Mechanotransduction and the regulation of mTORC1 signaling in skeletal muscle
Open accessAbstract
Mechanical stimuli play a major role in the regulation of skeletal muscle mass, and the maintenance of muscle mass contributes significantly to disease prevention and issues associated with the quality of life. Although the link between mechanical signals and the regulation of muscle mass has been recognized for decades, the mechanisms involved in converting mechanical information into the molecular events that control this process remain poorly defined. Nevertheless, our knowledge of these mechanisms is advancing and recent studies have revealed that signaling through a protein kinase called the mammalian target of rapamycin (mTOR) plays a central role in this event. In this review we will, (1) discuss the evidence which implicates mTOR in the mechanical regulation of skeletal muscle mass, (2) provide an overview of the mechanisms through which signaling by mTOR can be regulated, and (3) summarize our current knowledge of the potential mechanisms involved in the mechanical activation of mTOR signaling.
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
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?
In aged muscle, cytoskeletal stiffness and nuclear lamina disorganization severely impair physical signal transmission.
“In aged muscle, cytoskeletal stiffness and nuclear lamina disorganization severely impair physical signal transmission [107,108].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [108]
The Introduction (page unavailable) discusses age-related muscle loss and how skeletal muscle converts mechanical tension into biochemical signals. It does not say that cytoskeletal stiffness or nuclear lamina disorganization impairs physical signal transmission in aged muscle; searches for those terms found no supporting passage. (LLM, conf=0.76)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849 · see citing works
The Rag GTPases Bind Raptor and Mediate Amino Acid Signaling to mTORC1
Sancak, Y., Peterson, T. R., Shaul, Y. D., Lindquist, R. A., Thoreen, C. C., Bar-Peled, L., & Sabatini, D. M. (2008) · Science · doi:10.1126/science.1157535 · Cited by 2,773 · see citing works
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 · see citing works
Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464 · see citing works
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 · see citing works
Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
Inoki, K., Li, Y., Xu, T., & Guan, K.-L. (2003) · Genes & Development · doi:10.1101/gad.1110003 · Cited by 1,911 · see citing works
Rommel, 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 · see citing works
Guertin, D. A., Stevens, D. M., Thoreen, C. C., Burds, A. A., Kalaany, N. Y., Moffat, J., Brown, M., Fitzgerald, K. J., & Sabatini, D. M. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.10.007 · Cited by 1,409 · see citing works
Regulation of TORC1 by Rag GTPases in nutrient response
Kim, E., Goraksha-Hicks, P., Li, L., Neufeld, T. P., & Guan, K.-L. (2008) · Nature Cell Biology · doi:10.1038/ncb1753 · Cited by 1,349 · see citing works
The TSC1–TSC2 complex: a molecular switchboard controlling cell growth
Huang, J., & Manning, B. D. (2008) · Biochemical Journal · doi:10.1042/bj20080281 · Cited by 1,237 · cited 2× · see citing works
“Activated PKB can then phosphorylate and inhibit the activity of the tuberous sclerosis complex (TSC1/2) complex which is a GTPase-activating protein for a ras-family GTP-binding protein called Rheb (Huang and Manning, 2008).”
BackgroundMammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E
Fingar, D. C., Salama, S., Tsou, C., Harlow, E., & Blenis, J. (2002) · Genes & Development · doi:10.1101/gad.995802 · Cited by 1,093 · see citing works
Phosphatidic Acid-Mediated Mitogenic Activation of mTOR Signaling
Fang, Y., Vilella-Bach, M., Bachmann, R., Flanigan, A., & Chen, J. (2001) · Science · doi:10.1126/science.1066015 · Cited by 1,055 · see citing works
Molecular mechanisms of translational control
Gebauer, F., & Hentze, M. W. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1488 · Cited by 991 · see citing works
Fingar, D. C., Richardson, C. J., Tee, A. R., Cheatham, L. A., Tsou, C., & Blenis, J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.200-216.2004 · Cited by 865 · see citing works
Lee, R. C., Wang, Z., Heo, M., Ross, R., Janssen, I., & Heymsfield, S. B. (2000) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/72.3.796 · Cited by 854 · see citing works
Signaling in Muscle Atrophy and Hypertrophy
Sandri, M. (2008) · Physiology · doi:10.1152/physiol.00041.2007 · Cited by 830 · see citing works
Signaling functions of phosphatidic acid
WANG, X., DEVAIAH, S., ZHANG, W., & WELTI, R. (2006) · Progress in Lipid Research · doi:10.1016/j.plipres.2006.01.005 · Cited by 757 · see citing works
Nobukuni, T., Joaquin, M., Roccio, M., Dann, S. G., Kim, S. Y., Gulati, P., Byfield, M. P., Backer, J., Natt, F., Bos, J. L., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506925102 · Cited by 753 · see citing works
Pende, M., Um, S. H., Mieulet, V., Sticker, M., Goss, V. L., Mestan, J., Mueller, M., Fumagalli, S., Kozma, S. C., & Thomas, G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.8.3112-3124.2004 · Cited by 743 · see citing works
Baar, K., & Esser, K. (1999) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1999.276.1.c120 · Cited by 726 · see citing works
Control of p70 S6 kinase by kinase activity of FRAP in vivo
Brown, E. J., Beal, P. A., Keith, C. T., Chen, J., Shin, T. B., & Schreiber, S. L. (1995) · Nature · doi:10.1038/377441a0 · Cited by 705 · see citing works
Disruption of the p70s6k/p85s6k gene reveals a small mouse phenotype and a new functional S6 kinase
Shima, H., Pende, M., Chen, Y., Fumagalli, S., THOMAS, G. V., & Kozma, S. C. (1998) · The EMBO Journal · doi:10.1093/emboj/17.22.6649 · Cited by 636 · see citing works
Synthesis of the translational apparatus is regulated at the translational level.
Meyuhas, O. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01719.x · Cited by 570 · see citing works
<i>Physiology of a Microgravity Environment</i> Invited Review: Microgravity and skeletal muscle
Fitts, R. H., Riley, D. R., & Widrick, J. J. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.89.2.823 · Cited by 548 · see citing works
Yang, Q., & Guan, K. (2007) · Cell Research · doi:10.1038/cr.2007.64 · Cited by 540 · see citing works
Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity
Hahn-Windgassen, A., Nogueira, V., Chen, C.-C., Skeen, J. E., Sonenberg, N., & Hay, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502876200 · Cited by 539 · see citing works
Signalling to translation: How signal transduction pathways control the protein synthetic machinery
Proud, C. G. (2007) · Biochemical Journal · doi:10.1042/bj20070024 · Cited by 520 · see citing works
Phospholipase D: a lipid centric review
Jenkins, G. M., & Frohman, M. A. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5195-z · Cited by 510 · see citing works
Murakami, M., & Kudo, I. (2002) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a003101 · Cited by 509 · see citing works
Goodman, C. A., Mabrey, D. M., Frey, J. W., Miu, M. H., Schmidt, E. K., Pierre, P., & Hornberger, T. A. (2010) · The FASEB Journal · doi:10.1096/fj.10-168799 · Cited by 478 · see citing works
Atherton, P. J., Babraj, J. A., Smith, K., Singh, J., Rennie, M. J., & Wackerhage, H. (2005) · The FASEB Journal · doi:10.1096/fj.04-2179fje · Cited by 475 · see citing works
Drummond, M. J., Fry, C. S., Glynn, E. L., Dreyer, H. C., Dhanani, S., Timmerman, K. L., Volpi, E., & Rasmussen, B. B. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.163816 · Cited by 439 · cited 1× · see citing works
“Others have since repeated these observations and also demonstrated that rapamycin prevents the increase in protein synthesis that occurs in response to mechanical stimulation (Hornberger et al., 2004, Hornberger et al., 2003, Drummond et al., 2009, Kubica et al., 2005).”
BackgroundMechanism of work-induced hypertrophy of skeletal muscle
GOLDBERG, A. L., ETLINGER, J. D., GOLDSPINK, D. F., & JABLECKI, C. (1975) · Medicine and Science in Sports and Exercise · doi:10.1249/00005768-197500730-00016 · Cited by 402 · see citing works
Pallafacchina, G., Calabria, E., Serrano, A. L., Kalhovde, J. M., & Schiaffino, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142166599 · Cited by 402 · see citing works
Fast/Glycolytic Muscle Fiber Growth Reduces Fat Mass and Improves Metabolic Parameters in Obese Mice
Izumiya, Y., Hopkins, T., Morris, C., Sato, K., Zeng, L., Viereck, J., Hamilton, J. A., Ouchi, N., LeBrasseur, N. K., & Walsh, K. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.003 · Cited by 395 · see citing works
Ohanna, M., Sobering, A. K., Lapointe, T., Lorenzo, L., Praud, C., Petroulakis, E., Sonenberg, N., Kelly, P. A., Sotiropoulos, A., & Pende, M. (2005) · Nature Cell Biology · doi:10.1038/ncb1231 · Cited by 392 · see citing works
Upstream of the mammalian target of rapamycin: do all roads pass through mTOR?
Corradetti, M. N., & Guan, K.-L. (2006) · Oncogene · doi:10.1038/sj.onc.1209885 · Cited by 387 · see citing works
Rheb Activates mTOR by Antagonizing Its Endogenous Inhibitor, FKBP38
Bai, X., Ma, D., Liu, A., Shen, X., Wang, Q. J., Liu, Y., & Jiang, Y. (2007) · Science · doi:10.1126/science.1147379 · Cited by 382 · see citing works
Kimball, S., Shantz, L., Horetsky, R. L., & Jefferson, L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.17.11647 · Cited by 382 · see citing works
Amino acid regulation of TOR complex 1
Avruch, J., Long, X., Ortiz-Vega, S., Rapley, J., Papageorgiou, A., & Dai, N. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90645.2008 · Cited by 382 · see citing works
Localized infusion of IGF-I results in skeletal muscle hypertrophy in rats
Adams, G. R., & McCue, S. A. (1998) · Journal of Applied Physiology · doi:10.1152/jappl.1998.84.5.1716 · Cited by 377 · see citing works
Amino Acids Activate mTOR Complex 1 via Ca2+/CaM Signaling to hVps34
Gulati, P., Gaspers, L. D., Dann, S. G., Joaquin, M., Nobukuni, T., Natt, F., Kozma, S. C., Thomas, A. P., & Thomas, G. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.03.002 · Cited by 371 · see citing works
The benefits of strength training for older adults
SEGUIN, R. (2003) · American Journal of Preventive Medicine · doi:10.1016/s0749-3797(03)00177-6 · Cited by 354 · see citing works
The influence of immobilization and stretch on protein turnover of rat skeletal muscle.
Goldspink, D. F. (1977) · The Journal of Physiology · doi:10.1113/jphysiol.1977.sp011667 · Cited by 351 · see citing works
Rheb Binding to Mammalian Target of Rapamycin (mTOR) Is Regulated by Amino Acid Sufficiency
Long, X., Ortiz-Vega, S., Lin, Y., & Avruch, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500169200 · Cited by 349 · see citing works
p70s6k function is essential for G1 progression
Lane, H. A., Fernandez, A., Lamb, N. J. C., & Thomas, G. (1993) · Nature · doi:10.1038/363170a0 · Cited by 344 · see citing works
Reiling, J. H., & Sabatini, D. M. (2006) · Oncogene · doi:10.1038/sj.onc.1209889 · Cited by 338 · see citing works
Hornberger, T. A., Chu, W. K., Mak, Y. W., Hsiung, J. W., Huang, S. A., & Chien, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600678103 · Cited by 312 · see citing works
Self-citationThe class III PI(3)K Vps34 promotes autophagy and endocytosis but not TOR signaling in Drosophila
Juhász, G., Hill, J. H., Yan, Y., Sass, M., Baehrecke, E. H., Backer, J., & Neufeld, T. P. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200712051 · Cited by 311 · see citing works
Roles of phosphatidate phosphatase enzymes in lipid metabolism
Carman, G. M., & Han, G. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.10.003 · Cited by 301 · see citing works
Insulin and amino-acid regulation of mTOR signaling and kinase activity through the Rheb GTPase
Avruch, J., Hara, K., Lin, Y., Liu, M., Long, X., Ortiz-Vega, S., & Yonezawa, K. (2006) · Oncogene · doi:10.1038/sj.onc.1209882 · Cited by 297 · see citing works
Diacylglycerol kinases: Why so many of them?
Sakane, F., Imai, S.-I., Kai, M., Yasuda, S., & Kanoh, H. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2007.04.006 · Cited by 296 · see citing works
Kimball, S. R., Farrell, P. A., & Jefferson, L. S. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00221.2002 · Cited by 296 · see citing works
Adams, G. R., & Haddad, F. (1996) · Journal of Applied Physiology · doi:10.1152/jappl.1996.81.6.2509 · Cited by 287 · see citing works
Bruss, M. D., Arias, E. B., Lienhard, G. E., & Cartee, G. D. (2005) · Diabetes · doi:10.2337/diabetes.54.1.41 · Cited by 273 · see citing works
Hornberger, T. A., Stuppard, R., Conley, K. E., Fedele, M. J., Fiorotto, M. L., Chin, E. R., & Esser, K. A. (2004) · Biochemical Journal · doi:10.1042/bj20040274 · Cited by 256 · see citing works
Spangenburg, E. E., Roith, D. L., Ward, C. W., & Bodine, S. C. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.141507 · Cited by 254 · see citing works
Bolster, D. R., Kubica, N., Crozier, S. J., Williamson, D. L., Farrell, P. A., Kimball, S. R., & Jefferson, L. S. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.047019 · Cited by 251 · see citing works
Su, W., Yeku, O., Srinivas, O., Genna, A., Park, J.-S., Ren, H., Du, G., Gelb, M. H., Morris, A. J., & Frohman, M. A. (2008) · Molecular Pharmacology · doi:10.1124/mol.108.053298 · Cited by 251 · see citing works
TOR Mutations Confer Rapamycin Resistance by Preventing Interaction with FKBP12-Rapamycin
Lorenz, M. C., & Heitman, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.46.27531 · Cited by 238 · see citing works
O’Neil, T. K., Duffy, L. R., Frey, J. W., & Hornberger, T. A. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.173609 · Cited by 227 · see citing works
Kodaki, T., & Yamashita, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.11408 · Cited by 225 · see citing works
Role for Phospholipase D in Receptor-Mediated Endocytosis
Shen, Y., Xu, L., & Foster, D. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.2.595-602.2001 · Cited by 222 · see citing works
AMP-activated protein kinase and the regulation of glucose transport
FUJII, N. L., Jessen, N., & Goodyear, L. J. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00207.2006 · Cited by 218 · see citing works
Harris, T. E., Huffman, T. A., Chi, A., Shabanowitz, J., Hunt, D. F., Kumar, A. T., & Lawrence, J. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609537200 · Cited by 211 · see citing works
Kubica, N., Bolster, D. R., Farrell, P. A., Kimball, S. R., & Jefferson, L. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413732200 · Cited by 207 · see citing works
Akt signaling in skeletal muscle: regulation by exercise and passive stretch
Sakamoto, K., Aschenbach, W. G., Hirshman, M. F., & Goodyear, L. J. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00228.2003 · Cited by 206 · see citing works
Protein kinase B/Akt: a nexus of growth factor and cytokine signaling in determining muscle mass
Frost, R. A., & Lang, C. H. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00089.2007 · Cited by 200 · see citing works
Phospholipase D confers rapamycin resistance in human breast cancer cells
Chen, Y., Yang, Z., & Foster, D. A. (2003) · Oncogene · doi:10.1038/sj.onc.1206565 · Cited by 196 · see citing works
Proctor, D. N., Balagopal, P., & Nair, K. S. (1998) · Journal of Nutrition · doi:10.1093/jn/128.2.351s · Cited by 191 · see citing works
Regulation of mTOR by Phosphatidic Acid?
Foster, D. A. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3016 · Cited by 191 · see citing works
Aoki, J., Inoue, A., Makide, K., Saiki, N., & Arai, H. (2006) · Biochimie · doi:10.1016/j.biochi.2006.09.021 · Cited by 187 · see citing works
Molecular determinants of skeletal muscle mass: getting the “AKT” together
Nader, G. A. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.02.026 · Cited by 182 · see citing works
Phospholipase D1 is an effector of Rheb in the mTOR pathway
Sun, Y., Fang, Y., Yoon, M., Zhang, C., Roccio, M., Zwartkruis, F. J. T., Armstrong, M. D., Brown, H. A., & Chen, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712268105 · Cited by 179 · see citing works
Space travel directly induces skeletal muscle atrophy
Vandenburgh, H. H., Chromiak, J. A., Shansky, J., Tatto, M. D., & Lemaire, J. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.9.1031 · Cited by 179 · see citing works
Cloning and Characterization of Two Human Isozymes of Mg2+-independent Phosphatidic Acid Phosphatase
Kai, M., Wada, I., Imai, S.-I., Sakane, F., & Kanoh, H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24572 · Cited by 159 · see citing works
Aging-sensitive cellular and molecular mechanisms associated with skeletal muscle hypertrophy
Haddad, F., & Adams, G. R. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01227.2005 · Cited by 158 · see citing works
Chen, Y., Nader, G. A., Baar, K. R., Fedele, M. J., Hoffman, E. P., & Esser, K. A. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2002.021220 · Cited by 158 · see citing works
Veverka, V., Crabbe, T., Bird, I., Lennie, G., Muskett, F. W., Taylor, R. J., & Carr, M. D. (2007) · Oncogene · doi:10.1038/sj.onc.1210693 · Cited by 154 · see citing works
PROTEIN SYNTHESIS DURING WORK-INDUCED GROWTH OF SKELETAL MUSCLE
Goldberg, A. L. (1968) · The Journal of Cell Biology · doi:10.1083/jcb.36.3.653 · Cited by 152 · see citing works
Ávila‐Flores, A., Santos-Mendoza, T., Rincón, E., & Mérida, I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412296200 · Cited by 151 · see citing works
Signaling roles of diacylglycerol kinases
Topham, M. K. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20704 · Cited by 141 · see citing works
Lü, B., Jiang, Y. J., Zhou, Y., Xu, F. Y., Hatch, G. M., & Choy, P. C. (2005) · Biochemical Journal · doi:10.1042/bj20041348 · Cited by 127 · see citing works
Deshmukh, A. S., Coffey, V. G., Zhong, Z., Chibalin, A., Hawley, J. A., & Zierath, J. R. (2006) · Diabetes · doi:10.2337/db05-1419 · Cited by 126 · see citing works
Regulation of Glycogen Synthesis by Amino Acids in Cultured Human Muscle Cells
Armstrong, J. L., Bonavaud, S. M., Toole, B. J., & Yeaman, S. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m004812200 · Cited by 122 · see citing works
Hornberger, T., & Chien, S. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20671 · Cited by 120 · see citing works
Goodman, C. A., Miu, M. H., Frey, J. W., Mabrey, D. M., Lincoln, H. C., Ge, Y., Chen, J., & Hornberger, T. A. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-05-0454 · Cited by 120 · see citing works
Alternative phospholipase D/mTOR survival signal in human breast cancer cells
Chen, Y., Rodrik-Outmezguine, V. S., & Foster, D. A. (2004) · Oncogene · doi:10.1038/sj.onc.1208099 · Cited by 116 · see citing works
Dynamic phospholipid signaling by G protein-coupled receptors
Weernink, P. A. O., Li, H., Jakobs, K. H., & Schmidt, M. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.09.012 · Cited by 114 · see citing works
Stretch-induced prostaglandins and protein turnover in cultured skeletal muscle
Vandenburgh, H. H., Hatfaludy, S., Sohár, I., & Shansky, J. (1990) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1990.259.2.c232 · Cited by 113 · see citing works
hVps15, but not Ca2+/CaM, is required for the activity and regulation of hVps34 in mammalian cells
Yan, Y., Flinn, R. J., Wu, H., Schnur, R. S., & Backer, J. (2008) · Biochemical Journal · doi:10.1042/bj20081865 · Cited by 113 · see citing works
Interaction between the AMP-Activated Protein Kinase and mTOR Signaling Pathways
Kimball, S. R. (2006) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000233796.16411.13 · Cited by 109 · see citing works
Cleland, P. J. F., Appleby, G. J., Rattigan, S., & Clark, M. G. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84628-8 · Cited by 99 · see citing works
Spangenburg, E. E., & McBride, T. A. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00619.2005 · Cited by 97 · see citing works
Nutrient sensing in the mTOR/S6K1 signalling pathway
Gulati, P., & Thomas, G. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350236 · Cited by 95 · see citing works
mVps34 is activated following high‐resistance contractions
MacKenzie, M. G., Hamilton, D. L., Murray, J. T., Taylor, P. M., & Baar, K. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.159830 · Cited by 94 · see citing works
Identification of a novel human phosphatidic acid phosphatase type 2 isoform
Hooks, S. B., Ragan, S. P., & Lynch, K. R. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00421-9 · Cited by 90 · see citing works
Deletion of cytosolic phospholipase A2 promotes striated muscle growth
Haq, S., Kilter, H., Michael, A., Tao, J., O’Leary, E., Sun, X. M., Walters, B. M., Bhattacharya, K., Chen, X., Cui, L., et al. (2003) · Nature Medicine · doi:10.1038/nm891 · Cited by 89 · see citing works
Research hypotheses on muscle wasting, aging, loss of function and disability.
Pahor, M., & Kritchevsky, S. B. (1998) · PubMed · Cited by 84 · see citing works
Phosphatidic acid mediates activation of mTORC1 through the ERK signaling pathway
Winter, J. N., Fox, T. E., KESTER, M. A., Jefferson, L. S., & Kimball, S. R. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00039.2010 · Cited by 82 · see citing works
Selenoprotein-Deficient Transgenic Mice Exhibit Enhanced Exercise-Induced Muscle Growth
Hornberger, T. A., McLoughlin, T. J., Leszczynski, J. K., Armstrong, D., Esser, K. A., Jameson, R. R., Bowen, P. E., Hwang, E., Hou, H., Moustafa, M. E., et al. (2003) · Journal of Nutrition · doi:10.1093/jn/133.10.3091 · Cited by 80 · see citing works
Motion into mass: how does tension stimulate muscle growth?
Vandenburgh, H. H. (1987) · PubMed · Cited by 80 · see citing works
Chapter 2 Cell Signaling in Protein Synthesis
Mahoney, S. J., Dempsey, J. M., & Blenis, J. (2009) · Progress in molecular biology and translational science · doi:10.1016/s1877-1173(09)90002-3 · Cited by 78 · see citing works
Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase
Nanjundan, M., & Possmayer, F. (2003) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00029.2002 · Cited by 76 · see citing works
Stretch‐induced growth of skeletal myotubes correlates with activation of the sodium pump
Vandenburgh, H. H., & Kaufman, S. (1981) · Journal of Cellular Physiology · doi:10.1002/jcp.1041090203 · Cited by 72 · see citing works
Katayama, K., Kodaki, T., Nagamachi, Y., & Yamashita, S. (1998) · Biochemical Journal · doi:10.1042/bj3290647 · Cited by 70 · see citing works
Hornberger, T. A., Sukhija, K. B., Wang, X.-R., & Chien, S. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.08.045 · Cited by 63 · see citing works
Kim, J., Solis, R. S., Arias, E. B., & Cartee, G. D. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00909.2003 · Cited by 60 · see citing works
Time course of the MAPK and PI3-kinase response within 24 h of skeletal muscle overload
Carlson, C. J., Fan, Z., Gordon, S. E., & Booth, F. W. (2001) · Journal of Applied Physiology · doi:10.1152/jappl.2001.91.5.2079 · Cited by 59 · see citing works
PLD2 forms a functional complex with mTOR/raptor to transduce mitogenic signals
Ha, S. H., Kim, D., Kim, I.-S., Kim, J. H., Lee, M. N., Lee, H. J., Jong Heon, K. I. M., Jang, S. K., Suh, P., & Ryu, S. H. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.05.021 · Cited by 58 · see citing works
The Switch I Region of Rheb Is Critical for Its Interaction with FKBP38
Ma, D., Bai, X., Guo, S., & Jiang, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802356200 · Cited by 56 · see citing works
Coon, M. E., Ball, A. S., Pound, J., Ap, S., Hollenback, D., White, T., Tulinsky, J., Bonham, L., Morrison, D. K., Finney, R. E., et al. (2003) · PubMed · Cited by 54 · see citing works
Tang, W., Yuan, J., Chen, X., Gu, X., Luo, K., Li, J., Wan, B., Wang, Y., & Yu, L. (2006) · BMB Reports · doi:10.5483/bmbrep.2006.39.5.626 · Cited by 53 · see citing works
AMP-activated protein kinase regulation and action in skeletal muscle during exercise
Musi, N., Yu, H., & Goodyear, L. J. (2003) · Biochemical Society Transactions · doi:10.1042/bst0310191 · Cited by 50 · see citing works
RAG GTPases in nutrient-mediated TOR signaling pathway
Kim, E., & Guan, K. (2009) · Cell Cycle · doi:10.4161/cc.8.7.8124 · Cited by 36 · see citing works
Varma, S., & Khandelwal, R. L. (2006) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2006.07.016 · Cited by 35 · see citing works
The Measurement of Phospholipase D-Linked Signaling in Cells
Wakelam, M. J. O., Hodgkin, M. N., & Martin, A. (2003) · Humana Press eBooks · doi:10.1385/0-89603-298-1:271 · Cited by 23 · see citing works
Calcitriol transmembrane signalling: regulation of rat muscle phospholipase D activity
Facchinetti, M. M., Boland, R., & de Boland, A. R. (1998) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)34215-2 · Cited by 18 · see citing works
Takahashi, N., Nagamine, M., Tanno, S., Motomura, W., Kohgo, Y., & Okumura, T. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.040 · Cited by 14 · see citing works
Activation of Akt as a Potential Mediator of Adaptations that Reduce Muscle Injury
Lockhart, N. C., Baar, K., Mazzeo, R. S., & Brooks, S. V. (2006) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000222832.43520.27 · Cited by 6 · see citing works
Flagged first, then by citations
1 of the 121 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Kubica N Bolster DR Farrell PA Kimball SR Jefferson LS Resistance exercise increases muscle protein synthesis and translation of eukaryotic initiation factor 2Bepsilon mRNA in a mammalian target of rapamycin-dependent manner J Biol Chem 2005 280 7570 7580 15591312
Cited by
Sorted by citations
mTOR as a key regulator in maintaining skeletal muscle mass
Yoon, M.-S. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00788 · Cited by 495 · see citing works
Muscle protein synthesis in response to nutrition and exercise
Atherton, P. J., & Smith, K. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2011.225003 · Cited by 401 · see citing works
Leal, L. G., Lopes, M. A., & Batista, M. L. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01307 · Cited by 382 · see citing works
“Skeletal Muscle as an Immunogenic Organ The Concept of Myokines The SkM is a highly organized tissue at the micro and macroscopic level and is the body’s main protein reserve (Hornberger, 2011; Bentzinger et al., 2013).”
BackgroundStimuli and sensors that initiate skeletal muscle hypertrophy following resistance exercise
Wackerhage, H., Schoenfeld, B. J., Hamilton, D. L., Lehti, M., & Hulmi, J. J. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00685.2018 · Cited by 357 · see citing works
Mechanisms Modulating Skeletal Muscle Phenotype
Blaauw, B., Schiaffino, S., & Reggiani, C. (2013) · Comprehensive physiology · doi:10.1002/cphy.c130009 · Cited by 278 · see citing works
Measuring Protein Synthesis With SUnSET: A Valid Alternative to Traditional Techniques?
Goodman, C. A., & Hornberger, T. A. (2013) · Exercise and Sport Sciences Reviews · doi:10.1097/jes.0b013e3182798a95 · Cited by 233 · see citing works
Roberts, M. D., McCarthy, J. J., Hornberger, T. A., Phillips, S. M., Mackey, A. L., Nader, G. A., Boppart, M. D., Kavazis, A. N., Reidy, P. T., Ogasawara, R., et al. (2023) · Physiological Reviews · doi:10.1152/physrev.00039.2022 · Cited by 214 · see citing works
Farup, J., de Paoli, F., Bjerg, K., Riis, S., Ringgard, S., & Vissing, K. (2015) · Scandinavian Journal of Medicine & Science in Sports · doi:10.1111/sms.12396 · Cited by 195 · see citing works
Nunes, E. A., Stokes, T., McKendry, J., Currier, B. S., & Phillips, S. M. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00425.2021 · Cited by 183 · see citing works
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 178 · see citing works
The Hippo pathway effector YAP is a critical regulator of skeletal muscle fibre size
Watt, K. I., Turner, B. J., Hagg, A., Zhang, X., Davey, J. R., Qian, H., Beyer, C., Winbanks, C. E., Harvey, K. F., & Gregorevic, P. (2015) · Nature Communications · doi:10.1038/ncomms7048 · Cited by 164 · see citing works
You, J.-S., Lincoln, H. C., Kim, C.-R., Frey, J. W., Goodman, C. A., Zhong, X.-P., & Hornberger, T. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.531392 · Cited by 163 · see citing works
Bone and skeletal muscle: Key players in mechanotransduction and potential overlapping mechanisms
Goodman, C. A., Hornberger, T. A., & Robling, A. G. (2015) · Bone · doi:10.1016/j.bone.2015.04.014 · Cited by 155 · see citing works
Tang, H., Inoki, K., Lee, M. C., Wright, E., Khuong, A., Khuong, A., Sugiarto, S., Garner, M. S., Paik, J., DePinho, R. A., et al. (2014) · Science Signaling · doi:10.1126/scisignal.2004809 · Cited by 142 · see citing works
Myokines and Resistance Training: A Narrative Review
Zunner, B. E. M., Wachsmuth, N. B., Eckstein, M. L., Scherl, L., Schierbauer, J., Haupt, S., Stumpf, C., Reusch, L., & Moser, O. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073501 · Cited by 139 · see citing works
G protein-coupled receptor 56 regulates mechanical overload-induced muscle hypertrophy
White, J. P., Wrann, C. D., Rao, R. R., Nair, S. K., Jedrychowski, M. P., You, J.-S., Martínez-Redondo, V., Gygi, S. P., Ruas, J. L., Hornberger, T. A., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417898111 · Cited by 123 · see citing works
Self-citationBond, P. (2016) · Journal of the International Society of Sports Nutrition · doi:10.1186/s12970-016-0118-y · Cited by 121 · see citing works
Mammalian Target of Rapamycin (mTOR) Signaling Network in Skeletal Myogenesis
Ge, Y., & Chen, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.406942 · Cited by 119 · see citing works
Characterization and Regulation of Mechanical Loading‐Induced Compensatory Muscle Hypertrophy
Adams, G. R., & Bamman, M. M. (2012) · Comprehensive physiology · doi:10.1002/cphy.c110066 · Cited by 114 · see citing works
Roberts, M. D., Haun, C. T., Mobley, C. B., Mumford, P. W., Romero, M. A., Roberson, P. A., Vann, C. G., & McCarthy, J. J. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00834 · Cited by 107 · see citing works
Molecular Regulation of Exercise-Induced Muscle Fiber HypertrophyPreprint
Bamman, M. M., Roberts, B. M., & Adams, G. R. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a029751 · Cited by 95 · see citing works
The therapeutic potential of IGF-I in skeletal muscle repair
Song, Y., Song, J. L., Delafontaine, P., & Godard, M. P. (2013) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.03.004 · Cited by 98 · see citing works
Androgen-mediated regulation of skeletal muscle protein balance
Rossetti, M. L., Steiner, J. L., & Gordon, B. S. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.02.031 · Cited by 95 · see citing works
Gonzalez, A. M., Hoffman, J. R., Stout, J. R., Fukuda, D. H., & Willoughby, D. S. (2015) · Sports Medicine · doi:10.1007/s40279-015-0450-4 · Cited by 94 · see citing works
You, J. S., Frey, J. W., & Hornberger, T. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047258 · Cited by 88 · see citing works
Mammalian phospholipase D: Function, and therapeutics
McDermott, M. I., Wang, Y., Wakelam, M. J. O., & Bankaitis, V. A. (2019) · Progress in Lipid Research · doi:10.1016/j.plipres.2019.101018 · Cited by 86 · see citing works
Franchi, M. V., Ruoss, S., Valdivieso, P., Mitchell, K. W., Smith, K., Atherton, P. J., Narici, M. V., & Flück, M. (2018) · Acta Physiologica · doi:10.1111/apha.13056 · Cited by 83 · see citing works
Skeletal muscle mass and composition during mammalian hibernation
Cotton, C. J. (2016) · Journal of Experimental Biology · doi:10.1242/jeb.125401 · Cited by 78 · see citing works
Kaczka, P., Michalczyk, M. M., Jastrząb, R., Gawełczyk, M., & Kubicka, K. (2019) · Journal of Human Kinetics · doi:10.2478/hukin-2019-0070 · Cited by 76 · see citing works
Kathage, B., Gehlert, S., Ulbricht, A., Lüdecke, L., Tapia, V., Orfanos, Z., Wenzel, D., Bloch, W., Volkmer, R., Fleischmann, B. K., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.10.007 · Cited by 68 · see citing works
Powers, S. K., & Schrager, M. A. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102374 · Cited by 67 · see citing works
Regulation of mTORC1 by amino acids in mammalian cells: A general picture of recent advances
Zhang, S.-Z., Lin, X.-Y., Hou, Q.-L., Hu, Z.-Y., Wang, Y., & Wang, Z.-H. (2021) · Animal Nutrition · doi:10.1016/j.aninu.2021.05.003 · Cited by 56 · see citing works
A 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 60 · see citing works
ACTN3genotype and modulation of skeletal muscle response to exercise in human subjects
Norman, B., Esbjörnsson, M., Rundqvist, H., Österlund, T., Glenmark, B., & Jansson, E. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00557.2013 · Cited by 55 · see citing works
Regeneration of Skeletal Muscle After Eccentric Injury
Dueweke, J. J., Awan, T. M., & Mendias, C. L. (2016) · Journal of Sport Rehabilitation · doi:10.1123/jsr.2016-0107 · Cited by 55 · see citing works
Resistance Exercise, Aging, Disuse, and Muscle Protein Metabolism
McKendry, J., Stokes, T., Mcleod, J. C., & Phillips, S. M. (2021) · Comprehensive physiology · doi:10.1002/cphy.c200029 · Cited by 71 · see citing works
Gonzalez, A. M., Hoffman, J. R., Townsend, J. R., Jajtner, A. R., Boone, C. H., Beyer, K. S., Baker, K. M., Wells, A. J., Mangine, G. T., Robinson, E. H., et al. (2015) · Physiological Reports · doi:10.14814/phy2.12466 · Cited by 53 · see citing works
The mechanical activation of mTOR signaling: an emerging role for late endosome/lysosomal targeting
Jacobs, B. L., Goodman, C. A., & Hornberger, T. A. (2013) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-013-9367-4 · Cited by 52 · see citing works
A DGKζ-FoxO-ubiquitin proteolytic axis controls fiber size during skeletal muscle remodeling
You, J., Dooley, M. S., Kim, C.-R., Kim, E., Xu, W., Goodman, C. A., & Hornberger, T. A. (2018) · Science Signaling · doi:10.1126/scisignal.aao6847 · Cited by 50 · see citing works
Gordon, B. S., Steiner, J., Williamson, D. L., Lang, C. H., & Kimball, S. (2016) · American Journal of Physiology. Endocrinology and Metabolism · doi:10.1152/ajpendo.00059.2016 · Cited by 44 · see citing works
Rahbek, S. K., Farup, J., Møller, A. B., Vendelbo, M. H., Holm, L., Jessen, N., & Vissing, K. (2014) · Amino Acids · doi:10.1007/s00726-014-1792-1 · Cited by 46 · see citing works
Mechano‐signalling pathways in an experimental intensive critical illness myopathy model
Corpeño, R., Salah, H. A., Gastaldello, S., Martínez-Redondo, V., Ruas, J. L., Fury, W., Bai, Y., Gromada, J., Sartori, R., D, D. C. G., et al. (2016) · The Journal of Physiology · doi:10.1113/jp271973 · Cited by 43 · see citing works
Lee, F.-Y., Zhen, Y., Yuen, C.-M., Fan, R., Chen, Y.-T., Sheu, J., Chen, Y., Wang, C., Sun, C., & Yip, H. (2017) · PubMed Central · Cited by 42 · see citing works
Effects of Various Muscle Disuse States and Countermeasures on Muscle Molecular Signaling
Sharlo, K. A., Tyganov, S. A., Tomilovskaya, E., Викторович, П. Д., Saveko, A. A., & Shenkman, B. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010468 · Cited by 45 · see citing works
Mechanisms Modulating Skeletal Muscle Phenotype
Blaauw, B., Schiaffino, S., & Reggiani, C. (2013) · Comprehensive physiology · doi:10.1002/j.2040-4603.2013.tb00534.x · Cited by 38 · see citing works
Kirby, T. J. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01031.2018 · Cited by 37 · see citing works
Phospholipase D regulates the size of skeletal muscle cells through the activation of mTOR signaling
Jaafar, R., Larichaudy, J. D., Chanon, S., Euthine, V., Durand, C., Naro, F., Bertolino, P., Vidal, H., Lefai, É., & Némoz, G. (2013) · Cell Communication and Signaling · doi:10.1186/1478-811x-11-55 · Cited by 37 · see citing works
Solsona, R., Pavlin, L., Bernardi, H., & Sanchez, A. M. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052741 · Cited by 39 · see citing works
mTOR Signaling Components in Tumor Mechanobiology
Gargalionis, A. N., Papavassiliou, K. A., Basdra, E. K., & Papavassiliou, A. G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031825 · Cited by 36 · see citing works
Mechanical Signaling in the Pathophysiology of Critical Illness Myopathy
Corpeño, R., & Larsson, L. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00023 · Cited by 36 · see citing works
Sugg, K. B., Korn, M. A., Sarver, D. C., Markworth, J. F., & Mendias, C. L. (2017) · FEBS Letters · doi:10.1002/1873-3468.12571 · Cited by 35 · see citing works
Millward, D. J. (2021) · Nutrients · doi:10.3390/nu13030729 · Cited by 42 · see citing works
Hibernation: The search for treatments to prevent disuse-induced skeletal muscle atrophy
Bodine, S. C. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.06.003 · Cited by 34 · see citing works
Jacobs, B. L., McNally, R. M., Kim, K., Blanco, R., Privett, R. E., You, J., & Hornberger, T. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.777805 · Cited by 34 · see citing works
The metabolic and temporal basis of muscle hypertrophy in response to resistance exercise
Brook, M. S., Wilkinson, D. J., Smith, K., & Atherton, P. J. (2015) · European Journal of Sport Science · doi:10.1080/17461391.2015.1073362 · Cited by 32 · see citing works
Mechanotransduction pathways in skeletal muscle hypertrophy
Yamada, A. K., Verlengia, R., & Bueno Junior, C. R. (2012) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2011.641978 · Cited by 31 · see citing works
The mechanistic and ergogenic effects of phosphatidic acid in skeletal muscle.
Shad, B. J., Smeuninx, B., Atherton, P., & Breen, L. (2015) · Applied physiology, nutrition, and metabolism = Physiologie appliquee, nutrition et metabolisme · doi:10.1139/apnm-2015-0350 · Cited by 23 · see citing works
Mechanical Regulation of Protein Translation in the Cardiovascular System
Simpson, L. J., Reader, J. S., & Tzima, E. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00034 · Cited by 31 · see citing works
New roles for Smad signaling and phosphatidic acid in the regulation of skeletal muscle mass
Goodman, C. A., & Hornberger, T. A. (2014) · F1000Prime Reports · doi:10.12703/p6-20 · Cited by 30 · see citing works
Self-citationFirearms-related skeletal muscle trauma: pathophysiology and novel approaches for regeneration
Moriscot, A. S., Miyabara, E. H., Langeani, B., Belli, A., Egginton, S., & Bowen, T. S. (2021) · npj Regenerative Medicine · doi:10.1038/s41536-021-00127-1 · Cited by 30 · see citing works
Metabo-reciprocity in cell mechanics: feeling the demands/feeding the demand
Torrino, S., & Bertero, T. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.01.013 · Cited by 29 · see citing works
Mechanotransduction for therapeutic approaches: Cellular aging and rejuvenation
Han, H.-M., Kim, S.-Y., & Kim, D. (2025) · APL Bioengineering · doi:10.1063/5.0263236 · Cited by 29 · see citing works
Obi, S., Nakajima, T., Hasegawa, T., Nakamura, F., Sakuma, M., Toyoda, S., Tei, C., & Inoue, T. (2018) · FEBS Open Bio · doi:10.1002/2211-5463.12550 · Cited by 29 · see citing works
Melnik, B. C., & Schmitz, G. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101270 · Cited by 29 · see citing works
Resistance Exercise, Aging, Disuse, and Muscle Protein Metabolism
McKendry, J., Stokes, T., Mcleod, J. C., & Phillips, S. M. (2021) · Comprehensive physiology · doi:10.1002/j.2040-4603.2021.tb00179.x · Cited by 28 · see citing works
Impaired Adaptive Response to Mechanical Overloading in Dystrophic Skeletal Muscle
Joanne, P., Hourdé, C., Ochala, J., Caudéran, Y., Medja, F., Vignaud, A., Mouisel, É., Hadj‐Saïd, W., Arandel, L., Garcı́a, L., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035346 · Cited by 28 · see citing works
Mirzoev, T. M., & Shenkman, E. A. (2018) · Biochemistry (Moscow) · doi:10.1134/s0006297918110020 · Cited by 28 · see citing works
Zeng, Z., Jing, D., Zhang, X., Duan, Y., & XUE, F. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2304 · Cited by 26 · see citing works
Tyganov, S. A., Mochalova, E. P., Belova, S. P., Sharlo, K. A., Rozhkov, S. V., Kalashnikov, V. E., Turtikova, O. V., Mirzoev, T. M., & Shenkman, B. S. (2021) · Scientific Reports · doi:10.1038/s41598-021-89362-6 · Cited by 26 · see citing works
Alcohol, Resistance Exercise, and mTOR Pathway Signaling: An Evidence-Based Narrative Review
Levitt, D., Luk, H.-Y., & Vingren, J. (2022) · Biomolecules · doi:10.3390/biom13010002 · Cited by 24 · see citing works
D’Lugos, A. C., Patel, S. H., Ormsby, J. C., Curtis, D., Fry, C. S., Carroll, C. C., & Dickinson, J. M. (2018) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00922.2017 · Cited by 26 · see citing works
Physicochemical Niche Conditions and Mechanosensing by Osteocytes and Myocytes
Jin, J., Bakker, A. D., Wu, G., Klein‐Nulend, J., & Jaspers, R. T. (2019) · Current Osteoporosis Reports · doi:10.1007/s11914-019-00522-0 · Cited by 26 · see citing works
Resistance exercise and skeletal muscle: protein synthesis, degradation, and controversies
Ji, F., Lee, H. S., & Kim, J.-H. (2025) · European Journal of Applied Physiology · doi:10.1007/s00421-025-05832-z · Cited by 26 · see citing works
Møller, A. B., Vendelbo, M. H., Rahbek, S. K., Clasen, B. F., Schjerling, P., Vissing, K., & Jessen, N. (2013) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-013-1318-9 · Cited by 25 · see citing works
Nakanishi, R., Hirayama, Y., Tanaka, M., Maeshige, N., Kondo, H., Ishihara, A., Roy, R. R., & Fujino, H. (2016) · Nutrition Research · doi:10.1016/j.nutres.2016.10.007 · Cited by 24 · see citing works
Miao, Y., Yang, J., Xu, Z., Lü, J., Zhao, S., & Li, X. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16047976 · Cited by 23 · see citing works
Bird, S. P., Nienhuis, M. B., Biagioli, B., Pauw, K. D., & MEEUSEN, R. R. (2024) · Nutrients · doi:10.3390/nu16121886 · Cited by 23 · see citing works
Sumi, K., Ashida, K., & Nakazato, K. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00585.2019 · Cited by 22 · see citing works
Roth, C., Schoenfeld, B. J., & Behringer, M. (2022) · European Journal of Applied Physiology · doi:10.1007/s00421-022-04896-5 · Cited by 19 · see citing works
Melnik, B. C., Schmitz, G., John, S. M., Carrera‐Bastos, P., Lindeberg, S., & Cordain, L. (2013) · Nutrition & Metabolism · doi:10.1186/1743-7075-10-60 · Cited by 19 · see citing works
Stretch-activated signaling is modulated by stretch magnitude and contraction
Dyke, J. M. V., Bain, J. L. W., & Riley, D. A. (2013) · Muscle & Nerve · doi:10.1002/mus.23880 · Cited by 17 · see citing works
Lee, S., Kim, M., Kim, C., & Hwang, J. (2017) · Food Science and Biotechnology · doi:10.1007/s10068-017-0277-x · Cited by 17 · see citing works
Godwin, J. S., Sexton, C. L., Kontos, N. J., Ruple, B. A., Willoughby, D. S., Young, K. C., Mobley, C. B., & Roberts, M. D. (2023) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00596.2022 · Cited by 14 · see citing works
Mirzoev, T. M., Tyganov, S. A., & Shenkman, B. S. (2016) · Muscle & Nerve · doi:10.1002/mus.25235 · Cited by 16 · see citing works
Anabolic and Catabolic Signaling Pathways That Regulate Skeletal Muscle Mass
McCarthy, J. J., & Murach, K. A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813922-6.00024-2 · Cited by 16 · see citing works
Guadalupe‐Grau, A., Carnicero, J. A. C., Losa‐Reyna, J., Tresguerres, J., Gómez‐Cabrera, M. C., Castillo, C., Alfaro‐Acha, A., Rosado-Artalejo, C., Rodríguez‐Mañas, L., & García‐García, F. J. (2016) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2016.09.005 · Cited by 15 · see citing works
Diacylglycerol kinase η regulates C2C12 myoblast proliferation through the mTOR signaling pathway
Sakai, H., Murakami, C., Usuki, T., Lü, Q., Matsumoto, K., Urano, T., & Sakane, F. (2020) · Biochimie · doi:10.1016/j.biochi.2020.07.018 · Cited by 15 · see citing works
Schilder, R. J., Kimball, S. R., & Jefferson, L. S. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00400.2011 · Cited by 15 · see citing works
Su, C., Zhang, Z., Liang, B., Zhou, S., & Long, X. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1603568 · Cited by 15 · see citing works
Post-natal muscle growth and protein turnover: a narrative review of current understanding
Millward, D. J. (2023) · Nutrition Research Reviews · doi:10.1017/s0954422423000124 · Cited by 14 · see citing works
The Plateau in Muscle Growth with Resistance Training: An Exploration of Possible Mechanisms
Kataoka, R., Hammert, W. B., Yamada, Y., Song, J. S., Seffrin, A., Kang, A., Spitz, R. W., Wong, V. H. Y., & Loenneke, J. P. (2023) · Sports Medicine · doi:10.1007/s40279-023-01932-y · Cited by 16 · see citing works
Rindom, E., Herskind, J., Blaauw, B., Overgaard, K., Vissing, K., & de Paoli, F. V. (2020) · Acta Physiologica · doi:10.1111/apha.13540 · Cited by 13 · see citing works
Kinetic modeling of leucine-mediated signaling and protein metabolism in human skeletal muscle
McColl, T. J., & Clarke, D. C. (2023) · iScience · doi:10.1016/j.isci.2023.108634 · Cited by 11 · see citing works
Multimodal interventions for cachexia management
Reid, J., Blair, C., Dempster, M., McKeaveney, C., Slee, A., & Fitzsimons, D. (2025) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd015749.pub2 · Cited by 14 · see citing works
Characterization and Regulation of Mechanical Loading‐Induced Compensatory Muscle Hypertrophy
Adams, G. R., & Bamman, M. M. (2012) · Comprehensive physiology · doi:10.1002/j.2040-4603.2012.tb00474.x · Cited by 12 · see citing works
IMPROVING MUSCLE STRENGTH AND SIZE: THE IMPORTANCE OF TRAINING VOLUME, INTENSITY, AND STATUS
Mangine, G. T., Hoffman, J. R., Fukuda, D. H., Stout, J. R., & Ratamess, N. A. (2015) · Hrčak Portal of scientific journals of Croatia (University Computing Centre) · Cited by 12 · see citing works
Smeuninx, B., Nishimura, Y., McKendry, J., Limb, M. C., Smith, K., Atherton, P. J., & Breen, L. (2018) · Clinical Nutrition · doi:10.1016/j.clnu.2018.06.963 · Cited by 12 · see citing works
Ishii, N., Ogasawara, R., Kobayashi, K., & Nakazato, K. (2012) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.1.83 · Cited by 12 · see citing works
Mechanical Loading Modulates AMPK and mTOR Signaling in Muscle Cells
Zhou, X. J., Zhu, S., Li, J., Mateus, A., Williams, C., Gilthorpe, J. D., & Backman, L. J. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c00242 · Cited by 11 · see citing works
Control of Skeletal Muscle Cell Growth and Size Through Adhesion GPCRs
White, J. P. (2016) · Handbook of experimental pharmacology · doi:10.1007/978-3-319-41523-9_13 · Cited by 11 · see citing works
- Authors
- Hornberger, T. A.
- Affiliations
- University of Wisconsin System (US)
- Corresponding author
- Hornberger, Troy A.
- ORCID
- Hornberger, Troy A.
- Venue
- The International Journal of Biochemistry & Cell Biology
- Publisher
- Elsevier BV
- Published
- 2011-09
- Volume
- 43
- Issue
- 9
- Pages
- 1267-1276
- ISSN
- 1357-2725 (ISSN-L)
- PMC
- PMC3146557
- OpenAlex
- W2149598146
- Cited by
- 170
- References
- 121
- Citations by year
- 2026: 10 · 2025: 10 · 2024: 3 · 2023: 8 · 2022: 14 · 2021: 14 · 2020: 7 · 2019: 8 · 2018: 15 · 2017: 9 · 2016: 16 · 2015: 16 · 2014: 9 · 2013: 16 · 2012: 13
- FWCI
- 1.16
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The International Journal of Biochemistry & Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (AR057347)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- mechanotransduction, mTORC1 signaling, skeletal muscle mass, mechanical loading, muscle hypertrophy, muscle atrophy
- MeSH terms
- Mechanistic Target of Rapamycin Complex 1, Amino Acids, Animals, Humans, Muscle Spindles, Organ Size, Phosphatidic Acids, Phospholipase D, Protein Binding, Proteins, Signal Transduction, Gene Expression, Muscle, Skeletal, Phosphatidylinositol 3-Kinases, Mechanotransduction, Cellular, Multiprotein Complexes, 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