메뉴 건너뛰기
Journal of Virology
Volumn 90, Issue 17, 2016, Pages 7943-7955
Herpes simplex virus 2 virion host shutoff endoribonuclease activity is required to disrupt stress granule formation
Author keywords

[No Author keywords available]
Indexed keywords

INITIATION FACTOR 2ALPHA; MESSENGER RNA; RIBONUCLEASE; UNCLASSIFIED DRUG; VIRION HOST SHUTOFF PROTEIN; MUTANT PROTEIN; VIRAL PROTEIN; VIRION HOST SHUTOFF PROTEIN, SIMPLEXVIRUS;
EID: 84983543660     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00947-16     Document Type: Article
Times cited : (21)
References (80)
  • 1
    • 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
  • 2
    • 32544446451 scopus 로고    scopus 로고
    • Coping with stress: eIF2 kinases and translational control
    • Wek RC, Jiang HY, 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
  • 3
    • 84884587610 scopus 로고    scopus 로고
    • Stress granules and cell signaling:more than just a passing phase?
    • Kedersha N, Ivanov P, Anderson P. 2013. Stress granules and cell signaling:more than just a passing phase? Trends Biochem Sci 38:494-506. http://dx.doi.org/10.1016/j.tibs.2013.07.004.
    • (2013) Trends Biochem Sci , vol.38 , pp. 494-506
    • Kedersha, N.1    Ivanov, P.2    Anderson, P.3
  • 4
    • 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. 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
  • 5
    • 33845950751 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2alphaindependent 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. 2006. Eukaryotic initiation factor 2alphaindependent pathway of stress granule induction by the natural product pateamine A. J Biol Chem 281:32870-32878. http://dx.doi.org/10.1074/ jbc.M606149200.
    • (2006) J Biol Chem , vol.281 , 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
  • 6
    • 0034638837 scopus 로고    scopus 로고
    • Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to 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 of mRNA to 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
  • 8
    • 84888429488 scopus 로고    scopus 로고
    • RNA seeds higherorder assembly of FUS protein
    • Schwartz JC, Wang X, Podell ER, Cech TR. 2013. RNA seeds higherorder assembly of FUS protein. Cell Rep 5:918-925. http://dx.doi.org/10 .1016/j.celrep.2013.11.017.
    • (2013) Cell Rep , vol.5 , pp. 918-925
    • Schwartz, J.C.1    Wang, X.2    Podell, E.R.3    Cech, T.R.4
  • 11
    • 36049032156 scopus 로고    scopus 로고
    • The cold-inducible RNA-binding protein migrates from the nucleus to cytoplasmic stress granules by a methylation-dependent mechanism and acts as a translational repressor
    • De Leeuw F, Zhang T, Wauquier C, Huez G, Kruys V, Gueydan C. 2007. The cold-inducible RNA-binding protein migrates from the nucleus to cytoplasmic stress granules by a methylation-dependent mechanism and acts as a translational repressor. Exp Cell Res 313:4130-4144. http://dx.doi.org/10.1016/j.yexcr.2007.09.017.
    • (2007) Exp Cell Res , vol.313 , pp. 4130-4144
    • De Leeuw, F.1    Zhang, T.2    Wauquier, C.3    Huez, G.4    Kruys, V.5    Gueydan, C.6
  • 12
    • 33744516148 scopus 로고    scopus 로고
    • Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP
    • Dolzhanskaya N, Merz G, Aletta JM, Denman RB. 2006. Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP. J Cell Sci 119:1933-1946. http://dx.doi.org/10.1242/jcs.02882.
    • (2006) J Cell Sci , vol.119 , pp. 1933-1946
    • Dolzhanskaya, N.1    Merz, G.2    Aletta, J.M.3    Denman, R.B.4
  • 13
    • 37449030154 scopus 로고    scopus 로고
    • The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response
    • Kwon S, Zhang Y, Matthias P. 2007. The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response. Genes Dev 21:3381-3394. http://dx.doi.org/10.1101/gad.461107.
    • (2007) Genes Dev , vol.21 , pp. 3381-3394
    • Kwon, S.1    Zhang, Y.2    Matthias, P.3
  • 14
    • 53349165578 scopus 로고    scopus 로고
    • A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly
    • Ohn T, Kedersha N, Hickman T, Tisdale S, Anderson P. 2008. A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly. Nat Cell Biol 10:1224-1231. http://dx.doi.org/10.1038/ncb1783.
    • (2008) Nat Cell Biol , vol.10 , pp. 1224-1231
    • Ohn, T.1    Kedersha, N.2    Hickman, T.3    Tisdale, S.4    Anderson, P.5
  • 15
    • 84872189805 scopus 로고    scopus 로고
    • Quantitative proteomics and dynamic imaging reveal that G3BP-mediated stress granule assembly is poly(ADP-ribose)-dependent following exposure to MNNG-induced DNA alkylation
    • Isabelle M, Gagne JP, Gallouzi IE, Poirier GG. 2012. Quantitative proteomics and dynamic imaging reveal that G3BP-mediated stress granule assembly is poly(ADP-ribose)-dependent following exposure to MNNG-induced DNA alkylation. J Cell Sci 125:4555-4566. http://dx.doi .org/10.1242/jcs.106963.
    • (2012) J Cell Sci , vol.125 , pp. 4555-4566
    • Isabelle, M.1    Gagne, J.P.2    Gallouzi, I.E.3    Poirier, G.G.4
  • 16
    • 84862196500 scopus 로고    scopus 로고
    • Poly(ADP-ribose) regulates post-transcriptional gene regulation in the cytoplasm
    • Leung A, Todorova T, Ando Y, Chang P. 2012. Poly(ADP-ribose) regulates post-transcriptional gene regulation in the cytoplasm. RNA Biol 9:542-548. http://dx.doi.org/10.4161/rna.19899.
    • (2012) RNA Biol , vol.9 , pp. 542-548
    • Leung, A.1    Todorova, T.2    Ando, Y.3    Chang, P.4
  • 17
    • 79955957616 scopus 로고    scopus 로고
    • Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm
    • Leung AK, Vyas S, Rood JE, Bhutkar A, Sharp PA, Chang P. 2011. Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm. Mol Cell 42:489-499. http://dx.doi.org/10.1016/j.molcel.2011 .04.015.
    • (2011) Mol Cell , vol.42 , pp. 489-499
    • Leung, A.K.1    Vyas, S.2    Rood, J.E.3    Bhutkar, A.4    Sharp, P.A.5    Chang, P.6
  • 18
    • 84940503517 scopus 로고    scopus 로고
    • Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
    • Kroschwald S, Maharana S, Mateju D, Malinovska L, Nuske E, Poser I, Richter D, Alberti S. 2015. Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules. eLife 4:e06807. http://dx.doi.org/10.7554/eLife.06807.
    • (2015) eLife , vol.4
    • Kroschwald, S.1    Maharana, S.2    Mateju, D.3    Malinovska, L.4    Nuske, E.5    Poser, I.6    Richter, D.7    Alberti, S.8
  • 19
    • 0142026265 scopus 로고    scopus 로고
    • Disruption of microtubules inhibits cytoplasmic ribonucleoprotein stress granule formation
    • Ivanov PA, Chudinova EM, Nadezhdina ES. 2003. Disruption of microtubules inhibits cytoplasmic ribonucleoprotein stress granule formation. Exp Cell Res 290:227-233. http://dx.doi.org/10.1016/S0014-4827(03)00290-8.
    • (2003) Exp Cell Res , vol.290 , pp. 227-233
    • Ivanov, P.A.1    Chudinova, E.M.2    Nadezhdina, E.S.3
  • 20
    • 0037356739 scopus 로고    scopus 로고
    • RNP stress-granule formation is inhibited by microtubule disruption
    • Ivanov PA, Chudinova EM, Nadezhdina ES. 2003. RNP stress-granule formation is inhibited by microtubule disruption. Cell Biol Int 27:207-208. http://dx.doi.org/10.1016/S1065-6995(02)00341-4.
    • (2003) Cell Biol Int , vol.27 , pp. 207-208
    • Ivanov, P.A.1    Chudinova, E.M.2    Nadezhdina, E.S.3
  • 21
    • 73649097951 scopus 로고    scopus 로고
    • Role of microtubules in stress granule assembly: microtubule dynamical instability favors the formation of micrometric stress granules in cells
    • Chernov KG, Barbet A, Hamon L, Ovchinnikov LP, Curmi PA, Pastre D. 2009. Role of microtubules in stress granule assembly: microtubule dynamical instability favors the formation of micrometric stress granules in cells. J Biol Chem 284:36569-36580. http://dx.doi.org/10.1074/jbc .M109.042879.
    • (2009) J Biol Chem , vol.284 , pp. 36569-36580
    • Chernov, K.G.1    Barbet, A.2    Hamon, L.3    Ovchinnikov, L.P.4    Curmi, P.A.5    Pastre, D.6
  • 22
    • 70450285065 scopus 로고    scopus 로고
    • Dynein and kinesin regulate stress-granule and P-body dynamics
    • Loschi M, Leishman CC, Berardone N, Boccaccio GL. 2009. Dynein and kinesin regulate stress-granule and P-body dynamics. J Cell Sci 122:3973-3982. http://dx.doi.org/10.1242/jcs.051383.
    • (2009) J Cell Sci , vol.122 , pp. 3973-3982
    • Loschi, M.1    Leishman, C.C.2    Berardone, N.3    Boccaccio, G.L.4
  • 23
    • 84905870282 scopus 로고    scopus 로고
    • RNA granules and cytoskeletal links
    • Rajgor D, Shanahan CM. 2014. RNA granules and cytoskeletal links. Biochem Soc Trans 42:1206-1210. http://dx.doi.org/10.1042/BST20140067.
    • (2014) Biochem Soc Trans , vol.42 , pp. 1206-1210
    • Rajgor, D.1    Shanahan, C.M.2
  • 24
    • 84955625345 scopus 로고    scopus 로고
    • ATPase-modulated stress granules contain a diverse proteome and substructure
    • Jain S, Wheeler JR, Walters RW, Agrawal A, Barsic A, Parker R. 2016. ATPase-modulated stress granules contain a diverse proteome and substructure. Cell 164:487-498. http://dx.doi.org/10.1016/j.cell.2015.12.038.
    • (2016) Cell , vol.164 , pp. 487-498
    • Jain, S.1    Wheeler, J.R.2    Walters, R.W.3    Agrawal, A.4    Barsic, A.5    Parker, R.6
  • 25
    • 84874040052 scopus 로고    scopus 로고
    • Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling
    • Wippich F, Bodenmiller B, Trajkovska MG, Wanka S, Aebersold R, Pelkmans L. 2013. Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling. Cell 152:791-805. http://dx.doi.org/10.1016/j.cell.2013.01.033.
    • (2013) Cell , vol.152 , pp. 791-805
    • Wippich, F.1    Bodenmiller, B.2    Trajkovska, M.G.3    Wanka, S.4    Aebersold, R.5    Pelkmans, L.6
  • 26
    • 84864387040 scopus 로고    scopus 로고
    • Herpes simplex virus 2 infection impacts stress granule accumulation
    • Finnen RL, Pangka KR, Banfield BW. 2012. Herpes simplex virus 2 infection impacts stress granule accumulation. J Virol 86:8119-8130. http://dx.doi.org/10.1128/JVI.00313-12.
    • (2012) J Virol , vol.86 , pp. 8119-8130
    • Finnen, R.L.1    Pangka, K.R.2    Banfield, B.W.3
  • 27
    • 84907434194 scopus 로고    scopus 로고
    • The herpes simplex virus 2 virion-associated ribonuclease vhs interferes with stress granule formation
    • Finnen RL, Hay TJ, Dauber B, Smiley JR, Banfield BW. 2014. The herpes simplex virus 2 virion-associated ribonuclease vhs interferes with stress granule formation. J Virol 88:12727-12739. http://dx.doi .org/10.1128/JVI.01554-14.
    • (2014) J Virol , vol.88 , pp. 12727-12739
    • Finnen, R.L.1    Hay, T.J.2    Dauber, B.3    Smiley, J.R.4    Banfield, B.W.5
  • 28
    • 0036333951 scopus 로고    scopus 로고
    • mRNA degradation by the virion host shutoff (Vhs) protein of herpes simplex virus: genetic and biochemical evidence that Vhs is a nuclease
    • Everly DN, Jr, Feng P, Mian IS, Read GS. 2002. mRNA degradation by the virion host shutoff (Vhs) protein of herpes simplex virus: genetic and biochemical evidence that Vhs is a nuclease. J Virol 76:8560-8571. http://dx.doi.org/10.1128/JVI.76.17.8560-8571.2002.
    • (2002) J Virol , vol.76 , pp. 8560-8571
    • Everly, D.N.1    Feng, P.2    Mian, I.S.3    Read, G.S.4
  • 29
    • 0029919184 scopus 로고    scopus 로고
    • The virion host shutoff protein of herpes simplex virus type 1: messenger ribonucleolytic activity in vitro
    • Zelus BD, Stewart RS, Ross J. 1996. The virion host shutoff protein of herpes simplex virus type 1: messenger ribonucleolytic activity in vitro. J Virol 70:2411-2419.
    • (1996) J Virol , vol.70 , pp. 2411-2419
    • Zelus, B.D.1    Stewart, R.S.2    Ross, J.3
  • 31
    • 0018100597 scopus 로고
    • Anatomy of herpes simplex virus (HSV) DNA X. Mapping of viral genes by analysis of polypeptides and functions specified by HSV-1 × HSV-2 recombinants
    • Morse LS, Pereira L, Roizman B, Schaffer PA. 1978. Anatomy of herpes simplex virus (HSV) DNA. X. Mapping of viral genes by analysis of polypeptides and functions specified by HSV-1 × HSV-2 recombinants. J Virol 26:389-410.
    • (1978) J Virol , vol.26 , pp. 389-410
    • Morse, L.S.1    Pereira, L.2    Roizman, B.3    Schaffer, P.A.4
  • 32
    • 33846505946 scopus 로고    scopus 로고
    • Packaging of the virion host shutoff (Vhs) protein of herpes simplex virus: two forms of the Vhs polypeptide are associated with intranuclear B and C capsids, but only one is associated with enveloped virions
    • Read GS, Patterson M. 2007. Packaging of the virion host shutoff (Vhs) protein of herpes simplex virus: two forms of the Vhs polypeptide are associated with intranuclear B and C capsids, but only one is associated with enveloped virions. J Virol 81:1148-1161. http://dx.doi.org/10.1128/ JVI.01812-06.
    • (2007) J Virol , vol.81 , pp. 1148-1161
    • Read, G.S.1    Patterson, M.2
  • 33
    • 0026537536 scopus 로고
    • Identification and characterization of the virion-induced host shutoff product of herpes simplex virus gene UL41
    • Smibert CA, Johnson DC, Smiley JR. 1992. Identification and characterization of the virion-induced host shutoff product of herpes simplex virus gene UL41. J Gen Virol 73:467-470. http://dx.doi.org/10.1099/0022-1317-73-2-467.
    • (1992) J Gen Virol , vol.73 , pp. 467-470
    • Smibert, C.A.1    Johnson, D.C.2    Smiley, J.R.3
  • 34
    • 84939997955 scopus 로고    scopus 로고
    • Emerging roles for RNA degradation in viral replication and antiviral defense
    • Abernathy E, Glaunsinger B. 2015. Emerging roles for RNA degradation in viral replication and antiviral defense. Virology 479-480:600-608. http://dx.doi.org/10.1016/j.virol.2015.02.007.
    • (2015) Virology , vol.479-480 , pp. 600-608
    • Abernathy, E.1    Glaunsinger, B.2
  • 35
    • 84866149031 scopus 로고    scopus 로고
    • A common strategy for host RNA degradation by divergent viruses
    • Gaglia MM, Covarrubias S, Wong W, Glaunsinger BA. 2012. A common strategy for host RNA degradation by divergent viruses. J Virol 86:9527-9530. http://dx.doi.org/10.1128/JVI.01230-12.
    • (2012) J Virol , vol.86 , pp. 9527-9530
    • Gaglia, M.M.1    Covarrubias, S.2    Wong, W.3    Glaunsinger, B.A.4
  • 36
    • 0031058732 scopus 로고    scopus 로고
    • Repression of host RNA polymerase II transcription by herpes simplex virus type 1
    • Spencer CA, Dahmus ME, Rice SA. 1997. Repression of host RNA polymerase II transcription by herpes simplex virus type 1. J Virol 71:2031-2040.
    • (1997) J Virol , vol.71 , pp. 2031-2040
    • Spencer, C.A.1    Dahmus, M.E.2    Rice, S.A.3
  • 37
    • 0028029752 scopus 로고
    • Herpes simplex virus inhibits host cell splicing, and regulatory protein ICP27 is required for this effect
    • Hardy WR, Sandri-Goldin RM. 1994. Herpes simplex virus inhibits host cell splicing, and regulatory protein ICP27 is required for this effect. J Virol 68:7790-7799.
    • (1994) J Virol , vol.68 , pp. 7790-7799
    • Hardy, W.R.1    Sandri-Goldin, R.M.2
  • 38
    • 8644221609 scopus 로고    scopus 로고
    • Herpes simplex virus virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4H
    • Doepker RC, Hsu WL, Saffran HA, Smiley JR. 2004. Herpes simplex virus virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4H. J Virol 78:4684-4699. http://dx.doi.org/10.1128/ JVI.78.9.4684-4699.2004.
    • (2004) J Virol , vol.78 , pp. 4684-4699
    • Doepker, R.C.1    Hsu, W.L.2    Saffran, H.A.3    Smiley, J.R.4
  • 39
    • 22544452431 scopus 로고    scopus 로고
    • mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A
    • Feng P, Everly DN, Jr, Read GS. 2005. mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A. J Virol 79:9651-9664. http://dx.doi.org/10.1128/JVI.79.15.9651-9664 .2005.
    • (2005) J Virol , vol.79 , pp. 9651-9664
    • Feng, P.1    Everly, D.N.2    Read, G.S.3
  • 40
    • 77953302048 scopus 로고    scopus 로고
    • The virion host shutoff endonuclease (UL41) of herpes simplex virus interacts with the cellular cap-binding complex eIF4F
    • Page HG, Read GS. 2010. The virion host shutoff endonuclease (UL41) of herpes simplex virus interacts with the cellular cap-binding complex eIF4F. J Virol 84:6886-6890. http://dx.doi.org/10.1128/JVI.00166-10.
    • (2010) J Virol , vol.84 , pp. 6886-6890
    • Page, H.G.1    Read, G.S.2
  • 41
    • 79956061719 scopus 로고    scopus 로고
    • The herpes simplex virus 1 vhs protein enhances translation of viral true late mRNAs and virus production in a cell type-dependent manner
    • Dauber B, Pelletier J, Smiley JR. 2011. The herpes simplex virus 1 vhs protein enhances translation of viral true late mRNAs and virus production in a cell type-dependent manner. J Virol 85:5363-5373. http://dx.doi .org/10.1128/JVI.00115-11.
    • (2011) J Virol , vol.85 , pp. 5363-5373
    • Dauber, B.1    Pelletier, J.2    Smiley, J.R.3
  • 42
    • 84907428121 scopus 로고    scopus 로고
    • The herpes simplex virus 1 virion host shutoff protein enhances translation of viral late mRNAs by preventing mRNA overload
    • Dauber B, Saffran HA, Smiley JR. 2014. The herpes simplex virus 1 virion host shutoff protein enhances translation of viral late mRNAs by preventing mRNA overload. J Virol 88:9624-9632. http://dx.doi.org/10.1128/JVI .01350-14.
    • (2014) J Virol , vol.88 , pp. 9624-9632
    • Dauber, B.1    Saffran, H.A.2    Smiley, J.R.3
  • 43
    • 77952702091 scopus 로고    scopus 로고
    • Evidence for translational regulation by the herpes simplex virus virion host shutoff protein
    • Saffran HA, Read GS, Smiley JR. 2010. Evidence for translational regulation by the herpes simplex virus virion host shutoff protein. J Virol 84:6041-6049. http://dx.doi.org/10.1128/JVI.01819-09.
    • (2010) J Virol , vol.84 , pp. 6041-6049
    • Saffran, H.A.1    Read, G.S.2    Smiley, J.R.3
  • 44
    • 0032853361 scopus 로고    scopus 로고
    • Picornavirus internal ribosome entry site elements target RNA cleavage events induced by the herpes simplex virus virion host shutoff protein
    • Elgadi MM, Smiley JR. 1999. Picornavirus internal ribosome entry site elements target RNA cleavage events induced by the herpes simplex virus virion host shutoff protein. J Virol 73:9222-9231.
    • (1999) J Virol , vol.73 , pp. 9222-9231
    • Elgadi, M.M.1    Smiley, J.R.2
  • 45
    • 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
  • 46
    • 0345411633 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the virion host shutoff gene (UL41) of herpes simplex virus (HSV): analysis of functional differences between HSV type 1 (HSV-1) and HSV-2 alleles
    • Everly DN, Jr, Read GS. 1999. Site-directed mutagenesis of the virion host shutoff gene (UL41) of herpes simplex virus (HSV): analysis of functional differences between HSV type 1 (HSV-1) and HSV-2 alleles. J Virol 73:9117-9129.
    • (1999) J Virol , vol.73 , pp. 9117-9129
    • Everly, D.N.1    Read, G.S.2
  • 47
    • 0032475933 scopus 로고    scopus 로고
    • Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNAand PCNA binding to FEN-1 activity
    • Hosfield DJ, Mol CD, Shen B, Tainer JA. 1998. Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNAand PCNA binding to FEN-1 activity. Cell 95:135-146. http://dx.doi .org/10.1016/S0092-8674(00)81789-4.
    • (1998) Cell , vol.95 , pp. 135-146
    • Hosfield, D.J.1    Mol, C.D.2    Shen, B.3    Tainer, J.A.4
  • 49
    • 0025340198 scopus 로고
    • Comparative DNA sequence analysis of the host shutoff genes of different strains of herpes simplex virus: type 2 strain HG52 encodes a truncated UL41 product
    • Everett RD, Fenwick ML. 1990. Comparative DNA sequence analysis of the host shutoff genes of different strains of herpes simplex virus: type 2 strain HG52 encodes a truncated UL41 product. J Gen Virol 71:1387-1390. http://dx.doi.org/10.1099/0022-1317-71-6-1387.
    • (1990) J Gen Virol , vol.71 , pp. 1387-1390
    • Everett, R.D.1    Fenwick, M.L.2
  • 50
    • 41149134311 scopus 로고    scopus 로고
    • Selective ablation of virion host shutoff protein RNase activity attenuates herpes simplex virus 2 in mice
    • Korom M, Wylie KM, Morrison LA. 2008. Selective ablation of virion host shutoff protein RNase activity attenuates herpes simplex virus 2 in mice. J Virol 82:3642-3653. http://dx.doi.org/10.1128/JVI.02409-07.
    • (2008) J Virol , vol.82 , pp. 3642-3653
    • Korom, M.1    Wylie, K.M.2    Morrison, L.A.3
  • 51
    • 84860900591 scopus 로고    scopus 로고
    • Influenza A virus inhibits cytoplasmic stress granule formation
    • Khaperskyy DA, Hatchette TF, McCormick C. 2012. Influenza A virus inhibits cytoplasmic stress granule formation. FASEB J 26:1629-1639. http://dx.doi.org/10.1096/fj.11-196915.
    • (2012) FASEB J , vol.26 , pp. 1629-1639
    • Khaperskyy, D.A.1    Hatchette, T.F.2    McCormick, C.3
  • 53
    • 79955159135 scopus 로고    scopus 로고
    • En passant mutagenesis: a two step markerless Red recombination system
    • Tischer BK, Smith GA, Osterrieder N. 2010. En passant mutagenesis: a two step markerless Red recombination system. Methods Mol Biol 634:421-430. http://dx.doi.org/10.1007/978-1-60761-652-8_30.
    • (2010) Methods Mol Biol , vol.634 , pp. 421-430
    • Tischer, B.K.1    Smith, G.A.2    Osterrieder, N.3
  • 54
    • 4344700840 scopus 로고    scopus 로고
    • Evidence for separate binding and scaffolding domains in the immunosuppressive and antitumor marine natural product, pateamine A: design, synthesis, and activity studies leading to a potent simplified derivative
    • Romo D, Choi NS, Li S, Buchler I, Shi Z, Liu JO. 2004. Evidence for separate binding and scaffolding domains in the immunosuppressive and antitumor marine natural product, pateamine A: design, synthesis, and activity studies leading to a potent simplified derivative. J Am Chem Soc 126:10582-10588. http://dx.doi.org/10.1021/ja040065s.
    • (2004) J Am Chem Soc , vol.126 , pp. 10582-10588
    • Romo, D.1    Choi, N.S.2    Li, S.3    Buchler, I.4    Shi, Z.5    Liu, J.O.6
  • 55
    • 73949121101 scopus 로고    scopus 로고
    • Analysis of filamentous process induction and nuclear localization properties of the HSV-2 serine/threonine kinase Us3
    • Finnen RL, Roy BB, Zhang H, Banfield BW. 2010. Analysis of filamentous process induction and nuclear localization properties of the HSV-2 serine/threonine kinase Us3. Virology 397:23-33. http://dx.doi.org/10 .1016/j.virol.2009.11.012.
    • (2010) Virology , vol.397 , pp. 23-33
    • Finnen, R.L.1    Roy, B.B.2    Zhang, H.3    Banfield, B.W.4
  • 56
    • 0037302298 scopus 로고    scopus 로고
    • A subpopulation of tegument protein vhs localizes to detergent-insoluble lipid rafts in herpes simplex virus-infected cells
    • Lee GE, Church GA, Wilson DW. 2003. A subpopulation of tegument protein vhs localizes to detergent-insoluble lipid rafts in herpes simplex virus-infected cells. J Virol 77:2038-2045. http://dx.doi.org/10.1128/JVI .77.3.2038-2045.2003.
    • (2003) J Virol , vol.77 , pp. 2038-2045
    • Lee, G.E.1    Church, G.A.2    Wilson, D.W.3
  • 57
    • 0037225958 scopus 로고    scopus 로고
    • The attenuated pseudorabies virus strain Bartha fails to package the tegument proteins Us3 and VP22
    • Lyman MG, Demmin GL, Banfield BW. 2003. The attenuated pseudorabies virus strain Bartha fails to package the tegument proteins Us3 and VP22. J Virol 77:1403-1414. http://dx.doi.org/10.1128/JVI.77.2 .1403-1414.2003.
    • (2003) J Virol , vol.77 , pp. 1403-1414
    • Lyman, M.G.1    Demmin, G.L.2    Banfield, B.W.3
  • 58
    • 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. 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
  • 59
    • 33845597429 scopus 로고    scopus 로고
    • RNA-mediated sequestration of the RNA helicase eIF4A by pateamine A inhibits translation initiation
    • Bordeleau ME, Cencic R, Lindqvist L, Oberer M, Northcote P, Wagner G, Pelletier J. 2006. RNA-mediated sequestration of the RNA helicase eIF4A by pateamine A inhibits translation initiation. Chem Biol 13:1287-1295. http://dx.doi.org/10.1016/j.chembiol.2006.10.005.
    • (2006) Chem Biol , vol.13 , pp. 1287-1295
    • Bordeleau, M.E.1    Cencic, R.2    Lindqvist, L.3    Oberer, M.4    Northcote, P.5    Wagner, G.6    Pelletier, J.7
  • 61
    • 28444448743 scopus 로고    scopus 로고
    • Inhibition of eukaryotic translation initiation by the marine natural product pateamine A
    • Low WK, Dang Y, Schneider-Poetsch T, Shi Z, Choi NS, Merrick WC, Romo D, Liu JO. 2005. Inhibition of eukaryotic translation initiation by the marine natural product pateamine A. Mol Cell 20:709-722. http://dx .doi.org/10.1016/j.molcel.2005.10.008.
    • (2005) Mol Cell , vol.20 , pp. 709-722
    • Low, W.K.1    Dang, Y.2    Schneider-Poetsch, T.3    Shi, Z.4    Choi, N.S.5    Merrick, W.C.6    Romo, D.7    Liu, J.O.8
  • 63
    • 84873537120 scopus 로고    scopus 로고
    • Relationship of GW/P-bodies with stress granules
    • Stoecklin G, Kedersha N. 2013. Relationship of GW/P-bodies with stress granules. Adv Exp Med Biol 768:197-211. http://dx.doi.org/10.1007/978-1-4614-5107-5_12.
    • (2013) Adv Exp Med Biol , vol.768 , pp. 197-211
    • Stoecklin, G.1    Kedersha, N.2
  • 65
    • 0037370618 scopus 로고    scopus 로고
    • A single amino acid substitution in herpes simplex virus type 1 VP16 inhibits binding to the virion host shutoff protein and is incompatible with virus growth
    • Knez J, Bilan PT, Capone JP. 2003. A single amino acid substitution in herpes simplex virus type 1 VP16 inhibits binding to the virion host shutoff protein and is incompatible with virus growth. J Virol 77:2892-2902. http://dx.doi.org/10.1128/JVI.77.5.2892-2902.2003.
    • (2003) J Virol , vol.77 , pp. 2892-2902
    • Knez, J.1    Bilan, P.T.2    Capone, J.P.3
  • 66
    • 0029876445 scopus 로고    scopus 로고
    • Herpes simplex virus VP16 rescues viral mRNA from destruction by the virion host shutoff function
    • Lam Q, Smibert CA, Koop KE, Lavery C, Capone JP, Weinheimer SP, Smiley JR. 1996. Herpes simplex virus VP16 rescues viral mRNA from destruction by the virion host shutoff function. EMBO J 15:2575-2581.
    • (1996) EMBO J , vol.15 , pp. 2575-2581
    • Lam, Q.1    Smibert, C.A.2    Koop, K.E.3    Lavery, C.4    Capone, J.P.5    Weinheimer, S.P.6    Smiley, J.R.7
  • 67
    • 0028289280 scopus 로고
    • Herpes simplex virus VP16 forms a complex with the virion host shutoff protein vhs
    • Smibert CA, Popova B, Xiao P, Capone JP, Smiley JR. 1994. Herpes simplex virus VP16 forms a complex with the virion host shutoff protein vhs. J Virol 68:2339-2346.
    • (1994) J Virol , vol.68 , pp. 2339-2346
    • Smibert, C.A.1    Popova, B.2    Xiao, P.3    Capone, J.P.4    Smiley, J.R.5
  • 68
    • 35148822236 scopus 로고    scopus 로고
    • Replication-competent herpes simplex virus 1 isolates selected from cells transfected with a bacterial artificial chromosomeDNA lacking only the UL49 gene vary with respect to the defect in the UL41 gene encoding host shutoff RNase
    • Sciortino MT, Taddeo B, Giuffre-Cuculletto M, Medici MA, Mastino A, Roizman B. 2007. Replication-competent herpes simplex virus 1 isolates selected from cells transfected with a bacterial artificial chromosomeDNA lacking only the UL49 gene vary with respect to the defect in the UL41 gene encoding host shutoff RNase. J Virol 81:10924-10932. http://dx.doi.org /10.1128/JVI.01239-07.
    • (2007) J Virol , vol.81 , pp. 10924-10932
    • Sciortino, M.T.1    Taddeo, B.2    Giuffre-Cuculletto, M.3    Medici, M.A.4    Mastino, A.5    Roizman, B.6
  • 69
    • 0036168638 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 U(S)11 protein interacts with protein kinase R in infected cells and requires a 30-amino-acid sequence adjacent to a kinase substrate domain
    • Cassady KA, Gross M. 2002. The herpes simplex virus type 1 U(S)11 protein interacts with protein kinase R in infected cells and requires a 30-amino-acid sequence adjacent to a kinase substrate domain. J Virol 76:2029-2035. http://dx.doi.org/10.1128/jvi.76.5.2029-2035.2002.
    • (2002) J Virol , vol.76 , pp. 2029-2035
    • Cassady, K.A.1    Gross, M.2
  • 70
    • 0031710037 scopus 로고    scopus 로고
    • The herpes simplex virus US11 protein effectively compensates for the gamma1(34.5) gene if present before activation of protein kinase R by precluding its phosphorylation and that of the alpha subunit of eukaryotic translation initiation factor 2
    • Cassady KA, Gross M, Roizman B. 1998. The herpes simplex virus US11 protein effectively compensates for the gamma1(34.5) gene if present before activation of protein kinase R by precluding its phosphorylation and that of the alpha subunit of eukaryotic translation initiation factor 2. J Virol 72:8620-8626.
    • (1998) J Virol , vol.72 , pp. 8620-8626
    • Cassady, K.A.1    Gross, M.2    Roizman, B.3
  • 71
    • 33947428335 scopus 로고    scopus 로고
    • Maintenance of endoplasmic reticulum (ER) homeostasis in herpes simplex virus type 1-infected cells through the association of a viral glycoprotein with PERK, a cellular ER stress sensor
    • Mulvey M, Arias C, Mohr I. 2007. Maintenance of endoplasmic reticulum (ER) homeostasis in herpes simplex virus type 1-infected cells through the association of a viral glycoprotein with PERK, a cellular ER stress sensor. J Virol 81:3377-3390. http://dx.doi.org/10.1128/ JVI.02191-06.
    • (2007) J Virol , vol.81 , pp. 3377-3390
    • Mulvey, M.1    Arias, C.2    Mohr, I.3
  • 72
    • 0031017382 scopus 로고    scopus 로고
    • The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNAactivated protein kinase
    • He B, Gross M, Roizman B. 1997. The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNAactivated protein kinase. Proc Natl Acad Sci U S A 94:843-848. http://dx .doi.org/10.1073/pnas.94.3.843.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 843-848
    • He, B.1    Gross, M.2    Roizman, B.3
  • 73
    • 84930892539 scopus 로고    scopus 로고
    • Timing is everything: coordinated control of host shutoff by influenzaAvirus NS1 and PA-X proteins
    • Khaperskyy DA, McCormick C. 2015. Timing is everything: coordinated control of host shutoff by influenzaAvirus NS1 and PA-X proteins. J Virol 89:6528-6531. http://dx.doi.org/10.1128/JVI.00386-15.
    • (2015) J Virol , vol.89 , pp. 6528-6531
    • Khaperskyy, D.A.1    McCormick, C.2
  • 74
    • 3543058093 scopus 로고    scopus 로고
    • Herpes simplex virus 1 induces cytoplasmic accumulation of TIA-1/TIAR and both synthesis and cytoplasmic accumulation of tristetraprolin, two cellular proteins that bind and destabilize AU-rich RNAs
    • Esclatine A, Taddeo B, Roizman B. 2004. Herpes simplex virus 1 induces cytoplasmic accumulation of TIA-1/TIAR and both synthesis and cytoplasmic accumulation of tristetraprolin, two cellular proteins that bind and destabilize AU-rich RNAs. J Virol 78:8582-8592. http://dx.doi.org/10 .1128/JVI.78.16.8582-8592.2004.
    • (2004) J Virol , vol.78 , pp. 8582-8592
    • Esclatine, A.1    Taddeo, B.2    Roizman, B.3
  • 75
    • 84975322626 scopus 로고    scopus 로고
    • The herpes simplex virus virion host shutoff protein enhances translation of viral true late mRNAs independently of suppressing protein kinase R and stress granule formation
    • Dauber B, Poon D, Dos Santos T, Duguay BA, Mehta N, Saffran HA, Smiley JR. 2016. The herpes simplex virus virion host shutoff protein enhances translation of viral true late mRNAs independently of suppressing protein kinase R and stress granule formation. J Virol 90:6049-6057. http://dx.doi.org/10.1128/JVI.03180-15.
    • (2016) J Virol , vol.90 , pp. 6049-6057
    • Dauber, B.1    Poon, D.2    Dos Santos, T.3    Duguay, B.A.4    Mehta, N.5    Saffran, H.A.6    Smiley, J.R.7
  • 78
    • 84928787115 scopus 로고    scopus 로고
    • Stress granules regulate double-stranded RNAdependent protein kinase activation through a complex containing G3BP1 and Caprin1
    • Reineke LC, Kedersha N, Langereis MA, van Kuppeveld FJ, Lloyd RE. 2015. Stress granules regulate double-stranded RNAdependent protein kinase activation through a complex containing G3BP1 and Caprin1. mBio 6:e02486. http://dx.doi.org/10.1128/mBio .02486-14.
    • (2015) mBio , vol.6
    • Reineke, L.C.1    Kedersha, N.2    Langereis, M.A.3    van Kuppeveld, F.J.4    Lloyd, R.E.5
  • 79
    • 84923066571 scopus 로고    scopus 로고
    • The stress granule protein G3BP1 recruits protein kinase R to promote multiple innate immune antiviral responses
    • Reineke LC, Lloyd RE. 2015. The stress granule protein G3BP1 recruits protein kinase R to promote multiple innate immune antiviral responses. J Virol 89:2575-2589. http://dx.doi.org/10.1128/JVI.02791-14.
    • (2015) J Virol , vol.89 , pp. 2575-2589
    • Reineke, L.C.1    Lloyd, R.E.2
  • 80
    • 84922520038 scopus 로고    scopus 로고
    • Antiviral innate immunity and stress granule responses
    • Onomoto K, Yoneyama M, Fung G, Kato H, Fujita T. 2014. Antiviral innate immunity and stress granule responses. Trends Immunol 35:420-428. http://dx.doi.org/10.1016/j.it.2014.07.006.
    • (2014) Trends Immunol , vol.35 , pp. 420-428
    • Onomoto, K.1    Yoneyama, M.2    Fung, G.3    Kato, H.4    Fujita, T.5

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.