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Volumn 17, Issue 9, 1997, Pages 5426-5436

The insulin-induced signalling pathway leading to S6 and initiation factor 4E binding protein 1 phosphorylation bifurcates at a rapamycin- sensitive point immediately upstream of p70(s6k)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; GROWTH FACTOR RECEPTOR; INITIATION FACTOR; INSULIN; RAPAMYCIN; RIBOSOME PROTEIN;

EID: 0030806524     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.9.5426     Document Type: Article
Times cited : (215)

References (73)
  • 1
    • 0028356914 scopus 로고
    • Vertebrate mRNAs with a 5′-terminal pyrimidine tract are candidates for translational repression in quiescent cells: Characterization of the translational cis-regulatory element
    • Avni, D., S. Shama, F. Loreni, and O. Meyuhas. 1994. Vertebrate mRNAs with a 5′-terminal pyrimidine tract are candidates for translational repression in quiescent cells: characterization of the translational cis-regulatory element. Mol. Cell. Biol. 14:3822-3833.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3822-3833
    • Avni, D.1    Shama, S.2    Loreni, F.3    Meyuhas, O.4
  • 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, Jr. 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. 271:5033-5039.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5033-5039
    • Azpiazu, I.1    Saltiel, A.R.2    DePaoli-Roach, A.A.3    Lawrence Jr., J.C.4
  • 3
    • 0027415831 scopus 로고
    • Identification of 40S ribosomal protein S6 phosphorylation sites in Swiss mouse 3T3 fibroblasts stimulated with serum
    • Bandi, H. R., S. Ferrari, J. Krieg, H. E. Meyer, and G. Thomas. 1993. Identification of 40S ribosomal protein S6 phosphorylation sites in Swiss mouse 3T3 fibroblasts stimulated with serum. J. Biol. Chem. 268:4530-4533.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4530-4533
    • Bandi, H.R.1    Ferrari, S.2    Krieg, J.3    Meyer, H.E.4    Thomas, G.5
  • 4
    • 0030066934 scopus 로고    scopus 로고
    • Rapamycin blocks the phosphorylation of 4E-BP1 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-BP1 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
  • 8
    • 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
  • 9
    • 0029831167 scopus 로고    scopus 로고
    • Direct inhibition of the signalling 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, Jr., and R. T. Abraham. 1996. Direct inhibition of the signalling 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 Jr., J.C.5    Abraham, R.T.6
  • 10
    • 0026659046 scopus 로고
    • Rapamycin-FKBP specifically blocks growth-dependent activation of and signalling by the 70 kd S6 protein kinases
    • Chung, J., C. J. Kuo, G. R. Crabtree, and J. Blenis. 1992. Rapamycin-FKBP specifically blocks growth-dependent activation of and signalling by the 70 kd S6 protein kinases. 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
  • 11
    • 0029779604 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase and p70 S6 kinase participate in the regulation of protein turnover in skeletal muscle by insulin and insulin-like growth factor I
    • Dardevet, D., C. Sornet, T. Vary, and J. Grizard. 1996. Phosphatidylinositol 3-kinase and p70 S6 kinase participate in the regulation of protein turnover in skeletal muscle by insulin and insulin-like growth factor I. Endocrinology 137:4087-4094.
    • (1996) Endocrinology , vol.137 , pp. 4087-4094
    • Dardevet, D.1    Sornet, C.2    Vary, T.3    Grizard, J.4
  • 12
    • 0028253641 scopus 로고
    • CHO cells transformed by the translation factor eIF4E display increased c-myc expression but require overexpression of Max for tumorigenicity
    • DeBenedetti, 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
    • DeBenedetti, A.1    Joshi, B.2    Graff, J.R.3    Zimmer, S.G.4
  • 14
    • 0019221771 scopus 로고
    • Preferential stimulation of ribosomal protein synthesis by insulin and in the absence of ribosomal and messenger ribonucleic acid formation
    • DePhilip, R. M., W. A. Rudert, and I. Lieberman. 1980. Preferential stimulation of ribosomal protein synthesis by insulin and in the absence of ribosomal and messenger ribonucleic acid formation. Biochemistry 19:1662-1669.
    • (1980) Biochemistry , vol.19 , pp. 1662-1669
    • DePhilip, R.M.1    Rudert, W.A.2    Lieberman, I.3
  • 16
    • 0026012413 scopus 로고
    • Translational control of ornithine aminotransferase: Modulation by initiation factor eIF-4E
    • Fagan, R. J., A. Lazaris-Karatzas, N. Sonenberg, and R. 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
    • Fagan, R.J.1    Lazaris-Karatzas, A.2    Sonenberg, N.3    Rozen, R.4
  • 21
    • 0026688510 scopus 로고
    • Substrate recognition determinants of the mitogen-activated 70K S6 kinase from rat liver
    • Flotow, H., and G. Thomas. 1992. Substrate recognition determinants of the mitogen-activated 70K S6 kinase from rat liver. J. Biol. Chem. 267:3074-3078.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3074-3078
    • Flotow, H.1    Thomas, G.2
  • 22
    • 0029890687 scopus 로고    scopus 로고
    • Activation of the translational suppressor 4E-BP1 following infection with encephalomyocarditis virus and poliovirus
    • Gingras, A.-C., Y. Svitkin, G. J. Belsham, A. Pause, and N. Sonenberg. 1996. Activation of the translational suppressor 4E-BP1 following infection with encephalomyocarditis virus and poliovirus. Proc. Natl. Acad. Sci. USA 93: 5578-5583.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5578-5583
    • Gingras, A.-C.1    Svitkin, Y.2    Belsham, G.J.3    Pause, A.4    Sonenberg, N.5
  • 23
    • 0024297326 scopus 로고
    • Insulin stimulates the translation of ribosomal proteins and the transcription of rDNA in mouse myoblasts
    • Hammond, M., and L. H. Bowman. 1988. Insulin stimulates the translation of ribosomal proteins and the transcription of rDNA in mouse myoblasts. J. Biol. Chem. 263:17785-17791.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17785-17791
    • Hammond, M.1    Bowman, L.H.2
  • 26
    • 0028856331 scopus 로고
    • When is a lipid kinase not a lipid kinase? When it is a protein kinase
    • Hunter, T. 1995. When is a lipid kinase not a lipid kinase? When it is a protein kinase. Cell 83:1-4.
    • (1995) Cell , vol.83 , pp. 1-4
    • Hunter, T.1
  • 27
    • 0028207001 scopus 로고
    • Rapamycin selectively represses translation of the "polypyrimidine tract" mRNA family Proc
    • 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 91:4441-4445.
    • (1994) Natl. Acad. Sci. USA , vol.91 , pp. 4441-4445
    • Jefferies, H.B.J.1    Reinhard, C.2    Kozma, S.C.3    Thomas, G.4
  • 28
    • 0028169728 scopus 로고
    • Elongation factor-1a mRNA is selectively translated following mitogenic stimulation
    • Jefferies, H. B. J., G. Thomas, and G. Thomas. 1994. Elongation factor-1a mRNA is selectively translated following mitogenic stimulation. J. Biol. Chem. 269:4367-4372.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4367-4372
    • Jefferies, H.B.J.1    Thomas, G.2    Thomas, G.3
  • 31
    • 0028156740 scopus 로고
    • S6k containing a bifurcation to histone H3-HMG-like protein phosphorylation and c-fos-c-jun induction
    • S6k containing a bifurcation to histone H3-HMG-like protein phosphorylation and c-fos-c-jun induction. Mol. Cell. Biol. 14:1066-1074.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1066-1074
    • Kardalinou, E.1    Zhelev, N.2    Hazzalin, C.A.3    Mahadevan, L.C.4
  • 33
    • 0026031446 scopus 로고
    • Epitope tagging and protein surveillance
    • Kolodziej, P. A., and R. A. Young. 1991. Epitope tagging and protein surveillance. Methods Enzymol. 194:508-519.
    • (1991) Methods Enzymol. , vol.194 , pp. 508-519
    • Kolodziej, P.A.1    Young, R.A.2
  • 34
    • 0023726116 scopus 로고
    • Identification of the 40S ribosomal protein S6 phosphorylation sites induced by cycloheximide
    • Krieg, J., J. Hofsteenge, and G. Thomas. 1988. Identification of the 40S ribosomal protein S6 phosphorylation sites induced by cycloheximide. J. Biol. Chem. 263:11473-11477.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11473-11477
    • Krieg, J.1    Hofsteenge, J.2    Thomas, G.3
  • 35
    • 0024262085 scopus 로고
    • Analysis of 40S ribosomal protein S6 phosphorylation during the mitogenic response
    • Krieg, J., A. R. Olivier, and G. Thomas. 1988. Analysis of 40S ribosomal protein S6 phosphorylation during the mitogenic response. Methods Enzymol. 164:575.
    • (1988) Methods Enzymol. , vol.164 , pp. 575
    • Krieg, J.1    Olivier, A.R.2    Thomas, G.3
  • 37
    • 0344438664 scopus 로고
    • S6 kinases and MAP kinases: Sequential intermediates in insulin/mitogen-activated protein kinase cascades
    • J. R. Woodgett (ed.). Oxford University Press, Oxford, United Kingdom
    • Kyriakis, J. M., and J. Avruch. 1994. S6 kinases and MAP kinases: sequential intermediates in insulin/mitogen-activated protein kinase cascades, p. 84-184. In J. R. Woodgett (ed.), Protein kinases. Oxford University Press, Oxford, United Kingdom.
    • (1994) Protein Kinases , pp. 84-184
    • Kyriakis, J.M.1    Avruch, J.2
  • 40
    • 0026318582 scopus 로고
    • Purification and properties of mitogen-activated S6 kinase from rat liver and 3T3 cells
    • Lane, H. A., and G. Thomas. 1991. Purification and properties of mitogen-activated S6 kinase from rat liver and 3T3 cells. Methods Enzymol. 200:269-291.
    • (1991) Methods Enzymol. , vol.200 , pp. 269-291
    • Lane, H.A.1    Thomas, G.2
  • 43
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4γ and the translational repressors 4E-binding proteins
    • Mader, S., H. Lee, A. Pause, and N. Sonenberg. 1995. The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4γ and the translational repressors 4E-binding proteins. Mol. Cell. Biol. 15:4990-4997.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 46
    • 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, Jr., M. F. White, 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 Jr., M.G.2    White, M.F.3    Rhoads, R.E.4
  • 47
    • 0000732112 scopus 로고    scopus 로고
    • Translational control of ribosomal protein mRNAs in eukaryotes
    • J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Meyuhas, O., D. Avni, and S. Shama. 1996. Translational control of ribosomal protein mRNAs in eukaryotes, p. 363-388. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , pp. 363-388
    • Meyuhas, O.1    Avni, D.2    Shama, S.3
  • 50
    • 0023522187 scopus 로고
    • Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2
    • Nairn, A. C., and H. C. Palfrey. 1987. Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2. J. Biol. Chem. 262:17299-17303.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17299-17303
    • Nairn, A.C.1    Palfrey, H.C.2
  • 52
    • 0025291205 scopus 로고
    • Translational dynamics. Interactions between the translational factors, tRNA and ribosomes during eukaryotic protein synthesis
    • Nygard, O., and L. Nilsson. 1990. Translational dynamics. Interactions between the translational factors, tRNA and ribosomes during eukaryotic protein synthesis. Eur. J. Biochem. 191:1-17.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 1-17
    • Nygard, O.1    Nilsson, L.2
  • 53
    • 0023711798 scopus 로고
    • Calcium phosphate-mediated gene transfer: A highly efficient transfection system for stably transforming cells with plasmid DNA
    • Okayama, H., and C. A. Chen. 1988. Calcium phosphate-mediated gene transfer: a highly efficient transfection system for stably transforming cells with plasmid DNA. BioTechniques 6:632-638.
    • (1988) BioTechniques , vol.6 , pp. 632-638
    • Okayama, H.1    Chen, C.A.2
  • 54
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • Pause, A., G. J. Belsham, A.-C. Gingras, O. Donzé, T. A. Lin, J. C. Lawrence, Jr., 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.-C.3    Donzé, O.4    Lin, T.A.5    Lawrence Jr., J.C.6    Sonenberg, N.7
  • 56
    • 0026759874 scopus 로고
    • Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase
    • Price, D. J., J. R. Grove, V. Calvo, J. Avruch, and B. E. Bierer. 1992. Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase. Science 257:973-977.
    • (1992) Science , vol.257 , pp. 973-977
    • Price, D.J.1    Grove, J.R.2    Calvo, V.3    Avruch, J.4    Bierer, B.E.5
  • 57
    • 0028114771 scopus 로고
    • Turned on by insulin
    • Proud, C. G. 1994. Turned on by insulin. Nature 371:747-748.
    • (1994) Nature , vol.371 , pp. 747-748
    • Proud, C.G.1
  • 58
    • 0029966106 scopus 로고    scopus 로고
    • Regulation of translation elongation factor-2 by insulin via a rapamycin-sensitive signalling pathway
    • Redpath, N. T., E. J. Foulstone, and C. G. Proud. 1996. Regulation of translation elongation factor-2 by insulin via a 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
  • 62
    • 0028558986 scopus 로고
    • Role of SAPK/ERK kinase-1 in the stress-activated pathway regulating transcription factor c-Jun
    • Sanchez, I., R. T. Hughes, B. J. Mayer, K. Yee, J. R. Woodgett, J. Avruch, J. M. Kyriakis, and L. I. Zon. 1994. Role of SAPK/ERK kinase-1 in the stress-activated pathway regulating transcription factor c-Jun. Nature 372: 794-798.
    • (1994) Nature , vol.372 , pp. 794-798
    • Sanchez, I.1    Hughes, R.T.2    Mayer, B.J.3    Yee, K.4    Woodgett, J.R.5    Avruch, J.6    Kyriakis, J.M.7    Zon, L.I.8
  • 63
    • 0029168362 scopus 로고
    • Overexpression of initiation factor eIF-4E does not relieve the translational repression of ribosomal protein mRNAs in quiescent cells
    • Shama, S., D. Avni, R. M. Frederickson, N. Sonenberg, and O. Meyuhas. 1995. Overexpression of initiation factor eIF-4E does not relieve the translational repression of ribosomal protein mRNAs in quiescent cells. Gene Expr. 4:241-252.
    • (1995) Gene Expr. , vol.4 , pp. 241-252
    • Shama, S.1    Avni, D.2    Frederickson, R.M.3    Sonenberg, N.4    Meyuhas, O.5
  • 64
    • 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
  • 65
    • 0023514624 scopus 로고
    • Separation of multiple phosphorylated forms of 40S ribosomal protein S6 by two dimensional polyacrylamide gel electrophoresis
    • Siegmann, M., and G. Thomas. 1987. Separation of multiple phosphorylated forms of 40S ribosomal protein S6 by two dimensional polyacrylamide gel electrophoresis. Methods Enzymol. 146:362-369.
    • (1987) Methods Enzymol. , vol.146 , pp. 362-369
    • Siegmann, M.1    Thomas, G.2
  • 66
    • 0000831271 scopus 로고    scopus 로고
    • MRNA 5′ cap-binding protein eIF4E and control of cell growth
    • J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Sonenberg, N. 1996. mRNA 5′ cap-binding protein eIF4E and control of cell growth, p. 245-269. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , pp. 245-269
    • Sonenberg, N.1
  • 68
    • 0027400484 scopus 로고
    • Identification of insulin stimulated protein kinase-1 as the rabbit equivalent of rskmo-2. Identification of two threonines phosphorylated during activation of mitogen-activated protein kinase
    • Sutherland, C., D. G. Campbell, and P. Cohen. 1993. Identification of insulin stimulated protein kinase-1 as the rabbit equivalent of rskmo-2. Identification of two threonines phosphorylated during activation of mitogen-activated protein kinase. Eur. J. Biochem. 212:581-588.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 581-588
    • Sutherland, C.1    Campbell, D.G.2    Cohen, P.3
  • 70
    • 0028939115 scopus 로고
    • Multiple independent inputs are required for activation of the p70 S6 kinase
    • Weng, Q.-P., K. Andrabi, M. T. Kozlowski, J. R. Grove, and J. Avruch. 1995. Multiple independent inputs are required for activation of the p70 S6 kinase. Mol. Cell. Biol. 15:2333-2340.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2333-2340
    • Weng, Q.-P.1    Andrabi, K.2    Kozlowski, M.T.3    Grove, J.R.4    Avruch, J.5
  • 71
    • 0030011629 scopus 로고    scopus 로고
    • Phosphorylation of eIF4E 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 eIF4E 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
    • 0028085078 scopus 로고
    • The insulin signalling system
    • White, M. F., and C. R. Kahn. 1994. The insulin signalling system. J. Biol. Chem. 269:1-4.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1-4
    • White, M.F.1    Kahn, C.R.2
  • 73
    • 0025177034 scopus 로고
    • Oncogenic activation of the human trk proto-oncogene by recombination with the ribosomal large subunit protein L7a
    • Ziemiecki, A., R. G. Müller, F. Xiao-Chang, N. E. Hynes, and S. Kozma. 1990. Oncogenic activation of the human trk proto-oncogene by recombination with the ribosomal large subunit protein L7a. EMBO J. 9:191-196.
    • (1990) EMBO J. , vol.9 , pp. 191-196
    • Ziemiecki, A.1    Müller, R.G.2    Xiao-Chang, F.3    Hynes, N.E.4    Kozma, S.5


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