메뉴 건너뛰기




Volumn 8, Issue 1, 2017, Pages

Erratum to: Flavivirus infection uncouples translation suppression from cellular stress responses (mBio (2017) 8, 1, 10.1128/mBio.02150-16);Flavivirus infection uncouples translation suppression from cellular stress responses

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 2ALPHA; MITOGEN ACTIVATED PROTEIN KINASE 14; VIRUS RNA;

EID: 85014764249     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00488-17     Document Type: Erratum
Times cited : (91)

References (89)
  • 1
    • 84901057834 scopus 로고    scopus 로고
    • Translational control of immune responses: From transcripts to translatomes
    • Piccirillo CA, Bjur E, Topisirovic I, Sonenberg N, Larsson O. 2014. Translational control of immune responses: from transcripts to translatomes. Nat Immunol 15:503-511. https://doi.org/10.1038/ni.2891
    • (2014) Nat Immunol , vol.15 , pp. 503-511
    • Piccirillo, C.A.1    Bjur, E.2    Topisirovic, I.3    Sonenberg, N.4    Larsson, O.5
  • 2
    • 84870757284 scopus 로고    scopus 로고
    • Tinkering with translation: Protein synthesis in virus-infected cells
    • Walsh D, Mathews MB, Mohr I. 2013. Tinkering with translation: protein synthesis in virus-infected cells. Cold Spring Harb Perspect Biol 5:a012351. https://doi.org/10.1101/cshperspect.a012351
    • (2013) Cold Spring Harb Perspect Biol , vol.5
    • Walsh, D.1    Mathews, M.B.2    Mohr, I.3
  • 3
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • Holcik M, Sonenberg N. 2005. Translational control in stress and apoptosis. Nat Rev Mol Cell Biol 6:318-327. https://doi.org/10.1038/nrm1618
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 4
    • 34347225099 scopus 로고    scopus 로고
    • The dsRNA protein kinase PKR: Virus and cell control
    • García MA, Meurs EF, Esteban M. 2007. The dsRNA protein kinase PKR: virus and cell control. Biochimie 89:799-811. https://doi.org/10.1016/j.biochi.2007.03.001
    • (2007) Biochimie , vol.89 , pp. 799-811
    • García, M.A.1    Meurs, E.F.2    Esteban, M.3
  • 5
    • 39949085583 scopus 로고    scopus 로고
    • Stress granules: The Tao of RNA triage
    • Anderson P, Kedersha N. 2008. Stress granules: the Tao of RNA triage. Trends Biochem Sci 33:141-150. https://doi.org/10.1016/j.tibs.2007.12.003
    • (2008) Trends Biochem Sci , vol.33 , pp. 141-150
    • Anderson, P.1    Kedersha, N.2
  • 6
    • 0036154218 scopus 로고    scopus 로고
    • Evidence that ternary complex (EIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules
    • Kedersha N, Chen S, Gilks N, Li W, Miller IJ, Stahl J, Anderson P. 2002. Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules. Mol Biol Cell 13:195-210. https://doi.org/10.1091/mbc.01-05-0221
    • (2002) Mol Biol Cell , vol.13 , pp. 195-210
    • Kedersha, N.1    Chen, S.2    Gilks, N.3    Li, W.4    Miller, I.J.5    Stahl, J.6    Erson, P.7
  • 7
    • 0033611157 scopus 로고    scopus 로고
    • RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules
    • Kedersha NL, Gupta M, Li W, Miller I, Anderson P. 1999. RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules. J Cell Biol 147:1431-1442. https://doi.org/10.1083/jcb.147.7.1431
    • (1999) J Cell Biol , vol.147 , pp. 1431-1442
    • Kedersha, N.L.1    Gupta, M.2    Li, W.3    Miller, I.4    Erson, P.5
  • 8
    • 84872675863 scopus 로고    scopus 로고
    • Diversion of stress granules and P-bodies during viral infection
    • Reineke LC, Lloyd RE. 2013. Diversion of stress granules and P-bodies during viral infection. Virology 436:255-267. https://doi.org/10.1016/j.virol.2012.11.017
    • (2013) Virology , vol.436 , pp. 255-267
    • Reineke, L.C.1    Lloyd, R.E.2
  • 10
    • 81255160914 scopus 로고    scopus 로고
    • Viral subversion of the host protein synthesis machinery
    • Walsh D, Mohr I. 2011. Viral subversion of the host protein synthesis machinery. Nat Rev Microbiol 9:860-875. https://doi.org/10.1038/nrmicro2655
    • (2011) Nat Rev Microbiol , vol.9 , pp. 860-875
    • Walsh, D.1    Mohr, I.2
  • 11
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins
    • Mader S, Lee H, Pause A, Sonenberg N. 1995. The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins. Mol Cell Biol 15:4990-4997. https://doi.org/10.1128/MCB.15.9.4990
    • (1995) Mol Cell Biol , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 12
    • 0035527326 scopus 로고    scopus 로고
    • Translational regulation in cell stress and apoptosis. Roles of the eIF4E binding proteins
    • Clemens MJ. 2001. Translational regulation in cell stress and apoptosis. Roles of the eIF4E binding proteins. J Cell Mol Med 5:221-239. https://doi.org/10.1111/j.1582-4934.2001.tb00157.x
    • (2001) J Cell Mol Med , vol.5 , pp. 221-239
    • Clemens, M.J.1
  • 16
    • 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
    • Ueda T, Watanabe-Fukunaga R, Fukuyama H, Nagata S, Fukunaga R. 2004. 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. https://doi.org/10.1128/MCB.24.15.6539-6549.2004
    • (2004) Mol Cell Biol , vol.24 , pp. 6539-6549
    • Ueda, T.1    Watanabe-Fukunaga, R.2    Fukuyama, H.3    Nagata, S.4    Fukunaga, R.5
  • 17
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
    • Waskiewicz AJ, Flynn A, Proud CG, Cooper JA. 1997. Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J 16:1909-1920. https://doi.org/10.1093/emboj/16.8.1909
    • (1997) EMBO J , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3    Cooper, J.A.4
  • 18
    • 0036662182 scopus 로고    scopus 로고
    • The global emergence/resurgence of arboviral diseases as public health problems
    • Gubler DJ. 2002. The global emergence/resurgence of arboviral diseases as public health problems. Arch Med Res 33:330-342. https://doi.org/10.1016/S0188-4409(02)00378-8
    • (2002) Arch Med Res , vol.33 , pp. 330-342
    • Gubler, D.J.1
  • 21
    • 84878018415 scopus 로고    scopus 로고
    • Barriers to preclinical investigations of anti-dengue immunity and dengue pathogenesis
    • St John AL, Abraham SN, Gubler DJ. 2013. Barriers to preclinical investigations of anti-dengue immunity and dengue pathogenesis. Nat Rev Microbiol 11:420-426. https://doi.org/10.1038/nrmicro3030
    • (2013) Nat Rev Microbiol , vol.11 , pp. 420-426
    • St John, A.L.1    Abraham, S.N.2    Gubler, D.J.3
  • 22
    • 84938390836 scopus 로고    scopus 로고
    • Molecular insight into dengue virus pathogenesis and its implications for disease control
    • Diamond MS, Pierson TC. 2015. Molecular insight into dengue virus pathogenesis and its implications for disease control. Cell 162:488-492. https://doi.org/10.1016/j.cell.2015.07.005
    • (2015) Cell , vol.162 , pp. 488-492
    • Diamond, M.S.1    Pierson, T.C.2
  • 23
    • 84962082454 scopus 로고    scopus 로고
    • Zika virus
    • Musso D, Gubler DJ. 2016. Zika virus. Clin Microbiol Rev 29:487-524. https://doi.org/10.1128/CMR.00072-15
    • (2016) Clin Microbiol Rev , vol.29 , pp. 487-524
    • Musso, D.1    Gubler, D.J.2
  • 24
    • 84962055381 scopus 로고    scopus 로고
    • Zika virus: New clinical syndromes and its emergence in the Western Hemisphere
    • Lazear HM, Diamond MS. 2016. Zika virus: new clinical syndromes and its emergence in the Western Hemisphere. J Virol 90:4864-4875. https://doi.org/10.1128/JVI.00252-16
    • (2016) J Virol , vol.90 , pp. 4864-4875
    • Lazear, H.M.1    Diamond, M.S.2
  • 26
    • 0018770470 scopus 로고
    • Methylation status of intracellular dengue type 2 40S RNA
    • Cleaves GR, Dubin DT. 1979. Methylation status of intracellular dengue type 2 40S RNA. Virology 96:159-165. https://doi.org/10.1016/0042-6822(79)90181-8
    • (1979) Virology , vol.96 , pp. 159-165
    • Cleaves, G.R.1    Dubin, D.T.2
  • 27
    • 0025116324 scopus 로고
    • Flavivirus genome organization, expression, and replication
    • Chambers TJ, Hahn CS, Galler R, Rice CM. 1990. Flavivirus genome organization, expression, and replication. Annu Rev Microbiol 44: 649-688. https://doi.org/10.1146/annurev.mi.44.100190.003245
    • (1990) Annu Rev Microbiol , vol.44 , pp. 649-688
    • Chambers, T.J.1    Hahn, C.S.2    Galler, R.3    Rice, C.M.4
  • 28
    • 84891084459 scopus 로고    scopus 로고
    • Revisiting dengue virushost cell interaction: New insights into molecular and cellular virology
    • Acosta EG, Kumar A, Bartenschlager R. 2014. Revisiting dengue virushost cell interaction: new insights into molecular and cellular virology. Adv Virus Res 88:1-109. https://doi.org/10.1016/B978-0-12-800098-4.00001-5
    • (2014) Adv Virus Res , vol.88 , pp. 1-109
    • Acosta, E.G.1    Kumar, A.2    Bartenschlager, R.3
  • 30
    • 84872749486 scopus 로고    scopus 로고
    • Early dengue virus protein synthesis induces extensive rearrangement of the endoplasmic reticulum independent of the UPR and SREBP-2 pathway
    • Peña J, Harris E. 2012. Early dengue virus protein synthesis induces extensive rearrangement of the endoplasmic reticulum independent of the UPR and SREBP-2 pathway. PLoS One 7:e38202. https://doi.org/10.1371/journal.pone.0038202
    • (2012) Plos One , vol.7
    • Peña, J.1    Harris, E.2
  • 31
    • 79959344614 scopus 로고    scopus 로고
    • Flavivirus NS4A-induced autophagy protects cells against death and enhances virus replication
    • McLean JE, Wudzinska A, Datan E, Quaglino D, Zakeri Z. 2011. Flavivirus NS4A-induced autophagy protects cells against death and enhances virus replication. J Biol Chem 286:22147-22159. https://doi.org/10.1074/jbc.M110.192500
    • (2011) J Biol Chem , vol.286 , pp. 22147-22159
    • McLean, J.E.1    Wudzinska, A.2    Datan, E.3    Quaglino, D.4    Zakeri, Z.5
  • 34
    • 84936935012 scopus 로고    scopus 로고
    • Dengue virus NS proteins inhibit RIG-I/MAVS signaling by blocking TBK1/IRF3 phosphorylation: Dengue virus serotype 1 NS4A is a unique interferon-regulating virulence determinant
    • Dalrymple NA, Cimica V, Mackow ER. 2015. Dengue virus NS proteins inhibit RIG-I/MAVS signaling by blocking TBK1/IRF3 phosphorylation: dengue virus serotype 1 NS4A is a unique interferon-regulating virulence determinant. mBio 6:e00553-15. https://doi.org/10.1128/mBio.00553-15
    • (2015) Mbio , vol.6 , pp. e00515-e00553
    • Dalrymple, N.A.1    Cimica, V.2    Mackow, E.R.3
  • 35
    • 84905400783 scopus 로고    scopus 로고
    • G3BP1, G3BP2 and CAPRIN1 are required for translation of interferon stimulated mRNAs and are targeted by a dengue virus non-coding RNA
    • Bidet K, Dadlani D, Garcia-Blanco MA. 2014. G3BP1, G3BP2 and CAPRIN1 are required for translation of interferon stimulated mRNAs and are targeted by a dengue virus non-coding RNA. PLoS Pathog 10:e1004242. https://doi.org/10.1371/journal.ppat.1004242
    • (2014) Plos Pathog , vol.10
    • Bidet, K.1    Dadlani, D.2    Garcia-Blanco, M.A.3
  • 36
    • 34547456097 scopus 로고    scopus 로고
    • Interaction of TIA-1/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assembly
    • Emara MM, Brinton MA. 2007. Interaction of TIA-1/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assembly. Proc Natl Acad Sci USA 104: 9041-9046. https://doi.org/10.1073/pnas.0703348104
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 9041-9046
    • Emara, M.M.1    Brinton, M.A.2
  • 37
    • 79954601093 scopus 로고    scopus 로고
    • Dengue virus modulates the unfolded protein response in a time-dependent manner
    • Peña J, Harris E. 2011. Dengue virus modulates the unfolded protein response in a time-dependent manner. J Biol Chem 286:14226-14236. https://doi.org/10.1074/jbc.M111.222703
    • (2011) J Biol Chem , vol.286 , pp. 14226-14236
    • Peña, J.1    Harris, E.2
  • 38
    • 35748966391 scopus 로고    scopus 로고
    • Dengue virus serotype infection specifies the activation of the unfolded protein response
    • Umareddy I, Pluquet O, Wang QY, Vasudevan SG, Chevet E, Gu F. 2007. Dengue virus serotype infection specifies the activation of the unfolded protein response. Virol J 4:91. https://doi.org/10.1186/1743-422X-4-91
    • (2007) Virol J , vol.4 , pp. 91
    • Umareddy, I.1    Pluquet, O.2    Wang, Q.Y.3    Vasudevan, S.G.4    Chevet, E.5    Gu, F.6
  • 40
    • 33644778763 scopus 로고    scopus 로고
    • Dengue virus utilizes a novel strategy for translation initiation when cap-dependent translation is inhibited
    • Edgil D, Polacek C, Harris E. 2006. Dengue virus utilizes a novel strategy for translation initiation when cap-dependent translation is inhibited. J Virol 80:2976-2986. https://doi.org/10.1128/JVI.80.6.2976-2986.2006
    • (2006) J Virol , vol.80 , pp. 2976-2986
    • Edgil, D.1    Polacek, C.2    Harris, E.3
  • 43
    • 63949084607 scopus 로고    scopus 로고
    • SUnSET, a nonradioactive method to monitor protein synthesis
    • Schmidt EK, Clavarino G, Ceppi M, Pierre P. 2009. SUnSET, a nonradioactive method to monitor protein synthesis. Nat Methods 6:275-277. https://doi.org/10.1038/nmeth.1314
    • (2009) Nat Methods , vol.6 , pp. 275-277
    • Schmidt, E.K.1    Clavarino, G.2    Ceppi, M.3    Pierre, P.4
  • 44
    • 0006331359 scopus 로고
    • Inhibition of protein synthesis by puromycin
    • Nathans D. 1964. Inhibition of protein synthesis by puromycin. Fed Proc 23:984-989
    • (1964) Fed Proc , vol.23 , pp. 984-989
    • Nathans, D.1
  • 45
    • 0015216932 scopus 로고
    • The mechanism by which cycloheximide and related glutarimide antibiotics inhibit peptide synthesis on reticulocyte ribosomes
    • Obrig TG, Culp WJ, McKeehan WL, Hardesty B. 1971. The mechanism by which cycloheximide and related glutarimide antibiotics inhibit peptide synthesis on reticulocyte ribosomes. J Biol Chem 246:174-181
    • (1971) J Biol Chem , vol.246 , pp. 174-181
    • Obrig, T.G.1    Culp, W.J.2    McKeehan, W.L.3    Hardesty, B.4
  • 47
    • 84947327742 scopus 로고    scopus 로고
    • Methods for the characterization of stress granules in virus infected cells
    • Panas MD, Kedersha N, McInerney GM. 2015. Methods for the characterization of stress granules in virus infected cells. Methods 90:57-64. https://doi.org/10.1016/j.ymeth.2015.04.009
    • (2015) Methods , vol.90 , pp. 57-64
    • Panas, M.D.1    Kedersha, N.2    McInerney, G.M.3
  • 49
    • 20144378698 scopus 로고    scopus 로고
    • Heme-regulated inhibitor kinasemediated 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. 2005. Heme-regulated inhibitor kinasemediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure. J Biol Chem 280:16925-16933. https://doi.org/10.1074/jbc.M412882200
    • (2005) J Biol Chem , vol.280 , 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    Erson, P.8    Kaufman, R.J.9
  • 50
    • 84875802186 scopus 로고    scopus 로고
    • Nuclear localization of dengue virus nonstructural protein 5 does not strictly correlate with efficient viral RNA replication and inhibition of type I interferon signaling
    • Kumar A, Bühler S, Selisko B, Davidson A, Mulder K, Canard B, Miller S, Bartenschlager R. 2013. Nuclear localization of dengue virus nonstructural protein 5 does not strictly correlate with efficient viral RNA replication and inhibition of type I interferon signaling. J Virol 87:4545-4557. https://doi.org/10.1128/JVI.03083-12
    • (2013) J Virol , vol.87 , pp. 4545-4557
    • Kumar, A.1    Bühler, S.2    Selisko, B.3    Davidson, A.4    Mulder, K.5    Canard, B.6    Miller, S.7    Bartenschlager, R.8
  • 51
    • 0034870535 scopus 로고    scopus 로고
    • Activity of the hepatitis A virus IRES requires association between the cap-binding translation initiation factor (EIF4E) and eIF4G
    • Ali IK, McKendrick L, Morley SJ, Jackson RJ. 2001. Activity of the hepatitis A virus IRES requires association between the cap-binding translation initiation factor (eIF4E) and eIF4G. J Virol 75:7854-7863. https://doi.org/10.1128/JVI.75.17.7854-7863.2001
    • (2001) J Virol , vol.75 , pp. 7854-7863
    • Ali, I.K.1    McKendrick, L.2    Morley, S.J.3    Jackson, R.J.4
  • 52
    • 33749379882 scopus 로고    scopus 로고
    • Global translational responses to oxidative stress impact upon multiple levels of protein synthesis
    • Shenton D, Smirnova JB, Selley JN, Carroll K, Hubbard SJ, Pavitt GD, Ashe MP, Grant CM. 2006. Global translational responses to oxidative stress impact upon multiple levels of protein synthesis. J Biol Chem 281: 29011-29021. https://doi.org/10.1074/jbc.M601545200
    • (2006) J Biol Chem , vol.281 , pp. 29011-29021
    • Shenton, D.1    Smirnova, J.B.2    Selley, J.N.3    Carroll, K.4    Hubbard, S.J.5    Pavitt, G.D.6    Ashe, M.P.7    Grant, C.M.8
  • 53
    • 81055155799 scopus 로고    scopus 로고
    • Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes
    • Ingolia NT, Lareau LF, Weissman JS. 2011. Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes. Cell 147:789-802. https://doi.org/10.1016/j.cell.2011.10.002
    • (2011) Cell , vol.147 , pp. 789-802
    • Ingolia, N.T.1    Lareau, L.F.2    Weissman, J.S.3
  • 54
    • 0017577805 scopus 로고
    • Inhibition of translation in eukaryotic systems by harringtonine
    • Fresno M, Jiménez A, Vázquez D. 1977. Inhibition of translation in eukaryotic systems by harringtonine. Eur J Biochem 72:323-330. https://doi.org/10.1111/j.1432-1033.1977.tb11256.x
    • (1977) Eur J Biochem , vol.72 , pp. 323-330
    • Fresno, M.1    Jiménez, A.2    Vázquez, D.3
  • 55
    • 0025358704 scopus 로고
    • Increased phosphorylation of elongation factor 2 during mitosis in transformed human amnion cells correlates with a decreased rate of protein synthesis
    • Celis JE, Madsen P, Ryazanov AG. 1990. Increased phosphorylation of elongation factor 2 during mitosis in transformed human amnion cells correlates with a decreased rate of protein synthesis. Proc Natl Acad Sci USA87:4231-4235. https://doi.org/10.1073/pnas.87.11.4231
    • (1990) Proc Natl Acad Sci USA87 , pp. 4231-4235
    • Celis, J.E.1    Madsen, P.2    Ryazanov, A.G.3
  • 57
    • 84861302600 scopus 로고    scopus 로고
    • West Nile virus infections suppress early viral RNA synthesis and avoid inducing the cell stress granule response
    • Courtney SC, Scherbik SV, Stockman BM, Brinton MA. 2012. West Nile virus infections suppress early viral RNA synthesis and avoid inducing the cell stress granule response. J Virol 86:3647-3657. https://doi.org/10.1128/JVI.06549-11
    • (2012) J Virol , vol.86 , pp. 3647-3657
    • Courtney, S.C.1    Scherbik, S.V.2    Stockman, B.M.3    Brinton, M.A.4
  • 58
    • 33749493493 scopus 로고    scopus 로고
    • Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2alpha phosphorylation
    • Mazroui R, Sukarieh R, Bordeleau ME, Kaufman RJ, Northcote P, Tanaka J, Gallouzi I, Pelletier J. 2006. Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2alpha phosphorylation. Mol Biol Cell 17:4212-4219. https://doi.org/10.1091/mbc.E06-04-0318
    • (2006) Mol Biol Cell , vol.17 , pp. 4212-4219
    • Mazroui, R.1    Sukarieh, R.2    Bordeleau, M.E.3    Kaufman, R.J.4    Northcote, P.5    Tanaka, J.6    Gallouzi, I.7    Pelletier, J.8
  • 60
    • 33645714857 scopus 로고    scopus 로고
    • Phosphatebinding tag, a new tool to visualize phosphorylated proteins
    • Kinoshita E, Kinoshita-Kikuta E, Takiyama K, Koike T. 2006. Phosphatebinding tag, a new tool to visualize phosphorylated proteins. Mol Cell Proteomics 5:749-757. https://doi.org/10.1074/mcp.T500024-MCP200
    • (2006) Mol Cell Proteomics , vol.5 , pp. 749-757
    • Kinoshita, E.1    Kinoshita-Kikuta, E.2    Takiyama, K.3    Koike, T.4
  • 61
    • 84988352997 scopus 로고    scopus 로고
    • Integrated stress response of vertebrates is regulated by four eIF2alpha kinases
    • Taniuchi S, Miyake M, Tsugawa K, Oyadomari M, Oyadomari S. 2016. Integrated stress response of vertebrates is regulated by four eIF2alpha kinases. Sci Rep 6:32886. https://doi.org/10.1038/srep32886
    • (2016) Sci Rep , vol.6 , pp. 32886
    • Taniuchi, S.1    Miyake, M.2    Tsugawa, K.3    Oyadomari, M.4    Oyadomari, S.5
  • 62
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • Meurs E, Chong K, Galabru J, Thomas NS, Kerr IM, Williams BR, Hovanessian AG. 1990. Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell 62:379-390. https://doi.org/10.1016/0092-8674(90)90374-N
    • (1990) Cell , vol.62 , pp. 379-390
    • Meurs, E.1    Chong, K.2    Galabru, J.3    Thomas, N.S.4    Kerr, I.M.5    Williams, B.R.6    Hovanessian, A.G.7
  • 63
    • 0041703031 scopus 로고    scopus 로고
    • The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: Elucidation by GADD34-deficient mice
    • Kojima E, Takeuchi A, Haneda M, Yagi A, Hasegawa T, Yamaki K, Takeda K, Akira S, Shimokata K, Isobe K. 2003. The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: elucidation by GADD34-deficient mice. FASEB J 17:1573-1575. https://doi.org/10.1096/fj.02-1184fje
    • (2003) FASEB J , vol.17 , pp. 1573-1575
    • Kojima, E.1    Takeuchi, A.2    Haneda, M.3    Yagi, A.4    Hasegawa, T.5    Yamaki, K.6    Takeda, K.7    Akira, S.8    Shimokata, K.9    Isobe, K.10
  • 64
    • 0041315834 scopus 로고    scopus 로고
    • Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress
    • Ma Y, Hendershot LM. 2003. Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress. J Biol Chem 278:34864-34873. https://doi.org/10.1074/jbc.M301107200
    • (2003) J Biol Chem , vol.278 , pp. 34864-34873
    • Ma, Y.1    Hendershot, L.M.2
  • 65
    • 0037416211 scopus 로고    scopus 로고
    • Stressinduced gene expression requires programmed recovery from translational repression
    • Novoa I, Zhang Y, Zeng H, Jungreis R, Harding HP, Ron D. 2003. Stressinduced gene expression requires programmed recovery from translational repression. EMBO J 22:1180-1187. https://doi.org/10.1093/emboj/cdg112
    • (2003) EMBO J , vol.22 , pp. 1180-1187
    • Novoa, I.1    Zhang, Y.2    Zeng, H.3    Jungreis, R.4    Harding, H.P.5    Ron, D.6
  • 66
    • 84943338797 scopus 로고    scopus 로고
    • EIF4F: A retrospective
    • Merrick WC. 2015. eIF4F: a retrospective. J Biol Chem 290:24091-24099. https://doi.org/10.1074/jbc.R115.675280
    • (2015) J Biol Chem , vol.290 , pp. 24091-24099
    • Merrick, W.C.1
  • 69
    • 77957852191 scopus 로고    scopus 로고
    • Regulation of eukaryotic initiation factor 4E (EIF4E) phosphorylation by mitogenactivated protein kinase occurs through modulation of Mnk1-eIF4G interaction
    • Shveygert M, Kaiser C, Bradrick SS, Gromeier M. 2010. Regulation of eukaryotic initiation factor 4E (eIF4E) phosphorylation by mitogenactivated protein kinase occurs through modulation of Mnk1-eIF4G interaction. Mol Cell Biol 30:5160-5167. https://doi.org/10.1128/MCB.00448-10
    • (2010) Mol Cell Biol , vol.30 , pp. 5160-5167
    • Shveygert, M.1    Kaiser, C.2    Bradrick, S.S.3    Gromeier, M.4
  • 70
    • 0032981328 scopus 로고    scopus 로고
    • Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo
    • Waskiewicz AJ, Johnson JC, Penn B, Mahalingam M, Kimball SR, Cooper JA. 1999. Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo. Mol Cell Biol 19:1871-1880. https://doi.org/10.1128/MCB.19.3.1871
    • (1999) Mol Cell Biol , vol.19 , 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
  • 71
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (EIF4G) recruits mnk1 to phosphorylate eIF4E
    • Pyronnet S, Imataka H, Gingras AC, Fukunaga R, Hunter T, Sonenberg N. 1999. Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E. EMBO J 18:270-279. https://doi.org/10.1093/emboj/18.1.270
    • (1999) EMBO J , vol.18 , pp. 270-279
    • Pyronnet, S.1    Imataka, H.2    Gingras, A.C.3    Fukunaga, R.4    Hunter, T.5    Sonenberg, N.6
  • 72
    • 84929095310 scopus 로고    scopus 로고
    • Murine norovirus 1 (MNV1) replication induces translational control of the host by regulating eIF4E activity during infection
    • Royall E, Doyle N, Abdul-Wahab A, Emmott E, Morley SJ, Goodfellow I, Roberts LO, Locker N. 2015. Murine norovirus 1 (MNV1) replication induces translational control of the host by regulating eIF4E activity during infection. J Biol Chem 290:4748-4758. https://doi.org/10.1074/jbc.M114.602649
    • (2015) J Biol Chem , vol.290 , pp. 4748-4758
    • Royall, E.1    Doyle, N.2    Abdul-Wahab, A.3    Emmott, E.4    Morley, S.J.5    Goodfellow, I.6    Roberts, L.O.7    Locker, N.8
  • 73
    • 61749103876 scopus 로고    scopus 로고
    • Stability of eukaryotic translation initiation factor 4E mRNA is regulated by HuR, and this activity is dysregulated in cancer
    • Topisirovic I, Siddiqui N, Orolicki S, Skrabanek LA, Tremblay M, Hoang T, Borden KL. 2009. Stability of eukaryotic translation initiation factor 4E mRNA is regulated by HuR, and this activity is dysregulated in cancer. Mol Cell Biol 29:1152-1162. https://doi.org/10.1128/MCB.01532-08
    • (2009) Mol Cell Biol , vol.29 , pp. 1152-1162
    • Topisirovic, I.1    Siddiqui, N.2    Orolicki, S.3    Skrabanek, L.A.4    Tremblay, M.5    Hoang, T.6    Borden, K.L.7
  • 74
    • 0033862548 scopus 로고    scopus 로고
    • Phosphorylation of eIF-4E on Ser 209 in response to mitogenic and inflammatory stimuli is faithfully detected by specific antibodies
    • Tschopp C, Knauf U, Brauchle M, Zurini M, Ramage P, Glueck D, New L, Han J, Gram H. 2000. Phosphorylation of eIF-4E on Ser 209 in response to mitogenic and inflammatory stimuli is faithfully detected by specific antibodies. Mol Cell Biol Res Commun 3:205-211. https://doi.org/10.1006/mcbr.2000.0217
    • (2000) Mol Cell Biol Res Commun , vol.3 , pp. 205-211
    • Tschopp, C.1    Knauf, U.2    Brauchle, M.3    Zurini, M.4    Ramage, P.5    Glueck, D.6    New, L.7    Han, J.8    Gram, H.9
  • 75
    • 0346750817 scopus 로고    scopus 로고
    • Mnk1 is required for angiotensin II-induced protein synthesis in vascular smooth muscle cells
    • Ishida M, Ishida T, Nakashima H, Miho N, Miyagawa K, Chayama K, Oshima T, Kambe M, Yoshizumi M. 2003. Mnk1 is required for angiotensin II-induced protein synthesis in vascular smooth muscle cells. Circ Res 93:1218-1224. https://doi.org/10.1161/01.RES.0000105570.34585.F2
    • (2003) Circ Res , vol.93 , pp. 1218-1224
    • Ishida, M.1    Ishida, T.2    Nakashima, H.3    Miho, N.4    Miyagawa, K.5    Chayama, K.6    Oshima, T.7    Kambe, M.8    Yoshizumi, M.9
  • 76
    • 0028988138 scopus 로고
    • SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1
    • Cuenda A, Rouse J, Doza YN, Meier R, Cohen P, Gallagher TF, Young PR, Lee JC. 1995. SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1. FEBS Lett 364:229-233. https://doi.org/10.1016/0014-5793(95)00357-F
    • (1995) FEBS Lett , vol.364 , pp. 229-233
    • Cuenda, A.1    Rouse, J.2    Doza, Y.N.3    Meier, R.4    Cohen, P.5    Gallagher, T.F.6    Young, P.R.7    Lee, J.C.8
  • 77
    • 0343431521 scopus 로고    scopus 로고
    • Translational control of viral gene expression in eukaryotes
    • Gale M, Jr., Tan SL, Katze MG. 2000. Translational control of viral gene expression in eukaryotes. Microbiol Mol Biol Rev 64:239-280. https://doi.org/10.1128/MMBR.64.2.239-280.2000
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 239-280
    • Gale, M.1    Tan, S.L.2    Katze, M.G.3
  • 78
    • 33845809231 scopus 로고    scopus 로고
    • P bodies: At the crossroads of post-transcriptional pathways
    • Eulalio A, Behm-Ansmant I, Izaurralde E. 2007. P bodies: at the crossroads of post-transcriptional pathways. Nat Rev Mol Cell Biol 8:9-22. https://doi.org/10.1038/nrm2080
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 9-22
    • Eulalio, A.1    Behm-Ansmant, I.2    Izaurralde, E.3
  • 80
    • 33746516731 scopus 로고    scopus 로고
    • HnRNP A1 relocalization to the stress granules reflects a role in the stress response
    • Guil S, Long JC, Cáceres JF. 2006. hnRNP A1 relocalization to the stress granules reflects a role in the stress response. Mol Cell Biol 26: 5744-5758. https://doi.org/10.1128/MCB.00224-06
    • (2006) Mol Cell Biol , vol.26 , pp. 5744-5758
    • Guil, S.1    Long, J.C.2    Cáceres, J.F.3
  • 81
    • 23844516065 scopus 로고    scopus 로고
    • The Mnks are novel components in the control of TNF alpha biosynthesis and phosphorylate and regulate hnRNP A1
    • Buxadé M, Parra JL, Rousseau S, Shpiro N, Marquez R, Morrice N, Bain J, Espel E, Proud CG. 2005. The Mnks are novel components in the control of TNF alpha biosynthesis and phosphorylate and regulate hnRNP A1. Immunity 23:177-189. https://doi.org/10.1016/j.immuni.2005.06.009
    • (2005) Immunity , vol.23 , pp. 177-189
    • Buxadé, 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
  • 82
    • 84944907005 scopus 로고    scopus 로고
    • Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization
    • Molliex A, Temirov J, Lee J, Coughlin M, Kanagaraj AP, Kim HJ, Mittag T, Taylor JP. 2015. Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization. Cell 163: 123-133. https://doi.org/10.1016/j.cell.2015.09.015
    • (2015) Cell , vol.163 , pp. 123-133
    • Molliex, A.1    Temirov, J.2    Lee, J.3    Coughlin, M.4    Kanagaraj, A.P.5    Kim, H.J.6    Mittag, T.7    Taylor, J.P.8
  • 83
    • 84859219968 scopus 로고    scopus 로고
    • Balanced codon usage optimizes eukaryotic translational efficiency
    • Qian W, Yang JR, Pearson NM, Maclean C, Zhang J. 2012. Balanced codon usage optimizes eukaryotic translational efficiency. PLoS Genet 8:e1002603. https://doi.org/10.1371/journal.pgen.1002603
    • (2012) Plos Genet , vol.8
    • Qian, W.1    Yang, J.R.2    Pearson, N.M.3    Maclean, C.4    Zhang, J.5
  • 85
    • 84886400497 scopus 로고    scopus 로고
    • The distribution of synonymous codon choice in the translation initiation region of dengue virus
    • Zhou JH, Zhang J, Sun DJ, Ma Q, Chen HT, Ma LN, Ding YZ, Liu YS. 2013. The distribution of synonymous codon choice in the translation initiation region of dengue virus. PLoS One 8:e77239. https://doi.org/10.1371/journal.pone.0077239
    • (2013) Plos One , vol.8
    • Zhou, J.H.1    Zhang, J.2    Sun, D.J.3    Ma, Q.4    Chen, H.T.5    Ma, L.N.6    Ding, Y.Z.7    Liu, Y.S.8
  • 89
    • 84867186265 scopus 로고    scopus 로고
    • Translation suppression promotes stress granule formation and cell survival in response to cold shock
    • Hofmann S, Cherkasova V, Bankhead P, Bukau B, Stoecklin G. 2012. Translation suppression promotes stress granule formation and cell survival in response to cold shock. Mol Biol Cell 23:3786-3800. https://doi.org/10.1091/mbc.E12-04-0296
    • (2012) Mol Biol Cell , vol.23 , pp. 3786-3800
    • Hofmann, S.1    Cherkasova, V.2    Bankhead, P.3    Bukau, B.4    Stoecklin, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.