메뉴 건너뛰기




Volumn 83, Issue 22, 2009, Pages 11502-11513

Histone deacetylases 1 and 2 are phosphorylated at novel sites during Varicella-Zoster virus infection

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; PHOSPHOTRANSFERASE;

EID: 70350278896     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01318-09     Document Type: Article
Times cited : (30)

References (53)
  • 1
    • 0030055588 scopus 로고    scopus 로고
    • Varicella-zoster virus
    • Arvin, A. M. 1996. Varicella-zoster virus. Clin. Microbiol. Rev. 9:361-381.
    • (1996) Clin. Microbiol. Rev. , vol.9 , pp. 361-381
    • Arvin, A.M.1
  • 2
    • 3042636651 scopus 로고    scopus 로고
    • Herpes simplex virus protein kinase US3 activates and functionally overlaps protein kinase a to block apoptosis
    • Benetti, L., and B. Roizman. 2004. Herpes simplex virus protein kinase US3 activates and functionally overlaps protein kinase A to block apoptosis. Proc. Natl. Acad. Sci. USA 101:9411-9416.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9411-9416
    • Benetti, L.1    Roizman, B.2
  • 3
    • 8644265940 scopus 로고    scopus 로고
    • Differential requirement for cell fusion and virion formation in the pathogenesis of varicella-zoster virus infection in skin and T cells
    • DOI 10.1128/JVI.78.23.13293-13305.2004
    • Besser, J., M. Ikoma, K. Fabel, M. H. Sommer, L. Zerboni, C. Grose, and A. M. Arvin. 2004. Differential requirement for cell fusion and virion formation in the pathogenesis of varicella-zoster virus infection in skin and T cells. J. Virol. 78:13293-13305. (Pubitemid 39507834)
    • (2004) Journal of Virology , vol.78 , Issue.23 , pp. 13293-13305
    • Besser, J.1    Ikoma, M.2    Fabel, K.3    Sommer, M.H.4    Zerboni, L.5    Grose, C.6    Arvin, A.M.7
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 67449093074 scopus 로고    scopus 로고
    • Enumeration of an extremely high particle-to-PFU ratio for varicella-zoster virus
    • Carpenter, J. E., E. P. Henderson, and C. Grose. 2009. Enumeration of an extremely high particle-to-PFU ratio for varicella-zoster virus. J. Virol. 83: 6917-6921.
    • (2009) J. Virol. , vol.83 , pp. 6917-6921
    • Carpenter, J.E.1    Henderson, E.P.2    Grose, C.3
  • 7
    • 23744507862 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce reactivation of herpes simplex virus type 1 in a latency-associated transcript-independent manner in neuronal cells
    • Danaher, R. J., R. J. Jacob, M. R. Steiner, W. R. Allen, J. M. Hill, and C. S. Miller. 2005. Histone deacetylase inhibitors induce reactivation of herpes simplex virus type 1 in a latency-associated transcript-independent manner in neuronal cells. J. Neurovirol. 11:306-317.
    • (2005) J. Neurovirol. , vol.11 , pp. 306-317
    • Danaher, R.J.1    Jacob, R.J.2    Steiner, M.R.3    Allen, W.R.4    Hill, J.M.5    Miller, C.S.6
  • 8
    • 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
  • 9
    • 32444436099 scopus 로고    scopus 로고
    • Phosphorylation of the varicella-zoster virus (VZV) major transcriptional regulatory protein IE62 by the VZV open reading frame 66 protein kinase
    • Eisfeld, A. J., S. E. Turse, S. A. Jackson, E. C. Lerner, and P. R. Kinchington. 2006. Phosphorylation of the varicella-zoster virus (VZV) major transcriptional regulatory protein IE62 by the VZV open reading frame 66 protein kinase. J. Virol. 80:1710-1723.
    • (2006) J. Virol. , vol.80 , pp. 1710-1723
    • Eisfeld, A.J.1    Turse, S.E.2    Jackson, S.A.3    Lerner, E.C.4    Kinchington, P.R.5
  • 10
    • 34548157388 scopus 로고    scopus 로고
    • Downregulation of class I major histocompatibility complex surface expression by varicella-zoster virus involves open reading frame 66 protein kinase-dependent and -independent mechanisms
    • Eisfeld, A. J., M. B. Yee, A. Erazo, A. Abendroth, and P. R. Kinchington. 2007. Downregulation of class I major histocompatibility complex surface expression by varicella-zoster virus involves open reading frame 66 protein kinase-dependent and -independent mechanisms. J. Virol. 81:9034-9049.
    • (2007) J. Virol. , vol.81 , pp. 9034-9049
    • Eisfeld, A.J.1    Yee, M.B.2    Erazo, A.3    Abendroth, A.4    Kinchington, P.R.5
  • 11
    • 47749123866 scopus 로고    scopus 로고
    • Varicella-zoster virus open reading frame 66 protein kinase is required for efficient viral growth in primary human corneal stromal fibroblast cells
    • DOI 10.1128/JVI.00311-08
    • Erazo, A., M. B. Yee, N. Osterrieder, and P. R. Kinchington. 2008. Varicellazoster virus open reading frame 66 protein kinase is required for efficient viral growth in primary human corneal stromal fibroblast cells. J. Virol. 82:7653-7665. (Pubitemid 352031231)
    • (2008) Journal of Virology , vol.82 , Issue.15 , pp. 7653-7665
    • Erazo, A.1    Yee, M.B.2    Osterrieder, N.3    Kinchington, P.R.4
  • 12
    • 65549165903 scopus 로고    scopus 로고
    • Interferons and viral infections
    • Fensterl, V., and G. C. Sen. 2009. Interferons and viral infections. Biofactors 35:14-20.
    • (2009) Biofactors , vol.35 , pp. 14-20
    • Fensterl, V.1    Sen, G.C.2
  • 13
    • 0037205476 scopus 로고    scopus 로고
    • Phosphatase inhibition leads to histone deacetylases 1 and 2 phosphorylation and disruption of corepressor interactions
    • Galasinski, S. C., K. A. Resing, J. A. Goodrich, and N. G. Ahn. 2002. Phosphatase inhibition leads to histone deacetylases 1 and 2 phosphorylation and disruption of corepressor interactions. J. Biol. Chem. 277: 19618-19626.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19618-19626
    • Galasinski, S.C.1    Resing, K.A.2    Goodrich, J.A.3    Ahn, N.G.4
  • 14
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • Gregoretti, I. V., Y. M. Lee, and H. V. Goodson. 2004. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J. Mol. Biol. 338:17-31.
    • (2004) J. Mol. Biol. , vol.338 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 15
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • Grozinger, C. M., and S. L. Schreiber. 2002. Deacetylase enzymes: biological functions and the use of small-molecule inhibitors. Chem. Biol. 9:3-16.
    • (2002) Chem. Biol. , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 16
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • DOI 10.1038/38664
    • Grunstein, M. 1997. Histone acetylation in chromatin structure and transcription. Nature 389:349-352. (Pubitemid 27415209)
    • (1997) Nature , vol.389 , Issue.6649 , pp. 349-352
    • Grunstein, M.1
  • 17
    • 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., Y. Liang, G. Mandel, and B. Roizman. 2005. Components of the REST/CoREST/histone deacetylase repressor complex are disrupted, modified, and translocated in HSV-1-infected cells. Proc. Natl. Acad. Sci. USA 102:7571-7576.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7571-7576
    • Gu, H.1    Liang, Y.2    Mandel, G.3    Roizman, B.4
  • 18
    • 66149091440 scopus 로고    scopus 로고
    • Engagement of the lysine-specific demethylase/ HDAC1/CoREST/REST complex by herpes simplex virus 1
    • Gu, H., and B. Roizman. 2009. Engagement of the lysine-specific demethylase/ HDAC1/CoREST/REST complex by herpes simplex virus 1. J. Virol. 83:4376-4385.
    • (2009) J. Virol. , vol.83 , pp. 4376-4385
    • Gu, H.1    Roizman, B.2
  • 19
    • 36749032258 scopus 로고    scopus 로고
    • Herpes simplex virus-infected cell protein 0 blocks the silencing of viral DNA by dissociating histone deacetylases from the CoREST-REST complex
    • Gu, H., and B. Roizman. 2007. Herpes simplex virus-infected cell protein 0 blocks the silencing of viral DNA by dissociating histone deacetylases from the CoREST-REST complex. Proc. Natl. Acad. Sci. USA 104:17134-17139.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17134-17139
    • Gu, H.1    Roizman, B.2
  • 20
    • 0035136167 scopus 로고    scopus 로고
    • CREB-binding protein and histone deacetylase regulate the transcriptional activity of Kaposi's sarcoma-associated herpesvirus open reading frame 50
    • DOI 10.1128/JVI.75.4.1909-1917.2001
    • Gwack, Y., H. Byun, S. Hwang, C. Lim, and J. Choe. 2001. CREB-binding protein and histone deacetylase regulate the transcriptional activity of Kaposi's sarcoma-associated herpesvirus open reading frame 50. J. Virol. 75: 1909-1917. (Pubitemid 32110181)
    • (2001) Journal of Virology , vol.75 , Issue.4 , pp. 1909-1917
    • Gwack, Y.1    Byun, H.2    Hwang, S.3    Lim, C.4    Choe, J.5
  • 21
    • 57749170458 scopus 로고    scopus 로고
    • The many roles of histone deacetylases in development and physiology: Implications for disease and therapy
    • Haberland, M., R. L. Montgomery, and E. N. Olson. 2009. The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat. Rev. Genet. 10:32-42.
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 32-42
    • Haberland, M.1    Montgomery, R.L.2    Olson, E.N.3
  • 22
    • 0028971167 scopus 로고
    • The varicella-zoster virus (VZV) open reading frame 47 (ORF47) protein kinase is dispensable for viral replication and is not required for phosphorylation of ORF63 protein, the VZV homolog of herpes simplex virus ICP22
    • Heineman, T. C., and J. I. Cohen. 1995. The varicella-zoster virus (VZV) open reading frame 47 (ORF47) protein kinase is dispensable for viral replication and is not required for phosphorylation of ORF63 protein, the VZV homolog of herpes simplex virus ICP22. J. Virol. 69:7367-7370.
    • (1995) J. Virol. , vol.69 , pp. 7367-7370
    • Heineman, T.C.1    Cohen, J.I.2
  • 23
    • 0344995285 scopus 로고    scopus 로고
    • Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0
    • Hobbs, W. E., II, and N. A. DeLuca. 1999. Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0. J. Virol. 73:8245-8255.
    • (1999) J. Virol. , vol.73 , pp. 8245-8255
    • Hobbs II, W.E.1    DeLuca, N.A.2
  • 24
    • 20444377669 scopus 로고    scopus 로고
    • Varicella-zoster virus open reading frame 47 (ORF47) protein is critical for virus replication in dendritic cells and for spread to other cells
    • DOI 10.1016/j.virol.2005.04.024, PII S0042682205002576
    • Hu, H., and J. I. Cohen. 2005. Varicella-zoster virus open reading frame 47 (ORF47) protein is critical for virus replication in dendritic cells and for spread to other cells. Virology 337:304-311. (Pubitemid 40798998)
    • (2005) Virology , vol.337 , Issue.2 , pp. 304-311
    • Hu, H.1    Cohen, J.I.2
  • 25
    • 0037401625 scopus 로고    scopus 로고
    • Comparison of varicella-zoster virus ORF47 protein kinase and casein kinase II and their substrates
    • Kenyon, T. K., E. Homan, J. Storlie, M. Ikoma, and C. Grose. 2003. Comparison of varicella-zoster virus ORF47 protein kinase and casein kinase II and their substrates. J. Med. Virol. 70(Suppl. 1):S95-S102.
    • (2003) J. Med. Virol. , vol.70 , Issue.SUPPL. 1
    • Kenyon, T.K.1    Homan, E.2    Storlie, J.3    Ikoma, M.4    Grose, C.5
  • 26
    • 0034844017 scopus 로고    scopus 로고
    • Virion association of IE62, the varicella-zoster virus (VZV) major transcriptional regulatory protein, requires expression of the VZV open reading frame 66 protein kinase
    • Kinchington, P. R., K. Fite, A. Seman, and S. E. Turse. 2001. Virion association of IE62, the varicella-zoster virus (VZV) major transcriptional regulatory protein, requires expression of the VZV open reading frame 66 protein kinase. J. Virol. 75:9106-9113.
    • (2001) J. Virol. , vol.75 , pp. 9106-9113
    • Kinchington, P.R.1    Fite, K.2    Seman, A.3    Turse, S.E.4
  • 27
    • 0033981740 scopus 로고    scopus 로고
    • Nuclear accumulation of IE62, the varicella-zoster virus (VZV) major transcriptional regulatory protein, is inhibited by phosphorylation mediated by the VZV open reading frame 66 protein kinase
    • Kinchington, P. R., K. Fite, and S. E. Turse. 2000. Nuclear accumulation of IE62, the varicella-zoster virus (VZV) major transcriptional regulatory protein, is inhibited by phosphorylation mediated by the VZV open reading frame 66 protein kinase. J. Virol. 74:2265-2277.
    • (2000) J. Virol. , vol.74 , pp. 2265-2277
    • Kinchington, P.R.1    Fite, K.2    Turse, S.E.3
  • 28
    • 0031793463 scopus 로고    scopus 로고
    • Regulated nuclear localization of the varicella-zoster virus major regulatory protein, IE62
    • Kinchington, P. R., and S. E. Turse. 1998. Regulated nuclear localization of the varicella-zoster virus major regulatory protein, IE62. J. Infect. Dis. 178(Suppl. 1):S16-S21.
    • (1998) J. Infect. Dis. , vol.178 , Issue.SUPPL. 1
    • Kinchington, P.R.1    Turse, S.E.2
  • 29
    • 66149128368 scopus 로고    scopus 로고
    • Components of nuclear domain 10 bodies regulate varicella-zoster virus replication
    • Kyratsous, C. A., and S. J. Silverstein. 2009. Components of nuclear domain 10 bodies regulate varicella-zoster virus replication. J. Virol. 83:4262-4274.
    • (2009) J. Virol. , vol.83 , pp. 4262-4274
    • Kyratsous, C.A.1    Silverstein, S.J.2
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0023056495 scopus 로고
    • Alphaherpesviruses possess a gene homologous to the protein kinase gene family of eukaryotes and retroviruses
    • McGeoch, D. J., and A. J. Davison. 1986. Alphaherpesviruses possess a gene homologous to the protein kinase gene family of eukaryotes and retroviruses. Nucleic Acids Res. 14:1765-1777.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 1765-1777
    • McGeoch, D.J.1    Davison, A.J.2
  • 34
    • 0026472080 scopus 로고
    • Varicella-zoster virus open reading frame 61 protein is functionally homologous to herpes simplex virus type 1 ICP0
    • Moriuchi, H., M. Moriuchi, H. A. Smith, S. E. Straus, and J. I. Cohen. 1992. Varicella-zoster virus open reading frame 61 protein is functionally homologous to herpes simplex virus type 1 ICP0. J. Virol. 66:7303-7308.
    • (1992) J. Virol. , vol.66 , pp. 7303-7308
    • Moriuchi, H.1    Moriuchi, M.2    Smith, H.A.3    Straus, S.E.4    Cohen, J.I.5
  • 35
    • 0027232936 scopus 로고
    • Varicella-zoster virus (VZV) open reading frame 61 protein transactivates VZV gene promoters and enhances the infectivity of VZV DNA
    • Moriuchi, H., M. Moriuchi, S. E. Straus, and J. I. Cohen. 1993. Varicella-zoster virus (VZV) open reading frame 61 protein transactivates VZV gene promoters and enhances the infectivity of VZV DNA. J. Virol. 67:4290-4295. (Pubitemid 23180756)
    • (1993) Journal of Virology , vol.67 , Issue.7 , pp. 4290-4295
    • Moriuchi, H.1    Moriuchi, M.2    Straus, S.E.3    Cohen, J.I.4
  • 36
    • 0034997338 scopus 로고    scopus 로고
    • The US3 protein kinase blocks apoptosis induced by the d120 mutant of herpes simplex virus 1 at a premitochondrial stage
    • Munger, J., A. V. Chee, and B. Roizman. 2001. The US3 protein kinase blocks apoptosis induced by the d120 mutant of herpes simplex virus 1 at a premitochondrial stage. J. Virol. 75:5491-5497.
    • (2001) J. Virol. , vol.75 , pp. 5491-5497
    • Munger, J.1    Chee, A.V.2    Roizman, B.3
  • 37
    • 1342279571 scopus 로고    scopus 로고
    • The HSV-1 Us3 protein kinase is sufficient to block apoptosis induced by overexpression of a variety of Bcl-2 family members
    • Ogg, P. D., P. J. McDonell, B. J. Ryckman, C. M. Knudson, and R. J. Roller. 2004. The HSV-1 Us3 protein kinase is sufficient to block apoptosis induced by overexpression of a variety of Bcl-2 family members. Virology 319:212-224.
    • (2004) Virology , vol.319 , pp. 212-224
    • Ogg, P.D.1    McDonell, P.J.2    Ryckman, B.J.3    Knudson, C.M.4    Roller, R.J.5
  • 38
    • 0035861594 scopus 로고    scopus 로고
    • Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation
    • Pflum, M. K., 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.1    Tong, J.K.2    Lane, W.S.3    Schreiber, S.L.4
  • 39
    • 33745617128 scopus 로고    scopus 로고
    • ICP0 and the US3 protein kinase of herpes simplex virus 1 independently block histone deacetylation to enable gene expression
    • Poon, A. P., H. Gu, and B. Roizman. 2006. ICP0 and the US3 protein kinase of herpes simplex virus 1 independently block histone deacetylation to enable gene expression. Proc. Natl. Acad. Sci. USA 103:9993-9998.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9993-9998
    • Poon, A.P.1    Gu, H.2    Roizman, B.3
  • 40
    • 0242661003 scopus 로고    scopus 로고
    • 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
    • Poon, A. P. W., Y. Liang, and B. Roizman. 2003. 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. J. Virol. 77:12671-12678.
    • (2003) J. Virol. , vol.77 , pp. 12671-12678
    • Poon, A.P.W.1    Liang, Y.2    Roizman, B.3
  • 41
    • 33846785600 scopus 로고    scopus 로고
    • Mapping of key functions of the herpes simplex virus 1 US3 protein kinase: The US3 protein can form functional heteromultimeric structures derived from overlapping truncated polypeptides
    • Poon, A. P. W., and B. Roizman. 2007. Mapping of key functions of the herpes simplex virus 1 US3 protein kinase: the US3 protein can form functional heteromultimeric structures derived from overlapping truncated polypeptides. J. Virol. 81:1980-1989.
    • (2007) J. Virol. , vol.81 , pp. 1980-1989
    • Poon, A.P.W.1    Roizman, B.2
  • 42
    • 26444541842 scopus 로고    scopus 로고
    • T-cell tropism and the role of ORF66 protein in pathogenesis of varicella-zoster virus infection
    • DOI 10.1128/JVI.79.20.12921-12933.2005
    • Schaap, A., J. F. Fortin, M. Sommer, L. Zerboni, S. Stamatis, C. C. Ku, G. P. Nolan, and A. M. Arvin. 2005. T-cell tropism and the role of ORF66 protein in pathogenesis of varicella-zoster virus infection. J. Virol. 79:12921-12933. (Pubitemid 41433211)
    • (2005) Journal of Virology , vol.79 , Issue.20 , pp. 12921-12933
    • Schaap, A.1    Fortin, J.-F.2    Sommer, M.3    Zerboni, L.4    Stamatis, S.5    Ku, C.-C.6    Nolan, G.P.7    Arvin, A.M.8
  • 43
    • 33751229031 scopus 로고    scopus 로고
    • ORF66 protein kinase function is required for T-cell tropism of varicella-zoster virus in vivo
    • DOI 10.1128/JVI.00466-06
    • Schaap-Nutt, A., M. Sommer, X. Che, L. Zerboni, and A. M. Arvin. 2006. ORF66 protein kinase function is required for T-cell tropism of varicellazoster virus in vivo. J. Virol. 80:11806-11816. (Pubitemid 44788892)
    • (2006) Journal of Virology , vol.80 , Issue.23 , pp. 11806-11816
    • Schaap-Nutt, A.1    Sommer, M.2    Che, X.3    Zerboni, L.4    Arvin, A.M.5
  • 44
    • 38649123072 scopus 로고    scopus 로고
    • Conserved Metabolic Regulatory Functions of Sirtuins
    • DOI 10.1016/j.cmet.2007.11.006, PII S1550413107003415
    • Schwer, B., and E. Verdin. 2008. Conserved metabolic regulatory functions of sirtuins. Cell Metab. 7:104-112. (Pubitemid 351168554)
    • (2008) Cell Metabolism , vol.7 , Issue.2 , pp. 104-112
    • Schwer, B.1    Verdin, E.2
  • 45
    • 0024599635 scopus 로고
    • Identification of new protein kinaserelated genes in three herpesviruses, herpes simplex virus, varicella-zoster virus, and Epstein-Barr virus
    • Smith, R. F., and T. F. Smith. 1989. Identification of new protein kinaserelated genes in three herpesviruses, herpes simplex virus, varicella-zoster virus, and Epstein-Barr virus. J. Virol. 63:450-455.
    • (1989) J. Virol. , vol.63 , pp. 450-455
    • Smith, R.F.1    Smith, T.F.2
  • 46
    • 0033934283 scopus 로고    scopus 로고
    • Infection of human T lymphocytes with varicella-zoster virus: An analysis with viral mutants and clinical isolates
    • DOI 10.1128/JVI.74.4.1864-1870.2000
    • Soong, W., J. C. Schultz, A. C. Patera, M. H. Sommer, and J. I. Cohen. 2000. Infection of human T lymphocytes with varicella-zoster virus: an analysis with viral mutants and clinical isolates. J. Virol. 74:1864-1870. (Pubitemid 30434045)
    • (2000) Journal of Virology , vol.74 , Issue.4 , pp. 1864-1870
    • Soong, W.1    Schultz, J.C.2    Patera, A.C.3    Sommer, M.H.4    Cohen, J.I.5
  • 47
    • 0028009537 scopus 로고
    • Characterization of the putative protein kinases specified by varicella-zoster virus genes 47 and 66
    • Stevenson, D., K. L. Colman, and A. J. Davison. 1994. Characterization of the putative protein kinases specified by varicella-zoster virus genes 47 and 66. J. Gen. Virol. 75:317-326.
    • (1994) J. Gen. Virol. , vol.75 , pp. 317-326
    • Stevenson, D.1    Colman, K.L.2    Davison, A.J.3
  • 48
    • 54549084341 scopus 로고    scopus 로고
    • New insights into the role of the subnuclear structure ND10 for viral infection
    • Tavalai, N., and T. Stamminger. 2008. New insights into the role of the subnuclear structure ND10 for viral infection. Biochim. Biophys. Acta 1783: 2207-2221.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2207-2221
    • Tavalai, N.1    Stamminger, T.2
  • 49
    • 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
  • 50
    • 50149084461 scopus 로고    scopus 로고
    • Nuclear import of the varicella-zoster virus latency-associated protein ORF63 in primary neurons requires expression of the lytic protein ORF61 and occurs in a proteasome-dependent manner
    • Walters, M. S., C. A. Kyratsous, S. Wan, and S. Silverstein. 2008. Nuclear import of the varicella-zoster virus latency-associated protein ORF63 in primary neurons requires expression of the lytic protein ORF61 and occurs in a proteasome-dependent manner. J. Virol. 82:8673-8686.
    • (2008) J. Virol. , vol.82 , pp. 8673-8686
    • Walters, M.S.1    Kyratsous, C.A.2    Wan, S.3    Silverstein, S.4
  • 51
    • 67650921768 scopus 로고    scopus 로고
    • Regulation of the ORF61 promoter and ORF61 functions in varicella-zoster virus replication and pathogenesis
    • Wang, L., M. Sommer, J. Rajamani, and A. M. Arvin. 2009. Regulation of the ORF61 promoter and ORF61 functions in varicella-zoster virus replication and pathogenesis. J. Virol. 83:7560-7572.
    • (2009) J. Virol. , vol.83 , pp. 7560-7572
    • Wang, L.1    Sommer, M.2    Rajamani, J.3    Arvin, A.M.4
  • 52
    • 58549083988 scopus 로고    scopus 로고
    • Host restriction factors blocking retroviral replication
    • Wolf, D., and S. P. Goff. 2008. Host restriction factors blocking retroviral replication. Annu. Rev. Genet. 42:143-163.
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 143-163
    • Wolf, D.1    Goff, S.P.2
  • 53
    • 0037382681 scopus 로고    scopus 로고
    • Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression
    • Yang, X. J., and E. Seto. 2003. Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression. Curr. Opin. Genet. Dev. 13:143-153.
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 143-153
    • Yang, X.J.1    Seto, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.