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Identification of ubiquitin ligases required for skeletal muscle atrophy.
Open accessAbstract
Skeletal muscle adapts to decreases in activity and load by undergoing atrophy. To identify candidate molecular mediators of muscle atrophy, we performed transcript profiling. Although many genes were up-regulated in a single rat model of atrophy, only a small subset was universal in all atrophy models. Two of these genes encode ubiquitin ligases: Muscle RING Finger 1 ( MuRF1 ), and a gene we designate Muscle Atrophy F-box ( MAFbx ), the latter being a member of the SCF family of E3 ubiquitin ligases. Overexpression of MAFbx in myotubes produced atrophy, whereas mice deficient in either MAFbx or MuRF1 were found to be resistant to atrophy. These proteins are potential drug targets for the treatment of muscle atrophy.
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“The E3 ligase muscle RING‐finger protein‐1 (MuRF1), encoded by Trim63, and the F‐Box protein Atrogin‐1, encoded by Fbxo32, are key factors for ubiquitin‐proteasome system‐mediated protein degradation in muscle atrophy.”
From Sepsis induces interleukin 6, gp130/JAK2/STAT3, and muscle wasting (2022) · cites this paper as [7]
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In the citing paper
“A study examining MuRF1 and Atrogin1 gene expression in several models of muscle atrophy has also reported that their gene expression is up-regulated at different time points (Bodine et al., 2001).”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Bodine et al., 2001
In the citing paper
“MuRF1 knockout mice are not protected from denervation-induced muscle loss at 7 days and only partially protected (around 30%) at 14 days39. Moreover, the absence of MuRF1 does not protect from fasting or microgravity induced atrophy, while muscle mass is spared following glucocorticoid treatment43,44.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [39]
In the citing paper
“The first ubiquitin ligases that were identified to play a role in muscle loss were Atrogin-1/MAFbx and MuRF1. These two E3s are strongly upregulated in all the catabolic conditions so far tested in animals and are considered the master genes of muscle atrophy39.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [39]
In the citing paper
“Genes encoding for glycolysis and oxidative phosphorylation enzymes are coordinately suppressed in atrophying muscles during denervation, disuse, diabetes, cancer, fasting, and chronic kidney disease [10, 11, 13, 20].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [10]
In the citing paper
“Muscle atrophy requires the activation of gene transcription programs that regulate the expression of a subset of genes that are named atrophy-related genes or atrogenes [10–14].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [10]
In the citing paper
“Animal models that lack MURF-1 expression are protected from atrophy [71,72].”
From Omega-3 Fatty Acids and Skeletal Muscle Health (2015) · cites this paper as [71]
In the citing paper
“Mice deficient in either MAFbx or MuRF1 were demonstrated to be resistant to atrophy [7].”
From Nutraceuticals in the Prevention and Treatment of the Muscle Atrophy (2021) · cites this paper as [7]
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Cites
A simplified system for generating recombinant adenoviruses
He, T., Zhou, S., da Costa, L. T., Yu, J., Kinzler, K. W., & Vogelstein, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2509 · Cited by 3,209
Bodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752
Self-citationRommel, 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
Self-citationJoazeiro, C. A. P., & Weissman, A. M. (2000) · Cell · doi:10.1016/s0092-8674(00)00077-5 · Cited by 1,249
Skowyra, D., Craig, K. L., Tyers, M., Elledge, S. J., & Harper, J. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80403-1 · Cited by 1,233
Kipreos, E. T., & Pagano, M. (2000) · Genome biology · doi:10.1186/gb-2000-1-5-reviews3002 · Cited by 753
Ubiquitination: RING for destruction?
Freemont, P. S. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00287-6 · Cited by 522
Centner, T., Yano, J., Kimura, E., McElhinny, A., Pelin, K., Witt, C. C., Bang, M., Trombitás, K., Granzier, H., Gregorio, C. C., et al. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4448 · Cited by 402
What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
Jagoe, R. T., & Goldberg, A. L. (2001) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/00075197-200105000-00003 · Cited by 399
Identification of a family of human F-box proteins
Cenciarelli, C., Chiaur, D. S., Guardavaccaro, D., Parks, W. P., Vidal, M., & Pagano, M. (1999) · Current Biology · doi:10.1016/s0960-9822(00)80020-2 · Cited by 365
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Research works printed but not linked: 2
- Additional data and methods used in this study are described in the supplementary Web material available on Science Online at www.sciencemag.org/cgi/content/full/1065874/DC1. GenBank accession numbers are as follows: rat MAFbx ; human MAFbx ; and rat MuRF1 . For Northern methods and probe details ref. (2) of Web material. Knockouts were done with the proprietary Velocigene technology which allows for the rapid and high-throughput generation of custom gene mutations in mice (T. M. De Chiara W. T. Poueymirou D. M. Valenzuela G. D. Yancopoulos unpublished data).
- Bains W., Ponte P., Blau H. M., Kedes L., Mol. Cell. Biol. 4, 1449 (1984).
Cited by
Sorted by citations
Items 801–900 of 1,052
Chua, J. P., Reddy, S., Merry, D. E., Adachi, H., Katsuno, M., Sobue, G., Robins, D. M., & Lieberman, A. P. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt527 · Cited by 79
Cunha, T. F., Moreira, J. B. N., da Paixão, N. A., Campos, J. C., Monteiro, A. W. A., Bacurau, A. V. N., Júnior, C. R. B., Ferreira, J. C. B., & Brum, P. C. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00346.2011 · Cited by 79
Zhang, Y., Wang, J., Wang, X., Gao, T., Tian, H., Zhou, D., Zhang, L., Li, G., & Wang, X. (2020) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/nqz347 · Cited by 79
Costelli, P., & Baccino, F. M. (2003) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/01.mco.0000078984.18774.02 · Cited by 78
Cancer Cachexia: It’s Time for More Clinical Trials
Bossola, M., Pacelli, F., Tortorelli, A. P., & Doglietto, G. B. (2006) · Annals of Surgical Oncology · doi:10.1245/s10434-006-9179-5 · Cited by 78
MG132-mediated inhibition of the ubiquitin–proteasome pathway ameliorates cancer cachexia
Zhang, L., Tang, H., Kou, Y., Li, R., Zheng, Y., Wang, Q., Zhou, X., & Jin, L. (2013) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-013-1412-6 · Cited by 78
Jensen, T. E., Wojtaszewski, J. F. P., & Richter, E. A. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01979.x · Cited by 78
Degradation of sarcomeric and cytoskeletal proteins in cultured skeletal muscle cells
Purintrapiban, J., Wang, M.-C., & Forsberg, N. E. (2003) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s1096-4959(03)00201-x · Cited by 78
Role of Autophagy in COPD Skeletal Muscle Dysfunction
Hussain, S. N. A., & Sandri, M. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00893.2012 · Cited by 77
Sugawara, T., Ito, Y., NISHIZAWA, N., & Nagasawa, T. (2008) · Amino Acids · doi:10.1007/s00726-008-0180-0 · Cited by 77
Vary, T. C., Frost, R. A., & Lang, C. H. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00056.2008 · Cited by 77
Mendias, C. L., Kayupov, E., Bradley, J. R., Brooks, S. V., & Claflin, D. R. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00126.2011 · Cited by 77
Vitamin E in Sarcopenia: Current Evidences on Its Role in Prevention and Treatment
Khor, S. C., Karim, N. A., Ngah, W. Z. W., Yusof, Y. A. M., & Makpol, S. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/914853 · Cited by 77
Gene Expression Profiling in Slow-Type Calf Soleus Muscle of 30 Days Space-Flown Mice
Gambara, G., Salanova, M., Ciciliot, S., Furlan, S., Gutsmann, M., Schiffl, G., Ungethuem, U., Volpe, P., Gunga, H., & Blottner, D. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169314 · Cited by 78
Wei, W., Fareed, M. U., Evenson, A. R., Menconi, M. J., Yang, H., Petkova, V., & Hasselgren, P.-O. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00341.2004 · Cited by 77
Combaret, L., Taillandier, D., Dardevet, D. P., Béchet, D., Rallière, C., Claustre, A., Grizard, J., & Attaix, D. (2004) · Biochemical Journal · doi:10.1042/bj20031660 · Cited by 77
Nowell, M. M., Choi, H., & Rourke, B. C. (2010) · Journal of Comparative Physiology B · doi:10.1007/s00360-010-0505-7 · Cited by 76
McClung, J. M., McCord, T. J., Keum, S., Johnson, S., Annex, B. H., Marchuk, D. A., & Kontos, C. D. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.01.032 · Cited by 76
Tisdale, M. J. (2004) · Langenbeck s Archives of Surgery · doi:10.1007/s00423-004-0486-7 · Cited by 76
Kostrominova, T. Y., Dow, D. E., Dennis, R. G., Miller, R. A., & Faulkner, J. A. (2005) · Physiological Genomics · doi:10.1152/physiolgenomics.00210.2004 · Cited by 76
Howard, E. E., Pasiakos, S. M., Fussell, M. A., & Rodriguez, N. R. (2020) · Advances in Nutrition · doi:10.1093/advances/nmaa015 · Cited by 75
Optimal management of cancer anorexia–cachexia syndrome
Argiles, J. M., Oliván, M., Busquets, S., López-Soriano, F. J., & Argiles, J. M. (2010) · Cancer Management and Research · doi:10.2147/cmar.s7101 · Cited by 75
den Kamp, C. M. O., LANGEN, R. C. J., Minnaard, R., KELDERS, M. C. J. M., Snepvangers, F. J. M., Hesselink, M. K. C., Dingemans, A. C., & Schols, A. M. W. J. (2011) · Lung Cancer · doi:10.1016/j.lungcan.2011.09.012 · Cited by 75
Perera, S., Holt, M., Mankoo, B. S., & Gautel, M. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.12.024 · Cited by 75
Serra, C., Sandor, N. L., Jang, H., Lee, D. C., Toraldo, G., Guarneri, T., Wong, S., Zhang, A., Guo, W., Jasuja, R., et al. (2013) · Endocrinology · doi:10.1210/en.2013-1004 · Cited by 75
Cardiac ankyrin repeat protein is a marker of skeletal muscle pathological remodelling
Laure, L., Suel, L., Roudaut, C., Bourg, N., Ouali, A., Bartoli, M., Richard, I., & Danièle, N. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06814.x · Cited by 75
Raffaello, A., Laveder, P., Romualdi, C., Bean, C., Toniolo, L., Germinario, E., Megighian, A., Danieli‐Betto, D., Reggiani, C., & Lanfranchi, G. (2005) · Physiological Genomics · doi:10.1152/physiolgenomics.00051.2005 · Cited by 75
Age-Related Deficit in Load-Induced Skeletal Muscle Growth
Hwee, D. T., & Bodine, S. C. (2009) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glp026 · Cited by 74
Self-citationLiu, Y., Chen, F., Odle, J., Lin, X., Zhu, H., Shi, H., Hou, Y., & Yin, J. (2013) · The Journal of Nutrition · doi:10.3945/jn.113.176255 · Cited by 74
Network medicine, multimorbidity and the lung in the elderly
Faner, R., Cruz, T., López-Giraldo, A., & Agustí, A. G. N. (2014) · European Respiratory Journal · doi:10.1183/09031936.00078714 · Cited by 74
Spatial detection of fetal marker genes expressed at low level in adult human heart tissue
Asp, M., Salmén, F., Ståhl, P. L., Vicković, S., Felldin, U., Löfling, M., Navarro, J. F., Maaskola, J., Eriksson, M. J., Persson, B., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-13462-5 · Cited by 74
Gualtieri, P., Falcone, C., Romano, L., Macheda, S., Correale, P., Arciello, P., Polimeni, N., & LORENZO, A. D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134670 · Cited by 74
Hunt, L. C., Graça, F. A., Pagala, V., Wang, Y., Li, Y., Yuan, Z., Fan, Y., Labelle, M., Peng, J., & Demontis, F. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109971 · Cited by 74
Judson, R. N., Gray, S. R., Walker, C. A., Carroll, A. M., Itzstein, C., Lionikas, A., Zammit, P. S., Bari, C. D., & Wackerhage, H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059622 · Cited by 74
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Alamdari, N., O’Neal, P., & Hasselgren, P.-O. (2008) · Nutrition · doi:10.1016/j.nut.2008.09.002 · Cited by 74
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Sato, S., Ogura, Y., & Kumar, A. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00018 · Cited by 74
Kang, C., & Ji, L. L. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01354.2012 · Cited by 74
Plasma from septic shock patients induces loss of muscle protein
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Bogomolovas, J., Gasch, A., Šimkovic, F., Rigden, D. J., Labeit, S., & Mayans, O. M. (2014) · Open Biology · doi:10.1098/rsob.140041 · Cited by 74
Yakabe, M., Ogawa, S., Ota, H., Iijima, K., Eto, M., Ouchi, Y., & Akishita, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0191318 · Cited by 74
Hilder, T. L., Tou, J. C. L., Grindeland, R. E., Wade, C. E., & Graves, L. M. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00972-4 · Cited by 74
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Hałoń, M., Borkowska, A., Herman-Antosiewicz, A., & Antosiewicz, J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00165 · Cited by 73
Trevino, M. B., Zhang, X., Standley, R. A., Wang, M., Han, X., Reis, F. C. G., Periasamy, M., Yu, G., Kelly, D. P., Goodpaster, B. H., et al. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00161.2019 · Cited by 73
Rajan, V., & Mitch, W. E. (2007) · Pediatric Nephrology · doi:10.1007/s00467-007-0594-z · Cited by 73
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Cui, D., Xiong, X., & Zhao, Y. (2016) · Cell Division · doi:10.1186/s13008-016-0022-5 · Cited by 73
Cho, A., Christine, M., Malicdan, V., Miyakawa, M., Nonaka, I., Nishino, I., & Noguchi, S. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx192 · Cited by 73
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Attaix, D., & Baracos, V. E. (2010) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e328338b9a6 · Cited by 73
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Yin, J., Yang, L., Xie, Y., Liu, Y., Li, S., Yang, W., Xu, B., Ji, H., Ding, L., Wang, K., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04038-6 · Cited by 72
Caiozzo, V. J., Haddad, F., Lee, S., Baker, M., Paloski, W., & Baldwin, K. M. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91130.2008 · Cited by 72
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Aweida, D., Rudesky, I., Volodin, A., Shimko, E., & Cohen, S. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201802018 · Cited by 73
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Fanzani, A., Zanola, A., Rovetta, F., Rossi, S., & Aleo, M. F. (2010) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2010.11.003 · Cited by 73
Seaborne, R. A. E., Hughes, D. C., Turner, D. C., Owens, D. J., Baehr, L. M., Gorski, P. P., Semenova, E. A., Borisov, O., Larin, A. K., Popov, D. V., et al. (2019) · The Journal of Physiology · doi:10.1113/jp278073 · Cited by 72
Self-citationFyfe, J. J., Broatch, J. R., Trewin, A. J., Hanson, E. D., Argus, C. K., GARNHAM, A. P., Halson, S. L., Polman, R. C. J., Bishop, D. J., & Petersen, A. C. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00127.2019 · Cited by 72
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Chen, B., Xu, J., He, X., Xu, H., Li, G., Du, H., Nie, Q., & Zhang, X. (2015) · PLoS ONE · doi:10.1371/journal.pone.0137087 · Cited by 71
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Stephens, N. A., Skipworth, R. J. E., Gallagher, I. J., Greig, C. A., Guttridge, D. C., Ross, J. A., & Fearon, K. C. H. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12005 · Cited by 71
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Zeman, R. J., Zhao, J., Zhang, Y., Zhao, W., Wen, X., Wu, Y., Pan, J., Bauman, W. A., & Cardozo, C. P. (2009) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0643-5 · Cited by 71
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Schwartz, L. M. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.68 · Cited by 71
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Stefanetti, R. J., Lamon, S., Wallace, M. A., Vendelbo, M. H., Russell, A. P., & Vissing, K. (2014) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-014-1587-y · Cited by 71
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Rudolf, R., Bogomolovas, J., Strack, S., Choi, K. R., Khan, M. M., Wagner, A., Brohm, K., Hanashima, A., Gasch, A., Labeit, D., et al. (2012) · AGE · doi:10.1007/s11357-012-9468-9 · Cited by 71
Ogawa, M., Yamaji, R., Higashimura, Y., Harada, N., Ashida, H., Nakano, Y., & Inui, H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.276824 · Cited by 71
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Zhao, W., Qin, W., Pan, J., Wu, Y., Bauman, W. A., & Cardozo, C. P. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.11.123 · Cited by 71
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Bower, N. I., & Johnston, I. A. (2010) · Physiological Genomics · doi:10.1152/physiolgenomics.00065.2010 · Cited by 70
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Metadata
- Authors
- 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., Pan, Z.-Q., Valenzuela, D. M., DeChiara, T. M., Stitt, T. N., Yancopoulos, G. D., & Glass, D. J.
- Affiliations
- Regeneron (United States) (US)
- Applied Biosystems, 850 Lincoln Center Drive, Foster City, CA 94404, USA.
- Regeneron Pharmaceuticals, 777 Old Saw Mill River Road, Tarrytown, NY, 10591–6707, USA.
- Icahn School of Medicine at Mount Sinai (US)
- Corresponding author
- Glass, David J.
- ORCID
- Venue
- Science
- Published
- 2001-11-23
- Volume
- 294
- Issue
- 5547
- Pages
- 1704-1708
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2167033587
- Cited by
- 3,521
- References
- 18
- Citations by year
- 2026: 124 · 2025: 133 · 2024: 141 · 2023: 139 · 2022: 157 · 2021: 151 · 2020: 202 · 2019: 175 · 2018: 180 · 2017: 175 · 2016: 175 · 2015: 178 · 2014: 182 · 2013: 190 · 2012: 173
- FWCI
- 15.71
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Science (publishedVersion)
- 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 › Ubiquitin and proteasome pathways
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- skeletal muscle atrophy, ubiquitin ligase, MuRF1, atrogin-1, SCF ubiquitin ligase, F-box protein, myotubes
- MeSH terms
- Amino Acid Sequence, Animals, Cloning, Molecular, Creatine Kinase, DNA-Binding Proteins, Humans, Immobilization, Isoenzymes, Molecular Sequence Data, Muscle Denervation, Muscle Proteins, Muscular Atrophy, Peptide Synthases, Phenotype, Protein Binding, RNA, Messenger, Trans-Activators, Up-Regulation, Rats, Sprague-Dawley, Gene Deletion, MyoD Protein, Myogenin, Mice, Knockout, Muscle, Skeletal, Hindlimb Suspension, Gene Expression Profiling, SKP Cullin F-Box Protein Ligases, Mice, Rats, Myogenic Regulatory Factor 5, Creatine Kinase, MM Form
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