fibre size
Watt, K. I., Turner, B. J., Hagg, A., Zhang, X., Davey, J. R., Qian, H., Beyer, C., Winbanks, C. E., Harvey, K. F., & Gregorevic, P. (2015) · Nature Communications · doi:10.1038/ncomms7048 · Cited by 164 · see citing works
Self-citationPerturbed BMP signaling and denervation promote muscle wasting in cancer cachexia
Sartori, R., Hagg, A., Zampieri, S., Armani, A., Winbanks, C. E., Viana, L. R., Haidar, M., Watt, K. I., Qian, H., Pezzini, C., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.aay9592 · Cited by 158 · see citing works
Self-citationMorvan, F., Rondeau, J.-M., Zou, C., Minetti, G., Scheufler, C., Scharenberg, M., Jacobi, C., Brebbia, P., Ritter, V., Toussaint, G., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707925114 · Cited by 142 · 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 · see citing works
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 123 · 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
Kwon, J. H., Moon, K. M., & Min, K.-W. (2020) · Healthcare · doi:10.3390/healthcare8040378 · Cited by 116 · see citing works
S6K1 Is Required for Increasing Skeletal Muscle Force during Hypertrophy
Marabita, M., Baraldo, M., Solagna, F., Ceelen, J., Sartori, R., Nolte, H., Nemazanyy, I., Pyronnet, S., Krüger, M., Pende, M., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.020 · Cited by 116 · see citing works
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 · see citing works
Self-citationSupraphysiological 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 115 · see citing works
Myostatin/Activin Receptor Ligands in Muscle and the Development Status of Attenuating Drugs
Rodgers, B. D., & Ward, C. W. (2022) · Endocrine Reviews · doi:10.1210/endrev/bnab030 · Cited by 111 · see citing works
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 108 · see citing works
Cancer cachexia: multilevel metabolic dysfunction
Díaz, M. B., Rohm, M., & Herzig, S. (2024) · Nature Metabolism · doi:10.1038/s42255-024-01167-9 · Cited by 109 · see citing works
Receptor binding competition: A paradigm for regulating TGF-β family action
Martı́nez-Hackert, E., Sundan, A., & Holien, T. (2020) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2020.09.003 · Cited by 90 · see citing works
Follistatin is critical for mouse uterine receptivity and decidualization
Fullerton, P. T., Monsivais, D., Kommagani, R., & Matzuk, M. M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620903114 · Cited by 89 · see citing works
Ubiquitin Ligases at the Heart of Skeletal Muscle Atrophy Control
Peris-Moreno, D., Cussonneau, L., Combaret, L., Polge, C., & Taillandier, D. (2021) · Molecules · doi:10.3390/molecules26020407 · Cited by 87 · see citing works
Myostatin: a skeletal muscle chalone
Lee, S.-J. (2023) · Annual Review of Physiology · doi:10.1146/annurev-physiol-012422-112116 · Cited by 84 · see citing works
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 84 · see citing works
Bone Morphogenetic Protein–Based Therapeutic ApproachesPreprint
Lowery, J. W., & Rosen, V. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022327 · Cited by 84 · see citing works
Gaur, V., Connor, T., Sanigorski, A. J., Martin, S. D., Bruce, C. R., Henstridge, D. C., Bond, S. T., McEwen, K. A., Kerr-Bayles, L., Ashton, T. D., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.08.005 · Cited by 77 · see citing works
Self-citationThe 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 76 · see citing works
Self-citationActivation of Akt–mTORC1 signalling reverts cancer‐dependent muscle wasting
Geremia, A., Sartori, R., Baraldo, M., Nogara, L., Balmaceda, V., Dumitras, A. G., Ciciliot, S., Scalabrin, M., Nolte, H., & Blaauw, B. (2021) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12854 · Cited by 75 · see citing works
Decoding the transcriptome of denervated muscle at single‐nucleus resolution
Lin, H., Ma, X., Sun, Y., Peng, H., Wang, Y., Thomas, S. S., & Hu, Z. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13023 · Cited by 69 · see citing works
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 67 · see citing works
Novel myostatin-specific antibody enhances muscle strength in muscle disease models
Muramatsu, H., Kuramochi, T., Katada, H., Ueyama, A., Ruike, Y., Ohmine, K., Shida-Kawazoe, M., Miyano-Nishizawa, R., Shimizu, Y., Okuda, M., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-81669-8 · Cited by 61 · see citing works
Schreiber, I., Dörpholz, G., Ott, C., Kragesteen, B. K., Schanze, N., Lee, C. T., Köhrle, J., Mundlos, S., Ruschke, K., & Knaus, P. I. (2017) · Scientific Reports · doi:10.1038/s41598-017-17595-5 · Cited by 63 · see citing works
Loss of BMPR2 leads to high bone mass due to increased osteoblast activity
Lowery, J. W., Intini, G., Gamer, L. W., Lotinun, S., Salazar, V. S., Ohte, S., Cox, K. A., Baron, R., & Rosen, V. (2015) · Journal of Cell Science · doi:10.1242/jcs.156737 · Cited by 58 · see citing works
Penna, F., Baccino, F. M., & Costelli, P. (2014) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000048 · Cited by 58 · see citing works
Yang, Y., Yan, J., Fan, X., Chen, J., Wang, Z., Liu, X., Yi, G., Liu, Y., Niu, Y., Zhang, L., et al. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009910 · Cited by 55 · see citing works
Self-citationlncRNA Chronos is an aging-induced inhibitor of muscle hypertrophy
Neppl, R. L., Wu, C., & Walsh, K. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201612100 · Cited by 54 · see citing works
Abnormal Activation of BMP Signaling Causes Myopathy in Fbn2 Null Mice
Sengle, G., Carlberg, V. M., Tufa, S. F., Charbonneau, N. L., Smaldone, S., Carlson, E. J., Ramirez, F., Keene, D. R., & Sakai, L. Y. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005340 · Cited by 54 · see citing works
The Composition, Development, and Regeneration of Neuromuscular Junctions
Liu, W., & Chakkalakal, J. V. (2017) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2017.08.005 · Cited by 52 · see citing works
Davey, J. R., Watt, K. I., Parker, B. L., Chaudhuri, R., Ryall, J. G., Cunningham, L., Qian, H., Sartorelli, V., Sandri, M., Chamberlain, J., et al. (2016) · JCI Insight · doi:10.1172/jci.insight.85477 · Cited by 51 · see citing works
Self-citationInhibition of GDF8 (Myostatin) accelerates bone regeneration in diabetes mellitus type 2
Wallner, C., Jaurich, H., Wagner, J. M., Becerikli, M., Harati, K., Dadras, M., Lehnhardt, M., & Behr, B. (2017) · Scientific Reports · doi:10.1038/s41598-017-10404-z · Cited by 50 · see citing works
Si, Y., Kim, S., Cui, X., Zheng, L., Oh, S. J., Anderson, T., Alsharabati, M., Kazamel, M., Volpicelli‐Daley, L. A., Bamman, M. M., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0138425 · Cited by 48 · see citing works
Skeletal muscle reprogramming enhances reinnervation after peripheral nerve injury
Mehrotra, P., Jablonski, J., Toftegaard, J., Zhang, Y., Shahini, S., Wang, J., Hung, C. W., Ellis, R., Kayal, G., Rajabian, N., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-53276-4 · Cited by 47 · see citing works
Muscle aging and sarcopenia: The pathology, etiology, and most promising therapeutic targets
Grima-Terrén, M., Campanario, S., Ramírez‐Pardo, I., Cisneros, A., Hong, X., Perdiguero, E., Serrano, A. L., Isern, J., & Muñoz‐Cánoves, P. (2024) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2024.101319 · Cited by 49 · see citing works
BMPs and the muscle–bone connection
Sartori, R., & Sandri, M. (2015) · Bone · doi:10.1016/j.bone.2015.05.023 · Cited by 45 · see citing works
Molecular Mechanisms of Skeletal Muscle Atrophy in a Mouse Model of Cerebral Ischemia
Desgeorges, M. M., Devillard, X., Toutain, J., Divoux, D., Castells, J., Bernaudin, M., Touzani, O., & Freyssenet, D. G. (2015) · Stroke · doi:10.1161/strokeaha.114.008574 · Cited by 44 · see citing works
Huang, P., Schulz, T. J., Beauvais, A., Tseng, Y., & Gussoni, E. (2014) · Nature Communications · doi:10.1038/ncomms5063 · Cited by 44 · see citing works
The Role of TGFβ in Bone-Muscle Crosstalk
Regan, J. N., Trivedi, T., Guise, T. A., & Waning, D. L. (2017) · Current Osteoporosis Reports · doi:10.1007/s11914-017-0344-5 · Cited by 44 · see citing works
Rindom, E., & Vissing, K. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00547 · Cited by 43 · see citing works
Hoogaars, W. M. H., & Jaspers, R. T. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-1435-3_8 · Cited by 42 · see citing works
Bone Morphogenetic Proteins and myostatin pathways: key mediator of human sarcopenia
Scimeca, M., Piccirilli, E., Mastrangeli, F., Rao, C., Feola, M., Orlandi, A., Gasbarra, E., Bonanno, E., & Tarantino, U. (2017) · Journal of Translational Medicine · doi:10.1186/s12967-017-1143-6 · Cited by 41 · see citing works
Shero, J. A., Lindholm, M. E., Sandri, M. F., & Stanford, K. I. (2025) · Circulation Research · doi:10.1161/circresaha.124.325614 · Cited by 43 · see citing works
MuSK is a BMP co-receptor that shapes BMP responses and calcium signaling in muscle cells
Yilmaz, A., Kattamuri, C., Özdeşlik, R. N., Schmiedel, C., Mentzer, S., Schorl, C., Oancea, E., Thompson, T. B., & Fallon, J. R. (2016) · Science Signaling · doi:10.1126/scisignal.aaf0890 · Cited by 39 · see citing works
Role of IGF-I in follistatin-induced skeletal muscle hypertrophy
Barbé, C., Kalista, S., Loumaye, A., Ritvos, O., Lause, P., Ferracin, B., & Thissen, J. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00098.2015 · Cited by 38 · see citing works
Morel, J., Palao, J.-C., Castells, J., Desgeorges, M. M., Busso, T., Molliex, S. B., Jahnke, V. E., del Carmine, P., Gondin, J., Arnould, D., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-11440-5 · Cited by 38 · see citing works
An embryonic CaVβ1 isoform promotes muscle mass maintenance via GDF5 signaling in adult mouse
Traoré, M., Gentil, C., Benedetto, C., Hogrel, J.-Y., De la Grange, P., Cadot, B., Benkhelifa-Ziyyat, S., Julien, L., Lemaitre, M., Ferry, A., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aaw1131 · Cited by 36 · see citing works
La, L., Jiang, Y., Lin, H., Shen, H., Sohn, J., Alexander, P. G., & Tuan, R. S. (2019) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2019.06.001 · Cited by 36 · see citing works
Hitachi, K., Nakatani, M., Funasaki, S., Hijikata, I., Maekawa, M., Honda, M., & Tsuchida, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051628 · Cited by 35 · see citing works
Stanley, A., Tichy, E. D., Kocan, J., Roberts, D. W., Shore, E. M., & Mourkioti, F. (2022) · npj Regenerative Medicine · doi:10.1038/s41536-021-00201-8 · Cited by 35 · see citing works
Multiple MuSK signaling pathways and the aging neuromuscular junction
Fish, L. A., & Fallon, J. R. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.135014 · Cited by 34 · see citing works
Wischnewski, S., Thäwel, T., Ikenaga, C., Kocharyan, A., Lerma-Martin, C., Zulji, A., Rausch, H.-W., Brenner, D., Thomas, L., Kutza, M., et al. (2024) · Nature Aging · doi:10.1038/s43587-024-00645-9 · Cited by 31 · see citing works
Body Size and Tissue-Scaling Is Regulated by Motoneuron-Derived Activinß in Drosophila melanogaster
Moss-Taylor, L., Upadhyay, A., Pan, X., Kim, M.-J., & O’Connor, M. B. (2019) · Genetics · doi:10.1534/genetics.119.302394 · Cited by 33 · see citing works
Kim, J., Lee, Y., & Yi, H. (2016) · Experimental Physiology · doi:10.1113/ep085852 · Cited by 32 · see citing works
Lowery, J. W., Brookshire, B., & Rosen, V. (2016) · Stem Cells International · doi:10.1155/2016/7290686 · Cited by 31 · see citing works
Agarwal, S., Cholok, D. J., Loder, S. J., Li, J., Breuler, C. J., Chung, M. T., Hsieh, H. H. S., Ranganathan, K., Habbouche, J. A., Drake, J., et al. (2016) · JCI Insight · doi:10.1172/jci.insight.89805 · Cited by 31 · see citing works
Protective Role of Testicular Hormone INSL3 From Atrophy and Weakness in Skeletal Muscle
Ferlin, A., Toni, L. D., Agoulnik, A. I., Lunardon, G., Armani, A., Bortolanza, S., Blaauw, B., Sandri, M., & Foresta, C. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00562 · Cited by 31 · see citing works
Lau, P., Vico, L., & Rittweger, J. (2022) · Biomedicines · doi:10.3390/biomedicines10020342 · Cited by 32 · see citing works
Identification of genome‐wide selection signatures in the L imousin beef cattle breed
Gurgul, A., Szmatoła, T., Ropka‐Molik, K., Jasielczuk, I., Pawlina‐Tyszko, K., Semik, E., & Bugno‐Poniewierska, M. (2015) · Journal of Animal Breeding and Genetics · doi:10.1111/jbg.12196 · Cited by 31 · see citing works
Pasteuning-Vuhman, S., der Meulen, J. W. B.-V., van Putten, M., Overzier, M., ten Dijke, P., Kiełbasa, S. M., Arindrarto, W., Wolterbeek, R., Lezhnina, K. V., Ozerov, I. V., et al. (2016) · The FASEB Journal · doi:10.1096/fj.201600675r · Cited by 31 · see citing works
New roles for Smad signaling and phosphatidic acid in the regulation of skeletal muscle mass
Goodman, C. A., & Hornberger, T. A. (2014) · F1000Prime Reports · doi:10.12703/p6-20 · Cited by 30 · see citing works
Molecular Mechanisms of Cachexia: A Review
Neshan, M., Tsilimigras, D. I., Han, X., Hua Zhu, C., & Pawlik, T. M. (2024) · Cells · doi:10.3390/cells13030252 · Cited by 30 · see citing works
Growth factor treatment to overcome Alzheimer's dysfunctional signaling
Lauzon, M.-A., Daviau, A., Marcos, B., & Faucheux, N. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.02.018 · Cited by 30 · see citing works
Kuppusamy, P., Soundharrajan, I., Kim, D., Hwang, I., & Choi, K. C. (2019) · Phytomedicine · doi:10.1016/j.phymed.2019.152873 · Cited by 29 · see citing works
Davies, O. G., Liu, Y., Player, D. J., Martin, N. R. W., Grover, L. M., & Lewis, M. P. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00194 · Cited by 29 · see citing works
Self-citationMay, R. D., Frauchiger, D. A., Albers, C. E., Tekari, A., Benneker, L. M., Klenke, F. M., Hofstetter, W., & Gantenbein, B. (2019) · Current Stem Cell Research & Therapy · doi:10.2174/1574888x14666190628103528 · Cited by 28 · see citing works
Role of MicroRNAs and Long Non-Coding RNAs in Sarcopenia
Lee, J., & Kang, H. (2022) · Cells · doi:10.3390/cells11020187 · Cited by 28 · see citing works
Roy, A., & Kumar, A. (2022) · Nature Communications · doi:10.1038/s41467-022-29752-0 · Cited by 28 · see citing works
Follistatin-like 1 and its paralogs in heart development and cardiovascular disease
Horak, M., Fairweather, D., Kokkonen, P., Bednář, D., & Vašků, J. B. (2022) · Heart Failure Reviews · doi:10.1007/s10741-022-10262-6 · Cited by 28 · see citing works
IRS4, a novel modulator of BMP/Smad and Akt signalling during early muscle differentiation
Dörpholz, G., Murgai, A., Jatzlau, J., Horbelt, D., Belverdi, M. P., Heroven, C., Schreiber, I., Wendel, G., Ruschke, K., Stricker, S., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-08676-6 · Cited by 26 · see citing works
Bu-M-P-ing Iron: How BMP Signaling Regulates Muscle Growth and Regeneration
Borok, M. J., Mademtzoglou, D., & Relaix, F. (2020) · Journal of Developmental Biology · doi:10.3390/jdb8010004 · Cited by 26 · see citing works
Re-evaluation of the myoepithelial cells roles in the breast cancer progression
Shams, A. M. (2022) · Cancer Cell International · doi:10.1186/s12935-022-02829-y · Cited by 26 · see citing works
Bone Tissue as a Systemic Endocrine Regulator
Zofkova, I. (2015) · Physiological Research · doi:10.33549/physiolres.932900 · Cited by 25 · see citing works
Cussonneau, L., Boyer, C., Brun, C., Deval, C., Loizon, E., Meugnier, E., Guéret, É., Dubois, E., Taillandier, D., Polge, C., et al. (2021) · Cells · doi:10.3390/cells10081873 · Cited by 25 · see citing works
Pathophysiology and Emerging Molecular Therapeutic Targets in Heterotopic Ossification
Felix-Ilemhenbhio, F., Pickering, G. A. E., Kiss‐Toth, E., & Wilkinson, J. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23136983 · Cited by 26 · see citing works
Genetic Diversity and Selective Signature in Dabieshan Cattle Revealed by Whole-Genome Resequencing
Guan, X., Zhao, S., Xiang, W., Jin, H., Chen, N., Lei, C., Jia, Y., & Xu, L. (2022) · Biology · doi:10.3390/biology11091327 · Cited by 25 · see citing works
Smads as muscle biomarkers in amyotrophic lateral sclerosis
Si, Y., Cui, X., Kim, S., Wians, R., Sorge, R. E., Oh, S. J., Kwan, T., Alsharabati, M., Lu, L., Claussen, G. C., et al. (2014) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.117 · Cited by 25 · see citing works
Novel mutations in BMP1 induce a rare type of osteogenesis imperfecta
Xu, X., Lv, F., Song, Y., Li, L., Asan, Wei, X., Zhao, X., Jiang, Y., Wang, O., Xing, X., et al. (2018) · Clinica Chimica Acta · doi:10.1016/j.cca.2018.11.004 · Cited by 25 · see citing works
Morphological association between the muscles and bones in the craniofacial region
Yamamoto, M., Takada, H., Ishizuka, S., Kitamura, K., Jeong, J., Sato, M., Hinata, N., & Abe, S. (2020) · PLoS ONE · doi:10.1371/journal.pone.0227301 · Cited by 24 · see citing works
Myokines in Appetite Control and Energy Balance
Grannell, A., Kokkinos, A. D., & le Roux, C. W. (2022) · Muscles · doi:10.3390/muscles1010003 · Cited by 23 · see citing works
Extracellular matrilin-2 deposition controls the myogenic program timing during muscle regeneration
Deák, F., Mátés, L., Korpos, É., Zvara, Á., Szénási, T., Kiricsi, M., Mendler, L., Keller-Pintér, A., Ózsvári, B., Juhász, H., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.141556 · Cited by 23 · see citing works
- Authors
- Winbanks, C. E., Chen, J. L., Qian, H., Liu, Y., Bernardo, B. C., Beyer, C., Watt, K. I., Thomson, R. E., Connor, T., Turner, B. J., McMullen, J. R., Larsson, L., McGee, S. L., Harrison, C. A., & Gregorevic, P.
- Affiliations
- Baker Heart and Diabetes Institute (AU)
- Deakin University (AU)
- The University of Melbourne (AU)
- Uppsala University Hospital (SE)
- Monash University (AU)
- Corresponding author
- Gregorevic, Paul
- ORCID
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2013-10-21
- Volume
- 203
- Issue
- 2
- Pages
- 345-357
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC3812980
- OpenAlex
- W2154241781
- Cited by
- 225
- References
- 62
- Citations by year
- 2026: 9 · 2025: 18 · 2024: 23 · 2023: 16 · 2022: 21 · 2021: 20 · 2020: 17 · 2019: 15 · 2018: 12 · 2017: 17 · 2016: 17 · 2015: 23 · 2014: 14 · 2013: 3
- FWCI
- 8.50
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Figshare (submittedVersion, cc-by)
- Minerva Access (University of Melbourne) (submittedVersion, cc-by-nc-sa)
- 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 › Genetics › Neurogenetic and Muscular Disorders Research
- Keywords
- BMP signaling, skeletal muscle mass, muscle hypertrophy, muscle atrophy, denervation-induced atrophy, Smad1/5, mTOR signaling, BMP-7, BMP receptors, HDAC4, myogenin, neuromuscular junction, neuromuscular disorders
- MeSH terms
- Dependovirus, Animals, Disease Models, Animal, Female, Genetic Vectors, Histone Deacetylases, Humans, Hypertrophy, Mice, Inbred C57BL, Muscular Atrophy, Phosphorylation, Transduction, Genetic, Transfection, Genetic Therapy, Signal Transduction, Rats, Sprague-Dawley, Myogenin, Muscle, Skeletal, Muscle Development, Follistatin, Ubiquitin-Protein Ligases, Mice, Rats, Smad Proteins, Bone Morphogenetic Protein Receptors, Type I, Bone Morphogenetic Protein 7, HEK293 Cells, TOR Serine-Threonine Kinases
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
