메뉴 건너뛰기




Volumn 352, Issue 1, 2006, Pages 237-252

Herpes simplex virus regulatory proteins VP16 and ICP0 counteract an innate intranuclear barrier to viral gene expression

Author keywords

Cell fusion; Herpes simplex virus; ICP0; Innate immunity; Reovirus p14; Somatic cell hybrid; VP16

Indexed keywords

ICP0 PROTEIN; PROTEIN VP16; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 33746580534     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2006.04.021     Document Type: Article
Times cited : (29)

References (98)
  • 1
    • 0024536120 scopus 로고
    • Construction and characterization of a herpes simplex virus type 1 mutant unable to transinduce immediate-early gene expression
    • Ace C.I., McKee T.A., Ryan J.M., Cameron J.M., and Preston C.M. Construction and characterization of a herpes simplex virus type 1 mutant unable to transinduce immediate-early gene expression. J. Virol. 63 5 (1989) 2260-2269
    • (1989) J. Virol. , vol.63 , Issue.5 , pp. 2260-2269
    • Ace, C.I.1    McKee, T.A.2    Ryan, J.M.3    Cameron, J.M.4    Preston, C.M.5
  • 2
    • 0036852215 scopus 로고    scopus 로고
    • To kill or be killed: viral evasion of apoptosis
    • Benedict C.A., Norris P.S., and Ware C.F. To kill or be killed: viral evasion of apoptosis. Nat. Immunol. 3 11 (2002) 1013-1018
    • (2002) Nat. Immunol. , vol.3 , Issue.11 , pp. 1013-1018
    • Benedict, C.A.1    Norris, P.S.2    Ware, C.F.3
  • 3
    • 0036138854 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein ICP0 and is isolated RING finger domain act as ubiquitin E3 ligases in vitro
    • Boutell C., Sadis S., and Everett R.D. Herpes simplex virus type 1 immediate-early protein ICP0 and is isolated RING finger domain act as ubiquitin E3 ligases in vitro. J. Virol. 76 2 (2002) 841-850
    • (2002) J. Virol. , vol.76 , Issue.2 , pp. 841-850
    • Boutell, C.1    Sadis, S.2    Everett, R.D.3
  • 4
    • 0026533363 scopus 로고
    • Herpes simplex virus type 1 ICP0 regulates expression of immediate-early, early, and late genes in productively infected cells
    • Cai W., and Schaffer P.A. Herpes simplex virus type 1 ICP0 regulates expression of immediate-early, early, and late genes in productively infected cells. J. Virol. 66 5 (1992) 2904-2915
    • (1992) J. Virol. , vol.66 , Issue.5 , pp. 2904-2915
    • Cai, W.1    Schaffer, P.A.2
  • 5
    • 0027361738 scopus 로고
    • The herpes simplex virus type 1 regulatory protein ICP0 enhances virus replication during acute infection and reactivation from latency
    • Cai W., Astor T.L., Liptak L.M., Cho C., Coen D.M., and Schaffer P.A. The herpes simplex virus type 1 regulatory protein ICP0 enhances virus replication during acute infection and reactivation from latency. J. Virol. 67 12 (1993) 7501-7512
    • (1993) J. Virol. , vol.67 , Issue.12 , pp. 7501-7512
    • Cai, W.1    Astor, T.L.2    Liptak, L.M.3    Cho, C.4    Coen, D.M.5    Schaffer, P.A.6
  • 6
    • 0037941647 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein mediates interferon-based anti-herpes simplex virus 1 effects
    • Chee A.V., Lopez P., Pandolfi P.P., and Roizman B. Promyelocytic leukemia protein mediates interferon-based anti-herpes simplex virus 1 effects. J. Virol. 77 12 (2003) 7101-7105
    • (2003) J. Virol. , vol.77 , Issue.12 , pp. 7101-7105
    • Chee, A.V.1    Lopez, P.2    Pandolfi, P.P.3    Roizman, B.4
  • 7
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins
    • Chelbi-Alix M.K., and de The H. Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene 18 4 (1999) 935-941
    • (1999) Oncogene , vol.18 , Issue.4 , pp. 935-941
    • Chelbi-Alix, M.K.1    de The, H.2
  • 8
    • 0028970730 scopus 로고
    • Association of a M (r) 90,000 phosphoprotein with protein kinase PKR in cells exhibiting enhanced phosphorylation of translation initiation factor eIF-2 alpha and premature shutoff of protein synthesis after infection with gamma 134.5-mutants of herpes simplex virus 1
    • Chou J., Chen J.J., Gross M., and Roizman B. Association of a M (r) 90,000 phosphoprotein with protein kinase PKR in cells exhibiting enhanced phosphorylation of translation initiation factor eIF-2 alpha and premature shutoff of protein synthesis after infection with gamma 134.5-mutants of herpes simplex virus 1. Proc. Natl. Acad. Sci. U.S.A. 92 23 (1995) 10516-10520
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , Issue.23 , pp. 10516-10520
    • Chou, J.1    Chen, J.J.2    Gross, M.3    Roizman, B.4
  • 9
    • 1842483912 scopus 로고    scopus 로고
    • Reptilian reovirus utilizes a small type III protein with an external myristylated amino terminus to mediate cell-cell fusion
    • Corcoran J.A., and Duncan R. Reptilian reovirus utilizes a small type III protein with an external myristylated amino terminus to mediate cell-cell fusion. J. Virol. 78 8 (2004) 4342-4351
    • (2004) J. Virol. , vol.78 , Issue.8 , pp. 4342-4351
    • Corcoran, J.A.1    Duncan, R.2
  • 11
    • 0027514853 scopus 로고
    • A cosmid-based system for constructing mutants of herpes simplex virus type 1
    • Cunningham C., and Davison A.J. A cosmid-based system for constructing mutants of herpes simplex virus type 1. Virology 197 1 (1993) 116-124
    • (1993) Virology , vol.197 , Issue.1 , pp. 116-124
    • Cunningham, C.1    Davison, A.J.2
  • 12
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: dynamic sensors of DNA damage and cellular stress
    • Dellaire G., and Bazett-Jones D.P. PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. BioEssays 26 9 (2004) 963-977
    • (2004) BioEssays , vol.26 , Issue.9 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 13
    • 0036174361 scopus 로고    scopus 로고
    • Expression of herpes simplex virus ICP0 inhibits the induction of interferon-stimulated genes by viral infection
    • Eidson K.M., Hobbs W.E., Manning B.J., Carlson P., and DeLuca N.A. Expression of herpes simplex virus ICP0 inhibits the induction of interferon-stimulated genes by viral infection. J. Virol. 76 5 (2002) 2180-2191
    • (2002) J. Virol. , vol.76 , Issue.5 , pp. 2180-2191
    • Eidson, K.M.1    Hobbs, W.E.2    Manning, B.J.3    Carlson, P.4    DeLuca, N.A.5
  • 14
    • 0022110394 scopus 로고
    • Activation of cellular promoters during herpes simplex virus infection of biochemically transformed cells
    • Everett R.D. Activation of cellular promoters during herpes simplex virus infection of biochemically transformed cells. EMBO J. 4 (1985) 1973-1980
    • (1985) EMBO J. , vol.4 , pp. 1973-1980
    • Everett, R.D.1
  • 15
    • 0024512466 scopus 로고
    • Construction and characterization of herpes simplex virus type 1 mutants with defined lesions in immediate early gene 1
    • Everett R.D. Construction and characterization of herpes simplex virus type 1 mutants with defined lesions in immediate early gene 1. J. Gen. Virol. 70 Pt. 5 (1989) 1185-1202
    • (1989) J. Gen. Virol. , vol.70 , Issue.PART 5 , pp. 1185-1202
    • Everett, R.D.1
  • 16
    • 0033624137 scopus 로고    scopus 로고
    • ICP0, a regulator of herpes simplex virus during lytic and latent infection
    • Everett R.D. ICP0, a regulator of herpes simplex virus during lytic and latent infection. Bioessays 22 8 (2000) 761-770
    • (2000) Bioessays , vol.22 , Issue.8 , pp. 761-770
    • Everett, R.D.1
  • 17
    • 0035969103 scopus 로고    scopus 로고
    • DNA viruses and viral proteins that interact with PML nuclear bodies
    • Everett R.D. DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 20 49 (2001) 7266-7273
    • (2001) Oncogene , vol.20 , Issue.49 , pp. 7266-7273
    • Everett, R.D.1
  • 18
    • 33644821166 scopus 로고    scopus 로고
    • Interactions between DNA viruses, ND10 and the DNA damage response
    • Everett R.D. Interactions between DNA viruses, ND10 and the DNA damage response. Cell. Microbiol. 8 3 (2006) 365-374
    • (2006) Cell. Microbiol. , vol.8 , Issue.3 , pp. 365-374
    • Everett, R.D.1
  • 19
    • 0028039189 scopus 로고
    • HSV-1 IE protein Vmw110 causes redistribution of PML
    • Everett R.D., and Maul G.G. HSV-1 IE protein Vmw110 causes redistribution of PML. EMBO J. 13 21 (1994) 5062-5069
    • (1994) EMBO J. , vol.13 , Issue.21 , pp. 5062-5069
    • Everett, R.D.1    Maul, G.G.2
  • 20
    • 0028825230 scopus 로고
    • Point mutations in the herpes simplex virus type 1 Vmw110 RING finger helix affect activation of gene expression, viral growth, and interaction with PML-containing nuclear structures
    • Everett R., O'Hare P., O'Rourke D., Barlow P., and Orr A. Point mutations in the herpes simplex virus type 1 Vmw110 RING finger helix affect activation of gene expression, viral growth, and interaction with PML-containing nuclear structures. J. Virol. 69 11 (1995) 7339-7344
    • (1995) J. Virol. , vol.69 , Issue.11 , pp. 7339-7344
    • Everett, R.1    O'Hare, P.2    O'Rourke, D.3    Barlow, P.4    Orr, A.5
  • 21
    • 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., Freemont P., Saitoh H., Dasso M., Orr A., Kathoria M., and Parkinson J. The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J. Virol. 72 8 (1998) 6581-6591
    • (1998) J. Virol. , vol.72 , Issue.8 , 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
  • 22
    • 0032534802 scopus 로고    scopus 로고
    • A viral activator of gene expression functions via the ubiquitin-proteasome pathway
    • Everett R.D., Orr A., and Preston C.M. A viral activator of gene expression functions via the ubiquitin-proteasome pathway. EMBO J. 17 24 (1998) 7161-7169
    • (1998) EMBO J. , vol.17 , Issue.24 , pp. 7161-7169
    • Everett, R.D.1    Orr, A.2    Preston, C.M.3
  • 23
    • 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., Earnshaw W.C., Findlay J., and Lomonte P. Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110. EMBO J. 18 6 (1999) 1526-1538
    • (1999) EMBO J. , vol.18 , Issue.6 , pp. 1526-1538
    • Everett, R.D.1    Earnshaw, W.C.2    Findlay, J.3    Lomonte, P.4
  • 24
    • 0842347715 scopus 로고    scopus 로고
    • Phenotype of a herpes simplex virus type 1 mutant that fails to express immediate-early regulatory protein ICP0
    • Everett R.D., Boutell C., and Orr A. Phenotype of a herpes simplex virus type 1 mutant that fails to express immediate-early regulatory protein ICP0. J. Virol. 78 4 (2004) 1763-1774
    • (2004) J. Virol. , vol.78 , Issue.4 , pp. 1763-1774
    • Everett, R.D.1    Boutell, C.2    Orr, A.3
  • 25
    • 0842304512 scopus 로고    scopus 로고
    • Formation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexes
    • Everett R.D., Sourvinos G., Leiper C., Clements J.B., and Orr A. Formation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexes. J. Virol. 78 4 (2004) 1903-1917
    • (2004) J. Virol. , vol.78 , Issue.4 , pp. 1903-1917
    • Everett, R.D.1    Sourvinos, G.2    Leiper, C.3    Clements, J.B.4    Orr, A.5
  • 27
    • 0021847819 scopus 로고
    • Identification of immediate early genes from herpes simplex virus that transactivate the virus thymidine kinase gene
    • Gelman I.H., and Silverstein S. Identification of immediate early genes from herpes simplex virus that transactivate the virus thymidine kinase gene. Proc. Natl. Acad. Sci. U.S.A. 82 16 (1985) 5265-5269
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , Issue.16 , pp. 5265-5269
    • Gelman, I.H.1    Silverstein, S.2
  • 28
    • 10944260126 scopus 로고    scopus 로고
    • Retrovirus restriction factors
    • Goff S.P. Retrovirus restriction factors. Mol. Cell 16 6 (2004) 849-859
    • (2004) Mol. Cell , vol.16 , Issue.6 , pp. 849-859
    • Goff, S.P.1
  • 29
    • 0030799493 scopus 로고    scopus 로고
    • Molecular cloning of a new interferon-induced PML nuclear body-associated protein
    • Gongora C., David G., Pintard L., Tissot C., Hua T.D., Dejean A., and Mechti N. Molecular cloning of a new interferon-induced PML nuclear body-associated protein. J. Biol. Chem. 272 31 (1997) 19457-19463
    • (1997) J. Biol. Chem. , vol.272 , Issue.31 , pp. 19457-19463
    • Gongora, C.1    David, G.2    Pintard, L.3    Tissot, C.4    Hua, T.D.5    Dejean, A.6    Mechti, N.7
  • 30
    • 0033795196 scopus 로고    scopus 로고
    • Interferons: cell signalling, immune modulation, antiviral response and virus countermeasures
    • Goodbourn S., Didcock L., and Randall R.E. Interferons: cell signalling, immune modulation, antiviral response and virus countermeasures. J. Gen. Virol. 81 Pt. 10 (2000) 2341-2364
    • (2000) J. Gen. Virol. , vol.81 , Issue.PART 10 , pp. 2341-2364
    • Goodbourn, S.1    Didcock, L.2    Randall, R.E.3
  • 31
    • 0029894340 scopus 로고    scopus 로고
    • Interferon-modulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML)
    • Grotzinger T., Sternsdorf T., Jensen K., and Will H. Interferon-modulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML). Eur. J. Biochem. 238 2 (1996) 554-560
    • (1996) Eur. J. Biochem. , vol.238 , Issue.2 , pp. 554-560
    • Grotzinger, T.1    Sternsdorf, T.2    Jensen, K.3    Will, H.4
  • 32
    • 19644384912 scopus 로고    scopus 로고
    • Components of the REST/CoREST/histone deacetylase repressor complex are disrupted, modified, and translocated in HSV-1-infected cells
    • Gu H., Liang Y., Mandel G., and Roizman B. Components of the REST/CoREST/histone deacetylase repressor complex are disrupted, modified, and translocated in HSV-1-infected cells. Proc. Natl. Acad. Sci. U.S.A. 102 21 (2005) 7571-7576
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , Issue.21 , pp. 7571-7576
    • Gu, H.1    Liang, Y.2    Mandel, G.3    Roizman, B.4
  • 33
    • 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., Van Sant C., Lopez P., and Roizman B. 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. U.S.A. 99 2 (2002) 631-636
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , Issue.2 , pp. 631-636
    • Hagglund, R.1    Van Sant, C.2    Lopez, P.3    Roizman, B.4
  • 34
    • 0034977956 scopus 로고    scopus 로고
    • ICP0, ICP4, or VP16 expressed from adenovirus vectors induces reactivation of latent herpes simplex virus type 1 in primary cultures of latently infected trigeminal ganglion cells
    • Halford W.P., Kemp C.D., Isler J.A., Davido D.J., and Schaffer P.A. ICP0, ICP4, or VP16 expressed from adenovirus vectors induces reactivation of latent herpes simplex virus type 1 in primary cultures of latently infected trigeminal ganglion cells. J. Virol. 75 13 (2001) 6143-6153
    • (2001) J. Virol. , vol.75 , Issue.13 , pp. 6143-6153
    • Halford, W.P.1    Kemp, C.D.2    Isler, J.A.3    Davido, D.J.4    Schaffer, P.A.5
  • 35
    • 0025877135 scopus 로고
    • Establishment of latency in vitro by the herpes simplex virus type 1 mutant in 1814
    • Harris R.A., and Preston C.M. Establishment of latency in vitro by the herpes simplex virus type 1 mutant in 1814. J. Gen. Virol. 72 Pt. 4 (1991) 907-913
    • (1991) J. Gen. Virol. , vol.72 , Issue.PART 4 , pp. 907-913
    • Harris, R.A.1    Preston, C.M.2
  • 36
    • 0024323435 scopus 로고
    • Herpes simplex virus type 1 immediate-early protein Vmw110 reactivates latent herpes simplex virus type 2 in an in vitro latency system
    • Harris R.A., Everett R.D., Zhu X.X., Silverstein S., and Preston C.M. Herpes simplex virus type 1 immediate-early protein Vmw110 reactivates latent herpes simplex virus type 2 in an in vitro latency system. J. Virol. 63 8 (1989) 3513-3515
    • (1989) J. Virol. , vol.63 , Issue.8 , pp. 3513-3515
    • Harris, R.A.1    Everett, R.D.2    Zhu, X.X.3    Silverstein, S.4    Preston, C.M.5
  • 37
    • 4444298521 scopus 로고    scopus 로고
    • VP16-dependent association of chromatin-modifying coactivators and underrepresentation of histones at immediate-early gene promoters during herpes simplex virus infection
    • Herrera F.J., and Triezenberg S.J. VP16-dependent association of chromatin-modifying coactivators and underrepresentation of histones at immediate-early gene promoters during herpes simplex virus infection. J. Virol. 78 18 (2004) 9689-9696
    • (2004) J. Virol. , vol.78 , Issue.18 , pp. 9689-9696
    • Herrera, F.J.1    Triezenberg, S.J.2
  • 38
    • 0035106881 scopus 로고    scopus 로고
    • Efficient activation of viral genomes by levels of herpes simplex virus ICP0 insufficient to affect cellular gene expression or cell survival
    • Hobbs W.E., Brough D.E., Kovesdi I., and DeLuca N.A. Efficient activation of viral genomes by levels of herpes simplex virus ICP0 insufficient to affect cellular gene expression or cell survival. J. Virol. 75 7 (2001) 3391-3403
    • (2001) J. Virol. , vol.75 , Issue.7 , pp. 3391-3403
    • Hobbs, W.E.1    Brough, D.E.2    Kovesdi, I.3    DeLuca, N.A.4
  • 39
    • 0346147033 scopus 로고    scopus 로고
    • Body language: the function of PML nuclear bodies in apoptosis regulation
    • Hofmann T.G., and Will H. Body language: the function of PML nuclear bodies in apoptosis regulation. Cell Death Differ. 10 12 (2003) 1290-1299
    • (2003) Cell Death Differ. , vol.10 , Issue.12 , pp. 1290-1299
    • Hofmann, T.G.1    Will, H.2
  • 40
    • 0038714277 scopus 로고    scopus 로고
    • Relationship of herpes simplex virus genome configuration to productive and persistent infections
    • Jackson S.A., and DeLuca N.A. Relationship of herpes simplex virus genome configuration to productive and persistent infections. Proc. Natl. Acad. Sci. U.S.A. 100 13 (2003) 7871-7876
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , Issue.13 , pp. 7871-7876
    • Jackson, S.A.1    DeLuca, N.A.2
  • 41
    • 0029045486 scopus 로고
    • Quiescent viral genomes in human fibroblasts after infection with herpes simplex virus type 1 Vmw65 mutants
    • Jamieson D.R., Robinson L.H., Daksis J.I., Nicholl M.J., and Preston C.M. Quiescent viral genomes in human fibroblasts after infection with herpes simplex virus type 1 Vmw65 mutants. J. Gen. Virol. 76 Pt. 6 (1995) 1417-1431
    • (1995) J. Gen. Virol. , vol.76 , Issue.PART 6 , pp. 1417-1431
    • Jamieson, D.R.1    Robinson, L.H.2    Daksis, J.I.3    Nicholl, M.J.4    Preston, C.M.5
  • 42
    • 0030817931 scopus 로고    scopus 로고
    • Activation of gene expression by herpes simplex virus type 1 ICP0 occurs at the level of mRNA synthesis
    • Jordan R., and Schaffer P. Activation of gene expression by herpes simplex virus type 1 ICP0 occurs at the level of mRNA synthesis. J. Virol. 71 (1997) 6850-6862
    • (1997) J. Virol. , vol.71 , pp. 6850-6862
    • Jordan, R.1    Schaffer, P.2
  • 43
    • 20544474210 scopus 로고    scopus 로고
    • Pathogen recognition with Toll-like receptors
    • Kawai T., and Akira S. Pathogen recognition with Toll-like receptors. Curr. Opin. Immunol. 17 4 (2005) 338-344
    • (2005) Curr. Opin. Immunol. , vol.17 , Issue.4 , pp. 338-344
    • Kawai, T.1    Akira, S.2
  • 44
    • 4444250828 scopus 로고    scopus 로고
    • During lytic infection herpes simplex virus type 1 is associated with histones bearing modifications that correlate with active transcription
    • Kent J.R., Zeng P.Y., Atanasiu D., Gardner J., Fraser N.W., and Berger S.L. During lytic infection herpes simplex virus type 1 is associated with histones bearing modifications that correlate with active transcription. J. Virol. 78 18 (2004) 10178-10186
    • (2004) J. Virol. , vol.78 , Issue.18 , pp. 10178-10186
    • Kent, J.R.1    Zeng, P.Y.2    Atanasiu, D.3    Gardner, J.4    Fraser, N.W.5    Berger, S.L.6
  • 45
    • 0029031542 scopus 로고
    • Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation
    • Klemm R.D., Goodrich J.A., Zhou S., and Tjian R. Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation. Proc. Natl. Acad. Sci. U.S.A. 92 13 (1995) 5788-5792
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , Issue.13 , pp. 5788-5792
    • Klemm, R.D.1    Goodrich, J.A.2    Zhou, S.3    Tjian, R.4
  • 46
    • 0023144118 scopus 로고
    • Stages in the nuclear association of the herpes simplex virus transcriptional activator protein ICP4
    • Knipe D.M., Senechek D., Rice S.A., and Smith J.L. Stages in the nuclear association of the herpes simplex virus transcriptional activator protein ICP4. J. Virol. 61 2 (1987) 276-284
    • (1987) J. Virol. , vol.61 , Issue.2 , pp. 276-284
    • Knipe, D.M.1    Senechek, D.2    Rice, S.A.3    Smith, J.L.4
  • 48
    • 0029798373 scopus 로고    scopus 로고
    • Attenuation of DNA-dependent protein kinase activity and its catalytic subunit by the herpes simplex virus type 1 transactivator ICP0
    • Lees-Miller S.P., Long M.C., Kilvert M.A., Lam V., Rice S.A., and Spencer C.A. Attenuation of DNA-dependent protein kinase activity and its catalytic subunit by the herpes simplex virus type 1 transactivator ICP0. J. Virol. 70 11 (1996) 7471-7477
    • (1996) J. Virol. , vol.70 , Issue.11 , pp. 7471-7477
    • Lees-Miller, S.P.1    Long, M.C.2    Kilvert, M.A.3    Lam, V.4    Rice, S.A.5    Spencer, C.A.6
  • 49
    • 0019136475 scopus 로고
    • The structure of herpes simplex virus type 1 DNA as probed by microccal nuclease digestion
    • Leinbach S.S., and Summers W.C. The structure of herpes simplex virus type 1 DNA as probed by microccal nuclease digestion. J. Gen. Virol. 51 (1980) 45-59
    • (1980) J. Gen. Virol. , vol.51 , pp. 45-59
    • Leinbach, S.S.1    Summers, W.C.2
  • 50
    • 4544256756 scopus 로고    scopus 로고
    • Cytoplasmic PML function in TGF-beta signalling
    • Lin H.K., Bergmann S., and Pandolfi P.P. Cytoplasmic PML function in TGF-beta signalling. Nature 431 7005 (2004) 205-211
    • (2004) Nature , vol.431 , Issue.7005 , pp. 205-211
    • Lin, H.K.1    Bergmann, S.2    Pandolfi, P.P.3
  • 51
    • 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., Sullivan K.F., and Everett R.D. Degradation of nucleosome-associated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0. J. Biol. Chem. 276 8 (2001) 5829-5835
    • (2001) J. Biol. Chem. , vol.276 , Issue.8 , pp. 5829-5835
    • Lomonte, P.1    Sullivan, K.F.2    Everett, R.D.3
  • 52
    • 2942672088 scopus 로고    scopus 로고
    • Functional interaction between class II histone deacetylases and ICP0 of herpes simplex virus type 1
    • Lomonte P., Thomas J., Texier P., Caron C., Khochbin S., and Epstein A.L. Functional interaction between class II histone deacetylases and ICP0 of herpes simplex virus type 1. J. Virol. 78 13 (2004) 6744-6757
    • (2004) J. Virol. , vol.78 , Issue.13 , pp. 6744-6757
    • Lomonte, P.1    Thomas, J.2    Texier, P.3    Caron, C.4    Khochbin, S.5    Epstein, A.L.6
  • 53
    • 27644515513 scopus 로고    scopus 로고
    • The histone H3.3 chaperone HIRA is essential for chromatin assembly in the male pronucleus
    • Loppin B., Bonnefoy E., Anselme C., Laurencon A., Karr T.L., and Couble P. The histone H3.3 chaperone HIRA is essential for chromatin assembly in the male pronucleus. Nature 437 7063 (2005) 1386-1390
    • (2005) Nature , vol.437 , Issue.7063 , pp. 1386-1390
    • Loppin, B.1    Bonnefoy, E.2    Anselme, C.3    Laurencon, A.4    Karr, T.L.5    Couble, P.6
  • 54
    • 1542298307 scopus 로고    scopus 로고
    • Histone chaperones, a supporting role in the limelight
    • Loyola A., and Almouzni G. Histone chaperones, a supporting role in the limelight. Biochim. Biophys. Acta 1677 1-3 (2004) 3-11
    • (2004) Biochim. Biophys. Acta , vol.1677 , Issue.1-3 , pp. 3-11
    • Loyola, A.1    Almouzni, G.2
  • 55
    • 0031797865 scopus 로고    scopus 로고
    • An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein
    • Madani N., and Kabat D. An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. J. Virol. 72 12 (1998) 10251-10255
    • (1998) J. Virol. , vol.72 , Issue.12 , pp. 10251-10255
    • Madani, N.1    Kabat, D.2
  • 57
    • 0032143446 scopus 로고    scopus 로고
    • Nuclear domain 10, the site of DNA virus transcription and replication
    • Maul G.G. Nuclear domain 10, the site of DNA virus transcription and replication. BioEssays 20 (1998) 660-667
    • (1998) BioEssays , vol.20 , pp. 660-667
    • Maul, G.G.1
  • 58
    • 0037314175 scopus 로고    scopus 로고
    • Sequential recruitment of HAT and SWI/SNF components to condensed chromatin by VP16
    • Memedula S., and Belmont A.S. Sequential recruitment of HAT and SWI/SNF components to condensed chromatin by VP16. Curr. Biol. 13 3 (2003) 241-246
    • (2003) Curr. Biol. , vol.13 , Issue.3 , pp. 241-246
    • Memedula, S.1    Belmont, A.S.2
  • 59
    • 28844456962 scopus 로고    scopus 로고
    • Functional inaccessibility of quiescent herpes simplex virus genomes
    • Minaker R.L., Mossman K.L., and Smiley J.R. Functional inaccessibility of quiescent herpes simplex virus genomes. Virol. J. 2 1 (2005) 85
    • (2005) Virol. J. , vol.2 , Issue.1 , pp. 85
    • Minaker, R.L.1    Mossman, K.L.2    Smiley, J.R.3
  • 61
    • 0032708382 scopus 로고    scopus 로고
    • Truncation of the C-terminal acidic transcriptional activation domain of herpes simplex virus VP16 renders expression of the immediate-early genes almost entirely dependent on ICP0
    • Mossman K.L., and Smiley J.R. Truncation of the C-terminal acidic transcriptional activation domain of herpes simplex virus VP16 renders expression of the immediate-early genes almost entirely dependent on ICP0. J. Virol. 73 12 (1999) 9726-9733
    • (1999) J. Virol. , vol.73 , Issue.12 , pp. 9726-9733
    • Mossman, K.L.1    Smiley, J.R.2
  • 62
    • 0036150004 scopus 로고    scopus 로고
    • Herpes simplex virus ICP0 and ICP34.5 counteract distinct interferon-induced barriers to virus replication
    • Mossman K.L., and Smiley J.R. Herpes simplex virus ICP0 and ICP34.5 counteract distinct interferon-induced barriers to virus replication. J. Virol. 76 4 (2002) 1995-1998
    • (2002) J. Virol. , vol.76 , Issue.4 , pp. 1995-1998
    • Mossman, K.L.1    Smiley, J.R.2
  • 63
    • 0033935685 scopus 로고    scopus 로고
    • Herpes simplex virus ICP0 mutants are hypersensitive to interferon
    • Mossman K.L., Saffran H.A., and Smiley J.R. Herpes simplex virus ICP0 mutants are hypersensitive to interferon. J. Virol. 74 4 (2000) 2052-2056
    • (2000) J. Virol. , vol.74 , Issue.4 , pp. 2052-2056
    • Mossman, K.L.1    Saffran, H.A.2    Smiley, J.R.3
  • 64
    • 0022521909 scopus 로고
    • Chromosomal organization of the herpes simplex virus genome during acute infection of the mouse central nervous system
    • Muggeridge M.I., and Fraser N.W. Chromosomal organization of the herpes simplex virus genome during acute infection of the mouse central nervous system. J. Virol. 59 (1986) 764-767
    • (1986) J. Virol. , vol.59 , pp. 764-767
    • Muggeridge, M.I.1    Fraser, N.W.2
  • 65
    • 0037108977 scopus 로고    scopus 로고
    • A dominant block to HIV-1 replication at reverse transcription in simian cells
    • Munk C., Brandt S.M., Lucero G., and Landau N.R. A dominant block to HIV-1 replication at reverse transcription in simian cells. Proc. Natl. Acad. Sci. U.S.A. 99 21 (2002) 13843-13848
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , Issue.21 , pp. 13843-13848
    • Munk, C.1    Brandt, S.M.2    Lucero, G.3    Landau, N.R.4
  • 66
    • 2342584790 scopus 로고    scopus 로고
    • Toll-like receptors and the host defense against microbial pathogens: bringing specificity to the innate-immune system
    • Netea M.G., van der Graaf C., Van der Meer J.W., and Kullberg B.J. Toll-like receptors and the host defense against microbial pathogens: bringing specificity to the innate-immune system. J. Leukoc. Biol. 75 5 (2004) 749-755
    • (2004) J. Leukoc. Biol. , vol.75 , Issue.5 , pp. 749-755
    • Netea, M.G.1    van der Graaf, C.2    Van der Meer, J.W.3    Kullberg, B.J.4
  • 67
    • 27244444559 scopus 로고    scopus 로고
    • TRIM family proteins: retroviral restriction and antiviral defence
    • Nisole S., Stoye J.P., and Saib A. TRIM family proteins: retroviral restriction and antiviral defence. Nat. Rev., Microbiol. 3 10 (2005) 799-808
    • (2005) Nat. Rev., Microbiol. , vol.3 , Issue.10 , pp. 799-808
    • Nisole, S.1    Stoye, J.P.2    Saib, A.3
  • 68
    • 0024284873 scopus 로고
    • Herpes simplex virus regulatory elements and the immunoglobulin octamer domain bind a common factor and are both targets for virion transactivation
    • O'Hare P., and Gooding C.R. Herpes simplex virus regulatory elements and the immunoglobulin octamer domain bind a common factor and are both targets for virion transactivation. Cell 52 (1988) 435-445
    • (1988) Cell , vol.52 , pp. 435-445
    • O'Hare, P.1    Gooding, C.R.2
  • 69
    • 0022393681 scopus 로고
    • Three trans-acting regulatory proteins of herpes simplex virus modulate immediate-early gene expression in a pathway involving positive and negative feedback regulation
    • O'Hare P., and Hayward G.S. Three trans-acting regulatory proteins of herpes simplex virus modulate immediate-early gene expression in a pathway involving positive and negative feedback regulation. J. Virol. 56 3 (1985) 723-733
    • (1985) J. Virol. , vol.56 , Issue.3 , pp. 723-733
    • O'Hare, P.1    Hayward, G.S.2
  • 70
    • 0032889431 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein vmw110 induces the proteasome-dependent degradation of the catalytic subunit of DNA-dependent protein kinase
    • Parkinson J., Lees-Miller S.P., and Everett R.D. Herpes simplex virus type 1 immediate-early protein vmw110 induces the proteasome-dependent degradation of the catalytic subunit of DNA-dependent protein kinase. J. Virol. 73 1 (1999) 650-657
    • (1999) J. Virol. , vol.73 , Issue.1 , pp. 650-657
    • Parkinson, J.1    Lees-Miller, S.P.2    Everett, R.D.3
  • 72
    • 0033964244 scopus 로고    scopus 로고
    • Repression of viral transcription during herpes simplex virus latency
    • Preston C.M. Repression of viral transcription during herpes simplex virus latency. J. Gen. Virol. 81 Pt. 1 (2000) 1-19
    • (2000) J. Gen. Virol. , vol.81 , Issue.PART 1 , pp. 1-19
    • Preston, C.M.1
  • 73
    • 0030801241 scopus 로고    scopus 로고
    • Repression of gene expression upon infection of cells with herpes simplex virus type 1 mutants impaired for immediate-early protein synthesis
    • Preston C.M., and Nicholl M.J. Repression of gene expression upon infection of cells with herpes simplex virus type 1 mutants impaired for immediate-early protein synthesis. J. Virol. 71 10 (1997) 7807-7813
    • (1997) J. Virol. , vol.71 , Issue.10 , pp. 7807-7813
    • Preston, C.M.1    Nicholl, M.J.2
  • 74
    • 0023852244 scopus 로고
    • A complex formed between cell components and an HSV structural polypeptide binds to a viral immediate early gene regulatory DNA sequence
    • Preston C.M., Frame M.C., and Campbell M.E. A complex formed between cell components and an HSV structural polypeptide binds to a viral immediate early gene regulatory DNA sequence. Cell 52 3 (1988) 425-434
    • (1988) Cell , vol.52 , Issue.3 , pp. 425-434
    • Preston, C.M.1    Frame, M.C.2    Campbell, M.E.3
  • 75
    • 0021966699 scopus 로고
    • Stimulation of expression of a herpes simplex virus DNA-binding protein by two viral functions
    • Quinlan M.P., and Knipe D.M. Stimulation of expression of a herpes simplex virus DNA-binding protein by two viral functions. Mol. Cell. Biol. 5 (1985) 957-963
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 957-963
    • Quinlan, M.P.1    Knipe, D.M.2
  • 76
    • 0036284794 scopus 로고    scopus 로고
    • HIRA is critical for a nucleosome assembly pathway independent of DNA synthesis
    • Ray-Gallet D., Quivy J.P., Scamps C., Martini E.M., Lipinski M., and Almouzni G. HIRA is critical for a nucleosome assembly pathway independent of DNA synthesis. Mol. Cell 9 5 (2002) 1091-1100
    • (2002) Mol. Cell , vol.9 , Issue.5 , pp. 1091-1100
    • Ray-Gallet, D.1    Quivy, J.P.2    Scamps, C.3    Martini, E.M.4    Lipinski, M.5    Almouzni, G.6
  • 77
    • 0001142641 scopus 로고    scopus 로고
    • Herpes simplex viruses and their replication
    • Knipe D.M., Howley P.M., Griffin D.E., Lamb R.A., Martin M.A., Roizman B., and Strauss S.E. (Eds), Lippincott, Williams and Wilkins, Philadelphia
    • Roizman B., and Knipe D.M. Herpes simplex viruses and their replication. In: Knipe D.M., Howley P.M., Griffin D.E., Lamb R.A., Martin M.A., Roizman B., and Strauss S.E. (Eds). Field's Virology. 4th ed. (2001), Lippincott, Williams and Wilkins, Philadelphia 2381-2398
    • (2001) Field's Virology. 4th ed. , pp. 2381-2398
    • Roizman, B.1    Knipe, D.M.2
  • 78
    • 0023476485 scopus 로고
    • Herpes simplex virus genes involved in latency in vitro
    • Russell J., Stow N.D., Stow E.C., and Preston C.M. Herpes simplex virus genes involved in latency in vitro. J. Gen. Virol. 68 Pt. 12 (1987) 3009-3018
    • (1987) J. Gen. Virol. , vol.68 , Issue.PART 12 , pp. 3009-3018
    • Russell, J.1    Stow, N.D.2    Stow, E.C.3    Preston, C.M.4
  • 79
    • 0030958819 scopus 로고    scopus 로고
    • The herpes simplex virus immediate-early protein ICP0 affects transcription from the viral genome and infected-cell survival in the absence of ICP4 and ICP27
    • Samaniego L.A., Wu N., and DeLuca N.A. The herpes simplex virus immediate-early protein ICP0 affects transcription from the viral genome and infected-cell survival in the absence of ICP4 and ICP27. J. Virol. 71 6 (1997) 4614-4625
    • (1997) J. Virol. , vol.71 , Issue.6 , pp. 4614-4625
    • Samaniego, L.A.1    Wu, N.2    DeLuca, N.A.3
  • 80
    • 0031947861 scopus 로고    scopus 로고
    • Persistence and expression of the herpes simplex virus genome in the absence of immediate-early proteins
    • Samaniego L.A., Neiderhiser L., and DeLuca N.A. Persistence and expression of the herpes simplex virus genome in the absence of immediate-early proteins. J. Virol. 72 4 (1998) 3307-3320
    • (1998) J. Virol. , vol.72 , Issue.4 , pp. 3307-3320
    • Samaniego, L.A.1    Neiderhiser, L.2    DeLuca, N.A.3
  • 81
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy A.M., Gaddis N.C., Choi J.D., and Malim M.H. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418 6898 (2002) 646-650
    • (2002) Nature , vol.418 , Issue.6898 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 82
    • 0031788565 scopus 로고    scopus 로고
    • Evidence for a newly discovered cellular anti-HIV-1 phenotype
    • Simon J.H., Gaddis N.C., Fouchier R.A., and Malim M.H. Evidence for a newly discovered cellular anti-HIV-1 phenotype. Nat. Med. 4 12 (1998) 1397-1400
    • (1998) Nat. Med. , vol.4 , Issue.12 , pp. 1397-1400
    • Simon, J.H.1    Gaddis, N.C.2    Fouchier, R.A.3    Malim, M.H.4
  • 83
    • 0030745299 scopus 로고    scopus 로고
    • Truncation of the C-terminal acidic transcriptional activation domain of herpes simplex virus VP16 produces a phenotype similar to that of the in1814 linker insertion mutation
    • Smiley J.R., and Duncan J. Truncation of the C-terminal acidic transcriptional activation domain of herpes simplex virus VP16 produces a phenotype similar to that of the in1814 linker insertion mutation. J. Virol. 71 8 (1997) 6191-6193
    • (1997) J. Virol. , vol.71 , Issue.8 , pp. 6191-6193
    • Smiley, J.R.1    Duncan, J.2
  • 85
    • 0024465662 scopus 로고
    • The Oct-1 homoeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16
    • Stern S., Tanaka M., and Herr W. The Oct-1 homoeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16. Nature 341 6243 (1989) 624-630
    • (1989) Nature , vol.341 , Issue.6243 , pp. 624-630
    • Stern, S.1    Tanaka, M.2    Herr, W.3
  • 86
    • 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 Stow E.C. 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 Pt. 12 (1986) 2571-2585
    • (1986) J. Gen. Virol. , vol.67 , Issue.PART 12 , pp. 2571-2585
    • Stow, N.D.1    Stow, E.C.2
  • 87
    • 0023267788 scopus 로고
    • The HIV 'A' (sor) gene product is essential for virus infectivity
    • Strebel K., Daugherty D., Clouse K., Cohen D., Folks T., and Martin M.A. The HIV 'A' (sor) gene product is essential for virus infectivity. Nature 328 6132 (1987) 728-730
    • (1987) Nature , vol.328 , Issue.6132 , pp. 728-730
    • Strebel, K.1    Daugherty, D.2    Clouse, K.3    Cohen, D.4    Folks, T.5    Martin, M.A.6
  • 88
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys
    • Stremlau M., Owens C.M., Perron M.J., Kiessling M., Autissier P., and Sodroski J. The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. Nature 427 6977 (2004) 848-853
    • (2004) Nature , vol.427 , Issue.6977 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3    Kiessling, M.4    Autissier, P.5    Sodroski, J.6
  • 89
    • 0024024137 scopus 로고
    • Functional dissection of VP16, the trans-activator of herpes simplex virus immediate early gene expression
    • Triezenberg S.J., Kingsbury R.C., and McKnight S.L. Functional dissection of VP16, the trans-activator of herpes simplex virus immediate early gene expression. Genes Dev. 2 (1988) 718-729
    • (1988) Genes Dev. , vol.2 , pp. 718-729
    • Triezenberg, S.J.1    Kingsbury, R.C.2    McKnight, S.L.3
  • 90
    • 0030756675 scopus 로고    scopus 로고
    • Induced alpha helix in the VP16 activation domain upon binding to a human TAF
    • Uesugi M., Nyanguile O., Lu H., Levine A.J., and Verdine G.L. Induced alpha helix in the VP16 activation domain upon binding to a human TAF. Science 277 5330 (1997) 1310-1313
    • (1997) Science , vol.277 , Issue.5330 , pp. 1310-1313
    • Uesugi, M.1    Nyanguile, O.2    Lu, H.3    Levine, A.J.4    Verdine, G.L.5
  • 91
    • 14344252157 scopus 로고    scopus 로고
    • Induction and suppression of RNA silencing: insights from viral infections
    • Voinnet O. Induction and suppression of RNA silencing: insights from viral infections. Nat. Rev., Genet. 6 3 (2005) 206-220
    • (2005) Nat. Rev., Genet. , vol.6 , Issue.3 , pp. 206-220
    • Voinnet, O.1
  • 92
    • 0027179103 scopus 로고
    • Vif is crucial for human immunodeficiency virus type 1 proviral DNA synthesis in infected cells
    • von Schwedler U., Song J., Aiken C., and Trono D. Vif is crucial for human immunodeficiency virus type 1 proviral DNA synthesis in infected cells. J. Virol. 67 8 (1993) 4945-4955
    • (1993) J. Virol. , vol.67 , Issue.8 , pp. 4945-4955
    • von Schwedler, U.1    Song, J.2    Aiken, C.3    Trono, D.4
  • 93
    • 11144324185 scopus 로고    scopus 로고
    • Disruption of Erk-dependent type I interferon induction breaks the myxoma virus species barrier
    • Wang F., Ma Y., Barrett J.W., Gao X., Loh J., Barton E., Virgin H.W., and McFadden G. Disruption of Erk-dependent type I interferon induction breaks the myxoma virus species barrier. Nat. Immunol. 5 12 (2004) 1266-1274
    • (2004) Nat. Immunol. , vol.5 , Issue.12 , pp. 1266-1274
    • Wang, F.1    Ma, Y.2    Barrett, J.W.3    Gao, X.4    Loh, J.5    Barton, E.6    Virgin, H.W.7    McFadden, G.8
  • 94
    • 0026543979 scopus 로고
    • Deletion of the VP16 open reading frame of herpes simplex virus type 1
    • Weinheimer S.P., Boyd B.A., Durham S.K., Resnick J.L., and O'Boyle D.R. Deletion of the VP16 open reading frame of herpes simplex virus type 1. J. Virol. 66 1 (1992) 258-269
    • (1992) J. Virol. , vol.66 , Issue.1 , pp. 258-269
    • Weinheimer, S.P.1    Boyd, B.A.2    Durham, S.K.3    Resnick, J.L.4    O'Boyle, D.R.5
  • 95
    • 0025167974 scopus 로고
    • A cellular factor binds to the herpes simplex virus type 1 transactivator Vmw65 and is required for Vmw65-dependent protein-DNA complex assembly with Oct-1
    • Xiao P., and Capone J.P. A cellular factor binds to the herpes simplex virus type 1 transactivator Vmw65 and is required for Vmw65-dependent protein-DNA complex assembly with Oct-1. Mol. Cell. Biol. 10 9 (1990) 4974-4977
    • (1990) Mol. Cell. Biol. , vol.10 , Issue.9 , pp. 4974-4977
    • Xiao, P.1    Capone, J.P.2
  • 97
    • 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 Schaffer P.A. 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 10 (1995) 6249-6258
    • (1995) J. Virol. , vol.69 , Issue.10 , pp. 6249-6258
    • Yao, F.1    Schaffer, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.