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Volumn 36, Issue 11, 2014, Pages 1082-1090

How does oncogene transformation render tumor cells hypersensitive to nutrient deprivation?

Author keywords

EEF2 kinase (eEF2K); Metabolic stress; MRNA translation elongation; Oncogenes; Stress signaling

Indexed keywords

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ANGIOGENESIS INHIBITOR; DEOXYGLUCOSE; ELONGATION FACTOR 2; ELONGATION FACTOR 2 KINASE; GUANOSINE TRIPHOSPHATE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MESSENGER RNA; METFORMIN; MITOGEN ACTIVATED PROTEIN KINASE; ONCOPROTEIN; PROTEIN TYROSINE KINASE; RAPAMYCIN; S6 KINASE; EEF2K PROTEIN, HUMAN; KRAS PROTEIN, HUMAN; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; RAS PROTEIN;

EID: 84907879675     PISSN: 02659247     EISSN: 15211878     Source Type: Journal    
DOI: 10.1002/bies.201400085     Document Type: Article
Times cited : (9)

References (64)
  • 1
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • Hanahan D, Weinberg RA. 2011. Hallmarks of cancer: the next generation. Cell 144: 646-74.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 52649107626 scopus 로고    scopus 로고
    • Cancer cell metabolism: Warburg and beyond
    • Hsu PP, Sabatini DM. 2008. Cancer cell metabolism: Warburg and beyond. Cell 134: 703-7.
    • (2008) Cell , vol.134 , pp. 703-707
    • Hsu, P.P.1    Sabatini, D.M.2
  • 3
    • 20544449673 scopus 로고    scopus 로고
    • The glucose dependence of Akt-transformed cells can be reversed by pharmacologic activation of fatty acid beta-oxidation
    • Buzzai M, Bauer DE, Jones RG, Deberardinis RJ, et al. 2005. The glucose dependence of Akt-transformed cells can be reversed by pharmacologic activation of fatty acid beta-oxidation. Oncogene 24: 4165-73.
    • (2005) Oncogene , vol.24 , pp. 4165-4173
    • Buzzai, M.1    Bauer, D.E.2    Jones, R.G.3    Deberardinis, R.J.4
  • 4
    • 77952562382 scopus 로고    scopus 로고
    • Glucose addiction of TSC null cells is caused by failed mTORC1-dependent balancing of metabolic demand with supply
    • Choo AY, Kim SG, Vander Heiden MG, Mahoney SJ, et al. 2010. Glucose addiction of TSC null cells is caused by failed mTORC1-dependent balancing of metabolic demand with supply. Mol Cell 38: 487-99.
    • (2010) Mol Cell , vol.38 , pp. 487-499
    • Choo, A.Y.1    Kim, S.G.2    Vander Heiden, M.G.3    Mahoney, S.J.4
  • 5
    • 84894212463 scopus 로고    scopus 로고
    • Regulation of TORC1 in response to amino acid starvation via lysosomal recruitment of TSC2
    • Demetriades C, Doumpas N, Teleman AA. 2014. Regulation of TORC1 in response to amino acid starvation via lysosomal recruitment of TSC2. Cell 156: 786-99.
    • (2014) Cell , vol.156 , pp. 786-799
    • Demetriades, C.1    Doumpas, N.2    Teleman, A.A.3
  • 7
    • 84878271546 scopus 로고    scopus 로고
    • The eEF2 kinase confers resistance to nutrient deprivation by blocking translation elongation
    • Leprivier G, Remke M, Rotblat B, Dubuc A, et al. 2013. The eEF2 kinase confers resistance to nutrient deprivation by blocking translation elongation. Cell 153: 1064-79.
    • (2013) Cell , vol.153 , pp. 1064-1079
    • Leprivier, G.1    Remke, M.2    Rotblat, B.3    Dubuc, A.4
  • 8
    • 84869027086 scopus 로고    scopus 로고
    • ATF4 regulates MYC-mediated neuroblastoma cell death upon glutamine deprivation
    • Qing G, Li B, Vu A, Skuli N, et al. 2012. ATF4 regulates MYC-mediated neuroblastoma cell death upon glutamine deprivation. Cancer Cell 22: 631-44.
    • (2012) Cancer Cell , vol.22 , pp. 631-644
    • Qing, G.1    Li, B.2    Vu, A.3    Skuli, N.4
  • 9
    • 0032539534 scopus 로고    scopus 로고
    • A unique glucose-dependent apoptotic pathway induced by c-Myc
    • Shim H, Chun YS, Lewis BC, Dang CV. 1998. A unique glucose-dependent apoptotic pathway induced by c-Myc. Proc Natl Acad Sci USA 95: 1511-6.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1511-1516
    • Shim, H.1    Chun, Y.S.2    Lewis, B.C.3    Dang, C.V.4
  • 10
    • 62549151252 scopus 로고    scopus 로고
    • Why are tumour blood vessels abnormal and why is it important to know
    • Nagy JA, Chang SH, Dvorak AM, Dvorak HF. 2009. Why are tumour blood vessels abnormal and why is it important to know? Br J Cancer 100: 865-9.
    • (2009) Br J Cancer , vol.100 , pp. 865-869
    • Nagy, J.A.1    Chang, S.H.2    Dvorak, A.M.3    Dvorak, H.F.4
  • 11
    • 61849135453 scopus 로고    scopus 로고
    • Tumor suppressors and cell metabolism: a recipe for cancer growth
    • Jones RG, Thompson CB. 2009. Tumor suppressors and cell metabolism: a recipe for cancer growth. Genes Dev 23: 537-48.
    • (2009) Genes Dev , vol.23 , pp. 537-548
    • Jones, R.G.1    Thompson, C.B.2
  • 12
    • 0023158728 scopus 로고
    • Elevated levels of glucose transport and transporter messenger RNA are induced by ras or src oncogenes
    • Flier JS, Mueckler MM, Usher P, Lodish HF. 1987. Elevated levels of glucose transport and transporter messenger RNA are induced by ras or src oncogenes. Science 235: 1492-5.
    • (1987) Science , vol.235 , pp. 1492-1495
    • Flier, J.S.1    Mueckler, M.M.2    Usher, P.3    Lodish, H.F.4
  • 13
    • 0034698178 scopus 로고    scopus 로고
    • Deregulation of glucose transporter 1 and glycolytic gene expression by c-Myc
    • Osthus RC, Shim H, Kim S, Li Q, et al. 2000. Deregulation of glucose transporter 1 and glycolytic gene expression by c-Myc. J Biol Chem 275: 21797-800.
    • (2000) J Biol Chem , vol.275 , pp. 21797-21800
    • Osthus, R.C.1    Shim, H.2    Kim, S.3    Li, Q.4
  • 14
    • 57749088701 scopus 로고    scopus 로고
    • Myc regulates a transcriptional program that stimulates mitochondrial glutaminolysis and leads to glutamine addiction
    • Wise DR, DeBerardinis RJ, Mancuso A, Sayed N, et al. 2008. Myc regulates a transcriptional program that stimulates mitochondrial glutaminolysis and leads to glutamine addiction. Proc Natl Acad Sci USA 105: 18782-7.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 18782-18787
    • Wise, D.R.1    DeBerardinis, R.J.2    Mancuso, A.3    Sayed, N.4
  • 15
    • 64749116346 scopus 로고    scopus 로고
    • c-Myc suppression of miR-23a/b enhances mitochondrial glutaminase expression and glutamine metabolism
    • Gao P, Tchernyshyov I, Chang TC, Lee YS, et al. 2009. c-Myc suppression of miR-23a/b enhances mitochondrial glutaminase expression and glutamine metabolism. Nature 458: 762-5.
    • (2009) Nature , vol.458 , pp. 762-765
    • Gao, P.1    Tchernyshyov, I.2    Chang, T.C.3    Lee, Y.S.4
  • 16
    • 0030921103 scopus 로고    scopus 로고
    • c-Myc transactivation of LDH-A: implications for tumor metabolism and growth
    • Shim H, Dolde C, Lewis BC, Wu CS, et al. 1997. c-Myc transactivation of LDH-A: implications for tumor metabolism and growth. Proc Natl Acad Sci USA 94: 6658-63.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6658-6663
    • Shim, H.1    Dolde, C.2    Lewis, B.C.3    Wu, C.S.4
  • 17
    • 0028802746 scopus 로고
    • A hierarchy of ATP-consuming processes in mammalian cells
    • Buttgereit F, Brand MD. 1995. A hierarchy of ATP-consuming processes in mammalian cells. Biochem J 312: 163-7.
    • (1995) Biochem J , vol.312 , pp. 163-167
    • Buttgereit, F.1    Brand, M.D.2
  • 18
    • 84863763440 scopus 로고    scopus 로고
    • AMPK regulates NADPH homeostasis to promote tumour cell survival during energy stress
    • Jeon SM, Chandel NS, Hay N. 2012. AMPK regulates NADPH homeostasis to promote tumour cell survival during energy stress. Nature 485: 661-5.
    • (2012) Nature , vol.485 , pp. 661-665
    • Jeon, S.M.1    Chandel, N.S.2    Hay, N.3
  • 19
    • 80052697287 scopus 로고    scopus 로고
    • The role of autophagy in cancer: therapeutic implications
    • Yang ZJ, Chee CE, Huang S, Sinicrope FA. 2011. The role of autophagy in cancer: therapeutic implications. Mol Cancer Ther 10: 1533-41.
    • (2011) Mol Cancer Ther , vol.10 , pp. 1533-1541
    • Yang, Z.J.1    Chee, C.E.2    Huang, S.3    Sinicrope, F.A.4
  • 20
    • 45849105156 scopus 로고    scopus 로고
    • The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1
    • Sancak Y, Peterson TR, Shaul YD, Lindquist RA, et al. 2008. The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science 320: 1496-501.
    • (2008) Science , vol.320 , pp. 1496-1501
    • Sancak, Y.1    Peterson, T.R.2    Shaul, Y.D.3    Lindquist, R.A.4
  • 21
    • 79953728453 scopus 로고    scopus 로고
    • Eukaryotic elongation factor-2 (eEF2): its regulation and peptide chain elongation
    • Kaul G, Pattan G, Rafeequi T. 2011. Eukaryotic elongation factor-2 (eEF2): its regulation and peptide chain elongation. Cell Biochem Funct 29: 227-34.
    • (2011) Cell Biochem Funct , vol.29 , pp. 227-234
    • Kaul, G.1    Pattan, G.2    Rafeequi, T.3
  • 24
    • 0025868969 scopus 로고
    • Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes
    • Price NT, Redpath NT, Severinov KV, Campbell DG, et al. 1991. Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes. FEBS Lett 282: 253-8.
    • (1991) FEBS Lett , vol.282 , pp. 253-258
    • Price, N.T.1    Redpath, N.T.2    Severinov, K.V.3    Campbell, D.G.4
  • 25
    • 0035881470 scopus 로고    scopus 로고
    • Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase
    • Wang X, Li W, Williams M, Terada N, et al. 2001. Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase. EMBO J 20: 4370-9.
    • (2001) EMBO J , vol.20 , pp. 4370-4379
    • Wang, X.1    Li, W.2    Williams, M.3    Terada, N.4
  • 27
    • 84887258189 scopus 로고    scopus 로고
    • B-Raf mutation: a key player in molecular biology of cancer
    • Rahman MA, Salajegheh A, Smith RA, Lam AK. 2013. B-Raf mutation: a key player in molecular biology of cancer. Exp Mol Pathol 95: 336-42.
    • (2013) Exp Mol Pathol , vol.95 , pp. 336-342
    • Rahman, M.A.1    Salajegheh, A.2    Smith, R.A.3    Lam, A.K.4
  • 28
  • 29
    • 1642328617 scopus 로고    scopus 로고
    • Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398
    • Browne GJ, Finn SG, Proud CG. 2004. Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398. J Biol Chem 279: 12220-31.
    • (2004) J Biol Chem , vol.279 , pp. 12220-12231
    • Browne, G.J.1    Finn, S.G.2    Proud, C.G.3
  • 30
    • 84893455835 scopus 로고    scopus 로고
    • The dark face of AMPK as an essential tumor promoter
    • Jeon SM, Hay N. 2012. The dark face of AMPK as an essential tumor promoter. Cell Logist 2: 197-202.
    • (2012) Cell Logist , vol.2 , pp. 197-202
    • Jeon, S.M.1    Hay, N.2
  • 31
    • 84858782079 scopus 로고    scopus 로고
    • AMPK: a nutrient and energy sensor that maintains energy homeostasis
    • Hardie DG, Ross FA, Hawley SA. 2012. AMPK: a nutrient and energy sensor that maintains energy homeostasis. Nat Rev Mol Cell Biol 13: 251-62.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 251-262
    • Hardie, D.G.1    Ross, F.A.2    Hawley, S.A.3
  • 32
    • 0036438894 scopus 로고    scopus 로고
    • Regulation of peptide-chain elongation in mammalian cells
    • Browne GJ, Proud CG. 2002. Regulation of peptide-chain elongation in mammalian cells. Eur J Bio chem 269: 5360-8.
    • (2002) Eur J Bio chem , vol.269 , pp. 5360-5368
    • Browne, G.J.1    Proud, C.G.2
  • 33
    • 84873810502 scopus 로고    scopus 로고
    • Eukaryotic elongation factor 2 controls TNF-alpha translation in LPS-induced hepatitis
    • Gonzalez-Teran B, Cortes JR, Manieri E, Matesanz N, et al. 2013. Eukaryotic elongation factor 2 controls TNF-alpha translation in LPS-induced hepatitis. J Clin Invest 123: 164-78.
    • (2013) J Clin Invest , vol.123 , pp. 164-178
    • Gonzalez-Teran, B.1    Cortes, J.R.2    Manieri, E.3    Matesanz, N.4
  • 34
    • 1642363230 scopus 로고    scopus 로고
    • Loss of translational control in yeast compromised for the major mRNA decay pathway
    • Holmes LE, Campbell SG, De Long SK, Sachs AB, et al. 2004. Loss of translational control in yeast compromised for the major mRNA decay pathway. Mol Cell Biol 24: 2998-3010.
    • (2004) Mol Cell Biol , vol.24 , pp. 2998-3010
    • Holmes, L.E.1    Campbell, S.G.2    De Long, S.K.3    Sachs, A.B.4
  • 35
    • 84884887844 scopus 로고    scopus 로고
    • A perspective on mammalian upstream open reading frame function
    • Somers J, Poyry T, Willis AE. 2013. A perspective on mammalian upstream open reading frame function. Int J Biochem Cell Biol 45: 1690-700.
    • (2013) Int J Biochem Cell Biol , vol.45 , pp. 1690-1700
    • Somers, J.1    Poyry, T.2    Willis, A.E.3
  • 36
    • 0035853762 scopus 로고    scopus 로고
    • Internal ribosome entry site-mediated translation of a mammalian mRNA is regulated by amino acid availability
    • Fernandez J, Yaman I, Mishra R, Merrick WC, et al. 2001. Internal ribosome entry site-mediated translation of a mammalian mRNA is regulated by amino acid availability. J Biol Chem 276: 12285-91.
    • (2001) J Biol Chem , vol.276 , pp. 12285-12291
    • Fernandez, J.1    Yaman, I.2    Mishra, R.3    Merrick, W.C.4
  • 37
    • 33745838924 scopus 로고    scopus 로고
    • Amino acid starvation induces the SNAT2 neutral amino acid transporter by a mechanism that involves eukaryotic initiation factor 2alpha phosphorylation and cap-independent translation
    • Gaccioli F, Huang CC, Wang C, Bevilacqua E, et al. 2006. Amino acid starvation induces the SNAT2 neutral amino acid transporter by a mechanism that involves eukaryotic initiation factor 2alpha phosphorylation and cap-independent translation. J Biol Chem 281: 17929-40.
    • (2006) J Biol Chem , vol.281 , pp. 17929-17940
    • Gaccioli, F.1    Huang, C.C.2    Wang, C.3    Bevilacqua, E.4
  • 38
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • Holcik M, Sonenberg N. 2005. Translational control in stress and apoptosis. Nat Rev Mol Cell Biol 6: 318-27.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 39
    • 38849172516 scopus 로고    scopus 로고
    • Re-programming of translation following cell stress allows IRES-mediated translation to predominate
    • Spriggs KA, Stoneley M, Bushell M, Willis AE. 2008. Re-programming of translation following cell stress allows IRES-mediated translation to predominate. Biol Cell 100: 27-38.
    • (2008) Biol Cell , vol.100 , pp. 27-38
    • Spriggs, K.A.1    Stoneley, M.2    Bushell, M.3    Willis, A.E.4
  • 40
    • 35649001888 scopus 로고    scopus 로고
    • A hypoxia-controlled cap-dependent to cap-independent translation switch in breast cancer
    • Braunstein S, Karpisheva K, Pola C, Goldberg J, et al. 2007. A hypoxia-controlled cap-dependent to cap-independent translation switch in breast cancer. Mol Cell 28: 501-12.
    • (2007) Mol Cell , vol.28 , pp. 501-512
    • Braunstein, S.1    Karpisheva, K.2    Pola, C.3    Goldberg, J.4
  • 41
    • 0031869662 scopus 로고    scopus 로고
    • Translation of vascular endothelial growth factor mRNA by internal ribosome entry: implications for translation under hypoxia
    • Stein I, Itin A, Einat P, Skaliter R, et al. 1998. Translation of vascular endothelial growth factor mRNA by internal ribosome entry: implications for translation under hypoxia. Mol Cell Biol 18: 3112-9.
    • (1998) Mol Cell Biol , vol.18 , pp. 3112-3119
    • Stein, I.1    Itin, A.2    Einat, P.3    Skaliter, R.4
  • 42
    • 77953565102 scopus 로고    scopus 로고
    • The GCN2-ATF4 pathway is critical for tumour cell survival and proliferation in response to nutrient deprivation
    • Ye J, Kumanova M, Hart LS, Sloane K, et al. 2010. The GCN2-ATF4 pathway is critical for tumour cell survival and proliferation in response to nutrient deprivation. EMBO J 29: 2082-96.
    • (2010) EMBO J , vol.29 , pp. 2082-2096
    • Ye, J.1    Kumanova, M.2    Hart, L.S.3    Sloane, K.4
  • 43
    • 0033160190 scopus 로고    scopus 로고
    • A new internal-ribosome-entry-site motif potentiates XIAP-mediated cytoprotection
    • Holcik M, Lefebvre C, Yeh C, Chow T, et al. 1999. A new internal-ribosome-entry-site motif potentiates XIAP-mediated cytoprotection. Nat Cell Biol 1: 190-2.
    • (1999) Nat Cell Biol , vol.1 , pp. 190-192
    • Holcik, M.1    Lefebvre, C.2    Yeh, C.3    Chow, T.4
  • 44
    • 3142754413 scopus 로고    scopus 로고
    • BCL-2 translation is mediated via internal ribosome entry during cell stress
    • Sherrill KW, Byrd MP, Van Eden ME, Lloyd RE. 2004. BCL-2 translation is mediated via internal ribosome entry during cell stress. J Biol Chem 279: 29066-74.
    • (2004) J Biol Chem , vol.279 , pp. 29066-29074
    • Sherrill, K.W.1    Byrd, M.P.2    Van Eden, M.E.3    Lloyd, R.E.4
  • 45
    • 33744955344 scopus 로고    scopus 로고
    • Internal ribosome entry site-mediated translation of Apaf-1, but not XIAP, is regulated during UV-induced cell death
    • Ungureanu NH, Cloutier M, Lewis SM, de Silva N, et al. 2006. Internal ribosome entry site-mediated translation of Apaf-1, but not XIAP, is regulated during UV-induced cell death. J Biol Chem 281: 15155-63.
    • (2006) J Biol Chem , vol.281 , pp. 15155-15163
    • Ungureanu, N.H.1    Cloutier, M.2    Lewis, S.M.3    de Silva, N.4
  • 46
    • 34250307059 scopus 로고    scopus 로고
    • Ras transformation of RIE-1 cells activates cap-independent translation of ornithine decarboxylase: regulation by the Raf/MEK/ERK and phosphatidylinositol 3-kinase pathways
    • Origanti S, Shantz LM. 2007. Ras transformation of RIE-1 cells activates cap-independent translation of ornithine decarboxylase: regulation by the Raf/MEK/ERK and phosphatidylinositol 3-kinase pathways. Cancer Res 67: 4834-42.
    • (2007) Cancer Res , vol.67 , pp. 4834-4842
    • Origanti, S.1    Shantz, L.M.2
  • 47
    • 19944433283 scopus 로고    scopus 로고
    • Ribosome stalling regulates IRES-mediated translation in eukaryotes, a parallel to prokaryotic attenuation
    • Fernandez J, Yaman I, Huang C, Liu H, et al. 2005. Ribosome stalling regulates IRES-mediated translation in eukaryotes, a parallel to prokaryotic attenuation. Mol Cell 17: 405-16.
    • (2005) Mol Cell , vol.17 , pp. 405-416
    • Fernandez, J.1    Yaman, I.2    Huang, C.3    Liu, H.4
  • 48
    • 46149087988 scopus 로고    scopus 로고
    • Elongation factor 2 and fragile X mental retardation protein control the dynamic translation of Arc/Arg3.1 essential for mGluR-LTD
    • Park S, Park JM, Kim S, Kim JA, et al. 2008. Elongation factor 2 and fragile X mental retardation protein control the dynamic translation of Arc/Arg3.1 essential for mGluR-LTD. Neuron 59: 70-83.
    • (2008) Neuron , vol.59 , pp. 70-83
    • Park, S.1    Park, J.M.2    Kim, S.3    Kim, J.A.4
  • 49
    • 84888136766 scopus 로고    scopus 로고
    • Less is more: improving proteostasis by translation slow down
    • Sherman MY, Qian SB. 2013. Less is more: improving proteostasis by translation slow down. Trends Biochem Sci 38: 585-91.
    • (2013) Trends Biochem Sci , vol.38 , pp. 585-591
    • Sherman, M.Y.1    Qian, S.B.2
  • 50
    • 77649272553 scopus 로고    scopus 로고
    • Slowing bacterial translation speed enhances eukaryotic protein folding efficiency
    • Siller E, DeZwaan DC, Anderson JF, Freeman BC, et al. 2010. Slowing bacterial translation speed enhances eukaryotic protein folding efficiency. J Mol Biol 396: 1310-8.
    • (2010) J Mol Biol , vol.396 , pp. 1310-1318
    • Siller, E.1    DeZwaan, D.C.2    Anderson, J.F.3    Freeman, B.C.4
  • 51
    • 62049083910 scopus 로고    scopus 로고
    • Transient ribosomal attenuation coordinates protein synthesis and co-translational folding
    • Zhang G, Hubalewska M, Ignatova Z. 2009. Transient ribosomal attenuation coordinates protein synthesis and co-translational folding. Nat Struct Mol Biol 16: 274-80.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 274-280
    • Zhang, G.1    Hubalewska, M.2    Ignatova, Z.3
  • 52
    • 34948856961 scopus 로고    scopus 로고
    • Ribosome kinetics and aa-tRNA competition determine rate and fidelity of peptide synthesis
    • Fluitt A, Pienaar E, Viljoen H. 2007. Ribosome kinetics and aa-tRNA competition determine rate and fidelity of peptide synthesis. Comput Biol Chem 31: 335-46.
    • (2007) Comput Biol Chem , vol.31 , pp. 335-346
    • Fluitt, A.1    Pienaar, E.2    Viljoen, H.3
  • 53
    • 84870806182 scopus 로고    scopus 로고
    • A conserved eEF2 coding variant in SCA26 leads to loss of translational fidelity and increased susceptibility to proteostatic insult
    • Hekman KE, Yu GY, Brown CD, Zhu H, et al. 2012. A conserved eEF2 coding variant in SCA26 leads to loss of translational fidelity and increased susceptibility to proteostatic insult. Hum Mol Genet 21: 5472-83.
    • (2012) Hum Mol Genet , vol.21 , pp. 5472-5483
    • Hekman, K.E.1    Yu, G.Y.2    Brown, C.D.3    Zhu, H.4
  • 54
    • 84873467908 scopus 로고    scopus 로고
    • Cotranslational response to proteotoxic stress by elongation pausing of ribosomes
    • Liu B, Han Y, Qian SB. 2013. Cotranslational response to proteotoxic stress by elongation pausing of ribosomes. Mol Cell 49: 453-63.
    • (2013) Mol Cell , vol.49 , pp. 453-463
    • Liu, B.1    Han, Y.2    Qian, S.B.3
  • 55
    • 84873442839 scopus 로고    scopus 로고
    • Widespread regulation of translation by elongation pausing in heat shock
    • Shalgi R, Hurt JA, Krykbaeva I, Taipale M, et al. 2013. Widespread regulation of translation by elongation pausing in heat shock. Mol Cell 49: 439-52.
    • (2013) Mol Cell , vol.49 , pp. 439-452
    • Shalgi, R.1    Hurt, J.A.2    Krykbaeva, I.3    Taipale, M.4
  • 56
    • 0036086064 scopus 로고    scopus 로고
    • The unfolded protein response in nutrient sensing and differentiation
    • Kaufman RJ, Scheuner D, Schroder M, Shen X, et al. 2002. The unfolded protein response in nutrient sensing and differentiation. Nat Rev Mol Cell Biol 3: 411-21.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 411-421
    • Kaufman, R.J.1    Scheuner, D.2    Schroder, M.3    Shen, X.4
  • 57
    • 84881055345 scopus 로고    scopus 로고
    • Glucose starvation induces cell death in K-ras-transformed cells by interfering with the hexosamine biosynthesis pathway and activating the unfolded protein response
    • Palorini R, Cammarata FP, Balestrieri C, Monestiroli A, et al. 2013. Glucose starvation induces cell death in K-ras-transformed cells by interfering with the hexosamine biosynthesis pathway and activating the unfolded protein response. Cell Death Dis 4: e732.
    • (2013) Cell Death Dis , vol.4 , pp. e732
    • Palorini, R.1    Cammarata, F.P.2    Balestrieri, C.3    Monestiroli, A.4
  • 59
    • 0035826689 scopus 로고    scopus 로고
    • Rck2, a member of the calmodulin-protein kinase family, links protein synthesis to high osmolarity MAP kinase signaling in budding yeast
    • Teige M, Scheikl E, Reiser V, Ruis H, et al. 2001. Rck2, a member of the calmodulin-protein kinase family, links protein synthesis to high osmolarity MAP kinase signaling in budding yeast. Proc Natl Acad Sci USA 98: 5625-30.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5625-5630
    • Teige, M.1    Scheikl, E.2    Reiser, V.3    Ruis, H.4
  • 60
    • 64749108996 scopus 로고    scopus 로고
    • Tumours with PI3K activation are resistant to dietary restriction
    • Kalaany NY, Sabatini DM. 2009. Tumours with PI3K activation are resistant to dietary restriction. Nature 458: 725-31.
    • (2009) Nature , vol.458 , pp. 725-731
    • Kalaany, N.Y.1    Sabatini, D.M.2
  • 61
    • 84895529793 scopus 로고    scopus 로고
    • Calorie restriction and cancer prevention: a mechanistic perspective
    • Hursting SD, Dunlap SM, Ford NA, Hursting MJ, et al. 2013. Calorie restriction and cancer prevention: a mechanistic perspective. Cancer Metab 1: 10.
    • (2013) Cancer Metab , vol.1 , pp. 10
    • Hursting, S.D.1    Dunlap, S.M.2    Ford, N.A.3    Hursting, M.J.4
  • 62
    • 4143146391 scopus 로고    scopus 로고
    • Antiangiogenic and proapoptotic effects of dietary restriction on experimental mouse and human brain tumors
    • Mukherjee P, Abate LE, Seyfried TN. 2004. Antiangiogenic and proapoptotic effects of dietary restriction on experimental mouse and human brain tumors. Clin Cancer Res 10: 5622-59.
    • (2004) Clin Cancer Res , vol.10 , pp. 5622-5659
    • Mukherjee, P.1    Abate, L.E.2    Seyfried, T.N.3
  • 63
    • 84857407549 scopus 로고    scopus 로고
    • Antiangiogenic agents increase breast cancer stem cells via the generation of tumor hypoxia
    • Conley SJ, Gheordunescu E, Kakarala P, Newman B, et al. 2012. Antiangiogenic agents increase breast cancer stem cells via the generation of tumor hypoxia. Proc Natl Acad Sci USA 109: 2784-9.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 2784-2789
    • Conley, S.J.1    Gheordunescu, E.2    Kakarala, P.3    Newman, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.