메뉴 건너뛰기




Volumn 20, Issue 3, 2003, Pages 265-273

Translational control and metastatic progression: Enhanced activity of the mRNA cap-binding protein eIF-4E selectively enhances translation of metastasis-related mRNAs

Author keywords

Cyclin D1; eIF 4E; eIF 4F; Growth factors; Invasion; Metastasis; MMP 9; Translation initiation; Tumor progression; VEGF

Indexed keywords

CYCLIN D1; INITIATION FACTOR 4E; MATRIX METALLOPROTEINASE; MESSENGER RNA; PROTEIN BCL 2; RNA BINDING PROTEIN; VASCULOTROPIN;

EID: 0037273324     PISSN: 02620898     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1022943419011     Document Type: Review
Times cited : (210)

References (110)
  • 1
  • 2
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA. The hallmarks of cancer. Cell 2000; 100(1): 57-70.
    • (2000) Cell , vol.100 , Issue.1 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 3
    • 0021905896 scopus 로고
    • Genetic and epigenetic aspects of tumor progression
    • Liteplo RG, Frost P, Kerbel RS. Genetic and epigenetic aspects of tumor progression. Basic Life Sci 1985; 33: 285-305.
    • (1985) Basic Life Sci , vol.33 , pp. 285-305
    • Liteplo, R.G.1    Frost, P.2    Kerbel, R.S.3
  • 4
    • 0023095251 scopus 로고
    • Tumor cell instability, diversification, and progression to the metastatic phenotype: From oncogene to oncofetal expression
    • Nicholson GL. Tumor cell instability, diversification, and progression to the metastatic phenotype: From oncogene to oncofetal expression. Cancer Res 1987; 47: 1473-87.
    • (1987) Cancer Res , vol.47 , pp. 1473-1487
    • Nicholson, G.L.1
  • 5
    • 0031029853 scopus 로고    scopus 로고
    • Expression genetics in cancer: Shifting the focus from DNA to RNA
    • Sager R. Expression genetics in cancer: Shifting the focus from DNA to RNA. Proc Natl Acad Sci USA 1997; 94: 952-5.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 952-955
    • Sager, R.1
  • 6
    • 0033854863 scopus 로고    scopus 로고
    • Translational control of malignancy: The mRNA cap-binding protein, eIF-4E, as a central regulator of tumor formation, growth, invasion and metastasis
    • Zimmer SG, DeBenedetti A, Graff JR. Translational control of malignancy: The mRNA cap-binding protein, eIF-4E, as a central regulator of tumor formation, growth, invasion and metastasis. Anticancer Res 2000; 20(3A): 1343-51.
    • (2000) Anticancer Res , vol.20 , Issue.3 A , pp. 1343-1351
    • Zimmer, S.G.1    DeBenedetti, A.2    Graff, J.R.3
  • 7
    • 0242547980 scopus 로고    scopus 로고
    • The emerging role for the mRNA cap-binding protein, eIF-4E, in metastatic progression
    • Welch DR (ed). Dordrecht, The Netherlands: Kluwer Academic Publishers
    • Zimmer SG, Graff JR. The emerging role for the mRNA cap-binding protein, eIF-4E, in metastatic progression. In Welch DR (ed): Cancer Metastasis-Related Genes. Dordrecht, The Netherlands: Kluwer Academic Publishers 2002; 247-65.
    • (2002) Cancer Metastasis-Related Genes , pp. 247-265
    • Zimmer, S.G.1    Graff, J.R.2
  • 8
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • Dever TE. Gene-specific regulation by general translation factors. Cell 2002; 108(4): 545-56.
    • (2002) Cell , vol.108 , Issue.4 , pp. 545-556
    • Dever, T.E.1
  • 9
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras AC, Raught B, Sonenberg N. Regulation of translation initiation by FRAP/mTOR. Genes Dev 2001; 15(7): 807-26.
    • (2001) Genes Dev , vol.15 , Issue.7 , pp. 807-826
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 10
    • 0037192868 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase pathway regulates the phosphorylation of 4E-BP1 at multiple sites
    • Herbert TP, Tee AR, Proud CG. The extracellular signal-regulated kinase pathway regulates the phosphorylation of 4E-BP1 at multiple sites. J Biol Chem 2002; 277(13): 11591-6.
    • (2002) J Biol Chem , vol.277 , Issue.13 , pp. 11591-11596
    • Herbert, T.P.1    Tee, A.R.2    Proud, C.G.3
  • 11
    • 0032520009 scopus 로고    scopus 로고
    • 4E-BP1, a repressor of the mRNA translation, is phosphorylated and inactivated by the Akt (PKB) signaling pathway
    • Gingras AC, Kennedy SG, O'Leary MA et al. 4E-BP1, a repressor of the mRNA translation, is phosphorylated and inactivated by the Akt (PKB) signaling pathway. Genes Dev 1998; 12: 502-13.
    • (1998) Genes Dev , vol.12 , pp. 502-513
    • Gingras, A.C.1    Kennedy, S.G.2    O'Leary, M.A.3
  • 12
    • 0033153166 scopus 로고    scopus 로고
    • Regulation of 4E-BP1 phosphorylation: A novel two-step mechanism
    • Gingras AC, Gygi SP, Raught B et al. Regulation of 4E-BP1 phosphorylation: A novel two-step mechanism. Genes Dev 1999; 13: 1422-37.
    • (1999) Genes Dev , vol.13 , pp. 1422-1437
    • Gingras, A.C.1    Gygi, S.P.2    Raught, B.3
  • 13
    • 0030881836 scopus 로고    scopus 로고
    • Phosphorylation of the translational repressor PHAS-1 by the mammalian target of rapamycin
    • Brunn GJ, Hudson CC, Sekulic A et al. Phosphorylation of the translational repressor PHAS-1 by the mammalian target of rapamycin. Science 1997; 277: 99-101.
    • (1997) Science , vol.277 , pp. 99-101
    • Brunn, G.J.1    Hudson, C.C.2    Sekulic, A.3
  • 14
    • 0030716488 scopus 로고    scopus 로고
    • Regulation of eIF-4E BP1 phosphorylation by mTOR
    • Hara K, Yonezawa K, Kozlowoski MT et al. Regulation of eIF-4E BP1 phosphorylation by mTOR. J Biol Chem 1997; 272; 26457-63.
    • (1997) J Biol Chem , vol.272 , pp. 26457-26463
    • Hara, K.1    Yonezawa, K.2    Kozlowoski, M.T.3
  • 15
    • 0028786952 scopus 로고
    • Repression of cap-dependent translation by 4E-binding protein 1: Competition with p220 for binding to eukaryotic initiation factor-4E
    • Haghighat A, Mader S, Pause A et al. Repression of cap-dependent translation by 4E-binding protein 1: Competition with p220 for binding to eukaryotic initiation factor-4E. EMBO J 1995; 14: 5701-9.
    • (1995) EMBO J , vol.14 , pp. 5701-5709
    • Haghighat, A.1    Mader, S.2    Pause, A.3
  • 16
    • 0027969060 scopus 로고
    • Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form
    • Minich WB, Balasta ML, Goss DJ et al. Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form. Proc Natl Acad Sci USA 1994; 91(16): 7668-72.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.16 , pp. 7668-7672
    • Minich, W.B.1    Balasta, M.L.2    Goss, D.J.3
  • 17
    • 0029094367 scopus 로고
    • Serine 209, not serine 53, is the major site of phosphorylation in initiation factor eIF-4E in serum-treated Chinese hamster ovary cells
    • Flynn A, Proud CG. Serine 209, not serine 53, is the major site of phosphorylation in initiation factor eIF-4E in serum-treated Chinese hamster ovary cells. J Biol Chem 1995; 270 (37): 21684-8.
    • (1995) J Biol Chem , vol.270 , Issue.37 , pp. 21684-21688
    • Flynn, A.1    Proud, C.G.2
  • 18
    • 0029030440 scopus 로고
    • Phosphorylation of eukaryotic protein synthesis initiation factor 4E at ser-209
    • Joshi B, Cai AL, Keiper BD et al. Phosphorylation of eukaryotic protein synthesis initiation factor 4E at ser-209. J Biol Chem 1995; 270: 14597-603.
    • (1995) J Biol Chem , vol.270 , pp. 14597-14603
    • Joshi, B.1    Cai, A.L.2    Keiper, B.D.3
  • 19
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
    • Waskiewicz AJ, Flynn A, Proud CG et al. Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J 1997; 16: 1909-20.
    • (1997) EMBO J , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3
  • 20
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF-4E
    • Pyronnet S, Imataka H, Gingras AC et al. Human eukaryotic initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF-4E. EMBO J 1999; 18: 270-9.
    • (1999) EMBO J , vol.18 , pp. 270-279
    • Pyronnet, S.1    Imataka, H.2    Gingras, A.C.3
  • 21
    • 0036178103 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic translation initiation factor 4E is critical for growth
    • Lachance PE, Miron M, Raught B et al. Phosphorylation of eukaryotic translation initiation factor 4E is critical for growth. Mol Cell Biol 2002; 22(6): 1656-63.
    • (2002) Mol Cell Biol , vol.22 , Issue.6 , pp. 1656-1663
    • Lachance, P.E.1    Miron, M.2    Raught, B.3
  • 22
    • 0027421241 scopus 로고
    • Mechanism of action and regulation of protein synthesis initiation factor 4E: Effects on mRNA discrimination, cellular growth rate, and oncogenesis
    • Rhoads RE, Joshi-Barve S, Rinker-Schaeffer C. Mechanism of action and regulation of protein synthesis initiation factor 4E: Effects on mRNA discrimination, cellular growth rate, and oncogenesis. Prog Nucleic Acid Res Mol Biol 1993; 46: 183-219.
    • (1993) Prog Nucleic Acid Res Mol Biol , vol.46 , pp. 183-219
    • Rhoads, R.E.1    Joshi-Barve, S.2    Rinker-Schaeffer, C.3
  • 23
    • 0001270324 scopus 로고
    • The 5′ untranslated sequence of the c-sis/PDGF 2 transcript is a potent translational inhibitor
    • Rao CD, Pech M, Robbins KC et al. The 5′ untranslated sequence of the c-sis/PDGF 2 transcript is a potent translational inhibitor. Mol Cell Biol 1988; 8: 284-92.
    • (1988) Mol Cell Biol , vol.8 , pp. 284-292
    • Rao, C.D.1    Pech, M.2    Robbins, K.C.3
  • 24
    • 0027674241 scopus 로고
    • Regulation of platelet-derived growth factor A messenger RNA translation in differentiating F9 teratocarcinoma cells
    • Wang C, Stiles CD. Regulation of platelet-derived growth factor A messenger RNA translation in differentiating F9 teratocarcinoma cells. Cell Growth Diff 1993; 4: 871-7.
    • (1993) Cell Growth Diff , vol.4 , pp. 871-877
    • Wang, C.1    Stiles, C.D.2
  • 25
    • 0008566513 scopus 로고
    • High molecular mass forms of basic fibroblast growth factor are initiated by alternative CUG codons
    • Prats H, Kaghad M, Prats AP et al. High molecular mass forms of basic fibroblast growth factor are initiated by alternative CUG codons. Proc Natl Acad Sci USA 1989; 86: 1836-40.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1836-1840
    • Prats, H.1    Kaghad, M.2    Prats, A.P.3
  • 26
    • 0029617994 scopus 로고
    • Translational enhancement of FGF-2 by eIF-4 factors, and alternate utilization of CUG and AUG codons for translation initiation
    • Kevil C, Carter P, Hu B et al. Translational enhancement of FGF-2 by eIF-4 factors, and alternate utilization of CUG and AUG codons for translation initiation. Oncogene 1995; 11: 2339-48.
    • (1995) Oncogene , vol.11 , pp. 2339-2348
    • Kevil, C.1    Carter, P.2    Hu, B.3
  • 27
    • 0025917034 scopus 로고
    • Molecular cloning and structure of the human transforming growth factor-beta 2 gene promoter
    • Noma T, Glick AB, Geiser AG et al. Molecular cloning and structure of the human transforming growth factor-beta 2 gene promoter. Growth Factors 1991; 4: 247-55.
    • (1991) Growth Factors , vol.4 , pp. 247-255
    • Noma, T.1    Glick, A.B.2    Geiser, A.G.3
  • 28
    • 0025827065 scopus 로고
    • Inhibition of translation of transforming growth factor-beta 3 mRNA by its 5′ untranslated region
    • Arrick BA, Lee AL, Grendell RL et al. Inhibition of translation of transforming growth factor-beta 3 mRNA by its 5′ untranslated region. Mol Cell Biol 1991; 11: 4306-13.
    • (1991) Mol Cell Biol , vol.11 , pp. 4306-4313
    • Arrick, B.A.1    Lee, A.L.2    Grendell, R.L.3
  • 29
    • 0025007578 scopus 로고
    • Translational discrimination of mRNAs coding for human insulin-like growth factor II
    • Nilsson FC, Gammeltoft S, Christiansen J. Translational discrimination of mRNAs coding for human insulin-like growth factor II. J Biol Chem 1990; 265: 13431-4.
    • (1990) J Biol Chem , vol.265 , pp. 13431-13434
    • Nilsson, F.C.1    Gammeltoft, S.2    Christiansen, J.3
  • 30
    • 0029967638 scopus 로고    scopus 로고
    • Translational regulation for vascular permeability factor by eukaryotic initiation factor 4E: Implications for tumor angiogenesis
    • Kevil C, DeBenedetti A, Payne KD et al. Translational regulation for vascular permeability factor by eukaryotic initiation factor 4E: Implications for tumor angiogenesis. Int J Cancer 1996; 65: 785-90.
    • (1996) Int J Cancer , vol.65 , pp. 785-790
    • Kevil, C.1    DeBenedetti, A.2    Payne, K.D.3
  • 31
    • 0004961206 scopus 로고
    • Activation of the c-myc gene by translocation: A model for translational control
    • Saito H, Hayday AC, Wiman K et al. Activation of the c-myc gene by translocation: A model for translational control. Proc Natl Acad Sci USA 1983; 80: 7476-80.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 7476-7480
    • Saito, H.1    Hayday, A.C.2    Wiman, K.3
  • 32
    • 1542478512 scopus 로고
    • Differential efficiencies of in vitro translation of mouse c-myc transcripts differing in the 5′ untranslated region
    • Darveau A, Pelletier J, Sonenberg N. Differential efficiencies of in vitro translation of mouse c-myc transcripts differing in the 5′ untranslated region. Proc Natl Acad Sci USA 1985; 82: 2315-9.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 2315-2319
    • Darveau, A.1    Pelletier, J.2    Sonenberg, N.3
  • 33
    • 0028253641 scopus 로고
    • CHO cells transformed by the translation factor eIF-4E display increased c-myc expression, but require overexpression of Max for tumorigenicity
    • DeBenedetti A, Joshi B, Graff JR et al. CHO cells transformed by the translation factor eIF-4E display increased c-myc expression, but require overexpression of Max for tumorigenicity. Mol Cell Diff 1994; 2: 347-71.
    • (1994) Mol Cell Diff , vol.2 , pp. 347-371
    • DeBenedetti, A.1    Joshi, B.2    Graff, J.R.3
  • 34
    • 0024437890 scopus 로고
    • The product of a novel growth factor activated gene, fosB, interacts with Jun proteins enhancing their DNA binding activity
    • Zerial M, Toschi L, Ryseek RP et al. The product of a novel growth factor activated gene, fosB, interacts with Jun proteins enhancing their DNA binding activity. EMBO J 1989; 8: 805-13.
    • (1989) EMBO J , vol.8 , pp. 805-813
    • Zerial, M.1    Toschi, L.2    Ryseek, R.P.3
  • 35
    • 0030805545 scopus 로고    scopus 로고
    • The conserved 5′-untranslated leader of Spi-1 (PU.1) mRNA is highly structured and potently inhibits translation in vitro but not in vivo
    • Hensold JO, Stratton CA, Barth C. The conserved 5′-untranslated leader of Spi-1 (PU.1) mRNA is highly structured and potently inhibits translation in vitro but not in vivo. Nucleic Acids Res 1997; 25: 2869-76.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2869-2876
    • Hensold, J.O.1    Stratton, C.A.2    Barth, C.3
  • 36
    • 0029740136 scopus 로고    scopus 로고
    • Expression of a translationally regulated, dominant-negative CCAAT/enhancer-binding protein beta isoform and up-regulation of the eukaryotic translation initiation factor 2alpha are correlated with neoplastic transformation of mammary epithelial cells
    • Raught B, Gingras AC, James A et al. Expression of a translationally regulated, dominant-negative CCAAT/enhancer-binding protein beta isoform and up-regulation of the eukaryotic translation initiation factor 2alpha are correlated with neoplastic transformation of mammary epithelial cells. Cancer Res 1996; 56: 4382-6.
    • (1996) Cancer Res , vol.56 , pp. 4382-4386
    • Raught, B.1    Gingras, A.C.2    James, A.3
  • 37
    • 0033869876 scopus 로고    scopus 로고
    • Translational control of C/EBPalpha and C/EBPbeta isoform expression
    • Calkhoven CF, Muller C, Leutz A. Translational control of C/EBPalpha and C/EBPbeta isoform expression. Genes Dev 2000; 14: 1920-32.
    • (2000) Genes Dev , vol.14 , pp. 1920-1932
    • Calkhoven, C.F.1    Muller, C.2    Leutz, A.3
  • 38
    • 0027956208 scopus 로고
    • Enhanced translation: A novel mechanism of mdm2 oncogene overexpression identified in human tumor cells
    • Landers JE, Haines DS, Strauss JF 3rd et al. Enhanced translation: A novel mechanism of mdm2 oncogene overexpression identified in human tumor cells. Oncogene 1994; 9: 2745-50.
    • (1994) Oncogene , vol.9 , pp. 2745-2750
    • Landers, J.E.1    Haines, D.S.2    Strauss J.F. III3
  • 39
    • 0030795068 scopus 로고    scopus 로고
    • Translational enhancement of mdm2 oncogene expression in human tumor cells containing a stabilized wild-type p53 protein
    • Landers JE, Cassel SL, George DL. Translational enhancement of mdm2 oncogene expression in human tumor cells containing a stabilized wild-type p53 protein. Cancer Res 1997; 57: 3562-8.
    • (1997) Cancer Res , vol.57 , pp. 3562-3568
    • Landers, J.E.1    Cassel, S.L.2    George, D.L.3
  • 40
    • 0032568334 scopus 로고    scopus 로고
    • Overexpression of MDM2, due to enhanced translation, results in inactivation of wild-type p53 in Burkitt's lymphoma cells
    • Capoulade C, Bressac-de Paillerets B, Lefrere I et al. Overexpression of MDM2, due to enhanced translation, results in inactivation of wild-type p53 in Burkitt's lymphoma cells. Oncogene 1998; 16: 1603-10.
    • (1998) Oncogene , vol.16 , pp. 1603-1610
    • Capoulade, C.1    Bressac-De Paillerets, B.2    Lefrere, I.3
  • 41
    • 0033533737 scopus 로고    scopus 로고
    • Role of two upstream open reading frames in the translational control of oncogene mdm2
    • Brown CY, Mize GJ, Pineda M et al. Role of two upstream open reading frames in the translational control of oncogene mdm2. Oncogene 1999; 18: 5631-7.
    • (1999) Oncogene , vol.18 , pp. 5631-5637
    • Brown, C.Y.1    Mize, G.J.2    Pineda, M.3
  • 42
    • 0027365517 scopus 로고
    • Elevated levels of cyclin D1 protein in response to increased expression of eukaryotic initiation factor eIF4E
    • Rosenwald IB, Karatzas A, Sonenberg N et al. Elevated levels of cyclin D1 protein in response to increased expression of eukaryotic initiation factor eIF4E. Mol Cell Biol 1993; 13: 7358-63.
    • (1993) Mol Cell Biol , vol.13 , pp. 7358-7363
    • Rosenwald, I.B.1    Karatzas, A.2    Sonenberg, N.3
  • 43
    • 0029166967 scopus 로고
    • Eukaryotic translation initiation factor 4E regulates expression of cyclin D at transcriptional and posttranscriptional levels
    • Rosenwald EB, Kaspar R, Rosseau D et al. Eukaryotic translation initiation factor 4E regulates expression of cyclin D at transcriptional and posttranscriptional levels. J Biol Chem 1995; 270: 21176-80.
    • (1995) J Biol Chem , vol.270 , pp. 21176-21180
    • Rosenwald, E.B.1    Kaspar, R.2    Rosseau, D.3
  • 44
    • 0030041884 scopus 로고    scopus 로고
    • Translation initiation of omithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 4E
    • Rousseau D, Kaspar R, Rosenwald I et al. Translation initiation of omithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 4E. Proc Natl Acad Sci USA 1996; 93: 1065-70.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1065-1070
    • Rousseau, D.1    Kaspar, R.2    Rosenwald, I.3
  • 45
    • 0029666094 scopus 로고    scopus 로고
    • kip1 synthesis by platelet-derived growth factor in BALB/c 3T3 cells
    • kip1 synthesis by platelet-derived growth factor in BALB/c 3T3 cells. Mol Cell Biol 1996; 16: 4327-36.
    • (1996) Mol Cell Biol , vol.16 , pp. 4327-4336
    • Agrawal, D.1    Hauser, P.2    McPherson, F.3
  • 46
    • 0029670477 scopus 로고    scopus 로고
    • Translational control of p27kip1 accumulation during the cell cycle
    • Hengst L, Reed SI. Translational control of p27kip1 accumulation during the cell cycle. Science 1996; 271: 1861-4.
    • (1996) Science , vol.271 , pp. 1861-1864
    • Hengst, L.1    Reed, S.I.2
  • 47
    • 0029872060 scopus 로고    scopus 로고
    • The 5′ untranslated region of the N-methyl-D-aspartate receptor NR2A subunit controls efficiency of translation
    • Wood MW, Van Dongen HM, Van Dongen AM. The 5′ untranslated region of the N-methyl-D-aspartate receptor NR2A subunit controls efficiency of translation. J Biol Chem 1996; 271: 8115-20.
    • (1996) J Biol Chem , vol.271 , pp. 8115-8120
    • Wood, M.W.1    Van Dongen, H.M.2    Van Dongen, A.M.3
  • 48
    • 0033045101 scopus 로고    scopus 로고
    • Cell type-dependent and -independent control of HER-2/neu translation
    • Child SJ, Miller MK, Geballe AP. Cell type-dependent and -independent control of HER-2/neu translation. Int J Biochem Cell Biol 1999; 31: 201-13.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 201-213
    • Child, S.J.1    Miller, M.K.2    Geballe, A.P.3
  • 49
    • 0025302145 scopus 로고
    • Dissociation between interleukin-1 beta mRNA and protein synthesis in human peripheral blood mononuclear cells
    • Schindler R, Clark BD, Dinarello CA. Dissociation between interleukin-1 beta mRNA and protein synthesis in human peripheral blood mononuclear cells. J Biol Chem 1990; 265: 10232-7.
    • (1990) J Biol Chem , vol.265 , pp. 10232-10237
    • Schindler, R.1    Clark, B.D.2    Dinarello, C.A.3
  • 50
    • 0030008255 scopus 로고    scopus 로고
    • Interleukin (IL) 15/IL-T production by the adult T-cell leukemia cell line HuT-102 is associated with a human T-cell lymphotrophic virus type IR region/IL-15 fusion message that lacks many upstream AUGs that normally attenuate IL-15 mRNA translation
    • Bamford RN, Battiata AP, Burton JD et al. Interleukin (IL) 15/IL-T production by the adult T-cell leukemia cell line HuT-102 is associated with a human T-cell lymphotrophic virus type IR region/IL-15 fusion message that lacks many upstream AUGs that normally attenuate IL-15 mRNA translation. Proc Natl Acad Sci USA 1996; 93: 2897-902.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2897-2902
    • Bamford, R.N.1    Battiata, A.P.2    Burton, J.D.3
  • 51
    • 0028271504 scopus 로고
    • Overproduction of ornithine decarboxylase caused by relief of translational repression is associated with neoplastic transformation
    • Shantz LM, Pegg AE. Overproduction of ornithine decarboxylase caused by relief of translational repression is associated with neoplastic transformation. Cancer Res 1994; 54: 2313-6.
    • (1994) Cancer Res , vol.54 , pp. 2313-2316
    • Shantz, L.M.1    Pegg, A.E.2
  • 52
    • 0030011284 scopus 로고    scopus 로고
    • Regulation of ornithine decarboxylase in a transformed cell line that overexpresses translation initiation factor eIF-4E
    • Shantz LM, Hu RH, Pegg AE. Regulation of ornithine decarboxylase in a transformed cell line that overexpresses translation initiation factor eIF-4E. Cancer Res 1996; 56: 3265-9.
    • (1996) Cancer Res , vol.56 , pp. 3265-3269
    • Shantz, L.M.1    Hu, R.H.2    Pegg, A.E.3
  • 53
    • 0031558804 scopus 로고    scopus 로고
    • Translation of ODC mRNA and polyamine transport are suppressed in ras-transformed CREF cells by depleting translation initiation factor 4E
    • Graff JR, DeBenedetti A, Olson JW et al. Translation of ODC mRNA and polyamine transport are suppressed in ras-transformed CREF cells by depleting translation initiation factor 4E. BBRC 1997; 240: 15-20.
    • (1997) BBRC , vol.240 , pp. 15-20
    • Graff, J.R.1    DeBenedetti, A.2    Olson, J.W.3
  • 54
    • 0025834130 scopus 로고
    • Insulin induction of ornithine decarboxylase. Importance of mRNA secondary structure and phosphorylation of eukaryotic initiation factors eIF-4B and cIF4E
    • Manzella JM, Rychlik W, Rhoads RE et al. Insulin induction of ornithine decarboxylase. Importance of mRNA secondary structure and phosphorylation of eukaryotic initiation factors eIF-4B and cIF4E. J Biol Chem 1991; 266: 2383-9.
    • (1991) J Biol Chem , vol.266 , pp. 2383-2389
    • Manzella, J.M.1    Rychlik, W.2    Rhoads, R.E.3
  • 55
    • 0025277641 scopus 로고
    • The 5′- and 3′-untranslated regions of ornithine decarboxylase mRNA affect the translational efficiency
    • Grens A, Scheffler IE. The 5′- and 3′-untranslated regions of ornithine decarboxylase mRNA affect the translational efficiency. J Biol Chem 1990; 265: 11810-6.
    • (1990) J Biol Chem , vol.265 , pp. 11810-11816
    • Grens, A.1    Scheffler, I.E.2
  • 56
    • 0026012413 scopus 로고
    • Translational control of ornithine aminotransferase. Modulation by initiation factor eIF4E
    • Fagan RJ, Lazaris-Karatzas A, Sonenberg N et al. Translational control of ornithine aminotransferase. Modulation by initiation factor eIF4E. J Biol Chem 1991; 266: 16518-23.
    • (1991) J Biol Chem , vol.266 , pp. 16518-16523
    • Fagan, R.J.1    Lazaris-Karatzas, A.2    Sonenberg, N.3
  • 57
    • 0028071521 scopus 로고
    • Role of the 5′-untranslated region of the mRNA in the synthesis of S-adenosylmethionine decarboxylase and its regulation by spermine
    • Shantz LM, Viswanath R, Pegg AE. Role of the 5′-untranslated region of the mRNA in the synthesis of S-adenosylmethionine decarboxylase and its regulation by spermine. Biochem J 1994; 302: 765-72.
    • (1994) Biochem J , vol.302 , pp. 765-772
    • Shantz, L.M.1    Viswanath, R.2    Pegg, A.E.3
  • 58
    • 0023854838 scopus 로고
    • Translational activation of the lck proto-oncogene
    • Marth JD, Overell RW, Meier KE et al. Translational activation of the lck proto-oncogene. Nature 1988; 332: 171-3.
    • (1988) Nature , vol.332 , pp. 171-173
    • Marth, J.D.1    Overell, R.W.2    Meier, K.E.3
  • 59
    • 0031442452 scopus 로고    scopus 로고
    • Pim-1 protein expression is regulated by its 5′-untranslated region and translation initiation factor eIF4E
    • Hoover DS, Wingett DG, Zhang J et al. Pim-1 protein expression is regulated by its 5′-untranslated region and translation initiation factor eIF4E. Cell Growth Diff 1997; 8: 1371-80.
    • (1997) Cell Growth Diff , vol.8 , pp. 1371-1380
    • Hoover, D.S.1    Wingett, D.G.2    Zhang, J.3
  • 60
    • 0033544957 scopus 로고    scopus 로고
    • Translational regulation of ribonucleotide reductase by eukaryotic initiation factor 4E links protein synthesis to the control of DNA replication
    • Abid MR, Li Y, Anthony C et al. Translational regulation of ribonucleotide reductase by eukaryotic initiation factor 4E links protein synthesis to the control of DNA replication. J Biol Chem 1999; 274: 35991-8.
    • (1999) J Biol Chem , vol.274 , pp. 35991-35998
    • Abid, M.R.1    Li, Y.2    Anthony, C.3
  • 61
    • 0028652397 scopus 로고
    • Translational regulation of the mammalian growth-related protein P23: Involvement of eIF-4E
    • Bommer UA, Lazaris-Karatzas A, De Benedetti A et al. Translational regulation of the mammalian growth-related protein P23: Involvement of eIF-4E. Cell Mol Biol Res 1994; 40: 633-41.
    • (1994) Cell Mol Biol Res , vol.40 , pp. 633-641
    • Bommer, U.A.1    Lazaris-Karatzas, A.2    De Benedetti, A.3
  • 62
    • 0037086074 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase-9 (MMP-9) by translational efficiency in murine prostate carcinoma cells
    • Jiang Y, Muschel RJ. Regulation of matrix metalloproteinase-9 (MMP-9) by translational efficiency in murine prostate carcinoma cells. Cancer Res 2002; 62: 1910-4.
    • (2002) Cancer Res , vol.62 , pp. 1910-1914
    • Jiang, Y.1    Muschel, R.J.2
  • 63
    • 0037023780 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 induces translational regulation of Bcl-XL and Bcl-2 via a MEK-dependent pathway: Correlation with resistance to etoposide-induced apoptosis
    • Pardo OE, Arcaro A, Salerno G et al. Fibroblast growth factor-2 induces translational regulation of Bcl-XL and Bcl-2 via a MEK-dependent pathway: Correlation with resistance to etoposide-induced apoptosis. J Biol Chem 2002; 277: 12040-6.
    • (2002) J Biol Chem , vol.277 , pp. 12040-12046
    • Pardo, O.E.1    Arcaro, A.2    Salerno, G.3
  • 64
    • 0037031879 scopus 로고    scopus 로고
    • Translational regulation of the JunD messenger RNA
    • Short JD, Pfarr CM. Translational regulation of the JunD messenger RNA. J Biol Chem 2002; 277: 32697-705.
    • (2002) J Biol Chem , vol.277 , pp. 32697-32705
    • Short, J.D.1    Pfarr, C.M.2
  • 65
    • 0035825616 scopus 로고    scopus 로고
    • A translationally regulated Tousled kinase phosphorylates histone H3 and confers radioresistance when overexpressed
    • Li Y, DeFatta R, Anthony C et al. A translationally regulated Tousled kinase phosphorylates histone H3 and confers radioresistance when overexpressed. Oncogene 2001; 20: 726-38.
    • (2001) Oncogene , vol.20 , pp. 726-738
    • Li, Y.1    DeFatta, R.2    Anthony, C.3
  • 66
    • 0035908493 scopus 로고    scopus 로고
    • Blocking oncogenic Ras signaling for cancer therapy
    • Adjei AA. Blocking oncogenic Ras signaling for cancer therapy. J Natl Cancer Inst 2001; 93: 1062-74.
    • (2001) J Natl Cancer Inst , vol.93 , pp. 1062-1074
    • Adjei, A.A.1
  • 67
    • 0025309331 scopus 로고
    • Role of the Ha-ras (RasH) oncogene in mediating progression of the tumor cell phenotype
    • Review
    • Boylan JF, Jackson J, Steiner MR et al. Role of the Ha-ras (RasH) oncogene in mediating progression of the tumor cell phenotype. Anticancer Res 1990; 10: 717-24 (Review).
    • (1990) Anticancer Res , vol.10 , pp. 717-724
    • Boylan, J.F.1    Jackson, J.2    Steiner, M.R.3
  • 68
    • 0033957661 scopus 로고    scopus 로고
    • The PTEN tumor suppressor protein: An antagonist of phosphoinositide 3-kinase signaling
    • Vazquez F, Sellers WR. The PTEN tumor suppressor protein: An antagonist of phosphoinositide 3-kinase signaling. Biochim Biophys Acta 2000; 1470: M21-35.
    • (2000) Biochim Biophys Acta , vol.1470
    • Vazquez, F.1    Sellers, W.R.2
  • 69
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-Kinase AKT pathway in human cancer
    • Vivanco I, Sawyers CL. The phosphatidylinositol 3-Kinase AKT pathway in human cancer. Nat Rev Cancer 2002; 2: 489-501.
    • (2002) Nat Rev Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 70
    • 0036479998 scopus 로고    scopus 로고
    • Emerging targets in the AKT pathway for treatment of androgen-independent prostatic adenocarcinoma
    • Graff JR. Emerging targets in the AKT pathway for treatment of androgen-independent prostatic adenocarcinoma. Exp Opin Ther Targets 2002; 6: 103-13.
    • (2002) Exp Opin Ther Targets , vol.6 , pp. 103-113
    • Graff, J.R.1
  • 71
    • 0035694808 scopus 로고    scopus 로고
    • Resistance to rapamycin: A novel anticancer drug
    • Huang S, Houghton PJ. Resistance to rapamycin: A novel anticancer drug. Cancer Metastasis Rev 2001: 20: 69-78.
    • (2001) Cancer Metastasis Rev , vol.20 , pp. 69-78
    • Huang, S.1    Houghton, P.J.2
  • 72
    • 0037134480 scopus 로고    scopus 로고
    • 4E-binding proteins, the suppressors of eukaryotic initiation factor 4E, are down-regulated in cells with acquired or intrinsic resistance to rapamycin
    • Dilling MB, Germain GS, Dudkin L et al. 4E-binding proteins, the suppressors of eukaryotic initiation factor 4E, are down-regulated in cells with acquired or intrinsic resistance to rapamycin. J Biol Chem 2002; 277: 13907-17.
    • (2002) J Biol Chem , vol.277 , pp. 13907-13917
    • Dilling, M.B.1    Germain, G.S.2    Dudkin, L.3
  • 74
    • 0028918259 scopus 로고
    • The protooncogene/translation factor eIF-4E - A survey of its expression in breast carcinomas
    • Kerekatte V, Smiley K, Hu B et al. The protooncogene/translation factor eIF-4E - a survey of its expression in breast carcinomas. Int J Cancer 1995; 65: 27-31.
    • (1995) Int J Cancer , vol.65 , pp. 27-31
    • Kerekatte, V.1    Smiley, K.2    Hu, B.3
  • 75
    • 0030867624 scopus 로고    scopus 로고
    • Elevated expression of eIF-4E and FGF-2 isoforms during vascularization of breast carcinomas
    • Nathan CA, Carter P, Liu L et al. Elevated expression of eIF-4E and FGF-2 isoforms during vascularization of breast carcinomas. Oncogene 1997; 15: 1087-95.
    • (1997) Oncogene , vol.15 , pp. 1087-1095
    • Nathan, C.A.1    Carter, P.2    Liu, L.3
  • 76
    • 0030940199 scopus 로고    scopus 로고
    • Overexpression of eukaryotic initiation factor 4E (eIF4E) in breast carcinoma
    • Li BDL, Liu L, Dawson M et al. Overexpression of eukaryotic initiation factor 4E (eIF4E) in breast carcinoma. Cancer 1997; 79: 2385-9.
    • (1997) Cancer , vol.79 , pp. 2385-2389
    • Li, B.D.L.1    Liu, L.2    Dawson, M.3
  • 77
    • 0031795848 scopus 로고    scopus 로고
    • Clinical outcome in stage 1 to 3 breast carcinomas and eIF4E overexpression
    • Li BDL, McDonald J, Nassar R et al. Clinical outcome in stage 1 to 3 breast carcinomas and eIF4E overexpression. Ann Surg Soc 1998; 227: 756-62.
    • (1998) Ann Surg Soc , vol.227 , pp. 756-762
    • Li, B.D.L.1    McDonald, J.2    Nassar, R.3
  • 78
    • 0033521868 scopus 로고    scopus 로고
    • Elevated expression of eIF-4E in confined early breast cancer lesions: Possible role of hypoxia
    • DeFatta RJ, Turbat-Herrera EA, Li BD et al. Elevated expression of eIF-4E in confined early breast cancer lesions: Possible role of hypoxia. Int J Cancer 1999; 80: 516-22.
    • (1999) Int J Cancer , vol.80 , pp. 516-522
    • DeFatta, R.J.1    Turbat-Herrera, E.A.2    Li, B.D.3
  • 79
    • 0029993470 scopus 로고    scopus 로고
    • Overexpression of the protooncogene/translation factor 4E in breast-carcinoma cell lines
    • Anthony B, Carter P, DeBenedetti A. Overexpression of the protooncogene/translation factor 4E in breast-carcinoma cell lines. Int J Cancer 1996; 65: 858-63.
    • (1996) Int J Cancer , vol.65 , pp. 858-863
    • Anthony, B.1    Carter, P.2    DeBenedetti, A.3
  • 80
    • 0034660176 scopus 로고    scopus 로고
    • Progression of eIF4E gene amplification and overexpression in benign and malignant tumors of the head and neck
    • Haydon MS, Googe JD, Sorrells DS et al. Progression of eIF4E gene amplification and overexpression in benign and malignant tumors of the head and neck. Cancer 2000; 88: 2803-10.
    • (2000) Cancer , vol.88 , pp. 2803-2810
    • Haydon, M.S.1    Googe, J.D.2    Sorrells, D.S.3
  • 81
    • 0034235630 scopus 로고    scopus 로고
    • Correlation of p53 and the proto-oncogene eIF4E in larynx cancers: Prognostic implications
    • Nathan CA, Sanders K, Abreo FW et al. Correlation of p53 and the proto-oncogene eIF4E in larynx cancers: Prognostic implications. Cancer Res, 2000; 60: 3599-604.
    • (2000) Cancer Res , vol.60 , pp. 3599-3604
    • Nathan, C.A.1    Sanders, K.2    Abreo, F.W.3
  • 82
    • 0030808698 scopus 로고    scopus 로고
    • Detection of the proto-oncogene eIF4E in surgical margins may predict recurrence in head and neck cancer
    • Nathan CA, Liu L, Li B et al. Detection of the proto-oncogene eIF4E in surgical margins may predict recurrence in head and neck cancer. Oncogene 1997; 15: 579-84.
    • (1997) Oncogene , vol.15 , pp. 579-584
    • Nathan, C.A.1    Liu, L.2    Li, B.3
  • 83
    • 0033016896 scopus 로고    scopus 로고
    • Detection of the proto-oncogene eIF4E in larynx and hypopharynx cancers
    • Franklin S, Pho T, Abreo FW et al. Detection of the proto-oncogene eIF4E in larynx and hypopharynx cancers. Arch Otolaryngol Head Neck Surg 1999; 125: 177-82.
    • (1999) Arch Otolaryngol Head Neck Surg , vol.125 , pp. 177-182
    • Franklin, S.1    Pho, T.2    Abreo, F.W.3
  • 84
    • 13044311377 scopus 로고    scopus 로고
    • Progressive amplification and overexpression of the eukaryotic initiation factor 4E gene in different zones of head and neck cancers
    • Sorrells DL Jr, Ghali GE, DeBenedetti A et al. Progressive amplification and overexpression of the eukaryotic initiation factor 4E gene in different zones of head and neck cancers. J Oral Maxillofac Surg 1999; 57: 294-99.
    • (1999) J Oral Maxillofac Surg , vol.57 , pp. 294-299
    • Sorrells D.L., Jr.1    Ghali, G.E.2    DeBenedetti, A.3
  • 85
    • 0033031044 scopus 로고    scopus 로고
    • Expression of the eukaryotic translation initiation factors 4E and 2alpha in non-Hodgkin's lymphomas
    • Wang S, Rosenwald IB, Hutzler MJ et al. Expression of the eukaryotic translation initiation factors 4E and 2alpha in non-Hodgkin's lymphomas. Am J Pathol 1999; 155: 247-55.
    • (1999) Am J Pathol , vol.155 , pp. 247-255
    • Wang, S.1    Rosenwald, I.B.2    Hutzler, M.J.3
  • 86
    • 0342858949 scopus 로고    scopus 로고
    • 4E binding protein 1 expression is inversely correlated to the progression of gastrointestinal cancers
    • Martin ME, Perez MI, Redondo C et al. 4E binding protein 1 expression is inversely correlated to the progression of gastrointestinal cancers. Int J Biochem Cell Biol 2000; 32: 633-42.
    • (2000) Int J Biochem Cell Biol , vol.32 , pp. 633-642
    • Martin, M.E.1    Perez, M.I.2    Redondo, C.3
  • 87
    • 0033988498 scopus 로고    scopus 로고
    • Eukaryotic initiation factor-4E in superficial and muscle invasive bladder cancer and its correlation with vascular endothelial growth factor expression and tumor progression
    • Crew JP, Fuggle S, Bicknell R et al. Eukaryotic initiation factor-4E in superficial and muscle invasive bladder cancer and its correlation with vascular endothelial growth factor expression and tumor progression. Br J Cancer 2000; 82: 161-6.
    • (2000) Br J Cancer , vol.82 , pp. 161-166
    • Crew, J.P.1    Fuggle, S.2    Bicknell, R.3
  • 88
    • 0039656540 scopus 로고    scopus 로고
    • Upregulation of protein synthesis initiation factor eIF-4E is an early event during colon carcinogenesis
    • Rosenwald IB, Chen JJ, Wang S et al. Upregulation of protein synthesis initiation factor eIF-4E is an early event during colon carcinogenesis. Oncogene 1999; 18: 2507-17.
    • (1999) Oncogene , vol.18 , pp. 2507-2517
    • Rosenwald, I.B.1    Chen, J.J.2    Wang, S.3
  • 89
    • 85047677338 scopus 로고    scopus 로고
    • Spontaneous progression of a stage IV-S human neuroblastoma cell line involves the increased expression of the protooncogenes ras and eukaryotic initiation factor 4E
    • Fowler CL, Zimmer CC, Zimmer SG. Spontaneous progression of a stage IV-S human neuroblastoma cell line involves the increased expression of the protooncogenes ras and eukaryotic initiation factor 4E. Pediatr Pathol Mol Med 2000; 19: 433-47.
    • (2000) Pediatr Pathol Mol Med , vol.19 , pp. 433-447
    • Fowler, C.L.1    Zimmer, C.C.2    Zimmer, S.G.3
  • 90
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA cap
    • Lazaris-Karatzas A, Montine KS, Sonenberg N. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA cap. Nature 1990; 345: 544-7.
    • (1990) Nature , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 91
    • 0026583874 scopus 로고
    • The mRNA 5′ cap-binding protein, eIF-4E, cooperates with v-myc or E1A in the transforming of primary rodent fibroblasts
    • Lazaris-Karatzas A, Sonenberg N. The mRNA 5′ cap-binding protein, eIF-4E, cooperates with v-myc or E1A in the transforming of primary rodent fibroblasts. Mol Cell Biol 1992; 12: 1234-8.
    • (1992) Mol Cell Biol , vol.12 , pp. 1234-1238
    • Lazaris-Karatzas, A.1    Sonenberg, N.2
  • 92
    • 0026784679 scopus 로고
    • Ras mediates translation initiation factor 4E-induced malignant transformation
    • Lazaris-Karatzas A, Smith MR, Frederickson RM et al. Ras mediates translation initiation factor 4E-induced malignant transformation. Genes Dev 1992; 6: 1631-42.
    • (1992) Genes Dev , vol.6 , pp. 1631-1642
    • Lazaris-Karatzas, A.1    Smith, M.R.2    Frederickson, R.M.3
  • 93
    • 0027932788 scopus 로고
    • Induction of mesoderm in Xenopus laevis embryos by translation initiation factor 4E
    • Klein PS, Melton DA. Induction of mesoderm in Xenopus laevis embryos by translation initiation factor 4E. Science 1994; 265: 803-5.
    • (1994) Science , vol.265 , pp. 803-805
    • Klein, P.S.1    Melton, D.A.2
  • 94
    • 0034637435 scopus 로고    scopus 로고
    • Translational control of the antiapoptotic function of Ras
    • Polunovsky VA, Gingras AC, Sonenberg N et al. Translational control of the antiapoptotic function of Ras. J Biol Chem 2000; 275: 24776-80.
    • (2000) J Biol Chem , vol.275 , pp. 24776-24780
    • Polunovsky, V.A.1    Gingras, A.C.2    Sonenberg, N.3
  • 95
    • 0034624746 scopus 로고    scopus 로고
    • Inhibition of Myc-dependent apoptosis by eukaryotic translation initiation factor 4E requires cyclin D1
    • Tan A, Bitterman P, Sonenberg N et al. Inhibition of Myc-dependent apoptosis by eukaryotic translation initiation factor 4E requires cyclin D1. Oncogene 2000; 19: 1437-47.
    • (2000) Oncogene , vol.19 , pp. 1437-1447
    • Tan, A.1    Bitterman, P.2    Sonenberg, N.3
  • 96
    • 0029827631 scopus 로고    scopus 로고
    • Translational control of programmed cell death: Eukaryotic translation initiation factor 4E blocks apoptosis in growth-factor-restricted fibroblasts with physiologically expressed or deregulated Myc
    • Polunovsky VA, Rosenwald IB, Tan AT et al. Translational control of programmed cell death: Eukaryotic translation initiation factor 4E blocks apoptosis in growth-factor-restricted fibroblasts with physiologically expressed or deregulated Myc. Mol Cell Biol 1996; 16: 6573-81.
    • (1996) Mol Cell Biol , vol.16 , pp. 6573-6581
    • Polunovsky, V.A.1    Rosenwald, I.B.2    Tan, A.T.3
  • 97
    • 0343167422 scopus 로고    scopus 로고
    • Rapid induction of apoptosis mediated by peptides that bind initiation factor 4E
    • Herbert TP, Fahraeus R, Prescott A et al. Rapid induction of apoptosis mediated by peptides that bind initiation factor 4E. Curr Biol 2000; 10: 793-6.
    • (2000) Curr Biol , vol.10 , pp. 793-796
    • Herbert, T.P.1    Fahraeus, R.2    Prescott, A.3
  • 98
    • 0027362742 scopus 로고
    • Decreasing the level of translation initiation factor 4E with antisense RNA causes reversal of ras-mediated transformation and tumorigenesis of cloned rat embryo fibroblasts
    • Rinker-Schaeffer CW, Graff JR, DeBenedetti A et al. Decreasing the level of translation initiation factor 4E with antisense RNA causes reversal of ras-mediated transformation and tumorigenesis of cloned rat embryo fibroblasts. Int J Cancer 1993; 55: 841-7.
    • (1993) Int J Cancer , vol.55 , pp. 841-847
    • Rinker-Schaeffer, C.W.1    Graff, J.R.2    DeBenedetti, A.3
  • 99
    • 0028897627 scopus 로고
    • Reduction of translation initiation factor 4E reduces tumor growth, invasion and metastasis of ras-transformed cloned rat embryo fibroblast
    • Graff JR, Boghaert ER, DeBenedetti A et al. Reduction of translation initiation factor 4E reduces tumor growth, invasion and metastasis of ras-transformed cloned rat embryo fibroblast. Int J Cancer 1995; 60: 255-63.
    • (1995) Int J Cancer , vol.60 , pp. 255-263
    • Graff, J.R.1    Boghaert, E.R.2    DeBenedetti, A.3
  • 100
    • 0034120713 scopus 로고    scopus 로고
    • Antisense RNA to eIF4E suppresses oncogenic properties of a head and neck squamous cell carcinoma cell line
    • DeFatta RJ, Nathan CA, DeBenedetti A. Antisense RNA to eIF4E suppresses oncogenic properties of a head and neck squamous cell carcinoma cell line. Laryngoscope 2000; 110: 928-33.
    • (2000) Laryngoscope , vol.110 , pp. 928-933
    • DeFatta, R.J.1    Nathan, C.A.2    DeBenedetti, A.3
  • 101
    • 0030443685 scopus 로고    scopus 로고
    • The eIF-4E-binding proteins 1 and 2 are negative regulators of cell growth
    • Rousseau, D., Gingras A-C, Pause A et al. The eIF-4E-binding proteins 1 and 2 are negative regulators of cell growth. Oncogene 1996; 13: 2415-20.
    • (1996) Oncogene , vol.13 , pp. 2415-2420
    • Rousseau, D.1    Gingras, A.-C.2    Pause, A.3
  • 102
    • 0035845318 scopus 로고    scopus 로고
    • Antisense therapy in oncology: New hope for an old idea
    • Tamm I, Dorken B, Hartmann G. Antisense therapy in oncology: New hope for an old idea. Lancet 2001; 358: 489-97.
    • (2001) Lancet , vol.358 , pp. 489-497
    • Tamm, I.1    Dorken, B.2    Hartmann, G.3
  • 103
    • 0033065009 scopus 로고    scopus 로고
    • Toward antisense oligonucleotide therapy for cancer: ISIS compounds in clinical development
    • Holmlund JT, Monia BP, Kwoh TJ et al. Toward antisense oligonucleotide therapy for cancer: ISIS compounds in clinical development. Curr Opin Mol Ther 1999; 1: 372-85.
    • (1999) Curr Opin Mol Ther , vol.1 , pp. 372-385
    • Holmlund, J.T.1    Monia, B.P.2    Kwoh, T.J.3
  • 104
    • 0036174289 scopus 로고    scopus 로고
    • Rapamycin inhibits primary and metastatic tumor growth by antiangiogenesis: Involvement of vascular endothelial growth factor
    • Guba M, von Breitenbuch P, Steinbauer M et al. Rapamycin inhibits primary and metastatic tumor growth by antiangiogenesis: Involvement of vascular endothelial growth factor. Nat Med 2002; 8: 128-35.
    • (2002) Nat Med , vol.8 , pp. 128-135
    • Guba, M.1    Von Breitenbuch, P.2    Steinbauer, M.3
  • 105
    • 17944377486 scopus 로고    scopus 로고
    • Enhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR
    • Neshat MS, Mellinghoff IK, Tran C et al. Enhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR. Proc Natl Acad Sci USA 2001; 98: 10314-9.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10314-10319
    • Neshat, M.S.1    Mellinghoff, I.K.2    Tran, C.3
  • 106
    • 17944368972 scopus 로고    scopus 로고
    • An inhibitor of mTOR reduces neoplasia and normalizes p70/S6 kinase activity in Ptenmice
    • Podsypanina K, Lee RT, Politis C et al. An inhibitor of mTOR reduces neoplasia and normalizes p70/S6 kinase activity in Ptenmice. Proc Natl Acad Sci USA 2001; 98: 10320-5.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10320-10325
    • Podsypanina, K.1    Lee, R.T.2    Politis, C.3
  • 107
    • 0034722888 scopus 로고    scopus 로고
    • The rapamycin-sensitive signal transduction pathway as a target for cancer therapy
    • Hidalgo M, Rowinsky EK. The rapamycin-sensitive signal transduction pathway as a target for cancer therapy. Oncogene 2000; 19: 6680-6.
    • (2000) Oncogene , vol.19 , pp. 6680-6686
    • Hidalgo, M.1    Rowinsky, E.K.2
  • 108
    • 0036019373 scopus 로고    scopus 로고
    • Selective killing of cancer cells based on translational control of a suicide gene
    • DeFatta RJ, Li Y, De Benedetti A. Selective killing of cancer cells based on translational control of a suicide gene. Cancer Gene Ther 2002; 9: 573-8.
    • (2002) Cancer Gene Ther , vol.9 , pp. 573-578
    • DeFatta, R.J.1    Li, Y.2    De Benedetti, A.3
  • 109
    • 0036270720 scopus 로고    scopus 로고
    • A cancer gene therapy approach through translational control of a suicide gene
    • DeFatta RJ, Chervenak RP, De Benedetti A. A cancer gene therapy approach through translational control of a suicide gene. Cancer Gene Ther 2002; 9: 505-12.
    • (2002) Cancer Gene Ther , vol.9 , pp. 505-512
    • DeFatta, R.J.1    Chervenak, R.P.2    De Benedetti, A.3
  • 110
    • 0037226593 scopus 로고    scopus 로고
    • A molecular signature of metastasis in primary solid tumors
    • Ramaswamy S, Ross KN, Lander ES and Golub TR. A molecular signature of metastasis in primary solid tumors. Nat Gen 2003; 33: 49-54.
    • (2003) Nat Gen , vol.33 , pp. 49-54
    • Ramaswamy, S.1    Ross, K.N.2    Lander, E.S.3    Golub, T.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.