메뉴 건너뛰기




Volumn 77, Issue 23, 2003, Pages 12671-12678

Herpes Simplex Virus 1 Gene Expression Is Accelerated by Inhibitors of Histone Deacetylases in Rabbit Skin Cells Infected with a Mutant Carrying a cDNA Copy of the Infected-Cell Protein No. 0

Author keywords

[No Author keywords available]

Indexed keywords

BUTYRIC ACID; COMPLEMENTARY DNA; HISTONE DEACETYLASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 3; HISTONE DEACETYLASE INHIBITOR; INFECTED CELL PROTEIN NO. 0; MYCOTOXIN; PROTEIN KINASE; TRICHOSTATIN A; UNCLASSIFIED DRUG; US3 PROTEIN KINASE; VIRUS DNA; VIRUS PROTEIN;

EID: 0242661003     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.77.23.12671-12678.2003     Document Type: Article
Times cited : (80)

References (57)
  • 1
    • 0022346795 scopus 로고
    • Application of antibody to synthetic peptides for characterization of the intact and truncated α22 protein specified by herpes simplex virus 1 and the R325 α22-deletion mutant
    • Ackermann, M., M. Sarmiento, and B. Roizman. 1985. Application of antibody to synthetic peptides for characterization of the intact and truncated α22 protein specified by herpes simplex virus 1 and the R325 α22-deletion mutant. J. Virol. 56:207-215.
    • (1985) J. Virol. , vol.56 , pp. 207-215
    • Ackermann, M.1    Sarmiento, M.2    Roizman, B.3
  • 2
    • 0036138854 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein ICP0 and its isolated RING finger domain act as ubiquitin E3 ligases in vitro
    • Boutell, C., S. Sadis, and R. D. Everett. 2002. Herpes simplex virus type 1 immediate-early protein ICP0 and its isolated RING finger domain act as ubiquitin E3 ligases in vitro. J. Virol. 76:841-850.
    • (2002) J. Virol. , vol.76 , pp. 841-850
    • Boutell, C.1    Sadis, S.2    Everett, R.D.3
  • 3
    • 0036786424 scopus 로고    scopus 로고
    • Signal transduction and transcription factor modification during reactivation of Epstein-Barr virus from latency
    • Bryant, H., and P. J. Farrell. 2002. Signal transduction and transcription factor modification during reactivation of Epstein-Barr virus from latency. J. Virol. 76:10290-10298.
    • (2002) J. Virol. , vol.76 , pp. 10290-10298
    • Bryant, H.1    Farrell, P.J.2
  • 4
    • 0037941647 scopus 로고    scopus 로고
    • PML mediates interferon-based anti-herpes simplex virus 1 effects
    • Chee, A. V., P. Lopez, P. P. Pandolfi, and B. Roizman. 2003. PML mediates interferon-based anti-herpes simplex virus 1 effects. J. Virol. 77:7101-7105.
    • (2003) J. Virol. , vol.77 , pp. 7101-7105
    • Chee, A.V.1    Lopez, P.2    Pandolfi, P.P.3    Roizman, B.4
  • 5
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasome-dependent degradation of the nuclear body-associated PML and Sp100 proteins
    • Chelbi-Alix, M. K., and H. de The. 1999. Herpes virus induced proteasome-dependent degradation of the nuclear body-associated PML and Sp100 proteins. Oncogene 18:935-941.
    • (1999) Oncogene , vol.18 , pp. 935-941
    • Chelbi-Alix, M.K.1    De The, H.2
  • 6
    • 0037189568 scopus 로고    scopus 로고
    • SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities
    • David, G., M. A. Neptune, and R. A. DePinho. 2002. SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities. J. Biol. Chem. 277:23658-23663.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23658-23663
    • David, G.1    Neptune, M.A.2    DePinho, R.A.3
  • 7
    • 0024555760 scopus 로고
    • During latency, herpes simplex virus type 1 DNA is associated with nucleosomes in a chromatin structure
    • Deshmane, S. L., and N. W. Fraser. 1989. During latency, herpes simplex virus type 1 DNA is associated with nucleosomes in a chromatin structure. J. Virol. 63:943-947.
    • (1989) J. Virol. , vol.63 , pp. 943-947
    • Deshmane, S.L.1    Fraser, N.W.2
  • 8
    • 0014286962 scopus 로고
    • Characterization of herpes simplex virus strains differing in their effects on social behavior of infected cells
    • Ejercito, P., E. D. Kieff, and B. Roizman. 1968. Characterization of herpes simplex virus strains differing in their effects on social behavior of infected cells. J. Gen. Virol. 2:357-364.
    • (1968) J. Gen. Virol. , vol.2 , pp. 357-364
    • Ejercito, P.1    Kieff, E.D.2    Roizman, B.3
  • 9
    • 0021767941 scopus 로고
    • Transactivation of transcription by herpes virus products: Requirement for two HSV-1 immediate-early polypeptides for maximum activity
    • Everett, R. D. 1984. Transactivation of transcription by herpes virus products: requirement for two HSV-1 immediate-early polypeptides for maximum activity. EMBO J. 3:3135-3141.
    • (1984) EMBO J. , vol.3 , pp. 3135-3141
    • Everett, R.D.1
  • 10
    • 0033559253 scopus 로고    scopus 로고
    • Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110
    • Everett, R. D., W. C. Earnshaw, J. Findlay, and P. Lomonte. 1999. Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110. EMBO J. 18:1526-1538.
    • (1999) EMBO J. , vol.18 , pp. 1526-1538
    • Everett, R.D.1    Earnshaw, W.C.2    Findlay, J.3    Lomonte, P.4
  • 11
    • 0031878851 scopus 로고    scopus 로고
    • The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms
    • Everett, R. D., P. Freemont, P., H. Saitoh, M. Dasso, A. Orr, M. Kathoria, and J. Parkinson. 1998. The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J. Virol. 72:6581-6591.
    • (1998) J. Virol. , vol.72 , pp. 6581-6591
    • Everett, R.D.1    Freemont, P.2    Saitoh, H.3    Dasso, M.4    Orr, A.5    Kathoria, M.6    Parkinson, J.7
  • 12
    • 0028039189 scopus 로고
    • HSV-1 IE protein Vmw 110 causes redistribution of PML
    • Everett, R. D., and G. G. Maul. 1994. HSV-1 IE protein Vmw 110 causes redistribution of PML. EMBO J. 13:5062-5069.
    • (1994) EMBO J. , vol.13 , pp. 5062-5069
    • Everett, R.D.1    Maul, G.G.2
  • 13
    • 0030895008 scopus 로고    scopus 로고
    • A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein
    • Everett, R. D., M. Meredith, A. Orr, A. Cross, M. Kathoria, and J. Parkinson. 1997. A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein. EMBO J. 16:566-577.
    • (1997) EMBO J. , vol.16 , pp. 566-577
    • Everett, R.D.1    Meredith, M.2    Orr, A.3    Cross, A.4    Kathoria, M.5    Parkinson, J.6
  • 14
    • 0021847819 scopus 로고
    • Identification of immediate early genes from herpes simplex virus that transactivate the virus thymidine kinase gene
    • Gelman, I. H., and S. Silverstein. 1985. Identification of immediate early genes from herpes simplex virus that transactivate the virus thymidine kinase gene. Proc. Natl. Acad. Sci. USA 82:5265-5269.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5265-5269
    • Gelman, I.H.1    Silverstein, S.2
  • 15
    • 0015156237 scopus 로고
    • Compartmentalization of spermine and spermidine in the herpes simplex virion
    • Gibson, W., and B. Roizman. 1971. Compartmentalization of spermine and spermidine in the herpes simplex virion. Proc. Natl. Acad. Sci. USA 68:2818-2821.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2818-2821
    • Gibson, W.1    Roizman, B.2
  • 16
    • 0035136167 scopus 로고    scopus 로고
    • CREB-binding protein and histone deacetylase regulate the transcriptional activity of Kaposi's sarcoma-associated herpesvirus open reading frame 60
    • Gwack, Y., H. Byan, S. Hwang, C. Lim, and J. Cloe. 2001. CREB-binding protein and histone deacetylase regulate the transcriptional activity of Kaposi's sarcoma-associated herpesvirus open reading frame 60. J. Virol. 75: 1909-1917.
    • (2001) J. Virol. , vol.75 , pp. 1909-1917
    • Gwack, Y.1    Byan, H.2    Hwang, S.3    Lim, C.4    Cloe, J.5
  • 17
    • 0037062483 scopus 로고    scopus 로고
    • Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-l-infected cell protein 0
    • Hagglund, R., and B. Roizman. 2002. Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-l-infected cell protein 0. Proc. Natl. Acad. Sci. USA 99:7889-7894.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7889-7894
    • Hagglund, R.1    Roizman, B.2
  • 18
    • 0037154225 scopus 로고    scopus 로고
    • Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin conjugating enzymes
    • Hagglund, R., C. Van Sant, P. Lopez, and B. Roizman. 2002. Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin conjugating enzymes. Proc. Natl. Acad. Sci. USA 99:631-666.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 631-666
    • Hagglund, R.1    Van Sant, C.2    Lopez, P.3    Roizman, B.4
  • 19
    • 0036261558 scopus 로고    scopus 로고
    • Chromatin disruption and histone acetylation in regulation of the human immunodeficiency virus type 1 long terminal repeat by thyroid hormone receptor
    • Hsia, S.-C. V., and Y.-B. Shi. 2002. Chromatin disruption and histone acetylation in regulation of the human immunodeficiency virus type 1 long terminal repeat by thyroid hormone receptor. Mol. Cell. Biol. 22:4043-4052.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4043-4052
    • Hsia, S.-C.V.1    Shi, Y.-B.2
  • 20
    • 0029045486 scopus 로고
    • Quiescent viral genomes in human fibroblasts after infection with herpes simplex virus type 1 Vmw65 mutants
    • Jamieson, D. R., L. H. Robinson, J. I. Daksis, M. J. Nicholl, and C. M. Preston. 1985. Quiescent viral genomes in human fibroblasts after infection with herpes simplex virus type 1 Vmw65 mutants. J. Gen. Virol. 76:1417-1431.
    • (1985) J. Gen. Virol. , vol.76 , pp. 1417-1431
    • Jamieson, D.R.1    Robinson, L.H.2    Daksis, J.I.3    Nicholl, M.J.4    Preston, C.M.5
  • 21
    • 0031014985 scopus 로고    scopus 로고
    • Interaction of herpes simplex virus 1 α regulatory protein ICP0 with elongation factor 18: ICP0 affects translational machinery
    • Kawaguchi, Y., R. Bruni, and B. Roizman. 1997. Interaction of herpes simplex virus 1 α regulatory protein ICP0 with elongation factor 18: ICP0 affects translational machinery. J. Virol. 71:1019-1024.
    • (1997) J. Virol. , vol.71 , pp. 1019-1024
    • Kawaguchi, Y.1    Bruni, R.2    Roizman, B.3
  • 23
    • 0030820342 scopus 로고    scopus 로고
    • Herpes simplex virus 1 α regulatory protein ICP0 interacts with and stabilizes the cell cycle regulator cyclin D3
    • Kawaguchi, Y., C. Van Sant, and B. Roizman. 1997. Herpes simplex virus 1 α regulatory protein ICP0 interacts with and stabilizes the cell cycle regulator cyclin D3. J. Virol. 71:7328-7336.
    • (1997) J. Virol. , vol.71 , pp. 7328-7336
    • Kawaguchi, Y.1    Van Sant, C.2    Roizman, B.3
  • 24
    • 0033573922 scopus 로고    scopus 로고
    • Nuclear localization of the C1 factor (HCF) in sensory neurons correlates with reactivation of HSV from latency
    • Kristie, T. M., J. L. Vogel, and A. E. Sears. 1999. Nuclear localization of the C1 factor (HCF) in sensory neurons correlates with reactivation of HSV from latency. Proc. Natl. Acad. Sci. USA 96:1229-1233.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1229-1233
    • Kristie, T.M.1    Vogel, J.L.2    Sears, A.E.3
  • 25
    • 0019136475 scopus 로고
    • The structure of herpes simplex virus type 1 DNA as probed by micrococcal nuclease digestion
    • Leinbach, S. S., and W. C. Summers. 1980. The structure of herpes simplex virus type 1 DNA as probed by micrococcal nuclease digestion. J. Gen. Virol. 51:45-59.
    • (1980) J. Gen. Virol. , vol.51 , pp. 45-59
    • Leinbach, S.S.1    Summers, W.C.2
  • 27
    • 0035937114 scopus 로고    scopus 로고
    • Degradation of nucleosome-associated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0
    • Lomonte, P., K. F. Sullivan, and R. D. Everett. 2001. Degradation of nucleosome-associated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0. J. Biol. Chem. 276:5829-5835.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5829-5835
    • Lomonte, P.1    Sullivan, K.F.2    Everett, R.D.3
  • 28
    • 0036720433 scopus 로고    scopus 로고
    • Overexpression of promyelocytic leukemia protein precludes the dispersal of ND10 structures and has no effect on accumulation of infectious herpes simplex virus 1 or its proteins
    • Lopez, P., R. J. Jacob, and B. Roizman. 2002. Overexpression of promyelocytic leukemia protein precludes the dispersal of ND10 structures and has no effect on accumulation of infectious herpes simplex virus 1 or its proteins. J. Virol. 76:9355-9367.
    • (2002) J. Virol. , vol.76 , pp. 9355-9367
    • Lopez, P.1    Jacob, R.J.2    Roizman, B.3
  • 29
    • 0035082275 scopus 로고    scopus 로고
    • Requirements for the nuclear-cytoplasmic translocation of infected-cell protein 0 of herpes simplex virus 1
    • Lopez, P., C. Van Sant, and B. Roizman. 2001. Requirements for the nuclear-cytoplasmic translocation of infected-cell protein 0 of herpes simplex virus 1. J. Virol. 75:3832-3840.
    • (2001) J. Virol. , vol.75 , pp. 3832-3840
    • Lopez, P.1    Van Sant, C.2    Roizman, B.3
  • 30
    • 0028352769 scopus 로고
    • The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0
    • Maul, G. G., and R. D. Everett. 1994. The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0. J. Gen. Virol. 75:1223-1233.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1223-1233
    • Maul, G.G.1    Everett, R.D.2
  • 31
    • 0027769358 scopus 로고
    • Modification of discrete nuclear domains induced by herpes simplex virus type-1 immediate early gene-1 product (ICP0)
    • Maul, G. G., H. H. Guldner, and J. G. Spivack. 1993. Modification of discrete nuclear domains induced by herpes simplex virus type-1 immediate early gene-1 product (ICP0). J. Gen. Virol. 74:2679-2690.
    • (1993) J. Gen. Virol. , vol.74 , pp. 2679-2690
    • Maul, G.G.1    Guldner, H.H.2    Spivack, J.G.3
  • 32
    • 0029013765 scopus 로고
    • Separation of sequence requirements for HSV-1 Vmw110 multimerisation and interaction with a 135-kDa cellular protein
    • Meredith, M., A. Orr, M. Elliott, and R. D. Everett. 1995. Separation of sequence requirements for HSV-1 Vmw110 multimerisation and interaction with a 135-kDa cellular protein. Virology 209:174-187.
    • (1995) Virology , vol.209 , pp. 174-187
    • Meredith, M.1    Orr, A.2    Elliott, M.3    Everett, R.D.4
  • 33
    • 0028268666 scopus 로고
    • Herpes simplex virus type 1 immediate-early protein Vmw110 binds strongly and specifically to a 135-kDa cellular protein
    • Meredith, M., A. Orr, and R. D. Everett. 1994. Herpes simplex virus type 1 immediate-early protein Vmw110 binds strongly and specifically to a 135-kDa cellular protein. Virology 200:457-469.
    • (1994) Virology , vol.200 , pp. 457-469
    • Meredith, M.1    Orr, A.2    Everett, R.D.3
  • 34
    • 0022521909 scopus 로고
    • Chromosomal organization of the herpes simplex virus genome during acute infection of the mouse central nervous system
    • Muggeridge, M. I., and N. W. Fraser. 1986. Chromosomal organization of the herpes simplex virus genome during acute infection of the mouse central nervous system. J. Virol. 59:764-767.
    • (1986) J. Virol. , vol.59 , pp. 764-767
    • Muggeridge, M.I.1    Fraser, N.W.2
  • 35
    • 0036500165 scopus 로고    scopus 로고
    • Control of cytomegalovirus lytic gene expression by histone acetylation
    • Murphy, J. C., W. Fischle, E. Verdin, and J. H. Sinclair. 2002. Control of cytomegalovirus lytic gene expression by histone acetylation. EMBO J. 21: 1112-1120,
    • (2002) EMBO J. , vol.21 , pp. 1112-1120
    • Murphy, J.C.1    Fischle, W.2    Verdin, E.3    Sinclair, J.H.4
  • 37
    • 0021984653 scopus 로고
    • Evidence for a direct role for both the 175,000- and 110,000-molecular-weight immediate-early proteins of herpes simplex virus in the transactivation of delayed-early promoters
    • O'Hare, P., and G. S. Hayward. 1985. Evidence for a direct role for both the 175,000- and 110,000-molecular-weight immediate-early proteins of herpes simplex virus in the transactivation of delayed-early promoters. J. Virol. 53:751-760.
    • (1985) J. Virol. , vol.53 , pp. 751-760
    • O'Hare, P.1    Hayward, G.S.2
  • 38
    • 0031022820 scopus 로고    scopus 로고
    • Physical and functional interactions between herpes simplex virus immediate-early proteins ICP4 and ICP27
    • Panagiotidis, C. A., E. K. Lium, and S. J. Silverstein. 1997. Physical and functional interactions between herpes simplex virus immediate-early proteins ICP4 and ICP27. J. Virol. 71:1547-1557.
    • (1997) J. Virol. , vol.71 , pp. 1547-1557
    • Panagiotidis, C.A.1    Lium, E.K.2    Silverstein, S.J.3
  • 39
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription?
    • Pazin, M. J., and J. T. Kadonaga. 1997. What's up and down with histone deacetylation and transcription? Cell 89:325-328.
    • (1997) Cell , vol.89 , pp. 325-328
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 40
    • 0035861594 scopus 로고    scopus 로고
    • Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation
    • Pflum, M. K. H., J. K. Tong, W. S. Lane, and S. L. Schreiber. 2001. Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation. J. Biol. Chem. 276:47733-47741.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47733-47741
    • Pflum, M.K.H.1    Tong, J.K.2    Lane, W.S.3    Schreiber, S.L.4
  • 41
    • 0034468077 scopus 로고    scopus 로고
    • Posttranslational processing of infected-cell protein 22 mediated by viral protein kinases is sensitive to amino acid substitutions at distant sites and can be cell type specific
    • Poon, A. P. W., W. O. Ogle, and B. Roizman. 2000. Posttranslational processing of infected-cell protein 22 mediated by viral protein kinases is sensitive to amino acid substitutions at distant sites and can be cell type specific. J. Virol. 74:11210-11214.
    • (2000) J. Virol. , vol.74 , pp. 11210-11214
    • Poon, A.P.W.1    Ogle, W.O.2    Roizman, B.3
  • 42
    • 0031550784 scopus 로고    scopus 로고
    • 134.5 genes of herpes simplex virus 1
    • 134.5 genes of herpes simplex virus 1. Virology 229:98-105.
    • (1997) Virology , vol.229 , pp. 98-105
    • Poon, A.P.W.1    Roizman, B.2
  • 43
    • 0036776322 scopus 로고    scopus 로고
    • An early regulatory function required in cell-type-dependent manner is expressed by the genomic but not by the cDNA copy of the herpes simplex virus 1 gene encoding the infected-cell protein no. 0
    • Poon, A. P. W., S. J. Silverstein., and B. Roizman. 2002. An early regulatory function required in cell-type-dependent manner is expressed by the genomic but not by the cDNA copy of the herpes simplex virus 1 gene encoding the infected-cell protein no. 0. J. Virol. 76:9744-9755.
    • (2002) J. Virol. , vol.76 , pp. 9744-9755
    • Poon, A.P.W.1    Silverstein, S.J.2    Roizman, B.3
  • 45
    • 0027323128 scopus 로고
    • L13 protein kinase determines the accumulation of a subset of α and γ mRNAs and proteins in infected cells
    • L13 protein kinase determines the accumulation of a subset of α and γ mRNAs and proteins in infected cells. Proc. Natl. Acad. Sci. USA 90:6701-6705.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6701-6705
    • Purves, F.C.1    Ogle, W.O.2    Roizman, B.3
  • 46
    • 0026611071 scopus 로고
    • The UL13 gene of herpes simplex virus 1 encodes the functions for posttranslational processing associated with phosphorylation of the regulatory protein α22
    • Purves, F. C., and B. Roizman. 1992. The UL13 gene of herpes simplex virus 1 encodes the functions for posttranslational processing associated with phosphorylation of the regulatory protein α22. Proc. Natl. Acad. Sci. USA 89:7310-7314.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7310-7314
    • Purves, F.C.1    Roizman, B.2
  • 47
    • 0001142641 scopus 로고    scopus 로고
    • The replication of herpes simplex viruses
    • D. M. Knipe, P. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.). Lippincott-Williams and Wilkins, New York, N.Y.
    • Roizman, B., and D. M. Knipe. 2001. The replication of herpes simplex viruses, p. 2399-2459. In D. M. Knipe, P. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Fields virology, 4th ed. Lippincott-Williams and Wilkins, New York, N.Y.
    • (2001) Fields Virology, 4th Ed. , pp. 2399-2459
    • Roizman, B.1    Knipe, D.M.2
  • 48
    • 0026719341 scopus 로고
    • S11 is a virion component and associates with ribosomal 60S subunits
    • S11 is a virion component and associates with ribosomal 60S subunits. J. Virol. 66:3624-3632.
    • (1992) J. Virol. , vol.66 , pp. 3624-3632
    • Roller, R.J.1    Roizman, B.2
  • 49
    • 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
  • 50
    • 0022978685 scopus 로고
    • Isolation and characterization of a herpes simplex virus type 1 mutant containing a deletion within the gene encoding the immediate early polypeptide Vmw110
    • Stow, N. D., and E. C. Stow. 1986. Isolation and characterization of a herpes simplex virus type 1 mutant containing a deletion within the gene encoding the immediate early polypeptide Vmw110. J. Gen. Virol. 67:2571-2585.
    • (1986) J. Gen. Virol. , vol.67 , pp. 2571-2585
    • Stow, N.D.1    Stow, E.C.2
  • 51
    • 0037199944 scopus 로고    scopus 로고
    • Regulation of histone deacetylase 2 by protein kinase CK2
    • Tsai, S.-C., and E. Seto. 2002. Regulation of histone deacetylase 2 by protein kinase CK2. J. Biol. Chem. 277:31826-31833.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31826-31833
    • Tsai, S.-C.1    Seto, E.2
  • 52
    • 0035902533 scopus 로고    scopus 로고
    • The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin conjugating enzyme and possesses in vitro E3 ubiquitin ligase activity
    • Van Sant, C., R. Hagglund, P. Lopez, and B. Roizman. 2001. The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin conjugating enzyme and possesses in vitro E3 ubiquitin ligase activity. Proc. Natl. Acad. Sci. USA 98:8815-8820.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8815-8820
    • Van Sant, C.1    Hagglund, R.2    Lopez, P.3    Roizman, B.4
  • 53
    • 0033529219 scopus 로고    scopus 로고
    • A single amino acid substitution in the cyclin D binding domain of the infected cell protein no. 0 abrogates the neuroinvasiveness of herpes simplex virus without affecting its ability to replicate
    • Van Sant, C., Y. Kawaguchi, and B. Roizman. 1999. A single amino acid substitution in the cyclin D binding domain of the infected cell protein no. 0 abrogates the neuroinvasiveness of herpes simplex virus without affecting its ability to replicate. Proc. Natl. Acad. Sci. USA 96:8184-8189.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8184-8189
    • Van Sant, C.1    Kawaguchi, Y.2    Roizman, B.3
  • 54
    • 0035133052 scopus 로고    scopus 로고
    • Role of cyclin D3 in the biology of herpes simplex virus 1 ICP0
    • Van Sant, C., P. Lopez, S. J. Advani, and B. Roizman. 2001. Role of cyclin D3 in the biology of herpes simplex virus 1 ICP0. J. Virol. 75:1888-1898.
    • (2001) J. Virol. , vol.75 , pp. 1888-1898
    • Van Sant, C.1    Lopez, P.2    Advani, S.J.3    Roizman, B.4
  • 55
    • 0030922545 scopus 로고    scopus 로고
    • Transcriptional control. Sinful repression
    • Wolffe, A. P. 1997. Transcriptional control. Sinful repression. Nature 387: 16-17.
    • (1997) Nature , vol.387 , pp. 16-17
    • Wolffe, A.P.1
  • 56
    • 0029102140 scopus 로고
    • An activity specified by the osteosarcoma line U2OS can substitute functionally for ICP0, a major regulatory protein of herpes simplex virus type 1
    • Yao, F., and P. A. Schaffer. 1995. An activity specified by the osteosarcoma line U2OS can substitute functionally for ICP0, a major regulatory protein of herpes simplex virus type 1. J. Virol. 69:6249-6258.
    • (1995) J. Virol. , vol.69 , pp. 6249-6258
    • Yao, F.1    Schaffer, P.A.2
  • 57
    • 0034812721 scopus 로고    scopus 로고
    • The bovine herpesvirus 1 immediate-early protein (bICP0) associates with histone deacetylase 1 to activate transcription
    • Zhang Y., and C. Jones. 2001. The bovine herpesvirus 1 immediate-early protein (bICP0) associates with histone deacetylase 1 to activate transcription. J. Virol. 75:9571-9578.
    • (2001) J. Virol. , vol.75 , pp. 9571-9578
    • Zhang, Y.1    Jones, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.