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Volumn 90, Issue C, 2009, Pages 255-292

Chapter 7 The Regulation of Protein Synthesis in Cancer

Author keywords

Cancer; Clinical trials; Protein synthesis; Signal transduction; Translational control

Indexed keywords

INITIATION FACTOR 3;

EID: 77957042196     PISSN: 18771173     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1877-1173(09)90007-2     Document Type: Review
Times cited : (10)

References (235)
  • 1
    • 0003288676 scopus 로고
    • Beitrag zur histologie und Aetiologie der carcinoma histologische und experimentelle
    • Pianese G. Beitrag zur histologie und Aetiologie der carcinoma histologische und experimentelle. Beitr Pathol Anat Allgem Pathol 142 (1896) 1-193
    • (1896) Beitr Pathol Anat Allgem Pathol , vol.142 , pp. 1-193
    • Pianese, G.1
  • 2
    • 0017152766 scopus 로고
    • Changes in RNA in relation to growth of the fibroblast. IV. Alterations in the production and processing of mRNA and rRNA in resting and growing cells
    • Johnson L.F., Levis R., Abelson H.T., Green H., and Penman S. Changes in RNA in relation to growth of the fibroblast. IV. Alterations in the production and processing of mRNA and rRNA in resting and growing cells. J Cell Biol 71 (1976) 933-938
    • (1976) J Cell Biol , vol.71 , pp. 933-938
    • Johnson, L.F.1    Levis, R.2    Abelson, H.T.3    Green, H.4    Penman, S.5
  • 3
    • 0018221844 scopus 로고
    • The effect of protein degradation on cellular growth characteristics
    • Baxter G.C., and Stanners C.P. The effect of protein degradation on cellular growth characteristics. J Cell Physiol 96 (1978) 139-145
    • (1978) J Cell Physiol , vol.96 , pp. 139-145
    • Baxter, G.C.1    Stanners, C.P.2
  • 5
    • 0018745307 scopus 로고
    • Transformed cells have lost control of ribosome number through their growth cycle
    • Stanners C.P., Adams M.E., Harkins J.L., and Pollard J.W. Transformed cells have lost control of ribosome number through their growth cycle. J Cell Physiol 100 (1979) 127-138
    • (1979) J Cell Physiol , vol.100 , pp. 127-138
    • Stanners, C.P.1    Adams, M.E.2    Harkins, J.L.3    Pollard, J.W.4
  • 6
    • 0028802746 scopus 로고
    • A hierarchy of ATP-consuming processes in mammalian cells
    • Buttgereit F., and Brand M.D. A hierarchy of ATP-consuming processes in mammalian cells. Biochem J 312 Pt 1 (1995) 163-167
    • (1995) Biochem J , vol.312 , Issue.PART 1 , pp. 163-167
    • Buttgereit, F.1    Brand, M.D.2
  • 7
    • 33846648989 scopus 로고    scopus 로고
    • Controlling gene expression through RNA regulons: the role of the eukaryotic translation initiation factor eIF4E
    • Culjkovic B., Topisirovic I., and Borden K.L. Controlling gene expression through RNA regulons: the role of the eukaryotic translation initiation factor eIF4E. Cell Cycle 6 (2007) 65-69
    • (2007) Cell Cycle , vol.6 , pp. 65-69
    • Culjkovic, B.1    Topisirovic, I.2    Borden, K.L.3
  • 8
    • 0035802386 scopus 로고    scopus 로고
    • Structural and functional features of eukaryotic mRNA untranslated regions
    • Pesole G., Mignone F., Gissi C., Grillo G., Licciulli F., and Liuni S. Structural and functional features of eukaryotic mRNA untranslated regions. Gene 276 (2001) 73-81
    • (2001) Gene , vol.276 , pp. 73-81
    • Pesole, G.1    Mignone, F.2    Gissi, C.3    Grillo, G.4    Licciulli, F.5    Liuni, S.6
  • 9
    • 2342489456 scopus 로고    scopus 로고
    • eIF-4E expression and its role in malignancies and metastases
    • De Benedetti A., and Graff J.R. eIF-4E expression and its role in malignancies and metastases. Oncogene 23 (2004) 3189-3199
    • (2004) Oncogene , vol.23 , pp. 3189-3199
    • De Benedetti, A.1    Graff, J.R.2
  • 10
    • 0028918259 scopus 로고
    • The proto-oncogene/translation factor eIF4E: a survey of its expression in breast carcinomas
    • Kerekatte V., Smiley K., Hu B., Smith A., Gelder F., and De Benedetti A. The proto-oncogene/translation factor eIF4E: a survey of its expression in breast carcinomas. Int J Cancer 64 (1995) 27-31
    • (1995) Int J Cancer , vol.64 , pp. 27-31
    • Kerekatte, V.1    Smiley, K.2    Hu, B.3    Smith, A.4    Gelder, F.5    De Benedetti, A.6
  • 11
    • 0039656540 scopus 로고    scopus 로고
    • Upregulation of protein synthesis initiation factor eIF-4E is an early event during colon carcinogenesis
    • Rosenwald I.B., Chen J.J., Wang S., Savas L., London I.M., and Pullman J. Upregulation of protein synthesis initiation factor eIF-4E is an early event during colon carcinogenesis. Oncogene 18 (1999) 2507-2517
    • (1999) Oncogene , vol.18 , pp. 2507-2517
    • Rosenwald, I.B.1    Chen, J.J.2    Wang, S.3    Savas, L.4    London, I.M.5    Pullman, J.6
  • 12
    • 0035886531 scopus 로고    scopus 로고
    • Expression of eukaryotic translation initiation factors 4E and 2 alpha is increased frequently in bronchioloalveolar but not in squamous cell carcinomas of the lung
    • Rosenwald I.B., Hutzler M.J., Wang S., Savas L., and Fraire A.E. Expression of eukaryotic translation initiation factors 4E and 2 alpha is increased frequently in bronchioloalveolar but not in squamous cell carcinomas of the lung. Cancer 92 (2001) 2164-2171
    • (2001) Cancer , vol.92 , pp. 2164-2171
    • Rosenwald, I.B.1    Hutzler, M.J.2    Wang, S.3    Savas, L.4    Fraire, A.E.5
  • 13
    • 35648995212 scopus 로고    scopus 로고
    • Translational control in cancer development and progression
    • Mathews M.B., Sonenberg N., and Hershey J.W.B. (Eds), Cold Spring Harbor Press, Cold Spring Harbor
    • Schneider R.J., and Sonenberg N. Translational control in cancer development and progression. In: Mathews M.B., Sonenberg N., and Hershey J.W.B. (Eds). Translational control in biology and medicine (2007), Cold Spring Harbor Press, Cold Spring Harbor 401-432
    • (2007) Translational control in biology and medicine , pp. 401-432
    • Schneider, R.J.1    Sonenberg, N.2
  • 14
    • 38849180436 scopus 로고    scopus 로고
    • Targeting the eukaryotic translation initiation factor 4E for cancer therapy
    • Graff J.R., Konicek B.W., Carter J.H., and Marcusson E.G. Targeting the eukaryotic translation initiation factor 4E for cancer therapy. Cancer Res 68 (2008) 631-634
    • (2008) Cancer Res , vol.68 , pp. 631-634
    • Graff, J.R.1    Konicek, B.W.2    Carter, J.H.3    Marcusson, E.G.4
  • 15
    • 65949111747 scopus 로고    scopus 로고
    • eIF4E activation is commonly elevated in advanced human prostate cancers and significantly related to reduced patient survival
    • Graff J.R., Konicek B.W., Lynch R.L., Dumstorf C.A., Dowless M.S., McNulty A.M., et al. eIF4E activation is commonly elevated in advanced human prostate cancers and significantly related to reduced patient survival. Cancer Res 69 (2009) 3866-3873
    • (2009) Cancer Res , vol.69 , pp. 3866-3873
    • Graff, J.R.1    Konicek, B.W.2    Lynch, R.L.3    Dumstorf, C.A.4    Dowless, M.S.5    McNulty, A.M.6
  • 16
    • 42149195978 scopus 로고    scopus 로고
    • eIF4E, the mRNA cap-binding protein: from basic discovery to translational research
    • Sonenberg N. eIF4E, the mRNA cap-binding protein: from basic discovery to translational research. Biochem Cell Biol 86 (2008) 178-183
    • (2008) Biochem Cell Biol , vol.86 , pp. 178-183
    • Sonenberg, N.1
  • 17
    • 35348954728 scopus 로고    scopus 로고
    • Translational control: a target for cancer therapy
    • Thumma S.C., and Kratzke R.A. Translational control: a target for cancer therapy. Cancer Lett 258 (2007) 1-8
    • (2007) Cancer Lett , vol.258 , pp. 1-8
    • Thumma, S.C.1    Kratzke, R.A.2
  • 18
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap
    • Lazaris-Karatzas A., Montine K.S., and Sonenberg N. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap. Nature 345 (1990) 544-547
    • (1990) Nature , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 19
    • 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 S.G., DeBenedetti A., and Graff J.R. Translational control of malignancy: the mRNA cap-binding protein, eIF-4E, as a central regulator of tumor formation, growth, invasion and metastasis. Anticancer Res 20 (2000) 1343-1351
    • (2000) Anticancer Res , vol.20 , pp. 1343-1351
    • Zimmer, S.G.1    DeBenedetti, A.2    Graff, J.R.3
  • 20
    • 2442648845 scopus 로고    scopus 로고
    • The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis
    • Ruggero D., Montanaro L., Ma L., Xu W., Londei P., Cordon-Cardo C., et al. The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis. Nat Med 10 (2004) 484-486
    • (2004) Nat Med , vol.10 , pp. 484-486
    • Ruggero, D.1    Montanaro, L.2    Ma, L.3    Xu, W.4    Londei, P.5    Cordon-Cardo, C.6
  • 21
    • 1642586272 scopus 로고    scopus 로고
    • Survival signalling by Akt and eIF4E in oncogenesis and cancer therapy
    • Wendel H.G., De Stanchina E., Fridman J.S., Malina A., Ray S., Kogan S., et al. Survival signalling by Akt and eIF4E in oncogenesis and cancer therapy. Nature 428 (2004) 332-337
    • (2004) Nature , vol.428 , pp. 332-337
    • Wendel, H.G.1    De Stanchina, E.2    Fridman, J.S.3    Malina, A.4    Ray, S.5    Kogan, S.6
  • 23
    • 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 C.W., Graff J.R., De Benedetti A., Zimmer S.G., and Rhoads R.E. 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 55 (1993) 841-847
    • (1993) Int J Cancer , vol.55 , pp. 841-847
    • Rinker-Schaeffer, C.W.1    Graff, J.R.2    De Benedetti, A.3    Zimmer, S.G.4    Rhoads, R.E.5
  • 24
    • 25144470125 scopus 로고    scopus 로고
    • Growth inhibition of head and neck squamous carcinoma cells by small interfering RNAs targeting eIF4E or cyclin D1 alone or combined with cisplatin
    • Oridate N., Kim H.J., Xu X., and Lotan R. Growth inhibition of head and neck squamous carcinoma cells by small interfering RNAs targeting eIF4E or cyclin D1 alone or combined with cisplatin. Cancer Biol Ther 4 (2005) 318-323
    • (2005) Cancer Biol Ther , vol.4 , pp. 318-323
    • Oridate, N.1    Kim, H.J.2    Xu, X.3    Lotan, R.4
  • 25
    • 0026723117 scopus 로고
    • mRNAs containing extensive secondary structure in their 5′ non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E
    • Koromilas A.E., Lazaris-Karatzas A., and Sonenberg N. mRNAs containing extensive secondary structure in their 5′ non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E. EMBO J 11 (1992) 4153-4158
    • (1992) EMBO J , vol.11 , pp. 4153-4158
    • Koromilas, A.E.1    Lazaris-Karatzas, A.2    Sonenberg, N.3
  • 26
    • 0028897627 scopus 로고
    • Reduction of translation initiation factor 4E decreases the malignancy of ras-transformed cloned rat embryo fibroblasts
    • Graff J.R., Boghaert E.R., De Benedetti A., Tudor D.L., Zimmer C.C., Chan S.K., et al. Reduction of translation initiation factor 4E decreases the malignancy of ras-transformed cloned rat embryo fibroblasts. Int J Cancer 60 (1995) 255-263
    • (1995) Int J Cancer , vol.60 , pp. 255-263
    • Graff, J.R.1    Boghaert, E.R.2    De Benedetti, A.3    Tudor, D.L.4    Zimmer, C.C.5    Chan, S.K.6
  • 27
    • 0030443685 scopus 로고    scopus 로고
    • The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth
    • Rousseau D., Gingras A.C., Pause A., and Sonenberg N. The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth. Oncogene 13 (1996) 2415-2420
    • (1996) Oncogene , vol.13 , pp. 2415-2420
    • Rousseau, D.1    Gingras, A.C.2    Pause, A.3    Sonenberg, N.4
  • 28
    • 2942544833 scopus 로고    scopus 로고
    • Activation of translation complex eIF4F is essential for the genesis and maintenance of the malignant phenotype in human mammary epithelial cells
    • Avdulov S., Li S., Michalek V., Burrichter D., Peterson M., Perlman D.M., et al. Activation of translation complex eIF4F is essential for the genesis and maintenance of the malignant phenotype in human mammary epithelial cells. Cancer Cell 5 (2004) 553-563
    • (2004) Cancer Cell , vol.5 , pp. 553-563
    • Avdulov, S.1    Li, S.2    Michalek, V.3    Burrichter, D.4    Peterson, M.5    Perlman, D.M.6
  • 29
    • 0343167422 scopus 로고    scopus 로고
    • Rapid induction of apoptosis mediated by peptides that bind initiation factor eIF4E
    • Herbert T.P., Fahraeus R., Prescott A., Lane D.P., and Proud C.G. Rapid induction of apoptosis mediated by peptides that bind initiation factor eIF4E. Curr Biol 10 (2000) 793-796
    • (2000) Curr Biol , vol.10 , pp. 793-796
    • Herbert, T.P.1    Fahraeus, R.2    Prescott, A.3    Lane, D.P.4    Proud, C.G.5
  • 30
    • 34548028705 scopus 로고    scopus 로고
    • 4E-binding protein 1: a key molecular "funnel factor" in human cancer with clinical implications
    • Armengol G., Rojo F., Castellvi J., Iglesias C., Cuatrecasas M., Pons B., et al. 4E-binding protein 1: a key molecular "funnel factor" in human cancer with clinical implications. Cancer Res 67 (2007) 7551-7555
    • (2007) Cancer Res , vol.67 , pp. 7551-7555
    • Armengol, G.1    Rojo, F.2    Castellvi, J.3    Iglesias, C.4    Cuatrecasas, M.5    Pons, B.6
  • 31
    • 46749097944 scopus 로고    scopus 로고
    • Therapeutic suppression of translation initiation modulates chemosensitivity in a mouse lymphoma model
    • Bordeleau M.E., Robert F., Gerard B., Lindqvist L., Chen S.M., Wendel H.G., et al. Therapeutic suppression of translation initiation modulates chemosensitivity in a mouse lymphoma model. J Clin Invest 118 (2008) 2651-2660
    • (2008) J Clin Invest , vol.118 , pp. 2651-2660
    • Bordeleau, M.E.1    Robert, F.2    Gerard, B.3    Lindqvist, L.4    Chen, S.M.5    Wendel, H.G.6
  • 32
    • 65549108194 scopus 로고    scopus 로고
    • Combined analysis of eIF4E and 4E-binding protein expression predicts breast cancer survival and estimates eIF4E activity
    • Coleman L.J., Peter M.B., Teall T.J., Brannan R.A., Hanby A.M., Honarpisheh H., et al. Combined analysis of eIF4E and 4E-binding protein expression predicts breast cancer survival and estimates eIF4E activity. Br J Cancer 100 (2009) 1393-1399
    • (2009) Br J Cancer , vol.100 , pp. 1393-1399
    • Coleman, L.J.1    Peter, M.B.2    Teall, T.J.3    Brannan, R.A.4    Hanby, A.M.5    Honarpisheh, H.6
  • 33
    • 33646089881 scopus 로고    scopus 로고
    • Expression of the eukaryotic translation initiation factor 4E (eIF4E) and 4E-BP1 in esophageal cancer
    • Salehi Z., and Mashayekhi F. Expression of the eukaryotic translation initiation factor 4E (eIF4E) and 4E-BP1 in esophageal cancer. Clin Biochem 39 (2006) 404-409
    • (2006) Clin Biochem , vol.39 , pp. 404-409
    • Salehi, Z.1    Mashayekhi, F.2
  • 34
    • 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., Hochman T., Yee H., et al. A hypoxia-controlled cap-dependent to cap-independent translation switch in breast cancer. Mol Cell 28 (2007) 501-512
    • (2007) Mol Cell , vol.28 , pp. 501-512
    • Braunstein, S.1    Karpisheva, K.2    Pola, C.3    Goldberg, J.4    Hochman, T.5    Yee, H.6
  • 36
    • 34247467477 scopus 로고    scopus 로고
    • Frequent overexpression of the genes FXR1, CLAPM1 and EIF4G located on amplicon 3q26-27 in squamous cell carcinoma of the lung
    • Comtesse N., Keller A., Diesinger I., Bauer C., Kayser K., Huwer H., et al. Frequent overexpression of the genes FXR1, CLAPM1 and EIF4G located on amplicon 3q26-27 in squamous cell carcinoma of the lung. Int J Cancer 120 (2007) 2538-2544
    • (2007) Int J Cancer , vol.120 , pp. 2538-2544
    • Comtesse, N.1    Keller, A.2    Diesinger, I.3    Bauer, C.4    Kayser, K.5    Huwer, H.6
  • 37
    • 0037051093 scopus 로고    scopus 로고
    • Overexpression of the eukaryotic translation initiation factor 4G (eIF4G-1) in squamous cell lung carcinoma
    • Bauer C., Brass N., Diesinger I., Kayser K., Grasser F.A., and Meese E. Overexpression of the eukaryotic translation initiation factor 4G (eIF4G-1) in squamous cell lung carcinoma. Int J Cancer 98 (2002) 181-185
    • (2002) Int J Cancer , vol.98 , pp. 181-185
    • Bauer, C.1    Brass, N.2    Diesinger, I.3    Kayser, K.4    Grasser, F.A.5    Meese, E.6
  • 38
    • 0035880647 scopus 로고    scopus 로고
    • Translation initiation factor eIF-4G is immunogenic, overexpressed, and amplified in patients with squamous cell lung carcinoma
    • Bauer C., Diesinger I., Brass N., Steinhart H., Iro H., and Meese E.U. Translation initiation factor eIF-4G is immunogenic, overexpressed, and amplified in patients with squamous cell lung carcinoma. Cancer 92 (2001) 822-829
    • (2001) Cancer , vol.92 , pp. 822-829
    • Bauer, C.1    Diesinger, I.2    Brass, N.3    Steinhart, H.4    Iro, H.5    Meese, E.U.6
  • 39
    • 0031030030 scopus 로고    scopus 로고
    • Translation initiation factor eIF-4gamma is encoded by an amplified gene and induces an immune response in squamous cell lung carcinoma
    • Brass N., Heckel D., Sahin U., Pfreundschuh M., Sybrecht G.W., and Meese E. Translation initiation factor eIF-4gamma is encoded by an amplified gene and induces an immune response in squamous cell lung carcinoma. Hum Mol Genet 6 (1997) 33-39
    • (1997) Hum Mol Genet , vol.6 , pp. 33-39
    • Brass, N.1    Heckel, D.2    Sahin, U.3    Pfreundschuh, M.4    Sybrecht, G.W.5    Meese, E.6
  • 40
    • 67650080623 scopus 로고    scopus 로고
    • Essential role for eIF4GI overexpression in the pathogenesis of inflammatory breast cancer
    • Silvera D., Arju R., Darvishian F., Levine P.H., Zolfaghari L., Goldberg J., et al. Essential role for eIF4GI overexpression in the pathogenesis of inflammatory breast cancer. Nat Cell Biol 11 (2009) 903-908
    • (2009) Nat Cell Biol , vol.11 , pp. 903-908
    • Silvera, D.1    Arju, R.2    Darvishian, F.3    Levine, P.H.4    Zolfaghari, L.5    Goldberg, J.6
  • 42
    • 0033855877 scopus 로고    scopus 로고
    • Enhanced expression of translation factor mRNAs in hepatocellular carcinoma
    • Shuda M., Kondoh N., Tanaka K., Ryo A., Wakatsuki T., Hada A., et al. Enhanced expression of translation factor mRNAs in hepatocellular carcinoma. Anticancer Res 20 (2000) 2489-2494
    • (2000) Anticancer Res , vol.20 , pp. 2489-2494
    • Shuda, M.1    Kondoh, N.2    Tanaka, K.3    Ryo, A.4    Wakatsuki, T.5    Hada, A.6
  • 44
    • 67449104909 scopus 로고    scopus 로고
    • The tumour suppressor Pdcd4: recent advances in the elucidation of function and regulation
    • Lankat-Buttgereit B., and Goke R. The tumour suppressor Pdcd4: recent advances in the elucidation of function and regulation. Biol Cell 101 (2009) 309-317
    • (2009) Biol Cell , vol.101 , pp. 309-317
    • Lankat-Buttgereit, B.1    Goke, R.2
  • 45
    • 0037216626 scopus 로고    scopus 로고
    • The transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation
    • Yang H.S., Jansen A.P., Komar A.A., Zheng X., Merrick W.C., Costes S., et al. The transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation. Mol Cell Biol 23 (2003) 26-37
    • (2003) Mol Cell Biol , vol.23 , pp. 26-37
    • Yang, H.S.1    Jansen, A.P.2    Komar, A.A.3    Zheng, X.4    Merrick, W.C.5    Costes, S.6
  • 46
    • 33748042296 scopus 로고    scopus 로고
    • Initiation factor eIF3 and regulation of mRNA translation, cell growth, and cancer
    • Dong Z., and Zhang J.T. Initiation factor eIF3 and regulation of mRNA translation, cell growth, and cancer. Crit Rev Oncol Hematol 59 (2006) 169-180
    • (2006) Crit Rev Oncol Hematol , vol.59 , pp. 169-180
    • Dong, Z.1    Zhang, J.T.2
  • 47
    • 34247165835 scopus 로고    scopus 로고
    • Individual overexpression of five subunits of human translation initiation factor eIF3 promotes malignant transformation of immortal fibroblast cells
    • Zhang L., Pan X., and Hershey J.W. Individual overexpression of five subunits of human translation initiation factor eIF3 promotes malignant transformation of immortal fibroblast cells. J Biol Chem 282 (2007) 5790-5800
    • (2007) J Biol Chem , vol.282 , pp. 5790-5800
    • Zhang, L.1    Pan, X.2    Hershey, J.W.3
  • 48
    • 1842413082 scopus 로고    scopus 로고
    • Cloning of a novel protein overexpressed in human mammary carcinoma
    • Bachmann F., Banziger R., and Burger M.M. Cloning of a novel protein overexpressed in human mammary carcinoma. Cancer Res 57 (1997) 988-994
    • (1997) Cancer Res , vol.57 , pp. 988-994
    • Bachmann, F.1    Banziger, R.2    Burger, M.M.3
  • 49
    • 0032189714 scopus 로고    scopus 로고
    • Expression of p150 in cervical neoplasia and its potential value in predicting survival
    • Dellas A., Torhorst J., Bachmann F., Banziger R., Schultheiss E., and Burger M.M. Expression of p150 in cervical neoplasia and its potential value in predicting survival. Cancer 83 (1998) 1376-1383
    • (1998) Cancer , vol.83 , pp. 1376-1383
    • Dellas, A.1    Torhorst, J.2    Bachmann, F.3    Banziger, R.4    Schultheiss, E.5    Burger, M.M.6
  • 50
    • 0035364978 scopus 로고    scopus 로고
    • Identification of a 170-kDa protein over-expressed in lung cancers
    • Pincheira R., Chen Q., and Zhang J.T. Identification of a 170-kDa protein over-expressed in lung cancers. Br J Cancer 84 (2001) 1520-1527
    • (2001) Br J Cancer , vol.84 , pp. 1520-1527
    • Pincheira, R.1    Chen, Q.2    Zhang, J.T.3
  • 51
    • 0033046231 scopus 로고    scopus 로고
    • p150 expression and its prognostic value in squamous-cell carcinoma of the esophagus
    • Chen G., and Burger M.M. p150 expression and its prognostic value in squamous-cell carcinoma of the esophagus. Int J Cancer 84 (1999) 95-100
    • (1999) Int J Cancer , vol.84 , pp. 95-100
    • Chen, G.1    Burger, M.M.2
  • 52
    • 6344237621 scopus 로고    scopus 로고
    • p150 overexpression in gastric carcinoma: the association with p53, apoptosis and cell proliferation
    • Chen G., and Burger M.M. p150 overexpression in gastric carcinoma: the association with p53, apoptosis and cell proliferation. Int J Cancer 112 (2004) 393-398
    • (2004) Int J Cancer , vol.112 , pp. 393-398
    • Chen, G.1    Burger, M.M.2
  • 53
    • 2342656309 scopus 로고    scopus 로고
    • Role of eIF3 p170 in controlling synthesis of ribonucleotide reductase M2 and cell growth
    • Dong Z., Liu L.H., Han B., Pincheira R., and Zhang J.T. Role of eIF3 p170 in controlling synthesis of ribonucleotide reductase M2 and cell growth. Oncogene 23 (2004) 3790-3801
    • (2004) Oncogene , vol.23 , pp. 3790-3801
    • Dong, Z.1    Liu, L.H.2    Han, B.3    Pincheira, R.4    Zhang, J.T.5
  • 54
    • 0141521573 scopus 로고    scopus 로고
    • EIF3 p170, a mediator of mimosine effect on protein synthesis and cell cycle progression
    • Dong Z., and Zhang J.T. EIF3 p170, a mediator of mimosine effect on protein synthesis and cell cycle progression. Mol Biol Cell 14 (2003) 3942-3951
    • (2003) Mol Biol Cell , vol.14 , pp. 3942-3951
    • Dong, Z.1    Zhang, J.T.2
  • 55
    • 0033709896 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 3 p110 mRNA is overexpressed in testicular seminomas
    • Rothe M., Ko Y., Albers P., and Wernert N. Eukaryotic initiation factor 3 p110 mRNA is overexpressed in testicular seminomas. Am J Pathol 157 (2000) 1597-1604
    • (2000) Am J Pathol , vol.157 , pp. 1597-1604
    • Rothe, M.1    Ko, Y.2    Albers, P.3    Wernert, N.4
  • 56
    • 33645119208 scopus 로고    scopus 로고
    • Schwannomin inhibits tumorigenesis through direct interaction with the eukaryotic initiation factor subunit c (eIF3c)
    • Scoles D.R., Yong W.H., Qin Y., Wawrowsky K., and Pulst S.M. Schwannomin inhibits tumorigenesis through direct interaction with the eukaryotic initiation factor subunit c (eIF3c). Hum Mol Genet 15 (2006) 1059-1070
    • (2006) Hum Mol Genet , vol.15 , pp. 1059-1070
    • Scoles, D.R.1    Yong, W.H.2    Qin, Y.3    Wawrowsky, K.4    Pulst, S.M.5
  • 57
    • 0033052411 scopus 로고    scopus 로고
    • Amplification and overexpression of p40 subunit of eukaryotic translation initiation factor 3 in breast and prostate cancer
    • Nupponen N.N., Porkka K., Kakkola L., Tanner M., Persson K., Borg A., et al. Amplification and overexpression of p40 subunit of eukaryotic translation initiation factor 3 in breast and prostate cancer. Am J Pathol 154 (1999) 1777-1783
    • (1999) Am J Pathol , vol.154 , pp. 1777-1783
    • Nupponen, N.N.1    Porkka, K.2    Kakkola, L.3    Tanner, M.4    Persson, K.5    Borg, A.6
  • 58
    • 0035184312 scopus 로고    scopus 로고
    • Amplification of EIF3S3 gene is associated with advanced stage in prostate cancer
    • Saramaki O., Willi N., Bratt O., Gasser T.C., Koivisto P., Nupponen N.N., et al. Amplification of EIF3S3 gene is associated with advanced stage in prostate cancer. Am J Pathol 159 (2001) 2089-2094
    • (2001) Am J Pathol , vol.159 , pp. 2089-2094
    • Saramaki, O.1    Willi, N.2    Bratt, O.3    Gasser, T.C.4    Koivisto, P.5    Nupponen, N.N.6
  • 59
    • 67649392920 scopus 로고    scopus 로고
    • MYC and EIF3H coamplification significantly improve response and survival of non-small cell lung cancer patients (NSCLC) treated with gefitinib
    • Cappuzzo F., Varella-Garcia M., Rossi E., Gajapathy S., Valente M., Drabkin H., et al. MYC and EIF3H coamplification significantly improve response and survival of non-small cell lung cancer patients (NSCLC) treated with gefitinib. J Thorac Oncol 4 (2009) 472-478
    • (2009) J Thorac Oncol , vol.4 , pp. 472-478
    • Cappuzzo, F.1    Varella-Garcia, M.2    Rossi, E.3    Gajapathy, S.4    Valente, M.5    Drabkin, H.6
  • 60
    • 33746899672 scopus 로고    scopus 로고
    • Decreased expression of eukaryotic initiation factor 3f deregulates translation and apoptosis in tumor cells
    • Shi J., Kahle A., Hershey J.W., Honchak B.M., Warneke J.A., Leong S.P., et al. Decreased expression of eukaryotic initiation factor 3f deregulates translation and apoptosis in tumor cells. Oncogene 25 (2006) 4923-4936
    • (2006) Oncogene , vol.25 , pp. 4923-4936
    • Shi, J.1    Kahle, A.2    Hershey, J.W.3    Honchak, B.M.4    Warneke, J.A.5    Leong, S.P.6
  • 64
  • 65
    • 12344305214 scopus 로고    scopus 로고
    • eIF2 and the control of cell physiology
    • Proud C.G. eIF2 and the control of cell physiology. Semin Cell Dev Biol 16 (2005) 3-12
    • (2005) Semin Cell Dev Biol , vol.16 , pp. 3-12
    • Proud, C.G.1
  • 66
    • 0036856008 scopus 로고    scopus 로고
    • Translational control in the endoplasmic reticulum stress response
    • Ron D. Translational control in the endoplasmic reticulum stress response. J Clin Invest 110 (2002) 1383-1388
    • (2002) J Clin Invest , vol.110 , pp. 1383-1388
    • Ron, D.1
  • 67
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding H.P., Novoa I., Zhang Y., Zeng H., Wek R., Schapira M., et al. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 6 (2000) 1099-1108
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6
  • 68
    • 33947584856 scopus 로고    scopus 로고
    • Regulation of protein synthesis by the heme-regulated eIF2alpha kinase: relevance to anemias
    • Chen J.J. Regulation of protein synthesis by the heme-regulated eIF2alpha kinase: relevance to anemias. Blood 109 (2007) 2693-2699
    • (2007) Blood , vol.109 , pp. 2693-2699
    • Chen, J.J.1
  • 69
    • 0026701570 scopus 로고
    • Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase
    • Koromilas A.E., Roy S., Barber G.N., Katze M.G., and Sonenberg N. Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase. Science 257 (1992) 1685-1689
    • (1992) Science , vol.257 , pp. 1685-1689
    • Koromilas, A.E.1    Roy, S.2    Barber, G.N.3    Katze, M.G.4    Sonenberg, N.5
  • 70
    • 0029118217 scopus 로고
    • Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells
    • Donze O., Jagus R., Koromilas A.E., Hershey J.W., and Sonenberg N. Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells. EMBO J 14 (1995) 3828-3834
    • (1995) EMBO J , vol.14 , pp. 3828-3834
    • Donze, O.1    Jagus, R.2    Koromilas, A.E.3    Hershey, J.W.4    Sonenberg, N.5
  • 72
    • 47049103645 scopus 로고    scopus 로고
    • Increased susceptibility of breast cancer cells to stress mediated inhibition of protein synthesis
    • Pervin S., Tran A.H., Zekavati S., Fukuto J.M., Singh R., and Chaudhuri G. Increased susceptibility of breast cancer cells to stress mediated inhibition of protein synthesis. Cancer Res 68 (2008) 4862-4874
    • (2008) Cancer Res , vol.68 , pp. 4862-4874
    • Pervin, S.1    Tran, A.H.2    Zekavati, S.3    Fukuto, J.M.4    Singh, R.5    Chaudhuri, G.6
  • 73
    • 65249089098 scopus 로고    scopus 로고
    • ERdj5 sensitizes neuroblastoma cells to endoplasmic reticulum stress-induced apoptosis
    • Thomas C.G., and Spyrou G. ERdj5 sensitizes neuroblastoma cells to endoplasmic reticulum stress-induced apoptosis. J Biol Chem 284 (2009) 6282-6290
    • (2009) J Biol Chem , vol.284 , pp. 6282-6290
    • Thomas, C.G.1    Spyrou, G.2
  • 74
    • 0029061555 scopus 로고
    • Mutants of the RNA-dependent protein kinase (PKR) lacking double-stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation
    • Barber G.N., Wambach M., Thompson S., Jagus R., and Katze M.G. Mutants of the RNA-dependent protein kinase (PKR) lacking double-stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation. Mol Cell Biol 15 (1995) 3138-3146
    • (1995) Mol Cell Biol , vol.15 , pp. 3138-3146
    • Barber, G.N.1    Wambach, M.2    Thompson, S.3    Jagus, R.4    Katze, M.G.5
  • 75
    • 0027396813 scopus 로고
    • Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase
    • Meurs E.F., Galabru J., Barber G.N., Katze M.G., and Hovanessian A.G. Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase. Proc Natl Acad Sci USA 90 (1993) 232-236
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 232-236
    • Meurs, E.F.1    Galabru, J.2    Barber, G.N.3    Katze, M.G.4    Hovanessian, A.G.5
  • 76
    • 0033605371 scopus 로고    scopus 로고
    • Characterization of transgenic mice with targeted disruption of the catalytic domain of the double-stranded RNA-dependent protein kinase, PKR
    • Abraham N., Stojdl D.F., Duncan P.I., Methot N., Ishii T., Dube M., et al. Characterization of transgenic mice with targeted disruption of the catalytic domain of the double-stranded RNA-dependent protein kinase, PKR. J Biol Chem 274 (1999) 5953-5962
    • (1999) J Biol Chem , vol.274 , pp. 5953-5962
    • Abraham, N.1    Stojdl, D.F.2    Duncan, P.I.3    Methot, N.4    Ishii, T.5    Dube, M.6
  • 77
    • 0029590069 scopus 로고
    • Deficient signaling in mice devoid of double-stranded RNA-dependent protein kinase
    • Yang Y.L., Reis L.F., Pavlovic J., Aguzzi A., Schafer R., Kumar A., et al. Deficient signaling in mice devoid of double-stranded RNA-dependent protein kinase. EMBO J 14 (1995) 6095-6106
    • (1995) EMBO J , vol.14 , pp. 6095-6106
    • Yang, Y.L.1    Reis, L.F.2    Pavlovic, J.3    Aguzzi, A.4    Schafer, R.5    Kumar, A.6
  • 78
    • 0027383066 scopus 로고
    • Expression of the double-stranded RNA-dependent protein kinase (p68) in squamous cell carcinoma of the head and neck region
    • Haines III G.K., Becker S., Ghadge G., Kies M., Pelzer H., and Radosevich J.A. Expression of the double-stranded RNA-dependent protein kinase (p68) in squamous cell carcinoma of the head and neck region. Arch Otolaryngol Head Neck Surg 119 (1993) 1142-1147
    • (1993) Arch Otolaryngol Head Neck Surg , vol.119 , pp. 1142-1147
    • Haines III, G.K.1    Becker, S.2    Ghadge, G.3    Kies, M.4    Pelzer, H.5    Radosevich, J.A.6
  • 79
    • 0027324680 scopus 로고
    • Correlation of the expression of double-stranded RNA-dependent protein kinase (p68) with differentiation in head and neck squamous cell carcinoma
    • Haines G.K., Ghadge G.D., Becker S., Kies M., Pelzer H., Thimmappaya B., et al. Correlation of the expression of double-stranded RNA-dependent protein kinase (p68) with differentiation in head and neck squamous cell carcinoma. Virchows Arch B Cell Pathol Incl Mol Pathol 63 (1993) 289-295
    • (1993) Virchows Arch B Cell Pathol Incl Mol Pathol , vol.63 , pp. 289-295
    • Haines, G.K.1    Ghadge, G.D.2    Becker, S.3    Kies, M.4    Pelzer, H.5    Thimmappaya, B.6
  • 80
    • 0031458299 scopus 로고    scopus 로고
    • Interferon-responsive protein kinase (p68) and proliferating cell nuclear antigen are inversely distributed in head and neck squamous cell carcinoma
    • Haines III G.K., Panos R.J., Bak P.M., Brown T., Zielinski M., Leyland J., et al. Interferon-responsive protein kinase (p68) and proliferating cell nuclear antigen are inversely distributed in head and neck squamous cell carcinoma. Tumour Biol 19 (1998) 52-59
    • (1998) Tumour Biol , vol.19 , pp. 52-59
    • Haines III, G.K.1    Panos, R.J.2    Bak, P.M.3    Brown, T.4    Zielinski, M.5    Leyland, J.6
  • 81
    • 0033943112 scopus 로고    scopus 로고
    • Protein expression of double-stranded RNA-activated protein kinase in thyroid carcinomas: correlations with histologic types, pathologic parameters, and Ki-67 labeling
    • Terada T., Maeta H., Endo K., and Ohta T. Protein expression of double-stranded RNA-activated protein kinase in thyroid carcinomas: correlations with histologic types, pathologic parameters, and Ki-67 labeling. Hum Pathol 31 (2000) 817-821
    • (2000) Hum Pathol , vol.31 , pp. 817-821
    • Terada, T.1    Maeta, H.2    Endo, K.3    Ohta, T.4
  • 82
    • 0029990084 scopus 로고    scopus 로고
    • Expression of the protein kinase PKR in modulated by IRF-1 and is reduced in 5q-associated leukemias
    • Beretta L., Gabbay M., Berger R., Hanash S.M., and Sonenberg N. Expression of the protein kinase PKR in modulated by IRF-1 and is reduced in 5q-associated leukemias. Oncogene 12 (1996) 1593-1596
    • (1996) Oncogene , vol.12 , pp. 1593-1596
    • Beretta, L.1    Gabbay, M.2    Berger, R.3    Hanash, S.M.4    Sonenberg, N.5
  • 83
    • 0032189405 scopus 로고    scopus 로고
    • Aberrant expression of double-stranded RNA-dependent protein kinase in hepatocytes of chronic hepatitis and differentiated hepatocellular carcinoma
    • Shimada A., Shiota G., Miyata H., Kamahora T., Kawasaki H., Shiraki K., et al. Aberrant expression of double-stranded RNA-dependent protein kinase in hepatocytes of chronic hepatitis and differentiated hepatocellular carcinoma. Cancer Res 58 (1998) 4434-4438
    • (1998) Cancer Res , vol.58 , pp. 4434-4438
    • Shimada, A.1    Shiota, G.2    Miyata, H.3    Kamahora, T.4    Kawasaki, H.5    Shiraki, K.6
  • 84
    • 0034702174 scopus 로고    scopus 로고
    • Human breast cancer cells contain elevated levels and activity of the protein kinase, PKR
    • Kim S.H., Forman A.P., Mathews M.B., and Gunnery S. Human breast cancer cells contain elevated levels and activity of the protein kinase, PKR. Oncogene 19 (2000) 3086-3094
    • (2000) Oncogene , vol.19 , pp. 3086-3094
    • Kim, S.H.1    Forman, A.P.2    Mathews, M.B.3    Gunnery, S.4
  • 85
    • 0029655361 scopus 로고    scopus 로고
    • Expression of the double-stranded RNA-dependent protein kinase (p68) in human breast tissues
    • Haines G.K., Cajulis R., Hayden R., Duda R., Talamonti M., and Radosevich J.A. Expression of the double-stranded RNA-dependent protein kinase (p68) in human breast tissues. Tumour Biol 17 (1996) 5-12
    • (1996) Tumour Biol , vol.17 , pp. 5-12
    • Haines, G.K.1    Cajulis, R.2    Hayden, R.3    Duda, R.4    Talamonti, M.5    Radosevich, J.A.6
  • 87
    • 27144458505 scopus 로고    scopus 로고
    • ER stress-regulated translation increases tolerance to extreme hypoxia and promotes tumor growth
    • Bi M., Naczki C., Koritzinsky M., Fels D., Blais J., Hu N., et al. ER stress-regulated translation increases tolerance to extreme hypoxia and promotes tumor growth. EMBO J 24 (2005) 3470-3481
    • (2005) EMBO J , vol.24 , pp. 3470-3481
    • Bi, M.1    Naczki, C.2    Koritzinsky, M.3    Fels, D.4    Blais, J.5    Hu, N.6
  • 88
    • 33644852277 scopus 로고    scopus 로고
    • Gene expression during acute and prolonged hypoxia is regulated by distinct mechanisms of translational control
    • Koritzinsky M., Magagnin M.G., van den Beucken T., Seigneuric R., Savelkouls K., Dostie J., et al. Gene expression during acute and prolonged hypoxia is regulated by distinct mechanisms of translational control. EMBO J 25 (2006) 1114-1125
    • (2006) EMBO J , vol.25 , pp. 1114-1125
    • Koritzinsky, M.1    Magagnin, M.G.2    van den Beucken, T.3    Seigneuric, R.4    Savelkouls, K.5    Dostie, J.6
  • 89
  • 90
    • 39749116239 scopus 로고    scopus 로고
    • Hypoxia and regulation of messenger RNA translation
    • Koritzinsky M., and Wouters B.G. Hypoxia and regulation of messenger RNA translation. Methods Enzymol 435 (2007) 247-273
    • (2007) Methods Enzymol , vol.435 , pp. 247-273
    • Koritzinsky, M.1    Wouters, B.G.2
  • 91
    • 54549089738 scopus 로고    scopus 로고
    • Hypoxia signalling through mTOR and the unfolded protein response in cancer
    • Wouters B.G., and Koritzinsky M. Hypoxia signalling through mTOR and the unfolded protein response in cancer. Nat Rev Cancer 8 (2008) 851-864
    • (2008) Nat Rev Cancer , vol.8 , pp. 851-864
    • Wouters, B.G.1    Koritzinsky, M.2
  • 92
    • 60549106248 scopus 로고    scopus 로고
    • Inhibition of eIF2{alpha} dephosphorylation maximizes bortezomib efficiency and eliminates quiescent multiple myeloma cells surviving proteasome inhibitor therapy
    • Schewe D.M., and Aguirre-Ghiso J.A. Inhibition of eIF2{alpha} dephosphorylation maximizes bortezomib efficiency and eliminates quiescent multiple myeloma cells surviving proteasome inhibitor therapy. Cancer Res 69 (2009) 1545-1552
    • (2009) Cancer Res , vol.69 , pp. 1545-1552
    • Schewe, D.M.1    Aguirre-Ghiso, J.A.2
  • 94
    • 0038738334 scopus 로고    scopus 로고
    • Pre-ribosomes on the road from the nucleolus to the cytoplasm
    • Tschochner H., and Hurt E. Pre-ribosomes on the road from the nucleolus to the cytoplasm. Trends Cell Biol 13 (2003) 255-263
    • (2003) Trends Cell Biol , vol.13 , pp. 255-263
    • Tschochner, H.1    Hurt, E.2
  • 95
    • 0034114866 scopus 로고    scopus 로고
    • Nucleolar size indicates the rapidity of cell proliferation in cancer tissues
    • Derenzini M., Trere D., Pession A., Govoni M., Sirri V., and Chieco P. Nucleolar size indicates the rapidity of cell proliferation in cancer tissues. J Pathol 191 (2000) 181-186
    • (2000) J Pathol , vol.191 , pp. 181-186
    • Derenzini, M.1    Trere, D.2    Pession, A.3    Govoni, M.4    Sirri, V.5    Chieco, P.6
  • 96
    • 0034660892 scopus 로고    scopus 로고
    • The Pezcoller lecture: cancer cell cycles revisited
    • Sherr C.J. The Pezcoller lecture: cancer cell cycles revisited. Cancer Res 60 (2000) 3689-3695
    • (2000) Cancer Res , vol.60 , pp. 3689-3695
    • Sherr, C.J.1
  • 97
    • 0032618597 scopus 로고    scopus 로고
    • Regulation of mammalian ribosomal gene transcription by RNA polymerase I
    • Grummt I. Regulation of mammalian ribosomal gene transcription by RNA polymerase I. Prog Nucleic Acid Res Mol Biol 62 (1999) 109-154
    • (1999) Prog Nucleic Acid Res Mol Biol , vol.62 , pp. 109-154
    • Grummt, I.1
  • 98
    • 0033023081 scopus 로고    scopus 로고
    • Cell cycle-dependent regulation of RNA polymerase I transcription: the nucleolar transcription factor UBF is inactive in mitosis and early G1
    • Klein J., and Grummt I. Cell cycle-dependent regulation of RNA polymerase I transcription: the nucleolar transcription factor UBF is inactive in mitosis and early G1. Proc Natl Acad Sci USA 96 (1999) 6096-6101
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6096-6101
    • Klein, J.1    Grummt, I.2
  • 99
    • 0035253411 scopus 로고    scopus 로고
    • Cell-cycle-dependent translational control
    • Pyronnet S., and Sonenberg N. Cell-cycle-dependent translational control. Curr Opin Genet Dev 11 (2001) 13-18
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 13-18
    • Pyronnet, S.1    Sonenberg, N.2
  • 100
    • 0032535115 scopus 로고    scopus 로고
    • Mitotic silencing of human rRNA synthesis: inactivation of the promoter selectivity factor SL1 by cdc2/cyclin B-mediated phosphorylation
    • Heix J., Vente A., Voit R., Budde A., Michaelidis T.M., and Grummt I. Mitotic silencing of human rRNA synthesis: inactivation of the promoter selectivity factor SL1 by cdc2/cyclin B-mediated phosphorylation. EMBO J 17 (1998) 7373-7381
    • (1998) EMBO J , vol.17 , pp. 7373-7381
    • Heix, J.1    Vente, A.2    Voit, R.3    Budde, A.4    Michaelidis, T.M.5    Grummt, I.6
  • 101
    • 4544330157 scopus 로고    scopus 로고
    • Quantitative kinetic analysis of nucleolar breakdown and reassembly during mitosis in live human cells
    • Leung A.K., Gerlich D., Miller G., Lyon C., Lam Y.W., Lleres D., et al. Quantitative kinetic analysis of nucleolar breakdown and reassembly during mitosis in live human cells. J Cell Biol 166 (2004) 787-800
    • (2004) J Cell Biol , vol.166 , pp. 787-800
    • Leung, A.K.1    Gerlich, D.2    Miller, G.3    Lyon, C.4    Lam, Y.W.5    Lleres, D.6
  • 102
    • 0034707645 scopus 로고    scopus 로고
    • In vivo release of mitotic silencing of ribosomal gene transcription does not give rise to precursor ribosomal RNA processing
    • Sirri V., Roussel P., and Hernandez-Verdun D. In vivo release of mitotic silencing of ribosomal gene transcription does not give rise to precursor ribosomal RNA processing. J Cell Biol 148 (2000) 259-270
    • (2000) J Cell Biol , vol.148 , pp. 259-270
    • Sirri, V.1    Roussel, P.2    Hernandez-Verdun, D.3
  • 103
    • 0024473604 scopus 로고
    • G1 events and regulation of cell proliferation
    • Pardee A.B. G1 events and regulation of cell proliferation. Science 246 (1989) 603-608
    • (1989) Science , vol.246 , pp. 603-608
    • Pardee, A.B.1
  • 104
    • 0029094210 scopus 로고
    • Activation of mammalian ribosomal gene transcription requires phosphorylation of the nucleolar transcription factor UBF
    • Voit R., Kuhn A., Sander E.E., and Grummt I. Activation of mammalian ribosomal gene transcription requires phosphorylation of the nucleolar transcription factor UBF. Nucleic Acids Res 23 (1995) 2593-2599
    • (1995) Nucleic Acids Res , vol.23 , pp. 2593-2599
    • Voit, R.1    Kuhn, A.2    Sander, E.E.3    Grummt, I.4
  • 105
    • 0035923591 scopus 로고    scopus 로고
    • Phosphorylation of UBF at serine 388 is required for interaction with RNA polymerase I and activation of rDNA transcription
    • Voit R., and Grummt I. Phosphorylation of UBF at serine 388 is required for interaction with RNA polymerase I and activation of rDNA transcription. Proc Natl Acad Sci USA 98 (2001) 13631-13636
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13631-13636
    • Voit, R.1    Grummt, I.2
  • 106
    • 0026591023 scopus 로고
    • The nucleolar transcription factor mUBF is phosphorylated by casein kinase II in the C-terminal hyperacidic tail which is essential for transactivation
    • Voit R., Schnapp A., Kuhn A., Rosenbauer H., Hirschmann P., Stunnenberg H.G., et al. The nucleolar transcription factor mUBF is phosphorylated by casein kinase II in the C-terminal hyperacidic tail which is essential for transactivation. EMBO J 11 (1992) 2211-2218
    • (1992) EMBO J , vol.11 , pp. 2211-2218
    • Voit, R.1    Schnapp, A.2    Kuhn, A.3    Rosenbauer, H.4    Hirschmann, P.5    Stunnenberg, H.G.6
  • 107
    • 0026502471 scopus 로고
    • Differential phosphorylation and localization of the transcription factor UBF in vivo in response to serum deprivation. In vitro dephosphorylation of UBF reduces its transactivation properties
    • O'Mahony D.J., Xie W.Q., Smith S.D., Singer H.A., and Rothblum L.I. Differential phosphorylation and localization of the transcription factor UBF in vivo in response to serum deprivation. In vitro dephosphorylation of UBF reduces its transactivation properties. J Biol Chem 267 (1992) 35-38
    • (1992) J Biol Chem , vol.267 , pp. 35-38
    • O'Mahony, D.J.1    Xie, W.Q.2    Smith, S.D.3    Singer, H.A.4    Rothblum, L.I.5
  • 108
    • 0035930330 scopus 로고    scopus 로고
    • An immediate response of ribosomal transcription to growth factor stimulation in mammals is mediated by ERK phosphorylation of UBF
    • Stefanovsky V.Y., Pelletier G., Hannan R., Gagnon-Kugler T., Rothblum L.I., and Moss T. An immediate response of ribosomal transcription to growth factor stimulation in mammals is mediated by ERK phosphorylation of UBF. Mol Cell 8 (2001) 1063-1073
    • (2001) Mol Cell , vol.8 , pp. 1063-1073
    • Stefanovsky, V.Y.1    Pelletier, G.2    Hannan, R.3    Gagnon-Kugler, T.4    Rothblum, L.I.5    Moss, T.6
  • 109
    • 0043163868 scopus 로고    scopus 로고
    • EGFR family signaling and its association with breast cancer development and resistance to chemotherapy (review)
    • Navolanic P.M., Steelman L.S., and McCubrey J.A. EGFR family signaling and its association with breast cancer development and resistance to chemotherapy (review). Int J Oncol 22 (2003) 237-252
    • (2003) Int J Oncol , vol.22 , pp. 237-252
    • Navolanic, P.M.1    Steelman, L.S.2    McCubrey, J.A.3
  • 110
    • 0035839844 scopus 로고    scopus 로고
    • Translocations involving c-myc and c-myc function
    • Boxer L.M., and Dang C.V. Translocations involving c-myc and c-myc function. Oncogene 20 (2001) 5595-5610
    • (2001) Oncogene , vol.20 , pp. 5595-5610
    • Boxer, L.M.1    Dang, C.V.2
  • 111
    • 20044375377 scopus 로고    scopus 로고
    • c-Myc associates with ribosomal DNA and activates RNA polymerase I transcription
    • Arabi A., Wu S., Ridderstrale K., Bierhoff H., Shiue C., Fatyol K., et al. c-Myc associates with ribosomal DNA and activates RNA polymerase I transcription. Nat Cell Biol 7 (2005) 303-310
    • (2005) Nat Cell Biol , vol.7 , pp. 303-310
    • Arabi, A.1    Wu, S.2    Ridderstrale, K.3    Bierhoff, H.4    Shiue, C.5    Fatyol, K.6
  • 113
    • 0033539555 scopus 로고    scopus 로고
    • c-Myc enhances protein synthesis and cell size during B lymphocyte development
    • Iritani B.M., and Eisenman R.N. c-Myc enhances protein synthesis and cell size during B lymphocyte development. Proc Natl Acad Sci USA 96 (1999) 13180-13185
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13180-13185
    • Iritani, B.M.1    Eisenman, R.N.2
  • 114
    • 0034633761 scopus 로고    scopus 로고
    • Induction of ribosomal genes and hepatocyte hypertrophy by adenovirus-mediated expression of c-Myc in vivo
    • Kim S., Li Q., Dang C.V., and Lee L.A. Induction of ribosomal genes and hepatocyte hypertrophy by adenovirus-mediated expression of c-Myc in vivo. Proc Natl Acad Sci USA 97 (2000) 11198-11202
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11198-11202
    • Kim, S.1    Li, Q.2    Dang, C.V.3    Lee, L.A.4
  • 115
    • 0033772338 scopus 로고    scopus 로고
    • An encore for ribosome biogenesis in the control of cell proliferation
    • Thomas G. An encore for ribosome biogenesis in the control of cell proliferation. Nat Cell Biol 2 (2000) E71-E72
    • (2000) Nat Cell Biol , vol.2
    • Thomas, G.1
  • 116
    • 57749187631 scopus 로고    scopus 로고
    • Suppression of Myc oncogenic activity by ribosomal protein haploinsufficiency
    • Barna M., Pusic A., Zollo O., Costa M., Kondrashov N., Rego E., et al. Suppression of Myc oncogenic activity by ribosomal protein haploinsufficiency. Nature 456 (2008) 971-975
    • (2008) Nature , vol.456 , pp. 971-975
    • Barna, M.1    Pusic, A.2    Zollo, O.3    Costa, M.4    Kondrashov, N.5    Rego, E.6
  • 117
    • 0842346437 scopus 로고    scopus 로고
    • Principles of tumor suppression
    • Sherr C.J. Principles of tumor suppression. Cell 116 (2004) 235-246
    • (2004) Cell , vol.116 , pp. 235-246
    • Sherr, C.J.1
  • 119
    • 0001510491 scopus 로고    scopus 로고
    • The RB and p53 pathways in cancer
    • Sherr C.J., and McCormick F. The RB and p53 pathways in cancer. Cancer Cell 2 (2002) 103-112
    • (2002) Cancer Cell , vol.2 , pp. 103-112
    • Sherr, C.J.1    McCormick, F.2
  • 120
    • 0033867975 scopus 로고    scopus 로고
    • Repression of RNA polymerase I transcription by the tumor suppressor p53
    • Zhai W., and Comai L. Repression of RNA polymerase I transcription by the tumor suppressor p53. Mol Cell Biol 20 (2000) 5930-5938
    • (2000) Mol Cell Biol , vol.20 , pp. 5930-5938
    • Zhai, W.1    Comai, L.2
  • 121
    • 0034641878 scopus 로고    scopus 로고
    • Rb and p130 regulate RNA polymerase I transcription: Rb disrupts the interaction between UBF and SL-1
    • Hannan K.M., Hannan R.D., Smith S.D., Jefferson L.S., Lun M., and Rothblum L.I. Rb and p130 regulate RNA polymerase I transcription: Rb disrupts the interaction between UBF and SL-1. Oncogene 19 (2000) 4988-4999
    • (2000) Oncogene , vol.19 , pp. 4988-4999
    • Hannan, K.M.1    Hannan, R.D.2    Smith, S.D.3    Jefferson, L.S.4    Lun, M.5    Rothblum, L.I.6
  • 122
    • 1842334436 scopus 로고    scopus 로고
    • Mechanism of repression of RNA polymerase I transcription by the retinoblastoma protein
    • Voit R., Schafer K., and Grummt I. Mechanism of repression of RNA polymerase I transcription by the retinoblastoma protein. Mol Cell Biol 17 (1997) 4230-4237
    • (1997) Mol Cell Biol , vol.17 , pp. 4230-4237
    • Voit, R.1    Schafer, K.2    Grummt, I.3
  • 123
    • 0034459686 scopus 로고    scopus 로고
    • Retinoblastoma protein disrupts interactions required for RNA polymerase III transcription
    • Sutcliffe J.E., Brown T.R., Allison S.J., Scott P.H., and White R.J. Retinoblastoma protein disrupts interactions required for RNA polymerase III transcription. Mol Cell Biol 20 (2000) 9192-9202
    • (2000) Mol Cell Biol , vol.20 , pp. 9192-9202
    • Sutcliffe, J.E.1    Brown, T.R.2    Allison, S.J.3    Scott, P.H.4    White, R.J.5
  • 124
    • 0034306996 scopus 로고    scopus 로고
    • The Rb/E2F pathway: expanding roles and emerging paradigms
    • Harbour J.W., and Dean D.C. The Rb/E2F pathway: expanding roles and emerging paradigms. Genes Dev 14 (2000) 2393-2409
    • (2000) Genes Dev , vol.14 , pp. 2393-2409
    • Harbour, J.W.1    Dean, D.C.2
  • 126
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: positive and negative regulators of G1-phase progression
    • Sherr C.J., and Roberts J.M. CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev 13 (1999) 1501-1512
    • (1999) Genes Dev , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 127
    • 33845545430 scopus 로고    scopus 로고
    • Human tumor suppressor p14ARF negatively regulates rRNA transcription and inhibits UBF1 transcription factor phosphorylation
    • Ayrault O., Andrique L., Fauvin D., Eymin B., Gazzeri S., and Seite P. Human tumor suppressor p14ARF negatively regulates rRNA transcription and inhibits UBF1 transcription factor phosphorylation. Oncogene 25 (2006) 7577-7586
    • (2006) Oncogene , vol.25 , pp. 7577-7586
    • Ayrault, O.1    Andrique, L.2    Fauvin, D.3    Eymin, B.4    Gazzeri, S.5    Seite, P.6
  • 129
    • 0035157335 scopus 로고    scopus 로고
    • Enhanced expression of S8, L12, L23a, L27 and L30 ribosomal protein mRNAs in human hepatocellular carcinoma
    • Kondoh N., Shuda M., Tanaka K., Wakatsuki T., Hada A., and Yamamoto M. Enhanced expression of S8, L12, L23a, L27 and L30 ribosomal protein mRNAs in human hepatocellular carcinoma. Anticancer Res 21 (2001) 2429-2433
    • (2001) Anticancer Res , vol.21 , pp. 2429-2433
    • Kondoh, N.1    Shuda, M.2    Tanaka, K.3    Wakatsuki, T.4    Hada, A.5    Yamamoto, M.6
  • 130
    • 0025107361 scopus 로고
    • Noncoordinated expression of S6, S11, and S14 ribosomal protein genes in leukemic blast cells
    • Ferrari S., Manfredini R., Tagliafico E., Rossi E., Donelli A., Torelli G., et al. Noncoordinated expression of S6, S11, and S14 ribosomal protein genes in leukemic blast cells. Cancer Res 50 (1990) 5825-5828
    • (1990) Cancer Res , vol.50 , pp. 5825-5828
    • Ferrari, S.1    Manfredini, R.2    Tagliafico, E.3    Rossi, E.4    Donelli, A.5    Torelli, G.6
  • 131
    • 0032482206 scopus 로고    scopus 로고
    • Altered cellular responses by varying expression of a ribosomal protein gene: sequential coordination of enhancement and suppression of ribosomal protein S3a gene expression induces apoptosis
    • Naora H., Takai I., and Adachi M. Altered cellular responses by varying expression of a ribosomal protein gene: sequential coordination of enhancement and suppression of ribosomal protein S3a gene expression induces apoptosis. J Cell Biol 141 (1998) 741-753
    • (1998) J Cell Biol , vol.141 , pp. 741-753
    • Naora, H.1    Takai, I.2    Adachi, M.3
  • 132
    • 0034674714 scopus 로고    scopus 로고
    • Proliferation, but not growth, blocked by conditional deletion of 40S ribosomal protein S6
    • Volarevic S., Stewart M.J., Ledermann B., Zilberman F., Terracciano L., Montini E., et al. Proliferation, but not growth, blocked by conditional deletion of 40S ribosomal protein S6. Science 288 (2000) 2045-2047
    • (2000) Science , vol.288 , pp. 2045-2047
    • Volarevic, S.1    Stewart, M.J.2    Ledermann, B.3    Zilberman, F.4    Terracciano, L.5    Montini, E.6
  • 133
    • 0018307730 scopus 로고
    • Multiple phosphorylation of ribosomal protein S6 during transition of quiescent 3T3 cells into early G1, and cellular compartmentalization of the phosphate donor
    • Thomas G., Siegmann M., and Gordon J. Multiple phosphorylation of ribosomal protein S6 during transition of quiescent 3T3 cells into early G1, and cellular compartmentalization of the phosphate donor. Proc Natl Acad Sci USA 76 (1979) 3952-3956
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 3952-3956
    • Thomas, G.1    Siegmann, M.2    Gordon, J.3
  • 135
    • 17944368972 scopus 로고    scopus 로고
    • An inhibitor of mTOR reduces neoplasia and normalizes p70/S6 kinase activity in Pten+/- mice
    • Podsypanina K., Lee R.T., Politis C., Hennessy I., Crane A., Puc J., et al. An inhibitor of mTOR reduces neoplasia and normalizes p70/S6 kinase activity in Pten+/- mice. Proc Natl Acad Sci USA 98 (2001) 10320-10325
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10320-10325
    • Podsypanina, K.1    Lee, R.T.2    Politis, C.3    Hennessy, I.4    Crane, A.5    Puc, J.6
  • 136
    • 0034234924 scopus 로고    scopus 로고
    • A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells
    • Sekulic A., Hudson C.C., Homme J.L., Yin P., Otterness D.M., Karnitz L.M., et al. A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells. Cancer Res 60 (2000) 3504-3513
    • (2000) Cancer Res , vol.60 , pp. 3504-3513
    • Sekulic, A.1    Hudson, C.C.2    Homme, J.L.3    Yin, P.4    Otterness, D.M.5    Karnitz, L.M.6
  • 137
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
    • Inoki K., Li Y., Zhu T., Wu J., and Guan K.L. TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat Cell Biol 4 (2002) 648-657
    • (2002) Nat Cell Biol , vol.4 , pp. 648-657
    • Inoki, K.1    Li, Y.2    Zhu, T.3    Wu, J.4    Guan, K.L.5
  • 138
    • 0141919444 scopus 로고    scopus 로고
    • Aberrant regulation of translation initiation in tumorigenesis
    • Stoneley M., and Willis A.E. Aberrant regulation of translation initiation in tumorigenesis. Curr Mol Med 3 (2003) 597-603
    • (2003) Curr Mol Med , vol.3 , pp. 597-603
    • Stoneley, M.1    Willis, A.E.2
  • 139
    • 12344281782 scopus 로고    scopus 로고
    • The implications of structured 5′ untranslated regions on translation and disease
    • Pickering B.M., and Willis A.E. The implications of structured 5′ untranslated regions on translation and disease. Semin Cell Dev Biol 16 (2005) 39-47
    • (2005) Semin Cell Dev Biol , vol.16 , pp. 39-47
    • Pickering, B.M.1    Willis, A.E.2
  • 140
    • 0032967120 scopus 로고    scopus 로고
    • Translational control of growth factor and proto-oncogene expression
    • Willis A.E. Translational control of growth factor and proto-oncogene expression. Int J Biochem Cell Biol 31 (1999) 73-86
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 73-86
    • Willis, A.E.1
  • 141
    • 0021799353 scopus 로고
    • Insertion mutagenesis to increase secondary structure within the 5′ noncoding region of a eukaryotic mRNA reduces translational efficiency
    • Pelletier J., and Sonenberg N. Insertion mutagenesis to increase secondary structure within the 5′ noncoding region of a eukaryotic mRNA reduces translational efficiency. Cell 40 (1985) 515-526
    • (1985) Cell , vol.40 , pp. 515-526
    • Pelletier, J.1    Sonenberg, N.2
  • 142
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y., Maya R., Kazaz A., and Oren M. Mdm2 promotes the rapid degradation of p53. Nature 387 (1997) 296-299
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 143
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat M.H., Jones S.N., and Vousden K.H. Regulation of p53 stability by Mdm2. Nature 387 (1997) 299-303
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 144
    • 19944431662 scopus 로고    scopus 로고
    • Enhanced Mdm2 activity inhibits pRB function via ubiquitin-dependent degradation
    • Uchida C., Miwa S., Kitagawa K., Hattori T., Isobe T., Otani S., et al. Enhanced Mdm2 activity inhibits pRB function via ubiquitin-dependent degradation. EMBO J 24 (2005) 160-169
    • (2005) EMBO J , vol.24 , pp. 160-169
    • Uchida, C.1    Miwa, S.2    Kitagawa, K.3    Hattori, T.4    Isobe, T.5    Otani, S.6
  • 145
    • 14644417208 scopus 로고    scopus 로고
    • p53-independent activities of MDM2 and their relevance to cancer therapy
    • Zhang Z., and Zhang R. p53-independent activities of MDM2 and their relevance to cancer therapy. Curr Cancer Drug Targets 5 (2005) 9-20
    • (2005) Curr Cancer Drug Targets , vol.5 , pp. 9-20
    • Zhang, Z.1    Zhang, R.2
  • 146
    • 14644437751 scopus 로고    scopus 로고
    • MDM2 is a central node in the p53 pathway: 12 years and counting
    • Bond G.L., Hu W., and Levine A.J. MDM2 is a central node in the p53 pathway: 12 years and counting. Curr Cancer Drug Targets 5 (2005) 3-8
    • (2005) Curr Cancer Drug Targets , vol.5 , pp. 3-8
    • Bond, G.L.1    Hu, W.2    Levine, A.J.3
  • 147
    • 0030795068 scopus 로고    scopus 로고
    • Translational enhancement of mdm2 oncogene expression in human tumor cells containing a stabilized wild-type p53 protein
    • Landers J.E., Cassel S.L., and George D.L. Translational enhancement of mdm2 oncogene expression in human tumor cells containing a stabilized wild-type p53 protein. Cancer Res 57 (1997) 3562-3568
    • (1997) Cancer Res , vol.57 , pp. 3562-3568
    • Landers, J.E.1    Cassel, S.L.2    George, D.L.3
  • 148
    • 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., Ronsin M., Feunteun J., Tursz T., et al. Overexpression of MDM2, due to enhanced translation, results in inactivation of wild-type p53 in Burkitt's lymphoma cells. Oncogene 16 (1998) 1603-1610
    • (1998) Oncogene , vol.16 , pp. 1603-1610
    • Capoulade, C.1    Bressac-de Paillerets, B.2    Lefrere, I.3    Ronsin, M.4    Feunteun, J.5    Tursz, T.6
  • 149
    • 0033533737 scopus 로고    scopus 로고
    • Role of two upstream open reading frames in the translational control of oncogene mdm2
    • Brown C.Y., Mize G.J., Pineda M., George D.L., and Morris D.R. Role of two upstream open reading frames in the translational control of oncogene mdm2. Oncogene 18 (1999) 5631-5637
    • (1999) Oncogene , vol.18 , pp. 5631-5637
    • Brown, C.Y.1    Mize, G.J.2    Pineda, M.3    George, D.L.4    Morris, D.R.5
  • 150
    • 0037815066 scopus 로고    scopus 로고
    • The two upstream open reading frames of oncogene mdm2 have different translational regulatory properties
    • Jin X., Turcott E., Englehardt S., Mize G.J., and Morris D.R. The two upstream open reading frames of oncogene mdm2 have different translational regulatory properties. J Biol Chem 278 (2003) 25716-25721
    • (2003) J Biol Chem , vol.278 , pp. 25716-25721
    • Jin, X.1    Turcott, E.2    Englehardt, S.3    Mize, G.J.4    Morris, D.R.5
  • 151
    • 33645003172 scopus 로고    scopus 로고
    • BRCA1: cell cycle checkpoint, genetic instability, DNA damage response and cancer evolution
    • Deng C.X. BRCA1: cell cycle checkpoint, genetic instability, DNA damage response and cancer evolution. Nucleic Acids Res 34 (2006) 1416-1426
    • (2006) Nucleic Acids Res , vol.34 , pp. 1416-1426
    • Deng, C.X.1
  • 152
    • 0028330276 scopus 로고
    • Risks of cancer in BRCA1-mutation carriers. Breast cancer linkage consortium
    • Ford D., Easton D.F., Bishop D.T., Narod S.A., and Goldgar D.E. Risks of cancer in BRCA1-mutation carriers. Breast cancer linkage consortium. Lancet 343 (1994) 692-695
    • (1994) Lancet , vol.343 , pp. 692-695
    • Ford, D.1    Easton, D.F.2    Bishop, D.T.3    Narod, S.A.4    Goldgar, D.E.5
  • 153
    • 0037130887 scopus 로고    scopus 로고
    • Cancer incidence in BRCA1 mutation carriers
    • Thompson D., and Easton D.F. Cancer incidence in BRCA1 mutation carriers. J Natl Cancer Inst 94 (2002) 1358-1365
    • (2002) J Natl Cancer Inst , vol.94 , pp. 1358-1365
    • Thompson, D.1    Easton, D.F.2
  • 155
    • 0031874053 scopus 로고    scopus 로고
    • An important role for BRCA1 in breast cancer progression is indicated by its loss in a large proportion of non-familial breast cancers
    • Taylor J., Lymboura M., Pace P.E., A'Hern R.P., Desai A.J., Shousha S., et al. An important role for BRCA1 in breast cancer progression is indicated by its loss in a large proportion of non-familial breast cancers. Int J Cancer 79 (1998) 334-342
    • (1998) Int J Cancer , vol.79 , pp. 334-342
    • Taylor, J.1    Lymboura, M.2    Pace, P.E.3    A'Hern, R.P.4    Desai, A.J.5    Shousha, S.6
  • 156
    • 0032953384 scopus 로고    scopus 로고
    • Localization of human BRCA1 and its loss in high-grade, non-inherited breast carcinomas
    • Wilson C.A., Ramos L., Villasenor M.R., Anders K.H., Press M.F., Clarke K., et al. Localization of human BRCA1 and its loss in high-grade, non-inherited breast carcinomas. Nat Genet 21 (1999) 236-240
    • (1999) Nat Genet , vol.21 , pp. 236-240
    • Wilson, C.A.1    Ramos, L.2    Villasenor, M.R.3    Anders, K.H.4    Press, M.F.5    Clarke, K.6
  • 157
    • 0037053410 scopus 로고    scopus 로고
    • Structural determinants of BRCA1 translational regulation
    • Sobczak K., and Krzyzosiak W.J. Structural determinants of BRCA1 translational regulation. J Biol Chem 277 (2002) 17349-17358
    • (2002) J Biol Chem , vol.277 , pp. 17349-17358
    • Sobczak, K.1    Krzyzosiak, W.J.2
  • 158
    • 0028153709 scopus 로고
    • Enhanced translational efficiency of a novel transforming growth factor beta 3 mRNA in human breast cancer cells
    • Arrick B.A., Grendell R.L., and Griffin L.A. Enhanced translational efficiency of a novel transforming growth factor beta 3 mRNA in human breast cancer cells. Mol Cell Biol 14 (1994) 619-628
    • (1994) Mol Cell Biol , vol.14 , pp. 619-628
    • Arrick, B.A.1    Grendell, R.L.2    Griffin, L.A.3
  • 159
    • 0025827065 scopus 로고
    • Inhibition of translation of transforming growth factor-beta 3 mRNA by its 5′ untranslated region
    • Arrick B.A., Lee A.L., Grendell R.L., and Derynck R. Inhibition of translation of transforming growth factor-beta 3 mRNA by its 5′ untranslated region. Mol Cell Biol 11 (1991) 4306-4313
    • (1991) Mol Cell Biol , vol.11 , pp. 4306-4313
    • Arrick, B.A.1    Lee, A.L.2    Grendell, R.L.3    Derynck, R.4
  • 160
    • 14644415917 scopus 로고    scopus 로고
    • Identification of novel RARbeta2 transcript variants with short 5′-UTRs in normal and cancerous breast epithelial cells
    • Peng X., Mehta R.G., Tonetti D.A., and Christov K. Identification of novel RARbeta2 transcript variants with short 5′-UTRs in normal and cancerous breast epithelial cells. Oncogene 24 (2005) 1296-1301
    • (2005) Oncogene , vol.24 , pp. 1296-1301
    • Peng, X.1    Mehta, R.G.2    Tonetti, D.A.3    Christov, K.4
  • 161
    • 63249094087 scopus 로고    scopus 로고
    • Differential usage of alternate promoters of the human stress response gene ATF3 in stress response and cancer cells
    • Miyazaki K., Inoue S., Yamada K., Watanabe M., Liu Q., Watanabe T., et al. Differential usage of alternate promoters of the human stress response gene ATF3 in stress response and cancer cells. Nucleic Acids Res 37 (2009) 1438-1451
    • (2009) Nucleic Acids Res , vol.37 , pp. 1438-1451
    • Miyazaki, K.1    Inoue, S.2    Yamada, K.3    Watanabe, M.4    Liu, Q.5    Watanabe, T.6
  • 163
    • 63549144514 scopus 로고    scopus 로고
    • The complex relationship between BRCA1 and ERalpha in hereditary breast cancer
    • Gorski J.J., Kennedy R.D., Hosey A.M., and Harkin D.P. The complex relationship between BRCA1 and ERalpha in hereditary breast cancer. Clin Cancer Res 15 (2009) 1514-1518
    • (2009) Clin Cancer Res , vol.15 , pp. 1514-1518
    • Gorski, J.J.1    Kennedy, R.D.2    Hosey, A.M.3    Harkin, D.P.4
  • 164
    • 0035958521 scopus 로고    scopus 로고
    • A somatic mutation in the 5′UTR of BRCA1 gene in sporadic breast cancer causes down-modulation of translation efficiency
    • Signori E., Bagni C., Papa S., Primerano B., Rinaldi M., Amaldi F., et al. A somatic mutation in the 5′UTR of BRCA1 gene in sporadic breast cancer causes down-modulation of translation efficiency. Oncogene 20 (2001) 4596-4600
    • (2001) Oncogene , vol.20 , pp. 4596-4600
    • Signori, E.1    Bagni, C.2    Papa, S.3    Primerano, B.4    Rinaldi, M.5    Amaldi, F.6
  • 165
    • 34547885781 scopus 로고    scopus 로고
    • A mutation in the 5′ untranslated region of the BRCA1 gene in sporadic breast cancer causes downregulation of translation efficiency
    • Wang J., Lu C., Min D., Wang Z., and Ma X. A mutation in the 5′ untranslated region of the BRCA1 gene in sporadic breast cancer causes downregulation of translation efficiency. J Int Med Res 35 (2007) 564-573
    • (2007) J Int Med Res , vol.35 , pp. 564-573
    • Wang, J.1    Lu, C.2    Min, D.3    Wang, Z.4    Ma, X.5
  • 166
    • 33750030758 scopus 로고    scopus 로고
    • The regulation of INK4/ARF in cancer and aging
    • Kim W.Y., and Sharpless N.E. The regulation of INK4/ARF in cancer and aging. Cell 127 (2006) 265-275
    • (2006) Cell , vol.127 , pp. 265-275
    • Kim, W.Y.1    Sharpless, N.E.2
  • 167
    • 0032900535 scopus 로고    scopus 로고
    • Mutation of the CDKN2A 5′ UTR creates an aberrant initiation codon and predisposes to melanoma
    • Liu L., Dilworth D., Gao L., Monzon J., Summers A., Lassam N., et al. Mutation of the CDKN2A 5′ UTR creates an aberrant initiation codon and predisposes to melanoma. Nat Genet 21 (1999) 128-132
    • (1999) Nat Genet , vol.21 , pp. 128-132
    • Liu, L.1    Dilworth, D.2    Gao, L.3    Monzon, J.4    Summers, A.5    Lassam, N.6
  • 168
    • 26644454382 scopus 로고    scopus 로고
    • Increased expression of delta-catenin/neural plakophilin-related armadillo protein is associated with the down-regulation and redistribution of E-cadherin and p120ctn in human prostate cancer
    • Lu Q., Dobbs L.J., Gregory C.W., Lanford G.W., Revelo M.P., Shappell S., et al. Increased expression of delta-catenin/neural plakophilin-related armadillo protein is associated with the down-regulation and redistribution of E-cadherin and p120ctn in human prostate cancer. Hum Pathol 36 (2005) 1037-1048
    • (2005) Hum Pathol , vol.36 , pp. 1037-1048
    • Lu, Q.1    Dobbs, L.J.2    Gregory, C.W.3    Lanford, G.W.4    Revelo, M.P.5    Shappell, S.6
  • 169
    • 59149091500 scopus 로고    scopus 로고
    • Increased nucleotide polymorphic changes in the 5′-untranslated region of delta-catenin (CTNND2) gene in prostate cancer
    • Wang T., Chen Y.H., Hong H., Zeng Y., Zhang J., Lu J.P., et al. Increased nucleotide polymorphic changes in the 5′-untranslated region of delta-catenin (CTNND2) gene in prostate cancer. Oncogene 28 (2009) 555-564
    • (2009) Oncogene , vol.28 , pp. 555-564
    • Wang, T.1    Chen, Y.H.2    Hong, H.3    Zeng, Y.4    Zhang, J.5    Lu, J.P.6
  • 170
    • 31544462629 scopus 로고    scopus 로고
    • Thymidylate synthase pharmacogenetics
    • Marsh S. Thymidylate synthase pharmacogenetics. Invest New Drugs 23 (2005) 533-537
    • (2005) Invest New Drugs , vol.23 , pp. 533-537
    • Marsh, S.1
  • 171
    • 0035671827 scopus 로고    scopus 로고
    • Different lengths of a polymorphic repeat sequence in the thymidylate synthase gene affect translational efficiency but not its gene expression
    • Kawakami K., Salonga D., Park J.M., Danenberg K.D., Uetake H., Brabender J., et al. Different lengths of a polymorphic repeat sequence in the thymidylate synthase gene affect translational efficiency but not its gene expression. Clin Cancer Res 7 (2001) 4096-4101
    • (2001) Clin Cancer Res , vol.7 , pp. 4096-4101
    • Kawakami, K.1    Salonga, D.2    Park, J.M.3    Danenberg, K.D.4    Uetake, H.5    Brabender, J.6
  • 172
    • 2342421272 scopus 로고    scopus 로고
    • Targeting translation for treatment of cancer-a novel role for IRES?
    • Holcik M. Targeting translation for treatment of cancer-a novel role for IRES?. Curr Cancer Drug Targets 4 (2004) 299-311
    • (2004) Curr Cancer Drug Targets , vol.4 , pp. 299-311
    • Holcik, M.1
  • 173
    • 0034618402 scopus 로고    scopus 로고
    • A mutation in the c-myc-IRES leads to enhanced internal ribosome entry in multiple myeloma: a novel mechanism of oncogene de-regulation
    • Chappell S.A., LeQuesne J.P., Paulin F.E., deSchoolmeester M.L., Stoneley M., Soutar R.L., et al. A mutation in the c-myc-IRES leads to enhanced internal ribosome entry in multiple myeloma: a novel mechanism of oncogene de-regulation. Oncogene 19 (2000) 4437-4440
    • (2000) Oncogene , vol.19 , pp. 4437-4440
    • Chappell, S.A.1    LeQuesne, J.P.2    Paulin, F.E.3    deSchoolmeester, M.L.4    Stoneley, M.5    Soutar, R.L.6
  • 174
    • 0345549480 scopus 로고    scopus 로고
    • Members of the poly (rC) binding protein family stimulate the activity of the c-myc internal ribosome entry segment in vitro and in vivo
    • Evans J.R., Mitchell S.A., Spriggs K.A., Ostrowski J., Bomsztyk K., Ostarek D., et al. Members of the poly (rC) binding protein family stimulate the activity of the c-myc internal ribosome entry segment in vitro and in vivo. Oncogene 22 (2003) 8012-8020
    • (2003) Oncogene , vol.22 , pp. 8012-8020
    • Evans, J.R.1    Mitchell, S.A.2    Spriggs, K.A.3    Ostrowski, J.4    Bomsztyk, K.5    Ostarek, D.6
  • 175
    • 57749102689 scopus 로고    scopus 로고
    • IL-6-induced stimulation of c-myc translation in multiple myeloma cells is mediated by myc internal ribosome entry site function and the RNA-binding protein, hnRNP A1
    • Shi Y., Frost P.J., Hoang B.Q., Benavides A., Sharma S., Gera J.F., et al. IL-6-induced stimulation of c-myc translation in multiple myeloma cells is mediated by myc internal ribosome entry site function and the RNA-binding protein, hnRNP A1. Cancer Res 68 (2008) 10215-10222
    • (2008) Cancer Res , vol.68 , pp. 10215-10222
    • Shi, Y.1    Frost, P.J.2    Hoang, B.Q.3    Benavides, A.4    Sharma, S.5    Gera, J.F.6
  • 176
    • 0034710543 scopus 로고    scopus 로고
    • Translational upregulation of X-linked inhibitor of apoptosis (XIAP) increases resistance to radiation induced cell death
    • Holcik M., Yeh C., Korneluk R.G., and Chow T. Translational upregulation of X-linked inhibitor of apoptosis (XIAP) increases resistance to radiation induced cell death. Oncogene 19 (2000) 4174-4177
    • (2000) Oncogene , vol.19 , pp. 4174-4177
    • Holcik, M.1    Yeh, C.2    Korneluk, R.G.3    Chow, T.4
  • 178
    • 34047226825 scopus 로고    scopus 로고
    • Aberrant regulation of messenger RNA 3′-untranslated region in human cancer
    • Lopez de Silanes I., Quesada M.P., and Esteller M. Aberrant regulation of messenger RNA 3′-untranslated region in human cancer. Cell Oncol 29 (2007) 1-17
    • (2007) Cell Oncol , vol.29 , pp. 1-17
    • Lopez de Silanes, I.1    Quesada, M.P.2    Esteller, M.3
  • 179
    • 0035213198 scopus 로고    scopus 로고
    • Altered expression of the mRNA stability factor HuR promotes cyclooxygenase-2 expression in colon cancer cells
    • Dixon D.A., Tolley N.D., King P.H., Nabors L.B., McIntyre T.M., Zimmerman G.A., et al. Altered expression of the mRNA stability factor HuR promotes cyclooxygenase-2 expression in colon cancer cells. J Clin Invest 108 (2001) 1657-1665
    • (2001) J Clin Invest , vol.108 , pp. 1657-1665
    • Dixon, D.A.1    Tolley, N.D.2    King, P.H.3    Nabors, L.B.4    McIntyre, T.M.5    Zimmerman, G.A.6
  • 180
    • 65349120262 scopus 로고    scopus 로고
    • The mRNA binding proteins HuR and tristetraprolin regulate cyclooxygenase 2 expression during colon carcinogenesis
    • Young L.E., Sanduja S., Bemis-Standoli K., Pena E.A., Price R.L., and Dixon D.A. The mRNA binding proteins HuR and tristetraprolin regulate cyclooxygenase 2 expression during colon carcinogenesis. Gastroenterology 136 (2009) 1669-1679
    • (2009) Gastroenterology , vol.136 , pp. 1669-1679
    • Young, L.E.1    Sanduja, S.2    Bemis-Standoli, K.3    Pena, E.A.4    Price, R.L.5    Dixon, D.A.6
  • 181
    • 38349169664 scopus 로고    scopus 로고
    • Mechanisms of post-transcriptional regulation by microRNAs: are the answers in sight?
    • Filipowicz W., Bhattacharyya S.N., and Sonenberg N. Mechanisms of post-transcriptional regulation by microRNAs: are the answers in sight?. Nat Rev Genet 9 (2008) 102-114
    • (2008) Nat Rev Genet , vol.9 , pp. 102-114
    • Filipowicz, W.1    Bhattacharyya, S.N.2    Sonenberg, N.3
  • 182
    • 58249088751 scopus 로고    scopus 로고
    • MicroRNAs: target recognition and regulatory functions
    • Bartel D.P. MicroRNAs: target recognition and regulatory functions. Cell 136 (2009) 215-233
    • (2009) Cell , vol.136 , pp. 215-233
    • Bartel, D.P.1
  • 183
    • 67349217986 scopus 로고    scopus 로고
    • Molecular mechanisms of mTOR-mediated translational control
    • Ma X.M., and Blenis J. Molecular mechanisms of mTOR-mediated translational control. Nat Rev Mol Cell Biol 10 (2009) 307-318
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 307-318
    • Ma, X.M.1    Blenis, J.2
  • 185
    • 34347220473 scopus 로고    scopus 로고
    • Defining the role of mTOR in cancer
    • Guertin D.A., and Sabatini D.M. Defining the role of mTOR in cancer. Cancer Cell 12 (2007) 9-22
    • (2007) Cancer Cell , vol.12 , pp. 9-22
    • Guertin, D.A.1    Sabatini, D.M.2
  • 186
    • 61449235398 scopus 로고    scopus 로고
    • Not all substrates are treated equally: implications for mTOR, rapamycin-resistance and cancer therapy
    • Choo A.Y., and Blenis J. Not all substrates are treated equally: implications for mTOR, rapamycin-resistance and cancer therapy. Cell Cycle 8 (2009) 567-572
    • (2009) Cell Cycle , vol.8 , pp. 567-572
    • Choo, A.Y.1    Blenis, J.2
  • 187
    • 54949109808 scopus 로고    scopus 로고
    • PI3K/Akt: getting it right matters
    • Franke T.F. PI3K/Akt: getting it right matters. Oncogene 27 (2008) 6473-6488
    • (2008) Oncogene , vol.27 , pp. 6473-6488
    • Franke, T.F.1
  • 188
    • 33745307617 scopus 로고    scopus 로고
    • Ras, PI(3)K and mTOR signalling controls tumour cell growth
    • Shaw R.J., and Cantley L.C. Ras, PI(3)K and mTOR signalling controls tumour cell growth. Nature 441 (2006) 424-430
    • (2006) Nature , vol.441 , pp. 424-430
    • Shaw, R.J.1    Cantley, L.C.2
  • 189
    • 63749086305 scopus 로고    scopus 로고
    • ErbB receptors and signaling pathways in cancer
    • Hynes N.E., and MacDonald G. ErbB receptors and signaling pathways in cancer. Curr Opin Cell Biol 21 (2009) 177-184
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 177-184
    • Hynes, N.E.1    MacDonald, G.2
  • 190
    • 65949092291 scopus 로고    scopus 로고
    • PIK3CA mutations in human solid tumors: role in sensitivity to various therapeutic approaches
    • Ligresti G., Militello L., Steelman L.S., Cavallaro A., Basile F., Nicoletti F., et al. PIK3CA mutations in human solid tumors: role in sensitivity to various therapeutic approaches. Cell Cycle 8 (2009) 1352-1358
    • (2009) Cell Cycle , vol.8 , pp. 1352-1358
    • Ligresti, G.1    Militello, L.2    Steelman, L.S.3    Cavallaro, A.4    Basile, F.5    Nicoletti, F.6
  • 191
    • 51849086880 scopus 로고    scopus 로고
    • PTEN: a new guardian of the genome
    • Yin Y., and Shen W.H. PTEN: a new guardian of the genome. Oncogene 27 (2008) 5443-5453
    • (2008) Oncogene , vol.27 , pp. 5443-5453
    • Yin, Y.1    Shen, W.H.2
  • 192
    • 0037178781 scopus 로고    scopus 로고
    • Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action
    • 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 110 (2002) 177-189
    • (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
  • 193
    • 0037178786 scopus 로고    scopus 로고
    • mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery
    • Kim D.H., Sarbassov D.D., Ali S.M., King J.E., Latek R.R., Erdjument-Bromage H., et al. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110 (2002) 163-175
    • (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
  • 194
    • 0037623417 scopus 로고    scopus 로고
    • GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR
    • Kim D.H., Sarbassov D.D., Ali S.M., Latek R.R., Guntur K.V., Erdjument-Bromage H., et al. GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR. Mol Cell 11 (2003) 895-904
    • (2003) Mol Cell , vol.11 , pp. 895-904
    • Kim, D.H.1    Sarbassov, D.D.2    Ali, S.M.3    Latek, R.R.4    Guntur, K.V.5    Erdjument-Bromage, H.6
  • 195
    • 65949113601 scopus 로고    scopus 로고
    • Targeting mTOR with rapamycin: one dose does not fit all
    • Foster D.A., and Toschi A. Targeting mTOR with rapamycin: one dose does not fit all. Cell Cycle 8 (2009) 1026-1029
    • (2009) Cell Cycle , vol.8 , pp. 1026-1029
    • Foster, D.A.1    Toschi, A.2
  • 197
    • 59749090661 scopus 로고    scopus 로고
    • Activation of mTORC1 in two steps: Rheb-GTP activation of catalytic function and increased binding of substrates to raptor
    • Avruch J., Long X., Lin Y., Ortiz-Vega S., Rapley J., Papageorgiou A., et al. Activation of mTORC1 in two steps: Rheb-GTP activation of catalytic function and increased binding of substrates to raptor. Biochem Soc Trans 37 (2009) 223-226
    • (2009) Biochem Soc Trans , vol.37 , pp. 223-226
    • Avruch, J.1    Long, X.2    Lin, Y.3    Ortiz-Vega, S.4    Rapley, J.5    Papageorgiou, A.6
  • 198
    • 0041758428 scopus 로고    scopus 로고
    • Tuberous sclerosis: from tubers to mTOR
    • Kwiatkowski D.J. Tuberous sclerosis: from tubers to mTOR. Ann Hum Genet 67 (2003) 87-96
    • (2003) Ann Hum Genet , vol.67 , pp. 87-96
    • Kwiatkowski, D.J.1
  • 199
    • 37049024761 scopus 로고    scopus 로고
    • c-myc Repression of TSC2 contributes to control of translation initiation and Myc-induced transformation
    • Ravitz M.J., Chen L., Lynch M., and Schmidt E.V. c-myc Repression of TSC2 contributes to control of translation initiation and Myc-induced transformation. Cancer Res 67 (2007) 11209-11217
    • (2007) Cancer Res , vol.67 , pp. 11209-11217
    • Ravitz, M.J.1    Chen, L.2    Lynch, M.3    Schmidt, E.V.4
  • 200
    • 65949122722 scopus 로고    scopus 로고
    • Growth controls connect: interactions between c-myc and the tuberous sclerosis complex-mTOR pathway
    • Schmidt E.V., Ravitz M.J., Chen L., and Lynch M. Growth controls connect: interactions between c-myc and the tuberous sclerosis complex-mTOR pathway. Cell Cycle 8 (2009) 1344-1351
    • (2009) Cell Cycle , vol.8 , pp. 1344-1351
    • Schmidt, E.V.1    Ravitz, M.J.2    Chen, L.3    Lynch, M.4
  • 201
    • 50049125036 scopus 로고    scopus 로고
    • Aberrant Rheb-mediated mTORC1 activation and Pten haploinsufficiency are cooperative oncogenic events
    • Nardella C., Chen Z., Salmena L., Carracedo A., Alimonti A., Egia A., et al. Aberrant Rheb-mediated mTORC1 activation and Pten haploinsufficiency are cooperative oncogenic events. Genes Dev 22 (2008) 2172-2177
    • (2008) Genes Dev , vol.22 , pp. 2172-2177
    • Nardella, C.1    Chen, Z.2    Salmena, L.3    Carracedo, A.4    Alimonti, A.5    Egia, A.6
  • 203
    • 33646550165 scopus 로고    scopus 로고
    • Hypoxia inhibits protein synthesis through a 4E-BP1 and elongation factor 2 kinase pathway controlled by mTOR and uncoupled in breast cancer cells
    • Connolly E., Braunstein S., Formenti S., and Schneider R.J. Hypoxia inhibits protein synthesis through a 4E-BP1 and elongation factor 2 kinase pathway controlled by mTOR and uncoupled in breast cancer cells. Mol Cell Biol 26 (2006) 3955-3965
    • (2006) Mol Cell Biol , vol.26 , pp. 3955-3965
    • Connolly, E.1    Braunstein, S.2    Formenti, S.3    Schneider, R.J.4
  • 205
    • 26044474979 scopus 로고    scopus 로고
    • Expression of proline-rich Akt-substrate PRAS40 in cell survival pathway and carcinogenesis
    • Huang B., and Porter G. Expression of proline-rich Akt-substrate PRAS40 in cell survival pathway and carcinogenesis. Acta Pharmacol Sin 26 (2005) 1253-1258
    • (2005) Acta Pharmacol Sin , vol.26 , pp. 1253-1258
    • Huang, B.1    Porter, G.2
  • 206
    • 34248545489 scopus 로고    scopus 로고
    • PRAS40 deregulates apoptosis in malignant melanoma
    • Madhunapantula S.V., Sharma A., and Robertson G.P. PRAS40 deregulates apoptosis in malignant melanoma. Cancer Res 67 (2007) 3626-3636
    • (2007) Cancer Res , vol.67 , pp. 3626-3636
    • Madhunapantula, S.V.1    Sharma, A.2    Robertson, G.P.3
  • 207
    • 61349084198 scopus 로고    scopus 로고
    • Increased STAT-3 and synchronous activation of Raf-1-MEK-1-MAPK, and phosphatidylinositol 3-kinase-Akt-mTOR pathways in atypical and anaplastic meningiomas
    • Johnson M.D., O'Connell M., Vito F., and Bakos R.S. Increased STAT-3 and synchronous activation of Raf-1-MEK-1-MAPK, and phosphatidylinositol 3-kinase-Akt-mTOR pathways in atypical and anaplastic meningiomas. J Neurooncol 92 (2009) 129-136
    • (2009) J Neurooncol , vol.92 , pp. 129-136
    • Johnson, M.D.1    O'Connell, M.2    Vito, F.3    Bakos, R.S.4
  • 208
    • 0032431032 scopus 로고    scopus 로고
    • The PTEN/MMAC1 tumor suppressor phosphatase functions as a negative regulator of the phosphoinositide 3-kinase/Akt pathway
    • Wu X., Senechal K., Neshat M.S., Whang Y.E., and Sawyers C.L. The PTEN/MMAC1 tumor suppressor phosphatase functions as a negative regulator of the phosphoinositide 3-kinase/Akt pathway. Proc Natl Acad Sci USA 95 (1998) 15587-15591
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15587-15591
    • Wu, X.1    Senechal, K.2    Neshat, M.S.3    Whang, Y.E.4    Sawyers, C.L.5
  • 209
    • 6044223545 scopus 로고    scopus 로고
    • Activation of the Akt/mammalian target of rapamycin/4E-BP1 pathway by ErbB2 overexpression predicts tumor progression in breast cancers
    • Zhou X., Tan M., Stone Hawthorne V., Klos K.S., Lan K.H., Yang Y., et al. Activation of the Akt/mammalian target of rapamycin/4E-BP1 pathway by ErbB2 overexpression predicts tumor progression in breast cancers. Clin Cancer Res 10 (2004) 6779-6788
    • (2004) Clin Cancer Res , vol.10 , pp. 6779-6788
    • Zhou, X.1    Tan, M.2    Stone Hawthorne, V.3    Klos, K.S.4    Lan, K.H.5    Yang, Y.6
  • 210
    • 52049093470 scopus 로고    scopus 로고
    • Comparison of Akt/mTOR signaling in primary breast tumors and matched distant metastases
    • Akcakanat A., Sahin A., Shaye A.N., Velasco M.A., and Meric-Bernstam F. Comparison of Akt/mTOR signaling in primary breast tumors and matched distant metastases. Cancer 112 (2008) 2352-2358
    • (2008) Cancer , vol.112 , pp. 2352-2358
    • Akcakanat, A.1    Sahin, A.2    Shaye, A.N.3    Velasco, M.A.4    Meric-Bernstam, F.5
  • 211
    • 42949109848 scopus 로고    scopus 로고
    • The splicing factor SF2/ASF regulates translation initiation by enhancing phosphorylation of 4E-BP1
    • Michlewski G., Sanford J.R., and Caceres J.F. The splicing factor SF2/ASF regulates translation initiation by enhancing phosphorylation of 4E-BP1. Mol Cell 30 (2008) 179-189
    • (2008) Mol Cell , vol.30 , pp. 179-189
    • Michlewski, G.1    Sanford, J.R.2    Caceres, J.F.3
  • 213
    • 0037363075 scopus 로고    scopus 로고
    • Does the ribosome translate cancer?
    • Ruggero D., and Pandolfi P.P. Does the ribosome translate cancer?. Nat Rev Cancer 3 (2003) 179-192
    • (2003) Nat Rev Cancer , vol.3 , pp. 179-192
    • Ruggero, D.1    Pandolfi, P.P.2
  • 214
    • 53049084191 scopus 로고    scopus 로고
    • S6K1 plays a key role in glial transformation
    • Nakamura J.L., Garcia E., and Pieper R.O. S6K1 plays a key role in glial transformation. Cancer Res 68 (2008) 6516-6523
    • (2008) Cancer Res , vol.68 , pp. 6516-6523
    • Nakamura, J.L.1    Garcia, E.2    Pieper, R.O.3
  • 215
    • 27744569843 scopus 로고    scopus 로고
    • mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events
    • Holz M.K., Ballif B.A., Gygi S.P., and Blenis J. mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 123 (2005) 569-580
    • (2005) Cell , vol.123 , pp. 569-580
    • Holz, M.K.1    Ballif, B.A.2    Gygi, S.P.3    Blenis, J.4
  • 216
    • 33745570504 scopus 로고    scopus 로고
    • The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity
    • Shahbazian D., Roux P.P., Mieulet V., Cohen M.S., Raught B., Taunton J., et al. The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity. EMBO J 25 (2006) 2781-2791
    • (2006) EMBO J , vol.25 , pp. 2781-2791
    • Shahbazian, D.1    Roux, P.P.2    Mieulet, V.3    Cohen, M.S.4    Raught, B.5    Taunton, J.6
  • 218
  • 219
    • 43749110929 scopus 로고    scopus 로고
    • Suppression of programmed cell death 4 (PDCD4) protein expression by BCR-ABL-regulated engagement of the mTOR/p70 S6 kinase pathway
    • Carayol N., Katsoulidis E., Sassano A., Altman J.K., Druker B.J., and Platanias L.C. Suppression of programmed cell death 4 (PDCD4) protein expression by BCR-ABL-regulated engagement of the mTOR/p70 S6 kinase pathway. J Biol Chem 283 (2008) 8601-8610
    • (2008) J Biol Chem , vol.283 , pp. 8601-8610
    • Carayol, N.1    Katsoulidis, E.2    Sassano, A.3    Altman, J.K.4    Druker, B.J.5    Platanias, L.C.6
  • 220
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
    • Waskiewicz A.J., Flynn A., Proud C.G., and Cooper J.A. Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J 16 (1997) 1909-1920
    • (1997) EMBO J , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3    Cooper, J.A.4
  • 221
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E
    • Pyronnet S., Imataka H., Gingras A.C., Fukunaga R., Hunter T., and Sonenberg N. Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E. EMBO J 18 (1999) 270-279
    • (1999) EMBO J , vol.18 , pp. 270-279
    • Pyronnet, S.1    Imataka, H.2    Gingras, A.C.3    Fukunaga, R.4    Hunter, T.5    Sonenberg, N.6
  • 222
    • 60949110722 scopus 로고    scopus 로고
    • Modelling oncogenic Ras/Raf signalling in the mouse
    • Karreth F.A., and Tuveson D.A. Modelling oncogenic Ras/Raf signalling in the mouse. Curr Opin Genet Dev 19 (2009) 4-11
    • (2009) Curr Opin Genet Dev , vol.19 , pp. 4-11
    • Karreth, F.A.1    Tuveson, D.A.2
  • 224
    • 9244228003 scopus 로고    scopus 로고
    • Phosphorylation of the eukaryotic translation initiation factor eIF4E contributes to its transformation and mRNA transport activities
    • Topisirovic I., Ruiz-Gutierrez M., and Borden K.L. Phosphorylation of the eukaryotic translation initiation factor eIF4E contributes to its transformation and mRNA transport activities. Cancer Res 64 (2004) 8639-8642
    • (2004) Cancer Res , vol.64 , pp. 8639-8642
    • Topisirovic, I.1    Ruiz-Gutierrez, M.2    Borden, K.L.3
  • 225
    • 57349100323 scopus 로고    scopus 로고
    • Phosphorylation of eIF4E by MNKs supports protein synthesis, cell cycle progression and proliferation in prostate cancer cells
    • Bianchini A., Loiarro M., Bielli P., Busa R., Paronetto M.P., Loreni F., et al. Phosphorylation of eIF4E by MNKs supports protein synthesis, cell cycle progression and proliferation in prostate cancer cells. Carcinogenesis 29 (2008) 2279-2288
    • (2008) Carcinogenesis , vol.29 , pp. 2279-2288
    • Bianchini, A.1    Loiarro, M.2    Bielli, P.3    Busa, R.4    Paronetto, M.P.5    Loreni, F.6
  • 226
    • 68349135032 scopus 로고    scopus 로고
    • Regulation of autophagy through multiple independent hypoxic signaling pathways
    • Rouschop K.M., and Wouters B.G. Regulation of autophagy through multiple independent hypoxic signaling pathways. Curr Mol Med 9 (2009) 417-424
    • (2009) Curr Mol Med , vol.9 , pp. 417-424
    • Rouschop, K.M.1    Wouters, B.G.2
  • 227
    • 32444433450 scopus 로고    scopus 로고
    • Hypoxia-induced energy stress regulates mRNA translation and cell growth
    • Liu L., Cash T.P., Jones R.G., Keith B., Thompson C.B., and Simon M.C. Hypoxia-induced energy stress regulates mRNA translation and cell growth. Mol Cell 21 (2006) 521-531
    • (2006) Mol Cell , vol.21 , pp. 521-531
    • Liu, L.1    Cash, T.P.2    Jones, R.G.3    Keith, B.4    Thompson, C.B.5    Simon, M.C.6
  • 228
    • 38349056675 scopus 로고    scopus 로고
    • Hypoxia regulates TSC1/2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttling
    • DeYoung M.P., Horak P., Sofer A., Sgroi D., and Ellisen L.W. Hypoxia regulates TSC1/2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttling. Genes Dev 22 (2008) 239-251
    • (2008) Genes Dev , vol.22 , pp. 239-251
    • DeYoung, M.P.1    Horak, P.2    Sofer, A.3    Sgroi, D.4    Ellisen, L.W.5
  • 229
    • 1642355123 scopus 로고    scopus 로고
    • A novel mTOR-regulated phosphorylation site in elongation factor 2 kinase modulates the activity of the kinase and its binding to calmodulin
    • Browne G.J., and Proud C.G. A novel mTOR-regulated phosphorylation site in elongation factor 2 kinase modulates the activity of the kinase and its binding to calmodulin. Mol Cell Biol 24 (2004) 2986-2997
    • (2004) Mol Cell Biol , vol.24 , pp. 2986-2997
    • Browne, G.J.1    Proud, C.G.2
  • 230
    • 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., Alessi D.R., and Proud C.G. Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase. EMBO J 20 (2001) 4370-4379
    • (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
  • 231
    • 33846199233 scopus 로고    scopus 로고
    • Hypoxia-inducible factors: central regulators of the tumor phenotype
    • Gordan J.D., and Simon M.C. Hypoxia-inducible factors: central regulators of the tumor phenotype. Curr Opin Genet Dev 17 (2007) 71-77
    • (2007) Curr Opin Genet Dev , vol.17 , pp. 71-77
    • Gordan, J.D.1    Simon, M.C.2
  • 232
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • Holcik M., and Sonenberg N. Translational control in stress and apoptosis. Nat Rev Mol Cell Biol 6 (2005) 318-327
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 233
    • 64249128769 scopus 로고    scopus 로고
    • The molecular mechanisms that underlie the tumor suppressor function of LKB1
    • Fan D., Ma C., and Zhang H. The molecular mechanisms that underlie the tumor suppressor function of LKB1. Acta Biochim Biophys Sin (Shanghai) 41 (2009) 97-107
    • (2009) Acta Biochim Biophys Sin (Shanghai) , vol.41 , pp. 97-107
    • Fan, D.1    Ma, C.2    Zhang, H.3
  • 234
    • 0036837864 scopus 로고    scopus 로고
    • Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha
    • Koumenis C., Naczki C., Koritzinsky M., Rastani S., Diehl A., Sonenberg N., et al. Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha. Mol Cell Biol 22 (2002) 7405-7416
    • (2002) Mol Cell Biol , vol.22 , pp. 7405-7416
    • Koumenis, C.1    Naczki, C.2    Koritzinsky, M.3    Rastani, S.4    Diehl, A.5    Sonenberg, N.6
  • 235


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