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Volumn 6, Issue , 2016, Pages

The role of mTOR signalling in the regulation of skeletal muscle mass in a rodent model of resistance exercise

Author keywords

[No Author keywords available]

Indexed keywords

MTOR PROTEIN, RAT; MUSCLE PROTEIN; TARGET OF RAPAMYCIN KINASE;

EID: 84981187622     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep31142     Document Type: Article
Times cited : (132)

References (57)
  • 1
    • 84859778293 scopus 로고    scopus 로고
    • MTOR signaling in growth control and disease
    • Laplante, M. & Sabatini, D. M. mTOR signaling in growth control and disease. Cell 149, 274-293 (2012).
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 2
    • 78649348967 scopus 로고    scopus 로고
    • Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress
    • Sengupta, S., Peterson, T. R. & Sabatini, D. M. Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress. Mol Cell 40, 310-322 (2010).
    • (2010) Mol Cell , vol.40 , pp. 310-322
    • Sengupta, S.1    Peterson, T.R.2    Sabatini, D.M.3
  • 3
    • 80155142474 scopus 로고    scopus 로고
    • Rapamycin passes the torch: A new generation of mTOR inhibitors
    • Benjamin, D., Colombi, M., Moroni, C. & Hall, M. N. Rapamycin passes the torch: A new generation of mTOR inhibitors. Nat Rev Drug Discov 10, 868-880 (2011).
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 868-880
    • Benjamin, D.1    Colombi, M.2    Moroni, C.3    Hall, M.N.4
  • 4
    • 84880709668 scopus 로고    scopus 로고
    • MTORC1 phosphorylation sites encode their sensitivity to starvation and rapamycin
    • Kang, S. A. et al. mTORC1 phosphorylation sites encode their sensitivity to starvation and rapamycin. Science 341, 1236566 (2013).
    • (2013) Science , vol.341 , pp. 1236566
    • Kang, S.A.1
  • 5
    • 78651284554 scopus 로고    scopus 로고
    • The complexes of mammalian target of rapamycin
    • Zhou, H. & Huang, S. The complexes of mammalian target of rapamycin. Curr Protein Pept Sci 11, 409-424 (2010).
    • (2010) Curr Protein Pept Sci , vol.11 , pp. 409-424
    • Zhou, H.1    Huang, S.2
  • 6
    • 84908610762 scopus 로고    scopus 로고
    • Reassessment of the role of TSC, mTORC1 and microRNAs in amino acids-meditated translational control of TOP mRNAs
    • Patursky-Polischuk, I. et al. Reassessment of the role of TSC, mTORC1 and microRNAs in amino acids-meditated translational control of TOP mRNAs. PLoS One 9, e109410 (2014).
    • (2014) PLoS One , vol.9 , pp. e109410
    • Patursky-Polischuk, I.1
  • 7
    • 81255169943 scopus 로고    scopus 로고
    • The role of skeletal muscle mTOR in the regulation of mechanical load-induced growth
    • Goodman, C. A. et al. The role of skeletal muscle mTOR in the regulation of mechanical load-induced growth. J Physiol 589, 5485-5501 (2011).
    • (2011) J Physiol , vol.589 , pp. 5485-5501
    • Goodman, C.A.1
  • 8
    • 0035736260 scopus 로고    scopus 로고
    • Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
    • Bodine, S. C. et al. Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat Cell Biol 3, 1014-1019 (2001).
    • (2001) Nat Cell Biol , vol.3 , pp. 1014-1019
    • Bodine, S.C.1
  • 10
    • 48549107440 scopus 로고    scopus 로고
    • Differential effects of resistance and endurance exercise in the fed state on signalling molecule phosphorylation and protein synthesis in human muscle
    • Wilkinson, S. B. et al. Differential effects of resistance and endurance exercise in the fed state on signalling molecule phosphorylation and protein synthesis in human muscle. J Physiol 586, 3701-3717 (2008).
    • (2008) J Physiol , vol.586 , pp. 3701-3717
    • Wilkinson, S.B.1
  • 11
    • 33749351995 scopus 로고    scopus 로고
    • Resistance exercise increases AMPK activity and reduces 4E-BP1 phosphorylation and protein synthesis in human skeletal muscle
    • Dreyer, H. C. et al. Resistance exercise increases AMPK activity and reduces 4E-BP1 phosphorylation and protein synthesis in human skeletal muscle. J Physiol 576, 613-624 (2006).
    • (2006) J Physiol , vol.576 , pp. 613-624
    • Dreyer, H.C.1
  • 13
    • 84956748341 scopus 로고    scopus 로고
    • Acute resistance exercise activates rapamycin-sensitive and-insensitive mechanisms that control translational activity and capacity in skeletal muscle
    • West, D. W. et al. Acute resistance exercise activates rapamycin-sensitive and-insensitive mechanisms that control translational activity and capacity in skeletal muscle. J Physiol 594, 453-468 (2016).
    • (2016) J Physiol , vol.594 , pp. 453-468
    • West, D.W.1
  • 14
    • 36749081539 scopus 로고    scopus 로고
    • MTOR controls mitochondrial oxidative function through a YY1-PGC-1alpha transcriptional complex
    • Cunningham, J. T. et al. mTOR controls mitochondrial oxidative function through a YY1-PGC-1alpha transcriptional complex. Nature 450, 736-740 (2007).
    • (2007) Nature , vol.450 , pp. 736-740
    • Cunningham, J.T.1
  • 15
    • 18144386162 scopus 로고    scopus 로고
    • Selective activation of AMPK-PGC-1alpha or PKB-TSC2-mTOR signaling can explain specific adaptive responses to endurance or resistance training-like electrical muscle stimulation
    • Atherton, P. J. et al. Selective activation of AMPK-PGC-1alpha or PKB-TSC2-mTOR signaling can explain specific adaptive responses to endurance or resistance training-like electrical muscle stimulation. FASEB J 19, 786-788 (2005).
    • (2005) FASEB J , vol.19 , pp. 786-788
    • Atherton, P.J.1
  • 17
    • 84873699980 scopus 로고    scopus 로고
    • Co-ingestion of carbohydrate and whey protein isolates enhance PGC-1alpha mRNA expression: A randomised, single blind, cross over study
    • Hill, K. M., Stathis, C. G., Grinfeld, E., Hayes, A. & McAinch, A. J. Co-ingestion of carbohydrate and whey protein isolates enhance PGC-1alpha mRNA expression: A randomised, single blind, cross over study. J Int Soc Sports Nutr 10, 8 (2013).
    • (2013) J Int Soc Sports Nutr , vol.10 , pp. 8
    • Hill, K.M.1    Stathis, C.G.2    Grinfeld, E.3    Hayes, A.4    McAinch, A.J.5
  • 18
    • 81355132716 scopus 로고    scopus 로고
    • Resistance exercise enhances the molecular signaling of mitochondrial biogenesis induced by endurance exercise in human skeletal muscle
    • Wang, L., Mascher, H., Psilander, N., Blomstrand, E. & Sahlin, K. Resistance exercise enhances the molecular signaling of mitochondrial biogenesis induced by endurance exercise in human skeletal muscle. J Appl Physiol (1985) 111, 1335-1344 (2011).
    • (2011) J Appl Physiol (1985) , vol.111 , pp. 1335-1344
    • Wang, L.1    Mascher, H.2    Psilander, N.3    Blomstrand, E.4    Sahlin, K.5
  • 19
    • 0035735902 scopus 로고    scopus 로고
    • Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways
    • Rommel, C. et al. Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways. Nat Cell Biol 3, 1009-1013 (2001).
    • (2001) Nat Cell Biol , vol.3 , pp. 1009-1013
    • Rommel, C.1
  • 20
    • 20144365870 scopus 로고    scopus 로고
    • Initiation factor modifications in the preapoptotic phase
    • Morley, S. J., Coldwell, M. J. & Clemens, M. J. Initiation factor modifications in the preapoptotic phase. Cell Death Differ 12, 571-584 (2005).
    • (2005) Cell Death Differ , vol.12 , pp. 571-584
    • Morley, S.J.1    Coldwell, M.J.2    Clemens, M.J.3
  • 21
    • 0348111466 scopus 로고    scopus 로고
    • Ser-64 and Ser-111 in PHAS-I are dispensable for insulin-stimulated dissociation from eIF4E
    • Ferguson, G., Mothe-Satney, I. & Lawrence, J. C., Jr. Ser-64 and Ser-111 in PHAS-I are dispensable for insulin-stimulated dissociation from eIF4E. J Biol Chem 278, 47459-47465 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 47459-47465
    • Ferguson, G.1    Mothe-Satney, I.2    Lawrence, J.C.3
  • 22
    • 0034057277 scopus 로고    scopus 로고
    • Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression
    • Mothe-Satney, I., Yang, D., Fadden, P., Haystead, T. A. & Lawrence, J. C., Jr. Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression. Mol Cell Biol 20, 3558-3567 (2000).
    • (2000) Mol Cell Biol , vol.20 , pp. 3558-3567
    • Mothe-Satney, I.1    Yang, D.2    Fadden, P.3    Haystead, T.A.4    Lawrence, J.C.5
  • 23
    • 79953152152 scopus 로고    scopus 로고
    • Early activation of mTORC1 signalling in response to mechanical overload is independent of phosphoinositide 3-kinase/Akt signalling
    • Miyazaki, M., McCarthy, J. J., Fedele, M. J. & Esser, K. A. Early activation of mTORC1 signalling in response to mechanical overload is independent of phosphoinositide 3-kinase/Akt signalling. J Physiol 589, 1831-1846 (2011).
    • (2011) J Physiol , vol.589 , pp. 1831-1846
    • Miyazaki, M.1    McCarthy, J.J.2    Fedele, M.J.3    Esser, K.A.4
  • 24
    • 84867525052 scopus 로고    scopus 로고
    • Mechanical stimulation induces mTOR signaling via an ERK-independent mechanism: Implications for a direct activation of mTOR by phosphatidic acid
    • You, J. S., Frey, J. W. & Hornberger, T. A. Mechanical stimulation induces mTOR signaling via an ERK-independent mechanism: implications for a direct activation of mTOR by phosphatidic acid. PLoS One 7, e47258 (2012).
    • (2012) PLoS One , vol.7 , pp. e47258
    • You, J.S.1    Frey, J.W.2    Hornberger, T.A.3
  • 25
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim, J., Kundu, M., Viollet, B. & Guan, K. L. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat Cell Biol 13, 132-141 (2011).
    • (2011) Nat Cell Biol , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 26
    • 84881483132 scopus 로고    scopus 로고
    • Chronic rapamycin treatment or lack of S6K1 does not reduce ribosome activity in vivo
    • Garelick, M. G. et al. Chronic rapamycin treatment or lack of S6K1 does not reduce ribosome activity in vivo. Cell Cycle 12, 2493-2504 (2013).
    • (2013) Cell Cycle , vol.12 , pp. 2493-2504
    • Garelick, M.G.1
  • 27
    • 84859117806 scopus 로고    scopus 로고
    • Rapamycin-induced insulin resistance is mediated by mTORC2 loss and uncoupled from longevity
    • Lamming, D. W. et al. Rapamycin-induced insulin resistance is mediated by mTORC2 loss and uncoupled from longevity. Science 335, 1638-1643 (2012).
    • (2012) Science , vol.335 , pp. 1638-1643
    • Lamming, D.W.1
  • 28
    • 33646023695 scopus 로고    scopus 로고
    • Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB
    • Sarbassov, D. D. et al. Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB. Mol Cell 22, 159-168 (2006).
    • (2006) Mol Cell , vol.22 , pp. 159-168
    • Sarbassov, D.D.1
  • 29
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya, Y. et al. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 19, 5720-5728 (2000).
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1
  • 30
    • 84946945269 scopus 로고    scopus 로고
    • PGC-1alpha overexpression by in vivo transfection attenuates mitochondrial deterioration of skeletal muscle caused by immobilization
    • Kang, C., Goodman, C. A., Hornberger, T. A. & Ji, L. L. PGC-1alpha overexpression by in vivo transfection attenuates mitochondrial deterioration of skeletal muscle caused by immobilization. FASEB J 29, 4092-4106 (2015).
    • (2015) FASEB J , vol.29 , pp. 4092-4106
    • Kang, C.1    Goodman, C.A.2    Hornberger, T.A.3    Ji, L.L.4
  • 31
    • 33750825245 scopus 로고    scopus 로고
    • PGC-1alpha protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription
    • Sandri, M. et al. PGC-1alpha protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription. Proc Natl Acad Sci USA 103, 16260-16265 (2006).
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16260-16265
    • Sandri, M.1
  • 32
    • 84904865507 scopus 로고    scopus 로고
    • Ribosome biogenesis: Emerging evidence for a central role in the regulation of skeletal muscle mass
    • Chaillou, T., Kirby, T. J. & McCarthy, J. J. Ribosome biogenesis: emerging evidence for a central role in the regulation of skeletal muscle mass. J Cell Physiol 229, 1584-1594 (2014).
    • (2014) J Cell Physiol , vol.229 , pp. 1584-1594
    • Chaillou, T.1    Kirby, T.J.2    McCarthy, J.J.3
  • 33
    • 84863045210 scopus 로고    scopus 로고
    • Roles of the mammalian target of rapamycin, mTOR, in controlling ribosome biogenesis and protein synthesis
    • Iadevaia, V., Huo, Y., Zhang, Z., Foster, L. J. & Proud, C. G. Roles of the mammalian target of rapamycin, mTOR, in controlling ribosome biogenesis and protein synthesis. Biochem Soc Trans 40, 168-172 (2012).
    • (2012) Biochem Soc Trans , vol.40 , pp. 168-172
    • Iadevaia, V.1    Huo, Y.2    Zhang, Z.3    Foster, L.J.4    Proud, C.G.5
  • 34
    • 0242637318 scopus 로고    scopus 로고
    • MTOR-dependent regulation of ribosomal gene transcription requires S6K1 and is mediated by phosphorylation of the carboxy-Terminal activation domain of the nucleolar transcription factor UBF
    • Hannan, K. M. et al. mTOR-dependent regulation of ribosomal gene transcription requires S6K1 and is mediated by phosphorylation of the carboxy-Terminal activation domain of the nucleolar transcription factor UBF. Mol Cell Biol 23, 8862-8877 (2003).
    • (2003) Mol Cell Biol , vol.23 , pp. 8862-8877
    • Hannan, K.M.1
  • 35
    • 66149116366 scopus 로고    scopus 로고
    • Expression of growth-related genes in young and older human skeletal muscle following an acute stimulation of protein synthesis
    • Drummond, M. J. et al. Expression of growth-related genes in young and older human skeletal muscle following an acute stimulation of protein synthesis. J Appl Physiol (1985) 106, 1403-1411 (2009).
    • (2009) J Appl Physiol (1985) , vol.106 , pp. 1403-1411
    • Drummond, M.J.1
  • 36
    • 85004010215 scopus 로고    scopus 로고
    • Impact of resistance exercise on ribosome biogenesis is acutely regulated by post-exercise recovery strategies
    • Figueiredo, V. C. et al. Impact of resistance exercise on ribosome biogenesis is acutely regulated by post-exercise recovery strategies. Physiol Rep 4, e12670 (2016).
    • (2016) Physiol Rep , vol.4 , pp. e12670
    • Figueiredo, V.C.1
  • 37
    • 37449029143 scopus 로고    scopus 로고
    • Nutritional control of protein biosynthetic capacity by insulin via Myc in Drosophila
    • Teleman, A. A., Hietakangas, V., Sayadian, A. C. & Cohen, S. M. Nutritional control of protein biosynthetic capacity by insulin via Myc in Drosophila. Cell Metab 7, 21-32 (2008).
    • (2008) Cell Metab , vol.7 , pp. 21-32
    • Teleman, A.A.1    Hietakangas, V.2    Sayadian, A.C.3    Cohen, S.M.4
  • 38
    • 0030822785 scopus 로고    scopus 로고
    • Mixed muscle protein synthesis and breakdown after resistance exercise in humans
    • Phillips, S. M., Tipton, K. D., Aarsland, A., Wolf, S. E. & Wolfe, R. R. Mixed muscle protein synthesis and breakdown after resistance exercise in humans. Am J Physiol 273, E99-107 (1997).
    • (1997) Am J Physiol , vol.273 , pp. E99-107
    • Phillips, S.M.1    Tipton, K.D.2    Aarsland, A.3    Wolf, S.E.4    Wolfe, R.R.5
  • 39
    • 79960285539 scopus 로고    scopus 로고
    • Aging impairs contraction-induced human skeletal muscle mTORC1 signaling and protein synthesis
    • Fry, C. S. et al. Aging impairs contraction-induced human skeletal muscle mTORC1 signaling and protein synthesis. Skelet Muscle 1, 11 (2011).
    • (2011) Skelet Muscle , vol.1 , pp. 11
    • Fry, C.S.1
  • 40
    • 84948798847 scopus 로고    scopus 로고
    • Skeletal muscle hypertrophy adaptations predominate in the early stages of resistance exercise training, matching deuterium oxide-derived measures of muscle protein synthesis and mechanistic target of rapamycin complex 1 signaling
    • Brook, M. S. et al. Skeletal muscle hypertrophy adaptations predominate in the early stages of resistance exercise training, matching deuterium oxide-derived measures of muscle protein synthesis and mechanistic target of rapamycin complex 1 signaling. FASEB J 29, 4485-4496 (2015).
    • (2015) FASEB J , vol.29 , pp. 4485-4496
    • Brook, M.S.1
  • 41
    • 84873378527 scopus 로고    scopus 로고
    • Exercise metabolism and the molecular regulation of skeletal muscle adaptation
    • Egan, B. & Zierath, J. R. Exercise metabolism and the molecular regulation of skeletal muscle adaptation. Cell Metab 17, 162-184 (2013).
    • (2013) Cell Metab , vol.17 , pp. 162-184
    • Egan, B.1    Zierath, J.R.2
  • 42
    • 63849130621 scopus 로고    scopus 로고
    • Rapamycin administration in humans blocks the contraction-induced increase in skeletal muscle protein synthesis
    • Drummond, M. J. et al. Rapamycin administration in humans blocks the contraction-induced increase in skeletal muscle protein synthesis. J Physiol 587, 1535-1546 (2009).
    • (2009) J Physiol , vol.587 , pp. 1535-1546
    • Drummond, M.J.1
  • 43
    • 14844302667 scopus 로고    scopus 로고
    • Resistance exercise increases muscle protein synthesis and translation of eukaryotic initiation factor 2Bepsilon mRNA in a mammalian target of rapamycin-dependent manner
    • Kubica, N., Bolster, D. R., Farrell, P. A., Kimball, S. R. & Jefferson, L. S. 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 280, 7570-7580 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 7570-7580
    • Kubica, N.1    Bolster, D.R.2    Farrell, P.A.3    Kimball, S.R.4    Jefferson, L.S.5
  • 44
    • 2342452623 scopus 로고    scopus 로고
    • Resistance training enhances components of the insulin signaling cascade in normal and high-fat-fed rodent skeletal muscle
    • Krisan, A. D. et al. Resistance training enhances components of the insulin signaling cascade in normal and high-fat-fed rodent skeletal muscle. J Appl Physiol (1985) 96, 1691-1700 (2004).
    • (2004) J Appl Physiol (1985) , vol.96 , pp. 1691-1700
    • Krisan, A.D.1
  • 45
    • 84878539473 scopus 로고    scopus 로고
    • MTOR signaling response to resistance exercise is altered by chronic resistance training and detraining in skeletal muscle
    • Ogasawara, R. et al. mTOR signaling response to resistance exercise is altered by chronic resistance training and detraining in skeletal muscle. J Appl Physiol (1985) 114, 934-940 (2013).
    • (2013) J Appl Physiol (1985) , vol.114 , pp. 934-940
    • Ogasawara, R.1
  • 46
    • 84941578428 scopus 로고    scopus 로고
    • Rapamycin does not prevent increases in myofibrillar or mitochondrial protein synthesis following endurance exercise
    • Philp, A. et al. Rapamycin does not prevent increases in myofibrillar or mitochondrial protein synthesis following endurance exercise. J Physiol 593, 4275-4284 (2015).
    • (2015) J Physiol , vol.593 , pp. 4275-4284
    • Philp, A.1
  • 47
    • 84864523531 scopus 로고    scopus 로고
    • Rapamycin reverses elevated mTORC1 signaling in lamin A/C-deficient mice, rescues cardiac and skeletal muscle function, and extends survival
    • Ramos, F. J. et al. Rapamycin reverses elevated mTORC1 signaling in lamin A/C-deficient mice, rescues cardiac and skeletal muscle function, and extends survival. Sci Transl Med 4, 144ra103 (2012).
    • (2012) Sci Transl Med , vol.4 , pp. 144ra103
    • Ramos, F.J.1
  • 48
    • 84958214586 scopus 로고    scopus 로고
    • Comparative effects of whey protein versus L-leucine on skeletal muscle protein synthesis and markers of ribosome biogenesis following resistance exercise
    • Mobley, C. B. et al. Comparative effects of whey protein versus L-leucine on skeletal muscle protein synthesis and markers of ribosome biogenesis following resistance exercise. Amino Acids 48, 733-750 (2016).
    • (2016) Amino Acids , vol.48 , pp. 733-750
    • Mobley, C.B.1
  • 49
    • 84935488816 scopus 로고    scopus 로고
    • Ribosome biogenesis adaptation in resistance training-induced human skeletal muscle hypertrophy American journal of physiology
    • Figueiredo, V. C. et al. Ribosome biogenesis adaptation in resistance training-induced human skeletal muscle hypertrophy. American journal of physiology. Endocrinology and metabolism 309, E72-E83 (2015).
    • (2015) Endocrinology and Metabolism , vol.309 , pp. E72-E83
    • Figueiredo, V.C.1
  • 50
    • 84881056831 scopus 로고    scopus 로고
    • Metabolism, cell growth, and tumorigenesis
    • Dang, C. V. M. Y. C., metabolism, cell growth, and tumorigenesis. Cold Spring Harb Perspect Med 3, a014217 (2013).
    • (2013) Cold Spring Harb Perspect Med , vol.3 , pp. a014217
    • Dang, C.V.M.Y.C.1
  • 51
    • 84954397325 scopus 로고    scopus 로고
    • Myc coordinates transcription and translation to enhance transformation and suppress invasiveness
    • Elkon, R. et al. Myc coordinates transcription and translation to enhance transformation and suppress invasiveness. EMBO Rep 16, 1723-1736 (2015).
    • (2015) EMBO Rep , vol.16 , pp. 1723-1736
    • Elkon, R.1
  • 52
    • 84880352272 scopus 로고    scopus 로고
    • Myc and mTOR converge on a common node in protein synthesis control that confers synthetic lethality in Myc-driven cancers
    • Pourdehnad, M. et al. Myc and mTOR converge on a common node in protein synthesis control that confers synthetic lethality in Myc-driven cancers. Proc Natl Acad Sci USA 110, 11988-11993 (2013).
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 11988-11993
    • Pourdehnad, M.1
  • 53
    • 84861162312 scopus 로고    scopus 로고
    • Mechanical loading induces the expression of a Pol i regulon at the onset of skeletal muscle hypertrophy
    • von Walden, F., Casagrande, V., Ostlund Farrants, A. K. & Nader, G. A. Mechanical loading induces the expression of a Pol I regulon at the onset of skeletal muscle hypertrophy. Am J Physiol Cell Physiol 302, C1523-C1530 (2012).
    • (2012) Am J Physiol Cell Physiol , vol.302 , pp. C1523-C1530
    • Von Walden, F.1    Casagrande, V.2    Ostlund Farrants, A.K.3    Nader, G.A.4
  • 54
    • 84930226959 scopus 로고    scopus 로고
    • Target of rapamycin complex 2 regulates cell growth via myc in drosophila
    • Kuo, Y., Huang, H., Cai, T. & Wang, T. Target of Rapamycin Complex 2 regulates cell growth via Myc in Drosophila. Sci Rep 5, 10339 (2015).
    • (2015) Sci Rep , vol.5 , pp. 10339
    • Kuo, Y.1    Huang, H.2    Cai, T.3    Wang, T.4
  • 55
    • 84887430714 scopus 로고    scopus 로고
    • MTOR complex 2 controls glycolytic metabolism in glioblastoma through FoxO acetylation and upregulation of c-Myc
    • Masui, K. et al. mTOR complex 2 controls glycolytic metabolism in glioblastoma through FoxO acetylation and upregulation of c-Myc. Cell Metab 18, 726-739 (2013).
    • (2013) Cell Metab , vol.18 , pp. 726-739
    • Masui, K.1
  • 56
    • 77955443001 scopus 로고    scopus 로고
    • Critical roles for mTORC2-And rapamycin-insensitive mTORC1-complexes in growth and survival of BCR-ABLexpressing leukemic cells
    • Carayol, N. et al. Critical roles for mTORC2-And rapamycin-insensitive mTORC1-complexes in growth and survival of BCR-ABLexpressing leukemic cells. Proc Natl Acad Sci USA 107, 12469-12474 (2010).
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 12469-12474
    • Carayol, N.1
  • 57
    • 79954618679 scopus 로고    scopus 로고
    • Novel insights into the regulation of skeletal muscle protein synthesis as revealed by a new nonradioactive in vivo technique
    • Goodman, C. A. et al. Novel insights into the regulation of skeletal muscle protein synthesis as revealed by a new nonradioactive in vivo technique. FASEB J 25, 1028-1039 (2011).
    • (2011) FASEB J , vol.25 , pp. 1028-1039
    • Goodman, C.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.