메뉴 건너뛰기




Volumn 13, Issue 14, 2008, Pages 5359-5374

The Mnks: MAP kinase-interacting kinases (MAP kinase signal-integrating kinases)

Author keywords

Apoptosis; Cytokine; Initiation factor; MAP Kinase; Mnk; mRNA Translation; Review

Indexed keywords

EUKARYOTA;

EID: 52049088725     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3086     Document Type: Article
Times cited : (144)

References (94)
  • 1
    • 0030977270 scopus 로고    scopus 로고
    • MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates
    • DOI 10.1093/emboj/16.8.1921
    • Fukunaga R, and T. Hunter: Mnk1, a new MAP kinaseactivated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. EMBO J 16, 1921-1933 (1997) (Pubitemid 27170953)
    • (1997) EMBO Journal , vol.16 , Issue.8 , pp. 1921-1933
    • Fukunaga, R.1    Hunter, T.2
  • 2
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
    • DOI 10.1093/emboj/16.8.1909
    • Waskiewicz A. J, A. Flynn, C. G. Proud and J. A. Cooper: Mitogen-activated kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J 16, 1909-1920 (1997) (Pubitemid 27170952)
    • (1997) EMBO Journal , vol.16 , Issue.8 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3    Cooper, J.A.4
  • 3
    • 0032540244 scopus 로고    scopus 로고
    • The phosphorylation of eukaryotic initiation factor eIF4E in response to phorbol esters, cell stresses, and cytokines is mediated by distinct MAP kinase pathways
    • DOI 10.1074/jbc.273.16.9373
    • Wang X, A. Flynn, A. J. Waskiewicz, B. L. J. Webb, R. G. Vries, I. A. Baines, J. Cooper and C. G. Proud: The phosphorylation of eukaryotic initiation factor eIF4E in response to phorbol esters, cell stresses and cytokines is mediated by distinct MAP kinase pathways. J Biol Chem 273, 9373-9377 (1998) (Pubitemid 28183016)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.16 , pp. 9373-9377
    • Wang, X.1    Flynn, A.2    Waskiewicz, A.J.3    Webb, B.L.J.4    Vries, R.G.5    Baines, I.A.6    Cooper, J.A.7    Proud, C.G.8
  • 4
    • 0032981328 scopus 로고    scopus 로고
    • Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo
    • Waskiewicz A. J, J. C. Johnson, B. Penn, M. Mahalingam, S. R. Kimball and J. A. Cooper: Phosphorylation of the cap-binding protein eukaryotic translation factor 4E by protein kinase Mnk1 in vivo. Mol Cell Biol 19, 1871-1880 (1999) (Pubitemid 29098245)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.3 , pp. 1871-1880
    • Waskiewicz, A.J.1    Johnson, J.C.2    Penn, B.3    Mahalingam, M.4    Kimball, S.R.5    Cooper, J.A.6
  • 5
    • 3242719457 scopus 로고    scopus 로고
    • Mnk2 and Mnk1 are essential for constitutive and inducible phosphorylation of eukaryotic initiation factor 4E but not for cell growth or development
    • DOI 10.1128/MCB.24.15.6539-6549.2004
    • Ueda T, R. Watanabe-Fukunaga, H. Fukuyama, S. Nagata and R. Fukunaga: Mnk2 and Mnk1 are essential for constitutive and inducible phosphorylation of eukaryotic initiation factor 4E but not for cell growth or development. Mol Cell Biol 24, 6539-6549 (2004) (Pubitemid 38944335)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.15 , pp. 6539-6549
    • Ueda, T.1    Watanabe-Fukunaga, R.2    Fukuyama, H.3    Nagata, S.4    Fukunaga, R.5
  • 6
    • 2942530310 scopus 로고    scopus 로고
    • ERK and p38 MAPK-activated protein kinases: A family of protein kinases with diverse biological functions
    • DOI 10.1128/MMBR.68.2.320-344.2004
    • Roux P. P. and J. Blenis: ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions. Microbiol Mol Biol Rev 68, 320-344 (2004) (Pubitemid 38756868)
    • (2004) Microbiology and Molecular Biology Reviews , vol.68 , Issue.2 , pp. 320-344
    • Roux, P.P.1    Blenis, J.2
  • 7
    • 0034306706 scopus 로고    scopus 로고
    • Identification of the human Mnk2 gene (MKNK2) through protein interaction with estrogen receptor β
    • Slentz-Kesler K, J. T. Moore, M. Lombard, J. Zhang, R. Hollingsworth and M. P. Weiner: Identification of the human Mnk2 gene (MKNK2) through protein interaction with estrogen receptor β. Genomics 69, 63-71 (2000)
    • (2000) Genomics , vol.69 , pp. 63-71
    • Slentz-Kesler, K.1    Moore, J.T.2    Lombard, M.3    Zhang, J.4    Hollingsworth, R.5    Weiner, M.P.6
  • 9
    • 0037444809 scopus 로고    scopus 로고
    • Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity
    • DOI 10.1042/BJ20021806
    • Bardwell A. J, M. Abdollahi and L. Bardwell: Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity. Biochem J 370, 1077-1085 (2003) (Pubitemid 36399103)
    • (2003) Biochemical Journal , vol.370 , Issue.3 , pp. 1077-1085
    • Bardwell, A.J.1    Abdollahi, M.2    Bardwell, L.3
  • 10
    • 0034284131 scopus 로고    scopus 로고
    • Docking domains and substrate-specificity determination for MAP kinases
    • DOI 10.1016/S0968-0004(00)01627-3, PII S0968000400016273
    • Sharrocks A. D, S. H. Yang and A. Galanis: Docking domains and substrate-specificity determination for MAP kinases. Trends Biochem Sci. 25, 448-453 (2000) (Pubitemid 30662413)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.9 , pp. 448-453
    • Sharrocks, A.D.1    Yang, S.-H.2    Galanis, A.3
  • 11
    • 0033788484 scopus 로고    scopus 로고
    • A conserved docking motif in MAP kinases common to substrates, activators and regulators
    • Tanoue T, M. Adachi, T. Moriguchi and E. Nishida: A conserved docking motif in MAP kinases common to substrates, activators and regulators. Nat Cell Biol 2, 110-116 (2000)
    • (2000) Nat Cell Biol , vol.2 , pp. 110-116
    • Tanoue, T.1    Adachi, M.2    Moriguchi, T.3    Nishida, E.4
  • 12
    • 0034595707 scopus 로고    scopus 로고
    • 2-terminal UCR regions
    • DOI 10.1074/jbc.275.22.16609
    • MacKenzie S. J, G. S. Baillie, I. McPhee, G. B. Bolger and M. D. Houslay: ERK2 mitogen-activated protein kinase binding, phosphorylation, and regulation of the PDE4D cAMP-specific phosphodiesterases. The involvement of COOH-terminal docking sites and NH2-terminal UCR regions. J Biol Chem 275, 16609-16617 (2000) (Pubitemid 30398887)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 16609-16617
    • MacKenzie, S.J.1    Baillie, G.S.2    McPhee, I.3    Bolger, G.B.4    Houslay, M.D.5
  • 13
    • 4444258507 scopus 로고    scopus 로고
    • Identification and molecular characterization of Mnk1b, a splice variant of human MAP kinase-interacting kinase Mnk1
    • DOI 10.1016/j.yexcr.2004.06.006, PII S0014482704003325
    • O'Loghlen A, V. M. Gonzalez, D. Pineiro, M. I. Perez-Morgado, M. Salinas and M. E. Martin: Identification and molecular characterization of Mnk1b, a splice variant of human MAP kinase-interacting kinase Mnk1. Exp Cell Res. 299, 343-355 (2004) (Pubitemid 39179802)
    • (2004) Experimental Cell Research , vol.299 , Issue.2 , pp. 343-355
    • O'Loghlen, A.1    Gonzalez, V.M.2    Pineiro, D.3    Perez-Morgado, M.I.4    Salinas, M.5    Martin, M.E.6
  • 14
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4E
    • DOI 10.1093/emboj/18.1.270
    • Pyronnet S, H. Imataka, A. C. Gingras, R. Fukunaga, T. Hunter and N. Sonenberg: Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4E. EMBO J 18, 270-279 (1999) (Pubitemid 29005042)
    • (1999) EMBO Journal , vol.18 , Issue.1 , pp. 270-279
    • Pyronnet, S.1    Imataka, H.2    Gingras, A.-C.3    Fukunaga, R.4    Hunter, T.5    Sonenberg, N.6
  • 15
    • 0242497942 scopus 로고    scopus 로고
    • Features in the N and C termini of the MAPK-interacting kinase Mnk1 mediate its nucleocytoplasmic shuttling
    • DOI 10.1074/jbc.M302398200
    • Parra-Palau J. L, G. C. Scheper, M. L. Wilson and C. G. Proud: Features in the N and C termini of the MAPKinteracting kinase Mnk1 mediate its nucleocytoplasmic shuttling. J Biol Chem 278, 44197-44204 (2003) (Pubitemid 37377163)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 44197-44204
    • Parra-Palau, J.-L.1    Scheper, G.C.2    Wilson, M.L.3    Proud, C.G.4
  • 16
    • 0043133828 scopus 로고    scopus 로고
    • The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization
    • DOI 10.1128/MCB.23.16.5692-5705.2003
    • Scheper G. C, J.-L. Parra, M. L. Wilson, B. van Kollenburg, A. C. O. Vertegaal, Z.-G. Han and C. G. Proud: The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization. Mol Cell Biol 23, 5692-5705 (2003) (Pubitemid 36951333)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.16 , pp. 5692-5705
    • Scheper, G.C.1    Parra, J.L.2    Wilson, M.3    Van Kollenburg, B.4    Vertegaal, A.C.O.5    Han, Z.-G.6    Proud, C.G.7
  • 17
    • 0035133659 scopus 로고    scopus 로고
    • The MAP kinase signal-integrating kinase Mnk2 is an eIF4E kinase with high basal activity in mammalian cells
    • Scheper G. C, N. A. Morrice, M. Kleijn and C. G. Proud: The MAP kinase signal-integrating kinase Mnk2 is an eIF4E kinase with high basal activity in mammalian cells. Mol Cell Biol 21, 743-754 (2001)
    • (2001) Mol Cell Biol , vol.21 , pp. 743-754
    • Scheper, G.C.1    Morrice, N.A.2    Kleijn, M.3    Proud, C.G.4
  • 19
    • 0029831037 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein (MAP) kinase pathway by pervanadate, a potent inhibitor of tyrosine phosphatases
    • DOI 10.1074/jbc.271.36.22251
    • Zhao Z, Z. Tan, C. D. Diltz, M. You and E. H. Fischer: Activation of mitogen-activated protein (MAP) kinase pathway by pervanadate, a potent inhibitor of tyrosine phosphatases. J Biol Chem 271, 22251-22255 (1996) (Pubitemid 26303861)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.36 , pp. 22251-22255
    • Zhao, Z.1    Tan, Z.2    Diltz, C.D.3    You, M.4    Fischer, E.H.5
  • 20
    • 27844500638 scopus 로고    scopus 로고
    • Features of the catalytic domains and C termini of the MAPK signal-integrating kinases Mnk1 and Mnk2 determine their differing activities and regulatory properties
    • DOI 10.1074/jbc.M508356200
    • Parra J. L, M. Buxade and C. G. Proud: Features of the catalytic domains and C termini of the MAPK signal-integrating kinases Mnk1 and Mnk2 determine their differing activities and regulatory properties. J Biol Chem 280, 37623-37633 (2005) (Pubitemid 41642371)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.45 , pp. 37623-37633
    • Parra, J.L.1    Buxade, M.2    Proud, C.G.3
  • 21
    • 26444592983 scopus 로고    scopus 로고
    • Crystal structures of the Mnk2 kinase domain reveal an inhibitory conformation and a zinc binding site
    • DOI 10.1016/j.str.2005.07.013, PII S0969212605002728
    • Jauch R, S. Jakel, C. Netter, K. Schreiter, B. Aicher, H. Jackle and M. C. Wahl: Crystal structures of the Mnk2 kinase domain reveal an inhibitory conformation and a zinc binding site. Structure 13, 1559-1568 (2005) (Pubitemid 41427594)
    • (2005) Structure , vol.13 , Issue.10 , pp. 1559-1568
    • Jauch, R.1    Jakel, S.2    Netter, C.3    Schreiter, K.4    Aicher, B.5    Jackle, H.6    Wahl, M.C.7
  • 22
    • 33748358167 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases interacting kinases are autoinhibited by a reprogrammed activation segment
    • DOI 10.1038/sj.emboj.7601285, PII 7601285
    • Jauch R, M. K. Cho, S. Jakel, C. Netter, K. Schreiter, B. Aicher, M. Zweckstetter, H. Jackle and M. C. Wahl: Mitogen-activated protein kinases interacting kinases are autoinhibited by a reprogrammed activation segment. EMBO J 25, 4020-4032 (2006) (Pubitemid 44338744)
    • (2006) EMBO Journal , vol.25 , Issue.17 , pp. 4020-4032
    • Jauch, R.1    Cho, M.-K.2    Jakel, S.3    Netter, C.4    Schreiter, K.5    Aicher, B.6    Zweckstetter, M.7    Jackle, H.8    Wahl, M.C.9
  • 24
    • 23844516065 scopus 로고    scopus 로고
    • The Mnks are novel components in the control of TNFα biosynthesis and phosphorylate and regulate hnRNP A1
    • DOI 10.1016/j.immuni.2005.06.009, PII S1074761305002128
    • Buxade M, J. L. Parra, S. Rousseau, N. Shpiro, R. Marquez, N. Morrice, J. Bain, E. Espel and C. G. Proud: The Mnks Are Novel Components in the Control of TNFalpha Biosynthesis and Phosphorylate and Regulate hnRNP A1. Immunity 23, 177-189 (2005) (Pubitemid 41169287)
    • (2005) Immunity , vol.23 , Issue.2 , pp. 177-189
    • Buxade, M.1    Parra, J.L.2    Rousseau, S.3    Shpiro, N.4    Marquez, R.5    Morrice, N.6    Bain, J.7    Espel, E.8    Proud, C.G.9
  • 25
    • 33746516731 scopus 로고    scopus 로고
    • hnRNP A1 relocalization to the stress granules reflects a role in the stress response
    • DOI 10.1128/MCB.00224-06
    • Guil S, J. C. Long and J. F. Caceres: hnRNP A1 relocalization to the stress granules reflects a role in the stress response. Mol Cell Biol 26, 5744-5758 (2006) (Pubitemid 44134331)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.15 , pp. 5744-5758
    • Guil, S.1    Long, J.C.2    Caceres, J.F.3
  • 26
    • 38049153326 scopus 로고    scopus 로고
    • The PSF/p54nrb complex is a novel Mnk substrate that binds the mRNA for TNFalpha
    • Buxade M, N. Morrice, D. L. Krebs and C. G. Proud: The PSF/p54nrb complex is a novel Mnk substrate that binds the mRNA for TNFalpha. J Biol Chem 283, 57-65 (2007)
    • (2007) J Biol Chem , vol.283 , pp. 57-65
    • Buxade, M.1    Morrice, N.2    Krebs, D.L.3    Proud, C.G.4
  • 28
    • 33644521566 scopus 로고    scopus 로고
    • Regulation of sprouty stability by mnk1-dependent phosphorylation
    • Dasilva J, L. Xu, H. J. Kim, W. T. Miller and D. Bar-Sagi: Regulation of sprouty stability by mnk1-dependent phosphorylation. Mol Cell Biol 26, 1898-1907 (2006)
    • (2006) Mol Cell Biol , vol.26 , pp. 1898-1907
    • Dasilva, J.1    Xu, L.2    Kim, H.J.3    Miller, W.T.4    Bar-Sagi, D.5
  • 29
    • 0036438924 scopus 로고    scopus 로고
    • Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation?
    • DOI 10.1046/j.1432-1033.2002.03291.x
    • Scheper G. C. and C. G. Proud: Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation? Eur J Biochem 269, 5350-5359 (2002) (Pubitemid 35365524)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.22 , pp. 5350-5359
    • Scheper, G.C.1    Proud, C.G.2
  • 30
    • 0034928792 scopus 로고    scopus 로고
    • Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2
    • DOI 10.1128/MCB.21.16.5500-5511.2001
    • Knauf U, C. Tschopp and H. Gram: Negative regulation of protein translation by mitogen-activated protein kinaseinteracting kinases 1 and 2. Mol Cell Biol 21, 5500-5511 (2001) (Pubitemid 32702454)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.16 , pp. 5500-5511
    • Knauf, U.1    Tschopp, C.2    Gram, H.3
  • 32
    • 4544229717 scopus 로고    scopus 로고
    • 5-HT stimulates eEF2 dephosphorylation in a rapamycin-sensitive manner in Aplysia neurites
    • DOI 10.1111/j.1471-4159.2004.02634.x
    • Carroll M, O. Warren, X. Fan and W. S. Sossin: 5-HT stimulates eEF2 dephosphorylation in a rapamycinsensitive manner in Aplysia neurites. J Neurochem 90, 1464-1476 (2004) (Pubitemid 39223649)
    • (2004) Journal of Neurochemistry , vol.90 , Issue.6 , pp. 1464-1476
    • Carroll, M.1    Warren, O.2    Fan, X.3    Sossin, W.S.4
  • 33
    • 33644947020 scopus 로고    scopus 로고
    • Mnk is a negative regulator of cap-dependent translation in Aplysia neurons
    • Ross G, J. R. Dyer, V. F. Castellucci and W. S. Sossin: Mnk is a negative regulator of cap-dependent translation in Aplysia neurons. J Neurochem 97, 79-91 (2006)
    • (2006) J Neurochem , vol.97 , pp. 79-91
    • Ross, G.1    Dyer, J.R.2    Castellucci, V.F.3    Sossin, W.S.4
  • 34
    • 0036479313 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA
    • DOI 10.1074/jbc.M103607200
    • Scheper G. C, B. van Kollenburg, J. Hu, Y. Luo, D. J. Goss and C. G. Proud: Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA. J Biol Chem 277, 3303-3309 (2002) (Pubitemid 34953196)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3303-3309
    • Scheper, G.C.1    Van Kollenburg, B.2    Hu, J.3    Luo, Y.4    Goss, D.J.5    Proud, C.G.6
  • 35
    • 0037031845 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initiation factor (eIF) 4E is not required for de novo protein synthesis following recovery from hypertonic stress in human kidney cells
    • DOI 10.1074/jbc.C200376200
    • Morley S. J. and S. Naegele: Phosphorylation of eukaryotic initiation factor (eIF) 4E is not required for de novo protein synthesis following recovery from hypertonic stress in human kidney cells. J Biol Chem 277, 32855-32859 (2002) (Pubitemid 34984797)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 32855-32859
    • Morley, S.J.1    Naegele, S.2
  • 36
    • 1842831274 scopus 로고    scopus 로고
    • Phosphorylation of eIF4E by Mnk-1 enhances HSV-1 translation and replication in quiescent cells
    • DOI 10.1101/gad.1185304
    • Walsh D. and I. Mohr: Phosphorylation of eIF4E by Mnk-1 enhances HSV-1 translation and replication in quiescent cells. Genes Dev 18, 660-672 (2004) (Pubitemid 38489934)
    • (2004) Genes and Development , vol.18 , Issue.6 , pp. 660-672
    • Walsh, D.1    Mohr, I.2
  • 37
    • 20744448501 scopus 로고    scopus 로고
    • Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells
    • DOI 10.1128/JVI.79.13.8057-8064.2005
    • Walsh D, C. Perez, J. Notary and I. Mohr: Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells. J Virol 79, 8057-8064 (2005) (Pubitemid 40853509)
    • (2005) Journal of Virology , vol.79 , Issue.13 , pp. 8057-8064
    • Walsh, D.1    Perez, C.2    Notary, J.3    Mohr, I.4
  • 39
    • 35648962915 scopus 로고    scopus 로고
    • Inhibition of mammalian target of rapamycin induces phosphatidylinositol 3-kinase-dependent and Mnk-mediated eukaryotic translation initiation factor 4E phosphorylation
    • DOI 10.1128/MCB.00760-07
    • Wang X, P. Yue, C. B. Chan, K. Ye, T. Ueda, R. Watanabe-Fukunaga, R. Fukunaga, H. Fu, F. R. Khuri and S. Y. Sun: Inhibition of mammalian target of rapamycin induces phosphatidylinositol 3-kinase-dependent and Mnkmediated eukaryotic translation initiation factor 4E phosphorylation. Mol Cell Biol 27, 7405-7413 (2007) (Pubitemid 350033648)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.21 , pp. 7405-7413
    • Wang, X.1    Yue, P.2    Chan, C.-B.3    Ye, K.4    Ueda, T.5    Watanabe-Fukunaga, R.6    Fukunaga, R.7    Fu, H.8    Khuri, F.R.9    Sun, S.-Y.10
  • 40
    • 0002411516 scopus 로고    scopus 로고
    • Physical and functional interactions between the mRNA cap structure and the poly (A) tail
    • (Sonenberg, N, Hershey, J.W.B. and Mathews, M.B. Eds.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Sachs A. (2000) Physical and functional interactions between the mRNA cap structure and the poly (A) tail. In Translational control of gene expression (Sonenberg, N, Hershey, J.W.B. and Mathews, M.B. Eds.), pp. 447-465. Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (2000) Translational Control of Gene Expression , pp. 447-465
    • Sachs, A.1
  • 41
    • 33846991130 scopus 로고    scopus 로고
    • The mechanism of translation initiation in eukaryotes
    • (Mathews, M.B, Sonenberg, N. and Hershey, J.W.B. Eds.). Cold Spring Harbor Laboratory Press.
    • PestovaT.V, Lorsch, J.R. and Hellen, C.U.T. (2006) The mechanism of translation initiation in eukaryotes. In Translational Control in Biology and Medicine (Mathews, M.B, Sonenberg, N. and Hershey, J.W.B. Eds.), pp. 87-128. Cold Spring Harbor Laboratory Press.
    • (2006) Translational Control in Biology and Medicine , pp. 87-128
    • Pestova, T.V.1    Lorsch, J.R.2    Hellen, C.U.T.3
  • 42
    • 31144448042 scopus 로고    scopus 로고
    • AU-rich elements and associated factors: Are there unifying principles?
    • DOI 10.1093/nar/gki1012
    • Barreau C, L. Paillard and H. B. Osborne: AU-rich elements and associated factors: are there unifying principles? Nucleic Acids Res 33, 7138-7150 (2005) (Pubitemid 43125082)
    • (2005) Nucleic Acids Research , vol.33 , Issue.22 , pp. 7138-7150
    • Barreau, C.1    Paillard, L.2    Osborne, H.B.3
  • 43
    • 12344319508 scopus 로고    scopus 로고
    • The role of the AU-rich elements of mRNAs in controlling translation
    • DOI 10.1016/j.semcdb.2004.11.008, PII S1084952104001120, Protein Synthesis in Health and Disease
    • Espel E.: The role of the AU-rich elements of mRNAs in controlling translation. Semin Cell Dev Biol . 16, 59-67 (2005) (Pubitemid 40136538)
    • (2005) Seminars in Cell and Developmental Biology , vol.16 , Issue.1 , pp. 59-67
    • Espel, E.1
  • 44
    • 1342322145 scopus 로고    scopus 로고
    • Translational control by MAPK signaling in long-term synaptic plasticity and memory
    • DOI 10.1016/S0092-8674(04)00115-1, PII S0092867404001151
    • Kelleher R. J, III, A. Govindarajan, H. Y. Jung, H. Kang and S. Tonegawa: Translational control by MAPK signaling in long-term synaptic plasticity and memory. Cell 116, 467-479 (2004) (Pubitemid 38366322)
    • (2004) Cell , vol.116 , Issue.3 , pp. 467-479
    • Kelleher III, R.J.1    Govindarajan, A.2    Jung, H.-Y.3    Kang, H.4    Tonegawa, S.5
  • 46
    • 20444482051 scopus 로고    scopus 로고
    • MEK-ERK signaling controls Hdm2 oncoprotein expression by regulating hdm2 mRNA export to the cytoplasm
    • DOI 10.1074/jbc.M412334200
    • Phelps M, A. Phillips, M. Darley and J. P. Blaydes: MEK-ERK signaling controls Hdm2 oncoprotein expression by regulating hdm2 mRNA export to the cytoplasm. J Biol Chem 280, 16651-16658 (2005) (Pubitemid 41389122)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 16651-16658
    • Phelps, M.1    Phillips, A.2    Darley, M.3    Blaydes, J.P.4
  • 48
    • 34548241289 scopus 로고    scopus 로고
    • Tristetraprolin regulates TNF TNF-α mRNA stability via a proteasome dependent mechanism involving the combined action of the ERK and p38 pathways
    • DOI 10.1016/j.molimm.2007.05.017, PII S0161589007002271
    • Deleault K. M, S. J. Skinner and S. A. Brooks: Tristetraprolin regulates TNF TNF-alpha mRNA stability via a proteasome dependent mechanism involving the combined action of the ERK and p38 pathways. Mol Immunol 45, 13-24 (2008) (Pubitemid 47331659)
    • (2008) Molecular Immunology , vol.45 , Issue.1 , pp. 13-24
    • Deleault, K.M.1    Skinner, S.J.2    Brooks, S.A.3
  • 50
    • 32344445358 scopus 로고    scopus 로고
    • Posttranscriptional regulation of TNFα expression via eukaryotic initiation factor 4E (eIF4E) phosphorylation in mouse macrophages
    • DOI 10.1016/j.cyto.2005.11.017, PII S1043466605003467
    • Andersson K. and R. Sundler: Posttranscriptional regulation of TNFalpha expression via eukaryotic initiation factor 4E (eIF4E) phosphorylation in mouse macrophages. Cytokine 33, 52-7 (2006) (Pubitemid 43220353)
    • (2006) Cytokine , vol.33 , Issue.1 , pp. 52-57
    • Andersson, K.1    Sundler, R.2
  • 53
    • 0028215301 scopus 로고
    • RNA binding specificity of hnRNP A1: Significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicing
    • Burd C. G. and G. Dreyfuss: RNA binding specificity of hnRNP A1: significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicing. EMBO J 13, 1197-1204 (1994) (Pubitemid 24074726)
    • (1994) EMBO Journal , vol.13 , Issue.5 , pp. 1197-1204
    • Burd, C.G.1    Dreyfuss, G.2
  • 54
    • 0028178987 scopus 로고
    • The A1 and A1B proteins of heterogeneous nuclear ribonucleoparticles modulate 5' splice site selection in vivo
    • Yang X, M. R. Bani, S. J. Lu, S. Rowan, Y. Ben-David and B. Chabot: The A1 and A1B proteins of heterogeneous nuclear ribonucleoparticles modulate 5' splice site selection in vivo. Proc Natl Acad Sci USA 91, 6924-6928 (1994)
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6924-6928
    • Yang, X.1    Bani, M.R.2    Lu, S.J.3    Rowan, S.4    Ben-David, Y.5    Chabot, B.6
  • 55
    • 14244249827 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A1 is a novel internal ribosome entry site trans-acting factor that modulates alternative initiation of translation of the fibroblast growth factor 2 mRNA
    • DOI 10.1074/jbc.M411492200
    • Bonnal S, F. Pileur, C. Orsini, F. Parker, F. Pujol, A. C. Prats and S. Vagner: Heterogeneous nuclear ribonucleoprotein A1 is a novel internal ribosome entry site trans-acting factor that modulates alternative initiation of translation of the fibroblast growth factor 2 mRNA. J Biol Chem 280, 4144-4153 (2005) (Pubitemid 40288579)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4144-4153
    • Bonnal, S.1    Pileur, F.2    Orsini, C.3    Parker, F.4    Pujol, F.5    Prats, A.-C.6    Vagner, S.7
  • 56
    • 37049030005 scopus 로고    scopus 로고
    • Cytoplasmic relocalization of heterogeneous nuclear ribonucleoprotein A1 controls translation initiation of specific mRNAs
    • DOI 10.1091/mbc.E07-06-0603
    • Cammas A, F. Pileur, S. Bonnal, S. M. Lewis, N. Leveque, M. Holcik and S. Vagner: Cytoplasmic Relocalization of Heterogeneous Nuclear Ribonucleoprotein A1 Controls Translation Initiation of Specific mRNAs. Mol Biol Cell 18, 5048-5059 (2007) (Pubitemid 350246704)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.12 , pp. 5048-5059
    • Cammas, A.1    Pileur, F.2    Bonnal, S.3    Lewis, S.M.4    Leveque, N.5    Holcik, M.6    Vagner, S.7
  • 57
    • 0027523417 scopus 로고
    • Association of heterogeneous nuclear ribonucleoprotein A1 and C proteins with reiterated AUUUA sequences
    • Hamilton B. J, E. Nagy, J. S. Malter, B. A. Arrick and W. F. Rigby: Association of heterogeneous nuclear ribonucleoprotein A1 and C proteins with reiterated AUUUA sequences. J Biol Chem 268, 8881-8887 (1993) (Pubitemid 23118680)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.12 , pp. 8881-8887
    • Hamilton, B.J.1    Nagy, E.2    Malter, J.S.3    Arrick, B.A.4    Rigby, W.F.C.5
  • 58
    • 0030724902 scopus 로고    scopus 로고
    • Modulation of AUUUA response element binding by heterogeneous nuclear ribonucleoprotein A1 in human T lymphocytes: The roles of cytoplasmic location, transcription, and phosphorylation
    • DOI 10.1074/jbc.272.45.28732
    • Hamilton B. J, C. M. Burns, R. C. Nichols and W. F. Rigby: Modulation of AUUUA response element binding by heterogeneous nuclear ribonucleoprotein A1 in human T lymphocytes. The roles of cytoplasmic location, transcription, and phosphorylation. J Biol Chem 272, 28732-28741 (1997) (Pubitemid 27517831)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.45 , pp. 28732-28741
    • Hamilton, B.J.1    Burns, C.M.2    Nichols, R.C.3    Rigby, W.F.C.4
  • 59
    • 0027938535 scopus 로고
    • Enhanced stability of interleukin-2 mRNA in MLA 144 cells. Possible role of cytoplasmic AU-rich sequence-binding proteins
    • Henics T, A. Sanfridson, B. J. Hamilton, E. Nagy and W. F. Rigby: Enhanced stability of interleukin-2 mRNA in MLA 144 cells. Possible role of cytoplasmic AU-rich sequence-binding proteins. J Biol Chem 269, 5377-5383 (1994)
    • (1994) J Biol Chem , vol.269 , pp. 5377-5383
    • Henics, T.1    Sanfridson, A.2    Hamilton, B.J.3    Nagy, E.4    Rigby, W.F.5
  • 60
    • 0007570010 scopus 로고    scopus 로고
    • The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation
    • DOI 10.1083/jcb.149.2.307
    • van der Houven van Oordt, M. T. az-Meco, J. Lozano, A. R. Krainer, J. Moscat and J. F. Caceres: The MKK (3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation. J Cell Biol 149, 307-316 (2000) (Pubitemid 30227149)
    • (2000) Journal of Cell Biology , vol.149 , Issue.2 , pp. 307-316
    • Van Oordt, W.V.D.H.1    Diaz-Meco, M.T.2    Lozano, J.3    Krainer, A.R.4    Moscat, J.5    Caceres, J.F.6
  • 64
    • 34250797537 scopus 로고    scopus 로고
    • Specific trans-acting proteins interact with auxiliary RNA polyadenylation elements in the COX-2 3′-UTR
    • DOI 10.1261/rna.577707
    • Hall-Pogar T, S. Liang, L. K. Hague and C. S. Lutz: Specific trans-acting proteins interact with auxiliary RNA polyadenylation elements in the COX-2 3'-UTR. RNA 13, 1103-1115 (2007) (Pubitemid 46984900)
    • (2007) RNA , vol.13 , Issue.7 , pp. 1103-1115
    • Hall-Pogar, T.1    Liang, S.2    Hague, L.K.3    Lutz, C.S.4
  • 65
    • 0035159666 scopus 로고    scopus 로고
    • Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions
    • Shav-Tal Y, M. Cohen, S. Lapter, B. Dye, J. G. Patton, J. Vandekerckhove and D. Zipori: Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions. Mol Biol Cell 12, 2328-2340 (2001) (Pubitemid 33051959)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.8 , pp. 2328-2340
    • Shav-Tal, Y.1    Cohen, M.2    Lapter, S.3    Dye, B.4    Patton, J.G.5    Vandekerckhove, J.6    Zipori, D.7
  • 66
    • 0034663495 scopus 로고    scopus 로고
    • Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion
    • Akhmedov A. T. and B. S. Lopez: Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion. Nucleic Acids Res 28, 3022-3030 (2000) (Pubitemid 30624091)
    • (2000) Nucleic Acids Research , vol.28 , Issue.16 , pp. 3022-3030
    • Akhmedov, A.T.1    Lopez, B.S.2
  • 67
    • 0030774839 scopus 로고    scopus 로고
    • The prooncoprotein EWS binds calmodulin and is phosphorylated by protein kinase C through an IQ domain
    • DOI 10.1074/jbc.272.43.27369
    • Deloulme J. C, L. Prichard, O. Delattre and D. R. Storm: The prooncoprotein EWS binds calmodulin and is phosphorylated by protein kinase C through an IQ domain. J Biol Chem 272, 27369-27377 (1997) (Pubitemid 27452704)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.43 , pp. 27369-27377
    • Deloulme, J.C.1    Prichard, L.2    Delattre, O.3    Storm, D.R.4
  • 68
    • 33846268431 scopus 로고    scopus 로고
    • Phosphorylation by SR kinases regulates the binding of PTB-associated splicing factor (PSF) to the pre-mRNA polypyrimidine tract
    • DOI 10.1016/j.febslet.2006.12.015, PII S0014579306014529
    • Huang C. J, Z. Tang, R. J. Lin and P. W. Tucker: Phosphorylation by SR kinases regulates the binding of PTB-associated splicing factor (PSF) to the pre-mRNA polypyrimidine tract. FEBS Lett 581, 223-232 (2007) (Pubitemid 46110829)
    • (2007) FEBS Letters , vol.581 , Issue.2 , pp. 223-232
    • Huang, C.-J.1    Tang, Z.2    Lin, R.-J.3    Tucker, P.W.4
  • 69
    • 13444259420 scopus 로고    scopus 로고
    • nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1
    • DOI 10.1016/j.jmb.2004.12.034
    • Proteau A, S. Blier, A. L. Albert, S. B. Lavoie, A. M. Traish and M. Vincent: The multifunctional nuclear protein p54nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1. J Mol Biol 346, 1163-1172 (2005) (Pubitemid 40215536)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.4 , pp. 1163-1172
    • Proteau, A.1    Blier, S.2    Albert, A.L.3    Lavoie, S.B.4    Traish, A.M.5    Vincent, M.6
  • 70
    • 0037032415 scopus 로고    scopus 로고
    • nrb/NonO - Multi-functional nuclear proteins
    • DOI 10.1016/S0014-5793(02)03447-6, PII S0014579302034476
    • Shav-Tal Y. and D. Zipori: PSF and p54 (nrb)/NonO-multi-functional nuclear proteins. FEBS Lett 531, 109-114 (2002) (Pubitemid 35341179)
    • (2002) FEBS Letters , vol.531 , Issue.2 , pp. 109-114
    • Shav-Tal, Y.1    Zipori, D.2
  • 71
    • 33845987501 scopus 로고    scopus 로고
    • The VASPSpred-Sprouty domain puzzle
    • Bundschu K, U. Walter and K. Schuh: The VASPSpred-Sprouty domain puzzle. J Biol Chem 281, 36477-36481 (2006)
    • (2006) J Biol Chem , vol.281 , pp. 36477-36481
    • Bundschu, K.1    Walter, U.2    Schuh, K.3
  • 72
    • 0033756163 scopus 로고    scopus 로고
    • A misexpression sreen identifies genes that can modulate RAS1 pathway signaling in Drosophila melanogaster
    • Huang A. M. and G. M. Rubin: A misexpression sreen identifies genes that can modulate RAS1 pathway signaling in Drosophila melanogaster. Genetics 156, 1219-1230 (2000)
    • (2000) Genetics , vol.156 , pp. 1219-1230
    • Huang, A.M.1    Rubin, G.M.2
  • 75
    • 33744493376 scopus 로고    scopus 로고
    • Targeting tyrosine kinases in cancer: The second wave
    • DOI 10.1126/science.1125951
    • Baselga J.: Targeting tyrosine kinases in cancer: the second wave. Science 312, 1175-1178 (2006) (Pubitemid 43801135)
    • (2006) Science , vol.312 , Issue.5777 , pp. 1175-1178
    • Baselga, J.1
  • 78
    • 0035881526 scopus 로고    scopus 로고
    • PML RING suppresses oncogenic transformation by reducing the affinity of eIF4E for mRNA
    • DOI 10.1093/emboj/20.16.4547
    • Cohen N, M. Sharma, A. Kentsis, J. M. Perez, S. Strudwick and K. L. B. Borden: PML RING suppresses oncogenic transformation by reducing the affinity of eIF4E for mRNA. EMBO J 20, 4547-4559 (2001) (Pubitemid 32772048)
    • (2001) EMBO Journal , vol.20 , Issue.16 , pp. 4547-4559
    • Cohen, N.1    Sharma, M.2    Kentsis, A.3    Perez, J.M.4    Strudwick, S.5    Borden, K.L.B.6
  • 80
    • 0036516869 scopus 로고    scopus 로고
    • The emerging roles of translation factor eIF4E in the nucleus
    • DOI 10.1046/j.1432-0436.2002.700102.x
    • Strudwick S. and K. L. Borden: The emerging roles for translation factor eIF4E in the nucleus. Differentiation 70, 10-22 (2002) (Pubitemid 38232695)
    • (2002) Differentiation , vol.70 , Issue.1 , pp. 10-22
    • Strudwick, S.1    Borden, K.L.B.2
  • 81
    • 2342489456 scopus 로고    scopus 로고
    • eIF-4E expression and its role in malignancies and metastases
    • DOI 10.1038/sj.onc.1207545
    • De Benedetti A. and J. R. Graff: eIF-4E expression and its role in malignancies and metastases. Oncogene 23, 3189-3199 (2004) (Pubitemid 38638830)
    • (2004) Oncogene , vol.23 , Issue.18 , pp. 3189-3199
    • De Benedetti, A.1    Graff, J.R.2
  • 82
    • 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: Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5' cap. Nature 345, 544-547 (1990)
    • (1990) Nature , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 84
    • 0030041884 scopus 로고    scopus 로고
    • Translation initiation of ornithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 4E
    • DOI 10.1073/pnas.93.3.1065
    • Rousseau D, R. Kaspar, I. Rosenwald, L. Gehrke and N. Sonenberg: Translation initiation of ornithine decarboxylase and nucleocytoplasmic transport of cyclin D1 messenger-RNA are increased in cells overexpressing eukaryotic initiation factor 4E. Proc Natl Acad Sci USA 93, 1065-1070 (1996) (Pubitemid 26054368)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.3 , pp. 1065-1070
    • Rousseau, D.1    Kaspar, R.2    Rosenwald, I.3    Gehrke, L.4    Sonenberg, N.5
  • 86
    • 79959572144 scopus 로고    scopus 로고
    • MNK1 and EIF4E are downstream effectors of MEKs in the regulation of the nuclear export of HDM2 mRNA
    • Phillips A. and J. P. Blaydes: MNK1 and EIF4E are downstream effectors of MEKs in the regulation of the nuclear export of HDM2 mRNA. Oncogene 2007)
    • (2007) Oncogene
    • Phillips, A.1    Blaydes, J.P.2
  • 87
    • 9244228003 scopus 로고    scopus 로고
    • Phosphorylation of the eukaryotic translation initiation factor eIF4E contributes to its transformation and mRNA transport activities
    • DOI 10.1158/0008-5472.CAN-04-2677
    • Topisirovic I, M. Ruiz-Gutierrez and K. L. Borden: Phosphorylation of the eukaryotic translation initiation factor eIF4E contributes to its transformation and mRNA transport activities. Cancer Res 64, 8639-8642 (2004) (Pubitemid 39552077)
    • (2004) Cancer Research , vol.64 , Issue.23 , pp. 8639-8642
    • Topisirovic, I.1    Ruiz-Gutierrez, M.2    Borden, K.L.B.3
  • 88
    • 0031045972 scopus 로고    scopus 로고
    • LK6, a short lived protein kinase in Drosophila that can associate with microtubules and centrosomes
    • Kidd D. and J. W. Raff: LK6, a short-lived protein kinase in Drosophila that can associate with microtubules and centrosomes. J Cell Sci 110, 209-219 (1997) (Pubitemid 27075865)
    • (1997) Journal of Cell Science , vol.110 , Issue.2 , pp. 209-219
    • Kidd, D.1    Raff, J.W.2
  • 89
    • 0036178103 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic translation initiation factor 4E is critical for growth
    • DOI 10.1128/MCB.22.6.1656-1663.2002
    • Lachance P. E. D, M. Miron, B. Raught, N. Sonenberg and P. Lasko: Phosphorylation of eukaryotic translation initiation factor 4E is critical for growth. Mol Cell Biol 22, 1656-1663 (2002) (Pubitemid 34174983)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.6 , pp. 1656-1663
    • Lachance, P.E.D.1    Miron, M.2    Raught, B.3    Sonenberg, N.4    Lasko, P.5
  • 90
    • 13444309336 scopus 로고    scopus 로고
    • The Drosophila protein kinase LK6 is regulated by ERK and phosphorylates the eukaryotic initiation factor eIF4E in vivo
    • DOI 10.1042/BJ20040769
    • Parra-Palau J. L, G. C. Scheper, D. E. Harper and C. G. Proud: The Drosophila protein kinase LK6 is regulated by ERK and phosphorylates the eukaryotic initiation factor eIF4E in vivo. Biochem J 385, 695-702 (2005) (Pubitemid 40208829)
    • (2005) Biochemical Journal , vol.385 , Issue.3 , pp. 695-702
    • Parra-Palau, J.L.1    Scheper, G.C.2    Harper, D.E.3    Proud, C.G.4
  • 91
    • 11844257590 scopus 로고    scopus 로고
    • Drosophila Lk6 kinase controls phosphorylation of eukaryotic translation initiation factor 4E and promotes normal growth and development
    • DOI 10.1016/j.cub.2004.12.037, PII S0960982204009935
    • Arquier N, M. Bourouis, J. Colombani and P. Leopold: Drosophila Lk6 kinase controls phosphorylation of eukaryotic translation initiation factor 4E and promotes normal growth and development. Curr Biol 15, 19-23 (2005) (Pubitemid 40084697)
    • (2005) Current Biology , vol.15 , Issue.1 , pp. 19-23
    • Arquier, N.1    Bourouis, M.2    Colombani, J.3    Leopold, P.4
  • 92
    • 11844287569 scopus 로고    scopus 로고
    • Diet-dependent effects of the Drosophila Mnk1/Mnk2 homolog Lk6 on growth via eIF4E
    • DOI 10.1016/j.cub.2004.12.034, PII S0960982204009911
    • Reiling J. H, K. T. Doepfner, E. Hafen and H. Stocker: Diet-dependent effects of the Drosophila Mnk1/Mnk2 homolog Lk6 on growth via eIF4E. Curr Biol 15, 24-30 (2005) (Pubitemid 40084698)
    • (2005) Current Biology , vol.15 , Issue.1 , pp. 24-30
    • Reiling, J.H.1    Doepfner, K.T.2    Hafen, E.3    Stocker, H.4
  • 93
    • 0033929169 scopus 로고    scopus 로고
    • Regulation of eukaryotic initiation factor 4E phosphorylation in the nervous system of Aplysia californica
    • DOI 10.1046/j.1471-4159.2000.0750872.x
    • Dyer J. R. and W. S. Sossin: Regulation of eukaryotic initiation factor 4E phosphorylation in the nervous system of Aplysia californica. J Neurochem 75, 872-881 (2000) (Pubitemid 30485472)
    • (2000) Journal of Neurochemistry , vol.75 , Issue.2 , pp. 872-881
    • Dyer, J.R.1    Sossin, W.S.2
  • 94
    • 0345505221 scopus 로고    scopus 로고
    • An activity-dependent switch to cap-independent translation triggered by elF4E dephosphorylation
    • DOI 10.1038/nn1018
    • Dyer J. R, S. Michel, W. Lee, V. F. Castellucci, N. L. Wayne and W. S. Sossin: An activity-dependent switch to cap-independent translation triggered by eIF4E dephosphorylation. Nat Neurosci 6, 219-220 (2003) (Pubitemid 36278278)
    • (2003) Nature Neuroscience , vol.6 , Issue.3 , pp. 219-220
    • Dyer, J.R.1    Michel, S.2    Lee, W.3    Castellucci, V.F.4    Wayne, N.L.5    Sossin, W.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.