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Volumn 7, Issue 9, 1996, Pages 1157-1166

Effect of decreased fte-1 gene expression on protein synthesis, cell growth, and transformation

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA;

EID: 0029828041     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (36)

References (70)
  • 1
    • 0023646759 scopus 로고
    • Revenants of v-fos-transformed fibroblasts have mutations in cellular genes essential for transformation by other oncogenes
    • Zarbl, H., Latreille, J., and Jolicoeur, P. Revenants of v-fos-transformed fibroblasts have mutations in cellular genes essential for transformation by other oncogenes. Cell, 51: 357-369, 1987.
    • (1987) Cell , vol.51 , pp. 357-369
    • Zarbl, H.1    Latreille, J.2    Jolicoeur, P.3
  • 2
    • 0025784553 scopus 로고
    • Transformation effector and suppressor genes
    • Boylan, M. O., and Zarbl, H. Transformation effector and suppressor genes. J. Cell. Biochem., 46: 199-205, 1991.
    • (1991) J. Cell. Biochem. , vol.46 , pp. 199-205
    • Boylan, M.O.1    Zarbl, H.2
  • 3
    • 2342520813 scopus 로고
    • Detection of genes with a potential for suppressing the transformed phenotype associated with activated ras genes
    • Noda, M., Kitayama, H., Matsuzaki, T., Sugimoto, Y., Okayama, H., Bassin, R. H., and Ikawa, Y. Detection of genes with a potential for suppressing the transformed phenotype associated with activated ras genes. Proc. Natl. Acad. Sci. USA, 86: 162-166, 1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 162-166
    • Noda, M.1    Kitayama, H.2    Matsuzaki, T.3    Sugimoto, Y.4    Okayama, H.5    Bassin, R.H.6    Ikawa, Y.7
  • 4
    • 2142764184 scopus 로고
    • Partial reversion of the transformed phenotype in H-ras-transfected tumorigenic cells by transfer of a human gene
    • Schafer, R., Iyer, J., Iten, E., and Nirkko, A. C. Partial reversion of the transformed phenotype in H-ras-transfected tumorigenic cells by transfer of a human gene. Proc. Natl. Acad. Sci. USA, 85: 1590-1594, 1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1590-1594
    • Schafer, R.1    Iyer, J.2    Iten, E.3    Nirkko, A.C.4
  • 5
    • 0026338842 scopus 로고
    • Evidence for human DNA-mediated transfer of the suppressed phenotype into malignant Chinese hamster cells
    • Schafer, R., Nirkko, A. C., Ambuhl, P. M., Grzeschik, K-H., and Schwarte-Waldhoff, I. Evidence for human DNA-mediated transfer of the suppressed phenotype into malignant Chinese hamster cells. Oncogene, 6: 2221-2228, 1991.
    • (1991) Oncogene , vol.6 , pp. 2221-2228
    • Schafer, R.1    Nirkko, A.C.2    Ambuhl, P.M.3    Grzeschik, K.-H.4    Schwarte-Waldhoff, I.5
  • 6
    • 0026580801 scopus 로고
    • Fte-1, a v-fos transformation effector gene, encodes the mammalian homologue of a yeast gene involved in protein import into mitochondria
    • Kho, C. J., and Zarbl, H. Fte-1, a v-fos transformation effector gene, encodes the mammalian homologue of a yeast gene involved in protein import into mitochondria. Proc. Natl. Acad. Sci. USA, 89: 2200-2204, 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2200-2204
    • Kho, C.J.1    Zarbl, H.2
  • 7
    • 0026035390 scopus 로고
    • Mitochondrial protein import: Isolation and characterization of the Saccharomyces cerevisiae MFT1 gene
    • Garrett, J. M., Singh, K. K., Vonder Haar, R. A., and Emr, S. D. Mitochondrial protein import: isolation and characterization of the Saccharomyces cerevisiae MFT1 gene. Mol. & Gen. Genet., 225; 483-491, 1991.
    • (1991) Mol. & Gen. Genet. , vol.225 , pp. 483-491
    • Garrett, J.M.1    Singh, K.K.2    Vonder Haar, R.A.3    Emr, S.D.4
  • 8
    • 0026612309 scopus 로고
    • Aminoterminal acetylation of ribosomal proteins of Saccharomyces cerevisiae
    • Takakura, H., Tsunasawa, S., Miyagi, M., and Warner, J. R. Aminoterminal acetylation of ribosomal proteins of Saccharomyces cerevisiae. J. Biol. Chem., 267: 5442-5445, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5442-5445
    • Takakura, H.1    Tsunasawa, S.2    Miyagi, M.3    Warner, J.R.4
  • 9
    • 0026223669 scopus 로고
    • Identification of a novel S-phase-specific gene during the cell cycle in synchronous cultures of Catharanthus roseus cells
    • Ito, M., Kodama, H., and Komamine, A. Identification of a novel S-phase-specific gene during the cell cycle in synchronous cultures of Catharanthus roseus cells. Plant J., 1: 141-148, 1991.
    • (1991) Plant J. , vol.1 , pp. 141-148
    • Ito, M.1    Kodama, H.2    Komamine, A.3
  • 10
    • 0028371995 scopus 로고
    • Isolation and characterization of a rice cDNA similar to cyc07
    • Kidou, S., Umeda, M., Tsuge, T., Kato, A., and Uchimiya, H. Isolation and characterization of a rice cDNA similar to cyc07. Plant Mol. Biol., 24: 545-547, 1994.
    • (1994) Plant Mol. Biol. , vol.24 , pp. 545-547
    • Kidou, S.1    Umeda, M.2    Tsuge, T.3    Kato, A.4    Uchimiya, H.5
  • 11
    • 0026749327 scopus 로고
    • Tumor necrosis factor induces genes involved in inflammation, cellular and tissue repair, and metabolism in murine fibroblasts
    • Gordon, H. M., Kucera, G., Salvo, R., and Boss, J. M. Tumor necrosis factor induces genes involved in inflammation, cellular and tissue repair, and metabolism in murine fibroblasts. J. Immunol., 148: 4021-4027, 1992.
    • (1992) J. Immunol. , vol.148 , pp. 4021-4027
    • Gordon, H.M.1    Kucera, G.2    Salvo, R.3    Boss, J.M.4
  • 12
    • 0026574084 scopus 로고
    • A gene family homologous to the S-phase-specific gene in higher plants is essential for cell proliferation in Saccharomyces cerevisiae
    • Ito, M., Yasui, A., and Komamine, A. A gene family homologous to the S-phase-specific gene in higher plants is essential for cell proliferation in Saccharomyces cerevisiae. FEBS Lett., 301: 29-33, 1992.
    • (1992) FEBS Lett. , vol.301 , pp. 29-33
    • Ito, M.1    Yasui, A.2    Komamine, A.3
  • 13
    • 0026658021 scopus 로고
    • Human ribosomal protein S3a: Cloning of the cDNA and primary structure of the protein
    • Metspalu, A., Rebane, A., Hoth, S., Pooga, M., Stahl, J., and Kruppa, J. Human ribosomal protein S3a: cloning of the cDNA and primary structure of the protein. Gene (Amst.), 119: 313-316, 1992.
    • (1992) Gene (Amst.) , vol.119 , pp. 313-316
    • Metspalu, A.1    Rebane, A.2    Hoth, S.3    Pooga, M.4    Stahl, J.5    Kruppa, J.6
  • 14
    • 0025943409 scopus 로고
    • Expression of antisense RNA against initiation factor elF-4E mRNA in HeLa cells results in lengthened cell division times, diminished translation rates, and reduced levels of both elF-4E and the p220 component of elF-4E
    • de Benedetti, A., Joshi-Barve, S., Rinker-Schaeffe, C., and Rhoads, R. E. Expression of antisense RNA against initiation factor elF-4E mRNA in HeLa cells results in lengthened cell division times, diminished translation rates, and reduced levels of both elF-4E and the p220 component of elF-4E. Mol. Cell. Biol., 11: 5435-5445, 1991.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5435-5445
    • De Benedetti, A.1    Joshi-Barve, S.2    Rinker-Schaeffe, C.3    Rhoads, R.E.4
  • 15
    • 0025107684 scopus 로고
    • Overexpression of eukaryotic protein synthesis initiation factor 4E in HeLa cells results in aberrant growth and morphology
    • de Benedetti, A., and Rhoads, R. E. Overexpression of eukaryotic protein synthesis initiation factor 4E in HeLa cells results in aberrant growth and morphology. Proc. Natl. Acad. Sci. USA, 87: 8212-8216, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8212-8216
    • Benedetti, A.1    Rhoads, R.E.2
  • 16
    • 0025314596 scopus 로고
    • Malignant transformation by eukaryotic initiation factor subunit that binds to a mRNA 5′ cap
    • Lazaris-Karatzas, A., Montine, K. S., and Sonenberg, N. Malignant transformation by eukaryotic initiation factor subunit that binds to a mRNA 5′ cap. Nature (Lond.), 345: 544-547, 1990.
    • (1990) Nature (Lond.) , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 18
    • 0026572661 scopus 로고
    • Elevated expression of the ribosomal protein S2 gene in human tumors
    • Chiao, P. J., Shin, D. M., Sacks, P. G., Hong, W. K., and Tainsky, M. A. Elevated expression of the ribosomal protein S2 gene in human tumors. Mol. Carcinog., 5: 219-231, 1992.
    • (1992) Mol. Carcinog. , vol.5 , pp. 219-231
    • Chiao, P.J.1    Shin, D.M.2    Sacks, P.G.3    Hong, W.K.4    Tainsky, M.A.5
  • 20
  • 21
    • 0007253213 scopus 로고
    • Analysis of mammalian cell genetic regulation in situ by using retrovirus-derived "portable exons" carrying the Escherichia coli lacZ gene
    • Brenner, D. G., Lin-Chao, S., and Cohen, S. N. Analysis of mammalian cell genetic regulation in situ by using retrovirus-derived "portable exons" carrying the Escherichia coli lacZ gene. Proc. Natl. Acad. Sci. USA, 86: 5517-5521, 1989.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5517-5521
    • Brenner, D.G.1    Lin-Chao, S.2    Cohen, S.N.3
  • 22
    • 0021734287 scopus 로고
    • Characterization of two genes required for the position-effect control of yeast mating-type genes
    • Shore, D., Squire, M., and Nasmyth, K. A. Characterization of two genes required for the position-effect control of yeast mating-type genes. EMBO J., 3: 2817-2823, 1984.
    • (1984) EMBO J. , vol.3 , pp. 2817-2823
    • Shore, D.1    Squire, M.2    Nasmyth, K.A.3
  • 23
    • 0026297939 scopus 로고
    • The structure and biogenesis of yeast ribosomes
    • Woolford, J. L. The structure and biogenesis of yeast ribosomes. Adv. Genet., 29:63-118, 1991.
    • (1991) Adv. Genet. , vol.29 , pp. 63-118
    • Woolford, J.L.1
  • 25
    • 0024785875 scopus 로고
    • Retrovirus activation in embryonal carcinoma cells by cellular promoters
    • Peckham, I., Sobel, S., Comer, J., Jaenisch, R., and Barklis, E. Retrovirus activation in embryonal carcinoma cells by cellular promoters. Genes & Dev., 3: 2062-2071, 1989.
    • (1989) Genes & Dev. , vol.3 , pp. 2062-2071
    • Peckham, I.1    Sobel, S.2    Comer, J.3    Jaenisch, R.4    Barklis, E.5
  • 27
    • 0025744724 scopus 로고
    • Ribosomal protein genes are overexpressed in colorectal cancer: Isolation of a cDNA clone encoding the human S3 ribosomal protein
    • Pogue-Geile, K., Geiser, J. R., Shu, M., Miller, C., Wool, I. G., Meisler, A. I., and Pipas, J. M. Ribosomal protein genes are overexpressed in colorectal cancer: isolation of a cDNA clone encoding the human S3 ribosomal protein. Mol. Cell. Biol., 11: 3842-3849, 1991.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3842-3849
    • Pogue-Geile, K.1    Geiser, J.R.2    Shu, M.3    Miller, C.4    Wool, I.G.5    Meisler, A.I.6    Pipas, J.M.7
  • 28
    • 0027450784 scopus 로고
    • High-level expression of the ribosomal protein L19 in human breast tumors that overexpress erbB-2
    • Henry, J. L., Coggin, D. L., and King, C. R. High-level expression of the ribosomal protein L19 in human breast tumors that overexpress erbB-2. Cancer Res., 53: 1403-1408, 1993.
    • (1993) Cancer Res. , vol.53 , pp. 1403-1408
    • Henry, J.L.1    Coggin, D.L.2    King, C.R.3
  • 30
    • 0025294788 scopus 로고
    • Isolation and characterization of the human homologue of rig and its pseudogenes: The functional gene has features characteristic of housekeeping genes
    • Shiga, K., Yamamoto, H., and Okamoto, H. Isolation and characterization of the human homologue of rig and its pseudogenes: the functional gene has features characteristic of housekeeping genes. Proc. Natl. Acad. Sci. USA, 87: 3594-3598, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3594-3598
    • Shiga, K.1    Yamamoto, H.2    Okamoto, H.3
  • 32
    • 0029832593 scopus 로고    scopus 로고
    • Activation of tumor suppressor genes in nontumorigenic revertants of the HeLa cervical carcinoma cell line
    • Boylan, M. O., Athanassiou, M., Houle, B. Wang, Y., and Zarbl, H. Activation of tumor suppressor genes in nontumorigenic revertants of the HeLa cervical carcinoma cell line. Cell Growth & Differ., 7: 725-735, 1996.
    • (1996) Cell Growth & Differ. , vol.7 , pp. 725-735
    • Boylan, M.O.1    Athanassiou, M.2    Houle, B.3    Wang, Y.4    Zarbl, H.5
  • 33
    • 0019818270 scopus 로고
    • Coordinate control of synthesis of ribosomal ribonucleic acid and ribosomal proteins during nutritional shift-up in Saccharomyces cerevisiae
    • Kief, D. R., and Warner, J. R. Coordinate control of synthesis of ribosomal ribonucleic acid and ribosomal proteins during nutritional shift-up in Saccharomyces cerevisiae. Mol. Cell. Biol., 1: 1007-1015, 1981.
    • (1981) Mol. Cell. Biol. , vol.1 , pp. 1007-1015
    • Kief, D.R.1    Warner, J.R.2
  • 34
    • 84908768794 scopus 로고
    • Ribosomal protein gene expression in proliferating and nonproliferating cells
    • G. S. Stein and J. L. S. Stein (eds.), New York: Academic Press
    • Meyuhas, O. Ribosomal protein gene expression in proliferating and nonproliferating cells. In: G. S. Stein and J. L. S. Stein (eds.), Recombinant DNA and Cell Proliferation, pp. 243-267. New York: Academic Press, 1984.
    • (1984) Recombinant DNA and Cell Proliferation , pp. 243-267
    • Meyuhas, O.1
  • 35
    • 0019979317 scopus 로고
    • Ribosome proteins are synthesized preferentially in cells commencing growth
    • Tushinski, R. J., and Warner, J. R. Ribosome proteins are synthesized preferentially in cells commencing growth. J. Cell. Physiol., 112: 128-135, 1982.
    • (1982) J. Cell. Physiol. , vol.112 , pp. 128-135
    • Tushinski, R.J.1    Warner, J.R.2
  • 36
    • 0023879963 scopus 로고
    • A highly conserved mouse gene with a propensity to form pseudogenes in mammals
    • Heller, D. L., Gianola, K. M., and Leinwand, L. A. A highly conserved mouse gene with a propensity to form pseudogenes in mammals. Mol. Cell. Biol., 8: 2797-2803, 1988.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2797-2803
    • Heller, D.L.1    Gianola, K.M.2    Leinwand, L.A.3
  • 37
    • 0023022184 scopus 로고
    • Characterization of an mRNA encoding a human ribosomal protein homologous to the yeast L44 ribosomal protein
    • Davies, M. S., Henney, A., Ward, W. H. J., and Craig, R. K. Characterization of an mRNA encoding a human ribosomal protein homologous to the yeast L44 ribosomal protein. Gene (Amst.), 45: 183-191, 1986.
    • (1986) Gene (Amst.) , vol.45 , pp. 183-191
    • Davies, M.S.1    Henney, A.2    Ward, W.H.J.3    Craig, R.K.4
  • 38
    • 0026209338 scopus 로고
    • Nucleotide sequence and characterization of a maize cytoplasmic ribosomal protein S11 cDNA
    • Lebrun, M., and Freyssinet, G. Nucleotide sequence and characterization of a maize cytoplasmic ribosomal protein S11 cDNA, Plant Mol. Biol., 17: 265-268, 1991.
    • (1991) Plant Mol. Biol. , vol.17 , pp. 265-268
    • Lebrun, M.1    Freyssinet, G.2
  • 39
    • 0026521856 scopus 로고
    • cDNA sequence and expression of a tobacco cytoplasmic ribosomal protein L2 gene
    • Marty, I., and Meyer, Y. cDNA sequence and expression of a tobacco cytoplasmic ribosomal protein L2 gene. Nucleic Acids Res., 20: 1517-1522, 1992.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1517-1522
    • Marty, I.1    Meyer, Y.2
  • 40
    • 0028386814 scopus 로고
    • Meristem-specific gene expression directed by the promoter of the S-phase-specific gene, cyc07, in transgenic Arabidopsis
    • Ito, M., Sato, T., Fukuda, H., and Komamine, A. Meristem-specific gene expression directed by the promoter of the S-phase-specific gene, cyc07, in transgenic Arabidopsis. Plant Mol. Biol., 24: 863-878, 1994.
    • (1994) Plant Mol. Biol. , vol.24 , pp. 863-878
    • Ito, M.1    Sato, T.2    Fukuda, H.3    Komamine, A.4
  • 41
    • 0021102481 scopus 로고
    • The spatial arrangement of the complex between eukaryotic initiation factor elF-3 and 40S ribosomal subunit
    • Westermann, P., and Nygard, O. The spatial arrangement of the complex between eukaryotic initiation factor elF-3 and 40S ribosomal subunit. Biochim. Biophys. Acta, 741: 103-108, 1983.
    • (1983) Biochim. Biophys. Acta , vol.741 , pp. 103-108
    • Westermann, P.1    Nygard, O.2
  • 42
    • 84886618482 scopus 로고
    • Cross-linking of initiation factor elF-2 to protein of the small subunit of rat liver ribosomes
    • Westermann, P., Heumann, W., Bommer, U-A., Bielka, H., Nygard, O., and Hultin, T. Cross-linking of initiation factor elF-2 to protein of the small subunit of rat liver ribosomes. FEBS Lett., 97: 101-104, 1979.
    • (1979) FEBS Lett. , vol.97 , pp. 101-104
    • Westermann, P.1    Heumann, W.2    Bommer, U.-A.3    Bielka, H.4    Nygard, O.5    Hultin, T.6
  • 43
    • 0019888080 scopus 로고
    • Cross-linking of Met-tRNAf to elF-2b and to the ribosomal proteins S3a and S6 within the eukaryotic initiation complex, elF-2.GMPPCP.Met-tRNAf.small ribosomal subunit
    • Westermann, P., Nygard, O., and Bielka, H. Cross-linking of Met-tRNAf to elF-2b and to the ribosomal proteins S3a and S6 within the eukaryotic initiation complex, elF-2.GMPPCP.Met-tRNAf.small ribosomal subunit. Nucleic Acids Res., 10: 2387-2396, 1981.
    • (1981) Nucleic Acids Res. , vol.10 , pp. 2387-2396
    • Westermann, P.1    Nygard, O.2    Bielka, H.3
  • 44
    • 0021760787 scopus 로고
    • Cross-linking of initiation factor elF-3, 24-kDa cap-binding protein, and ribosomal protein S1, S3/S3a, S6, and S11 within the 48S pre-initiation complex
    • Westermann, P., and Nygard, O. Cross-linking of initiation factor elF-3, 24-kDa cap-binding protein, and ribosomal protein S1, S3/S3a, S6, and S11 within the 48S pre-initiation complex. Nucleic Acids Res., 12: 8887-8897, 1984.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 8887-8897
    • Westermann, P.1    Nygard, O.2
  • 45
    • 0017885830 scopus 로고
    • Cross-linking of proteins to ribosomal RNA in HeLa cell polysomes by sodium periodate
    • Svoboda, A. J., and McConkey, E. H. Cross-linking of proteins to ribosomal RNA in HeLa cell polysomes by sodium periodate. Biochem. Biophys. Res. Commun., 81: 1145-1152, 1979.
    • (1979) Biochem. Biophys. Res. Commun. , vol.81 , pp. 1145-1152
    • Svoboda, A.J.1    McConkey, E.H.2
  • 46
    • 0025733603 scopus 로고
    • Ribosomal RNA and translation
    • Noller, H. F. Ribosomal RNA and translation. Annu. Rev. Biochem., 60: 191-227, 1991.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 191-227
    • Noller, H.F.1
  • 47
    • 0025115303 scopus 로고
    • Immunoelectron microscopic studies on the location of ribosomal proteins on the surface of the 40S ribosomal subunit from rat liver
    • Lutsch, G., Stahl, J., Kargel, H-J., Noll, F., and Bielka, H. Immunoelectron microscopic studies on the location of ribosomal proteins on the surface of the 40S ribosomal subunit from rat liver. Eur. J. Cell Biol., 51: 140-150, 1990.
    • (1990) Eur. J. Cell Biol. , vol.51 , pp. 140-150
    • Lutsch, G.1    Stahl, J.2    Kargel, H.-J.3    Noll, F.4    Bielka, H.5
  • 49
    • 0025633118 scopus 로고
    • Homologous ribosomal protein genes on the human X and Y chromosomes: Escape from X inactivation and possible implications for Turner syndrome
    • Fisher, E. M. C., Beer-Romero, P., Brown, L. G., Ridley, A., McNeil, J. A., Lawrence, J. B., Willard, H. F., Bieber, F. R., and Page, D. C. Homologous ribosomal protein genes on the human X and Y chromosomes: escape from X inactivation and possible implications for Turner syndrome. Cell, 63: 1205-1218, 1990.
    • (1990) Cell , vol.63 , pp. 1205-1218
    • Fisher, E.M.C.1    Beer-Romero, P.2    Brown, L.G.3    Ridley, A.4    McNeil, J.A.5    Lawrence, J.B.6    Willard, H.F.7    Bieber, F.R.8    Page, D.C.9
  • 50
    • 0025776395 scopus 로고
    • Molecular cloning of the human gene, CCG2, that complements the BHK-derived temperature-sensitive cell cycle mutant tsBN63: Identity of CCG2 with the human X chromosomal SCAR/RPS4X gene
    • Watanabe, M., Furuno, N., Goebl, M., Go, M., Miyauchi, K., Sekiguchi, T., Basilico, C., and Nishimoto, T. Molecular cloning of the human gene, CCG2, that complements the BHK-derived temperature-sensitive cell cycle mutant tsBN63: identity of CCG2 with the human X chromosomal SCAR/RPS4X gene. J. Cell Sci., 100: 35-43, 1991.
    • (1991) J. Cell Sci. , vol.100 , pp. 35-43
    • Watanabe, M.1    Furuno, N.2    Goebl, M.3    Go, M.4    Miyauchi, K.5    Sekiguchi, T.6    Basilico, C.7    Nishimoto, T.8
  • 51
    • 0026518351 scopus 로고
    • Cap recap: The involvement of elF-4F in regulating gene expression
    • Thach, R. E. Cap recap: the involvement of elF-4F in regulating gene expression. Cell, 68: 177-180, 1992.
    • (1992) Cell , vol.68 , pp. 177-180
    • Thach, R.E.1
  • 52
    • 0026723117 scopus 로고
    • mRNAs containing extensive secondary structure in their 5′ noncoding region translate efficiently in cells expressing initiation factor elF-4E
    • Koromilas, A., Lazaris-Karatzas, A., and Sonenberg, N. mRNAs containing extensive secondary structure in their 5′ noncoding region translate efficiently in cells expressing initiation factor elF-4E. EMBO J., 11: 4153-4158, 1992.
    • (1992) EMBO J. , vol.11 , pp. 4153-4158
    • Koromilas, A.1    Lazaris-Karatzas, A.2    Sonenberg, N.3
  • 53
    • 0027365517 scopus 로고
    • Elevated levels of cyclin D1 protein in response to increased expression of eukaryotic initiation factor 4E
    • Rosenwald, I. B., Lazaris-Karatzas, A., Sonenberg, N., and Schmidt, E. V. Elevated levels of cyclin D1 protein in response to increased expression of eukaryotic initiation factor 4E. Mol. Cell. Biol., 13: 7358-7363, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7358-7363
    • Rosenwald, I.B.1    Lazaris-Karatzas, A.2    Sonenberg, N.3    Schmidt, E.V.4
  • 54
    • 0026733511 scopus 로고
    • Preferential translation of heat shock mRNAs in HeLa cells deficient in protein synthesis initiation factors elF-4E and elF-4G
    • Joshi-Barre, S., de Benedetti, A., and Rhoads, R. E. Preferential translation of heat shock mRNAs in HeLa cells deficient in protein synthesis initiation factors elF-4E and elF-4G. J. Biol. Chem., 267: 21038-21043, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21038-21043
    • Joshi-Barre, S.1    De Benedetti, A.2    Rhoads, R.E.3
  • 55
    • 0027482105 scopus 로고
    • Co-translational protein import into mitochondria: An alternative view
    • Verner, K. Co-translational protein import into mitochondria: an alternative view. Trends Biochem. Sci., 18: 366-371, 1993.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 366-371
    • Verner, K.1
  • 56
    • 0028791882 scopus 로고
    • Mutations altering the mitochondrial-cytoplasmic distribution of Modop implicate the actin cytoskeleton and mRNA 3′ ends and/or protein synthesis in mitochondrial delivery
    • Zoladek, T., Vaduva, G., Hunter, L. A., Boguta, M., Go, D. B., Martin, N., and Hopper, A. K. Mutations altering the mitochondrial-cytoplasmic distribution of Modop implicate the actin cytoskeleton and mRNA 3′ ends and/or protein synthesis in mitochondrial delivery. Mol. Cell. Biol., 15: 6884-6894, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6884-6894
    • Zoladek, T.1    Vaduva, G.2    Hunter, L.A.3    Boguta, M.4    Go, D.B.5    Martin, N.6    Hopper, A.K.7
  • 57
    • 0025779075 scopus 로고
    • Inhibition of growth of breast cancer cells in vitro by the ribosome-inactivating protein saporin 6
    • Gasperi-Campani, A., Zoli, W., Volpi, A., Roncuzzi, L., and Amadori, D. Inhibition of growth of breast cancer cells in vitro by the ribosome-inactivating protein saporin 6. Anticancer Res., 11: 1007-1012, 1991.
    • (1991) Anticancer Res. , vol.11 , pp. 1007-1012
    • Gasperi-Campani, A.1    Zoli, W.2    Volpi, A.3    Roncuzzi, L.4    Amadori, D.5
  • 58
    • 0026569275 scopus 로고
    • Specific binding of chromosomal protein HMG1 to DMA damaged by the anticancer drug cisplatin
    • Pil, P. M., and Lippard, J. L. Specific binding of chromosomal protein HMG1 to DMA damaged by the anticancer drug cisplatin. Science (Washington DC), 256: 234-237, 1992.
    • (1992) Science (Washington DC) , vol.256 , pp. 234-237
    • Pil, P.M.1    Lippard, J.L.2
  • 59
    • 0028860339 scopus 로고
    • Inhibition of HMGI-C protein synthesis suppresses retrovirally induced neoplastic transformation of rat thyroid cells
    • Berlingieri, M. T., Manfioletti, G., Santoro, M., Bandiera, A., Visconti, R., Giancotti, V., and Fusco, A. Inhibition of HMGI-C protein synthesis suppresses retrovirally induced neoplastic transformation of rat thyroid cells. Mol. Cell. Biol., 15: 1545-1553, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1545-1553
    • Berlingieri, M.T.1    Manfioletti, G.2    Santoro, M.3    Bandiera, A.4    Visconti, R.5    Giancotti, V.6    Fusco, A.7
  • 60
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidium thiocyanate-phenol chloroform extraction
    • Chomczynski, P., and Sacchi, N. Single-step method of RNA isolation by acid guanidium thiocyanate-phenol chloroform extraction. Anal. Biochem., 162: 156-159, 1987.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 62
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A. P., and Vogelstein, B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem., 132: 6-13, 1983.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 64
    • 0025283867 scopus 로고
    • Use of the T7 RNA polymerase to direct expression of cloned genes
    • D. V. Goeddel (ed.), San Diego, CA: Academic Press, Inc.
    • Studier, F. W., Rosenberg, A. H., Dunn, J. J., and Dubendorff, J. W. Use of the T7 RNA polymerase to direct expression of cloned genes. In: D. V. Goeddel (ed.), Methods in Enzymology, pp. 60-89. San Diego, CA: Academic Press, Inc., 1990.
    • (1990) Methods in Enzymology , pp. 60-89
    • Studier, F.W.1    Rosenberg, A.H.2    Dunn, J.J.3    Dubendorff, J.W.4
  • 65
    • 0022950668 scopus 로고
    • Purification and assay of intact human basic fibroblast growth factor using heparin-Sepharose chromatography
    • Sullivan, R., and Klagsburn, M. Purification and assay of intact human basic fibroblast growth factor using heparin-Sepharose chromatography. J. Tissue Cult. Methods, 10: 125-132, 1987.
    • (1987) J. Tissue Cult. Methods , vol.10 , pp. 125-132
    • Sullivan, R.1    Klagsburn, M.2
  • 66
    • 0018307473 scopus 로고
    • Autoradiography
    • W. B. Jakoby and I. H. Pastan (eds.), New York: Academic Press
    • Stein, G. H., and Yanishevsky, R. Autoradiography. In: W. B. Jakoby and I. H. Pastan (eds.), Methods in Enzymology, pp. 279-292. New York: Academic Press, 1979.
    • (1979) Methods in Enzymology , pp. 279-292
    • Stein, G.H.1    Yanishevsky, R.2
  • 67
    • 0021081495 scopus 로고
    • Membrane association of a 36,000-dalton substrate for tyrosine phosphorylation in chicken embryo fibroblasts transformed by avian sarcoma viruses
    • Radke, K., Carter, V. C., Moss, P., Dehazya, P., Schliwa, M., and Martin, G. S. Membrane association of a 36,000-dalton substrate for tyrosine phosphorylation in chicken embryo fibroblasts transformed by avian sarcoma viruses. J. Cell Biol., 97: 1601-1611, 1983.
    • (1983) J. Cell Biol. , vol.97 , pp. 1601-1611
    • Radke, K.1    Carter, V.C.2    Moss, P.3    Dehazya, P.4    Schliwa, M.5    Martin, G.S.6
  • 68
    • 0017647917 scopus 로고
    • Transfer of purified herpes thymidine kinase gene to cultured mouse cells
    • Wigler, M., Silverstein, S., Lee, L-S., Pellicer, A., Cheng, Y. C., and Axel, R. Transfer of purified herpes thymidine kinase gene to cultured mouse cells. Cell, 11: 223-232, 1977.
    • (1977) Cell , vol.11 , pp. 223-232
    • Wigler, M.1    Silverstein, S.2    Lee, L.-S.3    Pellicer, A.4    Cheng, Y.C.5    Axel, R.6
  • 69
    • 0021710934 scopus 로고
    • Hygromycin B phosphotransferase as a selectable marker for DNA transfer experiments with higher eukaryotic cells
    • Blochlinger, K., and Diggelmann, H. Hygromycin B phosphotransferase as a selectable marker for DNA transfer experiments with higher eukaryotic cells. Mol. Cell. Biol., 4: 2929-2931, 1984.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2929-2931
    • Blochlinger, K.1    Diggelmann, H.2
  • 70
    • 0027490605 scopus 로고
    • Regulation of eukaryotic translation initiation factor expression during T-cell activation
    • Chiorini, J. A., Boal, T. R., Miyamoto, S., and Safer, B. Regulation of eukaryotic translation initiation factor expression during T-cell activation. J. Biol. Chem., 268: 13748-13755, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13748-13755
    • Chiorini, J.A.1    Boal, T.R.2    Miyamoto, S.3    Safer, B.4


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