메뉴 건너뛰기
Molecular and Cellular Biology
Volumn 34, Issue 11, 2014, Pages 2003-2016
Activation of stress response pathways promotes formation of antiviral granules and restricts virus replication
Author keywords

[No Author keywords available]
Indexed keywords

INITIATION FACTOR; METISAZONE; RNA HELICASE;
EID: 84899831575     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01630-13     Document Type: Article
Times cited : (45)
References (66)
  • 2
    • 42449154473 scopus 로고    scopus 로고
    • Poxviridae: the viruses and their replication
    • Knipe DM, Howley PM Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE ed Lippincott Williams & Wilkins, Philadelphia, PA
    • Moss B. 2007. Poxviridae: the viruses and their replication, p 2906-2945. In Knipe DM, Howley PM Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), Fields virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields virology , pp. 2906-2945
    • Moss, B.1
  • 3
    • 0042353728 scopus 로고    scopus 로고
    • Vaccinia virus transcription
    • Broyles SS. 2003. Vaccinia virus transcription. J. Gen. Virol. 84:2293-2303. http://dx.doi.org/10.1099/vir.0.18942-0.
    • (2003) J. Gen. Virol. , vol.84 , pp. 2293-2303
    • Broyles, S.S.1
  • 4
    • 77954934610 scopus 로고    scopus 로고
    • Simultaneous high-resolution analysis of vaccinia virus and host cell transcrip-tomes by deep RNA sequencing
    • Yang Z, Bruno DP, Martens CA, Porcella SF, Moss B. 2010. Simultaneous high-resolution analysis of vaccinia virus and host cell transcrip-tomes by deep RNA sequencing. Proc. Natl. Acad. Sci. U. S. A. 107:11513-11518. http://dx.doi.org/10.1073/pnas.1006594107.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 11513-11518
    • Yang, Z.1    Bruno, D.P.2    Martens, C.A.3    Porcella, S.F.4    Moss, B.5
  • 5
    • 80053956769 scopus 로고    scopus 로고
    • Expression profiling of the intermediate and late stages of poxvirus replication
    • Yang Z, Reynolds SE, Martens CA, Bruno DP, Porcella SF, Moss B. 2011. Expression profiling of the intermediate and late stages of poxvirus replication. J. Virol. 85:9899-9908. http://dx.doi.org/10.1128/JVI.05446-11.
    • (2011) J. Virol. , vol.85 , pp. 9899-9908
    • Yang, Z.1    Reynolds, S.E.2    Martens, C.A.3    Bruno, D.P.4    Porcella, S.F.5    Moss, B.6
  • 7
    • 0017370502 scopus 로고
    • Phosphorylation of initiation factor elF-2 and the control of reticulocyte protein synthesis
    • Farrell PJ, Balkow K, Hunt T, Jackson RJ, Trachsel H. 1977. Phosphorylation of initiation factor elF-2 and the control of reticulocyte protein synthesis. Cell 11:187-200. http://dx.doi.org/10.1016/0092-8674(77)90330-0.
    • (1977) Cell , vol.11 , pp. 187-200
    • Farrell, P.J.1    Balkow, K.2    Hunt, T.3    Jackson, R.J.4    Trachsel, H.5
  • 8
    • 0025947970 scopus 로고
    • Characterization of a vaccinia virus-encoded double-stranded RNA-binding protein that may be involved in inhibition of the double-stranded RNA-dependent protein kinase
    • Watson JC, Chang HW, Jacobs BL. 1991. Characterization of a vaccinia virus-encoded double-stranded RNA-binding protein that may be involved in inhibition of the double-stranded RNA-dependent protein kinase. Virology 185:206-216. http://dx.doi.org/10.1016/0042-6822(91) 90768-7.
    • (1991) Virology , vol.185 , pp. 206-216
    • Watson, J.C.1    Chang, H.W.2    Jacobs, B.L.3
  • 9
    • 0026751682 scopus 로고
    • The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNAdependent protein kinase
    • Chang HW, Watson JC, Jacobs BL. 1992. The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNAdependent protein kinase. Proc. Natl. Acad. Sci. U. S. A. 89:4825-4829. http://dx.doi.org/10.1073/pnas.89.11.4825.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 4825-4829
    • Chang, H.W.1    Watson, J.C.2    Jacobs, B.L.3
  • 10
    • 67449107496 scopus 로고    scopus 로고
    • Vaccinia virus E3 suppresses expression of diverse cytokines through inhibition of the PKR, NF-kappaB, and IRF3 pathways
    • Myskiw C, Arsenio J, van Bruggen R, Deschambault Y, Cao J. 2009. Vaccinia virus E3 suppresses expression of diverse cytokines through inhibition of the PKR, NF-kappaB, and IRF3 pathways. J. Virol. 83:6757-6768. http://dx.doi.org/10.1128/JVI.02570-08.
    • (2009) J. Virol. , vol.83 , pp. 6757-6768
    • Myskiw, C.1    Arsenio, J.2    van Bruggen, R.3    Deschambault, Y.4    Cao, J.5
  • 11
    • 24644482311 scopus 로고    scopus 로고
    • Biological function of the vaccinia virus Z-DNAbinding protein E3L: gene transactivation and antiapoptotic activity in HeLa cells
    • Kwon J-A, Rich A. 2005. Biological function of the vaccinia virus Z-DNAbinding protein E3L: gene transactivation and antiapoptotic activity in HeLa cells. Proc. Natl. Acad. Sci. U. S. A. 102:12759-12764. http://dx.doi.org/10.1073/pnas.0506011102.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 12759-12764
    • Kwon, J.-A.1    Rich, A.2
  • 12
    • 0036037388 scopus 로고    scopus 로고
    • The role of the PKR-inhibitory genes, E3L and K3L, in determining vaccinia virus host range
    • Langland JO, Jacobs BL. 2002. The role of the PKR-inhibitory genes, E3L and K3L, in determining vaccinia virus host range. Virology 299:133-141. http://dx.doi.org/10.1006/viro.2002.1479.
    • (2002) Virology , vol.299 , pp. 133-141
    • Langland, J.O.1    Jacobs, B.L.2
  • 13
    • 0034082457 scopus 로고    scopus 로고
    • PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex
    • Bonnet MC, Weil R, Dam E, Hovanessian AG, Meurs EF. 2000. PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex. Mol. Cell. Biol. 20:4532-4542. http://dx.doi.org/10.1128/MCB.20.13.4532-4542.2000.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4532-4542
    • Bonnet, M.C.1    Weil, R.2    Dam, E.3    Hovanessian, A.G.4    Meurs, E.F.5
  • 14
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding HP, Novoa I, Zhang Y, Zeng H, Wek R, Schapira M, Ron D. 2000. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6:1099-1108. http://dx.doi.org/10.1016/S1097-2765(00)00108-8.
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 15
    • 0031891869 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase
    • Srivastava SP, Kumar KU, Kaufman RJ. 1998. Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase. J. Biol. Chem. 273:2416-2423. http://dx.doi.org/10.1074/jbc.273.4.2416.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2416-2423
    • Srivastava, S.P.1    Kumar, K.U.2    Kaufman, R.J.3
  • 16
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding HP, Zhang Y, Bertolotti A, Zeng H, Ron D. 2000. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol. Cell 5:897-904. http://dx.doi.org/10.1016/S1097-2765(00)80330-5.
    • (2000) Mol. Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 17
    • 0029006391 scopus 로고
    • The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids
    • Wek SA, Zhu S, Wek RC. 1995. The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids. Mol. Cell. Biol. 15:4497-4506.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4497-4506
    • Wek, S.A.1    Zhu, S.2    Wek, R.C.3
  • 18
    • 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 J-J, 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. http://dx.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    Anderson, P.8    Kaufman, R.J.9
  • 19
    • 0036856008 scopus 로고    scopus 로고
    • Translational control in the endoplasmic reticulum stress response
    • Ron D. 2002. Translational control in the endoplasmic reticulum stress response. J. Clin. Invest. 110:1383-1388. http://dx.doi.org/10.1172/JCI 16784.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1383-1388
    • Ron, D.1
  • 20
    • 3242699557 scopus 로고    scopus 로고
    • Global mRNA stabilization preferentially linked to translational repression during the endoplasmic reticulum stress response
    • Kawai T, Fan J, Mazan-Mamczarz K, Gorospe M. 2004. Global mRNA stabilization preferentially linked to translational repression during the endoplasmic reticulum stress response. Mol. Cell. Biol. 24:6773-6787. http://dx.doi.org/10.1128/MCB.24.15.6773-6787.2004.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6773-6787
    • Kawai, T.1    Fan, J.2    Mazan-Mamczarz, K.3    Gorospe, M.4
  • 21
    • 32544446451 scopus 로고    scopus 로고
    • Coping with stress: eIF2 kinases and translational control
    • Wek RC, Jiang H-Y, Anthony TG. 2006. Coping with stress: eIF2 kinases and translational control. Biochem. Soc. Trans. 34:7-11. http://dx.doi.org/10.1042/BST0340007.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 7-11
    • Wek, R.C.1    Jiang, H.-Y.2    Anthony, T.G.3
  • 22
    • 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. http://dx.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    Anderson, P.5
  • 23
    • 77952628837 scopus 로고    scopus 로고
    • Regulation of translation by stress granules and processing bodies
    • Kedersha N, Anderson P. 2009. Regulation of translation by stress granules and processing bodies. Prog. Mol. Biol. Transl. Sci. 90:155-185. http://dx.doi.org/10.1016/S1877-1173(09)90004-7.
    • (2009) Prog. Mol. Biol. Transl. Sci. , vol.90 , pp. 155-185
    • Kedersha, N.1    Anderson, P.2
  • 24
    • 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. http://dx.doi.org/10.1016/j.tibs.2007.12.003.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 141-150
    • Anderson, P.1    Kedersha, N.2
  • 25
    • 0034638837 scopus 로고    scopus 로고
    • Dynamic shuttling of TIA-1 accompanies the recruitment ofmRNAto mammalian stress granules
    • Kedersha N, Cho MR, Li W, Yacono PW, Chen S, Gilks N, Golan DE, Anderson P. 2000. Dynamic shuttling of TIA-1 accompanies the recruitment ofmRNAto mammalian stress granules. J. Cell Biol. 151:1257-1268. http://dx.doi.org/10.1083/jcb.151.6.1257.
    • (2000) J. Cell Biol. , vol.151 , pp. 1257-1268
    • Kedersha, N.1    Cho, M.R.2    Li, W.3    Yacono, P.W.4    Chen, S.5    Gilks, N.6    Golan, D.E.7    Anderson, P.8
  • 26
    • 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 M-E, 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. http://dx.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
  • 27
    • 84864032746 scopus 로고    scopus 로고
    • How do viruses interact with stress-associated RNA granules
    • Lloyd RE. 2012. How do viruses interact with stress-associated RNA granules? PLoS Pathog. 8:e1002741. http://dx.doi.org/10.1371/journal.ppat.1002741.
    • (2012) PLoS Pathog , vol.8
    • Lloyd, R.E.1
  • 29
    • 79957637174 scopus 로고    scopus 로고
    • Development of vaccinia reporter viruses for rapid, high content analysis of viral function at all stages of gene expression
    • Dower K, Rubins KH, Hensley LE, Connor JH. 2011. Development of vaccinia reporter viruses for rapid, high content analysis of viral function at all stages of gene expression. Antiviral Res. 91:72-80. http://dx.doi.org/10.1016/j.antiviral.2011.04.014.
    • (2011) Antiviral Res. , vol.91 , pp. 72-80
    • Dower, K.1    Rubins, K.H.2    Hensley, L.E.3    Connor, J.H.4
  • 31
    • 84934444135 scopus 로고    scopus 로고
    • Cell sensitivity assays: the MTT assay
    • Van Meerloo J, Kaspers GJL, Cloos J. 2011. Cell sensitivity assays: the MTT assay. Methods Mol. Biol. 731:237-245. http://dx.doi.org/10.1007/978-1-61779-080-5_20.
    • (2011) Methods Mol. Biol. , vol.731 , pp. 237-245
    • Van Meerloo, J.1    Kaspers, G.J.L.2    Cloos, J.3
  • 32
    • 0028087602 scopus 로고
    • A tetrazolium-based colorimetric MTT assay to quantitate human monocyte mediated cytotoxicity against leukemic cells from cell lines and patients with acute myeloid leukemia
    • Van de Loosdrecht AA, Beelen RH, Ossenkoppele GJ, Broekhoven MG, Langenhuijsen MM. 1994. A tetrazolium-based colorimetric MTT assay to quantitate human monocyte mediated cytotoxicity against leukemic cells from cell lines and patients with acute myeloid leukemia. J. Immunol. Methods 174:311-320. http://dx.doi.org/10.1016/0022-1759(94)90034-5.
    • (1994) J. Immunol. Methods , vol.174 , pp. 311-320
    • Van de Loosdrecht, A.A.1    Beelen, R.H.2    Ossenkoppele, G.J.3    Broekhoven, M.G.4    Langenhuijsen, M.M.5
  • 34
    • 0028115847 scopus 로고
    • Assembly of vaccinia virus: effects of rifampin on the intracellular distribution of viral protein p65
    • Sodeik B, Griffiths G, Ericsson M, Moss B, Doms RW. 1994. Assembly of vaccinia virus: effects of rifampin on the intracellular distribution of viral protein p65. J. Virol. 68:1103-1114.
    • (1994) J. Virol. , vol.68 , pp. 1103-1114
    • Sodeik, B.1    Griffiths, G.2    Ericsson, M.3    Moss, B.4    Doms, R.W.5
  • 35
    • 79957582537 scopus 로고    scopus 로고
    • Development of the smallmolecule antiviral ST-246 as a smallpox therapeutic
    • Grosenbach DW, Jordan R, Hruby DE. 2011. Development of the smallmolecule antiviral ST-246 as a smallpox therapeutic. Future Virol. 6:653-671. http://dx.doi.org/10.2217/fvl.11.27.
    • (2011) Future Virol. , vol.6 , pp. 653-671
    • Grosenbach, D.W.1    Jordan, R.2    Hruby, D.E.3
  • 36
    • 84899809341 scopus 로고    scopus 로고
    • Protein labeling and immunoprecipitation
    • 7.0.1-7.0.3 cb0700s15
    • Bonifacino J. 2002. Protein labeling and immunoprecipitation. Curr. Protoc. Cell Biol. 15:7.0.1-7.0.3. http://dx.doi.org/10.1002/0471143030.cb0700s15.
    • (2002) Curr. Protoc. Cell Biol. , vol.15
    • Bonifacino, J.1
  • 38
    • 34848865040 scopus 로고    scopus 로고
    • Colocalization of transcription and translation within cytoplasmic poxvirus factories coordinates viral expression and subjugates host functions
    • Katsafanas GC, Moss B. 2007. Colocalization of transcription and translation within cytoplasmic poxvirus factories coordinates viral expression and subjugates host functions. Cell Host Microbe 2:221-228. http://dx.doi.org/10.1016/j.chom.2007.08.005.
    • (2007) Cell Host Microbe , vol.2 , pp. 221-228
    • Katsafanas, G.C.1    Moss, B.2
  • 39
    • 0344443730 scopus 로고    scopus 로고
    • Azide-alkyne coupling: a powerful reaction for bioconjugate chemistry
    • Breinbauer R, Köhn M. 2003. Azide-alkyne coupling: a powerful reaction for bioconjugate chemistry. Chembiochem 4:1147-1149. http://dx.doi.org/10.1002/cbic.200300705.
    • (2003) Chembiochem , vol.4 , pp. 1147-1149
    • Breinbauer, R.1    Köhn, M.2
  • 40
    • 0037454346 scopus 로고    scopus 로고
    • Bioconjugation by copper(I)-catalyzed azide-alkyne [3 _ 2] cycloaddition
    • Wang Q, Chan TR, Hilgraf R, Fokin VV, Sharpless KB, Finn MG. 2003. Bioconjugation by copper(I)-catalyzed azide-alkyne [3 _ 2] cycloaddition. J. Am. Chem. Soc. 125:3192-3193. http://dx.doi.org/10.1021/ja021381e.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3192-3193
    • Wang, Q.1    Chan, T.R.2    Hilgraf, R.3    Fokin, V.V.4    Sharpless, K.B.5    Finn, M.G.6
  • 41
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective ligation of azides and terminal alkynes
    • Rostovtsev VV, Green LG, Fokin VV, Sharpless KB. 2002. A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes. Angew. Chem. Int. Ed. Engl. 41: 2596-2599. http://dx.doi.org/10.1002/1521-3773(20020715)41:14_2596::AID-ANIE25963.0.CO;2-4.
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, L.G.2    Fokin, V.V.3    Sharpless, K.B.4
  • 42
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: diverse chemical function from a few good reactions
    • Kolb HC, Finn MG, Sharpless KB. 2001. Click chemistry: diverse chemical function from a few good reactions. Angew. Chem. Int. Ed. Engl.40:2004-2021. http://www.renyi.hu/stipsicz/Mezo_DECEMBER/click/click.pdf.
    • (2001) Angew. Chem. Int. Ed. Eng , vol.40 , pp. 2004-2021
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 44
    • 38449123517 scopus 로고    scopus 로고
    • Mammalian stress granules and processing bodies
    • Kedersha N, Anderson P. 2007. Mammalian stress granules and processing bodies. Methods Enzymol. 431:61-81. http://dx.doi.org/10.1016/S0076-6879(07)31005-7.
    • (2007) Methods Enzymol. , vol.431 , pp. 61-81
    • Kedersha, N.1    Anderson, P.2
  • 45
    • 0000332478 scopus 로고
    • The development of vaccinia virus in Earle's L strain cells as examined by electron microscopy
    • Dales S, Siminovitch L. 1961. The development of vaccinia virus in Earle's L strain cells as examined by electron microscopy. J. Biophys. Biochem. Cytol. 10:475-503. http://dx.doi.org/10.1083/jcb.10.4.475.
    • (1961) J. Biophys. Biochem. Cytol. , vol.10 , pp. 475-503
    • Dales, S.1    Siminovitch, L.2
  • 46
    • 0035157752 scopus 로고    scopus 로고
    • Vaccinia virus DNA replication occurs in endoplasmic reticulum-enclosed cytoplasmic mini-nuclei
    • Tolonen N, Doglio L, Schleich S, Krijnse Locker J. 2001. Vaccinia virus DNA replication occurs in endoplasmic reticulum-enclosed cytoplasmic mini-nuclei. Mol. Biol. Cell 12:2031-2046. http://dx.doi.org/10.1091/mbc.12.7.2031.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2031-2046
    • Tolonen, N.1    Doglio, L.2    Schleich, S.3    Krijnse Locker, J.4
  • 47
    • 0030027575 scopus 로고    scopus 로고
    • Individual RNA recognition motifs of TIA-1 and TIAR have different RNA binding specificities
    • Dember LM, Kim ND, Liu KQ, Anderson P. 1996. Individual RNA recognition motifs of TIA-1 and TIAR have different RNA binding specificities. J. Biol. Chem. 271:2783-2788. http://dx.doi.org/10.1074/jbc.271.5.2783.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2783-2788
    • Dember, L.M.1    Kim, N.D.2    Liu, K.Q.3    Anderson, P.4
  • 48
    • 84871954468 scopus 로고    scopus 로고
    • Japanese encephalitis virus core protein inhibits stress granule formation through an interaction with caprin-1 and facilitates viral propagation
    • Katoh H, Okamoto T, Fukuhara T, Kambara H, Morita E, Mori Y, Kamitani W, Matsuura Y. 2013. Japanese encephalitis virus core protein inhibits stress granule formation through an interaction with caprin-1 and facilitates viral propagation. J. Virol. 87:489-502. http://dx.doi.org/10.1128/JVI.02186-12.
    • (2013) J. Virol. , vol.87 , pp. 489-502
    • Katoh, H.1    Okamoto, T.2    Fukuhara, T.3    Kambara, H.4    Morita, E.5    Mori, Y.6    Kamitani, W.7    Matsuura, Y.8
  • 50
    • 35848929915 scopus 로고    scopus 로고
    • Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase
    • White JP, Cardenas AM, Marissen WE, Lloyd RE. 2007. Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase. Cell Host Microbe 2:295-305. http://dx.doi.org/10.1016/j.chom.2007.08.006.
    • (2007) Cell Host Microbe , vol.2 , pp. 295-305
    • White, J.P.1    Cardenas, A.M.2    Marissen, W.E.3    Lloyd, R.E.4
  • 51
    • 84861313238 scopus 로고    scopus 로고
    • The amino terminus of the vaccinia virus E3 protein is necessary to inhibit the interferon response
    • White SD, Jacobs BL. 2012. The amino terminus of the vaccinia virus E3 protein is necessary to inhibit the interferon response. J. Virol. 86:5895-5904. http://dx.doi.org/10.1128/JVI.06889-11.
    • (2012) J. Virol. , vol.86 , pp. 5895-5904
    • White, S.D.1    Jacobs, B.L.2
  • 52
    • 0037416211 scopus 로고    scopus 로고
    • Stress-induced gene expression requires programmed recovery from translational repression
    • Novoa I, Zhang Y, Zeng H, Jungreis R, Harding HP, Ron D. 2003. Stress-induced gene expression requires programmed recovery from translational repression. EMBO J. 22:1180-1187. http://dx.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
  • 53
    • 0021213820 scopus 로고
    • Effects of 1-beta-D-arabinofuranosylcytosine incorporation on eukaryotic DNA template function
    • Kufe DW, Munroe D, Herrick D, Egan E, Spriggs D. 1984. Effects of 1-beta-D-arabinofuranosylcytosine incorporation on eukaryotic DNA template function. Mol. Pharmacol. 26:128-134.
    • (1984) Mol. Pharmacol. , vol.26 , pp. 128-134
    • Kufe, D.W.1    Munroe, D.2    Herrick, D.3    Egan, E.4    Spriggs, D.5
  • 54
    • 7244219995 scopus 로고    scopus 로고
    • An isatin-betathiosemicarbazone-resistant vaccinia virus containing a mutation in the second largest subunit of the viral RNA polymerase is defective in transcription elongation
    • Prins C, Cresawn SG, Condit RC. 2004. An isatin-betathiosemicarbazone-resistant vaccinia virus containing a mutation in the second largest subunit of the viral RNA polymerase is defective in transcription elongation. J. Biol. Chem. 279:44858-44871. http://dx.doi.org/10.1074/jbc. M408167200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44858-44871
    • Prins, C.1    Cresawn, S.G.2    Condit, R.C.3
  • 55
    • 0014693136 scopus 로고
    • Rifampicin: a specific inhibitor of vaccinia virus assembly
    • Moss B, Rosenblum EN, Katz E, Grimley PM. 1969. Rifampicin: a specific inhibitor of vaccinia virus assembly. Nature 224:1280-1284. http://dx.doi.org/10.1038/2241280a0.
    • (1969) Nature , vol.224 , pp. 1280-1284
    • Moss, B.1    Rosenblum, E.N.2    Katz, E.3    Grimley, P.M.4
  • 57
    • 0035031195 scopus 로고    scopus 로고
    • Introduction: the history of arsenic trioxide in cancer therapy
    • Antman KH. 2001. Introduction: the history of arsenic trioxide in cancer therapy. Oncologist 6(Suppl 2):1-2. http://dx.doi.org/10.1634/theoncologist.6-(suppl 2)-1-2
    • (2001) Oncologist , vol.6 , Issue.SUPPL. 2 , pp. 1-2
    • Antman, K.H.1
  • 58
    • 0002829905 scopus 로고
    • Action of iron, cod-liver oil, and arsenic on the globular richness of the blood
    • Cutler EG, Bradford EH. 1878. Action of iron, cod-liver oil, and arsenic on the globular richness of the blood. Am. J. Med. Sci. 75:74-84.
    • (1878) Am. J. Med. Sci. , vol.75 , pp. 74-84
    • Cutler, E.G.1    Bradford, E.H.2
  • 59
    • 33644916362 scopus 로고    scopus 로고
    • RNA granules
    • Anderson P, Kedersha N. 2006. RNA granules. J. Cell Biol. 172:803-808. http://dx.doi.org/10.1083/jcb.200512082.
    • (2006) J. Cell Biol. , vol.172 , pp. 803-808
    • Anderson, P.1    Kedersha, N.2
  • 60
    • 84871196139 scopus 로고    scopus 로고
    • Sequestration of G3BP coupled with efficient translation inhibits stress granules in Semliki Forest virus infection
    • Panas MD, Varjak M, Lulla A, Eng KE, Merits A, Karlsson Hedestam GB, McInerney GM. 2012. Sequestration of G3BP coupled with efficient translation inhibits stress granules in Semliki Forest virus infection. Mol. Biol. Cell 23:4701-4712. http://dx.doi.org/10.1091/mbc. E12-08-0619.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4701-4712
    • Panas, M.D.1    Varjak, M.2    Lulla, A.3    Eng, K.E.4    Merits, A.5    Karlsson Hedestam, G.B.6    McInerney, G.M.7
  • 61
    • 84869049624 scopus 로고    scopus 로고
    • Chikungunya virus nsP3 blocks stress granule assembly by recruitment of G3BP into cytoplasmic foci
    • Fros JJ, Domeradzka NE, Baggen J, Geertsema C, Flipse J, Vlak JM, Pijlman GP. 2012. Chikungunya virus nsP3 blocks stress granule assembly by recruitment of G3BP into cytoplasmic foci. J. Virol. 86:10873-10879. http://dx.doi.org/10.1128/JVI.01506-12.
    • (2012) J. Virol. , vol.86 , pp. 10873-10879
    • Fros, J.J.1    Domeradzka, N.E.2    Baggen, J.3    Geertsema, C.4    Flipse, J.5    Vlak, J.M.6    Pijlman, G.P.7
  • 62
    • 81255123305 scopus 로고    scopus 로고
    • Poliovirus unlinks TIA1 aggregation and mRNA stress granule formation
    • White JP, Lloyd RE. 2011. Poliovirus unlinks TIA1 aggregation and mRNA stress granule formation. J. Virol. 85:12442-12454. http://dx.doi.org/10.1128/JVI.05888-11.
    • (2011) J. Virol. , vol.85 , pp. 12442-12454
    • White, J.P.1    Lloyd, R.E.2
  • 63
    • 77949389673 scopus 로고    scopus 로고
    • Stable formation of compositionally unique stress granules in virusinfected cells
    • Piotrowska J, Hansen SJ, Park N, Jamka K, Sarnow P, Gustin KE. 2010. Stable formation of compositionally unique stress granules in virusinfected cells. J. Virol. 84:3654-3665. http://dx.doi.org/10.1128/JVI.01320-09.
    • (2010) J. Virol. , vol.84 , pp. 3654-3665
    • Piotrowska, J.1    Hansen, S.J.2    Park, N.3    Jamka, K.4    Sarnow, P.5    Gustin, K.E.6
  • 64
    • 84869218756 scopus 로고    scopus 로고
    • The NS1 protein of influenza A virus interacts with cellular processing bodies and stress granules through RNA-associated protein 55 (RAP55) during virus infection
    • Mok BW-Y, Song W, Wang P, Tai H, Chen Y, Zheng M, Wen X, Lau S-Y, Wu WL, Matsumoto K, Yuen K-Y, Chen H. 2012. The NS1 protein of influenza A virus interacts with cellular processing bodies and stress granules through RNA-associated protein 55 (RAP55) during virus infection. J. Virol. 86:12695-12707. http://dx.doi.org/10.1128/JVI.00647-12.
    • (2012) J. Virol. , vol.86 , pp. 12695-12707
    • Mok, B.W.-Y.1    Song, W.2    Wang, P.3    Tai, H.4    Chen, Y.5    Zheng, M.6    Wen, X.7    Lau, S.-Y.8    Wu, W.L.9    Matsumoto, K.10    Yuen, K.-Y.11    Chen, H.12

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.