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Volumn 17, Issue 9, 1997, Pages 5184-5192

Requirement of protein kinase Cζ for stimulation of protein synthesis by insulin

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; INSULIN; INSULIN RECEPTOR; INSULIN RECEPTOR SUBSTRATE 1; ISOENZYME; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE C; PROTEIN P21; RAS PROTEIN;

EID: 0030874374     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.17.9.5184     Document Type: Article
Times cited : (118)

References (72)
  • 2
    • 0029981389 scopus 로고    scopus 로고
    • Regulation of both glycogen synthase and PHAS-I by insulin in rat skeletal muscle involves mitogen-activated protein kinase-independent and rapamycin-sensitive pathways
    • Azpiazu, I., A. R. Saltiel, A. A. DePaoli-Roach, and J. C. Lawrence. 1996. Regulation of both glycogen synthase and PHAS-I by insulin in rat skeletal muscle involves mitogen-activated protein kinase-independent and rapamycin-sensitive pathways. J. Biol. Chem. 27:5033-5039.
    • (1996) J. Biol. Chem. , vol.27 , pp. 5033-5039
    • Azpiazu, I.1    Saltiel, A.R.2    DePaoli-Roach, A.A.3    Lawrence, J.C.4
  • 4
    • 0028314880 scopus 로고
    • Mechanism of differential regulation of IL-2 murine Th1 and Th2 cell subsets
    • Barve, S. S., D. A. Cohen, A. DeBenedetti, R. E. Rhoads, and A. M. Kaplan. 1994. Mechanism of differential regulation of IL-2 murine Th1 and Th2 cell subsets. J. Immunol. 152:1171-1181.
    • (1994) J. Immunol. , vol.152 , pp. 1171-1181
    • Barve, S.S.1    Cohen, D.A.2    DeBenedetti, A.3    Rhoads, R.E.4    Kaplan, A.M.5
  • 5
    • 0025095892 scopus 로고
    • The cell cycle: Myths and realities
    • Baserga, R. 1990. The cell cycle: myths and realities. Cancer Res. 50:6769-6771.
    • (1990) Cancer Res. , vol.50 , pp. 6769-6771
    • Baserga, R.1
  • 6
    • 0030066934 scopus 로고    scopus 로고
    • Rapamycin blocks the phosphorylation of 4E-BP and inhibits cap-dependent initiation of translation
    • Beretta, L., A. C. Gingras, Y. V. Svitkin, M. N. Hall, and N. Sonenberg. 1996. Rapamycin blocks the phosphorylation of 4E-BP and inhibits cap-dependent initiation of translation. EMBO J. 15:658-664.
    • (1996) EMBO J. , vol.15 , pp. 658-664
    • Beretta, L.1    Gingras, A.C.2    Svitkin, Y.V.3    Hall, M.N.4    Sonenberg, N.5
  • 10
    • 0030598885 scopus 로고    scopus 로고
    • A signalling pathway to translational control
    • Brown, E. J., and S. L. Schreiber. 1996. A signalling pathway to translational control. Cell 86:517-520.
    • (1996) Cell , vol.86 , pp. 517-520
    • Brown, E.J.1    Schreiber, S.L.2
  • 11
    • 0029831167 scopus 로고    scopus 로고
    • Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and Ly294002
    • Brunn, G. J., J. Williams, C. Sabers, G. Wiederrecht, J. C. Lawrence, and R. T. Abraham. 1996. Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and Ly294002. EMBO J. 15:5256-5267.
    • (1996) EMBO J. , vol.15 , pp. 5256-5267
    • Brunn, G.J.1    Williams, J.2    Sabers, C.3    Wiederrecht, G.4    Lawrence, J.C.5    Abraham, R.T.6
  • 12
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering, B. M., and P. J. Coffer. 1995. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376:599-602.
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.1    Coffer, P.J.2
  • 13
    • 0028308412 scopus 로고
    • Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase. DNA synthesis, and glucose transporter translocation
    • Cheatham, B., C. J. Vlahos, L. Cheatham, L. Wang, J. Blenis, and C. R. Kahn. 1994. Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase. DNA synthesis, and glucose transporter translocation. Mol. Cell. Biol. 14:4902-4911.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4902-4911
    • Cheatham, B.1    Vlahos, C.J.2    Cheatham, L.3    Wang, L.4    Blenis, J.5    Kahn, C.R.6
  • 15
    • 0026659046 scopus 로고
    • Rapamycin-FKBP specifically blocks growth-dependent activation of signaling by the 70 kd S6 protein kinase
    • Chung, J., C. J. Kuo, G. R. Crabtree, and J. Blenis. 1992. Rapamycin-FKBP specifically blocks growth-dependent activation of signaling by the 70 kd S6 protein kinase. Cell 69:1227-1236.
    • (1992) Cell , vol.69 , pp. 1227-1236
    • Chung, J.1    Kuo, C.J.2    Crabtree, G.R.3    Blenis, J.4
  • 16
    • 0027978816 scopus 로고
    • The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor 1 in the rat skeletal muscle cell line L6 is blocked by wortmannin, but not by rapamycin: Evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf
    • Cross, D. A. E., D. R. Alessi, J. R. Vandenheede, H. E. McDowell, H. S. Hundal, and P. Cohen. 1994. The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor 1 in the rat skeletal muscle cell line L6 is blocked by wortmannin, but not by rapamycin: evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf. Biochem. J. 303:21-26.
    • (1994) Biochem. J. , vol.303 , pp. 21-26
    • Cross, D.A.E.1    Alessi, D.R.2    Vandenheede, J.R.3    McDowell, H.E.4    Hundal, H.S.5    Cohen, P.6
  • 17
    • 0028253641 scopus 로고
    • CHO cells transformed by the translation factor eIF4E display increased c-Myc expression, but require overexpression of Max for tumorigenicity
    • De Benedetti, A., B. Joshi, J. R. Graff, and S. G. Zimmer. 1994. CHO cells transformed by the translation factor eIF4E display increased c-Myc expression, but require overexpression of Max for tumorigenicity. Mol. Cell. Differ. 2:347-371.
    • (1994) Mol. Cell. Differ. , vol.2 , pp. 347-371
    • De Benedetti, A.1    Joshi, B.2    Graff, J.R.3    Zimmer, S.G.4
  • 18
    • 0025107684 scopus 로고
    • Overexpression of eukaryotic protein synthesis initiation factor 4E in HeLa cells results in aberrant growth and morphology
    • De Benedetti, A., and R. E. Rhoads. 1990. 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) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8212-8216
    • De Benedetti, A.1    Rhoads, R.E.2
  • 19
    • 0030267336 scopus 로고    scopus 로고
    • The eIF-2α kinases and the control of protein synthesis
    • De Haro, C., R. Mendez, and J. Santoyo. 1996. The eIF-2α kinases and the control of protein synthesis. FASEB J. 10:1378-1387.
    • (1996) FASEB J. , vol.10 , pp. 1378-1387
    • De Haro, C.1    Mendez, R.2    Santoyo, J.3
  • 20
    • 0028082161 scopus 로고
    • Protein kinase C - A question of specificity
    • Dekker, L. V., and P. J. Parker. 1994. Protein kinase C - a question of specificity. Trends Biochem. Sci. 19:73-77.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 73-77
    • Dekker, L.V.1    Parker, P.J.2
  • 22
    • 0030013407 scopus 로고    scopus 로고
    • Both rapamycin-sensitive and -insensitive pathways are involved in the phosphorylation of the initiation factor-4E-binding protein (4E-BP1) in response to insulin in rat epididymal fat cells
    • Diggle, T. A., S. K. Moule, M. B. Avison, A. Flynn, E. J. Foulstone, C. G. Proud, and R. M. Denton. 1996. Both rapamycin-sensitive and -insensitive pathways are involved in the phosphorylation of the initiation factor-4E-binding protein (4E-BP1) in response to insulin in rat epididymal fat cells. Biochem. J. 316:447-453.
    • (1996) Biochem. J. , vol.316 , pp. 447-453
    • Diggle, T.A.1    Moule, S.K.2    Avison, M.B.3    Flynn, A.4    Foulstone, E.J.5    Proud, C.G.6    Denton, R.M.7
  • 23
    • 0021709170 scopus 로고
    • The accumulation of prominent tadpole mRNAs occurs at the beginnine of neurulation in Xenopus laevis embryos
    • Dworkin, M. B., A. Shruthkowski, M. Baumgarten, and E. Dworkin-Rastl. 1984. The accumulation of prominent tadpole mRNAs occurs at the beginnine of neurulation in Xenopus laevis embryos. Dev. Biol. 106:289-295.
    • (1984) Dev. Biol. , vol.106 , pp. 289-295
    • Dworkin, M.B.1    Shruthkowski, A.2    Baumgarten, M.3    Dworkin-Rastl, E.4
  • 24
    • 0026012413 scopus 로고
    • Translational control of ornithine aminotransferase. Modulation by initiation factor eIF-4E
    • Pagan, R. J., A. Lazaris-Karatzas, N. Sonenberg, and R. D. Rozen. 1991. Translational control of ornithine aminotransferase. Modulation by initiation factor eIF-4E. J. Biol. Chem. 266:16518-16523.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16518-16523
    • Pagan, R.J.1    Lazaris-Karatzas, A.2    Sonenberg, N.3    Rozen, R.D.4
  • 25
    • 0026496318 scopus 로고
    • Effects of insulin and phorbol esters on subcellular distribution of protein kinase C isoforms in rat adipocytes
    • Farese, R. V., M. L. Standaert, A. J. Francois, K. Ways, T. P. Arnold, H. Hernandez, and D. R. Cooper. 1992. Effects of insulin and phorbol esters on subcellular distribution of protein kinase C isoforms in rat adipocytes. Biochem. J. 288:319-323.
    • (1992) Biochem. J. , vol.288 , pp. 319-323
    • Farese, R.V.1    Standaert, M.L.2    Francois, A.J.3    Ways, K.4    Arnold, T.P.5    Hernandez, H.6    Cooper, D.R.7
  • 26
    • 0029791354 scopus 로고    scopus 로고
    • Cap-binding protein (eukaryotic initiation factor 4E) and 4E-inactivating protein BP-1 independently regulate cap-dependent translation
    • Feigenblum, D., and R. J. Schneider. 1996. Cap-binding protein (eukaryotic initiation factor 4E) and 4E-inactivating protein BP-1 independently regulate cap-dependent translation. Mol. Cell. Biol. 16:5450-5457.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5450-5457
    • Feigenblum, D.1    Schneider, R.J.2
  • 27
    • 0029864854 scopus 로고    scopus 로고
    • Insulin and phorbol ester stimulate initiation factor eIF-4E phosphorylation by distinct pathways in Chinese hamster ovary cells overexpressing the insulin receptor
    • Flynn, A., and C. G. Proud. 1996. Insulin and phorbol ester stimulate initiation factor eIF-4E phosphorylation by distinct pathways in Chinese hamster ovary cells overexpressing the insulin receptor. Eur. J. Biochem. 236:40-47.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 40-47
    • Flynn, A.1    Proud, C.G.2
  • 28
    • 0030199543 scopus 로고    scopus 로고
    • Insulin-stimulated phosphorylation of initiation factor 4E is mediated by the MAP kinase pathway
    • Flynn, A., and C. G. Proud. 1996. Insulin-stimulated phosphorylation of initiation factor 4E is mediated by the MAP kinase pathway. FEBS Lett. 389:162-166.
    • (1996) FEBS Lett. , vol.389 , pp. 162-166
    • Flynn, A.1    Proud, C.G.2
  • 29
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • Franke, T. F., D. R. Kaplan, L. C. Cantley, and A. Toker. 1997. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science 275:665-668.
    • (1997) Science , vol.275 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 30
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke, T. F., S. Yang, T. O. Chan, K. Datta, A. Kazlauskas, D. K. Morrison, D. R. Kaplan, and P. N. Tsichlis. 1995. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81:727-736.
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6    Kaplan, D.R.7    Tsichlis, P.N.8
  • 31
    • 0013604747 scopus 로고
    • Preparation of cytoplasmic RNA from tissue culture cells
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). Greene Publishing Associates, Inc., and John Wiley and Sons, Inc., New York, N.Y.
    • Gilman, M. 1994. Preparation of cytoplasmic RNA from tissue culture cells, p. 4.1.1-4.1.6. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). Current protocols in molecular biology, vol. 1. Greene Publishing Associates, Inc., and John Wiley and Sons, Inc., New York, N.Y.
    • (1994) Current Protocols in Molecular Biology , vol.1 , pp. 411-416
    • Gilman, M.1
  • 33
    • 0028786952 scopus 로고
    • Repression of cap-dependent translation by 4E-binding protein 1: Competition with p220 for binding to eukaryotic initiation factor-4E
    • Haghighat, A., S. Mader, A. Pause, and N. Sonenberg. 1995. Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E. EMBO J. 14:5701-5709.
    • (1995) EMBO J. , vol.14 , pp. 5701-5709
    • Haghighat, A.1    Mader, S.2    Pause, A.3    Sonenberg, N.4
  • 34
    • 0029972883 scopus 로고    scopus 로고
    • Evidence for a role of phosphatidylinositol 3-kinase in IL-4-induced germline C epsilon transcription
    • Ikizawa, K., K. Kajiwara, Y. Basaki, T. Koshio, and Y. Yanagihara. 1996. Evidence for a role of phosphatidylinositol 3-kinase in IL-4-induced germline C epsilon transcription. Cell. Immunol. 170:134-140.
    • (1996) Cell. Immunol. , vol.170 , pp. 134-140
    • Ikizawa, K.1    Kajiwara, K.2    Basaki, Y.3    Koshio, T.4    Yanagihara, Y.5
  • 35
    • 0028207001 scopus 로고
    • Rapamycin selectively represses translation of the "polypyrimidine tract" mRNA family
    • Jefferies, H. B. J., C. Reinhard, S. C. Kozma, and G. Thomas. 1994. Rapamycin selectively represses translation of the "polypyrimidine tract" mRNA family. Proc. Natl. Acad. Sci. USA 91:4441-1445.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4441-11445
    • Jefferies, H.B.J.1    Reinhard, C.2    Kozma, S.C.3    Thomas, G.4
  • 36
    • 0029617994 scopus 로고
    • Translational enhancement of FGF-2 by cIF-4 factors, and alternate utilization of CUG and AUG codons for translation initiation
    • Kevil, C., P. Carter, B. Hu, and A. DeBenedetti. 1995. Translational enhancement of FGF-2 by cIF-4 factors, and alternate utilization of CUG and AUG codons for translation initiation. Oncogene 11:2339-2348.
    • (1995) Oncogene , vol.11 , pp. 2339-2348
    • Kevil, C.1    Carter, P.2    Hu, B.3    DeBenedetti, A.4
  • 39
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap
    • Lazaris-Karatzas, A., K. S. Montine, and N. Sonenberg. 1990. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap. Nature 345:544-547.
    • (1990) Nature , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 40
  • 41
    • 0029095931 scopus 로고
    • Control of PHAS-I by insulin in 3T3-L1 adipocytes. Synthesis, degradation, and phosphorylation by a rapamycin-sensitive and mitogen-activated protein kinase-independent pathway
    • Lin, T. A., X. Kong, A. R. Saltiel, P. J. Blackshear, and J. C. Lawrence, Jr. 1995. Control of PHAS-I by insulin in 3T3-L1 adipocytes. Synthesis, degradation, and phosphorylation by a rapamycin-sensitive and mitogen-activated protein kinase-independent pathway. J. Biol. Chem. 270:18531-18538.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18531-18538
    • Lin, T.A.1    Kong, X.2    Saltiel, A.R.3    Blackshear, P.J.4    Lawrence Jr., J.C.5
  • 43
    • 0030013326 scopus 로고    scopus 로고
    • Stimulation of protein synthesis, eukaryotic translation initiation factor 4E phosphorylation, and PHAS-I phosphorylation by insulin requires insulin receptor substrate-1 and phosphatidylinositol 3-kinase
    • Mendez, R., M. G. Myers, M. F. While, and R. E. Rhoads. 1996. Stimulation of protein synthesis, eukaryotic translation initiation factor 4E phosphorylation, and PHAS-I phosphorylation by insulin requires insulin receptor substrate-1 and phosphatidylinositol 3-kinase. Mol. Cell. Biol. 16:2857-2864.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2857-2864
    • Mendez, R.1    Myers, M.G.2    While, M.F.3    Rhoads, R.E.4
  • 44
    • 0026718508 scopus 로고
    • Mechanism and regulation of eukaryotic protein synthesis
    • Merrick, W. C. 1992. Mechanism and regulation of eukaryotic protein synthesis. Microhiol. Rev. 56:291-315.
    • (1992) Microhiol. Rev. , vol.56 , pp. 291-315
    • Merrick, W.C.1
  • 45
    • 0027969060 scopus 로고
    • Chromatographic resolution of in vivo-phosphorylated and nonphosphorylated translation initiation factor eIF-4E. Demonstration of increased cap affinity of the phosphorylated form
    • Minich, W. B., M. L. Balasta, D. J. Goss, and R. E. Rhoads. 1994. Chromatographic resolution of in vivo-phosphorylated and nonphosphorylated translation initiation factor eIF-4E. Demonstration of increased cap affinity of the phosphorylated form. Proc. Natl. Acad. Sci. USA 91:7668-7672.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7668-7672
    • Minich, W.B.1    Balasta, M.L.2    Goss, D.J.3    Rhoads, R.E.4
  • 46
    • 0025352187 scopus 로고
    • Advanced mammalian gene transfer: High titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell line
    • Morgenstern, P., and H. Land. 1990. Advanced mammalian gene transfer: high titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell line. Nucleic Acids Res. 18:3587-3596.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3587-3596
    • Morgenstern, P.1    Land, H.2
  • 50
    • 0027535742 scopus 로고
    • Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate
    • Nakanishi, H., K. A. Brewer, and J. H. Exton. 1993. Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 268:13-16.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13-16
    • Nakanishi, H.1    Brewer, K.A.2    Exton, J.H.3
  • 51
    • 0028982138 scopus 로고
    • Growth-dependent translation of IGF-II mRNA by a rapamycin-sensitive pathway
    • Nielsen, F. C., L. Ostergaard, J. Nielsen, and J. Christiansen. 1995. Growth-dependent translation of IGF-II mRNA by a rapamycin-sensitive pathway. Nature 377:358-362.
    • (1995) Nature , vol.377 , pp. 358-362
    • Nielsen, F.C.1    Ostergaard, L.2    Nielsen, J.3    Christiansen, J.4
  • 53
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • Pause, A., G. J. Belsham, A. Gingras, O. Donze, T. Lin, J. C. Lawrence, and N. Sonenberg. 1994. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function. Nature 371:762-767.
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.3    Donze, O.4    Lin, T.5    Lawrence, J.C.6    Sonenberg, N.7
  • 54
    • 0028582139 scopus 로고
    • The guanine nucleotide-exchange factor, eIF-2B
    • Price, N., and C. Proud. 1994. The guanine nucleotide-exchange factor, eIF-2B. Biochimie 76:748-760.
    • (1994) Biochimie , vol.76 , pp. 748-760
    • Price, N.1    Proud, C.2
  • 55
    • 0029966106 scopus 로고    scopus 로고
    • Regulation of translation elongation factor-2 by insulin via rapamycin-sensitive signalling pathway
    • Redpath, N. T., E. J. Foulstone, and C. G. Proud. 1996. Regulation of translation elongation factor-2 by insulin via rapamycin-sensitive signalling pathway. EMBO J. 15:2291-2297.
    • (1996) EMBO J. , vol.15 , pp. 2291-2297
    • Redpath, N.T.1    Foulstone, E.J.2    Proud, C.G.3
  • 56
    • 0026265892 scopus 로고
    • Protein synthesis, cell growth, and oncogenesis
    • Rhoads, R. E. 1991. Protein synthesis, cell growth, and oncogenesis. Curr. Opin. Cell Biol. 3:1019-1024.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 1019-1024
    • Rhoads, R.E.1
  • 57
    • 0027407751 scopus 로고
    • Regulation of eukaryotic protein synthesis by initiation factors
    • Rhoads, R. E. 1993. Regulation of eukaryotic protein synthesis by initiation factors. J. Biol. Chem. 268:3017-3020.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3017-3020
    • Rhoads, R.E.1
  • 59
    • 0028907351 scopus 로고
    • Requirement of MAP kinase for differentiation of fibroblasts to adipocytes, for insulin activation of p90 S6 kinase and for insulin serum stimulation of DNA synthesis
    • Sale, E. M., P. G. P. Atkinson, and G. J. Sale. 1995. Requirement of MAP kinase for differentiation of fibroblasts to adipocytes, for insulin activation of p90 S6 kinase and for insulin serum stimulation of DNA synthesis. EMBO J. 14:674-684.
    • (1995) EMBO J. , vol.14 , pp. 674-684
    • Sale, E.M.1    Atkinson, P.G.P.2    Sale, G.J.3
  • 61
    • 0000386558 scopus 로고
    • Analysis of RNA by northern hybridization
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). Greene Publishing Associates, Inc., and John Wiley and Sons, Inc., New York, N.Y.
    • Selden, R. F. 1994. Analysis of RNA by northern hybridization, p. 4.9.1-4.9.7. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). Current protocols in molecular biology, vol. 1. Greene Publishing Associates, Inc., and John Wiley and Sons, Inc., New York, N.Y.
    • (1994) Current Protocols in Molecular Biology , vol.1 , pp. 491-497
    • Selden, R.F.1
  • 62
    • 0030018849 scopus 로고    scopus 로고
    • Inhibition of growth factor-induced protein synthesis by a selective MEK inhibitor in aortic smooth muscle cells
    • Servant, M. J., E. Giasson, and S. Meloche. 1996. Inhibition of growth factor-induced protein synthesis by a selective MEK inhibitor in aortic smooth muscle cells. J. Biol. Chem. 271:16047-16052.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16047-16052
    • Servant, M.J.1    Giasson, E.2    Meloche, S.3
  • 63
    • 0028271504 scopus 로고
    • Overproduction of ornithine decarboxylase caused by relief of translational repression is associated with neoplastic transformation
    • Shantz, L. M., and A. E. Pegg. 1994. Overproduction of ornithine decarboxylase caused by relief of translational repression is associated with neoplastic transformation. Cancer Res. 54:2313-2316.
    • (1994) Cancer Res. , vol.54 , pp. 2313-2316
    • Shantz, L.M.1    Pegg, A.E.2
  • 64
    • 0027445185 scopus 로고
    • Translation factors as effectors of cell growth and tumorigenesis
    • Sonenberg, N. 1993. Translation factors as effectors of cell growth and tumorigenesis. Curr. Opin. Cell Biol. 5:955-960.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 955-960
    • Sonenberg, N.1
  • 66
    • 0027510985 scopus 로고
    • Rapamycin blocks cell cycle progression of activated T cells prior to events characteristic of the middle to late G1 phase of the cycle
    • Terada, N., J. J. Lucas, A. Szepesi, R. A. Franklin, J. Domenico, and E. W. Gelfand. 1993. Rapamycin blocks cell cycle progression of activated T cells prior to events characteristic of the middle to late G1 phase of the cycle. J. Cell. Physiol. 154:7-15.
    • (1993) J. Cell. Physiol. , vol.154 , pp. 7-15
    • Terada, N.1    Lucas, J.J.2    Szepesi, A.3    Franklin, R.A.4    Domenico, J.5    Gelfand, E.W.6
  • 67
    • 0028032355 scopus 로고
    • Rapamycin selectively inhibits translation of mRNAs encoding elongation factors and ribosomal proteins
    • Terada, N., H. R. Patel, K. Takase, K. Kohno, and A. C. Nairn. 1994. Rapamycin selectively inhibits translation of mRNAs encoding elongation factors and ribosomal proteins. Proc. Natl. Acad. Sci. USA 91:11477-11481.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11477-11481
    • Terada, N.1    Patel, H.R.2    Takase, K.3    Kohno, K.4    Nairn, A.C.5
  • 69
    • 0027507755 scopus 로고
    • IRS-1: Essential for insulin- and IL-4-stimulated mitogenesis in hematopoietic cells
    • Wang, L., M. G. Myers, X. J. Sun, S. A. Aaronson, M. White, and J. H. Pierce. 1993. IRS-1: essential for insulin- and IL-4-stimulated mitogenesis in hematopoietic cells. Science 261:1591-1594.
    • (1993) Science , vol.261 , pp. 1591-1594
    • Wang, L.1    Myers, M.G.2    Sun, X.J.3    Aaronson, S.A.4    White, M.5    Pierce, J.H.6
  • 70
    • 0027396419 scopus 로고
    • Evidence for a role for protein kinase-C in the stimulation of protein synthesis by insulin in Swiss 3T3-fibroblasts
    • Welsh, G. I., and C. G. Proud. 1993. Evidence for a role for protein kinase-C in the stimulation of protein synthesis by insulin in Swiss 3T3-fibroblasts. FEBS Lett. 316:241-246.
    • (1993) FEBS Lett. , vol.316 , pp. 241-246
    • Welsh, G.I.1    Proud, C.G.2
  • 71
    • 0030011629 scopus 로고    scopus 로고
    • Phosphorylation of eIF-4E on serine 209 by protein kinase C is inhibited by the translational repressors, 4E-binding proteins
    • Whalen, S. G., A. C. Gingras, L. Amankwa, S. Mader, P. E. Branton, R. Aebersold, and N. Sonenberg. 1996. Phosphorylation of eIF-4E on serine 209 by protein kinase C is inhibited by the translational repressors, 4E-binding proteins. J. Biol. Chem. 271:11831-11837.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11831-11837
    • Whalen, S.G.1    Gingras, A.C.2    Amankwa, L.3    Mader, S.4    Branton, P.E.5    Aebersold, R.6    Sonenberg, N.7
  • 72
    • 0028036724 scopus 로고
    • Insulin receptor substrate-1 (IRS1) and She compete for a limited pool of Grb2 in mediating insulin downstream signaling
    • Yamauchi, K., and J. E. Pessin. 1994. Insulin receptor substrate-1 (IRS1) and She compete for a limited pool of Grb2 in mediating insulin downstream signaling. J. Biol. Chem. 269:31107-31114.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31107-31114
    • Yamauchi, K.1    Pessin, J.E.2


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