The DOI matches its Crossref record; 50 of the 51 references it cites were found in a registry or an index.
Skeletal Muscle-Specific Ablation of raptor, but Not of rictor, Causes Metabolic Changes and Results in Muscle Dystrophy
Open accessAbstract
Mammalian target of rapamycin (mTOR) is a central controller of cell growth. mTOR assembles into two distinct multiprotein complexes called mTOR complex 1 (mTORC1) and mTORC2. Here we show that the mTORC1 component raptor is critical for muscle function and prolonged survival. In contrast, muscles lacking the mTORC2 component rictor are indistinguishable from wild-type controls. Raptor-deficient muscles become progressively dystrophic, are impaired in their oxidative capacity, and contain increased glycogen stores, but they express structural components indicative of oxidative muscle fibers. Biochemical analysis indicates that these changes are probably due to loss of activation of direct downstream targets of mTORC1, downregulation of genes involved in mitochondrial biogenesis, including PGC1alpha, and hyperactivation of PKB/Akt. Finally, we show that activation of PKB/Akt does not require mTORC2. Together, these results demonstrate that muscle mTORC1 has an unexpected role in the regulation of the metabolic properties and that its function is essential for life.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Conditional deletion of mTOR with a concomitant expression of catalytically inactive mTOR, resulted in a growth rate defect that started after 1 week of age. Importantly, these mice show a more severe muscle loss when compared with the conditional RAPTOR knockout11.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [11]
In the citing paper
“While muscle-specific Rictor knockout mice do not show any overt phenotype conversely, Raptor- and mTOR-deficient mice display reduced postnatal growth, due to the reduced size of fast but not slow muscle fibers and a progressive muscular dystrophy phenotype11,12.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [11]
In the citing paper
“Deletion of the mTORC1 component raptor in mouse skeletal muscle affects PGC1α expression, reducing oxidative capacity36, and consequently inducing premature ageing.”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [36]
In the citing paper
“Knocking out the Raptor complex in adipose tissue enhances mitochondrial respiration244, but muscle-specific knockout causes muscular dystrophy in mice36.”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [36]
Citations
Cites
Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216
TOR signaling in growth and metabolism
Wullschleger, S., Loewith, R., & Hall, M. N. (2006) · Cell · doi:10.1016/j.cell.2006.01.016 · Cited by 5,787
Self-citationSandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012
Alessi, D. R., James, S. R., Downes, C. P., Holmes, A. B., Gaffney, P. R. J., Reese, C. B., & Cohen, P. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00122-9 · Cited by 2,874
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
Sarbassov, D. D., Ali, S. M., Kim, D.-H., Guertin, D. A., Latek, R. R., Erdjument-Bromage, H., Tempst, P., & Sabatini, D. M. (2004) · Current Biology · doi:10.1016/j.cub.2004.06.054 · Cited by 2,665
Transcriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres
Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546
Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
Jacinto, E., Loewith, R., Schmidt, A., Lin, S., Rüegg, M. A., Hall, A., & Hall, M. N. (2004) · Nature Cell Biology · doi:10.1038/ncb1183 · Cited by 2,097
Self-citationTargets for Cell Cycle Arrest by the Immunosuppressant Rapamycin in Yeast
Heitman, J., Movva, N. R., & Hall, M. N. (1991) · Science · doi:10.1126/science.1715094 · Cited by 2,055
Self-citationStitt, 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
Cited by
Sorted by citations
Items 201–300 of 638
Acute mTOR inhibition induces insulin resistance and alters substrate utilization in vivo
Kleinert, M., Sylow, L., Fazakerley, D. J., Krycer, J. R., Thomas, K. C., Oxboll, A., Jordy, A. B., Jensen, T. E., Yang, G., Schjerling, P., et al. (2014) · Molecular Metabolism · doi:10.1016/j.molmet.2014.06.004 · Cited by 89
Self-citationJaiswal, N., Gavin, M., Loro, E., Sostre‐Colón, J., Roberson, P. A., Uehara, K., Rivera‐Fuentes, N., Neinast, M., Arany, Z., Kimball, S. R., et al. (2022) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12846 · Cited by 79
Ye, L., Varamini, B., Lamming, D. W., Sabatini, D. M., & Baur, J. A. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2012.00177 · Cited by 85
Rosario, F. J., Gupta, M. B., Myatt, L., Powell, T. L., Glenn, J. P., Cox, L., & Jansson, T. (2019) · Scientific Reports · doi:10.1038/s41598-018-36265-8 · Cited by 77
Mammalian TOR signaling to the AGC kinases
Su, B., & Jacinto, E. (2011) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2011.618113 · Cited by 79
mTORC1 Plays an Important Role in Skeletal Development by Controlling Preosteoblast Differentiation
Fitter, S., Matthews, M. P., Martin, S. K., Xie, J., Ooi, S. S., Walkley, C. R., Codrington, J. D., Rüegg, M. A., Hall, M. N., Proud, C. G., et al. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00668-16 · Cited by 79
Self-citationSkeletal muscle mTORC1 regulates neuromuscular junction stability
Baraldo, M., Geremia, A., Pirazzini, M., Nogara, L., Solagna, F., Türk, C., Nolte, H., Romanello, V., Megighian, A., Boncompagni, S., et al. (2020) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12496 · Cited by 76
mTOR: A Potential New Target in Nonalcoholic Fatty Liver Disease
Feng, J., Qiu, S., Zhou, S., Tan, Y., Bai, Y., Cao, H., Guo, J., & Su, Z. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169196 · Cited by 73
Serra, C., Sandor, N. L., Jang, H., Lee, D. C., Toraldo, G., Guarneri, T., Wong, S., Zhang, A., Guo, W., Jasuja, R., et al. (2013) · Endocrinology · doi:10.1210/en.2013-1004 · Cited by 75
mTORC2 Signaling Drives the Development and Progression of Pancreatic Cancer
Driscoll, D. R., Karim, S. A., Sano, M., Gay, D. M., Jacob, W., Yu, J. Q., Mizukami, Y., Gopinathan, A., Jodrell, D. I., Evans, T. R. J., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-0810 · Cited by 78
Self-citationNorrmén, C., Figlia, G., Pfistner, P., Pereira, J. A., Bachofner, S., & Suter, U. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.3619-17.2018 · Cited by 74
Gureev, A. P., Popov, V. N., & Starkov, A. A. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113285 · Cited by 75
In vivo evidence for mTORC2-mediated actin cytoskeleton rearrangement in neurons
Angliker, N., & Rüegg, M. A. (2013) · BioArchitecture · doi:10.4161/bioa.26497 · Cited by 74
Self-citationRictor/mTORC2 facilitates central regulation of energy and glucose homeostasis
Kocalis, H. E., Hagan, S. L., George, L., Turney, M. K., Siuta, M., Laryea, G. N., Morris, L. C., Muglia, L. J., Printz, R. L., Stanwood, G. D., et al. (2014) · Molecular Metabolism · doi:10.1016/j.molmet.2014.01.014 · Cited by 76
Ferretti, R., Moura, E. G., dos Santos, V. C., Caldeira, E. J., Conte, M., Matsumura, C. Y., Pertille, A., & Mosqueira, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0199728 · Cited by 77
Is REDD1 a metabolic double agent? Lessons from physiology and pathology
Britto, F. A., Dumas, K., Giorgetti‐Peraldi, S., Ollendorff, V., & Favier, F. B. (2020) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00340.2020 · Cited by 72
mTOR-Dependent Regulation of PHLPP Expression Controls the Rapamycin Sensitivity in Cancer Cells
Liu, J., Stevens, P. D., & Gao, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.183087 · Cited by 72
Carson, R. P., Fu, C., Winzenburger, P. A., & Ess, K. C. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds414 · Cited by 70
IKKα and alternative NF-κB regulate PGC-1β to promote oxidative muscle metabolism
Bakkar, N., Ladner, K. J., Canan, B. D., Liyanarachchi, S., Bal, N. C., Pant, M., Periasamy, M., Li, Q., Janssen, P. M. L., & Guttridge, D. C. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201108118 · Cited by 74
Lkb1 Is Indispensable for Skeletal Muscle Development, Regeneration, and Satellite Cell Homeostasis
Shan, T., Zhang, P., Liang, X., Bi, P., Yue, F., & Kuang, S. (2014) · Stem Cells · doi:10.1002/stem.1788 · Cited by 74
High mitochondria content is associated with prostate cancer disease progression
Grupp, K., Jedrzejewska, K., Tsourlakis, M. C., Koop, C., Wilczak, W., Adam, M., Quaas, A., Sauter, G., Simon, R., Izbicki, J. R., et al. (2013) · Molecular Cancer · doi:10.1186/1476-4598-12-145 · Cited by 70
The Intriguing Regulators of Muscle Mass in Sarcopenia and Muscular Dystrophy
Sakuma, K., Aoi, W., & Yamaguchi, A. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00230 · Cited by 70
mTOR controls ChREBP transcriptional activity and pancreatic β cell survival under diabetic stress
Chau, G. C., Im, D. U., Kang, T. M., Bae, J. M., Kim, W., Pyo, S., Moon, E.-Y., & Um, S. H. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201701085 · Cited by 67
Ogasawara, R., & Suginohara, T. (2018) · The FASEB Journal · doi:10.1096/fj.201701422r · Cited by 66
Hypothalamic mTORC2 is essential for metabolic health and longevity
Chellappa, K., Brinkman, J. A., Mukherjee, S., Morrison, M., Alotaibi, M. I., Carbajal, K. A., Alhadeff, A. L., Perron, I. J., Yao, R., Purdy, C. S., et al. (2019) · Aging Cell · doi:10.1111/acel.13014 · Cited by 62
mTOR Inhibitor Therapy and Metabolic Consequences: Where Do We Stand?
Kezić, A., Popović, L., & Lalic, K. S. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2640342 · Cited by 68
Liu, L., Inoki, A., Fan, K., Mao, F., Shi, G., Jin, X., Zhao, M., Ney, G. M., Jones, M., Sun, S., et al. (2020) · Blood · doi:10.1182/blood.2020007975 · Cited by 62
mTOR controls embryonic and adult myogenesis via mTORC1
Rion, N., Castets, P., Lin, S., Enderle, L., Reinhard, J. R., Eickhorst, C., & Rüegg, M. A. (2019) · Development · doi:10.1242/dev.172460 · Cited by 68
Self-citationDamanti, S., Azzolino, D., Roncaglione, C., Arosio, B., Rossi, P. D., & Cesari, M. (2019) · Nutrients · doi:10.3390/nu11091991 · Cited by 72
Microbiota-induced tissue signals regulate ILC3-mediated antigen presentation
Lehmann, F. M., von Burg, N., Ivánek, R., Teufel, C., Horváth, E. J., Peter, A., Turchinovich, G., Staehli, D., Eichlisberger, T., de Agüero, M. G., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15612-2 · Cited by 69
Paez, H. G., Pitzer, C. R., & Alway, S. E. (2023) · Cells · doi:10.3390/cells12020249 · Cited by 71
Makki, K., Taront, S., Molendi‐Coste, O., Bouchaert, E., Neve, B., Eury, E., Lobbens, S., Labalette, M., Duez, H., Staels, B., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092684 · Cited by 67
Cardiac mTOR complex 2 preserves ventricular function in pressure-overload hypertrophy
Shende, P., Xu, L., Morandi, C., Pentassuglia, L., Heim, P., Lebboukh, S., Berthonneche, C., Pedrazzini, T., Kaufmann, B. A., Hall, M. N., et al. (2015) · Cardiovascular Research · doi:10.1093/cvr/cvv252 · Cited by 67
Self-citationActivation of AKT-mTOR Signaling Directs Tenogenesis of Mesenchymal Stem Cells
Cong, X. X., Rao, X. S., Lin, J., Liu, X. C., Zhang, G. A., Gao, X. K., He, M. Y., Shen, W., Fan, W., Pioletti, D. P., et al. (2018) · Stem Cells · doi:10.1002/stem.2765 · Cited by 65
mTORC1 signaling in energy balance and metabolic disease
Catania, C., Binder, E., & Cota, D. (2010) · International Journal of Obesity · doi:10.1038/ijo.2010.208 · Cited by 68
Haegens, A., Schols, A. M. W. J., van Essen, A. L., van Loon, L. J. C., & LANGEN, R. C. J. (2012) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201100695 · Cited by 66
The Complex Roles of Mechanistic Target of Rapamycin in Adipocytes and Beyond
Lee, P. L., Jung, S. M., & Guertin, D. A. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.01.004 · Cited by 66
Amino acid starvation has opposite effects on mitochondrial and cytosolic protein synthesis
Johnson, M. A., Vidoni, S., Durigon, R., Pearce, S. F., Rorbach, J., He, J., Brea-Calvo, G., Minczuk, M., Reyes, A., Holt, I. J., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093597 · Cited by 63
The role of mTORC1 in the regulation of skeletal muscle mass
Bodine, S. C. (2022) · Faculty Reviews · doi:10.12703/r/11-32 · Cited by 74
mTORC2 and AMPK differentially regulate muscle triglyceride content via Perilipin 3
Kleinert, M., Parker, B. L., Chaudhuri, R., Fazakerley, D. J., Serup, A. K., Thomas, K. C., Krycer, J. R., Sylow, L., Fritzen, A. M., Hoffman, N. J., et al. (2016) · Molecular Metabolism · doi:10.1016/j.molmet.2016.06.007 · Cited by 61
Self-citationCastro, W., Chelbi, S. T., Niogret, C., Ramón-Barros, C., Welten, S. P. M., Osterheld, K., Wang, H., Rota, G., Morgado, L., Vivier, É., et al. (2018) · Nature Immunology · doi:10.1038/s41590-018-0144-9 · Cited by 62
The Regulatory Effects of mTOR Complexes in the Differentiation and Function of CD4 + T Cell Subsets
Wang, P., Zhang, Q., Tan, L., Xu, Y., Xie, X., & Zhao, Y. X. (2020) · Journal of Immunology Research · doi:10.1155/2020/3406032 · Cited by 61
mTOR in health and in sickness
Liko, D., & Hall, M. N. (2015) · Journal of Molecular Medicine · doi:10.1007/s00109-015-1326-7 · Cited by 60
Self-citationA role for Raptor phosphorylation in the mechanical activation of mTOR signaling
Frey, J. W., Jacobs, B. L., Goodman, C. A., & Hornberger, T. A. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.11.009 · Cited by 65
mTORC2 critically regulates renal potassium handling
Grahammer, F., Nesterov, V., Ahmed, A., Steinhardt, F., Sandner, L., Arnold, F., Cordts, T., Negrea, S., Bertog, M., Rüegg, M. A., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci80304 · Cited by 59
Self-citationSpangenburg, E. E. (2009) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h09-010 · Cited by 64
Mammalian target of rapamycin complex 2 regulates muscle glucose uptake during exercise in mice
Kleinert, M., Parker, B. L., Fritzen, A. M., Knudsen, J. R., Jensen, T. E., Kjøbsted, R., Sylow, L., Ruegg, M., James, D. E., & Richter, E. A. (2017) · The Journal of Physiology · doi:10.1113/jp274203 · Cited by 59
Song, X., Shen, Q., Fan, L., Yu, Q., Jia, X., Sun, Y., Bai, W., & Kang, J. (2018) · Oncotarget · doi:10.18632/oncotarget.24190 · Cited by 61
Agrawal, P., Chen, Y., Schilling, B., Gibson, B. W., & Hughes, R. E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.328021 · Cited by 60
Gorre, N., Adhikari, D., Lindkvist, R., Brännström, M., Liu, K., & Shen, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110491 · Cited by 61
Kalista, S., Schakman, O., Gilson, H., Lause, P., Demeulder, B., Bertrand, L., Pende, M., & Thissen, J. (2011) · Endocrinology · doi:10.1210/en.2011-1687 · Cited by 60
Pten Loss Induces Autocrine FGF Signaling to Promote Skin Tumorigenesis
Hertzler-Schaefer, K., Mathew, G., Somani, A.-K. B., Tholpady, S. S., Kadakia, M., Chen, Y., Spandau, D. F., & Zhang, X. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.01.045 · Cited by 59
Sarcopenia in the aging high-fat fed rat: a pilot study for modeling sarcopenic obesity in rodents
Bollheimer, L. C., Buettner, R., Pongratz, G., Brunner-Ploss, R., Hechtl, C., Banas, M., Singler, K., Hamer, O. W., Stroszczynski, C., Sieber, C. C., et al. (2012) · Biogerontology · doi:10.1007/s10522-012-9405-4 · Cited by 57
Impaired mTORC1-Dependent Expression of Homer-3 Influences SCA1 Pathophysiology
Ruegsegger, C., Stucki, D., Steiner, S., Angliker, N., Radecke, J., Keller, E., Zuber, B., Rüegg, M. A., & Saxena, S. (2016) · Neuron · doi:10.1016/j.neuron.2015.11.033 · Cited by 55
Self-citationBiology of Activating Transcription Factor 4 (ATF4) and Its Role in Skeletal Muscle Atrophy
Ebert, S. M., Rasmussen, B. B., Judge, A. R., Judge, S. M., Larsson, L., Wek, R. C., Anthony, T. G., Marcotte, G. R., Miller, M. J., Yorek, M. A., et al. (2021) · Journal of Nutrition · doi:10.1093/jn/nxab440 · Cited by 64
Skeletal muscle protein balance in mTOR heterozygous mice in response to inflammation and leucine
Lang, C. H., Frost, R. A., Bronson, S. K., Lynch, C. J., & Vary, T. C. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00676.2009 · Cited by 57
Kong, B. C., Lassiter, K., Piekarski, A., Dridi, S., Reverter, A., Hudson, N. J., & Bottje, W. G. (2016) · PLoS ONE · doi:10.1371/journal.pone.0155679 · Cited by 61
Lee, H.-K., Kwon, B., Lemere, C. A., de la Monte, S., Itamura, K., Ha, A. Y., & Querfurth, H. W. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-161029 · Cited by 57
Modulation of asymmetric cell division as a mechanism to boost CD8 + T cell memory
Borsa, M., Barnstorf, I., Baumann, N. S., Pallmer, K., Yermanos, A., Gräbnitz, F., Barandun, N., Hausmann, A., Sandu, I., Barral, Y., et al. (2019) · Science Immunology · doi:10.1126/sciimmunol.aav1730 · Cited by 58
The role of mitochondria in mTOR‐regulated longevity
Wei, Y., Zhang, Y., Cai, Y., & Xu, M. (2015) · Biological Reviews · doi:10.1111/brv.12103 · Cited by 56
Mazelin, L., Panthu, B., Nicot, A.-S., Belotti, E., Tintignac, L. A. J., Teixeira, G., Zhang, Q., Risson, V., Baas, D., Delaune, E. A., et al. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.04.011 · Cited by 56
Resistance Exercise-Induced Hypertrophy: A Potential Role for Rapamycin-Insensitive mTOR
Ogasawara, R., Jensen, T. E., Goodman, C. A., & Hornberger, T. A. (2019) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000189 · Cited by 58
Dutchak, P. A., Estill-Terpack, S. J., Plec, A. A., Zhao, X., Yang, C., Chen, J., Ko, B., Deberardinis, R. J., Yu, Y., & Tu, B. P. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.058 · Cited by 53
Leucine limitation regulates myf5 and myoD expression and inhibits myoblast differentiation
Avérous, J., Gabillard, J., Seiliez, I., & Dardevet, D. P. (2011) · Experimental Cell Research · doi:10.1016/j.yexcr.2011.10.015 · Cited by 59
Immune Regulation by Rapamycin: Moving Beyond T Cells
Janes, M. R., & Fruman, D. A. (2009) · Science Signaling · doi:10.1126/scisignal.267pe25 · Cited by 58
Growth factor, energy and nutrient sensing signalling pathways in metabolic ageing
Bettedi, L., & Foukas, L. C. (2017) · Biogerontology · doi:10.1007/s10522-017-9724-6 · Cited by 55
Mammalian Target of Rapamycin (mTOR) Signaling at the Crossroad of Muscle Fiber Fate in Sarcopenia
Sirago, G., Picca, A., Calvani, R., Coelho‐Júnior, H. J., & Marzetti, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232213823 · Cited by 61
Hot topics in aging research: protein translation, 2009
Kennedy, B. K., & Kaeberlein, M. R. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00522.x · Cited by 54
Ye, L., Widlund, A. L., Sims, C. A., Lamming, D. W., Guan, Y., Davis, J. G., Sabatini, D. M., Harrison, D. E., Vang, O., & Baur, J. A. (2013) · Aging · doi:10.18632/aging.100576 · Cited by 56
Proteome-wide Adaptations of Mouse Skeletal Muscles during a Full Month in Space
Tascher, G., Brioche, T., Maes, P., Chopard, A., O’Gorman, D. J., Gauquelin‐Koch, G., Blanc, S., & Bertile, F. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00201 · Cited by 52
Britto, F. A., Cortade, F., Belloum, Y., Blaquière, M., Gallot, Y. S., Docquier, A., Pagano, A. F., Jublanc, É., Bendridi, N., Koechlin‐Ramonatxo, C., et al. (2018) · BMC Biology · doi:10.1186/s12915-018-0525-4 · Cited by 68
Langerhans cell homeostasis in mice is dependent on mTORC1 but not mTORC2 function
Kellersch, B., & Brocker, T. (2012) · Blood · doi:10.1182/blood-2012-06-439786 · Cited by 53
Yoon, S.-O., Shin, S., Karreth, F. A., Buel, G. R., Jedrychowski, M. P., Plas, D. R., Dedhar, S., Gygi, S. P., Roux, P. P., Dephoure, N., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.033 · Cited by 53
Linking Cancer Cachexia‐Induced Anabolic Resistance to Skeletal Muscle Oxidative Metabolism
Hardee, J. P., Montalvo, R. N., & Carson, J. A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/8018197 · Cited by 53
Skeletal Muscle Response to Deflazacort, Dexamethasone and Methylprednisolone
Fappi, A., Neves, J. D. C., Sanches, L. N., Silva, P. V. M. E., Sikusawa, G. Y., Brandão, T. C. P., Chadi, G., & Zanoteli, E. (2019) · Cells · doi:10.3390/cells8050406 · Cited by 54
Targeting mTOR and Glycolysis in HER2-Positive Breast Cancer
Holloway, R. W., & Marignani, P. A. (2021) · Cancers · doi:10.3390/cancers13122922 · Cited by 56
Kazi, A. A., Pruznak, A. M., Frost, R. A., & Lang, C. H. (2010) · Shock · doi:10.1097/shk.0b013e3181ecb57c · Cited by 52
A Skeletal Muscle Model of Infantile-onset Pompe Disease with Patient-specific iPS Cells
Yoshida, T., Awaya, T., Jonouchi, T., Kimura, R., Kimura, S., Era, T., Heike, T., & Sakurai, H. (2017) · Scientific Reports · doi:10.1038/s41598-017-14063-y · Cited by 56
Hodson, N., McGlory, C., Oikawa, S. Y., Jeromson, S., Song, Z., Rüegg, M. A., Hamilton, D. L., Phillips, S. M., & Philp, A. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00176.2017 · Cited by 51
Self-citationVilla-Cuesta, E., Holmbeck, M. A., & Rand, D. M. (2014) · Journal of Cell Science · doi:10.1242/jcs.142026 · Cited by 51
mTORC1 Links Protein Quality and Quantity Control by Sensing Chaperone Availability
Qian, S., Zhang, X., Sun, J., Bennink, J. R., Yewdell, J. W., & Patterson, C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.120295 · Cited by 52
Zhang, Z., Tsukikawa, M., Peng, M., Polyák, E., Nakamaru‐Ogiso, E., Ostrovsky, J., McCormack, S. E., Place, E., Clarke, C., Reiner, G., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069282 · Cited by 53
Chen, B. W., Chen, W., Liang, H., Liu, H., Liang, C., Zhi, X., Hu, L.-Q., Yu, X.-Z., Wei, T., Ma, T., et al. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-15-0029 · Cited by 50
Insulin resistance syndrome blunts the mitochondrial anabolic response following resistance exercise
Nilsson, M. I., Greene, N. P., Dobson, J. P., Wiggs, M. P., Gasier, H. G., Macias, B. R., Shimkus, K. L., & Fluckey, J. D. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00118.2010 · Cited by 55
Regulation of mRNA Translation as a Conserved Mechanism of Longevity Control
Mehta, R., Chandler-Brown, D., Ramos, F. J., Shamieh, L. S., & Kaeberlein, M. (2010) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4419-7002-2_2 · Cited by 44
Monotropein Improves Dexamethasone-Induced Muscle Atrophy via the AKT/mTOR/FOXO3a Signaling Pathways
Wang, P., Kang, S. Y., Kim, S. J., Park, Y., & Jung, H. W. (2022) · Nutrients · doi:10.3390/nu14091859 · Cited by 49
Rheb and mammalian target of rapamycin in mitochondrial homoeostasis
Groenewoud, M. J., & Zwartkruis, F. J. T. (2013) · Open Biology · doi:10.1098/rsob.130185 · Cited by 51
mTORC1 and the regulation of skeletal muscle anabolism and mass
Adegoke, O. A. J., Abdullahi, A., & Tavajohi‐Fini, P. (2012) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h2012-009 · Cited by 55
Alejandro, E. U., Bozadjieva-Kramer, N., Blandino-Rosano, M., Wasan, M., Elghazi, L., Vadrevu, S., Satin, L. S., & Bernal‐Mizrachi, E. (2017) · Diabetes · doi:10.2337/db16-1349 · Cited by 49
Glutamine at focus: versatile roles in cancer
Vitto, H. D., Pérez-Valencia, J. A., & Radosevich, J. A. (2015) · Tumor Biology · doi:10.1007/s13277-015-4671-9 · Cited by 54
Gene expression profiling of laser microdissected airway smooth muscle tissue in asthma and atopy
Yick, C. Y., Zwinderman, A. H., Kunst, P. W. A., Grünberg, K., Mauad, T., Chowdhury, S., Bel, E. H., Baas, F., Lutter, R., & Sterk, P. J. (2014) · Allergy · doi:10.1111/all.12452 · Cited by 47
Sawan, S. A., van Vliet, S., Parel, J. T., Beals, J. W., Mazzulla, M., West, D. W. D., Philp, A., Li, Z., Paluska, S. A., Burd, N. A., et al. (2018) · Physiological Reports · doi:10.14814/phy2.13628 · Cited by 52
Genome-wide shRNA screen reveals increased mitochondrial dependence upon mTORC2 addiction
Colombi, M., Molle, K. D., Benjamin, D., Rattenbacher-Kiser, K. F., Schaefer, C., Betz, C., Thiemeyer, A., Regenass, U., Hall, M. N., & Moroni, C. (2010) · Oncogene · doi:10.1038/onc.2010.539 · Cited by 46
Self-citationMolecular and biochemical regulation of skeletal muscle metabolism
Zumbaugh, M. D., Johnson, S., Shi, T. H., & Gerrard, D. E. (2022) · Journal of Animal Science · doi:10.1093/jas/skac035 · Cited by 56
Muscle aging and sarcopenia: The pathology, etiology, and most promising therapeutic targets
Grima-Terrén, M., Campanario, S., Ramírez‐Pardo, I., Cisneros, A., Hong, X., Perdiguero, E., Serrano, A. L., Isern, J., & Muñoz‐Cánoves, P. (2024) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2024.101319 · Cited by 52
Targeting TOR dependence in cancer
Janes, M. R., & Fruman, D. A. (2010) · Oncotarget · doi:10.18632/oncotarget.110 · Cited by 46
Chen, Z., Holland, W. L., Shelton, J. M., Ali, A., Zhan, X., Won, S., Tomisato, W., Liu, C., Li, X., Moresco, E. M. Y., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1406511111 · Cited by 46
André, C., & Cota, D. (2012) · Proceedings of The Nutrition Society · doi:10.1017/s0029665112000754 · Cited by 48
p110α of PI3K is necessary and sufficient for quiescence exit in adult muscle satellite cells
Wang, G., Zhu, H., Situ, C., Han, L., Yu, Y., Cheung, T. H., Liu, K., & Wu, Z. (2018) · The EMBO Journal · doi:10.15252/embj.201798239 · Cited by 49
Pancha, I., Shima, H., Higashitani, N., Igarashi, K., Higashitani, A., Tanaka, K., & Imamura, S. (2018) · The Plant Journal · doi:10.1111/tpj.14136 · Cited by 45
Metadata
- Authors
- Bentzinger, C. F., Romanino, K., Cloëtta, D., Lin, S., Mascarenhas, J. B., Oliveri, F., Xia, J., Casanova, E., Costa, C. F., Brink, M., Zorzato, F., Hall, M. N., & Rüegg, M. A.
- Affiliations
- University of Basel (CH)
- University Hospital of Basel (CH)
- Corresponding author
- Rüegg, Markus A.
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2008-11
- Volume
- 8
- Issue
- 5
- Pages
- 411-424
- ISSN
- 1550-4131 (ISSN-L)
- OpenAlex
- W2016815316
- Cited by
- 640
- References
- 51
- Citations by year
- 2026: 14 · 2025: 13 · 2024: 22 · 2023: 27 · 2022: 33 · 2021: 39 · 2020: 26 · 2019: 40 · 2018: 44 · 2017: 43 · 2016: 38 · 2015: 41 · 2014: 53 · 2013: 50 · 2012: 48
- FWCI
- 14.66
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- edoc (University of Basel) (acceptedVersion)
- Institutional Research Information System University of Ferrara (University of Ferrara) (submittedVersion)
- edoc (University of Basel)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- raptors, Rictor, mTORC1, mTORC2, skeletal muscle, muscular dystrophy, muscle metabolism, oxidative capacity, glycogen storage, mitochondrial biogenesis, PGC-1α, Akt signaling
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Mechanistic Target of Rapamycin Complex 1, Regulatory-Associated Protein of mTOR, Rapamycin-Insensitive Companion of mTOR Protein, Animals, Carrier Proteins, Enzyme Activation, Gene Expression Regulation, Mitochondria, Muscular Dystrophies, Phosphorylation, Proteins, Transcription Factors, Trans-Activators, Mice, Knockout, Muscle, Skeletal, Multiprotein Complexes, Adaptor Proteins, Signal Transducing, Proto-Oncogene Proteins c-akt, Oncogene Protein v-akt, Mice, TOR Serine-Threonine Kinases
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