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Volumn 10, Issue 12, 2011, Pages 1940-1947

mTOR signaling in protein homeostasis: Less is more?

Author keywords

Aging; Chaperone; Degradation; Folding; Ribosome; Stress response; Target of rapamycin; Translation

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEAT SHOCK TRANSCRIPTION FACTOR 1; INITIATION FACTOR 4E BINDING PROTEIN 1; MAMMALIAN TARGET OF RAPAMYCIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 2; PROTEASOME; PROTEIN KINASE B; RHEB PROTEIN; RIBOSOME PROTEIN; S6 KINASE; UBIQUITIN;

EID: 79959191028     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.10.12.15858     Document Type: Review
Times cited : (56)

References (88)
  • 1
    • 36748999400 scopus 로고    scopus 로고
    • New modes of translational control in development, behavior and disease
    • DOI: 10.1016/j.molcel.2007.11.018
    • Sonenberg N, Hinnebusch AG. New modes of translational control in development, behavior and disease. Mol Cell 2007; 28:721-9; DOI: 10.1016/j.molcel.2007.11.018.
    • (2007) Mol Cell , vol.28 , pp. 721-729
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 2
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • DOI: 10.1038/nrm2838
    • Jackson RJ, Hellen CU, Pestova TV. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 2010; 11:113-27; DOI: 10.1038/nrm2838.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 3
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • DOI: 10.1126/science.1068408
    • Hartl FU, Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2002; 295:1852-8; DOI: 10.1126/science.1068408.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 4
    • 0033953974 scopus 로고    scopus 로고
    • Protein folding in vivo: The importance of molecular chaperones
    • DOI: 10.1016/S0959-440X(99)00044-5
    • Feldman DE, Frydman J. Protein folding in vivo: the importance of molecular chaperones. Curr Opin Struct Biol 2000; 10:26-33; DOI: 10.1016/S0959-440X(99)00044-5.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 26-33
    • Feldman, D.E.1    Frydman, J.2
  • 5
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • DOI: 10.1038/nature02263
    • Goldberg AL. Protein degradation and protection against misfolded or damaged proteins. Nature 2003; 426:895-9; DOI: 10.1038/nature02263.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 6
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • DOI: 10.1146/annurev.biochem.68.1.1015
    • Voges D, Zwickl P, Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 1999; 68:1015-68; DOI: 10.1146/annurev.biochem.68.1.1015.
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 7
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • DOI: 10.1126/science.1141448
    • Balch WE, Morimoto RI, Dillin A, Kelly JW. Adapting proteostasis for disease intervention. Science 2008; 319:916-9; DOI: 10.1126/science.1141448.
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 8
    • 64949099855 scopus 로고    scopus 로고
    • Protein homeostasis and aging: Taking care of proteins from the cradle to the grave
    • DOI: 10.1093/gerona/gln071.
    • Morimoto RI, Cuervo AM. Protein homeostasis and aging: taking care of proteins from the cradle to the grave. J Gerontol A Biol Sci Med Sci 2009; 64:167-70; DOI: 10.1093/gerona/gln071.
    • (2009) J Gerontol A Biol Sci Med Sci , vol.64 , pp. 167-170
    • Morimoto, R.I.1    Cuervo, A.M.2
  • 9
    • 33744505375 scopus 로고    scopus 로고
    • Nutrient overload, insulin resistance and ribosomal protein S6 kinase 1, S6K1
    • DOI: 10.1016/j.cmet.2006.05.003
    • Um SH, D'Alessio D, Thomas G. Nutrient overload, insulin resistance and ribosomal protein S6 kinase 1, S6K1. Cell Metab 2006; 3:393-402; DOI: 10.1016/j.cmet.2006.05.003.
    • (2006) Cell Metab , vol.3 , pp. 393-402
    • Um, S.H.1    D'Alessio, D.2    Thomas, G.3
  • 10
    • 78649391422 scopus 로고    scopus 로고
    • Cellular metabolic stress: Considering how cells respond to nutrient excess
    • DOI: 10.1016/j.molcel.2010.10.004
    • Wellen KE, Thompson CB. Cellular metabolic stress: considering how cells respond to nutrient excess. Mol Cell 2010; 40:323-32; DOI: 10.1016/j.molcel. 2010.10.004.
    • (2010) Mol Cell , vol.40 , pp. 323-332
    • Wellen, K.E.1    Thompson, C.B.2
  • 11
    • 13944269223 scopus 로고    scopus 로고
    • The plasticity of aging: Insights from long-lived mutants
    • DOI: 10.1016/j.cell.2005.02.002
    • Kenyon C. The plasticity of aging: insights from long-lived mutants. Cell 2005; 120:449-60; DOI: 10.1016/j.cell.2005.02.002.
    • (2005) Cell , vol.120 , pp. 449-460
    • Kenyon, C.1
  • 12
    • 32044465506 scopus 로고    scopus 로고
    • Signaling in growth and metabolism
    • TOR DOI: 10.1016/j.cell.2006.01.016
    • Wullschleger S, Loewith R, Hall MN. TOR signaling in growth and metabolism. Cell 2006; 124:471-84; DOI: 10.1016/j.cell.2006.01.016.
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 13
    • 27544500981 scopus 로고    scopus 로고
    • Growing roles for the mTOR pathway
    • DOI: 10.1016/j.ceb.2005.09.009
    • Sarbassov D, Ali SM, Sabatini DM. Growing roles for the mTOR pathway. Curr Opin Cell Biol 2005; 17:596-603; DOI: 10.1016/j.ceb.2005.09.009.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 596-603
    • Sarbassov, D.1    Ali, S.M.2    Sabatini, D.M.3
  • 14
    • 33645738458 scopus 로고    scopus 로고
    • Complexity of the TOR signaling network
    • DOI: 10.1016/j.tcb.2006.02.002
    • Inoki K, Guan KL. Complexity of the TOR signaling network. Trends Cell Biol 2006; 16:206-12; DOI: 10.1016/j.tcb.2006.02.002.
    • (2006) Trends Cell Biol , vol.16 , pp. 206-212
    • Inoki, K.1    Guan, K.L.2
  • 15
    • 77955747346 scopus 로고    scopus 로고
    • With TOR, less is more: A key role for the conserved nutrient-sensing TOR pathway in aging
    • DOI: 10.1016/j.cmet.2010.05.001
    • Kapahi P, Chen D, Rogers AN, Katewa SD, Li PW, Thomas EL, et al. With TOR, less is more: a key role for the conserved nutrient-sensing TOR pathway in aging. Cell Metab 2010; 11:453-65; DOI: 10.1016/j.cmet.2010.05.001.
    • (2010) Cell Metab , vol.11 , pp. 453-465
    • Kapahi, P.1    Chen, D.2    Rogers, A.N.3    Katewa, S.D.4    Li, P.W.5    Thomas, E.L.6
  • 16
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: Integrators of cell stress, development and lifespan
    • DOI: 10.1038/nrm2938
    • Akerfelt M, Morimoto RI, Sistonen L. Heat shock factors: integrators of cell stress, development and lifespan. Nat Rev Mol Cell Biol 2010; 11:545-55; DOI: 10.1038/nrm2938.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 17
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • DOI: 10.1016/j.cell.2006.04.014
    • Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell 2006; 125:443-51; DOI: 10.1016/j.cell.2006.04.014.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 18
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • DOI: 10.1016/S0896-6273(01)00177-5
    • Sherman MY, Goldberg AL. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 2001; 29:15-32; DOI: 10.1016/S0896-6273(01)00177-5.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 19
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • DOI: 10.1101/gad.1657108
    • Morimoto RI. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev 2008; 22:1427-38; DOI: 10.1101/gad.1657108.
    • (2008) Genes Dev , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 20
    • 0029564954 scopus 로고
    • Heat shock transcription factors: Structure and regulation
    • DOI: 10.1146/annurev.cb.11.110195.002301
    • Wu C. Heat shock transcription factors: structure and regulation. Annu Rev Cell Dev Biol 1995; 11:441-69; DOI: 10.1146/annurev.cb.11.110195.002301.
    • (1995) Annu Rev Cell Dev Biol , vol.11 , pp. 441-469
    • Wu, C.1
  • 21
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones and negative regulators
    • DOI: 10.1101/gad.12.24.3788
    • Morimoto RI. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones and negative regulators. Genes Dev 1998; 12:3788-96; DOI: 10.1101/gad.12.24.3788.
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 22
    • 0142186172 scopus 로고    scopus 로고
    • Aging and molecular chaperones
    • DOI: 10.1016/S0531-5565(03)00185-2
    • Soti C, Csermely P. Aging and molecular chaperones. Exp Gerontol 2003; 38:1037-40; DOI: 10.1016/S0531-5565(03)00185-2.
    • (2003) Exp Gerontol , vol.38 , pp. 1037-1040
    • Soti, C.1    Csermely, P.2
  • 23
    • 0347419282 scopus 로고    scopus 로고
    • Oxidative stress and aging-the use of superoxide dismutase/catalase mimetics to extend lifespan
    • DOI: 10.1042/BST0311305
    • Sampayo JN, Gill MS, Lithgow GJ. Oxidative stress and aging-the use of superoxide dismutase/catalase mimetics to extend lifespan. Biochem Soc Trans 2003; 31:1305-7; DOI: 10.1042/BST0311305.
    • (2003) Biochem Soc Trans , vol.31 , pp. 1305-1307
    • Sampayo, J.N.1    Gill, M.S.2    Lithgow, G.J.3
  • 24
    • 0036021375 scopus 로고    scopus 로고
    • Genetic analysis of tissue aging in Caenorhabditis elegans: A role for heat-shock factor and bacterial proliferation
    • PubMed
    • Garigan D, Hsu AL, Fraser AG, Kamath RS, Ahringer J, Kenyon C. Genetic analysis of tissue aging in Caenorhabditis elegans: a role for heat-shock factor and bacterial proliferation. Genetics 2002; 161:1101-12. PubMed.
    • (2002) Genetics , vol.161 , pp. 1101-1112
    • Garigan, D.1    Hsu, A.L.2    Fraser, A.G.3    Kamath, R.S.4    Ahringer, J.5    Kenyon, C.6
  • 25
    • 0038701745 scopus 로고    scopus 로고
    • Regulation of aging and age-related disease by DAF-16 and heat-shock factor
    • DOI: 10.1126/science.1083701
    • Hsu AL, Murphy CT, Kenyon C. Regulation of aging and age-related disease by DAF-16 and heat-shock factor. Science 2003; 300:1142-5; DOI: 10.1126/science.1083701.
    • (2003) Science , vol.300 , pp. 1142-1145
    • Hsu, A.L.1    Murphy, C.T.2    Kenyon, C.3
  • 26
    • 0742323000 scopus 로고    scopus 로고
    • Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones
    • DOI: 10.1091/mbc.E03-07-0532
    • Morley JF, Morimoto RI. Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones. Mol Biol Cell 2004; 15:657-64; DOI: 10.1091/mbc.E03-07-0532.
    • (2004) Mol Biol Cell , vol.15 , pp. 657-664
    • Morley, J.F.1    Morimoto, R.I.2
  • 27
    • 33947264077 scopus 로고    scopus 로고
    • PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase
    • DOI: 10.1016/j.molcel.2007.03.003
    • Sancak Y, Thoreen CC, Peterson TR, Lindquist RA, Kang SA, Spooner E, et al. PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase. Mol Cell 2007; 25:903-15; DOI: 10.1016/j.molcel.2007.03.003.
    • (2007) Mol Cell , vol.25 , pp. 903-915
    • Sancak, Y.1    Thoreen, C.C.2    Peterson, T.R.3    Lindquist, R.A.4    Kang, S.A.5    Spooner, E.6
  • 28
    • 67349241955 scopus 로고    scopus 로고
    • DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival
    • DOI: 10.1016/j.cell.2009.03.046
    • Peterson TR, Laplante M, Thoreen CC, Sancak Y, Kang SA, Kuehl WM, et al. DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival. Cell 2009; 137:873-86; DOI: 10.1016/j.cell.2009.03.046.
    • (2009) Cell , vol.137 , pp. 873-886
    • Peterson, T.R.1    Laplante, M.2    Thoreen, C.C.3    Sancak, Y.4    Kang, S.A.5    Kuehl, W.M.6
  • 29
    • 0036753494 scopus 로고    scopus 로고
    • Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control
    • DOI: 10.1016/S1097-2765(02)00636-6
    • Loewith R, Jacinto E, Wullschleger S, Lorberg A, Crespo JL, Bonenfant D, et al. Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. Mol Cell 2002; 10:457-68; DOI: 10.1016/S1097-2765(02)00636-6.
    • (2002) Mol Cell , vol.10 , pp. 457-468
    • Loewith, R.1    Jacinto, E.2    Wullschleger, S.3    Lorberg, A.4    Crespo, J.L.5    Bonenfant, D.6
  • 30
    • 0037178786 scopus 로고    scopus 로고
    • mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery
    • DOI: 10.1016/S0092-8674(02)00808-5
    • Kim DH, Sarbassov DD, Ali SM, King JE, Latek RR, Erdjument-Bromage H, et al. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 2002; 110:163-75; DOI: 10.1016/S0092- 8674(02)00808-5.
    • (2002) Cell , vol.110 , pp. 163-175
    • Kim, D.H.1    Sarbassov, D.D.2    Ali, S.M.3    King, J.E.4    Latek, R.R.5    Erdjument-Bromage, H.6
  • 31
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
    • DOI: 10.1016/j.cub.2004.06.054
    • Sarbassov DD, Ali SM, Kim DH, Guertin DA, Latek RR, Erdjument-Bromage H, et al. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr Biol 2004; 14:1296-302; DOI: 10.1016/j.cub.2004.06.054.
    • (2004) Curr Biol , vol.14 , pp. 1296-1302
    • Sarbassov, D.D.1    Ali, S.M.2    Kim, D.H.3    Guertin, D.A.4    Latek, R.R.5    Erdjument-Bromage, H.6
  • 32
    • 0037178781 scopus 로고    scopus 로고
    • Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action
    • DOI: 10.1016/S0092-8674(02)00833-4
    • Hara K, Maruki Y, Long X, Yoshino K, Oshiro N, Hidayat S, et al. Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action. Cell 2002; 110:177-89; DOI: 10.1016/S0092-8674(02)00833-4.
    • (2002) Cell , vol.110 , pp. 177-189
    • Hara, K.1    Maruki, Y.2    Long, X.3    Yoshino, K.4    Oshiro, N.5    Hidayat, S.6
  • 33
    • 67349217986 scopus 로고    scopus 로고
    • Molecular mechanisms of mTOR-mediated translational control
    • DOI: 10.1038/nrm2672
    • Ma XM, Blenis J. Molecular mechanisms of mTOR-mediated translational control. Nat Rev Mol Cell Biol 2009; 10:307-18; DOI: 10.1038/nrm2672.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 307-318
    • Ma, X.M.1    Blenis, J.2
  • 35
    • 0642367846 scopus 로고    scopus 로고
    • Genetics: Influence of TOR kinase on lifespan in C. elegans
    • DOI: 10.1038/426620a
    • Vellai T, Takacs-Vellai K, Zhang Y, Kovacs AL, Orosz L, Muller F. Genetics: influence of TOR kinase on lifespan in C. elegans. Nature 2003; 426:620; DOI: 10.1038/426620a.
    • (2003) Nature , vol.426 , pp. 620
    • Vellai, T.1    Takacs-Vellai, K.2    Zhang, Y.3    Kovacs, A.L.4    Orosz, L.5    Muller, F.6
  • 36
    • 3042648746 scopus 로고    scopus 로고
    • Regulation of lifespan in Drosophila by modulation of genes in the TOR signaling pathway
    • DOI: 10.1016/j.cub.2004.03.059
    • Kapahi P, Zid BM, Harper T, Koslover D, Sapin V, Benzer S. Regulation of lifespan in Drosophila by modulation of genes in the TOR signaling pathway. Curr Biol 2004; 14:885-90; DOI: 10.1016/j.cub.2004.03.059.
    • (2004) Curr Biol , vol.14 , pp. 885-890
    • Kapahi, P.1    Zid, B.M.2    Harper, T.3    Koslover, D.4    Sapin, V.5    Benzer, S.6
  • 37
    • 27744511769 scopus 로고    scopus 로고
    • Regulation of yeast replicative life span by TOR and Sch9 in response to nutrients
    • DOI: 10.1126/science.1115535
    • Kaeberlein M, Powers RW, III, Steffen KK, Westman EA, Hu D, Dang N, et al. Regulation of yeast replicative life span by TOR and Sch9 in response to nutrients. Science 2005; 310:1193-6; DOI: 10.1126/science.1115535.
    • (2005) Science , vol.310 , pp. 1193-1196
    • Kaeberlein, M.1    Powers III, R.W.2    Steffen, K.K.3    Westman, E.A.4    Hu, D.5    Dang, N.6
  • 38
    • 30944458446 scopus 로고    scopus 로고
    • Extension of chronological life span in yeast by decreased TOR pathway signaling
    • DOI: 10.1101/gad.1381406
    • Powers RW, III, Kaeberlein M, Caldwell SD, Kennedy BK, Fields S. Extension of chronological life span in yeast by decreased TOR pathway signaling. Genes Dev 2006; 20:174-84; DOI: 10.1101/gad.1381406.
    • (2006) Genes Dev , vol.20 , pp. 174-184
    • Powers III, R.W.1    Kaeberlein, M.2    Caldwell, S.D.3    Kennedy, B.K.4    Fields, S.5
  • 39
    • 67650944993 scopus 로고    scopus 로고
    • Rapamycin fed late in life extends lifespan in genetically heterogeneous mice
    • PubMed
    • Harrison DE, Strong R, Sharp ZD, Nelson JF, Astle CM, Flurkey K, et al. Rapamycin fed late in life extends lifespan in genetically heterogeneous mice. Nature 2009; 460:392-5; PubMed.
    • (2009) Nature , vol.460 , pp. 392-395
    • Harrison, D.E.1    Strong, R.2    Sharp, Z.D.3    Nelson, J.F.4    Astle, C.M.5    Flurkey, K.6
  • 40
    • 77953293417 scopus 로고    scopus 로고
    • Aging: Past, present and future
    • Albany, NY PubMed
    • Blagosklonny MV, Campisi J, Sinclair DA. Aging: past, present and future. Aging (Albany, NY) 2009; 1:1-5; PubMed.
    • (2009) Aging , vol.1 , pp. 1-5
    • Blagosklonny, M.V.1    Campisi, J.2    Sinclair, D.A.3
  • 42
    • 50549087736 scopus 로고    scopus 로고
    • Growth stimulation leads to cellular senescence when the cell cycle is blocked
    • DOI: 10.4161/cc.7.21.6919
    • Demidenko ZN, Blagosklonny MV. Growth stimulation leads to cellular senescence when the cell cycle is blocked. Cell Cycle 2008; 7:3355-61; DOI: 10.4161/cc.7.21.6919.
    • (2008) Cell Cycle , vol.7 , pp. 3355-3361
    • Demidenko, Z.N.1    Blagosklonny, M.V.2
  • 43
    • 78650352864 scopus 로고    scopus 로고
    • Increasing healthy lifespan by suppressing aging in our lifetime: Preliminary proposal
    • DOI: 10.4161/cc.9.24.14360
    • Blagosklonny MV. Increasing healthy lifespan by suppressing aging in our lifetime: preliminary proposal. Cell Cycle 2010; 9:4788-94; DOI: 10.4161/cc.9.24.14360.
    • (2010) Cell Cycle , vol.9 , pp. 4788-4794
    • Blagosklonny, M.V.1
  • 44
    • 40649104735 scopus 로고    scopus 로고
    • Loss of the tuberous sclerosis complex tumor suppressors triggers the unfolded protein response to regulate insulin signaling and apoptosis
    • DOI: 10.1016/j.molcel.2007.12.023
    • Ozcan U, Ozcan L, Yilmaz E, Duvel K, Sahin M, Manning BD, et al. Loss of the tuberous sclerosis complex tumor suppressors triggers the unfolded protein response to regulate insulin signaling and apoptosis. Mol Cell 2008; 29:541-51; DOI: 10.1016/j.molcel.2007.12.023.
    • (2008) Mol Cell , vol.29 , pp. 541-551
    • Ozcan, U.1    Ozcan, L.2    Yilmaz, E.3    Duvel, K.4    Sahin, M.5    Manning, B.D.6
  • 45
    • 79953171531 scopus 로고    scopus 로고
    • PI3K-mTORC1 attenuates stress response by inhibiting cap-independent Hsp70 translation
    • DOI: 10.1074/jbc.M110.172882
    • Sun J, Conn CS, Han Y, Yeung V, Qian SB. PI3K-mTORC1 attenuates stress response by inhibiting cap-independent Hsp70 translation. J Biol Chem 2011; 286:6791-800; DOI: 10.1074/jbc.M110.172882.
    • (2011) J Biol Chem , vol.286 , pp. 6791-6800
    • Sun, J.1    Conn, C.S.2    Han, Y.3    Yeung, V.4    Qian, S.B.5
  • 46
    • 0038433304 scopus 로고    scopus 로고
    • Insulin activation of Rheb, a mediator of mTOR/S6K/4E-BP signaling, is inhibited by TSC1 and 2
    • DOI: 10.1016/S1097-2765(03)00220-X
    • Garami A, Zwartkruis FJ, Nobukuni T, Joaquin M, Roccio M, Stocker H, et al. Insulin activation of Rheb, a mediator of mTOR/S6K/4E-BP signaling, is inhibited by TSC1 and 2. Mol Cell 2003; 11:1457-66; DOI: 10.1016/S1097-2765(03) 00220-X.
    • (2003) Mol Cell , vol.11 , pp. 1457-1466
    • Garami, A.1    Zwartkruis, F.J.2    Nobukuni, T.3    Joaquin, M.4    Roccio, M.5    Stocker, H.6
  • 47
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • DOI: 10.1038/nrm1618
    • Holcik M, Sonenberg N. Translational control in stress and apoptosis. Nat Rev Mol Cell Biol 2005; 6:318-27; DOI: 10.1038/nrm1618.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 48
    • 78649375395 scopus 로고    scopus 로고
    • Translational regulation of gene expression during conditions of cell stress
    • DOI: 10.1016/j.molcel.2010.09.028
    • Spriggs KA, Bushell M, Willis AE. Translational regulation of gene expression during conditions of cell stress. Mol Cell 2010; 40:228-37; DOI: 10.1016/j.molcel.2010.09.028.
    • (2010) Mol Cell , vol.40 , pp. 228-237
    • Spriggs, K.A.1    Bushell, M.2    Willis, A.E.3
  • 49
    • 0022133046 scopus 로고
    • The preferential translation of Drosophila hsp70 mRNA requires sequences in the untranslated leader
    • DOI: 10.1016/0092-8674(85)90286-7
    • McGarry TJ, Lindquist S. The preferential translation of Drosophila hsp70 mRNA requires sequences in the untranslated leader. Cell 1985; 42:903-11; DOI: 10.1016/0092-8674(85)90286-7.
    • (1985) Cell , vol.42 , pp. 903-911
    • McGarry, T.J.1    Lindquist, S.2
  • 50
    • 38849172516 scopus 로고    scopus 로고
    • Re-programming of translation following cell stress allows IRES-mediated translation to predominate
    • DOI: 10.1042/BC20070098
    • Spriggs KA, Stoneley M, Bushell M, Willis AE. Re-programming of translation following cell stress allows IRES-mediated translation to predominate. Biol Cell 2008; 100:27-38; DOI: 10.1042/BC20070098.
    • (2008) Biol Cell , vol.100 , pp. 27-38
    • Spriggs, K.A.1    Stoneley, M.2    Bushell, M.3    Willis, A.E.4
  • 51
    • 28844434215 scopus 로고    scopus 로고
    • Takeover of host ribosomes by divergent IRES elements
    • DOI: 10.1042/BST20051479
    • Sarnow P, Cevallos RC, Jan E. Takeover of host ribosomes by divergent IRES elements. Biochem Soc Trans 2005; 33:1479-82; DOI: 10.1042/BST20051479.
    • (2005) Biochem Soc Trans , vol.33 , pp. 1479-1482
    • Sarnow, P.1    Cevallos, R.C.2    Jan, E.3
  • 52
    • 56249147509 scopus 로고    scopus 로고
    • Rapamycin differentially inhibits S6Ks and 4E-BP1 to mediate cell-type-specific repression of mRNA translation
    • DOI: 10.1073/pnas.0809136105
    • Choo AY, Yoon SO, Kim SG, Roux PP, Blenis J. Rapamycin differentially inhibits S6Ks and 4E-BP1 to mediate cell-type-specific repression of mRNA translation. Proc Natl Acad Sci USA 2008; 105:17414-9; DOI: 10.1073/pnas. 0809136105.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 17414-17419
    • Choo, A.Y.1    Yoon, S.O.2    Kim, S.G.3    Roux, P.P.4    Blenis, J.5
  • 53
    • 70350696063 scopus 로고    scopus 로고
    • Differential contribution of the m7G-cap to the 5' end-dependent translation initiation of mammalian mRNAs
    • DOI: 10.1093/nar/gkp665
    • Andreev DE, Dmitriev SE, Terenin IM, Prassolov VS, Merrick WC, Shatsky IN. Differential contribution of the m7G-cap to the 5' end-dependent translation initiation of mammalian mRNAs. Nucleic Acids Res 2009; 37:6135-47; DOI: 10.1093/nar/gkp665.
    • (2009) Nucleic Acids Res , vol.37 , pp. 6135-6147
    • Andreev, D.E.1    Dmitriev, S.E.2    Terenin, I.M.3    Prassolov, V.S.4    Merrick, W.C.5    Shatsky, I.N.6
  • 54
    • 70350159136 scopus 로고    scopus 로고
    • Enhancer of decapping proteins 1 and 2 are important for translation during heat stress in Saccharomyces cerevisiae
    • DOI: 10.1111/j.1365-2958.2009.06827.x
    • Neef DW, Thiele DJ. Enhancer of decapping proteins 1 and 2 are important for translation during heat stress in Saccharomyces cerevisiae. Mol Microbiol 2009; 73:1032-42; DOI: 10.1111/j.1365-2958.2009.06827.x.
    • (2009) Mol Microbiol , vol.73 , pp. 1032-1042
    • Neef, D.W.1    Thiele, D.J.2
  • 55
    • 78649348967 scopus 로고    scopus 로고
    • Regulation of the mTOR complex 1 pathway by nutrients, growth factors and stress
    • DOI: 10.1016/j.molcel.2010.09.026
    • Sengupta S, Peterson TR, Sabatini DM. Regulation of the mTOR complex 1 pathway by nutrients, growth factors and stress. Mol Cell 2010; 40:310-22; DOI: 10.1016/j.molcel.2010.09.026.
    • (2010) Mol Cell , vol.40 , pp. 310-322
    • Sengupta, S.1    Peterson, T.R.2    Sabatini, D.M.3
  • 56
    • 33750044112 scopus 로고    scopus 로고
    • Stress and mTORture signaling
    • DOI: 10.1038/sj.onc.1209889
    • Reiling JH, Sabatini DM. Stress and mTORture signaling. Oncogene 2006; 25:6373-83; DOI: 10.1038/sj.onc.1209889.
    • (2006) Oncogene , vol.25 , pp. 6373-6383
    • Reiling, J.H.1    Sabatini, D.M.2
  • 57
    • 4244067355 scopus 로고    scopus 로고
    • Differential role of hydrogen peroxide in UV-induced signal transduction
    • DOI: 10.1023/A:1015901232124
    • Ding M, Li J, Leonard SS, Shi X, Costa M, Castranova V, et al. Differential role of hydrogen peroxide in UV-induced signal transduction. Mol Cell Biochem 2002; 235:81-90; DOI: 10.1023/A:1015901232124.
    • (2002) Mol Cell Biochem , vol.235 , pp. 81-90
    • Ding, M.1    Li, J.2    Leonard, S.S.3    Shi, X.4    Costa, M.5    Castranova, V.6
  • 58
    • 0025850837 scopus 로고
    • Heat shock induces two distinct S6 protein kinase activities in quiescent mammalian fibroblasts
    • DOI: 10.1002/jcp.1041480210
    • Jurivich DA, Chung J, Blenis J. Heat shock induces two distinct S6 protein kinase activities in quiescent mammalian fibroblasts. J Cell Physiol 1991; 148:252-9; DOI: 10.1002/jcp.1041480210.
    • (1991) J Cell Physiol , vol.148 , pp. 252-259
    • Jurivich, D.A.1    Chung, J.2    Blenis, J.3
  • 59
    • 0035746430 scopus 로고    scopus 로고
    • Flow-induced DNA synthesis requires signaling to a translational control pathway
    • DOI: 10.1006/jsre.2001.6091
    • Kraiss LW, Ennis TM, Alto NM. Flow-induced DNA synthesis requires signaling to a translational control pathway. J Surg Res 2001; 97:20-6; DOI: 10.1006/jsre.2001.6091.
    • (2001) J Surg Res , vol.97 , pp. 20-26
    • Kraiss, L.W.1    Ennis, T.M.2    Alto, N.M.3
  • 60
    • 0037047429 scopus 로고    scopus 로고
    • Dynamic remodeling of transcription complexes by molecular chaperones
    • DOI: 10.1016/S0092-8674(02)00860-7
    • Morimoto RI. Dynamic remodeling of transcription complexes by molecular chaperones. Cell 2002; 110:281-4; DOI: 10.1016/S0092-8674(02)00860-7.
    • (2002) Cell , vol.110 , pp. 281-284
    • Morimoto, R.I.1
  • 61
    • 43549102208 scopus 로고    scopus 로고
    • HSP90: The Rosetta stone for cellular protein dynamics?
    • DOI: 10.4161/cc.7.8.5723
    • Dezwaan DC, Freeman BC. HSP90: the Rosetta stone for cellular protein dynamics? Cell Cycle 2008; 7:1006-12; DOI: 10.4161/cc.7.8.5723.
    • (2008) Cell Cycle , vol.7 , pp. 1006-1012
    • Dezwaan, D.C.1    Freeman, B.C.2
  • 62
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • DOI: 10.1083/jcb.200104079
    • Young JC, Moarefi I, Hartl FU. Hsp90: a specialized but essential protein-folding tool. J Cell Biol 2001; 154:267-73; DOI: 10.1083/jcb.200104079.
    • (2001) J Cell Biol , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 63
    • 77956260496 scopus 로고    scopus 로고
    • mTORC1 links protein quality and quantity control by sensing chaperone availability
    • DOI: 10.1074/jbc.M110.120295
    • Qian SB, Zhang X, Sun J, Bennink JR, Yewdell JW, Patterson C. mTORC1 links protein quality and quantity control by sensing chaperone availability. J Biol Chem 2010; 285:27385-95; DOI: 10.1074/jbc.M110.120295.
    • (2010) J Biol Chem , vol.285 , pp. 27385-27395
    • Qian, S.B.1    Zhang, X.2    Sun, J.3    Bennink, J.R.4    Yewdell, J.W.5    Patterson, C.6
  • 64
    • 34247118887 scopus 로고    scopus 로고
    • Signalling to translation: How signal transduction pathways control the protein synthetic machinery
    • DOI: 10.1042/BJ20070024
    • Proud CG. Signalling to translation: how signal transduction pathways control the protein synthetic machinery. Biochem J 2007; 403:217-34; DOI: 10.1042/BJ20070024.
    • (2007) Biochem J , vol.403 , pp. 217-234
    • Proud, C.G.1
  • 65
    • 33748298941 scopus 로고    scopus 로고
    • Nutrient regulates Tor1 nuclear localization and association with rDNA promoter
    • DOI: 10.1038/nature05020
    • Li H, Tsang CK, Watkins M, Bertram PG, Zheng XF. Nutrient regulates Tor1 nuclear localization and association with rDNA promoter. Nature 2006; 442:1058-61; DOI: 10.1038/nature05020.
    • (2006) Nature , vol.442 , pp. 1058-1061
    • Li, H.1    Tsang, C.K.2    Watkins, M.3    Bertram, P.G.4    Zheng, X.F.5
  • 66
    • 0345305803 scopus 로고    scopus 로고
    • Chromatin-mediated regulation of nucleolar structure and RNA Pol I localization by TOR
    • DOI: 10.1093/emboj/cdg578
    • Tsang CK, Bertram PG, Ai W, Drenan R, Zheng XF. Chromatin-mediated regulation of nucleolar structure and RNA Pol I localization by TOR. EMBO J 2003; 22:6045-56; DOI: 10.1093/emboj/cdg578.
    • (2003) EMBO J , vol.22 , pp. 6045-6056
    • Tsang, C.K.1    Bertram, P.G.2    Ai, W.3    Drenan, R.4    Zheng, X.F.5
  • 67
    • 77953512889 scopus 로고    scopus 로고
    • mTOR binds to the promoters of RNA polymerase I- And III-transcribed genes
    • DOI: 10.4161/cc.9.5.10876
    • Tsang CK, Liu H, Zheng XF. mTOR binds to the promoters of RNA polymerase I- and III-transcribed genes. Cell Cycle 2010; 9:953-7; DOI: 10.4161/cc.9.5.10876.
    • (2010) Cell Cycle , vol.9 , pp. 953-957
    • Tsang, C.K.1    Liu, H.2    Zheng, X.F.3
  • 68
    • 77955287244 scopus 로고    scopus 로고
    • mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, and targets their repressor Maf1
    • DOI: 10.1073/pnas.1005188107
    • Kantidakis T, Ramsbottom BA, Birch JL, Dowding SN, White RJ. mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, and targets their repressor Maf1. Proc Natl Acad Sci USA 2010; 107:11823-8; DOI: 10.1073/pnas.1005188107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 11823-11828
    • Kantidakis, T.1    Ramsbottom, B.A.2    Birch, J.L.3    Dowding, S.N.4    White, R.J.5
  • 69
    • 0033761629 scopus 로고    scopus 로고
    • Synthesis of the translational apparatus is regulated at the translational level
    • DOI: 10.1046/j.1432-327.2000.01719.x
    • Meyuhas O. Synthesis of the translational apparatus is regulated at the translational level. Eur J Biochem 2000; 267:6321-30; DOI: 10.1046/j.1432-327. 2000.01719.x.
    • (2000) Eur J Biochem , vol.267 , pp. 6321-6330
    • Meyuhas, O.1
  • 71
    • 0035200856 scopus 로고    scopus 로고
    • Amino acid-induced translation of TOP mRNAs is fully dependent on phosphatidylinositol-3-kinase-mediated signaling, is partially inhibited by rapamycin, and is independent of S6K1 and rpS6 phosphorylation
    • DOI: 10.1128/MCB.21.24.8671-83.2001
    • Tang H, Hornstein E, Stolovich M, Levy G, Livingstone M, Templeton D, et al. Amino acid-induced translation of TOP mRNAs is fully dependent on phosphatidylinositol-3-kinase-mediated signaling, is partially inhibited by rapamycin, and is independent of S6K1 and rpS6 phosphorylation. Mol Cell Biol 2001; 21:8671-83; DOI: 10.1128/MCB.21.24.8671-83.2001.
    • (2001) Mol Cell Biol , vol.21 , pp. 8671-8683
    • Tang, H.1    Hornstein, E.2    Stolovich, M.3    Levy, G.4    Livingstone, M.5    Templeton, D.6
  • 72
    • 11144356304 scopus 로고    scopus 로고
    • S6K1(-/-)/S6K2(-/-) mice exhibit perinatal lethality and rapamycin-sensitive 5′-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated protein kinase-dependent S6 kinase pathway
    • DOI: 10.1128/MCB.24.8.3112-24.2004
    • Pende M, Um SH, Mieulet V, Sticker M, Goss VL, Mestan J, et al. S6K1(-/-)/S6K2(-/-) mice exhibit perinatal lethality and rapamycin-sensitive 5′-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated protein kinase-dependent S6 kinase pathway. Mol Cell Biol 2004; 24:3112-24; DOI: 10.1128/MCB.24.8.3112-24.2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 3112-3124
    • Pende, M.1    Um, S.H.2    Mieulet, V.3    Sticker, M.4    Goss, V.L.5    Mestan, J.6
  • 73
    • 0041315722 scopus 로고    scopus 로고
    • La protein is associated with terminal oligopyrimidine mRNAs in actively translating polysomes
    • DOI: 10.1074/jbc.M300722200
    • Cardinali B, Carissimi C, Gravina P, Pierandrei-Amaldi P. La protein is associated with terminal oligopyrimidine mRNAs in actively translating polysomes. J Biol Chem 2003; 278:35145-51; DOI: 10.1074/jbc.M300722200.
    • (2003) J Biol Chem , vol.278 , pp. 35145-35151
    • Cardinali, B.1    Carissimi, C.2    Gravina, P.3    Pierandrei-Amaldi, P.4
  • 74
    • 10044259856 scopus 로고    scopus 로고
    • Nonphosphorylated human la antigen interacts with nucleolin at nucleolar sites involved in rRNA biogenesis
    • DOI: 10.1128/MCB.24.24.10894-904.2004
    • Intine RV, Dundr M, Vassilev A, Schwartz E, Zhao Y, Zhao Y, et al. Nonphosphorylated human La antigen interacts with nucleolin at nucleolar sites involved in rRNA biogenesis. Mol Cell Biol 2004; 24:10894-904; DOI: 10.1128/MCB.24.24.10894-904.2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 10894-10904
    • Intine, R.V.1    Dundr, M.2    Vassilev, A.3    Schwartz, E.4    Zhao, Y.5    Zhao, Y.6
  • 75
    • 59249097362 scopus 로고    scopus 로고
    • The TSC-mTOR pathway mediates translational activation of TOP mRNAs by insulin largely in a raptor- Or rictor-independent manner
    • DOI: 10.1128/MCB.00980-08
    • Patursky-Polischuk I, Stolovich-Rain M, Hausner-Hanochi M, Kasir J, Cybulski N, Avruch J, et al. The TSC-mTOR pathway mediates translational activation of TOP mRNAs by insulin largely in a raptor- or rictor-independent manner. Mol Cell Biol 2009; 29:640-9; DOI: 10.1128/MCB.00980-08.
    • (2009) Mol Cell Biol , vol.29 , pp. 640-649
    • Patursky-Polischuk, I.1    Stolovich-Rain, M.2    Hausner-Hanochi, M.3    Kasir, J.4    Cybulski, N.5    Avruch, J.6
  • 76
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • DOI: 10.1126/science.1106148
    • Sarbassov DD, Guertin DA, Ali SM, Sabatini DM. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 2005; 307:1098-101; DOI: 10.1126/science.1106148.
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 77
    • 79952293503 scopus 로고    scopus 로고
    • Activation of mTORC2 by Association with the Ribosome
    • DOI: 10.1016/j.cell.2011.02.014
    • Zinzalla V, Stracka D, Oppliger W, Hall MN. Activation of mTORC2 by Association with the Ribosome. Cell 2011; 144:757-68; DOI: 10.1016/j.cell.2011. 02.014.
    • (2011) Cell , vol.144 , pp. 757-768
    • Zinzalla, V.1    Stracka, D.2    Oppliger, W.3    Hall, M.N.4
  • 78
    • 79952296641 scopus 로고    scopus 로고
    • The Ribosome and TORC2: Collaborators for Cell Growth
    • DOI: 10.1016/j.cell.2011.02.029
    • Xie X, Guan KL. The Ribosome and TORC2: Collaborators for Cell Growth. Cell 2011; 144:640-2; DOI: 10.1016/j.cell.2011.02.029.
    • (2011) Cell , vol.144 , pp. 640-642
    • Xie, X.1    Guan, K.L.2
  • 79
    • 63649157049 scopus 로고    scopus 로고
    • How common are extraribosomal functions of ribosomal proteins?
    • DOI: 10.1016/j.molcel.2009.03.006
    • Warner JR, McIntosh KB. How common are extraribosomal functions of ribosomal proteins? Mol Cell 2009; 34:3-11; DOI: 10.1016/j.molcel.2009.03.006.
    • (2009) Mol Cell , vol.34 , pp. 3-11
    • Warner, J.R.1    McIntosh, K.B.2
  • 80
    • 70350497397 scopus 로고    scopus 로고
    • Signaling to p53: Ribosomal proteins find their way
    • DOI: 10.1016/j.ccr.2009.09.024
    • Zhang Y, Lu H. Signaling to p53: ribosomal proteins find their way. Cancer Cell 2009; 16:369-77; DOI: 10.1016/j.ccr.2009.09.024.
    • (2009) Cancer Cell , vol.16 , pp. 369-377
    • Zhang, Y.1    Lu, H.2
  • 81
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding and degrading proteins
    • DOI: 10.1126/science.286.5446.1888
    • Wickner S, Maurizi MR, Gottesman S. Posttranslational quality control: folding, refolding and degrading proteins. Science 1999; 286:1888-93; DOI: 10.1126/science.286.5446.1888.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 82
    • 0021646339 scopus 로고
    • Stability of the cellular translation process
    • DOI: 10.1016/S0074-7696(08)61325-X
    • Kirkwood TB, Holliday R, Rosenberger RF. Stability of the cellular translation process. Int Rev Cytol 1984; 92:93-132; DOI: 10.1016/S0074-7696(08) 61325-X.
    • (1984) Int Rev Cytol , vol.92 , pp. 93-132
    • Kirkwood, T.B.1    Holliday, R.2    Rosenberger, R.F.3
  • 83
    • 33644872508 scopus 로고    scopus 로고
    • Characterization of rapidly degraded polypeptides in mammalian cells reveals a novel layer of nascent protein quality control
    • DOI: 10.1074/jbc.M509126200
    • Qian SB, Princiotta MF, Bennink JR, Yewdell JW. Characterization of rapidly degraded polypeptides in mammalian cells reveals a novel layer of nascent protein quality control. J Biol Chem 2006; 281:392-400; DOI: 10.1074/jbc.M509126200.
    • (2006) J Biol Chem , vol.281 , pp. 392-400
    • Qian, S.B.1    Princiotta, M.F.2    Bennink, J.R.3    Yewdell, J.W.4
  • 84
    • 36749050097 scopus 로고    scopus 로고
    • Mathews MB, Sonenberg N, Hershey JWB. (Eds.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Raught B, Gingras AC. Translational Control in Biology and Medicine. Mathews MB, Sonenberg N, Hershey JWB. (Eds.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York 2007; 369-400.
    • (2007) Translational Control in Biology and Medicine , pp. 369-400
    • Raught, B.1    Gingras, A.C.2
  • 85
    • 0036438894 scopus 로고    scopus 로고
    • Regulation of peptide-chain elongation in mammalian cells
    • DOI: 10.1046/j.1432-1033.2002.03290.x
    • Browne GJ, Proud CG. Regulation of peptide-chain elongation in mammalian cells. Eur J Biochem 2002; 269:5360-8; DOI: 10.1046/j.1432-1033.2002.03290.x.
    • (2002) Eur J Biochem , vol.269 , pp. 5360-5368
    • Browne, G.J.1    Proud, C.G.2
  • 86
    • 0035881470 scopus 로고    scopus 로고
    • Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase
    • DOI: 10.1093/emboj/20.16.4370
    • Wang X, Li W, Williams M, Terada N, Alessi DR, Proud CG. Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase. EMBO J 2001; 20:4370-9; DOI: 10.1093/emboj/20.16.4370.
    • (2001) EMBO J , vol.20 , pp. 4370-4379
    • Wang, X.1    Li, W.2    Williams, M.3    Terada, N.4    Alessi, D.R.5    Proud, C.G.6
  • 87
    • 62049083910 scopus 로고    scopus 로고
    • Transient ribosomal attenuation coordinates protein synthesis and co-translational folding
    • DOI: 10.1038/nsmb.1554
    • Zhang G, Hubalewska M, Ignatova Z. Transient ribosomal attenuation coordinates protein synthesis and co-translational folding. Nat Struct Mol Biol 2009; 16:274-80; DOI: 10.1038/nsmb.1554.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 274-280
    • Zhang, G.1    Hubalewska, M.2    Ignatova, Z.3
  • 88
    • 77649272553 scopus 로고    scopus 로고
    • Slowing bacterial translation speed enhances eukaryotic protein folding efficiency
    • DOI: 10.1016/j.jmb.2009.12.042
    • Siller E, Dezwaan DC, Anderson JF, Freeman BC, Barral JM. Slowing bacterial translation speed enhances eukaryotic protein folding efficiency. J Mol Biol 2010; 396:1310-8; DOI: 10.1016/j.jmb.2009.12.042.
    • (2010) J Mol Biol , vol.396 , pp. 1310-1318
    • Siller, E.1    Dezwaan, D.C.2    Anderson, J.F.3    Freeman, B.C.4    Barral, J.M.5


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