The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
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.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
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]
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
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
Flagged first, then by citations
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 101–200 of 1,052
Innervation and neuromuscular control in ageing skeletal muscle
Hepple, R. T., & Rice, C. L. (2015) · The Journal of Physiology · doi:10.1113/jp270561 · Cited by 417
Role of β-Adrenoceptor Signaling in Skeletal Muscle: Implications for Muscle Wasting and Disease
Lynch, G. S., & Ryall, J. G. (2008) · Physiological Reviews · doi:10.1152/physrev.00028.2007 · Cited by 410
Intracellular signaling during skeletal muscle atrophy
Kandarian, S. C., & Jackman, R. W. (2005) · Muscle & Nerve · doi:10.1002/mus.20442 · Cited by 405
Bodine, S. C. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.06.011 · Cited by 403
Self-citationLéger, B., Cartoni, R., Praz, M., Lamon, S., Dériaz, O., Crettenand, A., Gobelet, C., Rohmer, P., Konzelmann, M., Lüthi, F., et al. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.116715 · Cited by 403
Jung, T., Catalgol, B., & Grune, T. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.04.001 · Cited by 401
Effects of aging on human skeletal muscle after immobilization and retraining
Suetta, C., Hvid, L. G., Justesen, L., Christensen, U., Neergaard, K., Simonsen, L., Ortenblad, N., Magnusson, S. P., Kjaer, M., & Aagaard, P. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00290.2009 · Cited by 400
High Throughput Gene Expression Measurement with Real Time PCR in a Microfluidic Dynamic Array
Spurgeon, S. L., Jones, R. C., & Ramakrishnan, R. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001662 · Cited by 397
Lloyd, A. C. (2013) · Cell · doi:10.1016/j.cell.2013.08.053 · Cited by 393
Axon pathology in neurological disease: a neglected therapeutic target
Coleman, M. P., & Perry, V. H. (2002) · Trends in Neurosciences · doi:10.1016/s0166-2236(02)02255-5 · Cited by 387
The Neuromuscular Junction: Aging at the Crossroad between Nerves and Muscle
González‐Freire, M., de Cabo, R., Studenski, S. A., & Ferrucci, L. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00208 · Cited by 386
Molecular and cellular mechanisms of skeletal muscle atrophy: an update
Fanzani, A., Conraads, V. M., Penna, F., & Martinet, W. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-012-0074-6 · Cited by 386
Atrogin-1, MuRF-1, and sarcopenia
Gumucio, J. P., & Mendias, C. L. (2012) · Endocrine · doi:10.1007/s12020-012-9751-7 · Cited by 378
The role and regulation of MAFbx/atrogin-1 and MuRF1 in skeletal muscle atrophy
Foletta, V. C., White, L. J., Larsen, A., Léger, B., & Russell, A. P. (2011) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-010-0919-9 · Cited by 376
The spatial and temporal organization of ubiquitin networks
Grabbe, C., Husnjak, K., & Đikić, I. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3099 · Cited by 375
Mechanisms of disuse muscle atrophy: role of oxidative stress
Powers, S. K., Kavazis, A. N., & DeRuisseau, K. C. (2005) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00469.2004 · Cited by 368
Identification of the circadian transcriptome in adult mouse skeletal muscle
McCarthy, J. J., Andrews, J. L., McDearmon, E. L., Campbell, K. S., Barber, B. K., Miller, B. H., Walker, J. R., Hogenesch, J. B., Takahashi, J. S., & Esser, K. A. (2007) · Physiological Genomics · doi:10.1152/physiolgenomics.00066.2007 · Cited by 368
Waddell, D. S., Baehr, L. M., van den Brandt, J., Johnsen, S. A., Reichardt, H. M., Furlow, J. D., & Bodine, S. C. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00646.2007 · Cited by 368
Self-citationThe role of leucine and its metabolites in protein and energy metabolism
Duan, Y., Li, F., Li, Y., Tang, Y., Kong, X., Feng, Z., Anthony, T. G., Watford, M., Hou, Y., Wu, G., et al. (2015) · Amino Acids · doi:10.1007/s00726-015-2067-1 · Cited by 364
Gene expression profile of aging in human muscle
Welle, S. L., Brooks, A. I., Delehanty, J. M., Needler, N. A., & Thornton, C. A. (2003) · Physiological Genomics · doi:10.1152/physiolgenomics.00049.2003 · Cited by 364
Signaling pathways perturbing muscle mass.
Glass, D. J. (2010) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e32833862df · Cited by 359
Self-citationMuscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I
Kedar, V., McDonough, H., Arya, R., Li, H., Rockman, H. A., & Patterson, C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404341102 · Cited by 358
NF-κB–mediated Pax7 dysregulation in the muscle microenvironment promotes cancer cachexia
He, W. A., Berardi, E., Cardillo, V. M., Acharyya, S., Aulino, P., Thomas-Ahner, J., Wang, J., Bloomston, M., Muscarella, P., Nau, P., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci68523 · Cited by 357
TNF-α and cancer cachexia: Molecular insights and clinical implications
Patel, H. J., & Patel, B. M. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.11.033 · Cited by 357
Miller, M. K., Bang, M., Witt, C. C., Labeit, D., Trombitas, C., Watanabe, K., Granzier, H. L. M., McElhinny, A., Gregorio, C. C., & Labeit, S. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.09.012 · Cited by 356
The FOXO3a Transcription Factor Regulates Cardiac Myocyte Size Downstream of AKT Signaling
Skurk, C., Izumiya, Y., Maatz, H., Razeghi, P., Shiojima, I., Sandri, M., Sato, K., Zeng, L., Schiekofer, S., Pimentel, D. R., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500528200 · Cited by 355
Fuentes, E. N., Valdés, J. A., Molina, A., & Björnsson, B. T. (2013) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2013.06.009 · Cited by 358
Mitochondrial dysfunction: roles in skeletal muscle atrophy
Chen, X., Ji, Y., Liu, R., Zhu, X., Wang, K., Yang, X., Liu, B., Gao, Z., Huang, Y. H., Shen, Y., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04369-z · Cited by 362
Raben, N., Hill, V., Shea, L., Takikita, S., Baum, R., Mizushima, N., Ralston, E., & Plotz, P. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn292 · Cited by 352
Muscle-specific expression of IGF-1 blocks angiotensin II–induced skeletal muscle wasting
Song, Y., Li, Y., Du, J., Mitch, W. E., Rosenthal, N. A., & Delafontaine, P. (2005) · Journal of Clinical Investigation · doi:10.1172/jci22324 · Cited by 352
Bonetto, A., Aydogdu, T., Kunzevitzky, N., Guttridge, D. C., Khuri, S., Koniaris, L. G., & Zimmers, T. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022538 · Cited by 348
Sanchez, A. M., Csibi, A., Raibon, A., Cornille, K., Gay, S., Bernardi, H., & Candau, R. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23399 · Cited by 306
Kunkel, S. D., Suneja, M., Ebert, S. M., Bongers, K. S., Fox, D. K., Malmberg, S. E., Alipour, F., Shields, R. K., & Adams, C. M. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.020 · Cited by 345
“Previous studies demonstrated that skeletal muscle atrophy is driven by conserved changes in skeletal muscle gene expression (Bodine et al., 2001a; Sandri et al., 2004).”
FoxO transcription factors: their roles in the maintenance of skeletal muscle homeostasis
Sanchez, A. M. J., Candau, R. B., & Bernardi, H. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1513-z · Cited by 349
Patterns of gene expression in atrophying skeletal muscles: response to food deprivation
Jagoe, R. T., Lecker, S. H., Gomes, M., & Goldberg, A. L. (2002) · The FASEB Journal · doi:10.1096/fj.02-0312com · Cited by 344
Mechanisms of metabolic dysfunction in cancer-associated cachexiaPreprint
Petruzzelli, M., & Wagner, E. F. (2016) · Genes & Development · doi:10.1101/gad.276733.115 · Cited by 344
Lagirand-Cantaloube, J., Offner, N., Csibi, A., Leibovitch, M.-P., Batonnet‐Pichon, S., Tintignac, L. A. J., Segura, C. T., & Leibovitch, S. A. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.52 · Cited by 344
PI3 Kinase Regulation of Skeletal Muscle Hypertrophy and Atrophy
Glass, D. J. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_78 · Cited by 343
Self-citationKawabata, K., Mukai, R., & Ishisaka, A. (2015) · Food & Function · doi:10.1039/c4fo01178c · Cited by 336
Cancer cachexia: molecular mechanisms and treatment strategies
Setiawan, T., Sari, I. N., Wijaya, Y. T., Julianto, N. M., Muhammad, J. A., Lee, H., Chae, J. H., & Kwon, H. Y. (2023) · Journal of Hematology & Oncology · doi:10.1186/s13045-023-01454-0 · Cited by 342
Reza, M. M., Subramaniyam, N., Sim, C. M., Ge, X., Sathiakumar, D., McFarlane, C., Sharma, M., & Kambadur, R. (2017) · Nature Communications · doi:10.1038/s41467-017-01131-0 · Cited by 335
Human skeletal muscle possesses an epigenetic memory of hypertrophy
Seaborne, R. A., Strauss, J., Cocks, M., Shepherd, S., O’Brien, T. D., van Someren, K. A., Bell, P. G., Murgatroyd, C., Morton, J. P., Stewart, C. E., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-20287-3 · Cited by 334
Li, Y.-P., Chen, Y., Li, A. S., & Reid, M. B. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00129.2003 · Cited by 334
Overview of the Muscle Cytoskeleton
Henderson, C. A., Gomez, C. G., Novak, S. M., Mi‐Mi, L., & Gregorio, C. C. (2017) · Comprehensive physiology · doi:10.1002/cphy.c160033 · Cited by 333
A guide to understanding endoplasmic reticulum stress in metabolic disorders
Lemmer, I. L., Willemsen, N., Hilal, N., & Bartelt, A. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101169 · Cited by 334
TRIM Proteins Regulate Autophagy and Can Target Autophagic Substrates by Direct Recognition
Mandell, M. A., Jain, A., Arko‐Mensah, J., Chauhan, S., Kimura, T., Dinkins, C., Silvestri, G., Münch, J., Kirchhoff, F., Simonsen, A., et al. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.06.013 · Cited by 331
Inflammation: Roles in Skeletal Muscle Atrophy
Ji, Y., Li, M., Chang, M., Liu, R., Qiu, J., Wang, K., Deng, C., Shen, Y., Zhu, J., Wang, W., et al. (2022) · Antioxidants · doi:10.3390/antiox11091686 · Cited by 329
Development and evaluation of silk fibroin-based nerve grafts used for peripheral nerve regeneration
Yang, Y., Ding, F., Wu, J., Hu, W. H., Liu, W., Liu, J., & Gu, X. (2007) · Biomaterials · doi:10.1016/j.biomaterials.2007.09.001 · Cited by 328
Muscle regeneration: cellular and molecular events.
Karalaki, M., Fili, S., Philippou, Α., & Koutsilieris, M. (2009) · PubMed · Cited by 328
Mourkioti, F., Kratsios, P., Luedde, T., Song, Y.-H., Delafontaine, P., Adami, R., Parente, V., Bottinelli, R., Pasparakis, M., & Rosenthal, N. A. (2006) · Journal of Clinical Investigation · doi:10.1172/jci28721 · Cited by 326
Drug‐screening platform based on the contractility of tissue‐engineered muscle
Vandenburgh, H. H., Shansky, J., Benesch, F., Barbata, V., Reid, J., Thorrez, L., Valentini, R. F., & Crawford, G. (2008) · Muscle & Nerve · doi:10.1002/mus.20931 · Cited by 324
Regulation of Muscle Protein Degradation
Lee, S. W., Dai, G., Hu, Z., Wang, X., Du, J., & Mitch, W. E. (2004) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000127211.86206.e1 · Cited by 324
Acharyya, S., Butchbach, M. E. R., Sahenk, Z., Wang, H., Saji, M., Carathers, M., Ringel, M. D., Skipworth, R. J. E., Fearon, K. C. H., Hollingsworth, M. A., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.10.004 · Cited by 323
Assist–Control Mechanical Ventilation Attenuates Ventilator-induced Diaphragmatic Dysfunction
Sassoon, C. S. H., Zhu, E., & Caiozzo, V. J. (2004) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200401-042oc · Cited by 321
Dodson, S., Baracos, V. E., Jatoi, A., Evans, W. J., Cella, D., Dalton, J. T., & Steiner, M. S. (2011) · Annual Review of Medicine · doi:10.1146/annurev-med-061509-131248 · Cited by 319
Tumor necrosis factor-alpha inhibits myogenic differentiation through myod protein destabilization
Langen, R. C. J., van der Velden, J. L. J., Schols, A. M. W. J., Kelders, M. C. J. M., Wouters, E. F. M., & Janssen‐Heininger, Y. M. W. (2004) · The FASEB Journal · doi:10.1096/fj.03-0251com · Cited by 319
Kaneki, H., Guo, R., Chen, D., Yao, Z., Schwarz, E. M., Zhang, Y. E., Boyce, B. F., & Xing, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509430200 · Cited by 315
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
Witt, S. H., Granzier, H. L. M., Witt, C. C., & Labeit, S. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.05.021 · Cited by 312
Foxo Transcription Factors Blunt Cardiac Hypertrophy by Inhibiting Calcineurin Signaling
Ni, Y. G., Berenji, K., Wang, N., Oh, M., Sachan, N., Dey, A., Cheng, J., Lu, G., Morris, D. J., Castrillón, D. H., et al. (2006) · Circulation · doi:10.1161/circulationaha.106.637124 · Cited by 309
Wilson, G. J., Wilson, J. M., & Manninen, A. H. (2008) · Nutrition & Metabolism · doi:10.1186/1743-7075-5-1 · Cited by 306
Gong, C., Li, Z., Ramanujan, K., Clay, I., Zhang, Y., Lemire-Brachat, S., & Glass, D. J. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.05.009 · Cited by 305
Self-citationDownstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle
Mammucari, C., Schiaffino, S., & Sandri, M. (2008) · Autophagy · doi:10.4161/auto.5905 · Cited by 303
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
Development of proteasome inhibitors as research tools and cancer drugs
Goldberg, A. L. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201210077 · Cited by 298
Mechanisms Modulating Skeletal Muscle Phenotype
Blaauw, B., Schiaffino, S., & Reggiani, C. (2013) · Comprehensive physiology · doi:10.1002/cphy.c130009 · Cited by 298
Wang, X., Hu, W. H., Cao, Y., Yao, J., Wu, J., & Gu, X. (2005) · Brain · doi:10.1093/brain/awh517 · Cited by 293
MicroRNAs in skeletal muscle: Their role and regulation in development, disease and function
Güller, I., & Russell, A. P. (2010) · The Journal of Physiology · doi:10.1113/jphysiol.2010.194175 · Cited by 290
Judge, S. M., DODD, S. L., McClung, J. M., & Judge, A. R. (2008) · The FASEB Journal · doi:10.1096/fj.08-110163 · Cited by 289
Muscle Atrophy Induced by Mechanical Unloading: Mechanisms and Potential Countermeasures
Gao, Y., Arfat, Y., Wang, H., & Goswami, N. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00235 · Cited by 289
Myostatin Gene Deletion Prevents Glucocorticoid-Induced Muscle Atrophy
Gilson, H., Schakman, O., Combaret, L., Lause, P., Grobet, L., Attaix, D., Ketelslegers, J., & Thissen, J. (2006) · Endocrinology · doi:10.1210/en.2006-0539 · Cited by 288
Early onset of inflammation and later involvement of TGFβ in Duchenne muscular dystrophy
Chen, Y. W., Nagaraju, K., Bakay, M. A., McIntyre, O., Rawat, R., Shi, R., & Hoffman, E. P. (2005) · Neurology · doi:10.1212/01.wnl.0000173836.09176.c4 · Cited by 287
Sardiello, M., Cairo, S., Fontanella, B., Ballabio, A., & Meroni, G. (2008) · BMC Evolutionary Biology · doi:10.1186/1471-2148-8-225 · Cited by 287
Energetic Trade-Offs and Hypometabolic States Promote Disease Tolerance
Ganeshan, K., Nikkanen, J., Man, K., Leong, Y. A., Sogawa, Y., Maschek, J. A., Van Ry, T., Chagwedera, D. N., Cox, J. E., & Chawla, A. (2019) · Cell · doi:10.1016/j.cell.2019.01.050 · Cited by 286
The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy
Murton, A. J., Constantin, D., & Greenhaff, P. L. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.10.011 · Cited by 286
Review of muscle wasting associated with chronic kidney disease
Workeneh, B., & Mitch, W. E. (2010) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.2010.28608b · Cited by 285
Fresh insights into glucocorticoid-induced diabetes mellitus and new therapeutic directions
Li, J.-X., & Cummins, C. L. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-022-00683-6 · Cited by 285
Léger, B., Derave, W., Bock, K. D., Hespel, P., & Russell, A. P. (2008) · Rejuvenation Research · doi:10.1089/rej.2007.0588 · Cited by 285
Mann, G., Mora, S., Madu, G., & Adegoke, O. A. J. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.702826 · Cited by 283
The muscle-specific ubiquitin ligase atrogin-1/MAFbx mediates statin-induced muscle toxicity
Hanai, J., Cao, P., Tanksale, P., Imamura, S., Koshimizu, E., Zhao, J., Kishi, S., Yamashita, M., Phillips, P. S., Sukhatme, V. P., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32741 · Cited by 281
Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3
Fielitz, J., Kim, M.-S., Shelton, J. M., Latif, S., Spencer, J. A., Glass, D. J., Richardson, J. A., Bassel‐Duby, R., & Olson, E. N. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32827 · Cited by 280
Self-citationIGF-1, inflammation and stem cells: interactions during muscle regeneration
Mourkioti, F., & Rosenthal, N. A. (2005) · Trends in Immunology · doi:10.1016/j.it.2005.08.002 · Cited by 279
Bindels, L. B., Beck, R., Schakman, O., Martin, J. C., De Backer, F., Sohet, F. M., Dewulf, E. M., Pachikian, B. D., Neyrinck, A. M., Thissen, J.-P., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037971 · Cited by 278
Egan, B., & Sharples, A. P. (2023) · Physiological Reviews · doi:10.1152/physrev.00054.2021 · Cited by 278
Excitation‐transcription coupling in skeletal muscle: the molecular pathways of exercise
Gundersen, K. (2010) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/j.1469-185x.2010.00161.x · Cited by 281
Global analysis of gene expression patterns during disuse atrophy in rat skeletal muscle
Stevenson, E. J., Giresi, P. G., Koncarevic, A., & Kandarian, S. C. (2003) · The Journal of Physiology · doi:10.1111/j.1469-7793.2003.00033.x · Cited by 278
Exercise and gene expression: physiological regulation of the human genome through physical activity
Booth, F. W., Chakravarthy, M. V., & Spangenburg, E. E. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2002.019265 · Cited by 277
Schefold, J. C., Bierbrauer, J., & Weber‐Carstens, S. (2010) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-010-0010-6 · Cited by 278
Inflammation induced loss of skeletal muscle
Londhe, P., & Guttridge, D. C. (2015) · Bone · doi:10.1016/j.bone.2015.03.015 · Cited by 276
Tokuzawa, Y., Kaiho, E., Maruyama, M., Takahashi, K., Mitsui, K., Maeda, M., Niwa, H., & Yamanaka, S. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.8.2699-2708.2003 · Cited by 276
Ferraro, E., Giammarioli, A. M., Chiandotto, S., Spoletini, I., & Rosano, G. M. C. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5773 · Cited by 275
The regulation of muscle mass by endogenous glucocorticoids
Braun, T. P., & Marks, D. L. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00012 · Cited by 273
Therapeutic glucocorticoids: mechanisms of actions in rheumatic diseases
Hardy, R., Raza, K., & Cooper, M. S. (2020) · Nature Reviews Rheumatology · doi:10.1038/s41584-020-0371-y · Cited by 273
The role of E3 ubiquitin-ligases MuRF-1 and MAFbx in loss of skeletal muscle mass
Rom, O., & Reznick, A. Z. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.12.031 · Cited by 271
Muscle Giants: Molecular Scaffolds in Sarcomerogenesis
Kontrogianni‐Konstantopoulos, A., Ackermann, M. A., Bowman, A. L., Yap, S. V., & Bloch, R. J. (2009) · Physiological Reviews · doi:10.1152/physrev.00017.2009 · Cited by 268
Myofibrillar protein turnover: The proteasome and the calpains1,2
Goll, D. E., Neti, G., Mares, S. W., & Thompson, V. F. (2008) · Journal of Animal Science · doi:10.2527/jas.2007-0395 · Cited by 268
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
Self-citationTestosterone regulation of Akt/mTORC1/FoxO3a signaling in skeletal muscle
White, J. P., Gao, S., Puppa, M., Sato, S., Welle, S. L., & Carson, J. A. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.10.019 · Cited by 267
Heat shock response and autophagy—cooperation and control
Dokładny, K., Myers, O., & Moseley, P. L. (2015) · Autophagy · doi:10.1080/15548627.2015.1009776 · Cited by 268
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
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
