The DOI matches its Crossref record; 43 of the 44 references it cites were found in a registry or an index.
Myostatin negatively regulates satellite cell activation and self-renewal
Open accessAbstract
Satellite cells are quiescent muscle stem cells that promote postnatal muscle growth and repair. Here we show that myostatin, a TGF-β member, signals satellite cell quiescence and also negatively regulates satellite cell self-renewal. BrdU labeling in vivo revealed that, among the Myostatin-deficient satellite cells, higher numbers of satellite cells are activated as compared with wild type. In contrast, addition of Myostatin to myofiber explant cultures inhibits satellite cell activation. Cell cycle analysis confirms that Myostatin up-regulated p21, a Cdk inhibitor, and decreased the levels and activity of Cdk2 protein in satellite cells. Hence, Myostatin negatively regulates the G1 to S progression and thus maintains the quiescent status of satellite cells. Immunohistochemical analysis with CD34 antibodies indicates that there is an increased number of satellite cells per unit length of freshly isolated Mstn−/− muscle fibers. Determination of proliferation rate suggests that this elevation in satellite cell number could be due to increased self-renewal and delayed expression of the differentiation gene (myogenin) in Mstn−/− adult myoblasts. Taken together, these results suggest that Myostatin is a potent negative regulator of satellite cell activation and thus signals the quiescence of satellite cells.
Overview
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
Verification
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 the citing paper
“The induction of p21 could negatively regulate the G1 to S progression of satellite cells19.”
From In vivo partial reprogramming of myofibers promotes muscle regeneration by remodeling the stem cell niche (2021) · cites this paper as [19]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
Isolation and functional properties of murine hematopoietic stem cells that are replicating in vivo.
Goodell, M. A., Brose, K., Paradis, G. A., Conner, A. N., & Mulligan, R. C. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.4.1797 · Cited by 2,902
Pax7 Is Required for the Specification of Myogenic Satellite Cells
Seale, P., Sabourin, L. A., Girgis-Gabardo, A., Mansouri, A., Gruß, P., & Rudnicki, M. A. (2000) · Cell · doi:10.1016/s0092-8674(00)00066-0 · Cited by 2,345
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
Mutations in myostatin ( GDF8 ) 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
Self-citationMyostatin, a Negative Regulator of Muscle Growth, Functions by Inhibiting Myoblast Proliferation
Thomas, M., Langley, B., Berry, C., Sharma, M., Kirk, S., Bass, J., & Kambadur, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004356200 · Cited by 1,014
Self-citationCornelison, D., & Wold, B. J. (1997) · Developmental Biology · doi:10.1006/dbio.1997.8721 · Cited by 934
Expression of Cd34 and Myf5 Defines the Majority of Quiescent Adult Skeletal Muscle Satellite Cells
Beauchamp, J. R., Heslop, L., Yu, D. S., Tajbakhsh, S., Kelly, R. G., Wernig, A., BUCKINGHAM, M. E., Partridge, T. A., & Zammit, P. S. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.6.1221 · Cited by 917
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
Self-citationFunctional 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
Flagged first, then by citations
1 of the 44 references couldn’t be matched to a known paper.
Research works printed but not linked: 4
- 1989, Med. Sci. Sports Exerc., 21, S164
- 1999, Am. J. Physiol., 277, R601
- 1993, Mol. Cell Biol. Hum. Dis. Ser., 3, 210
- 1997, Methods Mol. Biol., 75, 131
Cited by
Sorted by citations
Myostatin Mutation Associated with Gross Muscle Hypertrophy in a Child
Schuelke, M., Wagner, K. R., Stolz, L. E., Hübner, C., Riebel, T., Kömen, W., Braun, T., Tobin, J. F., & Lee, S.-J. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa040933 · Cited by 1,399
Muscle wasting in disease: molecular mechanisms and promising therapies
Cohen, S., Nathan, J. A., & Goldberg, A. L. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4467 · Cited by 1,089
Reversal of Cancer Cachexia and Muscle Wasting by ActRIIB Antagonism Leads to Prolonged Survival
Zhou, X., Wang, J. L., Lu, J., Song, Y., Kwak, K. S., Jiao, Q., Rosenfeld, R., Chen, Q., Boone, T. C., Simonet, W. S., et al. (2010) · Cell · doi:10.1016/j.cell.2010.07.011 · Cited by 960
REGULATION OF MUSCLE MASS BY MYOSTATIN
Lee, S.-J. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.012103.135836 · Cited by 819
Sarcopenia: etiology, clinical consequences, intervention, and assessment
Lang, T., Streeper, T., Cawthon, P. M., Baldwin, K., Taaffe, D. R., & Harris, T. B. (2009) · Osteoporosis International · doi:10.1007/s00198-009-1059-y · Cited by 815
The Molecular Bases of Training Adaptation
Coffey, V. G., & Hawley, J. A. (2007) · Sports Medicine · doi:10.2165/00007256-200737090-00001 · Cited by 756
Glucocorticoid-Induced Skeletal Muscle Atrophy
Schakman, O., Kalista, S., Barbé, C., Loumaye, A., & Thissen, J. P. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.036 · Cited by 705
Skeletal muscle: A review of molecular structure and function, in health and disease
Mukund, K., & Subramaniam, S. (2019) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1462 · Cited by 805
Notch Signaling Is Necessary to Maintain Quiescence in Adult Muscle Stem Cells
Bjornson, C. R. R., Cheung, T. H., Liu, L., Tripathi, P. V., Steeper, K. M., & Rando, T. A. (2012) · Stem Cells · doi:10.1002/stem.773 · Cited by 598
A review on the mechanisms of blood-flow restriction resistance training-induced muscle hypertrophy
Pearson, S. J., & Hussain, S. R. (2015) · Sports Medicine · doi:10.1007/s40279-014-0264-9 · Cited by 592
Signaling pathways controlling skeletal muscle mass
Egerman, M. A., & Glass, D. J. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.857291 · Cited by 555
Mechanisms of glucocorticoid-induced myopathy
Schakman, O., Gilson, H., & Thissen, J. P. (2008) · Journal of Endocrinology · doi:10.1677/joe-07-0606 · Cited by 521
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
Molecular Signature of Quiescent Satellite Cells in Adult Skeletal Muscle
Fukada, S.-I., Uezumi, A., Ikemoto, M., Masuda, S., Segawa, M., Tanimura, N., Yamamoto, H., Miyagoe-Suzuki, Y., & Takeda, S. (2007) · Stem Cells · doi:10.1634/stemcells.2007-0019 · Cited by 506
Muscle stem cells in development, regeneration, and diseasePreprint
Shi, X., & Garry, D. J. (2006) · Genes & Development · doi:10.1101/gad.1419406 · Cited by 502
Lenk, K., Schuler, G. C., & Adams, V. (2010) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-010-0007-1 · Cited by 498
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 496
Self-citationControl of satellite cell function in muscle regeneration and its disruption in ageing
Sousa-Victor, P., García-Prat, L., & Muñoz-Cánoves, P. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00421-2 · Cited by 476
Dhawan, J., & Rando, T. A. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.10.007 · Cited by 466
New fundamental resistance exercise determinants of molecular and cellular muscle adaptations
Toigo, M., & Boutellier, U. (2006) · European Journal of Applied Physiology · doi:10.1007/s00421-006-0238-1 · Cited by 437
Bowen, T. S., Schuler, G. C., & Adams, V. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12043 · Cited by 445
Cellular and molecular mechanisms underlying age-related skeletal muscle wasting and weakness
Ryall, J. G., Schertzer, J. D., & Lynch, G. S. (2008) · Biogerontology · doi:10.1007/s10522-008-9131-0 · Cited by 423
Wagers, A. J., & Conboy, I. M. (2005) · Cell · doi:10.1016/j.cell.2005.08.021 · Cited by 416
Tissue-Specific Stem Cells: Lessons from the Skeletal Muscle Satellite Cell
Brack, A. S., & Rando, T. A. (2012) · Cell stem cell · doi:10.1016/j.stem.2012.04.001 · Cited by 421
Myostatin and the skeletal muscle atrophy and hypertrophy signaling pathways
Rodriguez, J., Vernus, B., Chelh, I., Cassar-Malek, I., Gabillard, J. C., Hadj Sassi, A., Seiliez, I., Picard, B., & Bonnieu, A. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1689-x · Cited by 397
Differentiation plasticity regulated by TGF-β family proteins in development and disease
Derynck, R., & Akhurst, R. J. (2007) · Nature Cell Biology · doi:10.1038/ncb434 · Cited by 421
Environment and plasticity of myogenesis in teleost fish
Johnston, I. A. (2006) · Journal of Experimental Biology · doi:10.1242/jeb.02153 · Cited by 406
Satellite cells in human skeletal muscle plasticity
Snijders, T., Nederveen, J. P., McKay, B. R., Joanisse, S., Verdijk, L. B., van Loon, L. J. C., & Parise, G. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00283 · Cited by 381
The emerging biology of satellite cells and their therapeutic potential
Kuang, S., & Rudnicki, M. A. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.12.004 · Cited by 351
Regulatory factors and cell populations involved in skeletal muscle regeneration
Broek, R. W. T., Grefte, S., & den Hoff, J. W. V. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22127 · Cited by 315
Zhang, L., Rajan, V., Lin, E., Hu, Z., Han, H. Q., Zhou, X., Song, Y., Min, H., Wang, X., Du, J., et al. (2011) · The FASEB Journal · doi:10.1096/fj.10-176917 · Cited by 323
Myostatin/activin pathway antagonism: molecular basis and therapeutic potential
Han, H. Q., Zhou, X., Mitch, W. E., & Goldberg, A. L. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.019 · Cited by 314
Advances in signaling in vertebrate regeneration as a prelude to regenerative medicinePreprint
Stoick-Cooper, C. L., Moon, R. T., & Weidinger, G. (2007) · Genes & Development · doi:10.1101/gad.1540507 · Cited by 309
Shan, T., Liang, X., Bi, P., & Kuang, S. (2013) · The FASEB Journal · doi:10.1096/fj.12-225755 · Cited by 301
Cell Lineages and the Logic of Proliferative Control
Lander, A. D., Gokoffski, K. K., Wan, F. Y. M., Nie, Q. H., & Calof, A. L. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000015 · Cited by 294
Qiu, J., Thapaliya, S., Runkana, A., Yang, Y., Tsien, C. D., Mohan, M. L., Narayanan, A. S., Eghtesad, B., Mozdziak, P. E., McDonald, C., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317049110 · Cited by 294
The muscle fiber type–fiber size paradox: hypertrophy or oxidative metabolism?
Wessel, T. V., HAAN, A. D., van der Laarse, W. J., & Jaspers, R. T. (2010) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1545-0 · Cited by 303
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
A Mechanistic Approach to Blood Flow Occlusion
Loenneke, J. P., Wilson, G. J., & Wilson, J. M. (2009) · International Journal of Sports Medicine · doi:10.1055/s-0029-1239499 · Cited by 298
TGF-β Family Signaling in Mesenchymal DifferentiationPreprint
Grafe, I., Alexander, S., Peterson, J. R., Snider, T. N., Lévi, B., Lee, B., & Mishina, Y. M. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022202 · Cited by 278
Relationships between Transforming Growth Factor-β1, Myostatin, and Decorin
Zhu, J., Li, Y., Shen, W., Qiao, C., Ambrosio, F., Lavasani, M., Nozaki, M., Branca, M. F., & Huard, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704146200 · Cited by 270
Myostatin Directly Regulates Skeletal Muscle Fibrosis
Li, Z. B., Kollias, H. D., & Wagner, K. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802585200 · Cited by 267
The origin of intermuscular adipose tissue and its pathophysiological implications
Vettor, R., Milan, G., Franzin, C., Sanna, M., Coppi, P. D., Rizzuto, R., & Federspil, G. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00229.2009 · Cited by 274
Kim, J.-S., Cross, J. M., & Bamman, M. M. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00464.2004 · Cited by 264
Day, K., Shefer, G., Shearer, A., & Yablonka-Reuveni, Z. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.01.006 · Cited by 254
Gilson, H., Schakman, O., Kalista, S., Lause, P., Tsuchida, K., & Thissen, J.-P. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00193.2009 · Cited by 248
The effects of obesity on skeletal muscle regeneration
Akhmedov, D., & Berdeaux, R. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00371 · Cited by 241
A Phase 1/2a Follistatin Gene Therapy Trial for Becker Muscular Dystrophy
Mendell, J. R., Sahenk, Z., Malik, V., Gomez, A. M., Flanigan, K. M., Lowes, L. P., Alfano, L. N., Berry, K., Meadows, E., Lewis, S., et al. (2014) · Molecular Therapy · doi:10.1038/mt.2014.200 · Cited by 254
Myostatin propeptide‐mediated amelioration of dystrophic pathophysiology
Bogdanovich, S., Perkins, K. J., Krag, T. O. B., Whittemore, L.-A., & Khurana, T. S. (2005) · The FASEB Journal · doi:10.1096/fj.04-2796com · Cited by 244
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 241
Regulation of muscle growth in neonates
Davis, T. A., & Fiorotto, M. L. (2008) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e32831cef9f · Cited by 244
Clinical, Agricultural, and Evolutionary Biology of Myostatin: A Comparative Review
Rodgers, B. D., & Garikipati, D. K. (2008) · Endocrine Reviews · doi:10.1210/er.2008-0003 · Cited by 243
IL-7 is expressed and secreted by human skeletal muscle cells
Haugen, F., Norheim, F., Lian, H., Wensaas, A. J., Dueland, S., Berg, O., Funderud, A., Skålhegg, B. S., Raastad, T., & Drevon, C. A. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00094.2009 · Cited by 237
Role of TGF-β signaling in inherited and acquired myopathies
Burks, T. N., & Cohn, R. D. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-19 · Cited by 245
Aged Stem Cells Reprogram Their Daily Rhythmic Functions to Adapt to Stress
Solanas, G., Peixoto, F. O., Perdiguero, E., Jardí, M., Ruiz‐Bonilla, V., Datta, D., Symeonidi, A., Castellanos‐Martín, A., Welz, P.-S., Caballero, J. M., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.035 · Cited by 234
Girgenrath, S., Song, K., & Whittemore, L.-A. (2004) · Muscle & Nerve · doi:10.1002/mus.20175 · Cited by 238
Bayol, S. A., Simbi, B. H., & Stickland, N. C. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.088989 · Cited by 229
Waters, D. L. (2010) · Clinical Interventions in Aging · doi:10.2147/cia.s6920 · Cited by 226
Yang, W., Zhang, Y., Li, Y., Wu, Z., & Zhu, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610185200 · Cited by 221
Inflammaging: Implications in Sarcopenia
Antuña, E., Cachán-Vega, C., Bermejo-Millo, J. C., Potes, Y., Caballero, B., Vega‐Naredo, I., Coto‐Montes, A. M., & García-González, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315039 · Cited by 234
Improved muscle healing through enhanced regeneration and reduced fibrosis in myostatin-null mice
McCroskery, S., Thomas, M., Platt, L., Hennebry, A., Nishimura, T., McLeay, L. M., Sharma, M., & Kambadur, R. (2005) · Journal of Cell Science · doi:10.1242/jcs.02482 · Cited by 219
Self-citationBiochemistry and Biology of GDF11 and Myostatin
Walker, R. G., Poggioli, T., Katsimpardi, L., Buchanan, S. M., Oh, J., Wattrus, S. J., Heidecker, B., Fong, Y. W., Rubin, L. L., Ganz, P., et al. (2016) · Circulation Research · doi:10.1161/circresaha.116.308391 · Cited by 217
Joulia-Ekaza, D., & Cabello, G. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.04.012 · Cited by 211
Artaza, J. N., Bhasin, S., Magee, T. R., Reisz‐Porszasz, S., Shen, R., Groome, N. P., Fareez, M. M., & González-Cadavid, N. F. (2005) · Endocrinology · doi:10.1210/en.2005-0362 · Cited by 206
Satellite Cell Dysfunction and Impaired IGF-1 Signaling Cause CKD-Induced Muscle Atrophy
Zhang, L., Wang, X. H., Wang, H., Du, J., & Mitch, W. E. (2010) · Journal of the American Society of Nephrology · doi:10.1681/asn.2009060571 · Cited by 207
Elevated expression of activins promotes muscle wasting and cachexia
Chen, J. L., Walton, K. L., Winbanks, C. E., Murphy, K. T., Thomson, R. E., Makanji, Y., Qian, H., Lynch, G. S., Harrison, C. A., & Gregorevic, P. (2013) · The FASEB Journal · doi:10.1096/fj.13-245894 · Cited by 207
Muscle hypertrophy driven by myostatin blockade does not require stem/precursor-cell activity
Amthor, H., Otto, A., Vulin, A., Rochat, A., Dumonceaux, J., Garcı́a, L., Mouisel, É., Hourdé, C., Macharia, R., Friedrichs, M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811129106 · Cited by 210
Bartoli, M., & Richard, I. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.12.012 · Cited by 207
Dubois, V., Laurent, M., Boonen, S., Vanderschueren, D., & Claessens, F. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0883-3 · Cited by 197
Decorin binds myostatin and modulates its activity to muscle cells
Miura, T., Kishioka, Y., Wakamatsu, J., Hattori, A., Hennebry, A., Berry, C., Sharma, M., Kambadur, R., & Nishimura, T. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.12.060 · Cited by 196
Self-citationKovacheva, E. L., Hikim, A. P. S., Shen, R., Sinha, I., & Sinha‐Hikim, I. (2009) · Endocrinology · doi:10.1210/en.2009-1177 · Cited by 201
Brooks, N. E., & Myburgh, K. H. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00099 · Cited by 206
Hennebry, A., Berry, C., Siriett, V., O'Callaghan, P., Chau, L., Watson, T. J., Sharma, M., & Kambadur, R. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00259.2007 · Cited by 193
Self-citationTargeting transforming growth factor-β receptors in pulmonary hypertension
Guignabert, C., & Humbert, M. J. C. (2020) · European Respiratory Journal · doi:10.1183/13993003.02341-2020 · Cited by 203
Judson, R. N., Tremblay, A. M., Knopp, P., White, R. B., Urcia, R., De Bari, C., Zammit, P. S., Camargo, F. D., & Wackerhage, H. (2012) · Journal of Cell Science · doi:10.1242/jcs.109546 · Cited by 190
Tendons of myostatin-deficient mice are small, brittle, and hypocellular
Mendias, C. L., Bakhurin, K. I., & Faulkner, J. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707069105 · Cited by 199
Hulmi, J. J., Kovanen, V., Selänne, H., Kraemer, W. J., Häkkinen, K., & Mero, A. A. (2009) · Amino Acids · doi:10.1007/s00726-008-0150-6 · Cited by 189
Modulation of reactive oxygen species in skeletal muscle by myostatin is mediated through NF-κB
Sriram, S., Subramanian, S., Sathiakumar, D., Venkatesh, R., Salerno, M. S., McFarlane, C. D., Kambadur, R., & Sharma, M. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00734.x · Cited by 189
Self-citationHeinemeier, K. M., Olesen, J. L., Schjerling, P., Haddad, F., Langberg, H., Baldwin, K. M., & Kjær, M. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00866.2006 · Cited by 189
Crosstalk between adipokines and myokines in fat browning
Rodríguez, A., Becerril, S., Ezquerro, S., Méndez-Giménez, L., & Frühbeck, G. (2016) · Acta Physiologica · doi:10.1111/apha.12686 · Cited by 196
Mendias, C. L., Gumucio, J. P., Davis, M. E., Bromley, C. W., Davis, C. S., & Brooks, S. V. (2011) · Muscle & Nerve · doi:10.1002/mus.22232 · Cited by 192
Stem cell activation in skeletal muscle regeneration
Fu, X., Wang, H.-T., & Hu, P. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1819-5 · Cited by 161
Muscle regeneration in the prolonged absence of myostatin
Wagner, K. R., Liu, X., Chang, X., & Allen, R. E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408729102 · Cited by 193
Petersen, A. M. W., Magkos, F., Atherton, P. J., Selby, A., Smith, K., Rennie, M. J., Pedersen, B. K., & Mittendorfer, B. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00301.2007 · Cited by 191
Suetta, C., Frandsen, U., Mackey, A. L., Jensen, L., Hvid, L. G., Bayer, M. L., Petersson, S. J., Schrøder, H. D., Andersen, J. L., Aagaard, P., et al. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.257121 · Cited by 191
Metabolic comorbidities in Cushing's syndrome
Ferraù, F., & Korbonits, M. (2015) · European Journal of Endocrinology · doi:10.1530/eje-15-0354 · Cited by 226
Wozniak, A. C., Kong, J., Bock, E., Pilipowicz, O., & Anderson, J. E. (2004) · Muscle & Nerve · doi:10.1002/mus.20263 · Cited by 179
Heterogeneity in the muscle satellite cell population
Biressi, S., & Rando, T. A. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.09.003 · Cited by 168
Mechanisms Limiting Body Growth in Mammals
Lui, J. C. K., & Baron, J. (2011) · Endocrine Reviews · doi:10.1210/er.2011-0001 · Cited by 170
Proteomic analysis of bovine skeletal muscle hypertrophy
Bouley, J., Meunier, B., Chambon, C., SMET, S. D., Hocquette, J.-F. J.-F., & Picard, B. B. (2005) · PROTEOMICS · doi:10.1002/pmic.200400925 · Cited by 169
Lee, S., Huynh, T. V., Lee, Y., Sebald, S. M., Wilcox‐Adelman, S. A., Iwamori, N., Lepper, C., Matzuk, M. M., & Fan, C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206410109 · Cited by 177
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 171
Self-citationContractile properties of EDL and soleus muscles of myostatin-deficient mice
Mendias, C. L., Marcin, J. E., Calerdon, D. R., & Faulkner, J. A. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00126.2006 · Cited by 170
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 170
Myostatin promotes the terminal differentiation of embryonic muscle progenitorsPreprint
Manceau, M., Gros, J., Savage, K., Thomé, V., McPherron, A. C., Paterson, B., & Marcelle, C. (2008) · Genes & Development · doi:10.1101/gad.454408 · Cited by 171
The myostatin gene: physiology and pharmacological relevance
Joulia-Ekaza, D., & Cabello, G. (2007) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2006.11.011 · Cited by 162
Durieux, A., Amirouche, A., Banzet, S., Koulmann, N., Bonnefoy, R., Pasdeloup, M., Mouret, C., Bigard, X. A., Peinnequin, A., & Freyssenet, D. G. (2007) · Endocrinology · doi:10.1210/en.2006-1500 · Cited by 162
Miller, T. M., Kim, S. H., Yamanaka, K., Hester, M. E., Umapathi, P., Arnson, H. A., Rizo, L., Mendell, J. R., Gage, F. H., Cleveland, D. W., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609411103 · Cited by 172
Zhang, C., McFarlane, C., Lokireddy, S., Bonala, S., Ge, X., Masuda, S., Gluckman, P. D., Sharma, M., & Kambadur, R. (2011) · Diabetologia · doi:10.1007/s00125-011-2079-7 · Cited by 158
Self-citationGe, G., Hopkins, D. R., Ho, W., & Greenspan, D. S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.14.5846-5858.2005 · Cited by 158
Metadata
- Authors
- McCroskery, S., Thomas, M., Maxwell, L., Sharma, M., & Kambadur, R.
- Affiliations
- University of Auckland (NZ)
- AgResearch (NZ)
- Corresponding author
- Kambadur, Ravi
- ORCID
- Thomas, Mark
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2003-09-08
- Volume
- 162
- Issue
- 6
- Pages
- 1135-1147
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2172861
- OpenAlex
- W2048134135
- Cited by
- 784
- References
- 44
- Citations by year
- 2026: 20 · 2025: 20 · 2024: 22 · 2023: 17 · 2022: 25 · 2021: 32 · 2020: 26 · 2019: 25 · 2018: 33 · 2017: 28 · 2016: 42 · 2015: 38 · 2014: 54 · 2013: 54 · 2012: 48
- FWCI
- 11.05
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- 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 (clinical) › Neurogenetic and Muscular Disorders Research
- Keywords
- myostatin, satellite cells, muscle stem cells, quiescence, self-renewal, satellite cell activation, p21, CDK2, G1/S cell cycle progression, myogenesis, myogenin, Mstn knockout mice, TGF-beta signaling
- MeSH terms
- Animals, Cell Differentiation, Cell Division, Regeneration, Down-Regulation, Up-Regulation, G1 Phase, S Phase, Transforming Growth Factor beta, Cyclins, Protein Serine-Threonine Kinases, Myogenin, Mice, Knockout, Muscle, Skeletal, Muscle Fibers, Skeletal, Gene Expression Regulation, Developmental, Cyclin-Dependent Kinases, Antigens, CD34, Feedback, Physiological, Myoblasts, Satellite Cells, Skeletal Muscle, CDC2-CDC28 Kinases, Cyclin-Dependent Kinase Inhibitor p21, Cyclin-Dependent Kinase 2, Mice, Myostatin
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
