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
AKT/PKB Signaling: Navigating the Network
Manning, B. D., & Toker, A. (2017) · Cell · doi:10.1016/j.cell.2017.04.001 · Cited by 3,772
Fiber Types in Mammalian Skeletal Muscles
Schiaffino, S., & Reggiani, C. (2011) · Physiological Reviews · doi:10.1152/physrev.00031.2010 · Cited by 3,022
Self-citationExercise Metabolism and the Molecular Regulation of Skeletal Muscle Adaptation
Egan, B., & Zierath, J. R. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2012.12.012 · Cited by 2,084
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
FoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953
Self-citationBaracos, V. E., Martin, L., Korc, M., Guttridge, D. C., & Fearon, K. C. H. (2018) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.105 · Cited by 1,738
Regulation of Mammalian Autophagy in Physiology and Pathophysiology
Ravikumar, B., Sarkar, S., Davies, J. E., Futter, M., García-Arencibia, M., Green-Thompson, Z. W., Jiménez-Sánchez, M., Korolchuk, V. I., Lichtenberg, M., Luo, S., et al. (2010) · Physiological Reviews · doi:10.1152/physrev.00030.2009 · Cited by 1,789
Cancer cachexia: understanding the molecular basis
Argilés, J. M. A., Busquets, S., Stemmler, B., & López-Soriano, F. J. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3829 · Cited by 1,567
Mechanisms regulating skeletal muscle growth and atrophy
Schiaffino, S., Dyar, K. A., Ciciliot, S., Blaauw, B., & Sandri, M. (2013) · The FEBS Journal · doi:10.1111/febs.12253 · Cited by 1,492
Self-citationZhao, J., Brault, J. J., Schild, A., Cao, P., Sandri, M., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.004 · Cited by 1,489
Self-citationLysosomal calcium signalling regulates autophagy through calcineurin and TFEB
Medina, D. L., Paola, S. D., Peluso, I., Armani, A., Stefani, D. D., Venditti, R., Montefusco, S., Rosato, A. S., Prezioso, C., Forrester, A. R., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3114 · Cited by 1,452
Self-citationUbiquitination in disease pathogenesis and treatment
Popovic, D., Vucic, D., & Đikić, I. (2014) · Nature Medicine · doi:10.1038/nm.3739 · Cited by 1,443
IKKβ/NF-κB Activation Causes Severe Muscle Wasting in Mice
Cai, D., Frantz, J. D., Tawa, N. E., Melendez, P. A., Oh, B.-C., Lidov, H. G. W., Hasselgren, P.-O., Frontera, W. R., Lee, J., Glass, D. J., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.027 · Cited by 1,367
(2004) · doi:10.1016/s0092-8674(04)00452-0 · Cited by 1,356
FOXO transcription factors at the interface between longevity and tumor suppression
Greer, E. L., & Brunet, A. (2005) · Oncogene · doi:10.1038/sj.onc.1209086 · Cited by 1,340
Cellular and molecular mechanisms of muscle atrophy
Bonaldo, P., & Sandri, M. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.010389 · Cited by 1,284
Self-citationAutophagy is required to maintain muscle mass.
Masiero, E., Agatea, L., Mammucari, C., Blaauw, B., Loro, E., Komatsu, M., Metzger, D., Reggiani, C., Schiaffino, S., & Sandri, M. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.10.008 · Cited by 1,282
Self-citationProtein degradation by the ubiquitin-proteasome pathway in normal and disease states
Lecker, S. H., Goldberg, A. L., & Mitch, W. E. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006010083 · Cited by 1,234
Self-citationCancer Cachexia: Mediators, Signaling, and Metabolic Pathways
Fearon, K. C. H., Glass, D. J., & Guttridge, D. C. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.06.011 · Cited by 1,244
Tisdale, M. J. (2009) · Physiological Reviews · doi:10.1152/physrev.00016.2008 · Cited by 1,216
Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx/atrogin-1
Bodine, S. C., & Baehr, L. M. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00204.2014 · Cited by 1,159
Muscle wasting in disease: molecular mechanisms and promising therapies
Cohen, S., Nathan, J. A., & Goldberg, A. L. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4467 · Cited by 1,089
Self-citationThe SCF ubiquitin ligase: insights into a molecular machine
Cardozo, T., & Pagano, M. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1471 · Cited by 1,114
Dynamic FoxO transcription factors
Huang, H., & Tindall, D. J. (2007) · Journal of Cell Science · doi:10.1242/jcs.001222 · Cited by 1,124
Skeletal muscle hypertrophy and atrophy signaling pathways
Glass, D. J. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.04.018 · Cited by 1,106
Maltais, F., Decramer, M., Casaburi, R. H., Barreiro, E., Burelle, Y., Debigaré, R., Dekhuijzen, P. N. R., Franssen, F. M. E., Gayan‐Ramirez, G., Gea, J., et al. (2014) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201402-0373st · Cited by 1,165
Hill, J. A., & Olson, E. N. (2008) · New England Journal of Medicine · doi:10.1056/nejmra072139 · Cited by 1,111
FOXOs: signalling integrators for homeostasis maintenance
Eijkelenboom, A., & Burgering, B. M. T. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3507 · Cited by 1,110
The Molecular Basis of Skeletal Muscle Atrophy
Jackman, R. W., & Kandarian, S. C. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00579.2003 · Cited by 1,008
Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607795103 · Cited by 974
Self-citationLoffredo, F. S., Steinhauser, M. L., Jay, S. M., Gannon, J., Pancoast, J. R., Yalamanchi, P., Sinha, M., Dall’Osso, C., Khong, D., Shadrach, J. L., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.015 · Cited by 948
“Although it is plausible that the antihypertrophic effect of rGDF11 is mediated by FoxO-dependent proteasomemediated protein degradation (Sandri et al., 2004), our data do not explain the differential effects of rGDF11 and myostatin.”
Reversal of Cancer Cachexia and Muscle Wasting by ActRIIB Antagonism Leads to Prolonged Survival
Zhou, X., Wang, J. L., Lu, J., Song, Y., Kwak, K. S., Jiao, Q., Rosenfeld, R., Chen, Q., Boone, T. C., Simonet, W. S., et al. (2010) · Cell · doi:10.1016/j.cell.2010.07.011 · Cited by 960
Self-citationSignaling in Muscle Atrophy and Hypertrophy
Sandri, M. (2008) · Physiology · doi:10.1152/physiol.00041.2007 · Cited by 866
Self-citationRegulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models
Schiaffino, S., & Mammucari, C. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-4 · Cited by 816
“Small interfering RNA to FoxO1 and FoxO3 Knockdown of FoxO1 and FoxO3 by RNA interference Prevention of atrogin-1 reporter upregulation induced by starvation [ 91 ]”
BackgroundInfluentialSelf-citationSignaling Pathways in Skeletal Muscle Remodeling
Bassel‐Duby, R., & Olson, E. N. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142622 · Cited by 823
Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size
Trendelenburg, A. U., Meyer, A., Rohner, D., Boyle, J., Hatakeyama, S., & Glass, D. J. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00105.2009 · Cited by 792
The Interplay Between Mitochondrial Dynamics and Mitophagy
Twig, G., & Shirihai, O. S. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3779 · Cited by 778
Ward, N. C., Watts, G. F., & Eckel, R. H. (2019) · Circulation Research · doi:10.1161/circresaha.118.312782 · Cited by 799
Transcriptional mechanisms regulating skeletal muscle differentiation, growth and homeostasis
Braun, T., & Gautel, M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3118 · Cited by 713
The Molecular Bases of Training Adaptation
Coffey, V. G., & Hawley, J. A. (2007) · Sports Medicine · doi:10.2165/00007256-200737090-00001 · Cited by 756
Long live FOXO : unraveling the role of FOXO proteins in aging and longevity
Martins, R., Lithgow, G. J., & Link, W. (2015) · Aging Cell · doi:10.1111/acel.12427 · Cited by 758
Satellite Cells and Skeletal Muscle Regeneration
Dumont, N. A., Bentzinger, C. F., Sincennes, M., & Rudnicki, M. A. (2015) · Comprehensive Physiology · doi:10.1002/cphy.c140068 · Cited by 719
Milan, G., Romanello, V., Pescatore, F., Armani, A., Paik, J.-H., Frasson, L., Seydel, A., Zhao, J., Abraham, R., Goldberg, A. L., et al. (2015) · Nature Communications · doi:10.1038/ncomms7670 · Cited by 709
Self-citationGlucocorticoid-Induced Skeletal Muscle Atrophy
Schakman, O., Kalista, S., Barbé, C., Loumaye, A., & Thissen, J. P. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.036 · Cited by 705
Rejuvenation of the muscle stem cell population restores strength to injured aged muscles
Cosgrove, B. D., Gilbert, P. M., Porpiglia, E., Mourkioti, F., Lee, S. P., Corbel, S. Y., Llewellyn, M. E., Delp, S. L., & Blau, H. M. (2014) · Nature Medicine · doi:10.1038/nm.3464 · Cited by 677
The E3 Ligase MuRF1 Degrades Myosin Heavy Chain Protein in Dexamethasone-Treated Skeletal Muscle
Clarke, B. A., Drujan, D., Willis, M. S., Murphy, L. O., Corpina, R. A., Burova, E., Rakhilin, S. V., Stitt, T. N., Patterson, C., Latres, E., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.09.009 · Cited by 683
Skeletal muscle: A review of molecular structure and function, in health and disease
Mukund, K., & Subramaniam, S. (2019) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1462 · Cited by 805
FOXO/4E-BP Signaling in Drosophila Muscles Regulates Organism-wide Proteostasis during Aging
Demontis, F., & Perrimon, N. (2010) · Cell · doi:10.1016/j.cell.2010.10.007 · Cited by 656
Bentzinger, C. F., Romanino, K., Cloëtta, D., Lin, S., Mascarenhas, J. B., Oliveri, F., Xia, J., Casanova, E., Costa, C. F., Brink, M., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.10.002 · Cited by 640
Oxidative Stress, Molecular Inflammation and Sarcopenia
Meng, S.-J., & Yu, L.-J. (2010) · International Journal of Molecular Sciences · doi:10.3390/ijms11041509 · Cited by 637
Muscle type and fiber type specificity in muscle wasting
Ciciliot, S., Rossi, C. A., Dyar, K. A., Blaauw, B., & Schiaffino, S. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.016 · Cited by 644
Self-citationMechanisms of muscle wasting in chronic kidney disease
Wang, X. H., & Mitch, W. E. (2014) · Nature Reviews Nephrology · doi:10.1038/nrneph.2014.112 · Cited by 630
FOXO transcription factors: key regulators of cellular quality control
Webb, A. E., & Brunet, A. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.02.003 · Cited by 649
Wang, X., Hu, Z., Hu, J., Du, J., & Mitch, W. E. (2006) · Endocrinology · doi:10.1210/en.2006-0251 · Cited by 600
The miRNA-212/132 family regulates both cardiac hypertrophy and cardiomyocyte autophagy
Ucar, A., Gupta, S. K., Fiedler, J., Erikci, E., Kardasinski, M., Batkai, S., Dangwal, S., Kumarswamy, R., Bang, C., Holzmann, A., et al. (2012) · Nature Communications · doi:10.1038/ncomms2090 · Cited by 610
Sacheck, J. M., Ohtsuka, A., McLary, S. C., & Goldberg, A. L. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00073.2004 · Cited by 606
Self-citationFoxO proteins in insulin action and metabolism
Barthel, A., Schmoll, D., & Unterman, T. G. (2005) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2005.03.010 · Cited by 615
FoxO transcription factors in the maintenance of cellular homeostasis during aging
Salih, D. A., & Brunet, A. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.02.005 · Cited by 604
Li, Y.-P., Chen, Y., John, J., Moylan, J. S., Jin, B., Mann, D. L., & Reid, M. B. (2005) · The FASEB Journal · doi:10.1096/fj.04-2364com · Cited by 634
Mitochondrial fission and remodelling contributes to muscle atrophy
Romanello, V., Guadagnin, E., Gomes, L., Roder, I., Sandri, C., Petersen, Y., Milan, G., Masiero, E., Del Piccolo, P., Foretz, M., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.60 · Cited by 596
Self-citationA review on the mechanisms of blood-flow restriction resistance training-induced muscle hypertrophy
Pearson, S. J., & Hussain, S. R. (2015) · Sports Medicine · doi:10.1007/s40279-014-0264-9 · Cited by 592
Sacheck, J. M., Hyatt, J. K., Raffaello, A., Thomas Jagoe, R., Roy, R. R., Reggie Edgerton, V., Lecker, S. H., & Goldberg, A. L. (2007) · The FASEB Journal · doi:10.1096/fj.06-6604com · Cited by 585
Self-citationSalminen, A., Huuskonen, J., Ojala, J., Kauppinen, A., Kaarniranta, K., & Suuronen, T. (2008) · Ageing Research Reviews · doi:10.1016/j.arr.2007.09.002 · Cited by 581
The gut microbiota influences skeletal muscle mass and function in mice
Lahiri, S., Kim, H., Garcia-Perez, I., Reza, M. M., Martin, K. A., Kundu, P., Cox, L. M., Selkrig, J., Posma, J. M., Zhang, H., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aan5662 · Cited by 580
Kamei, Y., Miura, S., SUZUKI, M. T., Kai, Y., Mizukami, J., Taniguchi, T., Mochida, K., Tomoko, H. A. T. A., Matsuda, J., Aburatani, H., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400674200 · Cited by 588
Understanding cachexia as a cancer metabolism syndrome
Porporato, P. E. (2016) · Oncogenesis · doi:10.1038/oncsis.2016.3 · Cited by 562
FoxO1 protects against pancreatic β cell failure through NeuroD and MafA induction
Kitamura, Y., Kitamura, T., Kruse, J.-P., Raum, J. C., Stein, R. W., Gu, W. J., & Accili, D. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.08.004 · Cited by 565
Signaling pathways controlling skeletal muscle mass
Egerman, M. A., & Glass, D. J. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.857291 · Cited by 555
The role of FoxO in the regulation of metabolism
Gross, D. N., van den Heuvel, A. P. J., & Birnbaum, M. J. (2008) · Oncogene · doi:10.1038/onc.2008.25 · Cited by 571
Grumati, P., Coletto, L., Sabatelli, P., Cescon, M., Angelin, A., Bertaggia, E., Blaauw, B., Urciuolo, A., Tiepolo, T., Merlini, L., et al. (2010) · Nature Medicine · doi:10.1038/nm.2247 · Cited by 540
Self-citationCancer cachexia is regulated by selective targeting of skeletal muscle gene products
Acharyya, S., Ladner, K. J., Nelsen, L., Damrauer, J. S., Reiser, P. J., Swoap, S. J., & D, D. C. G. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20174 · Cited by 541
Glucocorticoids, metabolism and metabolic diseases
Vegiopoulos, A., & Herzig, S. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2007.05.015 · Cited by 535
Role of Inflammation in Muscle Homeostasis and Myogenesis
Costamagna, D., Costelli, P., Sampaolesi, M., & Penna, F. (2015) · Mediators of Inflammation · doi:10.1155/2015/805172 · Cited by 554
Latres, E., Amini, A. R., Amini, A. A., Griffiths, J., Martin, F. J., Wei, Y., Lin, H. C., Yancopoulos, G. D., & Glass, D. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407517200 · Cited by 538
Smad2 and 3 transcription factors control muscle mass in adulthood
Sartori, R., Milan, G., Patron, M., Mammucari, C., Blaauw, B., Abraham, R., & Sandri, M. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00104.2009 · Cited by 517
Self-citationFoxO1 Regulates Multiple Metabolic Pathways in the Liver
Zhang, W., Patil, S., Chauhan, B., Guo, S., Powell, D. R., Le, J., Klotsas, A., Matika, R. W., Xiao, X., Franks, R. R., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600272200 · Cited by 522
Sarcopenia in chronic kidney disease: what have we learned so far?
Sabatino, A., Cuppari, L., Stenvinkel, P., Lindholm, B., & Avesani, C. M. (2020) · Journal of Nephrology · doi:10.1007/s40620-020-00840-y · Cited by 549
Mechanisms of glucocorticoid-induced myopathy
Schakman, O., Gilson, H., & Thissen, J. P. (2008) · Journal of Endocrinology · doi:10.1677/joe-07-0606 · Cited by 521
Skeletal Muscle Is a Primary Target of SOD1G93A-Mediated Toxicity
Dobrowolny, G., Aucello, M., Rizzuto, E., Beccafico, S., Mammucari, C., Bonconpagni, S., Belia, S., Wannenes, F., Nicoletti, C., Del Prete, Z., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.09.002 · Cited by 513
Self-citationCritical role of FOXO3a in carcinogenesis
Liu, Y., Ao, X., Ding, W., Ponnusamy, M., Wu, W., Hao, X., Yu, W., Wang, Y., Li, P., & Wang, J. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0856-3 · Cited by 511
Greenhaff, P. L., Karagounis, L. G., Peirce, N., Simpson, E. J., Hazell, M., Layfield, R., Wackerhage, H., Smith, K., Atherton, P., Selby, A., et al. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90411.2008 · Cited by 495
Crosstalk between Glucocorticoid Receptor and Nutritional Sensor mTOR in Skeletal Muscle
Shimizu, N., Yoshikawa, N., Ito, N., Maruyama, T., Suzuki, Y., Takeda, S.-I., Nakae, J., Tagata, Y., Nishitani, S., Takehana, K., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.01.001 · Cited by 498
AMPK in skeletal muscle function and metabolism
Kjøbsted, R., Hingst, J. R., Fentz, J., Foretz, M., Sanz, M.-N., Pehmøller, C. K., Shum, M., Marette, A., Mounier, R., Treebak, J. T., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700442r · Cited by 517
Targeting Proteins for Destruction by the Ubiquitin System: Implications for Human Pathobiology
Schwartz, A. L., & Ciechanover, A. J. (2008) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.051208.165340 · Cited by 498
Lenk, K., Schuler, G. C., & Adams, V. (2010) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-010-0007-1 · Cited by 498
Effects of Exercise and Aging on Skeletal MusclePreprint
Distéfano, G., & Goodpaster, B. H. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a029785 · Cited by 530
McFarlane, C., Plummer, E., Thomas, M., Hennebry, A., Ashby, M. G., Ling, N., Smith, H., Sharma, M., & Kambadur, R. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20757 · Cited by 496
BMP signaling controls muscle mass
Sartori, R., Schirwis, E., Blaauw, B., Bortolanza, S., Zhao, J., Enzo, E., Stantzou, A., Mouisel, E., Toniolo, L., Ferry, A., et al. (2013) · Nature Genetics · doi:10.1038/ng.2772 · Cited by 467
Self-citationLouis, E., Raue, U., Yang, Y., Jemiolo, B., & Trappe, S. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00679.2007 · Cited by 478
Sandri, M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.056 · Cited by 451
Self-citationMyogenin and Class II HDACs Control Neurogenic Muscle Atrophy by Inducing E3 Ubiquitin Ligases
Moresi, V., Williams, A. H., Meadows, E., Flynn, J. M., Potthoff, M. J., McAnally, J., Shelton, J. M., Backs, J., Klein, W. H., Richardson, J. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.09.004 · Cited by 457
Mitochondrial quality control and muscle mass maintenance.
Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434
Self-citationTalbot, J. C., & Maves, L. (2016) · Wiley Interdisciplinary Reviews Developmental Biology · doi:10.1002/wdev.230 · Cited by 494
New fundamental resistance exercise determinants of molecular and cellular muscle adaptations
Toigo, M., & Boutellier, U. (2006) · European Journal of Applied Physiology · doi:10.1007/s00421-006-0238-1 · Cited by 437
Li, H., Kedar, V., Zhang, C., McDonough, H., Arya, R., Wang, D.-Z., & Patterson, C. (2004) · Journal of Clinical Investigation · doi:10.1172/jci22220 · Cited by 439
FoxO Transcription Factors Promote Autophagy in Cardiomyocytes
Sengupta, A., Molkentin, J. D., & Yutzey, K. E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.024406 · Cited by 446
Bowen, T. S., Schuler, G. C., & Adams, V. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12043 · Cited by 445
Autophagy Impairment in Muscle Induces Neuromuscular Junction Degeneration and Precocious Aging
Carnio, S., LoVerso, F., Baraibar, M. A., Longa, E., Khan, M. M., Maffei, M., Reischl, M., Canepari, M., Loefler, S., Kern, H., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.07.061 · Cited by 423
Self-citationMechanisms Regulating Neuromuscular Junction Development and Function and Causes of Muscle Wasting
Tintignac, L. A. J., Brenner, H.-R., & Rüegg, M. A. (2015) · Physiological Reviews · doi:10.1152/physrev.00033.2014 · Cited by 449
Roberts, E. W., Deonarine, A., Jones, J. O., Denton, A. E., Feig, C., Lyons, S. K., Espéli, M., Kraman, M., McKenna, B., Wells, R. J. B., et al. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20122344 · Cited by 428
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