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Volumn 17, Issue 1, 2016, Pages

Distinct recruitment of human eIF4E isoforms to processing bodies and stress granules

Author keywords

Arsenite; EIF4E2; EIF4E3; Eukaryotic translation initiation factor 4E (eIF4E); Heat shock; PB; Processing body (P body); SG; Stress granule; Translation control; Translation initiation factor

Indexed keywords

ARSENIC TRIOXIDE; BINDING PROTEIN; EUKARYOTIC TRANSLATION INITIATION FACTOR 4E1; EUKARYOTIC TRANSLATION INITIATION FACTOR 4E2; EUKARYOTIC TRANSLATION INITIATION FACTOR 4E3; EUKARYOTIC TRANSLATION INITIATION FACTOR 4E3 B; EUKARYOTIC TRANSLATION INITIATION FACTOR 4G1; EUKARYOTIC TRANSLATION INITIATION FACTOR 4G3; INITIATION FACTOR 4E; INITIATION FACTOR 4G; ISOPROTEIN; MESSENGER RNA; POLYADENYLATE BINDING PROTEIN 1; UNCLASSIFIED DRUG; CAP BINDING PROTEIN; EIF4E2 PROTEIN, HUMAN; EIF4E3 PROTEIN, HUMAN; POLYADENYLIC ACID BINDING PROTEIN;

EID: 84984602118     PISSN: None     EISSN: 14712199     Source Type: Journal    
DOI: 10.1186/s12867-016-0072-x     Document Type: Article
Times cited : (37)

References (68)
  • 1
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson RJ, Hellen CUT, Pestova TV. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Bio. 2010;11(2):113-27.
    • (2010) Nat Rev Mol Cell Bio , vol.11 , Issue.2 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.T.2    Pestova, T.V.3
  • 3
    • 84863803532 scopus 로고    scopus 로고
    • Targeting mnks for cancer therapy
    • Hou JQ, Lam F, Proud C, Wang SD. Targeting mnks for cancer therapy. Oncotarget. 2012;3(2):118-31.
    • (2012) Oncotarget , vol.3 , Issue.2 , pp. 118-131
    • Hou, J.Q.1    Lam, F.2    Proud, C.3    Wang, S.D.4
  • 4
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function
    • Pause A, Belsham GJ, Gingras AC, Donze O, Lin TA, Lawrence JC Jr, Sonenberg N. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function. Nature. 1994;371(6500):762-7.
    • (1994) Nature , vol.371 , Issue.6500 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.C.3    Donze, O.4    Lin, T.A.5    Lawrence, J.C.6    Sonenberg, N.7
  • 5
    • 0034660062 scopus 로고    scopus 로고
    • A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA 5' cap-binding protein, eIF4E
    • Dostie J, Ferraiuolo M, Pause A, Adam SA, Sonenberg N. A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA 5' cap-binding protein, eIF4E. EMBO J. 2000;19(12):3142-56.
    • (2000) EMBO J , vol.19 , Issue.12 , pp. 3142-3156
    • Dostie, J.1    Ferraiuolo, M.2    Pause, A.3    Adam, S.A.4    Sonenberg, N.5
  • 6
    • 0033565233 scopus 로고    scopus 로고
    • Repressor binding to a dorsal regulatory site traps human eIF4E in a high cap-affinity state
    • Ptushkina M, von der Haar T, Karim MM, Hughes JM, McCarthy JE. Repressor binding to a dorsal regulatory site traps human eIF4E in a high cap-affinity state. EMBO J. 1999;18(14):4068-75.
    • (1999) EMBO J , vol.18 , Issue.14 , pp. 4068-4075
    • Ptushkina, M.1    Haar, T.2    Karim, M.M.3    Hughes, J.M.4    McCarthy, J.E.5
  • 7
    • 0033152072 scopus 로고    scopus 로고
    • Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G
    • Marcotrigiano J, Gingras AC, Sonenberg N, Burley SK. Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. Mol Cell. 1999;3(6):707-16.
    • (1999) Mol Cell , vol.3 , Issue.6 , pp. 707-716
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 9
    • 41149176379 scopus 로고    scopus 로고
    • Ectopic expression of eIF4E-transporter triggers the movement of eIF4E into P-bodies, inhibiting steady-state translation but not the pioneer round of translation
    • Lee HC, Cho H, Kim YK. Ectopic expression of eIF4E-transporter triggers the movement of eIF4E into P-bodies, inhibiting steady-state translation but not the pioneer round of translation. Biochem Biophys Res Commun. 2008;369(4):1160-5.
    • (2008) Biochem Biophys Res Commun , vol.369 , Issue.4 , pp. 1160-1165
    • Lee, H.C.1    Cho, H.2    Kim, Y.K.3
  • 10
    • 84879574106 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha (HIF-1alpha) promotes cap-dependent translation of selective mRNAs through up-regulating initiation factor eIF4E1 in breast cancer cells under hypoxia conditions
    • Yi T, Papadopoulos E, Hagner PR, Wagner G. Hypoxia-inducible factor-1alpha (HIF-1alpha) promotes cap-dependent translation of selective mRNAs through up-regulating initiation factor eIF4E1 in breast cancer cells under hypoxia conditions. J Biol Chem. 2013;288(26):18732-42.
    • (2013) J Biol Chem , vol.288 , Issue.26 , pp. 18732-18742
    • Yi, T.1    Papadopoulos, E.2    Hagner, P.R.3    Wagner, G.4
  • 11
    • 15944389880 scopus 로고    scopus 로고
    • Functional analysis of seven genes encoding eight translation initiation factor 4E (eIF4E) isoforms in Drosophila
    • Hernandez G, Altmann M, Sierra JM, Urlaub H, Diez del Corral R, Schwartz P, Rivera-Pomar R. Functional analysis of seven genes encoding eight translation initiation factor 4E (eIF4E) isoforms in Drosophila. Mech Dev. 2005;122(4):529-43.
    • (2005) Mech Dev , vol.122 , Issue.4 , pp. 529-543
    • Hernandez, G.1    Altmann, M.2    Sierra, J.M.3    Urlaub, H.4    Diez del Corral, R.5    Schwartz, P.6    Rivera-Pomar, R.7
  • 13
    • 67650543838 scopus 로고    scopus 로고
    • eIF4E: new family members, new binding partners, new roles
    • Rhoads RE. eIF4E: new family members, new binding partners, new roles. J Biol Chem. 2009;284(25):16711-5.
    • (2009) J Biol Chem , vol.284 , Issue.25 , pp. 16711-16715
    • Rhoads, R.E.1
  • 14
    • 84862282796 scopus 로고    scopus 로고
    • On the diversification of the translation apparatus across eukaryotes
    • Hernandez G, Proud CG, Preiss T, Parsyan A. On the diversification of the translation apparatus across eukaryotes. Comp Funct Genomics. 2012;2012:256848.
    • (2012) Comp Funct Genomics , vol.2012 , pp. 256848
    • Hernandez, G.1    Proud, C.G.2    Preiss, T.3    Parsyan, A.4
  • 15
    • 84940824655 scopus 로고    scopus 로고
    • Positive mRNA Translational Control in Germ Cells by Initiation Factor Selectivity
    • Friday AJ, Keiper BD. Positive mRNA Translational Control in Germ Cells by Initiation Factor Selectivity. BioMed Res Int. 2015;2015:327963.
    • (2015) BioMed Res Int , vol.2015 , pp. 327963
    • Friday, A.J.1    Keiper, B.D.2
  • 16
    • 84867544436 scopus 로고    scopus 로고
    • Translational control in the Caenorhabditis elegans germ line
    • Nousch M, Eckmann CR. Translational control in the Caenorhabditis elegans germ line. Adv Exp Med Biol. 2013;757:205-47.
    • (2013) Adv Exp Med Biol , vol.757 , pp. 205-247
    • Nousch, M.1    Eckmann, C.R.2
  • 19
    • 2942522541 scopus 로고    scopus 로고
    • Characterization of mammalian eIF4E-family members
    • Joshi B, Cameron A, Jagus R. Characterization of mammalian eIF4E-family members. Eur J Biochem. 2004;271(11):2189-203.
    • (2004) Eur J Biochem , vol.271 , Issue.11 , pp. 2189-2203
    • Joshi, B.1    Cameron, A.2    Jagus, R.3
  • 21
    • 18844397041 scopus 로고    scopus 로고
    • A new paradigm for translational control: inhibition via 5'-3' mRNA tethering by Bicoid and the eIF4E cognate 4EHP
    • Cho PF, Poulin F, Cho-Park YA, Cho-Park IB, Chicoine JD, Lasko P, Sonenberg N. A new paradigm for translational control: inhibition via 5'-3' mRNA tethering by Bicoid and the eIF4E cognate 4EHP. Cell. 2005;121(3):411-23.
    • (2005) Cell , vol.121 , Issue.3 , pp. 411-423
    • Cho, P.F.1    Poulin, F.2    Cho-Park, Y.A.3    Cho-Park, I.B.4    Chicoine, J.D.5    Lasko, P.6    Sonenberg, N.7
  • 22
    • 33749989519 scopus 로고    scopus 로고
    • Cap-dependent translational inhibition establishes two opposing morphogen gradients in Drosophila embryos
    • Cho PF, Gamberi C, Cho-Park YA, Cho-Park IB, Lasko P, Sonenberg N. Cap-dependent translational inhibition establishes two opposing morphogen gradients in Drosophila embryos. Curr Biol. 2006;16(20):2035-41.
    • (2006) Curr Biol , vol.16 , Issue.20 , pp. 2035-2041
    • Cho, P.F.1    Gamberi, C.2    Cho-Park, Y.A.3    Cho-Park, I.B.4    Lasko, P.5    Sonenberg, N.6
  • 24
    • 84944565412 scopus 로고    scopus 로고
    • Tristetraprolin recruits eukaryotic initiation factor 4E2 to repress translation of AU-rich element-containing mRNAs
    • Tao X, Gao G. Tristetraprolin recruits eukaryotic initiation factor 4E2 to repress translation of AU-rich element-containing mRNAs. Mol Cell Biol. 2015;35(22):3921-32.
    • (2015) Mol Cell Biol , vol.35 , Issue.22 , pp. 3921-3932
    • Tao, X.1    Gao, G.2
  • 27
    • 11144323221 scopus 로고    scopus 로고
    • Translation of a small subset of Caenorhabditis elegans mRNAs is dependent on a specific eukaryotic translation initiation factor 4E isoform
    • Dinkova TD, Keiper BD, Korneeva NL, Aamodt EJ, Rhoads RE. Translation of a small subset of Caenorhabditis elegans mRNAs is dependent on a specific eukaryotic translation initiation factor 4E isoform. Mol Cell Biol. 2005;25(1):100-13.
    • (2005) Mol Cell Biol , vol.25 , Issue.1 , pp. 100-113
    • Dinkova, T.D.1    Keiper, B.D.2    Korneeva, N.L.3    Aamodt, E.J.4    Rhoads, R.E.5
  • 28
    • 0037226593 scopus 로고    scopus 로고
    • A molecular signature of metastasis in primary solid tumors
    • Ramaswamy S, Ross KN, Lander ES, Golub TR. A molecular signature of metastasis in primary solid tumors. Nat Genet. 2003;33(1):49-54.
    • (2003) Nat Genet , vol.33 , Issue.1 , pp. 49-54
    • Ramaswamy, S.1    Ross, K.N.2    Lander, E.S.3    Golub, T.R.4
  • 31
    • 17844371700 scopus 로고    scopus 로고
    • A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies
    • Andrei MA, Ingelfinger D, Heintzmann R, Achsel T, Rivera-Pomar R, Luhrmann R. A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies. RNA. 2005;11(5):717-27.
    • (2005) RNA , vol.11 , Issue.5 , pp. 717-727
    • Andrei, M.A.1    Ingelfinger, D.2    Heintzmann, R.3    Achsel, T.4    Rivera-Pomar, R.5    Luhrmann, R.6
  • 32
    • 72149114598 scopus 로고    scopus 로고
    • The Hsp90 inhibitor geldanamycin abrogates colocalization of eIF4E and eIF4E-transporter into stress granules and association of eIF4E with eIF4G
    • Suzuki Y, Minami M, Suzuki M, Abe K, Zenno S, Tsujimoto M, Matsumoto K, Minami Y. The Hsp90 inhibitor geldanamycin abrogates colocalization of eIF4E and eIF4E-transporter into stress granules and association of eIF4E with eIF4G. J Biol Chem. 2009;284(51):35597-604.
    • (2009) J Biol Chem , vol.284 , Issue.51 , pp. 35597-35604
    • Suzuki, Y.1    Minami, M.2    Suzuki, M.3    Abe, K.4    Zenno, S.5    Tsujimoto, M.6    Matsumoto, K.7    Minami, Y.8
  • 35
    • 0035166679 scopus 로고    scopus 로고
    • Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses
    • Lu L, Han AP, Chen JJ. Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses. Mol Cell Biol. 2001;21(23):7971-80.
    • (2001) Mol Cell Biol , vol.21 , Issue.23 , pp. 7971-7980
    • Lu, L.1    Han, A.P.2    Chen, J.J.3
  • 36
    • 20144378698 scopus 로고    scopus 로고
    • Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure
    • McEwen E, Kedersha N, Song B, Scheuner D, Gilks N, Han A, Chen JJ, Anderson P, Kaufman RJ. Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure. J Biol Chem. 2005;280(17):16925-33.
    • (2005) J Biol Chem , vol.280 , Issue.17 , pp. 16925-16933
    • McEwen, E.1    Kedersha, N.2    Song, B.3    Scheuner, D.4    Gilks, N.5    Han, A.6    Chen, J.J.7    Anderson, P.8    Kaufman, R.J.9
  • 38
    • 33845950751 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2alpha-independent pathway of stress granule induction by the natural product pateamine A
    • Dang Y, Kedersha N, Low WK, Romo D, Gorospe M, Kaufman R, Anderson P, Liu JO. Eukaryotic initiation factor 2alpha-independent pathway of stress granule induction by the natural product pateamine A. J Biol Chem. 2006;281(43):32870-8.
    • (2006) J Biol Chem , vol.281 , Issue.43 , pp. 32870-32878
    • Dang, Y.1    Kedersha, N.2    Low, W.K.3    Romo, D.4    Gorospe, M.5    Kaufman, R.6    Anderson, P.7    Liu, J.O.8
  • 39
    • 84870270861 scopus 로고    scopus 로고
    • Selenite targets eIF4E-binding protein-1 to inhibit translation initiation and induce the assembly of non-canonical stress granules
    • Fujimura K, Sasaki AT, Anderson P. Selenite targets eIF4E-binding protein-1 to inhibit translation initiation and induce the assembly of non-canonical stress granules. Nucleic Acids Res. 2012;40(16):8099-110.
    • (2012) Nucleic Acids Res , vol.40 , Issue.16 , pp. 8099-8110
    • Fujimura, K.1    Sasaki, A.T.2    Anderson, P.3
  • 40
    • 57749192735 scopus 로고    scopus 로고
    • Real-time and quantitative imaging of mammalian stress granules and processing bodies
    • Kedersha N, Tisdale S, Hickman T, Anderson P. Real-time and quantitative imaging of mammalian stress granules and processing bodies. Methods Enzymol. 2008;448:521-52.
    • (2008) Methods Enzymol , vol.448 , pp. 521-552
    • Kedersha, N.1    Tisdale, S.2    Hickman, T.3    Anderson, P.4
  • 41
    • 84873537120 scopus 로고    scopus 로고
    • Relationship of GW/P-bodies with stress granules
    • Stoecklin G, Kedersha N. Relationship of GW/P-bodies with stress granules. Adv Exp Med Biol. 2013;768:197-211.
    • (2013) Adv Exp Med Biol , vol.768 , pp. 197-211
    • Stoecklin, G.1    Kedersha, N.2
  • 42
    • 33845809231 scopus 로고    scopus 로고
    • P bodies: at the crossroads of post-transcriptional pathways
    • Eulalio A, Behm-Ansmant I, Izaurralde E. P bodies: at the crossroads of post-transcriptional pathways. Nat Rev Mol Cell Bio. 2007;8(1):9-22.
    • (2007) Nat Rev Mol Cell Bio , vol.8 , Issue.1 , pp. 9-22
    • Eulalio, A.1    Behm-Ansmant, I.2    Izaurralde, E.3
  • 43
  • 44
    • 66249103703 scopus 로고    scopus 로고
    • RNA granules: post-transcriptional and epigenetic modulators of gene expression
    • Anderson P, Kedersha N. RNA granules: post-transcriptional and epigenetic modulators of gene expression. Nat Rev Mol Cell Biol. 2009;10(6):430-6.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.6 , pp. 430-436
    • Anderson, P.1    Kedersha, N.2
  • 45
    • 84859199615 scopus 로고    scopus 로고
    • Sequestration of highly expressed mRNAs in cytoplasmic granules, P-bodies, and stress granules enhances cell viability
    • Lavut A, Raveh D. Sequestration of highly expressed mRNAs in cytoplasmic granules, P-bodies, and stress granules enhances cell viability. PLoS Genet. 2012;8(2):e1002527.
    • (2012) PLoS Genet , vol.8 , Issue.2
    • Lavut, A.1    Raveh, D.2
  • 48
    • 66149131406 scopus 로고    scopus 로고
    • The eIF4E-binding proteins are modifiers of cytoplasmic eIF4E relocalization during the heat shock response
    • Sukarieh R, Sonenberg N, Pelletier J. The eIF4E-binding proteins are modifiers of cytoplasmic eIF4E relocalization during the heat shock response. Am J Physiol Cell Physiol. 2009;296(5):C1207-17.
    • (2009) Am J Physiol Cell Physiol , vol.296 , Issue.5 , pp. C1207-C1217
    • Sukarieh, R.1    Sonenberg, N.2    Pelletier, J.3
  • 49
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem. 1987;162(1):156-9.
    • (1987) Anal Biochem , vol.162 , Issue.1 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 50
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A, Tomas H, Havlis J, Olsen JV, Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc. 2006;1(6):2856-60.
    • (2006) Nat Protoc , vol.1 , Issue.6 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 51
    • 84864724013 scopus 로고    scopus 로고
    • N-terminal domain of nuclear IL-1alpha shows structural similarity to the C-terminal domain of Snf1 and binds to the HAT/core module of the SAGA complex
    • Zamostna B, Novak J, Vopalensky V, Masek T, Burysek L, Pospisek M. N-terminal domain of nuclear IL-1alpha shows structural similarity to the C-terminal domain of Snf1 and binds to the HAT/core module of the SAGA complex. PLoS ONE. 2012;7(8):e41801.
    • (2012) PLoS ONE , vol.7 , Issue.8
    • Zamostna, B.1    Novak, J.2    Vopalensky, V.3    Masek, T.4    Burysek, L.5    Pospisek, M.6
  • 52
    • 79952591194 scopus 로고    scopus 로고
    • Polysome analysis and RNA purification from sucrose gradients
    • Masek T, Valasek L, Pospisek M. Polysome analysis and RNA purification from sucrose gradients. Methods Mol Biol. 2011;703:293-309.
    • (2011) Methods Mol Biol. , vol.703 , pp. 293-309
    • Masek, T.1    Valasek, L.2    Pospisek, M.3
  • 53
    • 27844576586 scopus 로고    scopus 로고
    • Structural basis for mRNA cap-binding regulation of eukaryotic initiation factor 4E by 4E-binding protein, studied by spectroscopic, X-ray crystal structural, and molecular dynamics simulation methods
    • Tomoo K, Matsushita Y, Fujisaki H, Abiko F, Shen X, Taniguchi T, Miyagawa H, Kitamura K, Miura K, Ishida T. Structural basis for mRNA cap-binding regulation of eukaryotic initiation factor 4E by 4E-binding protein, studied by spectroscopic, X-ray crystal structural, and molecular dynamics simulation methods. Biochim Biophys Acta. 2005;1753(2):191-208.
    • (2005) Biochim Biophys Acta , vol.1753 , Issue.2 , pp. 191-208
    • Tomoo, K.1    Matsushita, Y.2    Fujisaki, H.3    Abiko, F.4    Shen, X.5    Taniguchi, T.6    Miyagawa, H.7    Kitamura, K.8    Miura, K.9    Ishida, T.10
  • 54
    • 33750434479 scopus 로고    scopus 로고
    • Cap-free structure of eIF4E suggests a basis for conformational regulation by its ligands
    • Volpon L, Osborne MJ, Topisirovic I, Siddiqui N, Borden KL. Cap-free structure of eIF4E suggests a basis for conformational regulation by its ligands. EMBO J. 2006;25(21):5138-49.
    • (2006) EMBO J , vol.25 , Issue.21 , pp. 5138-5149
    • Volpon, L.1    Osborne, M.J.2    Topisirovic, I.3    Siddiqui, N.4    Borden, K.L.5
  • 55
    • 34547788872 scopus 로고    scopus 로고
    • Crystallographic and mass spectrometric characterisation of eIF4E with N7-alkylated cap derivatives
    • Brown CJ, McNae I, Fischer PM, Walkinshaw MD. Crystallographic and mass spectrometric characterisation of eIF4E with N7-alkylated cap derivatives. J Mol Biol. 2007;372(1):7-15.
    • (2007) J Mol Biol , vol.372 , Issue.1 , pp. 7-15
    • Brown, C.J.1    McNae, I.2    Fischer, P.M.3    Walkinshaw, M.D.4
  • 56
    • 79961172566 scopus 로고    scopus 로고
    • Structural scaffold for eIF4E binding selectivity of 4E-BP isoforms: crystal structure of eIF4E binding region of 4E-BP2 and its comparison with that of 4E-BP1
    • Fukuyo A, In Y, Ishida T, Tomoo K. Structural scaffold for eIF4E binding selectivity of 4E-BP isoforms: crystal structure of eIF4E binding region of 4E-BP2 and its comparison with that of 4E-BP1. J Pept Sci. 2011;17(9):650-7.
    • (2011) J Pept Sci , vol.17 , Issue.9 , pp. 650-657
    • Fukuyo, A.1    In, Y.2    Ishida, T.3    Tomoo, K.4
  • 57
    • 33745894330 scopus 로고    scopus 로고
    • Translation repression in human cells by microRNA-induced gene silencing requires RCK/p54
    • Chu CY, Rana TM. Translation repression in human cells by microRNA-induced gene silencing requires RCK/p54. PLoS Biol. 2006;4(7):e210.
    • (2006) PLoS Biol , vol.4 , Issue.7
    • Chu, C.Y.1    Rana, T.M.2
  • 58
    • 16844365216 scopus 로고    scopus 로고
    • The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules
    • Wilczynska A, Aigueperse C, Kress M, Dautry F, Weil D. The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules. J Cell Sci. 2005;118(5):981-92.
    • (2005) J Cell Sci , vol.118 , Issue.5 , pp. 981-992
    • Wilczynska, A.1    Aigueperse, C.2    Kress, M.3    Dautry, F.4    Weil, D.5
  • 59
    • 70350367745 scopus 로고    scopus 로고
    • Unravelling the ultrastructure of stress granules and associated P-bodies in human cells
    • Souquere S, Mollet S, Kress M, Dautry F, Pierron G, Weil D. Unravelling the ultrastructure of stress granules and associated P-bodies in human cells. J Cell Sci. 2009;122(Pt 20):3619-26.
    • (2009) J Cell Sci , vol.122 , pp. 3619-3626
    • Souquere, S.1    Mollet, S.2    Kress, M.3    Dautry, F.4    Pierron, G.5    Weil, D.6
  • 61
    • 56749098074 scopus 로고    scopus 로고
    • Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing
    • Pan Q, Shai O, Lee LJ, Frey BJ, Blencowe BJ. Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing. Nat Genet. 2008;40(12):1413-5.
    • (2008) Nat Genet , vol.40 , Issue.12 , pp. 1413-1415
    • Pan, Q.1    Shai, O.2    Lee, L.J.3    Frey, B.J.4    Blencowe, B.J.5
  • 62
    • 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
    • Scheper GC, Parra JL, Wilson M, Van Kollenburg B, Vertegaal AC, Han ZG, Proud CG. 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. 2003;23(16):5692-705.
    • (2003) Mol Cell Biol , vol.23 , Issue.16 , pp. 5692-5705
    • Scheper, G.C.1    Parra, J.L.2    Wilson, M.3    Kollenburg, B.4    Vertegaal, A.C.5    Han, Z.G.6    Proud, C.G.7
  • 63
    • 84882645365 scopus 로고    scopus 로고
    • Investigating the consequences of eIF4E2 (4EHP) interaction with 4E-transporter on its cellular distribution in HeLa cells
    • Kubacka D, Kamenska A, Broomhead H, Minshall N, Darzynkiewicz E, Standart N. Investigating the consequences of eIF4E2 (4EHP) interaction with 4E-transporter on its cellular distribution in HeLa cells. PLoS ONE. 2013;8(8):e72761.
    • (2013) PLoS ONE , vol.8 , Issue.8
    • Kubacka, D.1    Kamenska, A.2    Broomhead, H.3    Minshall, N.4    Darzynkiewicz, E.5    Standart, N.6
  • 64
    • 77952486777 scopus 로고    scopus 로고
    • Transmembrane receptor DCC associates with protein synthesis machinery and regulates translation
    • Tcherkezian J, Brittis PA, Thomas F, Roux PP, Flanagan JG. Transmembrane receptor DCC associates with protein synthesis machinery and regulates translation. Cell. 2010;141(4):632-44.
    • (2010) Cell , vol.141 , Issue.4 , pp. 632-644
    • Tcherkezian, J.1    Brittis, P.A.2    Thomas, F.3    Roux, P.P.4    Flanagan, J.G.5
  • 66
    • 57349158716 scopus 로고    scopus 로고
    • Translationally repressed mRNA transiently cycles through stress granules during stress
    • Mollet S, Cougot N, Wilczynska A, Dautry F, Kress M, Bertrand E, Weil D. Translationally repressed mRNA transiently cycles through stress granules during stress. Mol Biol Cell. 2008;19(10):4469-79.
    • (2008) Mol Biol Cell , vol.19 , Issue.10 , pp. 4469-4479
    • Mollet, S.1    Cougot, N.2    Wilczynska, A.3    Dautry, F.4    Kress, M.5    Bertrand, E.6    Weil, D.7
  • 67
    • 84861231813 scopus 로고    scopus 로고
    • Translational control in cellular and developmental processes
    • Kong J, Lasko P. Translational control in cellular and developmental processes. Nat Rev Genet. 2012;13(6):383-94.
    • (2012) Nat Rev Genet , vol.13 , Issue.6 , pp. 383-394
    • Kong, J.1    Lasko, P.2
  • 68
    • 84930352302 scopus 로고    scopus 로고
    • The eukaryotic translation initiation factor eIF4E in the nucleus: taking the road less traveled
    • Osborne MJ, Borden KL. The eukaryotic translation initiation factor eIF4E in the nucleus: taking the road less traveled. Immunol Rev. 2015;263(1):210-23.
    • (2015) Immunol Rev , vol.263 , Issue.1 , pp. 210-223
    • Osborne, M.J.1    Borden, K.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.