메뉴 건너뛰기




Volumn 87, Issue 1, 2013, Pages 94-109

mRNA decay during herpes simplex virus (HSV) infections: Mutations that affect translation of an mRNA influence the sites at which it is cleaved by the HSV virion host shutoff (Vhs) protein

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DNA; MESSENGER RNA; THYMIDINE KINASE; UNCLASSIFIED DRUG; VIRION HOST SHUTOFF PROTEIN; VIRUS PROTEIN;

EID: 84871948027     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01557-12     Document Type: Article
Times cited : (29)

References (140)
  • 1
    • 34249950342 scopus 로고    scopus 로고
    • Herpes simplex viruses
    • Knipe DM, Howley PM, Griffin DE, Martin MA, Lamb RA, Roizman B, Straus SE (ed), Fields virology, 5th ed, Lippincott Williams & Wilkins, Philadelphia, PA
    • Roizman B, Knipe DM, Whitley RJ. 2007. Herpes simplex viruses, p 2501-2601. In Knipe DM, Howley PM, Griffin DE, Martin MA, Lamb RA, Roizman B, Straus SE (ed), Fields virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) , pp. 2501-2601
    • Roizman, B.1    Knipe, D.M.2    Whitley, R.J.3
  • 2
    • 84929297526 scopus 로고    scopus 로고
    • Initiation of transcription and RNA synthesis, processing and transport in HSV and VZV infected cells. In Arvin A, Campadelli-Fiume G, Mocarski E, Moore PS, Roizman B, Whitley R, Yamanishi K (ed)
    • Cambridge University Press, Cambridge, United Kingdom
    • Sandri-Goldin RM. 2007. Initiation of transcription and RNA synthesis, processing and transport in HSV and VZV infected cells. In Arvin A, Campadelli-Fiume G, Mocarski E, Moore PS, Roizman B, Whitley R, Yamanishi K (ed), Human herpesviruses: biology, therapy, and immunoprophylaxis. Cambridge University Press, Cambridge, United Kingdom. http://www.ncbi.nlm.nih.gov/books/NBK47363/.
    • (2007) Human herpesviruses: biology, therapy, and immunoprophylaxis
    • Sandri-goldin, R.M.1
  • 3
    • 79955374737 scopus 로고    scopus 로고
    • Activities of ICP0 involved in the reversal of silencing of quiescent herpes simplex virus 1.
    • Ferenczy MW, Ranayhossaini DJ, DeLuca NA. 2011. Activities of ICP0 involved in the reversal of silencing of quiescent herpes simplex virus 1. J. Virol. 85:4993-5002.
    • (2011) J. Virol. , vol.85 , pp. 4993-5002
    • Ferenczy, M.W.1    Ranayhossaini, D.J.2    Deluca, N.A.3
  • 4
    • 52649115135 scopus 로고    scopus 로고
    • Early events pre-initiation of alphaherpes viral gene expression. In Arvin A, Campadelli-Fiume G, Mocarski E, Moore PS, Roizman B, Whitley R, Yamanishi K (ed)
    • Cambridge University Press, Cambridge, United Kingdom
    • Kristie TM. 2007. Early events pre-initiation of alphaherpes viral gene expression. In Arvin A, Campadelli-Fiume G, Mocarski E, Moore PS, Roizman B, Whitley R, Yamanishi K (ed), Human herpesviruses: biology, therapy, and immunoprophylaxis. Cambridge University Press, Cambridge, United Kingdom. http://www.ncbi.nlm.nih.gov/books/NBK47386/.
    • (2007) Human herpesviruses: biology, therapy, and immunoprophylaxis
    • Kristie, T.M.1
  • 5
    • 79958102996 scopus 로고    scopus 로고
    • Herpes simplex virus 1 ICP4 forms complexes with TFIID and mediator in virus-infected cells.
    • Lester JT, DeLuca NA. 2011. Herpes simplex virus 1 ICP4 forms complexes with TFIID and mediator in virus-infected cells. J. Virol. 85:5733- 5744.
    • (2011) J. Virol. , vol.85 , pp. 5733-5744
    • Lester, J.T.1    Deluca, N.A.2
  • 6
    • 39749144518 scopus 로고    scopus 로고
    • Binding of ICP4, TATA-binding protein, and RNA polymerase II to herpes simplex virus type 1 immediate-early, early, and late promoters in virus-infected cells
    • Sampath P, DeLuca NA. 2008. Binding of ICP4, TATA-binding protein, and RNA polymerase II to herpes simplex virus type 1 immediate-early, early, and late promoters in virus-infected cells. J. Virol. 82:2339 -2349.
    • (2008) J. Virol. , vol.82 , pp. 2339-2349
    • Sampath, P.1    Deluca, N.A.2
  • 7
    • 2642548884 scopus 로고    scopus 로고
    • Differential cellular requirements for activation of herpes simplex virus type 1 early (tk) and late (gC) promoters by ICP4.
    • Zabierowski S, DeLuca NA. 2004. Differential cellular requirements for activation of herpes simplex virus type 1 early (tk) and late (gC) promoters by ICP4. J. Virol. 78:6162- 6170.
    • (2004) J. Virol. , vol.78 , pp. 6162-6170
    • Zabierowski, S.1    Deluca, N.A.2
  • 8
    • 41149156363 scopus 로고    scopus 로고
    • Stabilized binding of TBP to the TATA box of herpes simplex virus type 1 early (tk) and late (gC) promoters by TFIIA and ICP4.
    • Zabierowski SE, DeLuca NA. 2008. Stabilized binding of TBP to the TATA box of herpes simplex virus type 1 early (tk) and late (gC) promoters by TFIIA and ICP4. J. Virol. 82:3546 -3554.
    • (2008) J. Virol. , vol.82 , pp. 3546-3554
    • Zabierowski, S.E.1    Deluca, N.A.2
  • 9
    • 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
  • 10
    • 0027978459 scopus 로고
    • Properties of an HSV-1 regulatory protein that appears to impair host cell splicing
    • Sandri-Goldin RM. 1994. Properties of an HSV-1 regulatory protein that appears to impair host cell splicing. Infect. Agents Dis. 3:59-67.
    • (1994) Infect. Agents Dis. , vol.3 , pp. 59-67
    • Sandri-goldin, R.M.1
  • 11
    • 0031731263 scopus 로고    scopus 로고
    • Interactions between a herpes simplex virus regulatory protein and cellular mRNA processing pathways
    • Sandri-Goldin RM. 1998. Interactions between a herpes simplex virus regulatory protein and cellular mRNA processing pathways. Methods 16:95-104.
    • (1998) Methods , vol.16 , pp. 95-104
    • Sandri-goldin, R.M.1
  • 12
    • 0037387122 scopus 로고    scopus 로고
    • ICP27 interacts with SRPK1 to mediate HSV splicing inhibition by altering SR protein phosphorylation
    • Sciabica KS, Dai QJ, Sandri-Goldin RM. 2003. ICP27 interacts with SRPK1 to mediate HSV splicing inhibition by altering SR protein phosphorylation. EMBO J. 22:1608 -1619.
    • (2003) EMBO J. , vol.22 , pp. 1608-1619
    • Sciabica, K.S.1    Dai, Q.J.2    Sandri-goldin, R.M.3
  • 13
    • 0036892520 scopus 로고    scopus 로고
    • ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway
    • Chen IH, Sciabica KS, Sandri-Goldin RM. 2002. ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway. J. Virol. 76:12877-12889.
    • (2002) J. Virol. , vol.76 , pp. 12877-12889
    • Chen, I.H.1    Sciabica, K.S.2    Sandri-goldin, R.M.3
  • 14
    • 77649196687 scopus 로고    scopus 로고
    • ICP27 phosphorylation site mutants display altered functional interactions with cellular export factors Aly/REF and TAP/NXF1 but are able to bind herpes simplex virus 1 RNA
    • Corbin-Lickfett KA, Rojas S, Li L, Cocco MJ, Sandri-Goldin RM. 2010. ICP27 phosphorylation site mutants display altered functional interactions with cellular export factors Aly/REF and TAP/NXF1 but are able to bind herpes simplex virus 1 RNA. J. Virol. 84:2212-2222.
    • (2010) J. Virol. , vol.84 , pp. 2212-2222
    • Corbin-lickfett, K.A.1    Rojas, S.2    Li, L.3    Cocco, M.J.4    Sandri-goldin, R.M.5
  • 15
    • 77953313233 scopus 로고    scopus 로고
    • Three arginine residues within the RGG box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export
    • Corbin-Lickfett KA, Souki SK, Cocco MJ, Sandri-Goldin RM. 2010. Three arginine residues within the RGG box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export. J. Virol. 84:6367- 6376.
    • (2010) J. Virol. , vol.84 , pp. 6367-6376
    • Corbin-lickfett, K.A.1    Souki, S.K.2    Cocco, M.J.3    Sandri-goldin, R.M.4
  • 16
    • 79952144800 scopus 로고    scopus 로고
    • Head-to-tail intramolecular interaction of herpes simplex virus type 1 regulatory protein ICP27 is important for its interaction with cellular mRNA export receptor TAP/ NXF1
    • doi:10.1128/mBio.00268-310
    • Hernandez FP, Sandri-Goldin RM. 2010. Head-to-tail intramolecular interaction of herpes simplex virus type 1 regulatory protein ICP27 is important for its interaction with cellular mRNA export receptor TAP/ NXF1. mBio 1:e00268 -10. doi:10.1128/mBio.00268-310.
    • (2010) mBio , vol.1
    • Hernandez, F.P.1    Sandri-goldin, R.M.2
  • 17
    • 67449086121 scopus 로고    scopus 로고
    • The cellular RNA export receptor TAP/NXF1 is required for ICP27-mediated export of herpes simplex virus 1 RNA, but the TREX complex adaptor protein Aly/REF appears to be dispensable
    • Johnson LA, Li L, Sandri-Goldin RM. 2009. The cellular RNA export receptor TAP/NXF1 is required for ICP27-mediated export of herpes simplex virus 1 RNA, but the TREX complex adaptor protein Aly/REF appears to be dispensable. J. Virol. 83:6335- 6346.
    • (2009) J. Virol. , vol.83 , pp. 6335-6346
    • Johnson, L.A.1    Li, L.2    Sandri-goldin, R.M.3
  • 18
    • 59749101894 scopus 로고    scopus 로고
    • Efficient nuclear export of herpes simplex virus 1 transcripts requires both RNA binding by ICP27 and ICP27 interaction with TAP/NXF1
    • Johnson LA, Sandri-Goldin RM. 2009. Efficient nuclear export of herpes simplex virus 1 transcripts requires both RNA binding by ICP27 and ICP27 interaction with TAP/NXF1. J. Virol. 83:1184 -1192.
    • (2009) J. Virol. , vol.83 , pp. 1184-1192
    • Johnson, L.A.1    Sandri-goldin, R.M.2
  • 20
    • 9944257747 scopus 로고    scopus 로고
    • Viral regulation of mRNA export
    • Sandri-Goldin RM. 2004. Viral regulation of mRNA export. J. Virol. 78:4389-4396.
    • (2004) J. Virol. , vol.78 , pp. 4389-4396
    • Sandri-goldin, R.M.1
  • 21
    • 79959965814 scopus 로고    scopus 로고
    • A herpesvirus kinase that masquerades as Akt: you don't have to look like Akt, to act like it
    • Chuluunbaatar U, Mohr I. 2011. A herpesvirus kinase that masquerades as Akt: you don't have to look like Akt, to act like it. Cell Cycle 10:2064- 2068.
    • (2011) Cell Cycle , vol.10 , pp. 2064-2068
    • Chuluunbaatar, U.1    Mohr, I.2
  • 22
    • 78649857803 scopus 로고    scopus 로고
    • Constitutive mTORC1 activation by a herpesvirus Akt surrogate stimulates mRNA translation and viral replication
    • Chuluunbaatar U, Roller R, Feldman ME, Brown S, Shokat KM, Mohr I. 2010. Constitutive mTORC1 activation by a herpesvirus Akt surrogate stimulates mRNA translation and viral replication. Genes Dev. 24:2627- 2639.
    • (2010) Genes Dev. , vol.24 , pp. 2627-2639
    • Chuluunbaatar, U.1    Roller, R.2    Feldman, M.E.3    Brown, S.4    Shokat, K.M.5    Mohr, I.6
  • 23
    • 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.
    • (2011) J. Virol. , vol.85 , pp. 5363-5373
    • Dauber, B.1    Pelletier, J.2    Smiley, J.R.3
  • 24
    • 15244345883 scopus 로고    scopus 로고
    • Control of VP16 translation by the herpes simplex virus type 1 immediate-early protein ICP27
    • Ellison KS, Maranchuk RA, Mottet KL, Smiley JR. 2005. Control of VP16 translation by the herpes simplex virus type 1 immediate-early protein ICP27. J. Virol. 79:4120-4131.
    • (2005) J. Virol. , vol.79 , pp. 4120-4131
    • Ellison, K.S.1    Maranchuk, R.A.2    Mottet, K.L.3    Smiley, J.R.4
  • 25
    • 32644446560 scopus 로고    scopus 로고
    • Phosphorylation and dephosphorylation events that regulate viral mRNA translation
    • Mohr I. 2006. Phosphorylation and dephosphorylation events that regulate viral mRNA translation. Virus Res. 119:89 -99.
    • (2006) Virus Res. , vol.119 , pp. 89-99
    • Mohr, I.1
  • 26
    • 33746214712 scopus 로고    scopus 로고
    • Resistance of mRNA translation to acute endoplasmic reticulum stress-inducing agents in herpes simplex virus type 1-infected cells requires multiple virus-encoded functions
    • Mulvey M, Arias C, Mohr I. 2006. Resistance of mRNA translation to acute endoplasmic reticulum stress-inducing agents in herpes simplex virus type 1-infected cells requires multiple virus-encoded functions. J. Virol. 80:7354 -7363.
    • (2006) J. Virol. , vol.80 , pp. 7354-7363
    • Mulvey, M.1    Arias, C.2    Mohr, I.3
  • 27
    • 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.
    • (2007) J. Virol. , vol.81 , pp. 3377-3390
    • Mulvey, M.1    Arias, C.2    Mohr, I.3
  • 28
    • 0141566327 scopus 로고    scopus 로고
    • Regulation of eIF2alpha phosphorylation by different functions that act during discrete phases in the herpes simplex virus type 1 life cycle
    • Mulvey M, Poppers J, Sternberg D, Mohr I. 2003. Regulation of eIF2alpha phosphorylation by different functions that act during discrete phases in the herpes simplex virus type 1 life cycle. J. Virol. 77:10917- 10928.
    • (2003) J. Virol. , vol.77 , pp. 10917-10928
    • Mulvey, M.1    Poppers, J.2    Sternberg, D.3    Mohr, I.4
  • 29
    • 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.
    • (2010) J. Virol. , vol.84 , pp. 6041-6049
    • Saffran, H.A.1    Read, G.S.2    Smiley, J.R.3
  • 30
    • 1842831274 scopus 로고    scopus 로고
    • Phosphorylation of eIF4E by Mnk-1 enhances HSV-1 translation and replication in quiescent cells
    • Walsh D, Mohr I. 2004. Phosphorylation of eIF4E by Mnk-1 enhances HSV-1 translation and replication in quiescent cells. Genes Dev. 18:660- 672.
    • (2004) Genes Dev. , vol.18 , pp. 660-672
    • Walsh, D.1    Mohr, I.2
  • 31
    • 32644444260 scopus 로고    scopus 로고
    • Assembly of an active translation initiation factor complex by a viral protein
    • Walsh D, Mohr I. 2006. Assembly of an active translation initiation factor complex by a viral protein. Genes Dev. 20:461- 472.
    • (2006) Genes Dev. , vol.20 , pp. 461-472
    • Walsh, D.1    Mohr, I.2
  • 32
    • 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.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 860-875
    • Walsh, D.1    Mohr, I.2
  • 33
    • 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.
    • (2002) J. Virol. , vol.76 , pp. 8560-8571
    • Everly Jr., D.N.1    Feng, P.2    Mian, I.S.3    Read, G.S.4
  • 34
    • 0034796322 scopus 로고    scopus 로고
    • mRNA decay during herpesvirus infections: interaction between a putative viral nuclease and a cellular translation factor
    • Feng P, Everly DN, Jr. , Read GS. 2001. mRNA decay during herpesvirus infections: interaction between a putative viral nuclease and a cellular translation factor. J. Virol. 75:10272-10280.
    • (2001) J. Virol. , vol.75 , pp. 10272-10280
    • Feng, P.1    Everly Jr., D.N.2    Read, G.S.3
  • 35
    • 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.
    • (2005) J. Virol. , vol.79 , pp. 9651-9664
    • Feng, P.1    Everly Jr., D.N.2    Read, G.S.3
  • 36
    • 0023108018 scopus 로고
    • A mutant of herpes simplex virus type 1 exhibits increased stability of immediate-early (alpha) mRNAs
    • Oroskar AA, Read GS. 1987. A mutant of herpes simplex virus type 1 exhibits increased stability of immediate-early (alpha) mRNAs. J. Virol. 61:604-606.
    • (1987) J. Virol. , vol.61 , pp. 604-606
    • Oroskar, A.A.1    Read, G.S.2
  • 37
    • 0024521222 scopus 로고
    • Control of mRNA stability by the virion host shutoff function of herpes simplex virus
    • Oroskar AA, Read GS. 1989. Control of mRNA stability by the virion host shutoff function of herpes simplex virus. J. Virol. 63:1897-1906.
    • (1989) J. Virol. , vol.63 , pp. 1897-1906
    • Oroskar, A.A.1    Read, G.S.2
  • 38
    • 0001798701 scopus 로고    scopus 로고
    • Control of mRNA stability during herpes simplex virus infections
    • Harford JB, Morris DR (ed), mRNA metabolism and post-transcriptional gene regulation, 1st ed, Wiley-Liss, Inc., New York, NY
    • Read GS. 1997. Control of mRNA stability during herpes simplex virus infections, p 311-321. In Harford JB, Morris DR (ed), mRNA metabolism and post-transcriptional gene regulation, 1st ed, vol 17. Wiley-Liss, Inc., New York, NY.
    • (1997) , vol.17 , pp. 311-321
    • Read, G.S.1
  • 39
    • 45749139207 scopus 로고    scopus 로고
    • Small interfering RNAs that deplete the cellular translation factor eIF4H impede mRNA degradation by the virion host shutoff protein of herpes simplex virus
    • Sarma N, Agarwal D, Shiflett LA, Read GS. 2008. Small interfering RNAs that deplete the cellular translation factor eIF4H impede mRNA degradation by the virion host shutoff protein of herpes simplex virus. J. Virol. 82:6600-6609.
    • (2008) J. Virol. , vol.82 , pp. 6600-6609
    • Sarma, N.1    Agarwal, D.2    Shiflett, L.A.3    Read, G.S.4
  • 40
    • 0022178431 scopus 로고
    • Degradation of cellular mRNAs induced by a virion-associated factor during herpes simplex virus infection of Vero cells
    • Schek N, Bachenheimer SL. 1985. Degradation of cellular mRNAs induced by a virion-associated factor during herpes simplex virus infection of Vero cells. J. Virol. 55:601- 610.
    • (1985) J. Virol. , vol.55 , pp. 601-610
    • Schek, N.1    Bachenheimer, S.L.2
  • 41
    • 0346373732 scopus 로고    scopus 로고
    • Herpes simplex virus virion host shutoff protein: immune evasion mediated by a viral RNase? J
    • Smiley JR. 2004. Herpes simplex virus virion host shutoff protein: immune evasion mediated by a viral RNase? J. Virol. 78:1063-1068.
    • (2004) Virol. , vol.78 , pp. 1063-1068
    • Smiley, J.R.1
  • 42
    • 0023182175 scopus 로고
    • Effects of herpes simplex virus on mRNA stability
    • Strom T, Frenkel N. 1987. Effects of herpes simplex virus on mRNA stability. J. Virol. 61:2198 -2207.
    • (1987) J. Virol. , vol.61 , pp. 2198-2207
    • Strom, T.1    Frenkel, N.2
  • 43
    • 0037168545 scopus 로고    scopus 로고
    • The patterns of accumulation of cellular RNAs in cells infected with a wild-type and a mutant herpes simplex virus 1 lacking the virion host shutoff gene
    • Taddeo B, Esclatine A, Roizman B. 2002. The patterns of accumulation of cellular RNAs in cells infected with a wild-type and a mutant herpes simplex virus 1 lacking the virion host shutoff gene. Proc. Natl. Acad. Sci. U. S. A. 99:17031-17036.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 17031-17036
    • Taddeo, B.1    Esclatine, A.2    Roizman, B.3
  • 44
    • 0032864835 scopus 로고    scopus 로고
    • The herpes simplex virus vhs protein induces endoribonucleolytic cleavage of target RNAs in cell extracts
    • Elgadi MM, Hayes CE, Smiley JR. 1999. The herpes simplex virus vhs protein induces endoribonucleolytic cleavage of target RNAs in cell extracts. J. Virol. 73:7153-7164.
    • (1999) J. Virol. , vol.73 , pp. 7153-7164
    • Elgadi, M.M.1    Hayes, C.E.2    Smiley, J.R.3
  • 45
    • 33748511878 scopus 로고    scopus 로고
    • The virion host shutoff protein (UL41) of herpes simplex virus 1 is an endoribonuclease with a substrate specificity similar to that of RNase A
    • Taddeo B, Roizman B. 2006. The virion host shutoff protein (UL41) of herpes simplex virus 1 is an endoribonuclease with a substrate specificity similar to that of RNase A. J. Virol. 80:9341-9345.
    • (2006) J. Virol. , vol.80 , pp. 9341-9345
    • Taddeo, B.1    Roizman, B.2
  • 46
    • 33644552729 scopus 로고    scopus 로고
    • The U(L)41 protein of herpes simplex virus 1 degrades RNA by endonucleolytic cleavage in absence of other cellular or viral proteins
    • Taddeo B, Zhang W, Roizman B. 2006. The U(L)41 protein of herpes simplex virus 1 degrades RNA by endonucleolytic cleavage in absence of other cellular or viral proteins. Proc. Natl. Acad. Sci. U. S. A. 103:2827- 2832.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 2827-2832
    • Taddeo, B.1    Zhang, W.2    Roizman, B.3
  • 47
    • 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
  • 48
    • 0027420465 scopus 로고
    • Isolation of a herpes simplex virus type 1 mutant with a deletion in the virion host shutoff gene and identification of multiple forms of the vhs (UL41) polypeptide
    • Read GS, Karr BM, Knight K. 1993. Isolation of a herpes simplex virus type 1 mutant with a deletion in the virion host shutoff gene and identification of multiple forms of the vhs (UL41) polypeptide. J. Virol. 67: 7149-7160.
    • (1993) J. Virol. , vol.67 , pp. 7149-7160
    • Read, G.S.1    Karr, B.M.2    Knight, K.3
  • 49
    • 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.
    • (2007) J. Virol. , vol.81 , pp. 1148-1161
    • Read, G.S.1    Patterson, M.2
  • 50
    • 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.
    • (1992) J. Gen. Virol. , vol.73 , pp. 467-470
    • Smibert, C.A.1    Johnson, D.C.2    Smiley, J.R.3
  • 51
    • 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.
    • (1990) J. Gen. Virol. , vol.71 , pp. 1387-1390
    • Everett, R.D.1    Fenwick, M.L.2
  • 52
    • 0000523828 scopus 로고
    • The effects of herpesviruses on cellular macromolecular synthesis
    • In Fraenkel-Conrat H, Wagner RR (ed), Plenum Publishing Corp., New York, NY
    • Fenwick ML. 1984. The effects of herpesviruses on cellular macromolecular synthesis, p 359-390. In Fraenkel-Conrat H, Wagner RR (ed), Comprehensive virology, vol 19. Plenum Publishing Corp., New York, NY.
    • (1984) Comprehensive virology , vol.19 , pp. 359-390
    • Fenwick, M.L.1
  • 53
    • 0025651655 scopus 로고
    • Inactivation of the shutoff gene (UL41) of herpes simplex virus types 1 and 2
    • Fenwick ML, Everett RD. 1990. Inactivation of the shutoff gene (UL41) of herpes simplex virus types 1 and 2. J. Gen. Virol. 71, 2961-2967.
    • (1990) J. Gen. Virol. , vol.71 , pp. 2961-2967
    • Fenwick, M.L.1    Everett, R.D.2
  • 54
    • 0025058827 scopus 로고
    • Transfer of UL41, the gene controlling virion-associated host cell shutoff, between different strains of herpes simplex virus
    • Fenwick ML, Everett RD. 1990. Transfer of UL41, the gene controlling virion-associated host cell shutoff, between different strains of herpes simplex virus. J. Gen. Virol. 71:411- 418.
    • (1990) J. Gen. Virol. , vol.71 , pp. 411-418
    • Fenwick, M.L.1    Everett, R.D.2
  • 55
    • 0021139610 scopus 로고
    • Early virion-associated suppression of cellular protein synthesis by herpes simplex virus is accompanied by inactivation of mRNA
    • Fenwick ML, McMenamin MM. 1984. Early virion-associated suppression of cellular protein synthesis by herpes simplex virus is accompanied by inactivation of mRNA. J. Gen. Virol. 65:1225-1228.
    • (1984) J. Gen. Virol. , vol.65 , pp. 1225-1228
    • Fenwick, M.L.1    Mcmenamin, M.M.2
  • 56
    • 0020287593 scopus 로고
    • Early and delayed shut-off of host protein synthesis in cells infected with herpes simplex virus
    • Fenwick ML, Clark J. 1982. Early and delayed shut-off of host protein synthesis in cells infected with herpes simplex virus. J. Gen. Virol. 61: 121-125.
    • (1982) J. Gen. Virol. , vol.61 , pp. 121-125
    • Fenwick, M.L.1    Clark, J.2
  • 57
    • 0020526685 scopus 로고
    • Herpes simplex virus mutants defective in the virion-associated shutoff of host polypeptide synthesis and exhibiting abnormal synthesis of alpha (immediate early) viral polypeptides
    • Read GS, Frenkel N. 1983. Herpes simplex virus mutants defective in the virion-associated shutoff of host polypeptide synthesis and exhibiting abnormal synthesis of alpha (immediate early) viral polypeptides. J. Virol. 46:498 -512.
    • (1983) J. Virol. , vol.46 , pp. 498-512
    • Read, G.S.1    Frenkel, N.2
  • 58
    • 2642604294 scopus 로고
    • Herpes simplex virus-infected cells contain a function(s) that destabilizes both host and viral mRNAs
    • Kwong AD, Frenkel N. 1987. Herpes simplex virus-infected cells contain a function(s) that destabilizes both host and viral mRNAs. Proc. Natl. Acad. Sci. U. S. A. 84:1926 -1930.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 1926-1930
    • Kwong, A.D.1    Frenkel, N.2
  • 59
    • 0024452271 scopus 로고
    • The herpes simplex virus virion host shutoff function
    • Kwong AD, Frenkel N. 1989. The herpes simplex virus virion host shutoff function. J. Virol. 63:4834-4839.
    • (1989) J. Virol. , vol.63 , pp. 4834-4839
    • Kwong, A.D.1    Frenkel, N.2
  • 60
    • 0023866418 scopus 로고
    • Herpes simplex virus virion host shutoff function
    • Kwong AD, Kruper JA, Frenkel N. 1988. Herpes simplex virus virion host shutoff function. J. Virol. 62:912-921.
    • (1988) J. Virol. , vol.62 , pp. 912-921
    • Kwong, A.D.1    Kruper, J.A.2    Frenkel, N.3
  • 61
    • 1942421835 scopus 로고    scopus 로고
    • Herpes simplex virus 2 virion host shutoff protein interferes with type I interferon production and responsiveness
    • Duerst RJ, Morrison LA. 2004. Herpes simplex virus 2 virion host shutoff protein interferes with type I interferon production and responsiveness. Virology 322:158 -167.
    • (2004) Virology , vol.322 , pp. 158-167
    • Duerst, R.J.1    Morrison, L.A.2
  • 62
    • 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.
    • (2008) J. Virol. , vol.82 , pp. 3642-3653
    • Korom, M.1    Wylie, K.M.2    Morrison, L.A.3
  • 63
    • 0041888287 scopus 로고    scopus 로고
    • Herpes simplex virus type 2 virion host shutoff protein regulates alpha/beta interferon but not adaptive immune responses during primary infection in vivo
    • Murphy JA, Duerst RJ, Smith TJ, Morrison LA. 2003. Herpes simplex virus type 2 virion host shutoff protein regulates alpha/beta interferon but not adaptive immune responses during primary infection in vivo. J. Virol. 77:9337-9345.
    • (2003) J. Virol. , vol.77 , pp. 9337-9345
    • Murphy, J.A.1    Duerst, R.J.2    Smith, T.J.3    Morrison, L.A.4
  • 64
    • 60049094356 scopus 로고    scopus 로고
    • Host responses to wild-type and attenuated herpes simplex virus infection in the absence of Stat1
    • Pasieka TJ, Cilloniz C, Lu B, Teal TH, Proll SC, Katze MG, Leib DA. 2009. Host responses to wild-type and attenuated herpes simplex virus infection in the absence of Stat1. J. Virol. 83:2075-2087.
    • (2009) J. Virol. , vol.83 , pp. 2075-2087
    • Pasieka, T.J.1    Cilloniz, C.2    Lu, B.3    Teal, T.H.4    Proll, S.C.5    Katze, M.G.6    Leib, D.A.7
  • 66
    • 44949265437 scopus 로고    scopus 로고
    • Enhanced pathogenesis of an attenuated herpes simplex virus for mice lacking Stat1
    • Pasieka TJ, Lu B, Leib DA. 2008. Enhanced pathogenesis of an attenuated herpes simplex virus for mice lacking Stat1. J. Virol. 82:6052- 6055.
    • (2008) J. Virol. , vol.82 , pp. 6052-6055
    • Pasieka, T.J.1    Lu, B.2    Leib, D.A.3
  • 67
    • 69449088685 scopus 로고    scopus 로고
    • Increased eIF2alpha phosphorylation attenuates replication of herpes simplex virus 2 vhs mutants in mouse embryonic fibroblasts and correlates with reduced accumulation of the PKR antagonist ICP34.5
    • Wylie KM, Schrimpf JE, Morrison LA. 2009. Increased eIF2alpha phosphorylation attenuates replication of herpes simplex virus 2 vhs mutants in mouse embryonic fibroblasts and correlates with reduced accumulation of the PKR antagonist ICP34.5. J. Virol. 83:9151-9162.
    • (2009) J. Virol. , vol.83 , pp. 9151-9162
    • Wylie, K.M.1    Schrimpf, J.E.2    Morrison, L.A.3
  • 68
    • 81255163730 scopus 로고    scopus 로고
    • The virion host shutoff protein of herpes simplex virus 1 blocks the replication-independent activation of NF-kappaB in dendritic cells in the absence of type I interferon signaling
    • Cotter CR, Kim WK, Nguyen ML, Yount JS, Lopez CB, Blaho JA, Moran TM. 2011. The virion host shutoff protein of herpes simplex virus 1 blocks the replication-independent activation of NF-kappaB in dendritic cells in the absence of type I interferon signaling. J. Virol. 85: 12662-12672.
    • (2011) J. Virol. , vol.85 , pp. 12662-12672
    • Cotter, C.R.1    Kim, W.K.2    Nguyen, M.L.3    Yount, J.S.4    Lopez, C.B.5    Blaho, J.A.6    Moran, T.M.7
  • 69
    • 77949534318 scopus 로고    scopus 로고
    • The virion host shut-off (vhs) protein blocks a TLR-independent pathway of herpes simplex virus type 1 recognition in human and mouse dendritic cells
    • doi:10.1371/journal.pone.0008684
    • Cotter CR, Nguyen ML, Yount JS, Lopez CB, Blaho JA, Moran TM. 2010. The virion host shut-off (vhs) protein blocks a TLR-independent pathway of herpes simplex virus type 1 recognition in human and mouse dendritic cells. PLoS One 5:e8684. doi:10.1371/journal.pone.0008684.
    • (2010) PLoS One , vol.5
    • Cotter, C.R.1    Nguyen, M.L.2    Yount, J.S.3    Lopez, C.B.4    Blaho, J.A.5    Moran, T.M.6
  • 70
    • 0037333481 scopus 로고    scopus 로고
    • Deletion of the virion host shutoff protein (vhs) from herpes simplex virus (HSV) relieves the viral block to dendritic cell activation: potential of vhs- HSV vectors for dendritic cell-mediated immunotherapy
    • Samady L, Costigliola E, MacCormac L, McGrath Y, Cleverley S, Lilley CE, Smith J, Latchman DS, Chain B, Coffin RS. 2003. Deletion of the virion host shutoff protein (vhs) from herpes simplex virus (HSV) relieves the viral block to dendritic cell activation: potential of vhs- HSV vectors for dendritic cell-mediated immunotherapy. J. Virol. 77:3768- 3776.
    • (2003) J. Virol. , vol.77 , pp. 3768-3776
    • Samady, L.1    Costigliola, E.2    Maccormac, L.3    Mcgrath, Y.4    Cleverley, S.5    Lilley, C.E.6    Smith, J.7    Latchman, D.S.8    Chain, B.9    Coffin, R.S.10
  • 71
    • 33645980953 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 vhs-UL41 gene secures viral replication by temporarily evading apoptotic cellular response to infection: Vhs-UL41 activity might require interactions with elements of cellular mRNA degradation machinery
    • Barzilai A, Zivony-Elbom I, Sarid R, Noah E, Frenkel N. 2006. The herpes simplex virus type 1 vhs-UL41 gene secures viral replication by temporarily evading apoptotic cellular response to infection: Vhs-UL41 activity might require interactions with elements of cellular mRNA degradation machinery. J. Virol. 80:505-513.
    • (2006) J. Virol. , vol.80 , pp. 505-513
    • Barzilai, A.1    Zivony-elbom, I.2    Sarid, R.3    Noah, E.4    Frenkel, N.5
  • 72
    • 33746210101 scopus 로고    scopus 로고
    • Herpes simplex virus 1 precludes replenishment of the short-lived receptor of tumor necrosis factor alpha by virion host shutoff-dependent degradation of its mRNA
    • Liang L, Roizman B. 2006. Herpes simplex virus 1 precludes replenishment of the short-lived receptor of tumor necrosis factor alpha by virion host shutoff-dependent degradation of its mRNA. J. Virol. 80:7756- 7759.
    • (2006) J. Virol. , vol.80 , pp. 7756-7759
    • Liang, L.1    Roizman, B.2
  • 73
    • 0033919629 scopus 로고    scopus 로고
    • The role of the UL41 gene of herpes simplex virus type 1 in evasion of non-specific host defence mechanisms during primary infection
    • Suzutani T, Nagamine M, Shibaki T, Ogasawara M, Yoshida I, Daikoku T, Nishiyama Y, Azuma M. 2000. The role of the UL41 gene of herpes simplex virus type 1 in evasion of non-specific host defence mechanisms during primary infection. J. Gen. Virol. 81:1763-1771.
    • (2000) J. Gen. Virol. , vol.81 , pp. 1763-1771
    • Suzutani, T.1    Nagamine, M.2    Shibaki, T.3    Ogasawara, M.4    Yoshida, I.5    Daikoku, T.6    Nishiyama, Y.7    Azuma, M.8
  • 74
    • 0029887717 scopus 로고    scopus 로고
    • + CTL clones recognize HSV-2- infected fibroblasts after treatment with IFN- gamma or when virion host shutoff functions are disabled
    • + CTL clones recognize HSV-2- infected fibroblasts after treatment with IFN- gamma or when virion host shutoff functions are disabled. J. Immunol. 156:3901-3910.
    • (1996) J. Immunol. , vol.156 , pp. 3901-3910
    • Tigges, M.A.1    Leng, S.2    Johnson, D.C.3    Burke, R.L.4
  • 75
    • 0036634212 scopus 로고    scopus 로고
    • Cell surface major histocompatibility complex class II proteins are regulated by the products of the gamma(1)34.5 and U(L)41 genes of herpes simplex virus 1
    • Trgovcich J, Johnson D, Roizman B. 2002. Cell surface major histocompatibility complex class II proteins are regulated by the products of the gamma(1)34.5 and U(L)41 genes of herpes simplex virus 1. J. Virol. 76:6974-6986.
    • (2002) J. Virol. , vol.76 , pp. 6974-6986
    • Trgovcich, J.1    Johnson, D.2    Roizman, B.3
  • 76
    • 0027287539 scopus 로고
    • Effect of herpes simplex virus type-1 UL41 gene on the stability ofmRNAfrom the cellular genes: beta-actin, fibronectin, glucose transporter-1, and docking protein, and on virus intraperitoneal pathogenicity of newborn mice
    • Becker Y, Tavor E, Asher Y, Berkowiltz C, Moyal M. 1993. Effect of herpes simplex virus type-1 UL41 gene on the stability ofmRNAfrom the cellular genes: beta-actin, fibronectin, glucose transporter-1, and docking protein, and on virus intraperitoneal pathogenicity of newborn mice. Virus Genes 7:133-143.
    • (1993) Virus Genes , vol.7 , pp. 133-143
    • Becker, Y.1    Tavor, E.2    Asher, Y.3    Berkowiltz, C.4    Moyal, M.5
  • 77
    • 0036787163 scopus 로고    scopus 로고
    • Therapeutic vaccination with vhs(-) herpes simplex virus reduces the severity of recurrent herpetic stromal keratitis in mice
    • Keadle TL, Laycock KA, Morris JL, Leib DA, Morrison LA, Pepose JS, Stuart PM. 2002. Therapeutic vaccination with vhs(-) herpes simplex virus reduces the severity of recurrent herpetic stromal keratitis in mice. J. Gen. Virol. 83:2361-2365.
    • (2002) J. Gen. Virol. , vol.83 , pp. 2361-2365
    • Keadle, T.L.1    Laycock, K.A.2    Morris, J.L.3    Leib, D.A.4    Morrison, L.A.5    Pepose, J.S.6    Stuart, P.M.7
  • 78
    • 0036199215 scopus 로고    scopus 로고
    • Therapeutic immunization with a virion host shutoff-defective, replication- incompetent herpes simplex virus type 1 strain limits recurrent herpetic ocular infection
    • Keadle TL, Morrison LA, Morris JL, Pepose JS, Stuart PM. 2002. Therapeutic immunization with a virion host shutoff-defective, replication- incompetent herpes simplex virus type 1 strain limits recurrent herpetic ocular infection. J. Virol. 76:3615-3625.
    • (2002) J. Virol. , vol.76 , pp. 3615-3625
    • Keadle, T.L.1    Morrison, L.A.2    Morris, J.L.3    Pepose, J.S.4    Stuart, P.M.5
  • 80
    • 84855834605 scopus 로고    scopus 로고
    • Functional genomics reveals an essential and specific role for Stat1 in protection of the central nervous system following herpes simplex virus corneal infection
    • Pasieka TJ, Cilloniz C, Carter VS, Rosato P, Katze MG, Leib DA. 2011. Functional genomics reveals an essential and specific role for Stat1 in protection of the central nervous system following herpes simplex virus corneal infection. J. Virol. 85:12972-12981.
    • (2011) J. Virol. , vol.85 , pp. 12972-12981
    • Pasieka, T.J.1    Cilloniz, C.2    Carter, V.S.3    Rosato, P.4    Katze, M.G.5    Leib, D.A.6
  • 81
    • 0034066215 scopus 로고    scopus 로고
    • Herpes simplex virus virion host shutoff (vhs) activity alters periocular disease in mice
    • Smith TJ, Ackland-Berglund CE, Leib DA. 2000. Herpes simplex virus virion host shutoff (vhs) activity alters periocular disease in mice. J. Virol. 74:3598 -3604.
    • (2000) J. Virol. , vol.74 , pp. 3598-3604
    • Smith, T.J.1    Ackland-berglund, C.E.2    Leib, D.A.3
  • 82
    • 0036170919 scopus 로고    scopus 로고
    • Pathogenesis of herpes simplex virus type 2 virion host shutoff (vhs) mutants
    • Smith TJ, Morrison LA, Leib DA. 2002. Pathogenesis of herpes simplex virus type 2 virion host shutoff (vhs) mutants. J. Virol. 76:2054 -2061.
    • (2002) J. Virol. , vol.76 , pp. 2054-2061
    • Smith, T.J.1    Morrison, L.A.2    Leib, D.A.3
  • 83
    • 10044288578 scopus 로고    scopus 로고
    • Role of the VP16-binding domain of vhs in viral growth, host shutoff activity, and pathogenesis
    • Strand SS, Leib DA. 2004. Role of the VP16-binding domain of vhs in viral growth, host shutoff activity, and pathogenesis. J. Virol. 78:13562- 13572.
    • (2004) J. Virol. , vol.78 , pp. 13562-13572
    • Strand, S.S.1    Leib, D.A.2
  • 84
    • 0028838602 scopus 로고
    • Role of the virion host shutoff (vhs) of herpes simplex virus type 1 in latency and pathogenesis
    • Strelow LI, Leib DA. 1995. Role of the virion host shutoff (vhs) of herpes simplex virus type 1 in latency and pathogenesis. J. Virol. 69:6779-6786.
    • (1995) J. Virol. , vol.69 , pp. 6779-6786
    • Strelow, L.I.1    Leib, D.A.2
  • 85
    • 0031986439 scopus 로고    scopus 로고
    • Protection from primary infection and establishment of latency by vaccination with a herpes simplex virus type 1 recombinant deficient in the virion host shutoff (vhs) function
    • Walker J, Leib DA. 1998. Protection from primary infection and establishment of latency by vaccination with a herpes simplex virus type 1 recombinant deficient in the virion host shutoff (vhs) function. Vaccine 16:1-5.
    • (1998) Vaccine , vol.16 , pp. 1-5
    • Walker, J.1    Leib, D.A.2
  • 86
    • 1542723396 scopus 로고    scopus 로고
    • The herpes simplex virus 1 UL41 gene-dependent destabilization of cellular RNAs is selective and may be sequence-specific
    • Esclatine A, Taddeo B, Evans L, Roizman B. 2004. The herpes simplex virus 1 UL41 gene-dependent destabilization of cellular RNAs is selective and may be sequence-specific. Proc. Natl. Acad. Sci.U. S. A. 101:3603- 3608.
    • (2004) Proc. Natl. Acad. Sci.U. S. A. , vol.101 , pp. 3603-3608
    • Esclatine, A.1    Taddeo, B.2    Evans, L.3    Roizman, B.4
  • 87
    • 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.
    • (2004) J. Virol. , vol.78 , pp. 8582-8592
    • Esclatine, A.1    Taddeo, B.2    Roizman, B.3
  • 88
    • 11144223347 scopus 로고    scopus 로고
    • The UL41 protein of herpes simplex virus mediates selective stabilization or degradation of cellular mRNAs
    • Esclatine A, Taddeo B, Roizman B. 2004. The UL41 protein of herpes simplex virus mediates selective stabilization or degradation of cellular mRNAs. Proc. Natl. Acad. Sci.U. S. A. 101:18165-18170.
    • (2004) Proc. Natl. Acad. Sci.U. S. A. , vol.101 , pp. 18165-18170
    • Esclatine, A.1    Taddeo, B.2    Roizman, B.3
  • 89
    • 0344995285 scopus 로고    scopus 로고
    • Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0
    • Hobbs WE, DeLuca NA. 1999. Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0. J. Virol. 73:8245- 8255.
    • (1999) J. Virol. , vol.73 , pp. 8245-8255
    • Hobbs, W.E.1    Deluca, N.A.2
  • 90
    • 0032742697 scopus 로고    scopus 로고
    • Accumulation of specific RNAs encoding transcriptional factors and stress response proteins against a background of severe depletion of cellular RNAs in cells infected with herpes simplex virus 1
    • Khodarev NN, Advani SJ, Gupta N, Roizman B, Weichselbaum RR. 1999. Accumulation of specific RNAs encoding transcriptional factors and stress response proteins against a background of severe depletion of cellular RNAs in cells infected with herpes simplex virus 1. Proc. Natl. Acad. Sci. U. S. A. 96:12062-12067.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 12062-12067
    • Khodarev, N.N.1    Advani, S.J.2    Gupta, N.3    Roizman, B.4    Weichselbaum, R.R.5
  • 91
    • 1842457780 scopus 로고    scopus 로고
    • Transcriptional response of a common permissive cell type to infection by two diverse alphaherpesviruses
    • Ray N, Enquist LW. 2004. Transcriptional response of a common permissive cell type to infection by two diverse alphaherpesviruses. J. Virol. 78:3489 -3501.
    • (2004) J. Virol. , vol.78 , pp. 3489-3501
    • Ray, N.1    Enquist, L.W.2
  • 92
    • 8744299600 scopus 로고    scopus 로고
    • Post-transcriptional processing of cellular RNAs in herpes simplex virus-infected cells
    • Taddeo B, Esclatine A, Roizman B. 2004. Post-transcriptional processing of cellular RNAs in herpes simplex virus-infected cells. Biochem. Soc. Trans. 32:697-701.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 697-701
    • Taddeo, B.1    Esclatine, A.2    Roizman, B.3
  • 93
    • 0037689355 scopus 로고    scopus 로고
    • The stressinducible immediate-early responsive gene IEX-1 is activated in cells infected with herpes simplex virus 1, but several viral mechanisms, including 3= degradation of its RNA, preclude expression of the gene
    • Taddeo B, Esclatine A, Zhang W, Roizman B. 2003. The stressinducible immediate-early responsive gene IEX-1 is activated in cells infected with herpes simplex virus 1, but several viral mechanisms, including 3= degradation of its RNA, preclude expression of the gene. J. Virol. 77:6178-6187.
    • (2003) J. Virol. , vol.77 , pp. 6178-6187
    • Taddeo, B.1    Esclatine, A.2    Zhang, W.3    Roizman, B.4
  • 94
    • 33748930095 scopus 로고    scopus 로고
    • Herpes simplex virus ICP27 is required for virus-induced stabilization of the ARE-containing IEX-1 mRNA encoded by the human IER3 gene
    • Corcoran JA, Hsu WL, Smiley JR. 2006. Herpes simplex virus ICP27 is required for virus-induced stabilization of the ARE-containing IEX-1 mRNA encoded by the human IER3 gene. J. Virol. 80:9720 -9729.
    • (2006) J. Virol. , vol.80 , pp. 9720-9729
    • Corcoran, J.A.1    Hsu, W.L.2    Smiley, J.R.3
  • 95
    • 15244355273 scopus 로고    scopus 로고
    • Herpes simplex virus infection stabilizes cellular IEX-1 mRNA
    • Hsu WL, Saffran HA, Smiley JR. 2005. Herpes simplex virus infection stabilizes cellular IEX-1 mRNA. J. Virol. 79:4090-4098.
    • (2005) J. Virol. , vol.79 , pp. 4090-4098
    • Hsu, W.L.1    Saffran, H.A.2    Smiley, J.R.3
  • 96
    • 0026084164 scopus 로고
    • In vitro mRNA degradation system to study the virion host shutoff function of herpes simplex virus
    • Krikorian CR, Read GS. 1991. In vitro mRNA degradation system to study the virion host shutoff function of herpes simplex virus. J. Virol. 65:112-122.
    • (1991) J. Virol. , vol.65 , pp. 112-122
    • Krikorian, C.R.1    Read, G.S.2
  • 97
    • 0029154038 scopus 로고
    • The virion host shutoff protein of herpes simplex virus inhibits reporter gene expression in the absence of other viral gene products
    • Pak AS, Everly DN, Knight K, Read GS. 1995. The virion host shutoff protein of herpes simplex virus inhibits reporter gene expression in the absence of other viral gene products. Virology 211:491-506.
    • (1995) Virology , vol.211 , pp. 491-506
    • Pak, A.S.1    Everly, D.N.2    Knight, K.3    Read, G.S.4
  • 98
    • 0025866616 scopus 로고
    • Analysis of herpes simplex virusinduced mRNA destabilizing activity using an in vitro mRNA decay system
    • Sorenson CM, Hart PA, Ross J. 1991. Analysis of herpes simplex virusinduced mRNA destabilizing activity using an in vitro mRNA decay system. Nucleic Acids Res. 19:4459-4465.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4459-4465
    • Sorenson, C.M.1    Hart, P.A.2    Ross, J.3
  • 99
    • 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
  • 100
    • 0033544338 scopus 로고    scopus 로고
    • The virion host shutoff function of herpes simplex virus degrades the 5' end of a target mRNA before the 3' end
    • Karr BM, Read GS. 1999. The virion host shutoff function of herpes simplex virus degrades the 5' end of a target mRNA before the 3' end. Virology 264:195-204.
    • (1999) Virology , vol.264 , pp. 195-204
    • Karr, B.M.1    Read, G.S.2
  • 101
    • 0035168426 scopus 로고    scopus 로고
    • The vhs1 mutant form of herpes simplex virus virion host shutoff protein retains significant internal ribosome entry site-directedRNAcleavage activity
    • Lu P, Saffran HA, Smiley JR. 2001. The vhs1 mutant form of herpes simplex virus virion host shutoff protein retains significant internal ribosome entry site-directedRNAcleavage activity. J. Virol. 75:1072-1076.
    • (2001) J. Virol. , vol.75 , pp. 1072-1076
    • Lu, P.1    Saffran, H.A.2    Smiley, J.R.3
  • 102
    • 8644242205 scopus 로고    scopus 로고
    • RNA degradation induced by the herpes simplex virus vhs protein proceeds 5' to 3' in vitro
    • Perez-Parada J, Saffran HA, Smiley JR. 2004. RNA degradation induced by the herpes simplex virus vhs protein proceeds 5' to 3' in vitro. J. Virol. 78:13391-13394.
    • (2004) J. Virol. , vol.78 , pp. 13391-13394
    • Perez-parada, J.1    Saffran, H.A.2    Smiley, J.R.3
  • 103
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson RJ, Hellen CU, Pestova TV. 2010. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell Biol. 11:113-127.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 105
    • 33846991130 scopus 로고    scopus 로고
    • The mechanism of translation initiation in eukaryotes
    • Mathews MB, Sonenberg N, Hershey JWB (ed), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Pestova TV, Lorsch JR, Hellen CUT. 2007. The mechanism of translation initiation in eukaryotes, p 87-128. In Mathews MB, Sonenberg N, Hershey JWB (ed), Translational control in biology and medicine. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2007) Translational control in biology and medicine , pp. 87-128
    • Pestova, T.V.1    Lorsch, J.R.2    Hellen, C.U.T.3
  • 107
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG. 2009. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136:731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 109
    • 0033544894 scopus 로고    scopus 로고
    • Further biochemical and kinetic characterization of human eukaryotic initiation factor 4H
    • Richter NJ, Rogers GW, Jr, Hensold JO, Merrick WC. 1999. Further biochemical and kinetic characterization of human eukaryotic initiation factor 4H. J. Biol. Chem. 274:35415-35424.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35415-35424
    • Richter, N.J.1    Rogers Jr., G.W.2    Hensold, J.O.3    Merrick, W.C.4
  • 110
    • 0032571398 scopus 로고    scopus 로고
    • Purification and characterization of a new eukaryotic protein translation factor. Eukaryotic initiation factor 4H
    • Richter-Cook NJ, Dever TE, Hensold JO, Merrick WC. 1998. Purification and characterization of a new eukaryotic protein translation factor. Eukaryotic initiation factor 4H. J. Biol. Chem. 273:7579 -7587.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7579-7587
    • Richter-cook, N.J.1    Dever, T.E.2    Hensold, J.O.3    Merrick, W.C.4
  • 111
    • 0035918241 scopus 로고    scopus 로고
    • Further characterization of the helicase activity of eIF4A. Substrate specificity
    • Rogers GW, Jr, Lima WF, Merrick WC. 2001. Further characterization of the helicase activity of eIF4A. Substrate specificity. J. Biol. Chem. 276: 12598-12608.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12598-12608
    • Rogers Jr., G.W.1    Lima, W.F.2    Merrick, W.C.3
  • 112
    • 0035903136 scopus 로고    scopus 로고
    • Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F
    • Rogers GW, Jr, Richter NJ, Lima WF, Merrick WC. 2001. Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F. J. Biol. Chem. 276:30914 -30922.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30914-30922
    • Rogers Jr., G.W.1    Richter, N.J.2    Lima, W.F.3    Merrick, W.C.4
  • 113
    • 0040142238 scopus 로고    scopus 로고
    • Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A
    • Rogers GW, Jr, Richter NJ, Merrick WC. 1999. Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A. J. Biol. Chem. 274:12236 -12244.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12236-12244
    • Rogers Jr., G.W.1    Richter, N.J.2    Merrick, W.C.3
  • 114
    • 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.
    • (2010) J. Virol. , vol.84 , pp. 6886-6890
    • Page, H.G.1    Read, G.S.2
  • 115
    • 1842413671 scopus 로고    scopus 로고
    • Mutational analysis of the virion host shutoff gene (UL41) of herpes simplex virus (HSV): characterization of HSV type 1 (HSV-1)/HSV-2 chimeras
    • Everly DN, Jr. , Read GS. 1997. Mutational analysis of the virion host shutoff gene (UL41) of herpes simplex virus (HSV): characterization of HSV type 1 (HSV-1)/HSV-2 chimeras. J. Virol. 71:7157-7166.
    • (1997) J. Virol. , vol.71 , pp. 7157-7166
    • Everly Jr., D.N..1    Read, G.S.2
  • 116
    • 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 Jr., D.N.1    Read, G.S.2
  • 118
    • 0029053190 scopus 로고
    • Initiation of protein synthesis by the eukaryotic translational apparatus on circular RNAs
    • Chen CY, Sarnow P. 1995. Initiation of protein synthesis by the eukaryotic translational apparatus on circular RNAs. Science 268:415- 417.
    • (1995) Science , vol.268
    • Chen, C.Y.1    Sarnow, P.2
  • 119
    • 0032254089 scopus 로고    scopus 로고
    • Internal ribosome entry sites tests with circular mRNAs
    • Chen CY, Sarnow P. 1998. Internal ribosome entry sites tests with circular mRNAs. Methods Mol. Biol. 77:355-363.
    • (1998) Methods Mol. Biol. , vol.77 , pp. 355-363
    • Chen, C.Y.1    Sarnow, P.2
  • 121
    • 33646193306 scopus 로고    scopus 로고
    • Control of mammalian translation bymRNAstructure near caps
    • Babendure JR, Babendure JL, Ding JH, Tsien RY. 2006. Control of mammalian translation bymRNAstructure near caps.RNA12:851- 861.
    • (2006) RNA , vol.12 , pp. 851-861
    • Babendure, J.R.1    Babendure, J.L.2    Ding, J.H.3    Tsien, R.Y.4
  • 122
    • 0023665902 scopus 로고
    • An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAs
    • '-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 15:8125- 8148.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 123
    • 0026342613 scopus 로고
    • An analysis of vertebrate mRNA sequences: intimations of translational control
    • Kozak M. 1991. An analysis of vertebrate mRNA sequences: intimations of translational control. J. Cell Biol. 115:887-903.
    • (1991) J. Cell Biol. , vol.115 , pp. 887-903
    • Kozak, M.1
  • 124
    • 0025792297 scopus 로고
    • Structural features in eukaryotic mRNAs that modulate the initiation of translation
    • Kozak M. 1991. Structural features in eukaryotic mRNAs that modulate the initiation of translation. J. Biol. Chem. 266:19867-19870.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19867-19870
    • Kozak, M.1
  • 125
    • 0026729831 scopus 로고
    • Regulation of translation in eukaryotic systems
    • Kozak M. 1992. Regulation of translation in eukaryotic systems. Annu. Rev. Cell Biol. 8:197-225.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 197-225
    • Kozak, M.1
  • 126
    • 0028140591 scopus 로고
    • Features in the 5' non-coding sequences of rabbit alpha and beta-globin mRNAs that affect translational efficiency
    • ' non-coding sequences of rabbit alpha and beta-globin mRNAs that affect translational efficiency. J. Mol. Biol. 235:95-110.
    • (1994) J. Mol. Biol. , vol.235 , pp. 95-110
    • Kozak, M.1
  • 127
    • 0024546509 scopus 로고
    • The scanning model for translation: an update
    • Kozak M. 1989. The scanning model for translation: an update. J. Cell Biol. 108:229 -241.
    • (1989) J. Cell Biol. , vol.108 , pp. 229-241
    • Kozak, M.1
  • 128
    • 0037112055 scopus 로고    scopus 로고
    • The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection
    • Pestova TV, Kolupaeva VG. 2002. The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection. Genes Dev. 16:2906 -2922.
    • (2002) Genes Dev. , vol.16 , pp. 2906-2922
    • Pestova, T.V.1    Kolupaeva, V.G.2
  • 129
    • 42449155947 scopus 로고    scopus 로고
    • Cap-dependent eukaryotic initiation factor-mRNA interactions probed by cross-linking
    • Lindqvist L, Imataka H, Pelletier J. 2008. Cap-dependent eukaryotic initiation factor-mRNA interactions probed by cross-linking. RNA 14: 960-969.
    • (2008) RNA , vol.14 , pp. 960-969
    • Lindqvist, L.1    Imataka, H.2    Pelletier, J.3
  • 130
    • 0032572776 scopus 로고    scopus 로고
    • Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons
    • Pestova TV, Borukhov SI, Hellen CU. 1998. Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons. Nature 394:854-859.
    • (1998) Nature , vol.394 , pp. 854-859
    • Pestova, T.V.1    Borukhov, S.I.2    Hellen, C.U.3
  • 131
    • 57649234552 scopus 로고    scopus 로고
    • Translation initiation on mammalian mRNAs with structured 5'UTRs requires DExH-box protein DHX29
    • Pisareva VP, Pisarev AV, Komar AA, Hellen CU, Pestova TV. 2008. Translation initiation on mammalian mRNAs with structured 5'UTRs requires DExH-box protein DHX29. Cell 135:1237-1250.
    • (2008) Cell , vol.135 , pp. 1237-1250
    • Pisareva, V.P.1    Pisarev, A.V.2    Komar, A.A.3    Hellen, C.U.4    Pestova, T.V.5
  • 133
    • 0034682720 scopus 로고    scopus 로고
    • Initiation of protein synthesis from the A site of the ribosome
    • Wilson JE, Pestova TV, Hellen CU, Sarnow P. 2000. Initiation of protein synthesis from the A site of the ribosome. Cell 102:511-520.
    • (2000) Cell , vol.102 , pp. 511-520
    • Wilson, J.E.1    Pestova, T.V.2    Hellen, C.U.3    Sarnow, P.4
  • 135
    • 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.
    • (2004) J. Virol. , vol.78 , pp. 4684-4699
    • Doepker, R.C.1    Hsu, W.L.2    Saffran, H.A.3    Smiley, J.R.4
  • 136
    • 84864491902 scopus 로고    scopus 로고
    • The eukaryotic initiation factor eIF4H facilitates loop-binding, repetitive RNA unwinding by the eIF4A DEAD-box helicase
    • Sun Y, Atas E, Lindqvist L, Sonenberg N, Pelletier J, Meller A. 2012. The eukaryotic initiation factor eIF4H facilitates loop-binding, repetitive RNA unwinding by the eIF4A DEAD-box helicase. Nucleic Acids Res. 40:6199-6207.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 6199-6207
    • Sun, Y.1    Atas, E.2    Lindqvist, L.3    Sonenberg, N.4    Pelletier, J.5    Meller, A.6
  • 137
    • 1842335136 scopus 로고    scopus 로고
    • Translation of an uncapped mRNA involves scanning
    • Gunnery S, Maivali U, Mathews MB. 1997. Translation of an uncapped mRNA involves scanning. J. Biol. Chem. 272:21642-21646.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21642-21646
    • Gunnery, S.1    Maivali, U.2    Mathews, M.B.3
  • 139
    • 67749088599 scopus 로고    scopus 로고
    • The virion-packaged endoribonuclease of herpes simplex virus 1 cleaves mRNA in polyribosomes
    • Taddeo B, Zhang W, Roizman B. 2009. The virion-packaged endoribonuclease of herpes simplex virus 1 cleaves mRNA in polyribosomes. Proc. Natl. Acad. Sci.U. S. A. 106:12139 -12144.
    • (2009) Proc. Natl. Acad. Sci.U. S. A. , vol.106 , pp. 12139-12144
    • Taddeo, B.1    Zhang, W.2    Roizman, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.