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Volumn 81, Issue 3, 2007, Pages 1148-1161

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

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; POLYPEPTIDE; UNCLASSIFIED DRUG; VIRION HOST SHUTOFF PROTEIN; VIRUS PROTEIN; VIRUS RNA;

EID: 33846505946     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01812-06     Document Type: Article
Times cited : (26)

References (88)
  • 2
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • T. Hunter and B. M. Sefton ed, Academic Press, Inc, San Diego, CA
    • Boyle, W. J., P. Van Der Geer, and T. Hunter. 1991. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates, p. 110-149. In T. Hunter and B. M. Sefton (ed.), Protein phosphorylation, part B. Academic Press, Inc., San Diego, CA.
    • (1991) Protein phosphorylation, part B , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3
  • 3
    • 27144515901 scopus 로고    scopus 로고
    • Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies
    • Brengues, M., D. Teixeira, and R. Parker. 2005. Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies. Science 310:486-489.
    • (2005) Science , vol.310 , pp. 486-489
    • Brengues, M.1    Teixeira, D.2    Parker, R.3
  • 4
    • 0037384969 scopus 로고    scopus 로고
    • Membrane association of VP22, a herpes simplex virus type 1 tegument protein
    • Brignati, M. J., J. S. Loomis, J. W. Wills, and R. J. Courtney. 2003. Membrane association of VP22, a herpes simplex virus type 1 tegument protein. J. Virol. 77:4888-4898.
    • (2003) J. Virol , vol.77 , pp. 4888-4898
    • Brignati, M.J.1    Loomis, J.S.2    Wills, J.W.3    Courtney, R.J.4
  • 5
    • 0029949793 scopus 로고    scopus 로고
    • An endoplasmic reticulum-retained herpes simplex virus glycoprotein H is absent from secreted virions: Evidence for reenvelopment during egress
    • Browne, H., S. Bell, T. Minson, and D. W. Wilson. 1996. An endoplasmic reticulum-retained herpes simplex virus glycoprotein H is absent from secreted virions: evidence for reenvelopment during egress. J. Virol. 70:4311-4316.
    • (1996) J. Virol , vol.70 , pp. 4311-4316
    • Browne, H.1    Bell, S.2    Minson, T.3    Wilson, D.W.4
  • 6
    • 0034839596 scopus 로고    scopus 로고
    • Computational modeling of eukaryotic mRNA turnover
    • Cao, D., and R. Parker. 2001. Computational modeling of eukaryotic mRNA turnover. RNA 7:1192-1212.
    • (2001) RNA , vol.7 , pp. 1192-1212
    • Cao, D.1    Parker, R.2
  • 7
    • 0038402506 scopus 로고    scopus 로고
    • Computational modeling and experimental analysis of nonsense-mediated decay in yeast
    • Cao, D., and R. Parker. 2003. Computational modeling and experimental analysis of nonsense-mediated decay in yeast. Cell 113:533-545.
    • (2003) Cell , vol.113 , pp. 533-545
    • Cao, D.1    Parker, R.2
  • 8
    • 3943051423 scopus 로고    scopus 로고
    • Eukaryotic mRNA decapping
    • Coller, J., and R. Parker. 2004. Eukaryotic mRNA decapping. Annu. Rev. Biochem. 73:861-890.
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 861-890
    • Coller, J.1    Parker, R.2
  • 9
    • 0036792048 scopus 로고    scopus 로고
    • mRNA decay enzymes: Decappers conserved between yeast and mammals
    • Decker, C. J., and R. Parker. 2002. mRNA decay enzymes: decappers conserved between yeast and mammals. Proc. Natl. Acad. Sci. USA 99:12512-12514.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12512-12514
    • Decker, C.J.1    Parker, R.2
  • 10
    • 0027511720 scopus 로고
    • Mutations in herpes simplex virus type 1 genes encoding VP5 and VP23 abrogate capsid formation and cleavage of replicated DNA
    • Desai, P., N. A. DeLuca, J. C. Glorioso, and S. Person. 1993. Mutations in herpes simplex virus type 1 genes encoding VP5 and VP23 abrogate capsid formation and cleavage of replicated DNA. J. Virol. 67:1357-1364.
    • (1993) J. Virol , vol.67 , pp. 1357-1364
    • Desai, P.1    DeLuca, N.A.2    Glorioso, J.C.3    Person, S.4
  • 11
    • 8644221609 scopus 로고    scopus 로고
    • Herpes simplex virus virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4H
    • Doepker, R. C., W. L. Hsu, H. A. Saffran, and J. R. Smiley. 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
  • 12
    • 0032864835 scopus 로고    scopus 로고
    • The herpes simplex virus Vhs protein induces endoribonucleolytic cleavage of target RNAs in cell extracts
    • Elgadi, M. M., C. E. Hayes, and J. R. Smiley. 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
  • 13
    • 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, M. M., and J. R. Smiley. 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
  • 14
    • 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., B. Taddeo, L. Evans, and B. Roizman. 2004. The herpes simplex virus 1 UL41 gene-dependent destabilization of cellular RNAs is selective and may be sequence-specific. Proc. Natl. Acad. Sci. USA 101:3603-3608.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3603-3608
    • Esclatine, A.1    Taddeo, B.2    Evans, L.3    Roizman, B.4
  • 15
    • 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., B. Taddeo, and B. Roizman. 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
  • 16
    • 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, D. N., Jr., P. Feng, I. S. Mian, and G. S. Read. 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
  • 17
    • 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, D. N., Jr., and G. S. Read. 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
  • 18
    • 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, D. N., Jr., and G. S. Read. 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
  • 19
    • 0034796322 scopus 로고    scopus 로고
    • mRNA decay during herpesvirus infections: Interaction between a putative viral nuclease and a cellular translation factor
    • Feng, P., D. N. Everly, Jr., and G. S. Read. 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
  • 20
    • 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., D. N. Everly, Jr., and G. S. Read. 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
  • 21
    • 0021139610 scopus 로고
    • Early virion-associated suppression of cellular protein synthesis by herpes simplex virus is accompanied by inactivation of mRNA
    • Fenwick, M. L., and M. M. McMenamin. 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
  • 22
    • 0023785408 scopus 로고
    • Expression of a truncated viral trans-activator selectively impedes lytic infection by its cognate virus
    • Friedman, A. D., S. J. Triezenberg, and S. L. McKnight. 1988. Expression of a truncated viral trans-activator selectively impedes lytic infection by its cognate virus. Nature 335:452-454.
    • (1988) Nature , vol.335 , pp. 452-454
    • Friedman, A.D.1    Triezenberg, S.J.2    McKnight, S.L.3
  • 23
    • 0015427631 scopus 로고
    • Proteins specified by herpes simplex virus. 8. Characterization and composition of multiple capsid forms of subtypes 1 and 2
    • Gibson, W., and B. Roizman. 1972. Proteins specified by herpes simplex virus. 8. Characterization and composition of multiple capsid forms of subtypes 1 and 2. J. Virol. 10:1044-1052.
    • (1972) J. Virol , vol.10 , pp. 1044-1052
    • Gibson, W.1    Roizman, B.2
  • 24
    • 0015948224 scopus 로고
    • Proteins specified by herpes simplex virus. Staining and radiolabeling properties of B capsid and virion proteins in polyacrylamide gels
    • Gibson, W., and B. Roizman. 1974. Proteins specified by herpes simplex virus. Staining and radiolabeling properties of B capsid and virion proteins in polyacrylamide gels. J. Virol. 13:155-165.
    • (1974) J. Virol , vol.13 , pp. 155-165
    • Gibson, W.1    Roizman, B.2
  • 25
    • 0346367068 scopus 로고    scopus 로고
    • The cytoplasmic tail of herpes simplex virus glycoprotein H binds to the tegument protein VP16 in vitro and in vivo
    • Gross, S. T., C. A. Harley, and D. W. Wilson. 2003. The cytoplasmic tail of herpes simplex virus glycoprotein H binds to the tegument protein VP16 in vitro and in vivo. Virology 317:1-12.
    • (2003) Virology , vol.317 , pp. 1-12
    • Gross, S.T.1    Harley, C.A.2    Wilson, D.W.3
  • 27
    • 0016264832 scopus 로고
    • Proteins specified by herpes simplex virus. XII. The virion polypeptides of type 1 strains
    • Heine, J. W., R. W. Honess, E. Cassai, and B. Roizman. 1974. Proteins specified by herpes simplex virus. XII. The virion polypeptides of type 1 strains. J. Virol. 14:640-651.
    • (1974) J. Virol , vol.14 , pp. 640-651
    • Heine, J.W.1    Honess, R.W.2    Cassai, E.3    Roizman, B.4
  • 28
    • 0030871678 scopus 로고    scopus 로고
    • Capsid assembly and DNA packaging in herpes simplex virus
    • Homa, F. L., and J. C. Brown. 1997. Capsid assembly and DNA packaging in herpes simplex virus. Rev. Med. Virol. 7:107-122.
    • (1997) Rev. Med. Virol , vol.7 , pp. 107-122
    • Homa, F.L.1    Brown, J.C.2
  • 29
    • 0029019122 scopus 로고
    • Mutational analysis of the herpes simplex virus virion host shutoff protein: Evidence that Vhs functions in the absence of other viral proteins
    • Jones, F. E., C. A. Smibert, and J. R. Smiley. 1995. Mutational analysis of the herpes simplex virus virion host shutoff protein: evidence that Vhs functions in the absence of other viral proteins. J. Virol. 69:4863-4871.
    • (1995) J. Virol , vol.69 , pp. 4863-4871
    • Jones, F.E.1    Smibert, C.A.2    Smiley, J.R.3
  • 30
    • 18144387577 scopus 로고    scopus 로고
    • Structural basis for the physiological temperature dependence of the association of VP16 with the cytoplasmic tail of herpes simplex virus glycoprotein H
    • Kamen, D. E., S. T. Gross, M. E. Girvin, and D. W. Wilson. 2005. Structural basis for the physiological temperature dependence of the association of VP16 with the cytoplasmic tail of herpes simplex virus glycoprotein H. J. Virol. 79:6134-6141.
    • (2005) J. Virol , vol.79 , pp. 6134-6141
    • Kamen, D.E.1    Gross, S.T.2    Girvin, M.E.3    Wilson, D.W.4
  • 31
    • 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, B. M., and G. S. Read. 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
  • 32
    • 0020535197 scopus 로고
    • The effect of ammonium chloride and tunicamycin on the glycoprotein content and infectivity of herpes simplex virus type 1
    • Kousoulas, K. G., D. J. Bzik, N. A. DeLuca, and S. Person. 1983. The effect of ammonium chloride and tunicamycin on the glycoprotein content and infectivity of herpes simplex virus type 1. Virology 125:468-474.
    • (1983) Virology , vol.125 , pp. 468-474
    • Kousoulas, K.G.1    Bzik, D.J.2    DeLuca, N.A.3    Person, S.4
  • 33
    • 0026084164 scopus 로고
    • In vitro mRNA degradation system to study the virion host shutoff function of herpes simplex virus
    • Krikorian, C. R., and G. S. Read. 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
  • 34
    • 2642604294 scopus 로고
    • Herpes simplex virus-infected cells contain a function(s) that destabilizes both host and viral mRNAs
    • Kwong, A. D., and N. Frenkel. 1987. Herpes simplex virus-infected cells contain a function(s) that destabilizes both host and viral mRNAs. Proc. Natl. Acad. Sci. USA 84:1926-1930.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1926-1930
    • Kwong, A.D.1    Frenkel, N.2
  • 35
    • 0023866418 scopus 로고
    • Herpes simplex virus virion host shutoff function
    • Kwong, A. D., J. A. Kruper, and N. Frenkel. 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
  • 36
    • 0029876445 scopus 로고    scopus 로고
    • Herpes simplex virus VP16 rescues viral mRNA from destruction by the virion host shutoff function
    • Lam, Q., C. A. Smibert, K. E. Koop, C. Lavery, J. P. Capone, S. P. Weinheimer, and J. R. Smiley. 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
  • 37
    • 0037302298 scopus 로고    scopus 로고
    • A subpopulation of tegument protein Vhs localizes to detergent-insoluble lipid rafts in herpes simplex virus-infected cells
    • Lee, G. E., G. A. Church, and D. W. Wilson. 2003. A subpopulation of tegument protein Vhs localizes to detergent-insoluble lipid rafts in herpes simplex virus-infected cells. J. Virol. 77:2038-2045.
    • (2003) J. Virol , vol.77 , pp. 2038-2045
    • Lee, G.E.1    Church, G.A.2    Wilson, D.W.3
  • 38
    • 0035194288 scopus 로고    scopus 로고
    • Intracellular trafficking of the UL11 tegument protein of herpes simplex virus type 1
    • Loomis, J. S., J. B. Bowzard, R. J. Courtney, and J. W. Wills. 2001. Intracellular trafficking of the UL11 tegument protein of herpes simplex virus type 1. J. Virol. 75:12209-12219.
    • (2001) J. Virol , vol.75 , pp. 12209-12219
    • Loomis, J.S.1    Bowzard, J.B.2    Courtney, R.J.3    Wills, J.W.4
  • 39
    • 0142092454 scopus 로고    scopus 로고
    • Binding partners for the UL11 tegument protein of herpes simplex virus type 1
    • Loomis, J. S., R. J. Courtney, and J. W. Wills. 2003. Binding partners for the UL11 tegument protein of herpes simplex virus type 1. J. Virol. 77:11417-11424.
    • (2003) J. Virol , vol.77 , pp. 11417-11424
    • Loomis, J.S.1    Courtney, R.J.2    Wills, J.W.3
  • 40
    • 0035151479 scopus 로고    scopus 로고
    • Herpes simplex virus virion host shutoff protein requires a mammalian factor for efficient in vitro endoribonuclease activity
    • Lu, P., F. E. Jones, H. A. Saffran, and J. R. Smiley. 2001. Herpes simplex virus virion host shutoff protein requires a mammalian factor for efficient in vitro endoribonuclease activity. J. Virol. 75:1172-1185.
    • (2001) J. Virol , vol.75 , pp. 1172-1185
    • Lu, P.1    Jones, F.E.2    Saffran, H.A.3    Smiley, J.R.4
  • 41
    • 0035168426 scopus 로고    scopus 로고
    • The Vhs1 mutant form of herpes simplex virus virion host shutoff protein retains significant internal ribosome entry site-directed RNA cleavage activity
    • Lu, P., H. A. Saffran, and J. R. Smiley. 2001. The Vhs1 mutant form of herpes simplex virus virion host shutoff protein retains significant internal ribosome entry site-directed RNA cleavage 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
  • 42
    • 0026657882 scopus 로고
    • Noninfectious L-particles supply functions which can facilitate infection by HSV-1
    • McLauchlan, J., C. Addison, M. C. Craigie, and F. J. Rixon. 1992. Noninfectious L-particles supply functions which can facilitate infection by HSV-1. Virology 190:682-688.
    • (1992) Virology , vol.190 , pp. 682-688
    • McLauchlan, J.1    Addison, C.2    Craigie, M.C.3    Rixon, F.J.4
  • 43
    • 0036148284 scopus 로고    scopus 로고
    • Herpesvirus assembly and egress
    • Mettenleiter, T. C. 2002. Herpesvirus assembly and egress. J. Virol. 76:1537-1547.
    • (2002) J. Virol , vol.76 , pp. 1537-1547
    • Mettenleiter, T.C.1
  • 44
    • 9644268172 scopus 로고    scopus 로고
    • Budding events in herpesvirus morphogenesis
    • Mettenleiter, T. C. 2004. Budding events in herpesvirus morphogenesis. Virus Res. 106:167-180.
    • (2004) Virus Res , vol.106 , pp. 167-180
    • Mettenleiter, T.C.1
  • 45
    • 31144448686 scopus 로고    scopus 로고
    • Egress of alphaherpesviruses
    • Mettenleiter, T. C., T. Minson, and P. Wild. 2006. Egress of alphaherpesviruses. J. Virol. 80:1610-1612.
    • (2006) J. Virol , vol.80 , pp. 1610-1612
    • Mettenleiter, T.C.1    Minson, T.2    Wild, P.3
  • 46
    • 0036776468 scopus 로고    scopus 로고
    • In rat dorsal root ganglion neurons, herpes simplex virus type 1 tegument forms in the cytoplasm of the cell body
    • Miranda-Saksena, M., R. A. Boadle, P. Armati, and A. L. Cunningham. 2002. In rat dorsal root ganglion neurons, herpes simplex virus type 1 tegument forms in the cytoplasm of the cell body. J. Virol. 76:9934-9951.
    • (2002) J. Virol , vol.76 , pp. 9934-9951
    • Miranda-Saksena, M.1    Boadle, R.A.2    Armati, P.3    Cunningham, A.L.4
  • 49
    • 33144465751 scopus 로고    scopus 로고
    • Herpes simplex virus tegument protein VP16 is a component of primary enveloped virions
    • Naldinho-Souto, R., H. Browne, and T. Minson. 2006. Herpes simplex virus tegument protein VP16 is a component of primary enveloped virions. J. Virol. 80:2582-2584.
    • (2006) J. Virol , vol.80 , pp. 2582-2584
    • Naldinho-Souto, R.1    Browne, H.2    Minson, T.3
  • 50
    • 0026098298 scopus 로고
    • Structure of the herpes simplex virus capsid: Effects of extraction with guanidine hydrochloride and partial reconstitution of extracted capsids
    • Newcomb, W. W., and J. C. Brown. 1991. Structure of the herpes simplex virus capsid: effects of extraction with guanidine hydrochloride and partial reconstitution of extracted capsids. J. Virol. 65:613-620.
    • (1991) J. Virol , vol.65 , pp. 613-620
    • Newcomb, W.W.1    Brown, J.C.2
  • 51
    • 0028031336 scopus 로고
    • Cell-free assembly of the herpes simplex virus capsid
    • Newcomb, W. W., F. L. Homa, D. R. Thomsen, Z. Ye, and J. C. Brown. 1994. Cell-free assembly of the herpes simplex virus capsid. J. Virol. 68:6059-6063.
    • (1994) J. Virol , vol.68 , pp. 6059-6063
    • Newcomb, W.W.1    Homa, F.L.2    Thomsen, D.R.3    Ye, Z.4    Brown, J.C.5
  • 52
    • 0023108018 scopus 로고
    • A mutant of herpes simplex virus type 1 exhibits increased stability of immediate-early (alpha) mRNAs
    • Oroskar, A. A., and G. S. Read. 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
  • 53
    • 0024521222 scopus 로고
    • Control of mRNA stability by the virion host shutoff function of herpes simplex virus
    • Oroskar, A. A., and G. S. Read. 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
  • 54
    • 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, A. S., D. N. Everly, K. Knight, and G. S. Read. 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
  • 55
    • 0742288008 scopus 로고    scopus 로고
    • The enzymes and control of eukaryotic mRNA turnover
    • Parker, R., and H. Song. 2004. The enzymes and control of eukaryotic mRNA turnover. Nat. Struct. Mol. Biol. 11:121-127.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 121-127
    • Parker, R.1    Song, H.2
  • 56
    • 0001798701 scopus 로고    scopus 로고
    • Control of mRNA stability during herpes simplex virus infections
    • J. B. Harford and D. R. Morris ed, Wiley-Liss, Inc, New York, NY
    • Read, G. S. 1997. Control of mRNA stability during herpes simplex virus infections, p. 311-321. In J. B. Harford and D. R. Morris (ed.), mRNA metabolism and post-transcriptional gene regulation. Wiley-Liss, Inc., New York, NY.
    • (1997) mRNA metabolism and post-transcriptional gene regulation , pp. 311-321
    • Read, G.S.1
  • 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, G. S., and N. Frenkel. 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
    • 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, G. S., B. M. Karr, and K. Knight. 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
  • 59
    • 0034892972 scopus 로고    scopus 로고
    • U(L)31 and U(L)34 proteins of herpes simplex virus type 1 form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids
    • Reynolds, A. E., B. J. Ryckman, J. D. Baines, Y. Zhou, L. Liang, and R. J. Roller. 2001. U(L)31 and U(L)34 proteins of herpes simplex virus type 1 form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids. J. Virol. 75:8803-8817.
    • (2001) J. Virol , vol.75 , pp. 8803-8817
    • Reynolds, A.E.1    Ryckman, B.J.2    Baines, J.D.3    Zhou, Y.4    Liang, L.5    Roller, R.J.6
  • 60
    • 0036333663 scopus 로고    scopus 로고
    • Ultrastructural localization of the herpes simplex virus type 1 UL31, UL34, and US3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids
    • Reynolds, A. E., E. G. Wills, R. J. Roller, B. J. Ryckman, and J. D. Baines. 2002. Ultrastructural localization of the herpes simplex virus type 1 UL31, UL34, and US3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids. J. Virol. 76:8939-8952.
    • (2002) J. Virol , vol.76 , pp. 8939-8952
    • Reynolds, A.E.1    Wills, E.G.2    Roller, R.J.3    Ryckman, B.J.4    Baines, J.D.5
  • 61
    • 0026551804 scopus 로고
    • Assembly of enveloped tegument structures (L particles) can occur independently of virion maturation in herpes simplex virus type 1-infected cells
    • Rixon, F. J., C. Addison, and J. McLauchlan. 1992. Assembly of enveloped tegument structures (L particles) can occur independently of virion maturation in herpes simplex virus type 1-infected cells. J Gen. Virol. 73:277-284.
    • (1992) J Gen. Virol , vol.73 , pp. 277-284
    • Rixon, F.J.1    Addison, C.2    McLauchlan, J.3
  • 62
    • 0001142641 scopus 로고    scopus 로고
    • Herpes simplex viruses and their replication
    • D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus ed, 4th ed. Lippincott Williams & Williams, Philadelphia, PA
    • Roizman, B., and D. M. Knipe. 2001. Herpes simplex viruses and their replication, p. 2399-2459. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Fields virology, 4th ed. Lippincott Williams & Williams, Philadelphia, PA.
    • (2001) Fields virology , pp. 2399-2459
    • Roizman, B.1    Knipe, D.M.2
  • 63
    • 0023135555 scopus 로고
    • Deletion mutants in the gene encoding the herpes simplex virus type 1 immediate-early protein ICP0 exhibit impaired growth in cell culture
    • Sacks, W. R., and P. A. Schaffer. 1987. Deletion mutants in the gene encoding the herpes simplex virus type 1 immediate-early protein ICP0 exhibit impaired growth in cell culture. J. Virol. 61:829-839.
    • (1987) J. Virol , vol.61 , pp. 829-839
    • Sacks, W.R.1    Schaffer, P.A.2
  • 64
    • 0022178431 scopus 로고
    • Degradation of cellular mRNAs induced by a virion-associated factor during herpes simplex virus infection of Vero cells
    • Schek, N., and S. L. Bachenheimer. 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
  • 65
    • 0029873163 scopus 로고    scopus 로고
    • Identification and characterization of a small modular domain in the herpes simplex virus host shutoff protein sufficient for interaction with VP16
    • Schmelter, J., J. Knez, J. R. Smiley, and J. P. Capone. 1996. Identification and characterization of a small modular domain in the herpes simplex virus host shutoff protein sufficient for interaction with VP16. J. Virol. 70:2124-2131.
    • (1996) J. Virol , vol.70 , pp. 2124-2131
    • Schmelter, J.1    Knez, J.2    Smiley, J.R.3    Capone, J.P.4
  • 66
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • Sheth, U., and R. Parker. 2003. Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 300:805-808.
    • (2003) Science , vol.300 , pp. 805-808
    • Sheth, U.1    Parker, R.2
  • 67
    • 0035024157 scopus 로고    scopus 로고
    • Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment→deenvelopment→reenvelopment pathway
    • Skepper, J. N., A. Whiteley, H. Browne, and A. Minson. 2001. Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment→deenvelopment→reenvelopment pathway. J. Virol. 75:5697-5702.
    • (2001) J. Virol , vol.75 , pp. 5697-5702
    • Skepper, J.N.1    Whiteley, A.2    Browne, H.3    Minson, A.4
  • 68
    • 0026537536 scopus 로고
    • Identification and characterization of the virion-induced host shutoff product of herpes simplex virus gene UL41
    • Smibert, C. A., D. C. Johnson, and J. R. Smiley. 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
  • 69
    • 0028289280 scopus 로고
    • Herpes simplex virus VP16 forms a complex with the virion host shutoff protein Vhs
    • Smibert, C. A., B. Popova, P. Xiao, J. P. Capone, and J. R. Smiley. 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
  • 70
    • 0025866616 scopus 로고
    • Analysis of herpes simplex virus-induced mRNA destabilizing activity using an in vitro mRNA decay system
    • Sorenson, C. M., P. A. Hart, and J. Ross. 1991. Analysis of herpes simplex virus-induced 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
  • 71
    • 0020690955 scopus 로고
    • Characterization of herpes simplex virus 2 temperature-sensitive mutants whose lesions map in or near the coding sequences for the major DNA-binding protein
    • Spang, A. E., P. J. Godowski, and D. M. Knipe. 1983. Characterization of herpes simplex virus 2 temperature-sensitive mutants whose lesions map in or near the coding sequences for the major DNA-binding protein. J. Virol. 45:332-342.
    • (1983) J. Virol , vol.45 , pp. 332-342
    • Spang, A.E.1    Godowski, P.J.2    Knipe, D.M.3
  • 72
    • 0015253192 scopus 로고
    • Proteins specified by herpes simplex virus. V. Purification and structural proteins of the herpesvirion
    • Spear, P. G., and B. Roizman. 1972. Proteins specified by herpes simplex virus. V. Purification and structural proteins of the herpesvirion. J. Virol. 9:143-159.
    • (1972) J. Virol , vol.9 , pp. 143-159
    • Spear, P.G.1    Roizman, B.2
  • 73
    • 0023182175 scopus 로고
    • Effects of herpes simplex virus on mRNA stability
    • Strom, T., and N. Frenkel. 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
  • 74
    • 0026100629 scopus 로고
    • Identification and characterization of a novel non-infectious herpes simplex virus-related particle
    • Szilagyi, J. F., and C. Cunningham. 1991. Identification and characterization of a novel non-infectious herpes simplex virus-related particle. J. Gen. Virol. 72:661-668.
    • (1991) J. Gen. Virol , vol.72 , pp. 661-668
    • Szilagyi, J.F.1    Cunningham, C.2
  • 75
    • 8744299600 scopus 로고    scopus 로고
    • Post-transcriptional processing of cellular RNAs in herpes simplex virus-infected cells
    • Taddeo, B., A. Esclatine, and B. Roizman. 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
  • 76
    • 0037689355 scopus 로고    scopus 로고
    • The stress-inducible 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., A. Esclatine, W. Zhang, and B. Roizman. 2003. The stress-inducible 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
  • 77
    • 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., W. Zhang, and B. Roizman. 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. USA 103:2827-2832.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2827-2832
    • Taddeo, B.1    Zhang, W.2    Roizman, B.3
  • 78
    • 10644290789 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 DNA-packaging protein UL17 is a virion protein that is present in both the capsid and the tegument compartments
    • Thurlow, J. K., F. J. Rixon, M. Murphy, P. Targett-Adams, M. Hughes, and V. G. Preston. 2005. The herpes simplex virus type 1 DNA-packaging protein UL17 is a virion protein that is present in both the capsid and the tegument compartments. J. Virol. 79:150-158.
    • (2005) J. Virol , vol.79 , pp. 150-158
    • Thurlow, J.K.1    Rixon, F.J.2    Murphy, M.3    Targett-Adams, P.4    Hughes, M.5    Preston, V.G.6
  • 79
    • 0032829388 scopus 로고    scopus 로고
    • Effects of targeting herpes simplex virus type 1 gD to the endoplasmic reticulum and trans-Golgi network
    • Whiteley, A., B. Bruun, T. Minson, and H. Browne. 1999. Effects of targeting herpes simplex virus type 1 gD to the endoplasmic reticulum and trans-Golgi network. J. Virol. 73:9515-9520.
    • (1999) J. Virol , vol.73 , pp. 9515-9520
    • Whiteley, A.1    Bruun, B.2    Minson, T.3    Browne, H.4
  • 80
    • 0026002792 scopus 로고
    • Analysis with specific polyclonal antiserum indicates that the E1A-associated 300-kDa product is a stable nuclear phosphoprotein that undergoes cell cycle phase-specific modification
    • Yaciuk, P., and E. Moran. 1991. Analysis with specific polyclonal antiserum indicates that the E1A-associated 300-kDa product is a stable nuclear phosphoprotein that undergoes cell cycle phase-specific modification. Mol. Cell. Biol. 11:5389-5397.
    • (1991) Mol. Cell. Biol , vol.11 , pp. 5389-5397
    • Yaciuk, P.1    Moran, E.2
  • 81
    • 0024412055 scopus 로고
    • A major transcriptional regulatory protein (ICP4) of herpes simplex virus type 1 is associated with purified virions
    • Yao, F., and R. J. Courtney. 1989. A major transcriptional regulatory protein (ICP4) of herpes simplex virus type 1 is associated with purified virions. J. Virol. 63:3338-3344.
    • (1989) J. Virol , vol.63 , pp. 3338-3344
    • Yao, F.1    Courtney, R.J.2
  • 82
    • 0026552585 scopus 로고
    • Association of ICP0 but not ICP27 with purified virions of herpes simplex virus type 1
    • Yao, F., and R. J. Courtney. 1992. Association of ICP0 but not ICP27 with purified virions of herpes simplex virus type 1. J. Virol. 66:2709-2716.
    • (1992) J. Virol , vol.66 , pp. 2709-2716
    • Yao, F.1    Courtney, R.J.2
  • 83
    • 4644303568 scopus 로고    scopus 로고
    • Nucleocytoplasmic glycosylation, O-GlcNAc: Identification and site mapping
    • Zachara, N. E., W. D. Cheung, and G. W. Hart. 2004. Nucleocytoplasmic glycosylation, O-GlcNAc: identification and site mapping. Methods Mol. Biol. 284:175-194.
    • (2004) Methods Mol. Biol , vol.284 , pp. 175-194
    • Zachara, N.E.1    Cheung, W.D.2    Hart, G.W.3
  • 84
    • 3042613480 scopus 로고    scopus 로고
    • O-GlcNAc, a sensor of cellular state: The role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress
    • Zachara, N. E., and G. W. Hart. 2004. O-GlcNAc, a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress. Biochim. Biophys. Acta 1673:13-28.
    • (2004) Biochim. Biophys. Acta , vol.1673 , pp. 13-28
    • Zachara, N.E.1    Hart, G.W.2
  • 85
    • 33745272509 scopus 로고    scopus 로고
    • Cell signaling, the essential role of O-GlcNAc!
    • Zachara, N. E., and G. W. Hart. 2006. Cell signaling, the essential role of O-GlcNAc! Biochim. Biophys. Acta 1761:599-617.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 599-617
    • Zachara, N.E.1    Hart, G.W.2
  • 86
    • 3042534011 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells
    • Zachara, N. E., N. O'Donnell, W. D. Cheung, J. J. Mercer, J. D. Marth, and G. W. Hart. 2004. Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells. J. Biol. Chem. 279:30133-30142.
    • (2004) J. Biol. Chem , vol.279 , pp. 30133-30142
    • Zachara, N.E.1    O'Donnell, N.2    Cheung, W.D.3    Mercer, J.J.4    Marth, J.D.5    Hart, G.W.6
  • 87
    • 0029919184 scopus 로고    scopus 로고
    • The virion host shutoff protein of herpes simplex virus type 1: Messenger ribonucleolytic activity in vitro
    • Zelus, B. D., R. S. Stewart, and J. Ross. 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
  • 88
    • 0027476811 scopus 로고
    • Herpes simplex virus type 1 UL46 and UL47 deletion mutants lack VP11 and VP12 or VP13 and VP14, respectively, and exhibit altered viral thymidine kinase expression
    • Zhang, Y., and J. L. McKnight. 1993. Herpes simplex virus type 1 UL46 and UL47 deletion mutants lack VP11 and VP12 or VP13 and VP14, respectively, and exhibit altered viral thymidine kinase expression. J. Virol. 67:1482-1492.
    • (1993) J. Virol , vol.67 , pp. 1482-1492
    • Zhang, Y.1    McKnight, J.L.2


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