The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.
Open accessAbstract
Skeletal muscle atrophy is a debilitating response to fasting, disuse, cancer, and other systemic diseases. In atrophying muscles, the ubiquitin ligase, atrogin-1 (MAFbx), is dramatically induced, and this response is necessary for rapid atrophy. Here, we show that in cultured myotubes undergoing atrophy, the activity of the PI3K/AKT pathway decreases, leading to activation of Foxo transcription factors and atrogin-1 induction. IGF-1 treatment or AKT overexpression inhibits Foxo and atrogin-1 expression. Moreover, constitutively active Foxo3 acts on the atrogin-1 promoter to cause atrogin-1 transcription and dramatic atrophy of myotubes and muscle fibers. When Foxo activation is blocked by a dominant-negative construct in myotubes or by RNAi in mouse muscles in vivo, atrogin-1 induction during starvation and atrophy of myotubes induced by glucocorticoids are prevented. Thus, forkhead factor(s) play a critical role in the development of muscle atrophy, and inhibition of Foxo factors is an attractive approach to combat muscle wasting.
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
“Two muscle-specific E3 ubiquitin ligases, muscle RING finger 1 (MuRF1, also known as TRIM63) and muscle atrophy F-Box (MAFbx, also known as atrogin-1 or FBXO32), are thought to be key regulators of proteasomal proteolysis in skeletal muscle, especially under atrophy-inducing conditions (Cai et al., 2004; Sandri et al., 2004; Stitt et al., 2004).”
From Proteasome dysfunction induces muscle growth defects and protein aggregation (2014) · cites this paper as Sandri et al., 2004
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Two muscle-specific E3 ubiquitin ligases, MuRF1 and Atrogin1, are thought to be key regulators of proteasomal proteolysis in skeletal muscle, especially under atrophy-inducing conditions (Cai et al., 2004; Sandri et al., 2004).”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Sandri et al., 2004
Experimental — accuracy not yet measuredIn the citing paper
“Atrogin-1 plays a key role in muscle atrophy as muscle specific ubiquitin ligase.”
From GLP-1RA Liraglutide and Semaglutide Improves Obesity-Induced Muscle Atrophy via SIRT1 Pathway (2023) · cites this paper as [48]
In the citing paper
“FoxO family of transcription factors (FoxO1, FoxO3, and FoxO4) are critical mediators of the catabolic response during atrophy [9, 15, 16].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [9]
In the citing paper
“The IGF1–AKT-–mTOR axis increases protein synthesis by stimulating the translational machinery and simultaneously blocks FoxOs transcription factors and protein degradation [9].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [9]
In the citing paper
“Alterations in mPTP function are undoubtedly contributing to the aging-related loss of muscle mass and function, since mPTP opening can trigger several atrophy-regulating pathways.”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [17]
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
Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor
Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 5,594
A System for Stable Expression of Short Interfering RNAs in Mammalian Cells
Brummelkamp, T. R., Bernards, R., & Agami, R. (2002) · Science · doi:10.1126/science.1068999 · Cited by 4,295
Identification of ubiquitin ligases required for skeletal muscle atrophy.
Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521
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
Stitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00211-4 · Cited by 1,964
Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A., & Goldberg, A. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251541198 · Cited by 1,774
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
Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
Lecker, S. H., Jagoe, R. T., Gilbert, A., Gomes, M., Baracos, V., Bailey, J., Price, S. R., Mitch, W. E., & Goldberg, A. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-0610com · Cited by 1,539
Self-citationRubinson, D. A., Dillon, C. P., Kwiatkowski, A. V., Sievers, C., Yang, L., Kopinja, J. E., Rooney, D. L., Zhang, M., Ihrig, M. M., McManus, M. T., et al. (2003) · Nature Genetics · doi:10.1038/ng1117 · Cited by 1,499
Insulin-regulated hepatic gluconeogenesis through FOXO1–PGC-1α interaction
Puigserver, P., Rhee, J., Donovan, J., Walkey, C. J., Yoon, J. C., Oriente, F., Kitamura, Y., Altomonte, J., Dong, H., Accili, D., et al. (2003) · Nature · doi:10.1038/nature01667 · Cited by 1,487
Cited by
Sorted by citations
Items 301–400 of 1,032
Rieu, I., Magne, H., Savary‐Auzeloux, I., Avérous, J., Bos, C., Peyron, M., Combaret, L., & Dardevet, D. P. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.178319 · Cited by 193
Sharples, A. P., Stewart, C. E., & Seaborne, R. A. (2016) · Aging Cell · doi:10.1111/acel.12486 · Cited by 180
Recent progress toward understanding the molecular mechanisms that regulate skeletal muscle mass
Goodman, C. A., Mayhew, D. L., & Hornberger, T. A. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.07.013 · Cited by 183
Long, Y. C., Cheng, Z., Copps, K. D., & White, M. F. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00983-10 · Cited by 183
González‐Freire, M., Scalzo, P., D’Agostino, J., Moore, A. Z., Díaz‐Ruiz, A., Fabbri, E., Zane, A. C., Chen, B. H., Becker, K. G., Lehrmann, E., et al. (2018) · Aging Cell · doi:10.1111/acel.12725 · Cited by 181
Misregulation of autophagy and protein degradation systems in myopathies and muscular dystrophies.
Sandri, M., Coletto, L., Grumati, P., & Bonaldo, P. (2013) · Journal of Cell Science · doi:10.1242/jcs.114041 · Cited by 179
Self-citationRapamycin inhibits the growth and muscle-sparing effects of clenbuterol
Kline, W. O., Panaro, F. J., Yang, H., & Bodine, S. C. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00873.2006 · Cited by 177
Glucocorticoids and Skeletal Muscle
Bodine, S. C., & Furlow, J. D. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-2895-8_7 · Cited by 180
Insulin and IGF-1 receptors regulate FoxO-mediated signaling in muscle proteostasis
O'Neill, B. T., Lee, K. Y., Klaus, K. A., Softic, S., Krumpoch, M. T., Fentz, J., Stanford, K. I., Robinson, M. M., Cai, W., Kleinridders, A., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci86522 · Cited by 185
MG53-induced IRS-1 ubiquitination negatively regulates skeletal myogenesis and insulin signalling
Yi, J.-S., Park, J. S., Ham, Y., Nguyen, N. T. B., Lee, N.-R., Hong, J. H., Kim, B.-W., Lee, H., Lee, C. S., Jeong, B., et al. (2013) · Nature Communications · doi:10.1038/ncomms3354 · Cited by 179
Fan, J., Yang, X., Li, J., Shu, Z., Dai, J., Liu, X., Li, B., Jia, S., Kou, X., Yang, Y., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.15728 · Cited by 183
Runx1 prevents wasting, myofibrillar disorganization, and autophagy of skeletal muscle
Wang, X., Blagden, C., Fan, J., Nowak, S. J., Taniuchi, I., Littman, D. R., & Burden, S. J. (2005) · Genes & Development · doi:10.1101/gad.1318305 · Cited by 177
Inflammation and age-associated skeletal muscle deterioration (sarcopaenia)
Wang, J., Leung, K.-S., Chow, S. K.-H., & Cheung, W.-H. (2017) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2017.05.006 · Cited by 173
The FoxO transcription factors and metabolic regulation
Nakae, J., Oki, M., & Cao, Y. (2008) · FEBS Letters · doi:10.1016/j.febslet.2007.11.025 · Cited by 176
Wang, D., Yin, Y., Yang, Y., Lv, P.-J., Shi, Y. Q., Lu, L., & Wei, L.-B. (2014) · International Immunopharmacology · doi:10.1016/j.intimp.2014.02.002 · Cited by 178
IGF-1 is downregulated in experimental cancer cachexia
Costelli, P., Muscaritoli, M., Bossola, M., Penna, F., Reffo, P., Bonetto, A., Busquets, S., Bonelli, G., López-Soriano, F. J., Doglietto, G. B., et al. (2006) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00104.2006 · Cited by 182
Tisdale, M. J. (2010) · Current Opinion in Gastroenterology · doi:10.1097/mog.0b013e3283347e77 · Cited by 176
Fang, W., Tseng, Y., Lee, T., Fu, Y., Chang, W., Lo, W., Lin, C., & Lo, Y. (2021) · British Journal of Pharmacology · doi:10.1111/bph.15472 · Cited by 186
The ubiquitin-proteasome system in cardiac physiology and pathology
Powell, S. R. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00062.2006 · Cited by 175
Raue, U., Slivka, D. R., Jemioło, B., Hollon, C. J., & Trappe, S. W. (2007) · The Journals of Gerontology Series A · doi:10.1093/gerona/62.12.1407 · Cited by 176
Gea, J., Pascual-Guàrdia, S., Casadevall, C., Orozco‐Levi, M., & Barreiro, E. (2015) · PubMed Central · doi:10.3978/j.issn.2072-1439.2015.08.04 · Cited by 185
Carson, J. A., & Manolagas, S. C. (2015) · Bone · doi:10.1016/j.bone.2015.04.015 · Cited by 173
PGC-1α buffers ROS-mediated removal of mitochondria during myogenesis
Baldelli, S., Aquilano, K., & Ciriolo, M. R. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.458 · Cited by 175
Kitajima, Y., Yoshioka, K., & Suzuki, N. (2020) · The Journal of Physiological Sciences · doi:10.1186/s12576-020-00768-9 · Cited by 171
Qiang, L., Banks, A. S., & Accili, D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.140228 · Cited by 171
Autophagy: A Druggable Process
Morel, É., Mehrpour, M., Botti, J., Dupont, N., Hamaï, A., Nascimbeni, A. C., & Codogno, P. (2017) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104936 · Cited by 174
Plasticity of human skeletal muscle: gene expression to in vivo function
Harridge, S. D. R. (2007) · Experimental Physiology · doi:10.1113/expphysiol.2006.036525 · Cited by 179
Adams, C. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610510200 · Cited by 173
FoxO Transcription Factors Are Critical Regulators of Diabetes-Related Muscle Atrophy
O’Neill, B. T., Bhardwaj, G., Penniman, C. M., Krumpoch, M. T., Suarez Beltran, P. A., Klaus, K., Poro, K., Li, M., Pan, H., Dreyfuss, J. M., et al. (2019) · Diabetes · doi:10.2337/db18-0416 · Cited by 167
Glynn, E. L., Fry, C. S., Drummond, M. J., Dreyer, H. C., Dhanani, S., Volpi, E., & Rasmussen, B. B. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00077.2010 · Cited by 177
Fry, C. S., Drummond, M. J., Glynn, E. L., Dickinson, J. M., Gundermann, D. M., Timmerman, K. L., Walker, D. K., Volpi, E., & Rasmussen, B. B. (2013) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/gls209 · Cited by 165
Waste management—Cytokines, growth factors and cachexia
Saini, A., Al‐Shanti, N., & Stewart, C. E. (2006) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2006.09.006 · Cited by 168
On metabolic shift to lactate consumption in fed-batch culture of mammalian cells
Mulukutla, B. C., Gramer, M. J., & Hu, W. (2012) · Metabolic Engineering · doi:10.1016/j.ymben.2011.12.006 · Cited by 172
Coordinate activation of autophagy and the proteasome pathway by FoxO transcription factor
Zhao, J., Brault, J. J., Schild, A., & Goldberg, A. L. (2008) · Autophagy · doi:10.4161/auto.5633 · Cited by 164
Self-citationInterleukin-1 stimulates catabolism in C2C12 myotubes
Li, W. S., Moylan, J. S., Chambers, M. A., Smith, J. D., & Reid, M. B. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00626.2008 · Cited by 171
Ono, Y., Maejima, Y., Saito, M., Sakamoto, K., Horita, S., Shimomura, K., Inoue, S., & Kotani, J. (2020) · Scientific Reports · doi:10.1038/s41598-020-57714-3 · Cited by 169
Mascher, H., Tannerstedt, J., Brink-Elfegoun, T., Ekblom, B. T., Gustafsson, T. P., & Blomstrand, E. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00504.2007 · Cited by 165
Joseph, G. A., Wang, S. X., Jacobs, C. E., Zhou, W., Kimble, G. C., Tse, H. W., Eash, J. K., Shavlakadze, T., & Glass, D. J. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00141-19 · Cited by 158
Sishi, B., Loos, B., Ellis, B., Smith, W., du Toit, E. F., & Engelbrecht, A.-M. (2011) · Experimental Physiology · doi:10.1113/expphysiol.2010.054189 · Cited by 162
JunB transcription factor maintains skeletal muscle mass and promotes hypertrophy
Raffaello, A., Milan, G., Masiero, E., Carnio, S., Lee, D., Lanfranchi, G., Goldberg, A. L., & Sandri, M. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201001136 · Cited by 156
Self-citationInflammation and cachexia in chronic kidney disease
Cheung, W. W., Paik, K. H., & MAK, R. H. K. (2010) · Pediatric Nephrology · doi:10.1007/s00467-009-1427-z · Cited by 163
Laminin-211 in skeletal muscle function
Holmberg, J., & Durbeej, M. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.22618 · Cited by 161
Molecular Mechanisms of Muscle Atrophy
McKinnell, I. W., & Rudnicki, M. A. (2004) · Cell · doi:10.1016/j.cell.2004.12.007 · Cited by 166
Aging Affects the Transcriptional Regulation of Human Skeletal Muscle Disuse Atrophy
Suetta, C., Frandsen, U., Jensen, L., Jensen, M. M., Jespersen, J. G., Hvid, L. G., Bayer, M. L., Petersson, S. J., Schrøder, H. D., Andersen, J. L., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051238 · Cited by 164
ER stress in skeletal muscle remodeling and myopathies
Afroze, D., & Kumar, A. (2017) · FEBS Journal · doi:10.1111/febs.14358 · Cited by 168
Sestrin prevents atrophy of disused and aging muscles by integrating anabolic and catabolic signals
Segalés, J., Perdiguero, E., Serrano, A. L., Sousa-Victor, P., Ortet, L., Jardí, M., Budanov, A. V., Garcia-Prat, L., Sandri, M., Thomson, D. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-13832-9 · Cited by 153
Self-citationMuscle atrophy and preferential loss of myosin in prolonged critically ill patients*
Derde, S., Hermans, G., Derese, I., Güiza, F., Hedström, Y., Wouters, P. J., Bruyninckx, F., D’Hoore, A., Larsson, L., den Berghe, G. V., et al. (2011) · Critical Care Medicine · doi:10.1097/ccm.0b013e31822d7c18 · Cited by 166
The myogenic kinome: protein kinases critical to mammalian skeletal myogenesis
Knight, J. D. R., & Kothary, R. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-29 · Cited by 164
Bastie, C. C., Nahle, Z. A., McLoughlin, T. J., Esser, K. A., Zhang, W., Unterman, T. G., & Abumrad, N. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413625200 · Cited by 165
Codependent Activators Direct Myoblast-Specific MyoD Transcription
Hu, P., Geles, K. G., Paik, J.-H., DePinho, R. A., & Tjian, R. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.08.018 · Cited by 155
Baldwin, K., Haddad, F., Pandorf, C., Roy, R. R., & Edgerton, V. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00284 · Cited by 113
Triggers and mechanisms of skeletal muscle wasting in chronic obstructive pulmonary disease
LANGEN, R. C. J., Gosker, H. R., Remels, A. H. V., & Schols, A. M. W. J. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.06.015 · Cited by 167
Increased Proteolysis, Myosin Depletion, and Atrophic AKT-FOXO Signaling in Human Diaphragm Disuse
Levine, S., Biswas, C., Dierov, J. K., Barsotti, R., Shrager, J. B., Nguyen, T., Sonnad, S. S., Kucharchzuk, J. C., Kaiser, L. R., Singhal, S. K., et al. (2010) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200910-1487oc · Cited by 162
Ubiquitin–protein ligases in muscle wasting
Cao, P., Kim, H. J., & Lecker, S. H. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.11.010 · Cited by 157
Self-citationHuijing, P. A., & Jaspers, R. T. (2005) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2005.00457.x · Cited by 159
Mechanotransduction in skeletal muscle
Thomas, J. F. (2006) · Frontiers in bioscience · doi:10.2741/2057 · Cited by 159
Involvement of MicroRNAs in the Regulation of Muscle Wasting during Catabolic Conditions
Soares, R., Cagnin, S., Chemello, F., Silvestrin, M., Musarò, A., Pittà, C. D., Lanfranchi, G., & Sandri, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.561845 · Cited by 157
Self-citationThe ubiquitin–proteasome system in cardiac dysfunction
Mearini, G., Schlossarek, S., Willis, M. S., & Carrier, L. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.06.009 · Cited by 155
Urso, M. L., Scrimgeour, A. G., Chen, Y., Thompson, P. D., & Clarkson, P. M. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00180.2006 · Cited by 159
The emerging role of FOXO transcription factors in pancreatic β cells
Glauser, D. A., & Schlegel, W. (2007) · Journal of Endocrinology · doi:10.1677/joe-06-0191 · Cited by 153
Lokireddy, S., Wijesoma, I. W., Teng, S., Bonala, S., Gluckman, P. D., McFarlane, C., Sharma, M., & Kambadur, R. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.10.005 · Cited by 154
RetractedThe SCF-Fbxo40 Complex Induces IRS1 Ubiquitination in Skeletal Muscle, Limiting IGF1 Signaling
Shi, J., Luo, L., Eash, J. K., Ibebunjo, C., & Glass, D. J. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.09.011 · Cited by 153
Response of the ubiquitin-proteasome pathway to changes in muscle activity
Reid, M. B. (2005) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00545.2004 · Cited by 161
Perturbed BMP signaling and denervation promote muscle wasting in cancer cachexia
Sartori, R., Hagg, A., Zampieri, S., Armani, A., Winbanks, C. E., Viana, L. R., Haidar, M., Watt, K. I., Qian, H., Pezzini, C., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.aay9592 · Cited by 159
Self-citationMarco, S. D., Mazrouï, R., Dallaire, P., Chittur, S. V., Tenenbaum, S. A., Radzioch, D., Marette, A., & Gallouzi, I. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.15.6533-6545.2005 · Cited by 155
Foxk proteins repress the initiation of starvation-induced atrophy and autophagy programs
Bowman, C. J., Ayer, D. E., & Dynlacht, B. D. (2014) · Nature Cell Biology · doi:10.1038/ncb3062 · Cited by 153
Differential response of skeletal muscles to mTORC1 signaling during atrophy and hypertrophy
Bentzinger, C. F., Lin, S., Romanino, K., Castets, P., Guridi, M., Summermatter, S., Handschin, C., Tintignac, L. A., Hall, M. N., & Rüegg, M. A. (2013) · Skeletal Muscle · doi:10.1186/2044-5040-3-6 · Cited by 153
Dyar, K. A., Hubert, M. J., Mir, A. A., Ciciliot, S., Lutter, D., Greulich, F., Quagliarini, F., Kleinert, M., Fischer, K., Eichmann, T. O., et al. (2018) · PLoS Biology · doi:10.1371/journal.pbio.2005886 · Cited by 159
Self-citationPuig-Vilanova, E., Rodriguez, D. A., Lloreta, J., Ausin, P., Pascual-Guardia, S., Broquetas, J., Roca, J., Gea, J., & Barreiro, E. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.006 · Cited by 167
Angiotensin II, Oxidative Stress and Skeletal Muscle Wasting
Sukhanov, S., Yoshida, T., Tabony, A. M., Higashi, Y., Galvez, S., Delafontaine, P., & Semprun‐Prieto, L. (2011) · The American Journal of the Medical Sciences · doi:10.1097/maj.0b013e318222e620 · Cited by 158
Small-molecule therapies for cardiac hypertrophy: moving beneath the cell surface
McKinsey, T. A., & Kass, D. A. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2193 · Cited by 152
Circulating miR-130b mediates metabolic crosstalk between fat and muscle in overweight/obesity
Wang, Y., Li, Y., Wang, X.-Y., Zhang, D., Zhang, H., Wu, Q., He, Y., Wang, J.-Y., Zhang, L., Xia, H., et al. (2013) · Diabetologia · doi:10.1007/s00125-013-2996-8 · Cited by 153
Causal relationship between insulin resistance and sarcopenia
Liu, Z.-J., & Zhu, C. (2023) · Diabetology & Metabolic Syndrome · doi:10.1186/s13098-023-01022-z · Cited by 163
Therapeutic approaches for muscle wasting disorders
Lynch, G. S., Schertzer, J. D., & Ryall, J. G. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2006.11.004 · Cited by 155
Ca2+-dependent proteolysis in muscle wasting
Costelli, P., Reffo, P., Penna, F., Autelli, R., Bonelli, G., & Baccino, F. M. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.03.010 · Cited by 159
Identification of a Novel Pool of Extracellular Pro-myostatin in Skeletal Muscle
Anderson, S. B., Goldberg, A. L., & Whitman, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706678200 · Cited by 159
Self-citationPaul, P. K., Bhatnagar, S., Mishra, V. K., Srivastava, S., Darnay, B. G., Choi, Y., & Kumar, A. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06351-11 · Cited by 157
Atrogin-1 deficiency promotes cardiomyopathy and premature death via impaired autophagy
Zaglia, T., Milan, G., Ruhs, A., Franzoso, M., Bertaggia, E., Pianca, N., Carpi, A., Carullo, P., Pesce, P., Sacerdoti, D., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci66339 · Cited by 147
Self-citationLo Verso, F., Carnio, S., Vainshtein, A., & Sandri, M. (2014) · Autophagy · doi:10.4161/auto.32154 · Cited by 146
Self-citationSeiliez, I., Panserat, S., Lansard, M., Polakof, S., Plagnes‐Juan, E., Surget, A., Dias, K., Larquier, M., Kaushik, S., & Cassy, S. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00579.2010 · Cited by 149
Understanding the common mechanisms of heart and skeletal muscle wasting in cancer cachexia
Rausch, V., Sala, V., Penna, F., Porporato, P. E., & Ghigo, A. (2021) · Oncogenesis · doi:10.1038/s41389-020-00288-6 · Cited by 149
Iyer, S. V., Han, L., Bartell, S. M., Kim, H., Gubrij, I. B., de Cabo, R., O’Brien, C. A., Manolagas, S. C., & Almeida, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.561803 · Cited by 151
Does Oxidative Stress Modulate Limb Muscle Atrophy in Severe COPD Patients?
Fermoselle, C., Rabinovich, R., Ausín, P., Puig-Vilanova, E., Coronell, C., Sanchez, F., Roca, J., Gea, J., & Barreiro, E. (2012) · European Respiratory Journal · doi:10.1183/09031936.00137211 · Cited by 148
Cachexia in chronic obstructive pulmonary disease: new insights and therapeutic perspective
Sanders, K. J. C., Kneppers, A. E. M., van de Bool, C., LANGEN, R. C. J., & Schols, A. M. W. J. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12062 · Cited by 153
Chemello, F., Wang, Z., Li, H. Z., McAnally, J., Liu, N., Bassel‐Duby, R., & Olson, E. N. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2018391117 · Cited by 141
Dehoux, M., Beneden, R. V., Pasko, N., Lause, P., Verniers, J., Underwood, L. E., Ketelslegers, J., & Thissen, J. (2004) · Endocrinology · doi:10.1210/en.2004-0406 · Cited by 151
Cellular and molecular events controlling skeletal muscle mass in response to altered use
Favier, F. B., Benoit, H., & Freyssenet, D. G. (2008) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-007-0423-z · Cited by 156
Wasting mechanisms in muscular dystrophy
Shin, J. S., Tajrishi, M. M., Ogura, Y., & Kumar, A. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.001 · Cited by 151
Hodges, P. W., James, G., Blomster, L. V., Hall, L., Schmid, A. B., Shu, C. C., Little, C. B., & Melrose, J. (2015) · Spine · doi:10.1097/brs.0000000000000972 · Cited by 153
TFE3 regulates whole‐body energy metabolism in cooperation with TFEB
Pastore, N., Vainshtein, A., Klisch, T. J., Armani, A., Huynh, T., Herz, N. J., Polishchuk, E. V., Sandri, M., & Ballabio, A. (2017) · EMBO Molecular Medicine · doi:10.15252/emmm.201607204 · Cited by 149
Self-citationDentice, M., Marsili, A., Zavacki, A. M., Larsen, P. R., & Salvatore, D. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.05.007 · Cited by 151
Polge, C., Heng, A.-É., Jarzaguet, M., Ventadour, S., Claustre, A., Combaret, L., Béchet, D., Matondo, M., Uttenweiler‐Joseph, S., Monsarrat, B., et al. (2011) · The FASEB Journal · doi:10.1096/fj.11-180968 · Cited by 157
Kuo, T., Lew, M. J., Mayba, O., Harris, C. A., Speed, T. P., & Wang, J.-C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111334109 · Cited by 148
Exercise therapy for people with sarcopenic obesity: myokines and adipokines as effective actors
Alizadeh Pahlavani, H. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.811751 · Cited by 145
Zheng, B., Ohkawa, S., Li, H., Roberts‐Wilson, T. K., & Price, S. R. (2010) · The FASEB Journal · doi:10.1096/fj.09-151480 · Cited by 145
Muscle function in COPD: a complex interplay
Man, W. D., Donaldson, G. C., Maddocks, M. M., Martolini, & Polkey, M. I. (2012) · International Journal of COPD · doi:10.2147/copd.s28247 · Cited by 150
Molecular and Cellular Determinants of Skeletal Muscle Atrophy and Hypertrophy
Sartorelli, V., & Fulco, M. (2004) · Science s STKE · doi:10.1126/stke.2442004re11 · Cited by 155
Autophagy is essential to support skeletal muscle plasticity in response to endurance exercise
Sanchez, A. M. J., Bernardi, H., Py, G., & Candau, R. B. (2014) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00187.2014 · Cited by 125
Léger, B., Vergani, L., Sorarú, G., Hespel, P., Derave, W., Gobelet, C., D'Ascenzio, C., Angelini, C. I., & Russell, A. P. (2006) · The FASEB Journal · doi:10.1096/fj.05-5249fje · Cited by 147
Coffey, V. G., SHIELD, A. J., Canny, B. J., Carey, K. A., Cameron‐Smith, D., & Hawley, J. A. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00299.2005 · Cited by 144
Metadata
- Authors
- Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L.
- Affiliations
- Harvard University (US)
- Veneto Institute of Molecular Medicine (IT)
- Beth Israel Deaconess Medical Center (US)
- Boston University (US)
- Corresponding author
- Lecker, Stewart H
- Goldberg, Alfred L
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2004-04
- Volume
- 117
- Issue
- 3
- Pages
- 399-412
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3619734
- OpenAlex
- W2033797333
- Cited by
- 3,012
- References
- 41
- Citations by year
- 2026: 129 · 2025: 122 · 2024: 121 · 2023: 118 · 2022: 141 · 2021: 153 · 2020: 165 · 2019: 159 · 2018: 151 · 2017: 117 · 2016: 134 · 2015: 171 · 2014: 176 · 2013: 177 · 2012: 150
- FWCI
- 33.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- National Space Biomedical Research Institute
- European Commission (QLRT-2000-00530)
- National Institutes of Health (DK02707, DK62307)
- Ministero dell’Istruzione, dell’Università e della Ricerca
- Agenzia Spaziale Italiana
- Muscular Dystrophy Association
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › FOXO transcription factor regulation
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- FOXO transcription factors, atrogin-1, skeletal muscle atrophy, ubiquitin ligase, PI3K/Akt signaling, insulin-like growth factor I, FOXO3, forkhead transcription factor, starvation, glucocorticoids, myotubes, muscle atrophy, transcriptional regulation
- MeSH terms
- Adenoviridae, Animals, Cells, Cultured, Cloning, Molecular, Fasting, Gene Expression Regulation, Genetic Vectors, Glucocorticoids, Insulin-Like Growth Factor I, Ligases, Models, Biological, Muscle Proteins, Muscular Atrophy, Promoter Regions, Genetic, Proto-Oncogene Proteins, Transcription Factors, Signal Transduction, Protein Serine-Threonine Kinases, Muscle, Skeletal, Phosphatidylinositol 3-Kinases, Muscle Cells, RNA Interference, Ubiquitin-Protein Ligases, SKP Cullin F-Box Protein Ligases, Proto-Oncogene Proteins c-akt, Mice
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