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
Items 501–600 of 781
Harsløf, T., Frost, M., Nielsen, T. L., Husted, L. B., Nyegaard, M., Brixen, K., Børglum, A. D., Mosekilde, L., Andersen, M., Rejnmark, L., et al. (2013) · Calcified Tissue International · doi:10.1007/s00223-013-9702-1 · Cited by 13
Identification of TGF-β, inhibin βA and follistatin paralogs in the rainbow trout genome
de Mello, F., Streit, D. P., Sabin, N., & Gabillard, J. (2014) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2014.07.006 · Cited by 12
Multi-Cellular Functions of MG53 in Muscle Calcium Signaling and Regeneration
Benissan‐Messan, D., Zhu, H., Zhong, W., Tan, T., Ma, J., & Lee, P. H. U. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.583393 · Cited by 12
Laminin binds to myostatin and attenuates its signaling
Yasaka, N., Suzuki, K., Kishioka, Y., Wakamatsu, J., & Nishimura, T. (2013) · Animal Science Journal · doi:10.1111/asj.12052 · Cited by 12
Jatwani, A., & Tulsawani, R. (2021) · High Altitude Medicine & Biology · doi:10.1089/ham.2020.0172 · Cited by 11
Caetano-Anollés, K., Mishra, S., & Rodriguez‐Zas, S. L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0116828 · Cited by 11
Jones, J. C., Kroscher, K. A., & Dilger, A. C. (2014) · BMC Physiology · doi:10.1186/1472-6793-14-3 · Cited by 11
Molecular regulation of skeletal muscle tissue formation and development
Nesvadbová, M., & Bořilová, G. (2018) · Veterinární Medicína · doi:10.17221/7/2018-vetmed · Cited by 11
Tinklenberg, J. A., Siebers, E. M., Beatka, M. J., Fickau, B. A., Ayres, S., Meng, H., Yang, L., Simpson, P., Granzier, H. L. M., & Lawlor, M. W. (2018) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nly120 · Cited by 11
Gómez‐Requeni, P., Kraemer, M., & Canosa, L. F. (2019) · Fishes · doi:10.3390/fishes4030037 · Cited by 11
Srivastava, S., Rathor, R., Singh, S. N., & Suryakumar, G. (2022) · Biomarkers · doi:10.1080/1354750x.2022.2112290 · Cited by 11
Jeanplong, F., Osepchook, C. C., Falconer, S. J., Smith, H. K., Bass, J. J., McMahon, C. D., & Oldham, J. M. (2015) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2015.01.002 · Cited by 11
Decorin expression in quiescent myogenic cells
Nishimura, T., Nozu, K., Kishioka, Y., Wakamatsu, J., & Hattori, A. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.03.025 · Cited by 11
Miyata, H., Itoh, R., Satō, F., TAKEBE, N., Hada, T., & Tozaki, T. (2017) · The Journal of Physiological Sciences · doi:10.1007/s12576-017-0575-3 · Cited by 11
Huang, P., Pang, D., Wang, K., Xu, A., Yao, C., Li, M., You, W., Wang, Q., & Yu, H. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030643 · Cited by 12
Sun, T., Meng, X.-Z., Li, Y., Zhang, H., He, R., He, R., Liu, T., Lv, W., Xu, X., Shen, Y., et al. (2025) · Aquaculture · doi:10.1016/j.aquaculture.2025.743355 · Cited by 10
Horváth, L., Pekár, M., Švagera, Z., Horká, V., Mráz, M., & Bužga, M. (2025) · Physiological Research · doi:10.33549/physiolres.935751 · Cited by 14
Geometric control of myogenic cell fate
De‐Juan‐Pardo, E. M., Hoang, M. B.-T., & Conboy, I. M. (2006) · International Journal of Nanomedicine · doi:10.2147/nano.2006.1.2.203 · Cited by 10
Liu, Y., Xu, C., Asiamah, C. A., Ye, R., Pan, Y., Lu, L., Zhao, Z., Jiang, P., & Su, Y. (2021) · Gene · doi:10.1016/j.gene.2021.145884 · Cited by 10
Xue, L., Dong, X., Zhang, X., & Diallo, A. O. (2011) · DNA and Cell Biology · doi:10.1089/dna.2011.1263 · Cited by 9
Wang, R., Luo, D., Xiao, C., Lin, P., Liu, S., Xu, Q.-W., & Wang, Y. (2013) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2013/869398 · Cited by 10
Jørgensen, L. H., Sellathurai, J., Davis, E. E., Thedchanamoorthy, T., Al-Bader, R. W. A., Jensen, C. H., & Schrøder, H. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060692 · Cited by 12
Discovery of a Mammalian Splice Variant of Myostatin That Stimulates Myogenesis
Jeanplong, F., Falconer, S. J., Oldham, J. M., Thomas, M., Gray, T. S., Hennebry, A., Matthews, K. G., Kemp, F. C., Patel, K., Berry, C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081713 · Cited by 10
Self-citationACTN3 Genotype is Associated with Muscle Phenotypes in Women across the Adult Age Span
Walsh, S., Liu, D., Metter, E. J., Ferrucci, L., & Roth, S. M. (2008) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000322289.16416.12 · Cited by 11
Xing, H. J., Wang, Z. Y., Zhong, B., Ying, S. J., Nie, H., Zhou, Z. R., Fan, Y. X., & Wang, F. (2014) · Genetics and Molecular Research · doi:10.4238/2014.july.24.4 · Cited by 11
Aspectos fundamentales del crecimiento en ovinos
René Patiño, P., & CLEEF, E. V. (2010) · Revista Colombiana de Ciencia Animal - RECIA · doi:10.24188/recia.v2.n2.2010.322 · Cited by 10
Elashry, M. I., Schneider, V. C., Heimann, M., Wenisch, S., & Arnhold, S. (2025) · Journal of Developmental Biology · doi:10.3390/jdb13010005 · Cited by 11
Effects of Myostatin on Nuclear Morphology at the Myotendinous Junction
Amemiya, H., Yamamoto, M., Higa, K., Watanabe, G., Taniguchi, S., Kitamura, K., Jeong, J., Yanagisawa, N., Fukuda, K., & Abe, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076634 · Cited by 9
Patel, K., & Morgan, J. (2012) · Neuromuscular Disorders · doi:10.1016/j.nmd.2011.09.008 · Cited by 7
Clostridium perfringens α-toxin inhibits myogenic differentiation of C2C12 myoblasts
Takehara, M., Kobayashi, K., & Nagahama, M. (2020) · Anaerobe · doi:10.1016/j.anaerobe.2020.102265 · Cited by 9
Song, F., Ye, H., Shi, L., Ouyang, D., Sun, J., & Luo, J. (2022) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2022.111183 · Cited by 9
Ohno, Y., Matsuba, Y., Hashimoto, N., Sugiura, T., Ohira, Y., Yoshioka, T., & Goto, K. (2016) · International Journal of Medical Sciences · doi:10.7150/ijms.16267 · Cited by 10
Mothe‐Satney, I., Piquet, J., Murdaca, J., Sibille, B., Grimaldi, P. A., Neels, J. G., & Rousseau, A. (2016) · Biochimie · doi:10.1016/j.biochi.2016.12.001 · Cited by 9
Kostyunina, D. S., Ivanova, A. D., & Smirnova, О. V. (2018) · Human Physiology · doi:10.1134/s0362119718010127 · Cited by 10
Dividing to Keep Muscle Together: The Role of Satellite Cells in Aging Skeletal Muscle
Hepple, R. T. (2006) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2006.3.pe3 · Cited by 9
Zhao, X., Li, M., Xu, S., Junyan, S. U. N., & Liu, G. J. (2019) · Brazilian Journal of Poultry Science · doi:10.1590/1806-9061-2017-0710 · Cited by 8
Rashidlamir, A., Hosseini, S. R. A., Hejazi, K., & Motevalli, M. S. (2016) · Journal of Cardiovascular and Thoracic Research · doi:10.15171/jcvtr.2016.33 · Cited by 8
Santos, H. O., Cerqueira, H. S. C., & Tinsley, G. M. (2022) · Metabolites · doi:10.3390/metabo12111146 · Cited by 8
The quasi-parallel lives of satellite cells and atrophying muscle
Biressi, S. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00140 · Cited by 9
Chandraskeharan, K., & Martin, P. T. (2008) · Muscle & Nerve · doi:10.1002/mus.21198 · Cited by 8
Genxi, Z. (2012) · AFRICAN JOURNAL OF BIOTECHNOLOGY · doi:10.5897/ajb11.2858 · Cited by 8
Endesfelder, S., Kliche, A., Lochmüller, H., von Moers, A., & Speer, A. (2004) · Journal of Molecular Medicine · doi:10.1007/s00109-004-0607-3 · Cited by 8
Zhu, P., Li, H., Huang, G., Cui, J., Zhang, R., Cui, K., Yang, S., & Shi, D. (2017) · Animal Biotechnology · doi:10.1080/10495398.2017.1289941 · Cited by 8
Torres-Velarde, J. M., Llera‐Herrera, R., Ibarra‐Castro, L., García-Gasca, T., & Garcı́a-Gasca, A. (2019) · Molecular Biology Reports · doi:10.1007/s11033-019-05147-1 · Cited by 8
Approaching the Sarcopenic Patient with Nonalcoholic Steatohepatitis-related Cirrhosis
Gallo, P., Flagiello, V., Falcomatà, A., Pasquale, G. D., D’Avanzo, G., Terracciani, F., Picardi, A., & Gentilucci, U. V. (2024) · Journal of Clinical and Translational Hepatology · doi:10.14218/jcth.2023.00207 · Cited by 8
Omidizadeh, M., Kheiri, F., & Faghani, M. (2021) · Livestock Science · doi:10.1016/j.livsci.2021.104682 · Cited by 7
Podocan promoting skeletal muscle post‐injury regeneration by inhibiting TGF ‐β signaling pathway
Teng, H., Zheng, J., Liang, Y., Zhao, J., Yan, Y., Li, S., Li, S., & Tong, H. (2024) · The FASEB Journal · doi:10.1096/fj.202302158rr · Cited by 7
Long-term fasting induced basal thermogenesis flexibility in female Japanese quails
Xu, J.-H., Xu, X., Huang, X., Chen, K.-X., He, W., Li, M., & Liu, J.-S. (2024) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2024.111611 · Cited by 7
Tao, Z., Zhu, C., Song, C., Song, W., Ji, G., Shan, Y. J., Xu, W., & Li, H. (2015) · British Poultry Science · doi:10.1080/00071668.2015.1085958 · Cited by 7
Molecular and Cellular Mechanism of Muscle Regeneration
Sakuma, K., & Yamaguchi, A. (2012) · InTech eBooks · doi:10.5772/48229 · Cited by 4
Gene therapy with anabolic growth factors to prevent muscle atrophy
Schakman, O., & Thissen, J. (2006) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/01.mco.0000222101.21385.a6 · Cited by 7
Biochemical Interaction Between Muscle and Bone: A Physiological Reality?
Jaspers, R. T., & Bravenboer, N. (2014) · Clinical Reviews in Bone and Mineral Metabolism · doi:10.1007/s12018-014-9156-7 · Cited by 7
Carani, F. R., Duran, B. O. D. S., de Paula, T. G., Piedade, W. P., & Dal‐Pai‐Silva, M. (2013) · Acta Scientiarum Animal Sciences · doi:10.4025/actascianimsci.v35i3.18219 · Cited by 7
Transcriptomic profile of semitendinosus muscle of bulls of different breed and performance
Ciecierska, A., Motyl, T., & Sadkowski, T. (2020) · Journal of Applied Genetics · doi:10.1007/s13353-020-00577-1 · Cited by 7
Novel insights regarding mechanisms for treatment of sarcopenia
Kraemer, R. R., & Castracane, V. D. (2014) · Metabolism · doi:10.1016/j.metabol.2014.11.002 · Cited by 7
Jank, M., Zwierzchowski, L., Siadkowska, E., Budasz-Swiderska, M., Sadkowski, T., Oprzadek, J. M., & Motyl, T. (2006) · Journal of Animal and Feed Sciences · doi:10.22358/jafs/66909/2006 · Cited by 7
Exploring myostatin’s role and potential applications in fisheries and aquaculture: a review
Priyanka, P., Kashyap, S., Umesh, Verma, K., Singh, M., & Yadav, N. (2024) · Aquaculture International · doi:10.1007/s10499-024-01700-3 · Cited by 6
Balaprakash, K., Aanand, S., Manimekalai, D., Ande, M. P., & Lingam, R. S. S. (2024) · Aquaculture · doi:10.1016/j.aquaculture.2024.741960 · Cited by 6
Myostatin-driven muscle hypertrophy: a double-edged sword in muscle physiology
Dewasi, G., Nagda, P., Bahl, G., Jain, V., & Gupta, S. K. (2025) · Journal of Rare Diseases · doi:10.1007/s44162-025-00086-x · Cited by 8
Yang, F., Liu, S., Qu, J., & Zhang, Q. (2022) · Gene · doi:10.1016/j.gene.2022.146675 · Cited by 6
Qiu, M., Zhang, X., Liao, L., Zhang, N., & Liu, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252211988 · Cited by 7
Comparative proteomics of skeletal muscle mitochondria from myostatin-null mice
Puddick, J., & Martinus, R. D. (2011) · Cell Biology International Reports · doi:10.1042/cbr20110006 · Cited by 6
How β2-adrenergic agonists induce skeletal muscle hypertrophy?
Kitaura, T. (2013) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.2.423 · Cited by 5
Satkunskienė, D., Ratkevičius, A., Kamandulis, S., & Venckūnas, T. (2018) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2018-0369 · Cited by 6
A novel splice variant of the human MSTN gene encodes a myostatin‐specific myostatin inhibitor
Maeta, K., Farea, M., Nishio, H., & Matsuo, M. (2023) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13314 · Cited by 5
Molecular targets of cancer cachexia: Opportunities for pharmanutritional approaches
Sharma, M., Kambadur, R., Sriram, S., Lokireddy, S., & McFarlane, C. (2013) · PharmaNutrition · doi:10.1016/j.phanu.2013.07.002 · Cited by 6
Self-citationEffect of Thyroid Hormone on the Gene Expression of Myostatin in Rat Skeletal Muscle
Ma, Y., Xiaoqiang, C., Li, Q., An, X.-R., & Yongfu, C. (2009) · Asian-Australasian Journal of Animal Sciences · doi:10.5713/ajas.2009.80290 · Cited by 6
Design and Application of Bispecific Splice-Switching Oligonucleotides
Bestas, B., McClorey, G., Tedebark, U., Moreno, P. M. D., Roberts, T. C., Hammond, S. M., Smith, C. I. E., Wood, M. J. A., & Andaloussi, S. E. (2014) · Nucleic Acid Therapeutics · doi:10.1089/nat.2013.0462 · Cited by 6
Cytokines in Skeletal Muscle Growth and Decay
Orzechowski, A. (2017) · Springer eBooks · doi:10.1007/978-981-10-3292-9_5 · Cited by 7
Deng, B., Zhang, F., Wen, J., Shen, W., Gao, Q., Peng, X., Tan, J., Pu, Z., Ye, S., Wang, L., et al. (2020) · Genomics · doi:10.1016/j.ygeno.2020.01.024 · Cited by 6
Is the myonuclear domain ceiling hypothesis dead?
Aman, F. I., Khatib, E., AlNeaimi, A., Mohamed, A. A. M., Almulla, A. S., Zaidan, A. I., Alshafei, J., Habbal, O., Eldesouki, S., & Qaisar, R. (2021) · Singapore Medical Journal · doi:10.11622/smedj.2021103 · Cited by 6
Júnior, R. F., Souza, A. D. P., de Oliveira, A. A., Nunes, P. R. P., Michelin, M. A., Chica, J. E. L., Murta, E. F. C., & Orsatti, F. L. (2016) · Menopause Review/Przegląd Menopauzalny · doi:10.5114/pm.2016.65663 · Cited by 6
Stochastic dynamics of cell lineage in tissue homeostasis
Qiu, Y., Chen, W., & Nie, Q. H. (2019) · Discrete and Continuous Dynamical Systems - B · doi:10.3934/dcdsb.2018339 · Cited by 6
Yucel, N. D., & Blau, H. M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809880-6.00018-7 · Cited by 7
The therapeutic potential of agents that inactivate myostatin
Bishop, A., Kambadur, R., & Sharma, M. (2005) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.14.9.1099 · Cited by 6
Self-citationLü, J., Sun, D., Xu, L., Lu, G., Zhao, F., Wei, C., Zhang, L., Ding, J., Li, B., & Du, L. (2012) · Biochemical Genetics · doi:10.1007/s10528-012-9524-2 · Cited by 6
Moghadam, B. H., Johne, M., Golestani, F., Lorenz, K., Asad, M., Maculewicz, E., & Mastalerz, А. (2023) · Biology of Sport · doi:10.5114/biolsport.2023.123894 · Cited by 5
Skeletal muscle dysfunction in COPD: miRNAs, myokines and exercise
Maniscalco, M., Fuschillo, S., Ambrosino, P., Candia, C., Domenico, A. D., Lombardi, C., Motta, A., & Ambrosino, N. (2026) · ERJ Open Research · doi:10.1183/23120541.00887-2025 · Cited by 5
Lim, C., McKendry, J., Giacomin, T., Mcleod, J. C., Ng, S. Y., Currier, B. S., Coletta, G., & Phillips, S. M. (2023) · PLoS ONE · doi:10.1371/journal.pone.0286222 · Cited by 5
Gao, Y., Wang, S., Di, A., Hai, C., Wu, D., Hao, Z., Bu, L., Liu, X., Bai, C., Su, G., et al. (2024) · Journal of Integrative Agriculture · doi:10.1016/j.jia.2024.04.020 · Cited by 5
Mori, H., Kawai, N., Kinouchi, N., Hichijo, N., Ishida, T., Kawakami, E., Noji, S., & Tanaka, E. I. (2014) · Development Growth & Differentiation · doi:10.1111/dgd.12123 · Cited by 5
RetractedJiang, X., Huang, C.-X., Zhong, S.-S., Sun, C., & Zou, S. (2016) · Aquaculture · doi:10.1016/j.aquaculture.2016.11.014 · Cited by 5
Pathinathan, P., Uma, A., Prabu, E., Felix, N., Ahilan, B., & Antony, C. (2023) · Aquaculture · doi:10.1016/j.aquaculture.2023.740299 · Cited by 5
Some aspects of heat stress on the plasticity of skeletal muscle cells
Goto, K., Ohno, Y., Goto, A., Ikuta, A., Suzuki, M., Ohira, T., Tsuchiya, N., Nishizawa, S., Koya, T., Egawa, T., et al. (2012) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.1.197 · Cited by 5
Song, H., Ochi, E., Lee, K., Hiranuma, K., & Nakazato, K. (2012) · BMC Musculoskeletal Disorders · doi:10.1186/1471-2474-13-211 · Cited by 5
Rhoads, R., Rathbone, C. R., & Flann, K. L. (2009) · CRC Press eBooks · doi:10.1201/b15797-3 · Cited by 5
Дементьева, Н. В., Mitrofanova, O. V., Тыщенко, В. И., Terletskiy, V. P., & Yakovlev, A. F. (2017) · Russian Journal of Genetics Applied Research · doi:10.1134/s207905971701004x · Cited by 5
Age-related changes in myostatin expression in rat skeletal muscles
Shibaguchi, T., Maeoka, T., Yoshihara, T., Naıto, H., Goto, K., Yoshioka, T., & Sugiura, T. (2018) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.7.221 · Cited by 5
Yang, L., Zhang, K., Wu, Q., Li, J., Lai, S., Song, T. Z., & Zhang, M. (2019) · World Rabbit Science · doi:10.4995/wrs.2019.10610 · Cited by 5
Regeneration of Musculoskeletal Tissues
Stocum, D. L. (2006) · Elsevier eBooks · doi:10.1016/b978-012369371-6/50026-5 · Cited by 5
Tgf-β Signaling In Duchenne Muscular Dystrophy
Kemaladewi, D. U., Hoen, P. A. C. ’., ten Dijke, P., van Ommen, G. J., & Hoogaars, W. M. H. (2012) · Future Neurology · doi:10.2217/fnl.12.3 · Cited by 6
Regulation of muscle size in humans: role of myostatin?
Bamman, M. M. (2008) · PubMed · Cited by 5
Blau, H. M., Sacco, A., & Gilbert, P. M. (2009) · Elsevier eBooks · doi:10.1016/b978-0-12-374729-7.00030-5 · Cited by 5
Mechanism of satellite cell regulation by myokines
Furuichi, Y., & FUJII, N. L. (2017) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.6.311 · Cited by 5
Endocrine therapies for sarcopenia in older men
Solomon, A., & Bouloux, P. M. (2006) · British Journal of Hospital Medicine · doi:10.12968/hmed.2006.67.9.22000 · Cited by 5
Effects of statins on sarcopenia with focus on mechanistic insights and future perspectives
Zhang, X., Wang, X., Huang, L., Zhou, C., Qian, B., Luo, Z., & Chen, Y. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1669591 · Cited by 9
Efficacy of femtosecond lasers for application of acupuncture therapy
Ohta, M., Hosokawa, Y., Hatano, N., Sugano, A., Ito, A., & Takaoka, Y. (2016) · Lasers in Medical Science · doi:10.1007/s10103-016-2124-3 · Cited by 4
Дементьева, Н. В., Mitrofanova, O. V., Тыщенко, В. И., Terletskiy, V. P., & Yakovlev, A. F. (2016) · Vavilov Journal of Genetics and Breeding · doi:10.18699/vj16.154 · Cited by 4
Inactivation of Myostatin Delays Senescence via TREX1-SASP in Bovine Skeletal Muscle Cells
Yang, M., Gao, L., Gao, Y., Hao, Z., Zhou, X., Su, G., Bai, C., Wei, Z., Liu, X., Yang, L., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25105277 · Cited by 4
MicroRNA-33 inhibition ameliorates muscular dystrophy by enhancing skeletal muscle regeneration
Sowa, N., Horie, T., Ide, Y., Baba, O., Kora, K., Yoshida, T., Nakamura, Y., Matsumura, S., Matsushita, K., Imanaka, M., et al. (2025) · EMBO Molecular Medicine · doi:10.1038/s44321-025-00273-9 · Cited by 4
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
