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Volumn 5, Issue 1, 2010, Pages 65-83

Initiation of lytic DNA replication in Epstein-Barr virus: Search for a common family mechanism

Author keywords

BZLF1; EBV; Epstein Barr; OriLyt; Recombination; Repair; Replication; Zta

Indexed keywords

ATM PROTEIN; CCAAT ENHANCER BINDING PROTEIN ALPHA; CHECKPOINT KINASE 2; CYCLIN DEPENDENT KINASE INHIBITOR 1; DNA BINDING PROTEIN; DNA POLYMERASE; DOUBLE STRANDED DNA; EXONUCLEASE; HELICASE; IMMEDIATE EARLY PROTEIN BZLF1; LATENCY ASSOCIATED NUCLEAR ANTIGEN; LEUCINE ZIPPER PROTEIN; MRE11 PROTEIN; NIBRIN; PROTEIN P53; RAD50 PROTEIN; SINGLE STRANDED DNA; URACIL DNA GLYCOSIDASE; VIRUS DNA; VIRUS NUCLEOPROTEIN;

EID: 74049158642     PISSN: 17460794     EISSN: None     Source Type: Journal    
DOI: 10.2217/fvl.09.69     Document Type: Review
Times cited : (10)

References (266)
  • 1
    • 4944266319 scopus 로고    scopus 로고
    • Epstein-Barr virus: 40 years on
    • Young LS, Rickinson AB: Epstein-Barr virus: 40 years on. Nat. Rev. Cancer 4(10), 757-768 (2004).
    • (2004) Nat. Rev. Cancer , vol.4 , Issue.10 , pp. 757-768
    • Young, L.S.1    Rickinson, A.B.2
  • 2
    • 31144433632 scopus 로고    scopus 로고
    • The pleiotropic effects of Kaposi's sarcoma herpesvirus
    • Schulz TF: The pleiotropic effects of Kaposi's sarcoma herpesvirus. J. Pathol. 208(2), 187-198 (2006).
    • (2006) J. Pathol , vol.208 , Issue.2 , pp. 187-198
    • Schulz, T.F.1
  • 3
    • 0025823962 scopus 로고
    • Detection of anti-Epstein-Barr-virus transactivator (ZEBRA) antibodies in sera from patients with nasopharyngeal carcinoma
    • Implicates Epstein-Barr virus (EBV) lytic-cycle gene products as a causative agent in the formation of nasopharyngeal carcinoma, ■
    • Joab I, Nicolas JC, Schwaab G et al.: Detection of anti-Epstein-Barr-virus transactivator (ZEBRA) antibodies in sera from patients with nasopharyngeal carcinoma. Int. J. Cancer 48(5), 647-649 (1991). ■ Implicates Epstein-Barr virus (EBV) lytic-cycle gene products as a causative agent in the formation of nasopharyngeal carcinoma.
    • (1991) Int. J. Cancer , vol.48 , Issue.5 , pp. 647-649
    • Joab, I.1    Nicolas, J.C.2    Schwaab, G.3
  • 4
    • 9744256149 scopus 로고    scopus 로고
    • Reactivation of latent Epstein-Barr virus by methotrexate: A potential contributor to methotrexate-associated lymphomas
    • Implicates EBV lytic cycle as a causative agent in the formation of lymphomas in rheumatiod arthritis and poliomyositis patients treated with methotrexate, ■
    • Feng WH, Cohen JI, Fischer S et al.: Reactivation of latent Epstein-Barr virus by methotrexate: a potential contributor to methotrexate-associated lymphomas. J. Natl Cancer Inst. 96(22), 1691-1702 (2004). ■ Implicates EBV lytic cycle as a causative agent in the formation of lymphomas in rheumatiod arthritis and poliomyositis patients treated with methotrexate.
    • (2004) J. Natl Cancer Inst , vol.96 , Issue.22 , pp. 1691-1702
    • Feng, W.H.1    Cohen, J.I.2    Fischer, S.3
  • 5
    • 17044436199 scopus 로고    scopus 로고
    • Exposure to holoendemic malaria results in elevated Epstein-Barr virus loads in children
    • Moormann AM, Chelimo K, Sumba OP et al.: Exposure to holoendemic malaria results in elevated Epstein-Barr virus loads in children. J. Infect. Dis. 191(8), 1233-1238 (2005).
    • (2005) J. Infect. Dis , vol.191 , Issue.8 , pp. 1233-1238
    • Moormann, A.M.1    Chelimo, K.2    Sumba, O.P.3
  • 6
    • 34347359743 scopus 로고    scopus 로고
    • A molecular link between malaria and Epstein-Barr virus reactivation
    • The plasmodium falciparum 1 membrane protein is able to induce lytic EBV, ■
    • Chene A, Donati D, Guerreiro-Cacais AO et al.: A molecular link between malaria and Epstein-Barr virus reactivation. PLoS Pathog. 3(6), e80 (2007). ■ The plasmodium falciparum 1 membrane protein is able to induce lytic EBV.
    • (2007) PLoS Pathog , vol.3 , Issue.6
    • Chene, A.1    Donati, D.2    Guerreiro-Cacais, A.O.3
  • 7
    • 67649171850 scopus 로고    scopus 로고
    • Drug targets in herpes simplex and Epstein-Barr virus infections
    • Billaud G, Thouvenot D, Morfin F: Drug targets in herpes simplex and Epstein-Barr virus infections. Infect. Disord. Drug Targets 9(2), 117-125 (2009).
    • (2009) Infect. Disord. Drug Targets , vol.9 , Issue.2 , pp. 117-125
    • Billaud, G.1    Thouvenot, D.2    Morfin, F.3
  • 8
    • 14744270253 scopus 로고    scopus 로고
    • A Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 ORF50 deletion mutant is defective for reactivation of latent virus and DNA replication
    • Xu Y, AuCoin DP, Huete AR, Cei SA, Hanson LJ, Pari GS: A Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 ORF50 deletion mutant is defective for reactivation of latent virus and DNA replication. J. Virol. 79(6), 3479-3487 (2005).
    • (2005) J. Virol , vol.79 , Issue.6 , pp. 3479-3487
    • Xu, Y.1    AuCoin, D.P.2    Huete, A.R.3    Cei, S.A.4    Hanson, L.J.5    Pari, G.S.6
  • 9
    • 0034660443 scopus 로고    scopus 로고
    • Feederle R, Kost M, Baumann M et al.: The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators. EMBO J. 19(12), 3080-3089 (2000). ■ Classical genetic study where the BRLF1 or BZLF1 genes were knocked out in the context of the full viral genome.
    • Feederle R, Kost M, Baumann M et al.: The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators. EMBO J. 19(12), 3080-3089 (2000). ■ Classical genetic study where the BRLF1 or BZLF1 genes were knocked out in the context of the full viral genome.
  • 10
    • 0023036072 scopus 로고
    • Both Epstein-Barr virus (EBV)-encoded trans-acting factors, EB1 and EB2, are required to activate transcription from an EBV early promoter
    • Chevallier-Greco A, Manet E, Chavrier P, Mosnier C, Daillie J, Sergeant A: Both Epstein-Barr virus (EBV)-encoded trans-acting factors, EB1 and EB2, are required to activate transcription from an EBV early promoter. EMBO J. 5(12), 3243-3249 (1986).
    • (1986) EMBO J , vol.5 , Issue.12 , pp. 3243-3249
    • Chevallier-Greco, A.1    Manet, E.2    Chavrier, P.3    Mosnier, C.4    Daillie, J.5    Sergeant, A.6
  • 11
    • 1642457437 scopus 로고
    • Activation of expression of latent Epstein-Barr herpesvirus after gene transfer with a small cloned subfragment of heterogeneous viral DNA
    • Countryman J, Miller G: Activation of expression of latent Epstein-Barr herpesvirus after gene transfer with a small cloned subfragment of heterogeneous viral DNA. Proc. Natl Acad. Sci. USA 82(12), 4085-4089 (1985).
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , Issue.12 , pp. 4085-4089
    • Countryman, J.1    Miller, G.2
  • 12
    • 0024379416 scopus 로고
    • The spliced BZLF1 gene of Epstein-Barr virus (EBV) transactivates an early EBV promoter and induces the virus productive cycle
    • Rooney CM, Rowe DT, Ragot T, Farrell PJ: The spliced BZLF1 gene of Epstein-Barr virus (EBV) transactivates an early EBV promoter and induces the virus productive cycle. J. Virol. 63(7), 3109-3116 (1989).
    • (1989) J. Virol , vol.63 , Issue.7 , pp. 3109-3116
    • Rooney, C.M.1    Rowe, D.T.2    Ragot, T.3    Farrell, P.J.4
  • 13
    • 0022646563 scopus 로고
    • trans activation of the latent Epstein-Barr virus (EBV) genome after transfection of the EBV DNA fragment
    • Takada K, Shimizu N, Sakuma S, Ono Y: trans activation of the latent Epstein-Barr virus (EBV) genome after transfection of the EBV DNA fragment. J. Virol. 57(3), 1016-1022 (1986).
    • (1986) J. Virol , vol.57 , Issue.3 , pp. 1016-1022
    • Takada, K.1    Shimizu, N.2    Sakuma, S.3    Ono, Y.4
  • 14
    • 0035108091 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus K-bZIP protein is phosphorylated by cyclin-dependent kinases
    • Polson AG, Huang L, Lukac DM et al.: Kaposi's sarcoma-associated herpesvirus K-bZIP protein is phosphorylated by cyclin-dependent kinases. J. Virol. 75(7), 3175-3184 (2001).
    • (2001) J. Virol , vol.75 , Issue.7 , pp. 3175-3184
    • Polson, A.G.1    Huang, L.2    Lukac, D.M.3
  • 15
    • 37049006758 scopus 로고    scopus 로고
    • Overexpression of the Kaposi's sarcoma-associated herpesvirus transactivator K-Rta can complement a K-bZIP deletion BACmid and yields an enhanced growth phenotype
    • Kato-Noah T, Xu Y, Rossetto CC, Colletti K, Papouskova I, Pari GS: Overexpression of the Kaposi's sarcoma-associated herpesvirus transactivator K-Rta can complement a K-bZIP deletion BACmid and yields an enhanced growth phenotype. J. Virol. 81(24), 13519-13532 (2007).
    • (2007) J. Virol , vol.81 , Issue.24 , pp. 13519-13532
    • Kato-Noah, T.1    Xu, Y.2    Rossetto, C.C.3    Colletti, K.4    Papouskova, I.5    Pari, G.S.6
  • 16
    • 27644567614 scopus 로고    scopus 로고
    • Epstein-Barr virus lytic infection contributes to lymphoproliferative disease in a SCID mouse model
    • Demonstrates the importance of lytic replication and, specifically, the BZLF1 gene in EBV-induced tumorigenesis, ■■
    • Hong GK, Gulley ML, Feng WH, Delecluse HJ, Holley-Guthrie E, Kenney SC: Epstein-Barr virus lytic infection contributes to lymphoproliferative disease in a SCID mouse model. J. Virol. 79(22), 13993-14003 (2005). ■■ Demonstrates the importance of lytic replication and, specifically, the BZLF1 gene in EBV-induced tumorigenesis.
    • (2005) J. Virol , vol.79 , Issue.22 , pp. 13993-14003
    • Hong, G.K.1    Gulley, M.L.2    Feng, W.H.3    Delecluse, H.J.4    Holley-Guthrie, E.5    Kenney, S.C.6
  • 17
    • 27644499031 scopus 로고    scopus 로고
    • Epstein-Barr virus lytic infection is required for efficient production of the angiogenesis factor vascular endothelial growth factor in lymphoblastoid cell lines
    • Hong GK, Kumar P, Wang L et al.: Epstein-Barr virus lytic infection is required for efficient production of the angiogenesis factor vascular endothelial growth factor in lymphoblastoid cell lines. J. Virol. 79(22), 13984-13992 (2005).
    • (2005) J. Virol , vol.79 , Issue.22 , pp. 13984-13992
    • Hong, G.K.1    Kumar, P.2    Wang, L.3
  • 18
    • 0027201577 scopus 로고
    • Viral interleukin 10 is critical for the induction of B cell growth transformation by Epstein-Barr virus
    • Miyazaki I, Cheung RK, Dosch HM: Viral interleukin 10 is critical for the induction of B cell growth transformation by Epstein-Barr virus. J. Exp. Med. 178(2), 439-447 (1993).
    • (1993) J. Exp. Med , vol.178 , Issue.2 , pp. 439-447
    • Miyazaki, I.1    Cheung, R.K.2    Dosch, H.M.3
  • 19
    • 0028824268 scopus 로고
    • The Epstein-Barr virus encoded cytokine viral interleukin-10 enhances transformation of human B lymphocytes
    • Stuart AD, Stewart JP, Arrand JR, Mackett M: The Epstein-Barr virus encoded cytokine viral interleukin-10 enhances transformation of human B lymphocytes. Oncogene 11(9), 1711-1719 (1995).
    • (1995) Oncogene , vol.11 , Issue.9 , pp. 1711-1719
    • Stuart, A.D.1    Stewart, J.P.2    Arrand, J.R.3    Mackett, M.4
  • 20
    • 0026584291 scopus 로고
    • Interleukin 10 is a potent growth and differentiation factor for activated human B lymphocytes
    • Rousset F, Garcia E, Defrance T et al.: Interleukin 10 is a potent growth and differentiation factor for activated human B lymphocytes. Proc. Natl Acad. Sci. USA 89(5), 1890-1893 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , Issue.5 , pp. 1890-1893
    • Rousset, F.1    Garcia, E.2    Defrance, T.3
  • 21
    • 0024424127 scopus 로고
    • Epstein-Barr virus bicistronic mRNAs generated by facultative splicing code for two transcriptional trans-activators
    • Manet E, Gruffat H, Trescol-Biemont MC et al.: Epstein-Barr virus bicistronic mRNAs generated by facultative splicing code for two transcriptional trans-activators. EMBO J. 8(6), 1819-1826 (1989).
    • (1989) EMBO J , vol.8 , Issue.6 , pp. 1819-1826
    • Manet, E.1    Gruffat, H.2    Trescol-Biemont, M.C.3
  • 22
    • 0033604293 scopus 로고    scopus 로고
    • Gene expression from the ORF50/K8 region of Kaposi's sarcoma-associated herpesvirus
    • Seaman WT, Ye D, Wang RX, Hale EE, Weisse M, Quinlivan EB: Gene expression from the ORF50/K8 region of Kaposi's sarcoma-associated herpesvirus. Virology 263(2), 436-449 (1999).
    • (1999) Virology , vol.263 , Issue.2 , pp. 436-449
    • Seaman, W.T.1    Ye, D.2    Wang, R.X.3    Hale, E.E.4    Weisse, M.5    Quinlivan, E.B.6
  • 23
    • 18744390485 scopus 로고    scopus 로고
    • Reactivation of Epstein-Barr virus from latency
    • Amon W, Farrell PJ: Reactivation of Epstein-Barr virus from latency. Rev. Med. Virol. 15(3), 149-156 (2005).
    • (2005) Rev. Med. Virol , vol.15 , Issue.3 , pp. 149-156
    • Amon, W.1    Farrell, P.J.2
  • 24
    • 0030760456 scopus 로고    scopus 로고
    • Reactivation of Epstein-Barr virus: Regulation and function of the BZLF1 gene
    • Speck SH, Chatila T, Flemington E: Reactivation of Epstein-Barr virus: regulation and function of the BZLF1 gene. Trends Microbiol. 5(10), 399-405 (1997).
    • (1997) Trends Microbiol , vol.5 , Issue.10 , pp. 399-405
    • Speck, S.H.1    Chatila, T.2    Flemington, E.3
  • 25
    • 84929262107 scopus 로고    scopus 로고
    • Reactivation and lytic replication of EBV
    • Arvin A, Campadelli-Fiume G, Mocarski E et al, Eds, Cambridge University Press, NY, USA
    • Kenney SC: Reactivation and lytic replication of EBV. In: Human Herpesviruses. Arvin A, Campadelli-Fiume G, Mocarski E et al. (Eds). Cambridge University Press, NY, USA, 403-433 (2007).
    • (2007) Human Herpesviruses , pp. 403-433
    • Kenney, S.C.1
  • 26
    • 0022919477 scopus 로고
    • A method for identifying the viral genes required for herpesvirus DNA replication
    • Landmark study that identified the herpesvirus core lytic replication proteins using complementation assays and a plasmid containing the lytic origin, ■■
    • Challberg MD: A method for identifying the viral genes required for herpesvirus DNA replication. Proc. Natl Acad. Sci. USA 83(23), 9094-9098 (1986). ■■ Landmark study that identified the herpesvirus core lytic replication proteins using complementation assays and a plasmid containing the lytic origin.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , Issue.23 , pp. 9094-9098
    • Challberg, M.D.1
  • 27
    • 0026708186 scopus 로고
    • trans-acting requirements for replication of Epstein-Barr virus Ori-Lyt
    • Identification of the core replication proteins required for lytic EBV replication, ■
    • Fixman ED, Hayward GS, Hayward SD: trans-acting requirements for replication of Epstein-Barr virus Ori-Lyt. J. Virol. 66(8), 5030-5039 (1992). ■ Identification of the core replication proteins required for lytic EBV replication.
    • (1992) J. Virol , vol.66 , Issue.8 , pp. 5030-5039
    • Fixman, E.D.1    Hayward, G.S.2    Hayward, S.D.3
  • 28
    • 0027417232 scopus 로고
    • Open reading frames UL44, IRS1/TRS1, and UL36-38 are required for transient complementation of human cytomegalovirus OriLyt-dependent DNA synthesis
    • Pari GS, Kacica MA, Anders DG: Open reading frames UL44, IRS1/TRS1, and UL36-38 are required for transient complementation of human cytomegalovirus OriLyt-dependent DNA synthesis. J. Virol. 67(5), 2575-2582 (1993).
    • (1993) J. Virol , vol.67 , Issue.5 , pp. 2575-2582
    • Pari, G.S.1    Kacica, M.A.2    Anders, D.G.3
  • 29
    • 0027448623 scopus 로고
    • Eleven loci encoding trans-acting factors are required for transient complementation of human cytomegalovirus OriLyt-dependent DNA replication
    • Pari GS, Anders DG: Eleven loci encoding trans-acting factors are required for transient complementation of human cytomegalovirus OriLyt-dependent DNA replication. J. Virol. 67(12), 6979-6988 (1993).
    • (1993) J. Virol , vol.67 , Issue.12 , pp. 6979-6988
    • Pari, G.S.1    Anders, D.G.2
  • 30
    • 0035152285 scopus 로고    scopus 로고
    • Origin-independent assembly of Kaposi's sarcoma-associated herpesvirus DNA replication compartments in transient cotransfection assays and association with the ORF-K8 protein and cellular PML
    • Wu FY, Ahn JH, Alcendor DJ et al.: Origin-independent assembly of Kaposi's sarcoma-associated herpesvirus DNA replication compartments in transient cotransfection assays and association with the ORF-K8 protein and cellular PML. J. Virol. 75(3), 1487-1506 (2001).
    • (2001) J. Virol , vol.75 , Issue.3 , pp. 1487-1506
    • Wu, F.Y.1    Ahn, J.H.2    Alcendor, D.J.3
  • 31
    • 0026354526 scopus 로고
    • Primer terminus recognition and highly processive replication by Epstein-Barr virus DNA polymerase
    • Tsurumi T: Primer terminus recognition and highly processive replication by Epstein-Barr virus DNA polymerase. Biochem. J. 280(Pt 3), 703-708 (1991).
    • (1991) Biochem. J , vol.280 , Issue.PART 3 , pp. 703-708
    • Tsurumi, T.1
  • 32
    • 0025830042 scopus 로고
    • Characterization of 3′-to 5′-exonuclease activity associated with Epstein-Barr virus DNA polymerase
    • Tsurumi T: Characterization of 3′-to 5′-exonuclease activity associated with Epstein-Barr virus DNA polymerase. Virology 182(1), 376-381 (1991).
    • (1991) Virology , vol.182 , Issue.1 , pp. 376-381
    • Tsurumi, T.1
  • 33
    • 0034100143 scopus 로고    scopus 로고
    • The Epstein-Barr virus pol catalytic subunit physically interacts with the BBLF4-BSLF1- BBLF2/3 complex
    • Fujii K, Yokoyama N, Kiyono T et al.: The Epstein-Barr virus pol catalytic subunit physically interacts with the BBLF4-BSLF1- BBLF2/3 complex. J. Virol. 74(6), 2550-2557 (2000).
    • (2000) J. Virol , vol.74 , Issue.6 , pp. 2550-2557
    • Fujii, K.1    Yokoyama, N.2    Kiyono, T.3
  • 34
    • 0032697055 scopus 로고    scopus 로고
    • Assembly of the Epstein-Barr virus BBLF4, BSLF1 and BBLF2/3 proteins and their interactive properties
    • Yokoyama N, Fujii K, Hirata M et al.: Assembly of the Epstein-Barr virus BBLF4, BSLF1 and BBLF2/3 proteins and their interactive properties. J. Gen. Virol. 80(Pt 11), 2879-2887 (1999).
    • (1999) J. Gen. Virol , vol.80 , Issue.PART 11 , pp. 2879-2887
    • Yokoyama, N.1    Fujii, K.2    Hirata, M.3
  • 35
    • 0025784487 scopus 로고
    • Cooperation of EBV DNA polymerase and EA-D(BMRF1) in vitro and colocalization in nuclei of infected cells
    • Kiehl A, Dorsky DI: Cooperation of EBV DNA polymerase and EA-D(BMRF1) in vitro and colocalization in nuclei of infected cells. Virology 184(1), 330-340 (1991).
    • (1991) Virology , vol.184 , Issue.1 , pp. 330-340
    • Kiehl, A.1    Dorsky, D.I.2
  • 36
    • 0023270119 scopus 로고
    • Association of Epstein-Barr virus early antigen diffuse component and virus-specified DNA polymerase activity
    • Li JS, Zhou BS, Dutschman GE, Grill SP, Tan RS, Cheng YC: Association of Epstein-Barr virus early antigen diffuse component and virus-specified DNA polymerase activity. J. Virol. 61(9), 2947-2949 (1987).
    • (1987) J. Virol , vol.61 , Issue.9 , pp. 2947-2949
    • Li, J.S.1    Zhou, B.S.2    Dutschman, G.E.3    Grill, S.P.4    Tan, R.S.5    Cheng, Y.C.6
  • 37
    • 33646442894 scopus 로고    scopus 로고
    • The Epstein-Barr virus BMRF1 gene is essential for lytic virus replication
    • Neuhierl B, Delecluse HJ: The Epstein-Barr virus BMRF1 gene is essential for lytic virus replication. J. Virol. 80(10), 5078-5081 (2006).
    • (2006) J. Virol , vol.80 , Issue.10 , pp. 5078-5081
    • Neuhierl, B.1    Delecluse, H.J.2
  • 38
    • 0031592603 scopus 로고    scopus 로고
    • The Epstein-Barr virus (EBV) DNA polymerase accessory protein, BMRF1, activates the essential downstream component of the EBV OriLyt
    • Zhang Q, Holley-Guthrie E, Ge JQ, Dorsky D, Kenney S: The Epstein-Barr virus (EBV) DNA polymerase accessory protein, BMRF1, activates the essential downstream component of the EBV OriLyt. Virology 230(1), 22-34 (1997).
    • (1997) Virology , vol.230 , Issue.1 , pp. 22-34
    • Zhang, Q.1    Holley-Guthrie, E.2    Ge, J.Q.3    Dorsky, D.4    Kenney, S.5
  • 39
    • 69249096140 scopus 로고    scopus 로고
    • Epstein-Barr virus polymerase processivity factor enhances BALF2 promoter transcription as a coactivator for the BZLF1 immediate-early protein
    • Nakayama S, Murata T, Murayama K et al.: Epstein-Barr virus polymerase processivity factor enhances BALF2 promoter transcription as a coactivator for the BZLF1 immediate-early protein. J. Biol. Chem. 284, 21557-21568 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 21557-21568
    • Nakayama, S.1    Murata, T.2    Murayama, K.3
  • 40
    • 0034636035 scopus 로고    scopus 로고
    • Leading and lagging strand DNA synthesis in vitro by a reconstituted herpes simplex virus type 1 replisome
    • Falkenberg M, Lehman IR, Elias P: Leading and lagging strand DNA synthesis in vitro by a reconstituted herpes simplex virus type 1 replisome. Proc. Natl Acad. Sci. USA 97(8), 3896-3900 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , Issue.8 , pp. 3896-3900
    • Falkenberg, M.1    Lehman, I.R.2    Elias, P.3
  • 41
    • 0025151577 scopus 로고
    • Herpes simplex virus DNA synthesis at a preformed replication fork in vitro
    • Rabkin SD, Hanlon B: Herpes simplex virus DNA synthesis at a preformed replication fork in vitro. J. Virol. 64(10), 4957-4967 (1990).
    • (1990) J. Virol , vol.64 , Issue.10 , pp. 4957-4967
    • Rabkin, S.D.1    Hanlon, B.2
  • 42
    • 0022504850 scopus 로고
    • Identification of a varicella-zoster virus origin of DNA replication and its activation by herpes simplex virus type 1 gene products
    • Stow ND, Davison AJ: Identification of a varicella-zoster virus origin of DNA replication and its activation by herpes simplex virus type 1 gene products. J. Gen. Virol. 67(Pt 8), 1613-1623 (1986).
    • (1986) J. Gen. Virol , vol.67 , Issue.PART 8 , pp. 1613-1623
    • Stow, N.D.1    Davison, A.J.2
  • 43
    • 0029817470 scopus 로고    scopus 로고
    • Evidence that the UL84 gene product of human cytomegalovirus is essential for promoting OriLyt-dependent DNA replication and formation of replication compartments in cotransfection assays
    • Sarisky RT, Hayward GS: Evidence that the UL84 gene product of human cytomegalovirus is essential for promoting OriLyt-dependent DNA replication and formation of replication compartments in cotransfection assays. J. Virol. 70(11), 7398-7413 (1996).
    • (1996) J. Virol , vol.70 , Issue.11 , pp. 7398-7413
    • Sarisky, R.T.1    Hayward, G.S.2
  • 44
    • 0027256815 scopus 로고
    • The lytic origin of herpesvirus papio is highly homologous to Epstein-Barr virus Ori-Lyt: Evolutionary conservation of transcriptional activation and replication signals
    • Ryon JJ, Fixman ED, Houchens C et al.: The lytic origin of herpesvirus papio is highly homologous to Epstein-Barr virus Ori-Lyt: evolutionary conservation of transcriptional activation and replication signals. J. Virol. 67(7), 4006-4016 (1993).
    • (1993) J. Virol , vol.67 , Issue.7 , pp. 4006-4016
    • Ryon, J.J.1    Fixman, E.D.2    Houchens, C.3
  • 45
    • 10744231280 scopus 로고    scopus 로고
    • The Rep protein of adeno-associated virus type 2 interacts with single-stranded DNA-binding proteins that enhance viral replication
    • Stracker TH, Cassell GD, Ward P et al.: The Rep protein of adeno-associated virus type 2 interacts with single-stranded DNA-binding proteins that enhance viral replication. J. Virol. 78(1), 441-453 (2004).
    • (2004) J. Virol , vol.78 , Issue.1 , pp. 441-453
    • Stracker, T.H.1    Cassell, G.D.2    Ward, P.3
  • 46
    • 34247608619 scopus 로고    scopus 로고
    • Live covisualization of competing adeno-associated virus and herpes simplex virus type 1 DNA replication: Molecular mechanisms of interaction
    • Glauser DL, Strasser R, Laimbacher AS et al.: Live covisualization of competing adeno-associated virus and herpes simplex virus type 1 DNA replication: molecular mechanisms of interaction. J. Virol. 81(9), 4732-4743 (2007).
    • (2007) J. Virol , vol.81 , Issue.9 , pp. 4732-4743
    • Glauser, D.L.1    Strasser, R.2    Laimbacher, A.S.3
  • 47
    • 0023216413 scopus 로고
    • Herpes simplex virus infection generates large tandemly reiterated simian virus 40 DNA molecules in a transformed hamster cell line
    • Matz B: Herpes simplex virus infection generates large tandemly reiterated simian virus 40 DNA molecules in a transformed hamster cell line. J. Virol. 61(5), 1427-1434 (1987).
    • (1987) J. Virol , vol.61 , Issue.5 , pp. 1427-1434
    • Matz, B.1
  • 48
    • 0022973340 scopus 로고
    • A DNA binding protein specific for an origin of replication of herpes simplex virus type 1
    • Describes a study that led to the identification of UL9 as the herpes simplex virus (HSV) origin-binding protein, ■
    • Elias P, O'Donnell ME, Mocarski ES, Lehman IR: A DNA binding protein specific for an origin of replication of herpes simplex virus type 1. Proc. Natl Acad. Sci. USA 83(17), 6322-6326 (1986). ■ Describes a study that led to the identification of UL9 as the herpes simplex virus (HSV) origin-binding protein.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , Issue.17 , pp. 6322-6326
    • Elias, P.1    O'Donnell, M.E.2    Mocarski, E.S.3    Lehman, I.R.4
  • 49
    • 0007761340 scopus 로고
    • Herpes simplex virus DNA replication: The UL9 gene encodes an origin-binding protein
    • Describes a study that led to the identification of UL9 as the herpes simplex virus (HSV) origin-binding protein, ■
    • Olivo PD, Nelson NJ, Challberg MD: Herpes simplex virus DNA replication: the UL9 gene encodes an origin-binding protein. Proc. Natl Acad. Sci. USA 85(15), 5414-5418 (1988). ■ Describes a study that led to the identification of UL9 as the herpes simplex virus (HSV) origin-binding protein.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , Issue.15 , pp. 5414-5418
    • Olivo, P.D.1    Nelson, N.J.2    Challberg, M.D.3
  • 50
    • 0025894954 scopus 로고
    • The herpes simplex virus 1 origin binding protein: A DNA helicase
    • Bruckner RC, Crute JJ, Dodson MS, Lehman IR: The herpes simplex virus 1 origin binding protein: a DNA helicase. J. Biol. Chem. 266(4), 2669-2674 (1991).
    • (1991) J. Biol. Chem , vol.266 , Issue.4 , pp. 2669-2674
    • Bruckner, R.C.1    Crute, J.J.2    Dodson, M.S.3    Lehman, I.R.4
  • 51
    • 0026769351 scopus 로고
    • Purification and characterization of UL9, the herpes simplex virus type 1 origin-binding protein
    • Fierer DS, Challberg MD: Purification and characterization of UL9, the herpes simplex virus type 1 origin-binding protein. J. Virol. 66(7), 3986-3995 (1992).
    • (1992) J. Virol , vol.66 , Issue.7 , pp. 3986-3995
    • Fierer, D.S.1    Challberg, M.D.2
  • 52
    • 0028304810 scopus 로고
    • Herpes simplex virus DNA replication: A spacer sequence directs the ATP-dependent formation of a nucleoprotein complex at OriS
    • Gustafsson CM, Hammarsten O, Falkenberg M, Elias P: Herpes simplex virus DNA replication: a spacer sequence directs the ATP-dependent formation of a nucleoprotein complex at OriS. Proc. Natl Acad. Sci. USA 91(11), 4629-4633 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , Issue.11 , pp. 4629-4633
    • Gustafsson, C.M.1    Hammarsten, O.2    Falkenberg, M.3    Elias, P.4
  • 53
    • 0025946441 scopus 로고
    • Herpes simplex virus origin-binding protein (UL9) loops and distorts the viral replication origin
    • Koff A, Schwedes JF, Tegtmeyer P: Herpes simplex virus origin-binding protein (UL9) loops and distorts the viral replication origin. J. Virol. 65(6), 3284-3292 (1991).
    • (1991) J. Virol , vol.65 , Issue.6 , pp. 3284-3292
    • Koff, A.1    Schwedes, J.F.2    Tegtmeyer, P.3
  • 54
    • 0029923754 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 origin-binding protein carries out origin specific DNA unwinding and forms stem-loop structures
    • Makhov AM, Boehmer PE, Lehman IR, Griffith JD: The herpes simplex virus type 1 origin-binding protein carries out origin specific DNA unwinding and forms stem-loop structures. EMBO J. 15(7), 1742-1750 (1996).
    • (1996) EMBO J , vol.15 , Issue.7 , pp. 1742-1750
    • Makhov, A.M.1    Boehmer, P.E.2    Lehman, I.R.3    Griffith, J.D.4
  • 55
    • 0029902725 scopus 로고    scopus 로고
    • Visualization of the unwinding of long DNA chains by the herpes simplex virus type 1 UL9 protein and ICP8
    • Makhov AM, Boehmer PE, Lehman IR, Griffith JD: Visualization of the unwinding of long DNA chains by the herpes simplex virus type 1 UL9 protein and ICP8. J. Mol. Biol. 258(5), 789-799 (1996).
    • (1996) J. Mol. Biol , vol.258 , Issue.5 , pp. 789-799
    • Makhov, A.M.1    Boehmer, P.E.2    Lehman, I.R.3    Griffith, J.D.4
  • 56
    • 0037417785 scopus 로고    scopus 로고
    • Origin-specific unwinding of herpes simplex virus 1 DNA by the viral UL9 and ICP8 proteins: Visualization of a specific preunwinding complex
    • Makhov AM, Lee SS, Lehman IR, Griffith JD: Origin-specific unwinding of herpes simplex virus 1 DNA by the viral UL9 and ICP8 proteins: visualization of a specific preunwinding complex. Proc. Natl Acad. Sci. USA 100(3), 898-903 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , Issue.3 , pp. 898-903
    • Makhov, A.M.1    Lee, S.S.2    Lehman, I.R.3    Griffith, J.D.4
  • 57
    • 4143114587 scopus 로고    scopus 로고
    • Human cytomegalovirus UL84 oligomerization and heterodimerization domains act as transdominant inhibitors of OriLyt-dependent DNA replication: Evidence that IE2-UL84 and UL84-UL84 interactions are required for lytic DNA replication
    • Colletti KS, Xu Y, Cei SA, Tarrant M, Pari GS: Human cytomegalovirus UL84 oligomerization and heterodimerization domains act as transdominant inhibitors of OriLyt-dependent DNA replication: evidence that IE2-UL84 and UL84-UL84 interactions are required for lytic DNA replication. J. Virol. 78(17), 9203-9214 (2004).
    • (2004) J. Virol , vol.78 , Issue.17 , pp. 9203-9214
    • Colletti, K.S.1    Xu, Y.2    Cei, S.A.3    Tarrant, M.4    Pari, G.S.5
  • 58
    • 15744394113 scopus 로고    scopus 로고
    • Human cytomegalovirus UL84 is a phosphoprotein that exhibits UTPase activity and is a putative member of the DExD/H box family of proteins
    • Colletti KS, Xu Y, Yamboliev I, Pari GS: Human cytomegalovirus UL84 is a phosphoprotein that exhibits UTPase activity and is a putative member of the DExD/H box family of proteins. J. Biol. Chem. 280(12), 11955-11960 (2005).
    • (2005) J. Biol. Chem , vol.280 , Issue.12 , pp. 11955-11960
    • Colletti, K.S.1    Xu, Y.2    Yamboliev, I.3    Pari, G.S.4
  • 59
    • 34250837358 scopus 로고    scopus 로고
    • Human cytomegalovirus UL84 interacts with an RNA stem-loop sequence found within the RNA/DNA hybrid region of OriLyt
    • Identifcation of a stem-loop RNA structure, bound by UL84, within an RNA/DNA hybrid region of cytomegalovirus OriLyt, ■
    • Colletti KS, Smallenburg KE, Xu Y, Pari GS: Human cytomegalovirus UL84 interacts with an RNA stem-loop sequence found within the RNA/DNA hybrid region of OriLyt. J. Virol. 81(13), 7077-7085 (2007). ■ Identifcation of a stem-loop RNA structure, bound by UL84, within an RNA/DNA hybrid region of cytomegalovirus OriLyt.
    • (2007) J. Virol , vol.81 , Issue.13 , pp. 7077-7085
    • Colletti, K.S.1    Smallenburg, K.E.2    Xu, Y.3    Pari, G.S.4
  • 60
    • 6344258730 scopus 로고    scopus 로고
    • Human cytomegalovirus DNA replication requires transcriptional activation via an IE2- and UL84-responsive bidirectional promoter element within OriLyt
    • Xu Y, Cei SA, Rodriguez Huete A, Colletti KS, Pari GS: Human cytomegalovirus DNA replication requires transcriptional activation via an IE2- and UL84-responsive bidirectional promoter element within OriLyt. J. Virol. 78(21), 11664-11677 (2004).
    • (2004) J. Virol , vol.78 , Issue.21 , pp. 11664-11677
    • Xu, Y.1    Cei, S.A.2    Rodriguez Huete, A.3    Colletti, K.S.4    Pari, G.S.5
  • 61
    • 0025311439 scopus 로고
    • In vitro transcriptional activation, dimerization, and DNA-binding specificity of the Epstein-Barr virus Zta protein
    • Describes the identification of Zta as a candidate origin-binding protein for EBV, ■
    • Lieberman PM, Berk AJ: In vitro transcriptional activation, dimerization, and DNA-binding specificity of the Epstein-Barr virus Zta protein. J. Virol. 64(6), 2560-2568 (1990). ■ Describes the identification of Zta as a candidate origin-binding protein for EBV.
    • (1990) J. Virol , vol.64 , Issue.6 , pp. 2560-2568
    • Lieberman, P.M.1    Berk, A.J.2
  • 62
    • 0027282974 scopus 로고
    • A transcription factor with homology to the AP-1 family links RNA transcription and DNA replication in the lytic cycle of Epstein-Barr virus
    • Describes the identification of Zta as a candidate origin-binding protein for EBV, ■
    • Schepers A, Pich D, Hammerschmidt W: A transcription factor with homology to the AP-1 family links RNA transcription and DNA replication in the lytic cycle of Epstein-Barr virus. EMBO J. 12(10), 3921-3929 (1993). ■ Describes the identification of Zta as a candidate origin-binding protein for EBV.
    • (1993) EMBO J , vol.12 , Issue.10 , pp. 3921-3929
    • Schepers, A.1    Pich, D.2    Hammerschmidt, W.3
  • 63
    • 0028915139 scopus 로고
    • Replication of Epstein-Barr virus OriLyt: Lack of a dedicated virally encoded origin-binding protein and dependence on Zta in cotransfection assays
    • Describes the identification of Zta as a candidate origin-binding protein for EBV, ■
    • Fixman ED, Hayward GS, Hayward SD: Replication of Epstein-Barr virus OriLyt: lack of a dedicated virally encoded origin-binding protein and dependence on Zta in cotransfection assays. J. Virol. 69(5), 2998-3006 (1995). ■ Describes the identification of Zta as a candidate origin-binding protein for EBV.
    • (1995) J. Virol , vol.69 , Issue.5 , pp. 2998-3006
    • Fixman, E.D.1    Hayward, G.S.2    Hayward, S.D.3
  • 64
    • 0031710581 scopus 로고    scopus 로고
    • The Epstein-Barr virus lytic transactivator Zta interacts with the helicase-primase replication proteins
    • Gao Z, Krithivas A, Finan JE et al.: The Epstein-Barr virus lytic transactivator Zta interacts with the helicase-primase replication proteins. J. Virol. 72(11), 8559-8567 (1998).
    • (1998) J. Virol , vol.72 , Issue.11 , pp. 8559-8567
    • Gao, Z.1    Krithivas, A.2    Finan, J.E.3
  • 65
    • 10644288442 scopus 로고    scopus 로고
    • The Epstein-Barr virus replication protein BBLF2/3 provides an origin-tethering function through interaction with the zinc finger DNA binding protein ZBRK1 and the KAP-1 corepressor
    • Liao G, Huang J, Fixman ED, Hayward SD: The Epstein-Barr virus replication protein BBLF2/3 provides an origin-tethering function through interaction with the zinc finger DNA binding protein ZBRK1 and the KAP-1 corepressor. J. Virol. 79(1), 245-256 (2005).
    • (2005) J. Virol , vol.79 , Issue.1 , pp. 245-256
    • Liao, G.1    Huang, J.2    Fixman, E.D.3    Hayward, S.D.4
  • 66
    • 0034881576 scopus 로고    scopus 로고
    • Interaction with the Epstein-Barr virus helicase targets Zta to DNA replication compartments
    • Liao G, Wu FY, Hayward SD: Interaction with the Epstein-Barr virus helicase targets Zta to DNA replication compartments. J. Virol. 75(18), 8792-8802 (2001).
    • (2001) J. Virol , vol.75 , Issue.18 , pp. 8792-8802
    • Liao, G.1    Wu, F.Y.2    Hayward, S.D.3
  • 67
    • 0029931715 scopus 로고    scopus 로고
    • Functional and physical interactions between the Epstein-Barr virus (EBV) proteins BZLF1 and BMRF1: Effects on EBV transcription and lytic replication
    • Zhang Q, Hong Y, Dorsky D et al.: Functional and physical interactions between the Epstein-Barr virus (EBV) proteins BZLF1 and BMRF1: effects on EBV transcription and lytic replication. J. Virol. 70(8), 5131-5142 (1996).
    • (1996) J. Virol , vol.70 , Issue.8 , pp. 5131-5142
    • Zhang, Q.1    Hong, Y.2    Dorsky, D.3
  • 68
    • 0025290086 scopus 로고
    • The Epstein-Barr virus Zta transactivator: A member of the bZIP family with unique DNA-binding specificity and a dimerization domain that lacks the characteristic heptad leucine zipper motif
    • Chang YN, Dong DL, Hayward GS, Hayward SD: The Epstein-Barr virus Zta transactivator: a member of the bZIP family with unique DNA-binding specificity and a dimerization domain that lacks the characteristic heptad leucine zipper motif. J. Virol. 64(7), 3358-3369 (1990).
    • (1990) J. Virol , vol.64 , Issue.7 , pp. 3358-3369
    • Chang, Y.N.1    Dong, D.L.2    Hayward, G.S.3    Hayward, S.D.4
  • 69
    • 0025265593 scopus 로고
    • Structure and function of the Epstein-Barr virus BZLF1 protein
    • Packham G, Economou A, Rooney CM, Rowe DT, Farrell PJ: Structure and function of the Epstein-Barr virus BZLF1 protein. J. Virol. 64(5), 2110-2116 (1990).
    • (1990) J. Virol , vol.64 , Issue.5 , pp. 2110-2116
    • Packham, G.1    Economou, A.2    Rooney, C.M.3    Rowe, D.T.4    Farrell, P.J.5
  • 70
    • 0024469056 scopus 로고
    • Epstein-Barr virus BZLF1 trans-activator specifically binds to a consensus AP-1 site and is related to c-fos
    • Farrell PJ, Rowe DT, Rooney CM, Kouzarides T: Epstein-Barr virus BZLF1 trans-activator specifically binds to a consensus AP-1 site and is related to c-fos. EMBO J. 8(1), 127-132 (1989).
    • (1989) EMBO J , vol.8 , Issue.1 , pp. 127-132
    • Farrell, P.J.1    Rowe, D.T.2    Rooney, C.M.3    Kouzarides, T.4
  • 71
    • 0024357441 scopus 로고
    • The Epstein-Barr virus early protein EB1 activates transcription from different responsive elements including AP-1 binding sites
    • Urier G, Buisson M, Chambard P, Sergeant A: The Epstein-Barr virus early protein EB1 activates transcription from different responsive elements including AP-1 binding sites. EMBO J. 8(5), 1447-1453 (1989).
    • (1989) EMBO J , vol.8 , Issue.5 , pp. 1447-1453
    • Urier, G.1    Buisson, M.2    Chambard, P.3    Sergeant, A.4
  • 72
    • 0025255970 scopus 로고
    • The Zta transactivator involved in induction of lytic cycle gene expression in Epstein-Barr virus-infected lymphocytes binds to both AP-1 and ZRE sites in target promoter and enhancer regions
    • Characterization of Zta binding sites within EBV OriLyt, ■
    • Lieberman PM, Hardwick JM, Sample J, Hayward GS, Hayward SD: The Zta transactivator involved in induction of lytic cycle gene expression in Epstein-Barr virus-infected lymphocytes binds to both AP-1 and ZRE sites in target promoter and enhancer regions. J. Virol. 64(3), 1143-1155 (1990). ■ Characterization of Zta binding sites within EBV OriLyt.
    • (1990) J. Virol , vol.64 , Issue.3 , pp. 1143-1155
    • Lieberman, P.M.1    Hardwick, J.M.2    Sample, J.3    Hayward, G.S.4    Hayward, S.D.5
  • 73
    • 0025033396 scopus 로고
    • Epstein-Barr virus BZLF1 trans activator induces the promoter of a cellular cognate gene, c-fos
    • Flemington E, Speck SH: Epstein-Barr virus BZLF1 trans activator induces the promoter of a cellular cognate gene, c-fos. J. Virol. 64(9), 4549-4552 (1990).
    • (1990) J. Virol , vol.64 , Issue.9 , pp. 4549-4552
    • Flemington, E.1    Speck, S.H.2
  • 74
    • 0026680337 scopus 로고
    • Epstein-Barr virus BZLF1 transactivator is a negative regulator of Jun
    • Sato H, Takeshita H, Furukawa M, Seiki M: Epstein-Barr virus BZLF1 transactivator is a negative regulator of Jun. J. Virol. 66(8), 4732-4736 (1992).
    • (1992) J. Virol , vol.66 , Issue.8 , pp. 4732-4736
    • Sato, H.1    Takeshita, H.2    Furukawa, M.3    Seiki, M.4
  • 75
    • 61449105702 scopus 로고    scopus 로고
    • Down-regulation of MHC class II expression through inhibition of CIITA transcription by lytic transactivator Zta during Epstein-Barr virus reactivation
    • Li D, Qian L, Chen C et al.: Down-regulation of MHC class II expression through inhibition of CIITA transcription by lytic transactivator Zta during Epstein-Barr virus reactivation. J. Immunol. 182(4), 1799-1809 (2009).
    • (2009) J. Immunol , vol.182 , Issue.4 , pp. 1799-1809
    • Li, D.1    Qian, L.2    Chen, C.3
  • 76
    • 34247251319 scopus 로고    scopus 로고
    • Epstein-Barr virus lytic infection induces retinoic acid-responsive genes through induction of a retinol-metabolizing enzyme, DHRS9
    • Jones RJ, Dickerson S, Bhende PM, Delecluse HJ, Kenney SC: Epstein-Barr virus lytic infection induces retinoic acid-responsive genes through induction of a retinol-metabolizing enzyme, DHRS9. J. Biol. Chem. 282(11), 8317-8324 (2007).
    • (2007) J. Biol. Chem , vol.282 , Issue.11 , pp. 8317-8324
    • Jones, R.J.1    Dickerson, S.2    Bhende, P.M.3    Delecluse, H.J.4    Kenney, S.C.5
  • 77
    • 33746215094 scopus 로고    scopus 로고
    • Induction of the early growth response 1 gene by Epstein-Barr virus lytic transactivator Zta
    • Chang Y, Lee HH, Chen YT et al.: Induction of the early growth response 1 gene by Epstein-Barr virus lytic transactivator Zta. J. Virol. 80(15), 7748-7755 (2006).
    • (2006) J. Virol , vol.80 , Issue.15 , pp. 7748-7755
    • Chang, Y.1    Lee, H.H.2    Chen, Y.T.3
  • 78
    • 41149149117 scopus 로고    scopus 로고
    • Epstein- Barr virus lytic transactivator Zta enhances chemotactic activity through induction of interleukin-8 in nasopharyngeal carcinoma cells
    • Hsu M, Wu SY, Chang SS et al.: Epstein- Barr virus lytic transactivator Zta enhances chemotactic activity through induction of interleukin-8 in nasopharyngeal carcinoma cells. J. Virol. 82(7), 3679-3688 (2008).
    • (2008) J. Virol , vol.82 , Issue.7 , pp. 3679-3688
    • Hsu, M.1    Wu, S.Y.2    Chang, S.S.3
  • 79
    • 0037383748 scopus 로고    scopus 로고
    • A novel function for the Epstein-Barr virus transcription factor EB1/Zta: Induction of transcription of the hIL-10 gene
    • Mahot S, Sergeant A, Drouet E, Gruffat H: A novel function for the Epstein-Barr virus transcription factor EB1/Zta: induction of transcription of the hIL-10 gene. J. Gen. Virol. 84(Pt 4), 965-974 (2003).
    • (2003) J. Gen. Virol , vol.84 , Issue.PART 4 , pp. 965-974
    • Mahot, S.1    Sergeant, A.2    Drouet, E.3    Gruffat, H.4
  • 80
    • 0032872230 scopus 로고    scopus 로고
    • Characterization of the Epstein-Barr virus BALF2 promoter
    • Hung CH, Liu ST: Characterization of the Epstein-Barr virus BALF2 promoter. J. Gen. Virol. 80(Pt 10), 2747-2750 (1999).
    • (1999) J. Gen. Virol , vol.80 , Issue.PART 10 , pp. 2747-2750
    • Hung, C.H.1    Liu, S.T.2
  • 81
    • 33645017695 scopus 로고    scopus 로고
    • Regulation of the expression of the Epstein- Barr virus early gene BFRF1
    • Granato M, Farina A, Gonnella R et al.: Regulation of the expression of the Epstein- Barr virus early gene BFRF1. Virology 347(1), 109-116 (2006).
    • (2006) Virology , vol.347 , Issue.1 , pp. 109-116
    • Granato, M.1    Farina, A.2    Gonnella, R.3
  • 82
    • 0027175867 scopus 로고
    • Direct BRLF1 binding is required for cooperative BZLF1/BRLF1 activation of the Epstein-Barr virus early promoter, BMRF1
    • Quinlivan EB, Holley-Guthrie EA, Norris M, Gutsch D, Bachenheimer SL, Kenney SC: Direct BRLF1 binding is required for cooperative BZLF1/BRLF1 activation of the Epstein-Barr virus early promoter, BMRF1. Nucleic Acids Res. 21(14), 1999-2007 (1993).
    • (1993) Nucleic Acids Res , vol.21 , Issue.14 , pp. 1999-2007
    • Quinlivan, E.B.1    Holley-Guthrie, E.A.2    Norris, M.3    Gutsch, D.4    Bachenheimer, S.L.5    Kenney, S.C.6
  • 83
    • 63449134294 scopus 로고    scopus 로고
    • Dickerson SJ, Xing Y, Robinson AR, Seaman WT, Gruffat H, Kenney SC: Methylation-dependent binding of the Epstein-Barr virus BZLF1 protein to viral promoters. PLoS Pathog. 5(3), e1000356 (2009).
    • Dickerson SJ, Xing Y, Robinson AR, Seaman WT, Gruffat H, Kenney SC: Methylation-dependent binding of the Epstein-Barr virus BZLF1 protein to viral promoters. PLoS Pathog. 5(3), e1000356 (2009).
  • 84
    • 32444448106 scopus 로고    scopus 로고
    • Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein
    • Describes the acquisition of the first partial crystal structure of Zta, ■■
    • Petosa C, Morand P, Baudin F, Moulin M, Artero JB, Muller CW: Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein. Mol. Cell 21(4), 565-572 (2006). ■■ Describes the acquisition of the first partial crystal structure of Zta.
    • (2006) Mol. Cell , vol.21 , Issue.4 , pp. 565-572
    • Petosa, C.1    Morand, P.2    Baudin, F.3    Moulin, M.4    Artero, J.B.5    Muller, C.W.6
  • 85
    • 33645751236 scopus 로고    scopus 로고
    • Morand P, Budayova-Spano M, Perrissin M, Muller CW, Petosa C: Expression, purification, crystallization and preliminary x-ray analysis of a C-terminal fragment of the Epstein-Barr virus ZEBRA protein. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62(Pt 3), 210-214 (2006).
    • Morand P, Budayova-Spano M, Perrissin M, Muller CW, Petosa C: Expression, purification, crystallization and preliminary x-ray analysis of a C-terminal fragment of the Epstein-Barr virus ZEBRA protein. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62(Pt 3), 210-214 (2006).
  • 86
    • 0043169617 scopus 로고    scopus 로고
    • bZIP proteins of human γ-herpesviruses
    • Sinclair AJ: bZIP proteins of human γ-herpesviruses. J. Gen. Virol. 84(Pt 8), 1941-1949 (2003).
    • (2003) J. Gen. Virol , vol.84 , Issue.PART 8 , pp. 1941-1949
    • Sinclair, A.J.1
  • 87
    • 6944244957 scopus 로고    scopus 로고
    • The EBV lytic switch protein, Z, preferentially binds to and activates the methylated viral genome
    • First to describe the preferential binding of Zta to methylated DNA, ■
    • Bhende PM, Seaman WT, Delecluse HJ, Kenney SC: The EBV lytic switch protein, Z, preferentially binds to and activates the methylated viral genome. Nat. Genet. 36(10), 1099-1104 (2004). ■ First to describe the preferential binding of Zta to methylated DNA.
    • (2004) Nat. Genet , vol.36 , Issue.10 , pp. 1099-1104
    • Bhende, P.M.1    Seaman, W.T.2    Delecluse, H.J.3    Kenney, S.C.4
  • 88
    • 19944397140 scopus 로고    scopus 로고
    • BZLF1 activation of the methylated form of the BRLF1 immediate-early promoter is regulated by BZLF1 residue 186
    • Bhende PM, Seaman WT, Delecluse HJ, Kenney SC: BZLF1 activation of the methylated form of the BRLF1 immediate-early promoter is regulated by BZLF1 residue 186. J. Virol. 79(12), 7338-7348 (2005).
    • (2005) J. Virol , vol.79 , Issue.12 , pp. 7338-7348
    • Bhende, P.M.1    Seaman, W.T.2    Delecluse, H.J.3    Kenney, S.C.4
  • 89
    • 42949174160 scopus 로고    scopus 로고
    • Karlsson QH, Schelcher C, Verrall E, Petosa C, Sinclair AJ: Methylated DNA recognition during the reversal of epigenetic silencing is regulated by cysteine and serine residues in the Epstein-Barr virus lytic switch protein. PLoS Pathog. 4(3), e1000005 (2008).
    • Karlsson QH, Schelcher C, Verrall E, Petosa C, Sinclair AJ: Methylated DNA recognition during the reversal of epigenetic silencing is regulated by cysteine and serine residues in the Epstein-Barr virus lytic switch protein. PLoS Pathog. 4(3), e1000005 (2008).
  • 90
    • 33845427459 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus Ori-Lyt-dependent DNA replication: Dual role of replication and transcription activator
    • Wang Y, Tang Q, Maul GG, Yuan Y: Kaposi's sarcoma-associated herpesvirus Ori-Lyt-dependent DNA replication: dual role of replication and transcription activator. J. Virol. 80(24), 12171-12186 (2006).
    • (2006) J. Virol , vol.80 , Issue.24 , pp. 12171-12186
    • Wang, Y.1    Tang, Q.2    Maul, G.G.3    Yuan, Y.4
  • 91
    • 69249206510 scopus 로고    scopus 로고
    • Interaction of HCMV UL84 with C/EBPα transcription factor binding sites within OriLyt is essential for lytic DNA replication
    • Kagele D, Gao Y, Smallenburg K, Pari GS: Interaction of HCMV UL84 with C/EBPα transcription factor binding sites within OriLyt is essential for lytic DNA replication. Virology 392(1), 16-23 (2009).
    • (2009) Virology , vol.392 , Issue.1 , pp. 16-23
    • Kagele, D.1    Gao, Y.2    Smallenburg, K.3    Pari, G.S.4
  • 92
    • 0037223721 scopus 로고    scopus 로고
    • CCAAT/ enhancer binding protein a interacts with ZTA and mediates ZTA-induced p21(CIP-1) accumulation and G(1) cell cycle arrest during the Epstein-Barr virus lytic cycle
    • Wu FY, Chen H, Wang SE et al.: CCAAT/ enhancer binding protein a interacts with ZTA and mediates ZTA-induced p21(CIP-1) accumulation and G(1) cell cycle arrest during the Epstein-Barr virus lytic cycle. J. Virol. 77(2), 1481-1500 (2003).
    • (2003) J. Virol , vol.77 , Issue.2 , pp. 1481-1500
    • Wu, F.Y.1    Chen, H.2    Wang, S.E.3
  • 93
    • 0029657909 scopus 로고    scopus 로고
    • G0/G1 growth arrest mediated by a region encompassing the basic leucine zipper (bZIP) domain of the Epstein-Barr virus transactivator Zta
    • Cayrol C, Flemington E: G0/G1 growth arrest mediated by a region encompassing the basic leucine zipper (bZIP) domain of the Epstein-Barr virus transactivator Zta. J. Biol. Chem. 271(50), 31799-31802 (1996).
    • (1996) J. Biol. Chem , vol.271 , Issue.50 , pp. 31799-31802
    • Cayrol, C.1    Flemington, E.2
  • 94
    • 0030011018 scopus 로고    scopus 로고
    • The Epstein-Barr virus bZIP transcription factor Zta causes G0/G1 cell cycle arrest through induction of cyclin-dependent kinase inhibitors
    • Cayrol C, Flemington EK: The Epstein-Barr virus bZIP transcription factor Zta causes G0/G1 cell cycle arrest through induction of cyclin-dependent kinase inhibitors. EMBO J. 15(11), 2748-2759 (1996).
    • (1996) EMBO J , vol.15 , Issue.11 , pp. 2748-2759
    • Cayrol, C.1    Flemington, E.K.2
  • 95
    • 0032876837 scopus 로고    scopus 로고
    • Genetic dissection of cell growth arrest functions mediated by the Epstein-Barr virus lytic gene product, Zta
    • Rodriguez A, Armstrong M, Dwyer D, Flemington E: Genetic dissection of cell growth arrest functions mediated by the Epstein-Barr virus lytic gene product, Zta. J. Virol. 73(11), 9029-9038 (1999).
    • (1999) J. Virol , vol.73 , Issue.11 , pp. 9029-9038
    • Rodriguez, A.1    Armstrong, M.2    Dwyer, D.3    Flemington, E.4
  • 96
    • 4344575045 scopus 로고    scopus 로고
    • CCAAT/ enhancer binding protein α binds to the Epstein-Barr virus (EBV) ZTA protein through oligomeric interactions and contributes to cooperative transcriptional activation of the ZTA promoter through direct binding to the ZII and ZIIIB motifs during induction of the EBV lytic cycle
    • Wu FY, Wang SE, Chen H, Wang L, Hayward SD, Hayward GS: CCAAT/ enhancer binding protein α binds to the Epstein-Barr virus (EBV) ZTA protein through oligomeric interactions and contributes to cooperative transcriptional activation of the ZTA promoter through direct binding to the ZII and ZIIIB motifs during induction of the EBV lytic cycle. J. Virol. 78(9), 4847-4865 (2004).
    • (2004) J. Virol , vol.78 , Issue.9 , pp. 4847-4865
    • Wu, F.Y.1    Wang, S.E.2    Chen, H.3    Wang, L.4    Hayward, S.D.5    Hayward, G.S.6
  • 97
    • 0035031922 scopus 로고    scopus 로고
    • Herpesvirus lytic replication and the cell cycle: Arresting new developments
    • Flemington EK: Herpesvirus lytic replication and the cell cycle: arresting new developments. J. Virol. 75(10), 4475-4481 (2001).
    • (2001) J. Virol , vol.75 , Issue.10 , pp. 4475-4481
    • Flemington, E.K.1
  • 98
    • 0036677565 scopus 로고    scopus 로고
    • Lytic replication-associated protein (RAP) encoded by Kaposi sarcoma-associated herpesvirus causes p21CIP-1-mediated G1 cell cycle arrest through CCAAT/enhancer-binding protein-a
    • First to describe a role for C/EBP-a in herpesvirus lytic replication, ■
    • Wu FY, Tang QQ, Chen H et al.: Lytic replication-associated protein (RAP) encoded by Kaposi sarcoma-associated herpesvirus causes p21CIP-1-mediated G1 cell cycle arrest through CCAAT/enhancer-binding protein-a. Proc. Natl Acad. Sci. USA 99(16), 10683-10688 (2002). ■ First to describe a role for C/EBP-a in herpesvirus lytic replication.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.16 , pp. 10683-10688
    • Wu, F.Y.1    Tang, Q.Q.2    Chen, H.3
  • 99
    • 33846629003 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus-encoded protein kinase and its interaction with K-bZIP
    • Izumiya Y, Izumiya C, Van Geelen A et al.: Kaposi's sarcoma-associated herpesvirus-encoded protein kinase and its interaction with K-bZIP. J. Virol. 81(3), 1072-1082 (2007).
    • (2007) J. Virol , vol.81 , Issue.3 , pp. 1072-1082
    • Izumiya, Y.1    Izumiya, C.2    Van Geelen, A.3
  • 100
    • 0035422278 scopus 로고    scopus 로고
    • Human-herpesvirus-8-encoded K8 protein colocalizes with the promyelocytic leukemia protein (PML) bodies and recruits p53 to the PML bodies
    • Katano H, Ogawa-Goto K, Hasegawa H, Kurata T, Sata T: Human-herpesvirus-8-encoded K8 protein colocalizes with the promyelocytic leukemia protein (PML) bodies and recruits p53 to the PML bodies. Virology 286(2), 446-455 (2001).
    • (2001) Virology , vol.286 , Issue.2 , pp. 446-455
    • Katano, H.1    Ogawa-Goto, K.2    Hasegawa, H.3    Kurata, T.4    Sata, T.5
  • 101
    • 0041488861 scopus 로고    scopus 로고
    • Cell cycle arrest by Kaposi's sarcoma-associated herpesvirus replication-associated protein is mediated at both the transcriptional and posttranslational levels by binding to CCAAT/enhancer-binding protein α and p21(CIP-1)
    • Wu FY, Wang SE, Tang QQ et al.: Cell cycle arrest by Kaposi's sarcoma-associated herpesvirus replication-associated protein is mediated at both the transcriptional and posttranslational levels by binding to CCAAT/enhancer-binding protein α and p21(CIP-1). J. Virol. 77(16), 8893-8914 (2003).
    • (2003) J. Virol , vol.77 , Issue.16 , pp. 8893-8914
    • Wu, F.Y.1    Wang, S.E.2    Tang, Q.Q.3
  • 102
    • 0042890345 scopus 로고    scopus 로고
    • CCAAT/enhancer-binding protein-α is induced during the early stages of Kaposi's sarcoma-associated herpesvirus (KSHV) lytic cycle reactivation and together with the KSHV replication and transcription activator (RTA) cooperatively stimulates the viral RTA, MTA, and PAN promoters
    • Wang SE, Wu FY, Yu Y, Hayward GS: CCAAT/enhancer-binding protein-α is induced during the early stages of Kaposi's sarcoma-associated herpesvirus (KSHV) lytic cycle reactivation and together with the KSHV replication and transcription activator (RTA) cooperatively stimulates the viral RTA, MTA, and PAN promoters. J. Virol. 77(17), 9590-9612 (2003).
    • (2003) J. Virol , vol.77 , Issue.17 , pp. 9590-9612
    • Wang, S.E.1    Wu, F.Y.2    Yu, Y.3    Hayward, G.S.4
  • 103
    • 0037333854 scopus 로고    scopus 로고
    • K-bZIP of Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 (KSHV/HHV-8) binds KSHV/HHV-8 Rta and represses Rta-mediated transactivation
    • Liao W, Tang Y, Lin SF, Kung HJ, Giam CZ: K-bZIP of Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 (KSHV/HHV-8) binds KSHV/HHV-8 Rta and represses Rta-mediated transactivation. J. Virol. 77(6), 3809-3815 (2003).
    • (2003) J. Virol , vol.77 , Issue.6 , pp. 3809-3815
    • Liao, W.1    Tang, Y.2    Lin, S.F.3    Kung, H.J.4    Giam, C.Z.5
  • 104
    • 69249208678 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 K-bZIP modulates LANA mediated suppression of lytic origin-dependent DNA synthesis
    • Rossetto C, Yamboliev I, Pari GS: Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 K-bZIP modulates LANA mediated suppression of lytic origin-dependent DNA synthesis. J. Virol. 83(17), 8492-8501 (2009).
    • (2009) J. Virol , vol.83 , Issue.17 , pp. 8492-8501
    • Rossetto, C.1    Yamboliev, I.2    Pari, G.S.3
  • 105
    • 66149155481 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus K-bZIP protein is necessary for lytic viral gene expression, DNA replication, and virion production in primary effusion lymphoma cell lines
    • Lefort S, Flamand L: Kaposi's sarcoma-associated herpesvirus K-bZIP protein is necessary for lytic viral gene expression, DNA replication, and virion production in primary effusion lymphoma cell lines. J. Virol. 83(11), 5869-5880 (2009).
    • (2009) J. Virol , vol.83 , Issue.11 , pp. 5869-5880
    • Lefort, S.1    Flamand, L.2
  • 106
    • 0038709728 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus lytic origin (ori-Lyt)-dependent DNA replication: Identification of the ori-Lyt and association of K8 bZip protein with the origin
    • Lin CL, Li H, Wang Y, Zhu FX, Kudchodkar S, Yuan Y: Kaposi's sarcoma-associated herpesvirus lytic origin (ori-Lyt)-dependent DNA replication: identification of the ori-Lyt and association of K8 bZip protein with the origin. J. Virol. 77(10), 5578-5588 (2003).
    • (2003) J. Virol , vol.77 , Issue.10 , pp. 5578-5588
    • Lin, C.L.1    Li, H.2    Wang, Y.3    Zhu, F.X.4    Kudchodkar, S.5    Yuan, Y.6
  • 107
    • 27144531199 scopus 로고    scopus 로고
    • A redox-sensitive cysteine in Zta is required for Epstein-Barr virus lytic cycle DNA replication
    • Wang P, Day L, Dheekollu J, Lieberman PM: A redox-sensitive cysteine in Zta is required for Epstein-Barr virus lytic cycle DNA replication. J. Virol. 79(21), 13298-13309 (2005).
    • (2005) J. Virol , vol.79 , Issue.21 , pp. 13298-13309
    • Wang, P.1    Day, L.2    Dheekollu, J.3    Lieberman, P.M.4
  • 108
    • 0034842669 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-associated herpesvirus K8 protein interacts with CREB-binding protein (CBP) and represses CBP-mediated transcription
    • Hwang S, Gwack Y, Byun H, Lim C, Choe J: The Kaposi's sarcoma-associated herpesvirus K8 protein interacts with CREB-binding protein (CBP) and represses CBP-mediated transcription. J. Virol. 75(19), 9509-9516 (2001).
    • (2001) J. Virol , vol.75 , Issue.19 , pp. 9509-9516
    • Hwang, S.1    Gwack, Y.2    Byun, H.3    Lim, C.4    Choe, J.5
  • 109
    • 19944370490 scopus 로고    scopus 로고
    • Investigation of the multimerization region of the Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) protein K-bZIP: The proposed leucine zipper region encodes a multimerization domain with an unusual structure
    • Al Mehairi S, Cerasoli E, Sinclair AJ: Investigation of the multimerization region of the Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) protein K-bZIP: the proposed leucine zipper region encodes a multimerization domain with an unusual structure. J. Virol. 79(12), 7905-7910 (2005).
    • (2005) J. Virol , vol.79 , Issue.12 , pp. 7905-7910
    • Al Mehairi, S.1    Cerasoli, E.2    Sinclair, A.J.3
  • 110
    • 36048978977 scopus 로고    scopus 로고
    • Transcriptional repression of K-Rta by Kaposi's sarcoma-associated herpesvirus K-bZIP is not required for OriLyt-dependent DNA replication
    • Rossetto C, Gao Y, Yamboliev I, Papouskova I, Pari G: Transcriptional repression of K-Rta by Kaposi's sarcoma-associated herpesvirus K-bZIP is not required for OriLyt-dependent DNA replication. Virology 369(2), 340-350 (2007).
    • (2007) Virology , vol.369 , Issue.2 , pp. 340-350
    • Rossetto, C.1    Gao, Y.2    Yamboliev, I.3    Papouskova, I.4    Pari, G.5
  • 111
    • 1242328736 scopus 로고    scopus 로고
    • Amplification of the Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 lytic origin of DNA replication is dependent upon a cis-acting AT-rich region and an ORF50 response element and the trans-acting factors ORF50 (K-Rta) and K8 (K-bZIP)
    • AuCoin DP, Colletti KS, Cei SA, Papouskova I, Tarrant M, Pari GS: Amplification of the Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 lytic origin of DNA replication is dependent upon a cis-acting AT-rich region and an ORF50 response element and the trans-acting factors ORF50 (K-Rta) and K8 (K-bZIP). Virology 318(2), 542-555 (2004).
    • (2004) Virology , vol.318 , Issue.2 , pp. 542-555
    • AuCoin, D.P.1    Colletti, K.S.2    Cei, S.A.3    Papouskova, I.4    Tarrant, M.5    Pari, G.S.6
  • 112
    • 3543068693 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus ori-Lyt-dependent DNA replication: Cis-acting requirements for replication and ori-Lyt-associated RNA transcription
    • Wang Y, Li H, Chan MY, Zhu FX, Lukac DM, Yuan Y: Kaposi's sarcoma-associated herpesvirus ori-Lyt-dependent DNA replication: cis-acting requirements for replication and ori-Lyt-associated RNA transcription. J. Virol. 78(16), 8615-8629 (2004).
    • (2004) J. Virol , vol.78 , Issue.16 , pp. 8615-8629
    • Wang, Y.1    Li, H.2    Chan, M.Y.3    Zhu, F.X.4    Lukac, D.M.5    Yuan, Y.6
  • 113
    • 0020338299 scopus 로고
    • Localization of an origin of DNA replication within the TRS/IRS repeated region of the herpes simplex virus type 1 genome
    • Describes identification of the first herpesvirus lytic origins, ■■
    • Stow ND: Localization of an origin of DNA replication within the TRS/IRS repeated region of the herpes simplex virus type 1 genome. EMBO J. 1(7), 863-867 (1982). ■■ Describes identification of the first herpesvirus lytic origins.
    • (1982) EMBO J , vol.1 , Issue.7 , pp. 863-867
    • Stow, N.D.1
  • 114
    • 0021082753 scopus 로고
    • Characterization of the TRS/IRS origin of DNA replication of herpes simplex virus type 1
    • Describes identification of the first herpesvirus lytic origins, ■■
    • Stow ND, McMonagle EC: Characterization of the TRS/IRS origin of DNA replication of herpes simplex virus type 1. Virology 130(2), 427-438 (1983). ■■ Describes identification of the first herpesvirus lytic origins.
    • (1983) Virology , vol.130 , Issue.2 , pp. 427-438
    • Stow, N.D.1    McMonagle, E.C.2
  • 115
    • 0021928091 scopus 로고
    • Cloning, sequencing, and functional analysis of OriL, a herpes simplex virus type 1 origin of DNA synthesis
    • Describes identification of the first herpesvirus lytic origins, ■■
    • Weller SK, Spadaro A, Schaffer JE, Murray AW, Maxam AM, Schaffer PA: Cloning, sequencing, and functional analysis of OriL, a herpes simplex virus type 1 origin of DNA synthesis. Mol. Cell. Biol 5(5), 930-942 (1985). ■■ Describes identification of the first herpesvirus lytic origins.
    • (1985) Mol. Cell. Biol , vol.5 , Issue.5 , pp. 930-942
    • Weller, S.K.1    Spadaro, A.2    Schaffer, J.E.3    Murray, A.W.4    Maxam, A.M.5    Schaffer, P.A.6
  • 116
    • 26444460204 scopus 로고    scopus 로고
    • Site-directed mutagenesis of large DNA palindromes: Construction and in vitro characterization of herpes simplex virus type 1 mutants containing point mutations that eliminate the OriL or OriS initiation function
    • Balliet JW, Min JC, Cabatingan MS, Schaffer PA: Site-directed mutagenesis of large DNA palindromes: construction and in vitro characterization of herpes simplex virus type 1 mutants containing point mutations that eliminate the OriL or OriS initiation function. J. Virol. 79(20), 12783-12797 (2005).
    • (2005) J. Virol , vol.79 , Issue.20 , pp. 12783-12797
    • Balliet, J.W.1    Min, J.C.2    Cabatingan, M.S.3    Schaffer, P.A.4
  • 117
    • 0023908122 scopus 로고
    • A 67-base-pair segment from the Ori-S region of herpes simplex virus type 1 encodes origin function
    • Deb S, Doelberg M: A 67-base-pair segment from the Ori-S region of herpes simplex virus type 1 encodes origin function. J. Virol. 62(7), 2516-2519 (1988).
    • (1988) J. Virol , vol.62 , Issue.7 , pp. 2516-2519
    • Deb, S.1    Doelberg, M.2
  • 118
    • 0023803303 scopus 로고
    • Sequence and structural requirements of a herpes simplex viral DNA replication origin
    • Identification of the critical elements within the HSV lytic origins, ■
    • Lockshon D, Galloway DA: Sequence and structural requirements of a herpes simplex viral DNA replication origin. Mol. Cell. Biol 8(10), 4018-4027 (1988). ■ Identification of the critical elements within the HSV lytic origins.
    • (1988) Mol. Cell. Biol , vol.8 , Issue.10 , pp. 4018-4027
    • Lockshon, D.1    Galloway, D.A.2
  • 119
    • 0023720930 scopus 로고
    • Characterization of major recognition sequences for a herpes simplex virus type 1 origin-binding protein
    • Koff A, Tegtmeyer P: Characterization of major recognition sequences for a herpes simplex virus type 1 origin-binding protein. J. Virol. 62(11), 4096-4103 (1988).
    • (1988) J. Virol , vol.62 , Issue.11 , pp. 4096-4103
    • Koff, A.1    Tegtmeyer, P.2
  • 120
    • 0025293028 scopus 로고
    • Two binding sites for the herpes simplex virus type 1 UL9 protein are required for efficient activity of the oriS replication origin
    • Weir HM, Stow ND: Two binding sites for the herpes simplex virus type 1 UL9 protein are required for efficient activity of the oriS replication origin. J. Gen. Virol. 71 ( Pt 6), 1379-1385 (1990).
    • (1990) J. Gen. Virol , vol.71 , Issue.PART 6 , pp. 1379-1385
    • Weir, H.M.1    Stow, N.D.2
  • 121
    • 0023698910 scopus 로고
    • Identification and characterization of OriLyt, a lytic origin of DNA replication of Epstein-Barr virus
    • Describes the identification of the EBV OriLyt, ■
    • Hammerschmidt W, Sugden B: Identification and characterization of OriLyt, a lytic origin of DNA replication of Epstein-Barr virus. Cell 55(3), 427-433 (1988). ■ Describes the identification of the EBV OriLyt.
    • (1988) Cell , vol.55 , Issue.3 , pp. 427-433
    • Hammerschmidt, W.1    Sugden, B.2
  • 122
    • 0027207953 scopus 로고
    • cis-acting elements in the lytic origin of DNA replication of Epstein-Barr virus
    • Describes the identification of the EBV OriLyt, ■
    • Schepers A, Pich D, Mankertz J, Hammerschmidt W: cis-acting elements in the lytic origin of DNA replication of Epstein-Barr virus. J. Virol. 67(7), 4237-4245 (1993). ■ Describes the identification of the EBV OriLyt.
    • (1993) J. Virol , vol.67 , Issue.7 , pp. 4237-4245
    • Schepers, A.1    Pich, D.2    Mankertz, J.3    Hammerschmidt, W.4
  • 123
    • 0029944992 scopus 로고    scopus 로고
    • Activation of OriLyt, the lytic origin of DNA replication of Epstein-Barr virus, by BZLF1
    • Schepers A, Pich D, Hammerschmidt W: Activation of OriLyt, the lytic origin of DNA replication of Epstein-Barr virus, by BZLF1. Virology 220(2), 367-376 (1996).
    • (1996) Virology , vol.220 , Issue.2 , pp. 367-376
    • Schepers, A.1    Pich, D.2    Hammerschmidt, W.3
  • 124
    • 0033230606 scopus 로고    scopus 로고
    • Cellular transcription factors recruit viral replication proteins to activate the Epstein-Barr virus origin of lytic DNA replication, OriLyt
    • Baumann M, Feederle R, Kremmer E, Hammerschmidt W: Cellular transcription factors recruit viral replication proteins to activate the Epstein-Barr virus origin of lytic DNA replication, OriLyt. EMBO J. 18(21), 6095-6105 (1999).
    • (1999) EMBO J , vol.18 , Issue.21 , pp. 6095-6105
    • Baumann, M.1    Feederle, R.2    Kremmer, E.3    Hammerschmidt, W.4
  • 125
    • 0028872262 scopus 로고
    • Cellular proteins bind to the downstream component of the lytic origin of DNA replication of Epstein-Barr virus
    • Gruffat H, Renner O, Pich D, Hammerschmidt W: Cellular proteins bind to the downstream component of the lytic origin of DNA replication of Epstein-Barr virus. J. Virol. 69(3), 1878-1886 (1995).
    • (1995) J. Virol , vol.69 , Issue.3 , pp. 1878-1886
    • Gruffat, H.1    Renner, O.2    Pich, D.3    Hammerschmidt, W.4
  • 126
    • 0030873281 scopus 로고    scopus 로고
    • A particular DNA structure is required for the function of a cis-acting component of the Epstein-Barr virus OriLyt origin of replication
    • Portes-Sentis S, Sergeant A, Gruffat H: A particular DNA structure is required for the function of a cis-acting component of the Epstein-Barr virus OriLyt origin of replication. Nucleic Acids Res. 25(7), 1347-1354 (1997).
    • (1997) Nucleic Acids Res , vol.25 , Issue.7 , pp. 1347-1354
    • Portes-Sentis, S.1    Sergeant, A.2    Gruffat, H.3
  • 127
    • 0025666546 scopus 로고    scopus 로고
    • Gruffat H, Manet E, Rigolet A, Sergeant A: The enhancer factor R of Epstein-Barr virus (EBV) is a sequence-specific DNA binding protein. Nucleic Acids Res. 18(23), 6835-6843 (1990). ■ Characterization of Rta as a lytic origin-binding protein.
    • Gruffat H, Manet E, Rigolet A, Sergeant A: The enhancer factor R of Epstein-Barr virus (EBV) is a sequence-specific DNA binding protein. Nucleic Acids Res. 18(23), 6835-6843 (1990). ■ Characterization of Rta as a lytic origin-binding protein.
  • 128
    • 0036310446 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) contains two functional lytic origins of DNA replication
    • AuCoin DP, Colletti KS, Xu Y, Cei SA, Pari GS: Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) contains two functional lytic origins of DNA replication. J. Virol. 76(15), 7890-7896 (2002).
    • (2002) J. Virol , vol.76 , Issue.15 , pp. 7890-7896
    • AuCoin, D.P.1    Colletti, K.S.2    Xu, Y.3    Cei, S.A.4    Pari, G.S.5
  • 129
    • 84929267586 scopus 로고    scopus 로고
    • Reactivation and lytic replication of KSHV
    • Arvin A, Campadelli-Fiume G, Mocarski E et al, Eds, Cambridge University Press, NY, USA
    • Lukac DM, Yuan Y: Reactivation and lytic replication of KSHV. In: Human Herpesviruses. Arvin A, Campadelli-Fiume G, Mocarski E et al. (Eds). Cambridge University Press, NY, USA, 434-460 (2007).
    • (2007) Human Herpesviruses , pp. 434-460
    • Lukac, D.M.1    Yuan, Y.2
  • 130
    • 33748919690 scopus 로고    scopus 로고
    • Evaluation of the lytic origins of replication of Kaposi's sarcoma-associated virus/human herpesvirus 8 in the context of the viral genome
    • Xu Y, Rodriguez-Huete A, Pari GS: Evaluation of the lytic origins of replication of Kaposi's sarcoma-associated virus/human herpesvirus 8 in the context of the viral genome. J. Virol. 80(19), 9905-9909 (2006).
    • (2006) J. Virol , vol.80 , Issue.19 , pp. 9905-9909
    • Xu, Y.1    Rodriguez-Huete, A.2    Pari, G.S.3
  • 131
    • 64849098120 scopus 로고    scopus 로고
    • Identification and functional characterization of the left origin of lytic replication of murine γ-herpesvirus 68
    • Gong D, Qi J, Arumugaswami V, Sun R, Deng H: Identification and functional characterization of the left origin of lytic replication of murine γ-herpesvirus 68. Virology 387(2), 285-295 (2009).
    • (2009) Virology , vol.387 , Issue.2 , pp. 285-295
    • Gong, D.1    Qi, J.2    Arumugaswami, V.3    Sun, R.4    Deng, H.5
  • 132
    • 4143097024 scopus 로고    scopus 로고
    • Identification of cis sequences required for lytic DNA replication and packaging of murine g-herpesvirus 68
    • Deng H, Chu JT, Park NH, Sun R: Identification of cis sequences required for lytic DNA replication and packaging of murine g-herpesvirus 68. J. Virol. 78(17), 9123-9131 (2004).
    • (2004) J. Virol , vol.78 , Issue.17 , pp. 9123-9131
    • Deng, H.1    Chu, J.T.2    Park, N.H.3    Sun, R.4
  • 133
    • 67749096154 scopus 로고    scopus 로고
    • The M10 locus of murine g-herpesvirus 68 contributes to both the lytic and latent phase of infection
    • doi: 10.1128/JVI.00629-09 , Epub ahead of print
    • Flach B, Steer B, Thakur NN, Haas J, Adler H: The M10 locus of murine g-herpesvirus 68 contributes to both the lytic and latent phase of infection. J. Virol. doi: 10.1128/JVI.00629-09 (2009) (Epub ahead of print).
    • (2009) J. Virol
    • Flach, B.1    Steer, B.2    Thakur, N.N.3    Haas, J.4    Adler, H.5
  • 134
    • 0025228048 scopus 로고
    • Identification of the lytic origin of DNA replication in human cytomegalovirus by a novel approach utilizing ganciclovir-induced chain termination
    • Hamzeh FM, Lietman PS, Gibson W, Hayward GS: Identification of the lytic origin of DNA replication in human cytomegalovirus by a novel approach utilizing ganciclovir-induced chain termination. J. Virol. 64(12), 6184-6195 (1990).
    • (1990) J. Virol , vol.64 , Issue.12 , pp. 6184-6195
    • Hamzeh, F.M.1    Lietman, P.S.2    Gibson, W.3    Hayward, G.S.4
  • 135
    • 0026725448 scopus 로고
    • Boundaries and structure of human cytomegalovirus OriLyt, a complex origin for lytic-phase DNA replication
    • Anders DG, Kacica MA, Pari G, Punturieri SM: Boundaries and structure of human cytomegalovirus OriLyt, a complex origin for lytic-phase DNA replication. J. Virol. 66(6), 3373-3384 (1992).
    • (1992) J. Virol , vol.66 , Issue.6 , pp. 3373-3384
    • Anders, D.G.1    Kacica, M.A.2    Pari, G.3    Punturieri, S.M.4
  • 136
    • 14744268640 scopus 로고    scopus 로고
    • Analysis of human cytomegalovirus OriLyt sequence requirements in the context of the viral genome
    • Borst EM, Messerle M: Analysis of human cytomegalovirus OriLyt sequence requirements in the context of the viral genome. J. Virol. 79(6), 3615-3626 (2005).
    • (2005) J. Virol , vol.79 , Issue.6 , pp. 3615-3626
    • Borst, E.M.1    Messerle, M.2
  • 137
    • 0031949591 scopus 로고    scopus 로고
    • Human cytomegalovirus OriLyt sequence requirements
    • Zhu Y, Huang L, Anders DG: Human cytomegalovirus OriLyt sequence requirements. J. Virol. 72(6), 4989-4996 (1998).
    • (1998) J. Virol , vol.72 , Issue.6 , pp. 4989-4996
    • Zhu, Y.1    Huang, L.2    Anders, D.G.3
  • 138
    • 0026085293 scopus 로고
    • Multicomponent origin of cytomegalovirus lytic-phase DNA replication
    • Anders DG, Punturieri SM: Multicomponent origin of cytomegalovirus lytic-phase DNA replication. J. Virol. 65(2), 931-937 (1991).
    • (1991) J. Virol , vol.65 , Issue.2 , pp. 931-937
    • Anders, D.G.1    Punturieri, S.M.2
  • 139
    • 0026741818 scopus 로고
    • Human cytomegalovirus origin of DNA replication (OriLyt) resides within a highly complex repetitive region
    • Masse MJ, Karlin S, Schachtel GA, Mocarski ES: Human cytomegalovirus origin of DNA replication (OriLyt) resides within a highly complex repetitive region. Proc. Natl Acad. Sci. USA 89(12), 5246-5250 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , Issue.12 , pp. 5246-5250
    • Masse, M.J.1    Karlin, S.2    Schachtel, G.A.3    Mocarski, E.S.4
  • 140
    • 84929295980 scopus 로고    scopus 로고
    • DNA synthesis and late viral gene expression
    • Arvin A, Campadelli-Fiume G, Mocarski, E et al, Eds, Cambridge University Press, NY, USA
    • Anders DG, Kerry JA, Pari GS: DNA synthesis and late viral gene expression. In: Human Herpesviruses. Arvin A, Campadelli-Fiume G, Mocarski, E et al. (Eds). Cambridge University Press, NY, USA, 295-310 (2007).
    • (2007) Human Herpesviruses , pp. 295-310
    • Anders, D.G.1    Kerry, J.A.2    Pari, G.S.3
  • 141
    • 0029931716 scopus 로고    scopus 로고
    • The variable 3μ ends of a human cytomegalovirus OriLyt transcript (SRT) overlap an essential, conserved replicator element
    • Huang L, Zhu Y, Anders DG: The variable 3μ ends of a human cytomegalovirus OriLyt transcript (SRT) overlap an essential, conserved replicator element. J. Virol. 70(8), 5272-5281 (1996).
    • (1996) J. Virol , vol.70 , Issue.8 , pp. 5272-5281
    • Huang, L.1    Zhu, Y.2    Anders, D.G.3
  • 142
    • 0031851748 scopus 로고    scopus 로고
    • Identification of persistent RNA-DNA hybrid structures within the origin of replication of human cytomegalovirus
    • Prichard MN, Jairath S, Penfold ME, St Jeor S, Bohlman MC, Pari GS: Identification of persistent RNA-DNA hybrid structures within the origin of replication of human cytomegalovirus. J. Virol. 72(9), 6997-7004 (1998).
    • (1998) J. Virol , vol.72 , Issue.9 , pp. 6997-7004
    • Prichard, M.N.1    Jairath, S.2    Penfold, M.E.3    St Jeor, S.4    Bohlman, M.C.5    Pari, G.S.6
  • 143
    • 0029819872 scopus 로고    scopus 로고
    • Use of transdominant mutants of the origin-binding protein (UL9) of herpes simplex virus type 1 to define functional domains
    • Malik AK, Weller SK: Use of transdominant mutants of the origin-binding protein (UL9) of herpes simplex virus type 1 to define functional domains. J. Virol. 70(11), 7859-7866 (1996).
    • (1996) J. Virol , vol.70 , Issue.11 , pp. 7859-7866
    • Malik, A.K.1    Weller, S.K.2
  • 144
    • 0035794155 scopus 로고    scopus 로고
    • Residues within the conserved helicase motifs of UL9, the origin-binding protein of herpes simplex virus-1, are essential for helicase activity but not for dimerization or origin binding activity
    • Marintcheva B, Weller SK: Residues within the conserved helicase motifs of UL9, the origin-binding protein of herpes simplex virus-1, are essential for helicase activity but not for dimerization or origin binding activity. J. Biol. Chem. 276(9), 6605-6615 (2001).
    • (2001) J. Biol. Chem , vol.276 , Issue.9 , pp. 6605-6615
    • Marintcheva, B.1    Weller, S.K.2
  • 145
    • 0042389522 scopus 로고    scopus 로고
    • Existence of transdominant and potentiating mutants of UL9, the herpes simplex virus type 1 origin-binding protein, suggests that levels of UL9 protein may be regulated during infection
    • Marintcheva B, Weller SK: Existence of transdominant and potentiating mutants of UL9, the herpes simplex virus type 1 origin-binding protein, suggests that levels of UL9 protein may be regulated during infection. J. Virol. 77(17), 9639-9651 (2003).
    • (2003) J. Virol , vol.77 , Issue.17 , pp. 9639-9651
    • Marintcheva, B.1    Weller, S.K.2
  • 146
    • 33646187186 scopus 로고    scopus 로고
    • DNA binding activity of the herpes simplex virus type 1 origin binding protein, UL9, can be modulated by sequences in the N terminus: Correlation between transdominance and DNA binding
    • Chattopadhyay S, Weller SK: DNA binding activity of the herpes simplex virus type 1 origin binding protein, UL9, can be modulated by sequences in the N terminus: correlation between transdominance and DNA binding. J. Virol. 80(9), 4491-4500 (2006).
    • (2006) J. Virol , vol.80 , Issue.9 , pp. 4491-4500
    • Chattopadhyay, S.1    Weller, S.K.2
  • 147
    • 0030967646 scopus 로고    scopus 로고
    • Unwinding of the box I element of a herpes simplex virus type 1 origin by a complex of the viral origin binding protein, single-strand DNA binding protein, and single-stranded DNA
    • Lee SS, Lehman IR: Unwinding of the box I element of a herpes simplex virus type 1 origin by a complex of the viral origin binding protein, single-strand DNA binding protein, and single-stranded DNA. Proc. Natl Acad. Sci. USA 94(7), 2838-2842 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , Issue.7 , pp. 2838-2842
    • Lee, S.S.1    Lehman, I.R.2
  • 148
    • 0034034279 scopus 로고    scopus 로고
    • Unwinding of a herpes simplex virus type 1 origin of replication
    • He X, Lehman IR: Unwinding of a herpes simplex virus type 1 origin of replication (Ori(S)) by a complex of the viral origin binding protein and the single-stranded DNA binding protein. J. Virol. 74(12), 5726-5728 (2000).
    • (2000) J. Virol , vol.74 , Issue.12 , pp. 5726-5728
    • He, X.1    Lehman, I.R.2
  • 149
    • 0025064563 scopus 로고
    • The origin binding protein of herpes simplex virus 1 binds cooperatively to the viral origin of replication OriS
    • Elias P, Gustafsson CM, Hammarsten O: The origin binding protein of herpes simplex virus 1 binds cooperatively to the viral origin of replication OriS. J. Biol. Chem. 265(28), 17167-17173 (1990).
    • (1990) J. Biol. Chem , vol.265 , Issue.28 , pp. 17167-17173
    • Elias, P.1    Gustafsson, C.M.2    Hammarsten, O.3
  • 150
    • 0034008142 scopus 로고    scopus 로고
    • A novel conformation of the herpes simplex virus origin of DNA replication recognized by the origin binding protein
    • Aslani A, Simonsson S, Elias P: A novel conformation of the herpes simplex virus origin of DNA replication recognized by the origin binding protein. J. Biol. Chem. 275(8), 5880-5887 (2000).
    • (2000) J. Biol. Chem , vol.275 , Issue.8 , pp. 5880-5887
    • Aslani, A.1    Simonsson, S.2    Elias, P.3
  • 151
    • 3142685517 scopus 로고    scopus 로고
    • Functional properties of the herpes simplex virus type I origin-binding protein are controlled by precise interactions with the activated form of the origin of DNA replication
    • Macao B, Olsson M, Elias P: Functional properties of the herpes simplex virus type I origin-binding protein are controlled by precise interactions with the activated form of the origin of DNA replication. J. Biol. Chem. 279(28), 29211-29217 (2004).
    • (2004) J. Biol. Chem , vol.279 , Issue.28 , pp. 29211-29217
    • Macao, B.1    Olsson, M.2    Elias, P.3
  • 152
    • 0035912769 scopus 로고    scopus 로고
    • Complementary intrastrand base pairing during initiation of herpes simplex virus type 1 DNA replication
    • Identification of a critical DNA hairpin formed at an inverted repeat within the essential region of HSV OriLyt, ■
    • Aslani A, Macao B, Simonsson S, Elias P: Complementary intrastrand base pairing during initiation of herpes simplex virus type 1 DNA replication. Proc. Natl Acad. Sci. USA 98(13), 7194-7199 (2001). ■ Identification of a critical DNA hairpin formed at an inverted repeat within the essential region of HSV OriLyt.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , Issue.13 , pp. 7194-7199
    • Aslani, A.1    Macao, B.2    Simonsson, S.3    Elias, P.4
  • 153
    • 0037175027 scopus 로고    scopus 로고
    • ATP-dependent unwinding of a minimal origin of DNA replication by the origin-binding protein and the single-strand DNA-binding protein ICP8 from herpes simplex virus type I
    • Aslani A, Olsson M, Elias P: ATP-dependent unwinding of a minimal origin of DNA replication by the origin-binding protein and the single-strand DNA-binding protein ICP8 from herpes simplex virus type I. J. Biol. Chem. 277(43), 41204-41212 (2002).
    • (2002) J. Biol. Chem , vol.277 , Issue.43 , pp. 41204-41212
    • Aslani, A.1    Olsson, M.2    Elias, P.3
  • 154
    • 67650273080 scopus 로고    scopus 로고
    • Stepwise evolution of the herpes simplex virus origin binding protein and origin of replication
    • Olsson M, Tang KW, Persson C, Wilhelmsson LM, Billeter M, Elias P: Stepwise evolution of the herpes simplex virus origin binding protein and origin of replication. J. Biol. Chem. 284(24), 16246-16255 (2009).
    • (2009) J. Biol. Chem , vol.284 , Issue.24 , pp. 16246-16255
    • Olsson, M.1    Tang, K.W.2    Persson, C.3    Wilhelmsson, L.M.4    Billeter, M.5    Elias, P.6
  • 155
    • 0037321633 scopus 로고    scopus 로고
    • Helicase motif Ia is involved in single-strand DNA-binding and helicase activities of the herpes simplex virus type 1 origin-binding protein, UL9
    • Marintcheva B, Weller SK: Helicase motif Ia is involved in single-strand DNA-binding and helicase activities of the herpes simplex virus type 1 origin-binding protein, UL9. J. Virol. 77(4), 2477-2488 (2003).
    • (2003) J. Virol , vol.77 , Issue.4 , pp. 2477-2488
    • Marintcheva, B.1    Weller, S.K.2
  • 156
    • 0030586695 scopus 로고    scopus 로고
    • Epstein-Barr virus single-stranded DNA-binding protein: Purification, characterization, and action on DNA synthesis by the viral DNA polymerase
    • Tsurumi T, Kobayashi A, Tamai K et al.: Epstein-Barr virus single-stranded DNA-binding protein: purification, characterization, and action on DNA synthesis by the viral DNA polymerase. Virology 222(2), 352-364 (1996).
    • (1996) Virology , vol.222 , Issue.2 , pp. 352-364
    • Tsurumi, T.1    Kobayashi, A.2    Tamai, K.3
  • 157
    • 0022432553 scopus 로고
    • DNA sequence of the region in the genome of herpes simplex virus type 1 containing the genes for DNA polymerase and the major DNA binding protein
    • Quinn JP, McGeoch DJ: DNA sequence of the region in the genome of herpes simplex virus type 1 containing the genes for DNA polymerase and the major DNA binding protein. Nucleic Acids Res. 13(22), 8143-8163 (1985).
    • (1985) Nucleic Acids Res , vol.13 , Issue.22 , pp. 8143-8163
    • Quinn, J.P.1    McGeoch, D.J.2
  • 158
    • 13244284795 scopus 로고    scopus 로고
    • The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding
    • Crystal structure of the herpesvirus ssDNA-binding protien, ■■
    • Mapelli M, Panjikar S, Tucker PA: The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding. J. Biol. Chem. 280(4), 2990-2997 (2005). ■■ Crystal structure of the herpesvirus ssDNA-binding protien.
    • (2005) J. Biol. Chem , vol.280 , Issue.4 , pp. 2990-2997
    • Mapelli, M.1    Panjikar, S.2    Tucker, P.A.3
  • 160
    • 0025949185 scopus 로고
    • The major herpes simplex virus type-1 DNA-binding protein is a zinc metalloprotein
    • Gupte SS, Olson JW, Ruyechan WT: The major herpes simplex virus type-1 DNA-binding protein is a zinc metalloprotein. J. Biol. Chem. 266(18), 11413-11416 (1991).
    • (1991) J. Biol. Chem , vol.266 , Issue.18 , pp. 11413-11416
    • Gupte, S.S.1    Olson, J.W.2    Ruyechan, W.T.3
  • 161
    • 0021816390 scopus 로고
    • An immunoassay for the study of DNA-binding activities of herpes simplex virus protein ICP8
    • Lee CK, Knipe DM: An immunoassay for the study of DNA-binding activities of herpes simplex virus protein ICP8. J. Virol. 54(3), 731-738 (1985).
    • (1985) J. Virol , vol.54 , Issue.3 , pp. 731-738
    • Lee, C.K.1    Knipe, D.M.2
  • 162
    • 0027970455 scopus 로고
    • Association of origin binding protein and single strand DNA-binding protein, ICP8, during herpes simplex virus type 1 DNA replication in vivo
    • Boehmer PE, Craigie MC, Stow ND, Lehman IR: Association of origin binding protein and single strand DNA-binding protein, ICP8, during herpes simplex virus type 1 DNA replication in vivo. J. Biol. Chem. 269(46), 29329-29334 (1994).
    • (1994) J. Biol. Chem , vol.269 , Issue.46 , pp. 29329-29334
    • Boehmer, P.E.1    Craigie, M.C.2    Stow, N.D.3    Lehman, I.R.4
  • 163
    • 0027227630 scopus 로고
    • Physical interaction between the herpes simplex virus 1 origin-binding protein and single-stranded DNA-binding protein ICP8
    • Boehmer PE, Lehman IR: Physical interaction between the herpes simplex virus 1 origin-binding protein and single-stranded DNA-binding protein ICP8. Proc. Natl Acad. Sci. USA 90(18), 8444-8448 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , Issue.18 , pp. 8444-8448
    • Boehmer, P.E.1    Lehman, I.R.2
  • 164
    • 0035853081 scopus 로고    scopus 로고
    • An initial ATP-independent step in the unwinding of a herpes simplex virus type I origin of replication by a complex of the viral origin-binding protein and single-strand DNA-binding protein
    • He X, Lehman IR: An initial ATP-independent step in the unwinding of a herpes simplex virus type I origin of replication by a complex of the viral origin-binding protein and single-strand DNA-binding protein. Proc. Natl Acad. Sci. USA 98(6), 3024-3028 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , Issue.6 , pp. 3024-3028
    • He, X.1    Lehman, I.R.2
  • 165
    • 0038468334 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 alkaline nuclease and single-stranded DNA binding protein mediate strand exchange in vitro
    • Suggests a similarity between herpesvirus replication proteins and the λ RED recombination machinery, ■
    • Reuven NB, Staire AE, Myers RS, Weller SK: The herpes simplex virus type 1 alkaline nuclease and single-stranded DNA binding protein mediate strand exchange in vitro. J. Virol. 77(13), 7425-7433 (2003). ■ Suggests a similarity between herpesvirus replication proteins and the λ RED recombination machinery.
    • (2003) J. Virol , vol.77 , Issue.13 , pp. 7425-7433
    • Reuven, N.B.1    Staire, A.E.2    Myers, R.S.3    Weller, S.K.4
  • 166
    • 0027452772 scopus 로고
    • Herpes simplex virus type 1 ICP8: Helix-destabilizing properties
    • Boehmer PE, Lehman IR: Herpes simplex virus type 1 ICP8: helix-destabilizing properties. J. Virol. 67(2), 711-715 (1993).
    • (1993) J. Virol , vol.67 , Issue.2 , pp. 711-715
    • Boehmer, P.E.1    Lehman, I.R.2
  • 167
    • 0027269858 scopus 로고
    • Herpes simplex virus 1 single-strand DNA-binding protein (ICP8) will promote homologous pairing and strand transfer
    • Bortner C, Hernandez TR, Lehman IR, Griffith J: Herpes simplex virus 1 single-strand DNA-binding protein (ICP8) will promote homologous pairing and strand transfer. J. Mol. Biol. 231(2), 241-250 (1993).
    • (1993) J. Mol. Biol , vol.231 , Issue.2 , pp. 241-250
    • Bortner, C.1    Hernandez, T.R.2    Lehman, I.R.3    Griffith, J.4
  • 168
    • 0026584148 scopus 로고
    • Herpes simplex virus type 1 recombination: Role of DNA replication and viral a sequences
    • Dutch RE, Bruckner RC, Mocarski ES, Lehman IR: Herpes simplex virus type 1 recombination: role of DNA replication and viral a sequences. J. Virol. 66(1), 277-285 (1992).
    • (1992) J. Virol , vol.66 , Issue.1 , pp. 277-285
    • Dutch, R.E.1    Bruckner, R.C.2    Mocarski, E.S.3    Lehman, I.R.4
  • 169
    • 0038052925 scopus 로고    scopus 로고
    • The herpes simplex virus type-1 single-strand DNA-binding protein (ICP8) promotes strand invasion
    • Nimonkar AV, Boehmer PE: The herpes simplex virus type-1 single-strand DNA-binding protein (ICP8) promotes strand invasion. J. Biol. Chem. 278(11), 9678-9682 (2003).
    • (2003) J. Biol. Chem , vol.278 , Issue.11 , pp. 9678-9682
    • Nimonkar, A.V.1    Boehmer, P.E.2
  • 170
    • 0344875220 scopus 로고    scopus 로고
    • On the mechanism of strand assimilation by the herpes simplex virus type-1 single-strand DNA-binding protein (ICP8)
    • Nimonkar AV, Boehmer PE: On the mechanism of strand assimilation by the herpes simplex virus type-1 single-strand DNA-binding protein (ICP8). Nucleic Acids Res. 31(18), 5275-5281 (2003).
    • (2003) Nucleic Acids Res , vol.31 , Issue.18 , pp. 5275-5281
    • Nimonkar, A.V.1    Boehmer, P.E.2
  • 171
    • 0041335636 scopus 로고    scopus 로고
    • Reconstitution of recombination-dependent DNA synthesis in herpes simplex virus 1
    • Nimonkar AV, Boehmer PE: Reconstitution of recombination-dependent DNA synthesis in herpes simplex virus 1. Proc. Natl Acad. Sci. USA 100(18), 10201-10206 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , Issue.18 , pp. 10201-10206
    • Nimonkar, A.V.1    Boehmer, P.E.2
  • 172
    • 0027428415 scopus 로고
    • Renaturation of complementary DNA strands by herpes simplex virus type 1 ICP8
    • Dutch RE, Lehman IR: Renaturation of complementary DNA strands by herpes simplex virus type 1 ICP8. J. Virol. 67(12), 6945-6949 (1993).
    • (1993) J. Virol , vol.67 , Issue.12 , pp. 6945-6949
    • Dutch, R.E.1    Lehman, I.R.2
  • 173
    • 0031946624 scopus 로고    scopus 로고
    • Overexpression, purification and helix-destabilizing properties of Epstein-Barr virus ssDNA-binding protein
    • Tsurumi T, Kishore J, Yokoyama N et al.: Overexpression, purification and helix-destabilizing properties of Epstein-Barr virus ssDNA-binding protein. J. Gen. Virol. 79(Pt 5), 1257-1264 (1998).
    • (1998) J. Gen. Virol , vol.79 , Issue.PART 5 , pp. 1257-1264
    • Tsurumi, T.1    Kishore, J.2    Yokoyama, N.3
  • 174
    • 0018393080 scopus 로고
    • The structure and isomerization of herpes simplex virus genomes
    • Roizman B: The structure and isomerization of herpes simplex virus genomes. Cell 16(3), 481-494 (1979).
    • (1979) Cell , vol.16 , Issue.3 , pp. 481-494
    • Roizman, B.1
  • 175
    • 0031008223 scopus 로고    scopus 로고
    • Herpes simplex virus DNA replication
    • Boehmer PE, Lehman IR: Herpes simplex virus DNA replication. Annu. Rev. Biochem. 66, 347-384 (1997).
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 347-384
    • Boehmer, P.E.1    Lehman, I.R.2
  • 176
    • 0037256890 scopus 로고    scopus 로고
    • Herpes virus replication
    • Boehmer PE, Nimonkar AV: Herpes virus replication. IUBMB Life 55(1), 13-22 (2003).
    • (2003) IUBMB Life , vol.55 , Issue.1 , pp. 13-22
    • Boehmer, P.E.1    Nimonkar, A.V.2
  • 177
    • 0033215473 scopus 로고    scopus 로고
    • Replication of herpes simplex virus DNA
    • Lehman IR, Boehmer PE: Replication of herpes simplex virus DNA. J. Biol. Chem. 274(40), 28059-28062 (1999).
    • (1999) J. Biol. Chem , vol.274 , Issue.40 , pp. 28059-28062
    • Lehman, I.R.1    Boehmer, P.E.2
  • 178
    • 25144503893 scopus 로고    scopus 로고
    • Circularization of the herpes simplex virus type 1 genome upon lytic infection
    • Strang BL, Stow ND: Circularization of the herpes simplex virus type 1 genome upon lytic infection. J. Virol. 79(19), 12487-12494 (2005).
    • (2005) J. Virol , vol.79 , Issue.19 , pp. 12487-12494
    • Strang, B.L.1    Stow, N.D.2
  • 179
    • 0020604123 scopus 로고
    • Replicative forms of human cytomegalovirus DNA with joined termini are found in permissively infected human cells but not in non-permissive Balb/c-3T3 mouse cells
    • LaFemina RL, Hayward GS: Replicative forms of human cytomegalovirus DNA with joined termini are found in permissively infected human cells but not in non-permissive Balb/c-3T3 mouse cells. J. Gen. Virol. 64(Pt 2), 373-389 (1983).
    • (1983) J. Gen. Virol , vol.64 , Issue.PART 2 , pp. 373-389
    • LaFemina, R.L.1    Hayward, G.S.2
  • 180
    • 0021127801 scopus 로고
    • Fusion of the termini of the murine cytomegalovirus genome after infection
    • Marks JR, Spector DH: Fusion of the termini of the murine cytomegalovirus genome after infection. J. Virol. 52(1), 24-28 (1984).
    • (1984) J. Virol , vol.52 , Issue.1 , pp. 24-28
    • Marks, J.R.1    Spector, D.H.2
  • 181
    • 0028047319 scopus 로고
    • Human cytomegalovirus DNA replicates after early circularization by concatemer formation, and inversion occurs within the concatemer
    • McVoy MA, Adler SP: Human cytomegalovirus DNA replicates after early circularization by concatemer formation, and inversion occurs within the concatemer. J. Virol. 68(2), 1040-1051 (1994).
    • (1994) J. Virol , vol.68 , Issue.2 , pp. 1040-1051
    • McVoy, M.A.1    Adler, S.P.2
  • 182
    • 0025130597 scopus 로고
    • Concatameric replication of Epstein-Barr virus: Structure of the termini in virus-producer and newly transformed cell lines
    • Sato H, Takimoto T, Tanaka S, Tanaka J, Raab-Traub N: Concatameric replication of Epstein-Barr virus: structure of the termini in virus-producer and newly transformed cell lines. J. Virol. 64(11), 5295-5300 (1990).
    • (1990) J. Virol , vol.64 , Issue.11 , pp. 5295-5300
    • Sato, H.1    Takimoto, T.2    Tanaka, S.3    Tanaka, J.4    Raab-Traub, N.5
  • 183
    • 0027247550 scopus 로고
    • A concatenated form of Epstein-Barr viral DNA in l ymphoblastoid cell lines induced by transfection with BZLF1
    • Cho MS, Tran VM: A concatenated form of Epstein-Barr viral DNA in l ymphoblastoid cell lines induced by transfection with BZLF1. Virology 194(2), 838-842 (1993).
    • (1993) Virology , vol.194 , Issue.2 , pp. 838-842
    • Cho, M.S.1    Tran, V.M.2
  • 184
    • 0027435961 scopus 로고
    • Demonstration of circularization of herpes simplex virus DNA following infection using pulsed field gel electrophoresis
    • Garber DA, Beverley SM, Coen DM: Demonstration of circularization of herpes simplex virus DNA following infection using pulsed field gel electrophoresis. Virology 197(1), 459-462 (1993).
    • (1993) Virology , vol.197 , Issue.1 , pp. 459-462
    • Garber, D.A.1    Beverley, S.M.2    Coen, D.M.3
  • 185
    • 0017264404 scopus 로고
    • Concatemeric forms of intracellular herpesvirus DNA
    • Ben-Porat T, Kaplan AS, Stehn B, Rubenstein AS: Concatemeric forms of intracellular herpesvirus DNA. Virology 69(2), 547-560 (1976).
    • (1976) Virology , vol.69 , Issue.2 , pp. 547-560
    • Ben-Porat, T.1    Kaplan, A.S.2    Stehn, B.3    Rubenstein, A.S.4
  • 186
    • 0028269715 scopus 로고
    • Study of the structure of replicative intermediates of HSV-1 DNA by pulsed-field gel electrophoresis
    • Severini A, Morgan AR, Tovell DR, Tyrrell DL: Study of the structure of replicative intermediates of HSV-1 DNA by pulsed-field gel electrophoresis. Virology 200(2), 428-435 (1994).
    • (1994) Virology , vol.200 , Issue.2 , pp. 428-435
    • Severini, A.1    Morgan, A.R.2    Tovell, D.R.3    Tyrrell, D.L.4
  • 187
    • 0018354176 scopus 로고
    • Anatomy of herpes simplex virus DNA. XII. Accumulation of head-to-tail concatemers in nuclei of infected cells and their role in the generation of the four isomeric arrangements of viral DNA
    • Jacob RJ, Morse LS, Roizman B: Anatomy of herpes simplex virus DNA. XII. Accumulation of head-to-tail concatemers in nuclei of infected cells and their role in the generation of the four isomeric arrangements of viral DNA. J. Virol. 29(2), 448-457 (1979).
    • (1979) J. Virol , vol.29 , Issue.2 , pp. 448-457
    • Jacob, R.J.1    Morse, L.S.2    Roizman, B.3
  • 188
    • 0019467017 scopus 로고
    • Structure of replicating herpes simplex virus DNA
    • Jongeneel CV, Bachenheimer SL: Structure of replicating herpes simplex virus DNA. J. Virol. 39(2), 656-660 (1981).
    • (1981) J. Virol , vol.39 , Issue.2 , pp. 656-660
    • Jongeneel, C.V.1    Bachenheimer, S.L.2
  • 189
    • 0017714305 scopus 로고
    • Replication of herpesvirus DNA. II. Sedimentation characteristics of newly synthesized DNA
    • Ben-Porat T, Tokazewski SA: Replication of herpesvirus DNA. II. Sedimentation characteristics of newly synthesized DNA. Virology 79(2), 292-301 (1977).
    • (1977) Virology , vol.79 , Issue.2 , pp. 292-301
    • Ben-Porat, T.1    Tokazewski, S.A.2
  • 190
    • 0017088583 scopus 로고
    • Replicating DNA of herpes simplex virus type 1
    • Hirsch I, Roubal J, Vonka V: Replicating DNA of herpes simplex virus type 1. Intervirology 7(3), 155-175 (1976).
    • (1976) Intervirology , vol.7 , Issue.3 , pp. 155-175
    • Hirsch, I.1    Roubal, J.2    Vonka, V.3
  • 191
    • 0021912943 scopus 로고
    • A noninverting genome of a viable herpes simplex virus 1: Presence of head-to-tail linkages in packaged genomes and requirements for circularization after infection
    • Poffenberger KL, Roizman B: A noninverting genome of a viable herpes simplex virus 1: presence of head-to-tail linkages in packaged genomes and requirements for circularization after infection. J. Virol. 53(2), 587-595 (1985).
    • (1985) J. Virol , vol.53 , Issue.2 , pp. 587-595
    • Poffenberger, K.L.1    Roizman, B.2
  • 192
    • 0027944256 scopus 로고
    • Rolling circle DNA replication in vitro by a complex of herpes simplex virus type 1-encoded enzymes
    • Reconstitution of rolling-circle replication by herpesvirus core lytic replication proteins in vitro, ■■
    • Skaliter R, Lehman IR: Rolling circle DNA replication in vitro by a complex of herpes simplex virus type 1-encoded enzymes. Proc. Natl Acad. Sci. USA 91(22), 10665-10669 (1994). ■■ Reconstitution of rolling-circle replication by herpesvirus core lytic replication proteins in vitro.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , Issue.22 , pp. 10665-10669
    • Skaliter, R.1    Lehman, I.R.2
  • 193
    • 0030030921 scopus 로고    scopus 로고
    • Rolling circle DNA replication by extracts of herpes simplex virus type 1-infected human cells
    • Skaliter R, Makhov AM, Griffith JD, Lehman IR: Rolling circle DNA replication by extracts of herpes simplex virus type 1-infected human cells. J. Virol. 70(2), 1132-1136 (1996).
    • (1996) J. Virol , vol.70 , Issue.2 , pp. 1132-1136
    • Skaliter, R.1    Makhov, A.M.2    Griffith, J.D.3    Lehman, I.R.4
  • 194
    • 0029985571 scopus 로고    scopus 로고
    • Branched structures in the intracellular DNA of herpes simplex virus type 1
    • Severini A, Scraba DG, Tyrrell DL: Branched structures in the intracellular DNA of herpes simplex virus type 1. J. Virol. 70(5), 3169-3175 (1996).
    • (1996) J. Virol , vol.70 , Issue.5 , pp. 3169-3175
    • Severini, A.1    Scraba, D.G.2    Tyrrell, D.L.3
  • 195
    • 0017686751 scopus 로고
    • Anatomy of herpes simplex virus DNA VIII. Properties of the replicating DNA
    • Jacob RJ, Roizman B: Anatomy of herpes simplex virus DNA VIII. Properties of the replicating DNA. J. Virol. 23(2), 394-411 (1977).
    • (1977) J. Virol , vol.23 , Issue.2 , pp. 394-411
    • Jacob, R.J.1    Roizman, B.2
  • 196
    • 0029950096 scopus 로고    scopus 로고
    • Plasmid-like replicative intermediates of the Epstein-Barr virus lytic origin of DNA replication
    • Pfuller R, Hammerschmidt W: Plasmid-like replicative intermediates of the Epstein-Barr virus lytic origin of DNA replication. J. Virol. 70(6), 3423-3431 (1996).
    • (1996) J. Virol , vol.70 , Issue.6 , pp. 3423-3431
    • Pfuller, R.1    Hammerschmidt, W.2
  • 197
    • 0028100354 scopus 로고
    • Herpes simplex virus replicative concatemers contain L components in inverted orientation
    • Bataille D, Epstein A: Herpes simplex virus replicative concatemers contain L components in inverted orientation. Virology 203(2), 384-388 (1994).
    • (1994) Virology , vol.203 , Issue.2 , pp. 384-388
    • Bataille, D.1    Epstein, A.2
  • 198
    • 0018856052 scopus 로고
    • Recombination and linkage between structural and regulatory genes of herpes simplex virus type 1: Study of the functional organization of the genome
    • Honess RW, Buchan A, Halliburton IW, Watson DH: Recombination and linkage between structural and regulatory genes of herpes simplex virus type 1: study of the functional organization of the genome. J. Virol. 34(3), 716-742 (1980).
    • (1980) J. Virol , vol.34 , Issue.3 , pp. 716-742
    • Honess, R.W.1    Buchan, A.2    Halliburton, I.W.3    Watson, D.H.4
  • 199
    • 0022372556 scopus 로고
    • Intermolecular recombination of the herpes simplex virus type 1 genome analysed using two strains differing in restriction enzyme cleavage sites
    • Umene K: Intermolecular recombination of the herpes simplex virus type 1 genome analysed using two strains differing in restriction enzyme cleavage sites. J. Gen. Virol. 66(Pt 12), 2659-2670 (1985).
    • (1985) J. Gen. Virol , vol.66 , Issue.PART 12 , pp. 2659-2670
    • Umene, K.1
  • 200
    • 0026558778 scopus 로고
    • Analysis of intrastrain recombination in herpes simplex virus type 1 strain 17 and herpes simplex virus type 2 strain HG52 using restriction endonuclease sites as unselected markers and temperature-sensitive lesions as selected markers
    • Brown SM, Subak-Sharpe JH, Harland J, MacLean AR: Analysis of intrastrain recombination in herpes simplex virus type 1 strain 17 and herpes simplex virus type 2 strain HG52 using restriction endonuclease sites as unselected markers and temperature-sensitive lesions as selected markers. J. Gen. Virol. 73(Pt 2), 293-301 (1992).
    • (1992) J. Gen. Virol , vol.73 , Issue.PART 2 , pp. 293-301
    • Brown, S.M.1    Subak-Sharpe, J.H.2    Harland, J.3    MacLean, A.R.4
  • 201
    • 0020639079 scopus 로고
    • Characterization of a viable, noninverting herpes simplex virus 1 genome derived by insertion and deletion of sequences at the junction of components L and S
    • Poffenberger KL, Tabares E, Roizman B: Characterization of a viable, noninverting herpes simplex virus 1 genome derived by insertion and deletion of sequences at the junction of components L and S. Proc. Natl Acad. Sci. USA 80(9), 2690-2694 (1983).
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , Issue.9 , pp. 2690-2694
    • Poffenberger, K.L.1    Tabares, E.2    Roizman, B.3
  • 202
    • 0022504772 scopus 로고
    • Herpes simplex virus 1 recombinants with noninverting genomes frozen in different isomeric arrangements are capable of independent replication
    • Jenkins FJ, Roizman B: Herpes simplex virus 1 recombinants with noninverting genomes frozen in different isomeric arrangements are capable of independent replication. J. Virol. 59(2), 494-499 (1986).
    • (1986) J. Virol , vol.59 , Issue.2 , pp. 494-499
    • Jenkins, F.J.1    Roizman, B.2
  • 203
    • 0020444012 scopus 로고
    • Herpesvirus-dependent amplification and inversion of cell-associated viral thymidine kinase gene flanked by viral a sequences and linked to an origin of viral DNA replication
    • Mocarski ES, Roizman B: Herpesvirus-dependent amplification and inversion of cell-associated viral thymidine kinase gene flanked by viral a sequences and linked to an origin of viral DNA replication. Proc. Natl Acad. Sci. USA 79(18), 5626-5630 (1982).
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , Issue.18 , pp. 5626-5630
    • Mocarski, E.S.1    Roizman, B.2
  • 204
    • 0028915144 scopus 로고
    • Structure and role of the terminal repeats of Epstein-Barr virus in processing and packaging of virion DNA
    • Zimmermann J, Hammerschmidt W: Structure and role of the terminal repeats of Epstein-Barr virus in processing and packaging of virion DNA. J. Virol. 69(5), 3147-3155 (1995).
    • (1995) J. Virol , vol.69 , Issue.5 , pp. 3147-3155
    • Zimmermann, J.1    Hammerschmidt, W.2
  • 205
    • 0028944806 scopus 로고
    • Herpes simplex virus type 1 DNA replication is specifically required for high-frequency homologous recombination between repeated sequences
    • Dutch RE, Bianchi V, Lehman IR: Herpes simplex virus type 1 DNA replication is specifically required for high-frequency homologous recombination between repeated sequences. J. Virol. 69(5), 3084-3089 (1995).
    • (1995) J. Virol , vol.69 , Issue.5 , pp. 3084-3089
    • Dutch, R.E.1    Bianchi, V.2    Lehman, I.R.3
  • 206
    • 0029615505 scopus 로고
    • Herpes simplex virus type 1 replication and recombination
    • Bataille D, Epstein AL: Herpes simplex virus type 1 replication and recombination. Biochimie 77(10), 787-795 (1995).
    • (1995) Biochimie , vol.77 , Issue.10 , pp. 787-795
    • Bataille, D.1    Epstein, A.L.2
  • 207
    • 0023681344 scopus 로고
    • Inversion events in the HSV-1 genome are directly mediated by the viral DNA replication machinery and lack sequence specificity
    • Demonstrates the nonspecific recombination potential of herpesvirus core lytic-replication proteins, ■■
    • Weber PC, Challberg MD, Nelson NJ, Levine M, Glorioso JC: Inversion events in the HSV-1 genome are directly mediated by the viral DNA replication machinery and lack sequence specificity. Cell 54(3), 369-381 (1988). ■■ Demonstrates the nonspecific recombination potential of herpesvirus core lytic-replication proteins.
    • (1988) Cell , vol.54 , Issue.3 , pp. 369-381
    • Weber, P.C.1    Challberg, M.D.2    Nelson, N.J.3    Levine, M.4    Glorioso, J.C.5
  • 208
    • 0025177307 scopus 로고
    • Recombinogenic properties of herpes simplex virus type 1 DNA sequences resident in simian virus 40 minichromosomes
    • Weber PC, Levine M, Glorioso JC: Recombinogenic properties of herpes simplex virus type 1 DNA sequences resident in simian virus 40 minichromosomes. J. Virol. 64(1), 300-306 (1990).
    • (1990) J. Virol , vol.64 , Issue.1 , pp. 300-306
    • Weber, P.C.1    Levine, M.2    Glorioso, J.C.3
  • 209
    • 0033996242 scopus 로고    scopus 로고
    • Machinery to support genome segment inversion exists in a herpesvirus which does not naturally contain invertible elements
    • McVoy MA, Ramnarain D: Machinery to support genome segment inversion exists in a herpesvirus which does not naturally contain invertible elements. J. Virol. 74(10), 4882-4887 (2000).
    • (2000) J. Virol , vol.74 , Issue.10 , pp. 4882-4887
    • McVoy, M.A.1    Ramnarain, D.2
  • 210
    • 0031583844 scopus 로고    scopus 로고
    • A major DNA binding protein encoded by BALF2 open reading frame of Epstein-Barr virus (EBV) forms a complex with other EBV DNA-binding proteins: DNAase, EA-D, and DNA polymerase
    • Zeng Y, Middeldorp J, Madjar JJ, Ooka T: A major DNA binding protein encoded by BALF2 open reading frame of Epstein-Barr virus (EBV) forms a complex with other EBV DNA-binding proteins: DNAase, EA-D, and DNA polymerase. Virology 239(2), 285-295 (1997).
    • (1997) Virology , vol.239 , Issue.2 , pp. 285-295
    • Zeng, Y.1    Middeldorp, J.2    Madjar, J.J.3    Ooka, T.4
  • 211
    • 68149163563 scopus 로고    scopus 로고
    • A bridge crosses the active-site canyon of the Epstein-Barr virus nuclease with DNase and RNase activities
    • Buisson M, Geoui T, Flot D et al.: A bridge crosses the active-site canyon of the Epstein-Barr virus nuclease with DNase and RNase activities. J. Mol. Biol. (2009).
    • (2009) J. Mol. Biol
    • Buisson, M.1    Geoui, T.2    Flot, D.3
  • 212
    • 0025017812 scopus 로고
    • Purification and properties of Epstein-Barr virus DNase expressed in Escherichia coli
    • Stolzenberg MC, Ooka T: Purification and properties of Epstein-Barr virus DNase expressed in Escherichia coli. J. Virol. 64(1), 96-104 (1990).
    • (1990) J. Virol , vol.64 , Issue.1 , pp. 96-104
    • Stolzenberg, M.C.1    Ooka, T.2
  • 213
    • 0037373496 scopus 로고    scopus 로고
    • Site-directed mutagenesis in a conserved motif of Epstein-Barr virus DNase that is homologous to the catalytic centre of type II restriction endonucleases
    • Liu MT, Hu HP, Hsu TY, Chen JY: Site-directed mutagenesis in a conserved motif of Epstein-Barr virus DNase that is homologous to the catalytic centre of type II restriction endonucleases. J. Gen. Virol. 84(Pt 3), 677-686 (2003).
    • (2003) J. Gen. Virol , vol.84 , Issue.PART 3 , pp. 677-686
    • Liu, M.T.1    Hu, H.P.2    Hsu, T.Y.3    Chen, J.Y.4
  • 214
    • 0029037293 scopus 로고
    • Characterization of Epstein-Barr virus DNase and its interaction with the major DNA binding protein
    • Lin SF, Hsu TY, Liu MY et al.: Characterization of Epstein-Barr virus DNase and its interaction with the major DNA binding protein. Virology 208(2), 712-722 (1995).
    • (1995) Virology , vol.208 , Issue.2 , pp. 712-722
    • Lin, S.F.1    Hsu, T.Y.2    Liu, M.Y.3
  • 215
    • 65349192186 scopus 로고    scopus 로고
    • The Epstein-Barr virus alkaline exonuclease BGLF5 serves pleiotropic functions in virus replication
    • Feederle R, Bannert H, Lips H, Muller-Lantzsch N, Delecluse HJ: The Epstein-Barr virus alkaline exonuclease BGLF5 serves pleiotropic functions in virus replication. J. Virol. 83(10), 4952-4962 (2009).
    • (2009) J. Virol , vol.83 , Issue.10 , pp. 4952-4962
    • Feederle, R.1    Bannert, H.2    Lips, H.3    Muller-Lantzsch, N.4    Delecluse, H.J.5
  • 217
    • 33847686708 scopus 로고    scopus 로고
    • Using or abusing: Viruses and the cellular DNA damage response
    • Lilley CE, Schwartz RA, Weitzman MD: Using or abusing: viruses and the cellular DNA damage response. Trends Microbiol. 15(3), 119-126 (2007).
    • (2007) Trends Microbiol , vol.15 , Issue.3 , pp. 119-126
    • Lilley, C.E.1    Schwartz, R.A.2    Weitzman, M.D.3
  • 218
    • 0142182192 scopus 로고    scopus 로고
    • The role of DNA recombination in herpes simplex virus DNA replication
    • Wilkinson DE, Weller SK: The role of DNA recombination in herpes simplex virus DNA replication. IUBMB Life 55(8), 451-458 (2003).
    • (2003) IUBMB Life , vol.55 , Issue.8 , pp. 451-458
    • Wilkinson, D.E.1    Weller, S.K.2
  • 220
    • 24044489232 scopus 로고    scopus 로고
    • Activation of ataxia telangiectasia-mutated DNA damage checkpoint signal transduction elicited by herpes simplex virus infection
    • Shirata N, Kudoh A, Daikoku T et al.: Activation of ataxia telangiectasia-mutated DNA damage checkpoint signal transduction elicited by herpes simplex virus infection. J. Biol. Chem. 280(34), 30336-30341 (2005).
    • (2005) J. Biol. Chem , vol.280 , Issue.34 , pp. 30336-30341
    • Shirata, N.1    Kudoh, A.2    Daikoku, T.3
  • 221
    • 4644296028 scopus 로고    scopus 로고
    • Recruitment of cellular recombination and repair proteins to sites of herpes simplex virus type 1 DNA replication is dependent on the composition of viral proteins within prereplicative sites and correlates with the induction of the DNA damage response
    • Cellular recombination/repair proteins implicated in herpesvirus replication, ■■
    • Wilkinson DE, Weller SK: Recruitment of cellular recombination and repair proteins to sites of herpes simplex virus type 1 DNA replication is dependent on the composition of viral proteins within prereplicative sites and correlates with the induction of the DNA damage response. J. Virol. 78(9), 4783-4796 (2004). ■■ Cellular recombination/repair proteins implicated in herpesvirus replication.
    • (2004) J. Virol , vol.78 , Issue.9 , pp. 4783-4796
    • Wilkinson, D.E.1    Weller, S.K.2
  • 222
    • 2442653990 scopus 로고    scopus 로고
    • Taylor TJ, Knipe DM: Proteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8. J. Virol. 78(11), 5856-5866 (2004).
    • Taylor TJ, Knipe DM: Proteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8. J. Virol. 78(11), 5856-5866 (2004).
  • 223
    • 3142710250 scopus 로고    scopus 로고
    • A human cellular protein activity (OF-1), which binds herpes simplex virus type 1 origin, contains the Ku70/Ku80 heterodimer
    • Murata LB, Dodson MS, Hall JD: A human cellular protein activity (OF-1), which binds herpes simplex virus type 1 origin, contains the Ku70/Ku80 heterodimer. J. Virol. 78(14), 7839-7842 (2004).
    • (2004) J. Virol , vol.78 , Issue.14 , pp. 7839-7842
    • Murata, L.B.1    Dodson, M.S.2    Hall, J.D.3
  • 224
    • 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 SP, Everett RD: 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), 650-657 (1999).
    • (1999) J. Virol , vol.73 , Issue.1 , pp. 650-657
    • Parkinson, J.1    Lees-Miller, S.P.2    Everett, R.D.3
  • 225
    • 42749092510 scopus 로고    scopus 로고
    • Chk2 is required for HSV-1 ICP0-mediated G2/M arrest and enhancement of virus growth
    • Li H, Baskaran R, Krisky DM et al.: Chk2 is required for HSV-1 ICP0-mediated G2/M arrest and enhancement of virus growth. Virology 375(1), 13-23 (2008).
    • (2008) Virology , vol.375 , Issue.1 , pp. 13-23
    • Li, H.1    Baskaran, R.2    Krisky, D.M.3
  • 226
    • 33746871757 scopus 로고    scopus 로고
    • Herpes simplex virus type I disrupts the ATR-dependent DNA-damage response during lytic infection
    • Wilkinson DE, Weller SK: Herpes simplex virus type I disrupts the ATR-dependent DNA-damage response during lytic infection. J. Cell Sci. 119(Pt 13), 2695-2703 (2006).
    • (2006) J. Cell Sci , vol.119 , Issue.PART 13 , pp. 2695-2703
    • Wilkinson, D.E.1    Weller, S.K.2
  • 227
    • 33846809462 scopus 로고    scopus 로고
    • Human cytomegalovirus disrupts both ataxia telangiectasia mutated protein (ATM)- and ATM-Rad3-related kinase-mediated DNA damage responses during lytic infection
    • Luo MH, Rosenke K, Czornak K, Fortunato EA: Human cytomegalovirus disrupts both ataxia telangiectasia mutated protein (ATM)- and ATM-Rad3-related kinase-mediated DNA damage responses during lytic infection. J. Virol. 81(4), 1934-1950 (2007).
    • (2007) J. Virol , vol.81 , Issue.4 , pp. 1934-1950
    • Luo, M.H.1    Rosenke, K.2    Czornak, K.3    Fortunato, E.A.4
  • 229
    • 14844336913 scopus 로고    scopus 로고
    • Epstein-Barr virus lytic replication elicits ATM checkpoint signal transduction while providing an S-phase-like cellular environment
    • Demonstrates that EBV activates the ATM DNA damage response pathway, ■
    • Kudoh A, Fujita M, Zhang L et al.: Epstein-Barr virus lytic replication elicits ATM checkpoint signal transduction while providing an S-phase-like cellular environment. J. Biol. Chem. 280(9), 8156-8163 (2005). ■ Demonstrates that EBV activates the ATM DNA damage response pathway.
    • (2005) J. Biol. Chem , vol.280 , Issue.9 , pp. 8156-8163
    • Kudoh, A.1    Fujita, M.2    Zhang, L.3
  • 230
    • 67449098555 scopus 로고    scopus 로고
    • Homologous recombinational repair factors are recruited and loaded onto the viral DNA genome in Epstein-Barr virus replication compartments
    • Demonstrates that cellular recombination proteins are recruited to EBV replication compartments, ■
    • Kudoh A, Iwahori S, Sato Y et al.: Homologous recombinational repair factors are recruited and loaded onto the viral DNA genome in Epstein-Barr virus replication compartments. J. Virol. 83(13), 6641-6651 (2009). ■ Demonstrates that cellular recombination proteins are recruited to EBV replication compartments.
    • (2009) J. Virol , vol.83 , Issue.13 , pp. 6641-6651
    • Kudoh, A.1    Iwahori, S.2    Sato, Y.3
  • 231
    • 42449139730 scopus 로고    scopus 로고
    • Epstein-Barr virus immediate-early protein Zta co-opts mitochondrial single-stranded DNA binding protein to promote viral and inhibit mitochondrial DNA replication
    • Wiedmer A, Wang P, Zhou J et al.: Epstein-Barr virus immediate-early protein Zta co-opts mitochondrial single-stranded DNA binding protein to promote viral and inhibit mitochondrial DNA replication. J. Virol. 82(9), 4647-4655 (2008).
    • (2008) J. Virol , vol.82 , Issue.9 , pp. 4647-4655
    • Wiedmer, A.1    Wang, P.2    Zhou, J.3
  • 232
    • 70350314472 scopus 로고    scopus 로고
    • Functional interaction between Epstein-Barr virus replication protein Zta and host DNA-damage response protein 53BP1
    • Bailey SG, Verrall E, Schelcher C, Rhie A, Doherty AJ, Sinclair AJ: Functional interaction between Epstein-Barr virus replication protein Zta and host DNA-damage response protein 53BP1. J. Virol. 83(21), 11116-11122 (2009).
    • (2009) J. Virol , vol.83 , Issue.21 , pp. 11116-11122
    • Bailey, S.G.1    Verrall, E.2    Schelcher, C.3    Rhie, A.4    Doherty, A.J.5    Sinclair, A.J.6
  • 233
    • 34247248708 scopus 로고    scopus 로고
    • Epstein-Barr virus-associated B-cell lymphoma in a patient with DNA ligase IV (LIG4) syndrome
    • EBV implicated as a causative agent in the formation of lymphomas in patients with DNA ligsase IV syndrome, ■
    • Toita N, Hatano N, Ono S et al.: Epstein-Barr virus-associated B-cell lymphoma in a patient with DNA ligase IV (LIG4) syndrome. Am. J. Med. Genet. A 143(7), 742-745 (2007). ■ EBV implicated as a causative agent in the formation of lymphomas in patients with DNA ligsase IV syndrome.
    • (2007) Am. J. Med. Genet. A , vol.143 , Issue.7 , pp. 742-745
    • Toita, N.1    Hatano, N.2    Ono, S.3
  • 234
    • 33744957331 scopus 로고    scopus 로고
    • Postreplicative mismatch repair factors are recruited to Epstein-Barr virus replication compartments
    • Demonstrates that cellular mismatch repair proteins are recruited to EBV replication compartments, ■
    • Daikoku T, Kudoh A, Sugaya Y et al.: Postreplicative mismatch repair factors are recruited to Epstein-Barr virus replication compartments. J. Biol. Chem. 281(16), 11422-11430 (2006). ■ Demonstrates that cellular mismatch repair proteins are recruited to EBV replication compartments.
    • (2006) J. Biol. Chem , vol.281 , Issue.16 , pp. 11422-11430
    • Daikoku, T.1    Kudoh, A.2    Sugaya, Y.3
  • 235
    • 67749088500 scopus 로고    scopus 로고
    • Topoisomerase I and RecQL1 function in Epstein-Barr virus lytic reactivation
    • Wang P, Rennekamp AJ, Yuan Y, Lieberman PM: Topoisomerase I and RecQL1 function in Epstein-Barr virus lytic reactivation. J. Virol. 83(16), 8090-8098 (2009).
    • (2009) J. Virol , vol.83 , Issue.16 , pp. 8090-8098
    • Wang, P.1    Rennekamp, A.J.2    Yuan, Y.3    Lieberman, P.M.4
  • 236
    • 36749009009 scopus 로고    scopus 로고
    • Xeroderma pigmentosum C is involved in Epstein Barr virus DNA replication
    • Lu CC, Chen YC, Wang JT, Yang PW, Chen MR: Xeroderma pigmentosum C is involved in Epstein Barr virus DNA replication. J. Gen. Virol. 88(Pt 12), 3234-243 (2007).
    • (2007) J. Gen. Virol , vol.88 , Issue.PART 12 , pp. 3234-3243
    • Lu, C.C.1    Chen, Y.C.2    Wang, J.T.3    Yang, P.W.4    Chen, M.R.5
  • 237
    • 34248339596 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus
    • Gershburg E, Raffa S, Torrisi MR, Pagano JS: Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus. J. Virol. 81(10), 5407-5412 (2007).
    • (2007) J. Virol , vol.81 , Issue.10 , pp. 5407-5412
    • Gershburg, E.1    Raffa, S.2    Torrisi, M.R.3    Pagano, J.S.4
  • 238
    • 34249910944 scopus 로고    scopus 로고
    • γ-herpesvirus kinase actively initiates a DNA damage response by inducing phosphorylation of H2AX to foster viral replication
    • Tarakanova VL, Leung-Pineda V, Hwang S et al.: γ-herpesvirus kinase actively initiates a DNA damage response by inducing phosphorylation of H2AX to foster viral replication. Cell Host Microbe 1(4), 275-286 (2007).
    • (2007) Cell Host Microbe , vol.1 , Issue.4 , pp. 275-286
    • Tarakanova, V.L.1    Leung-Pineda, V.2    Hwang, S.3
  • 239
    • 33744907726 scopus 로고    scopus 로고
    • Deregulation of DNA damage signal transduction by herpesvirus latency-associated M2
    • Liang X, Pickering MT, Cho NH et al.: Deregulation of DNA damage signal transduction by herpesvirus latency-associated M2. J. Virol. 80(12), 5862-5874 (2006).
    • (2006) J. Virol , vol.80 , Issue.12 , pp. 5862-5874
    • Liang, X.1    Pickering, M.T.2    Cho, N.H.3
  • 240
    • 34347244891 scopus 로고    scopus 로고
    • The IRF family, revisited
    • Paun A, Pitha PM: The IRF family, revisited. Biochimie 89(6-7), 744-753 (2007).
    • (2007) Biochimie , vol.89 , Issue.6-7 , pp. 744-753
    • Paun, A.1    Pitha, P.M.2
  • 241
    • 67449097025 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus viral interferon regulatory factor 4 targets MDM2 to deregulate the p53 tumor suppressor pathway
    • Lee HR, Toth Z, Shin YC et al.: Kaposi's sarcoma-associated herpesvirus viral interferon regulatory factor 4 targets MDM2 to deregulate the p53 tumor suppressor pathway. J. Virol. 83(13), 6739-6747 (2009).
    • (2009) J. Virol , vol.83 , Issue.13 , pp. 6739-6747
    • Lee, H.R.1    Toth, Z.2    Shin, Y.C.3
  • 242
    • 40149108605 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus ori-Lyt-dependent DNA replication: Involvement of host cellular factors
    • Wang Y, Li H, Tang Q, Maul GG, Yuan Y: Kaposi's sarcoma-associated herpesvirus ori-Lyt-dependent DNA replication: involvement of host cellular factors. J. Virol. 82(6), 2867-2882 (2008).
    • (2008) J. Virol , vol.82 , Issue.6 , pp. 2867-2882
    • Wang, Y.1    Li, H.2    Tang, Q.3    Maul, G.G.4    Yuan, Y.5
  • 243
    • 30644464100 scopus 로고    scopus 로고
    • TATA-binding protein and TBP-associated factors during herpes simplex virus type 1 infection: Localization at viral DNA replication sites
    • Quadt I, Gunther AK, Voss D, Schelhaas M, Knebel-Morsdorf D: TATA-binding protein and TBP-associated factors during herpes simplex virus type 1 infection: localization at viral DNA replication sites. Virus Res. 115(2), 207-213 (2006).
    • (2006) Virus Res , vol.115 , Issue.2 , pp. 207-213
    • Quadt, I.1    Gunther, A.K.2    Voss, D.3    Schelhaas, M.4    Knebel-Morsdorf, D.5
  • 244
    • 0028069405 scopus 로고
    • RNA polymerase II is aberrantly phosphorylated and localized to viral replication compartments following herpes simplex virus infection
    • Rice SA, Long MC, Lam V, Spencer CA: RNA polymerase II is aberrantly phosphorylated and localized to viral replication compartments following herpes simplex virus infection. J. Virol. 68(2), 988-1001 (1994).
    • (1994) J. Virol , vol.68 , Issue.2 , pp. 988-1001
    • Rice, S.A.1    Long, M.C.2    Lam, V.3    Spencer, C.A.4
  • 245
    • 0031036324 scopus 로고    scopus 로고
    • Association of herpes simplex virus regulatory protein ICP22 with transcriptional complexes containing EAP, ICP4, RNA polymerase II, and viral DNA requires posttranslational modification by the U(L)13 proteinkinase
    • Leopardi R, Ward PL, Ogle WO, Roizman B: Association of herpes simplex virus regulatory protein ICP22 with transcriptional complexes containing EAP, ICP4, RNA polymerase II, and viral DNA requires posttranslational modification by the U(L)13 proteinkinase. J. Virol. 71(2), 1133-1139 (1997).
    • (1997) J. Virol , vol.71 , Issue.2 , pp. 1133-1139
    • Leopardi, R.1    Ward, P.L.2    Ogle, W.O.3    Roizman, B.4
  • 246
    • 30444436433 scopus 로고    scopus 로고
    • Transcription factors and DNA replication origin selection
    • Kohzaki H, Murakami Y: Transcription factors and DNA replication origin selection. Bioessays 27(11), 1107-1116 (2005).
    • (2005) Bioessays , vol.27 , Issue.11 , pp. 1107-1116
    • Kohzaki, H.1    Murakami, Y.2
  • 247
    • 56449106852 scopus 로고    scopus 로고
    • Cellular transcription factors Sp1 and Sp3 suppress varicella-zoster virus origin-dependent DNA replication
    • Khalil MI, Hay J, Ruyechan WT: Cellular transcription factors Sp1 and Sp3 suppress varicella-zoster virus origin-dependent DNA replication. J. Virol. 82(23), 11723-11733 (2008).
    • (2008) J. Virol , vol.82 , Issue.23 , pp. 11723-11733
    • Khalil, M.I.1    Hay, J.2    Ruyechan, W.T.3
  • 248
    • 0024352084 scopus 로고
    • Responsiveness of the Epstein-Barr virus NotI repeat promoter to the Z transactivator is mediated in a cell-type-specific manner by two independent signal regions
    • Lieberman PM, Hardwick JM, Hayward SD: Responsiveness of the Epstein-Barr virus NotI repeat promoter to the Z transactivator is mediated in a cell-type-specific manner by two independent signal regions. J. Virol. 63(7), 3040-3050 (1989).
    • (1989) J. Virol , vol.63 , Issue.7 , pp. 3040-3050
    • Lieberman, P.M.1    Hardwick, J.M.2    Hayward, S.D.3
  • 249
    • 0023261757 scopus 로고
    • The herpes simplex virus origins of DNA synthesis in the S component are each contained in a transcribed open reading frame
    • Hubenthal-Voss J, Starr L, Roizman B: The herpes simplex virus origins of DNA synthesis in the S component are each contained in a transcribed open reading frame. J. Virol. 61(11), 3349-3355 (1987).
    • (1987) J. Virol , vol.61 , Issue.11 , pp. 3349-3355
    • Hubenthal-Voss, J.1    Starr, L.2    Roizman, B.3
  • 250
    • 0024110445 scopus 로고
    • Properties of two 5′-coterminal RNAs transcribed part way and across the S component origin of DNA synthesis of the herpes simplex virus 1 genome
    • Voss JH, Roizman B: Properties of two 5′-coterminal RNAs transcribed part way and across the S component origin of DNA synthesis of the herpes simplex virus 1 genome. Proc. Natl Acad. Sci. USA 85(22), 8454-8458 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , Issue.22 , pp. 8454-8458
    • Voss, J.H.1    Roizman, B.2
  • 251
    • 34250888716 scopus 로고    scopus 로고
    • Complexities associated with expression of Epstein-Barr virus (EBV) lytic origins of DNA replication
    • Xue SA, Griffin BE: Complexities associated with expression of Epstein-Barr virus (EBV) lytic origins of DNA replication. Nucleic Acids Res. 35(10), 3391-3406 (2007).
    • (2007) Nucleic Acids Res , vol.35 , Issue.10 , pp. 3391-3406
    • Xue, S.A.1    Griffin, B.E.2
  • 252
    • 0029796960 scopus 로고    scopus 로고
    • Properties of a primer RNA-DNA hybrid at the mouse mitochondrial DNA leading-strand origin of replication
    • Lee DY, Clayton DA: Properties of a primer RNA-DNA hybrid at the mouse mitochondrial DNA leading-strand origin of replication. J. Biol. Chem. 271(39), 24262-24269 (1996).
    • (1996) J. Biol. Chem , vol.271 , Issue.39 , pp. 24262-24269
    • Lee, D.Y.1    Clayton, D.A.2
  • 253
    • 70349739364 scopus 로고    scopus 로고
    • A role for G-quadruplex RNA binding by Epstein-Barr virus nuclear antigen 1 (EBNA1) in DNA replication and metaphase chromosome attachment
    • Norseen J, Johnson FB, Lieberman PM: A role for G-quadruplex RNA binding by Epstein-Barr virus nuclear antigen 1 (EBNA1) in DNA replication and metaphase chromosome attachment. J. Virol. 83(20), 10336-10346 (2009).
    • (2009) J. Virol , vol.83 , Issue.20 , pp. 10336-10346
    • Norseen, J.1    Johnson, F.B.2    Lieberman, P.M.3
  • 255
    • 33646737238 scopus 로고    scopus 로고
    • Epstein-Barr virus protein kinase BGLF4 is a virion tegument protein that dissociates from virions in a phosphorylation-dependent process and phosphorylates the viral immediate-early protein BZLF1
    • Asai R, Kato A, Kato K et al.: Epstein-Barr virus protein kinase BGLF4 is a virion tegument protein that dissociates from virions in a phosphorylation-dependent process and phosphorylates the viral immediate-early protein BZLF1. J. Virol. 80(11), 5125-5134 (2006).
    • (2006) J. Virol , vol.80 , Issue.11 , pp. 5125-5134
    • Asai, R.1    Kato, A.2    Kato, K.3
  • 256
    • 28044472990 scopus 로고    scopus 로고
    • Detection of Epstein-Barr virus BGLF4 protein kinase in virus replication compartments and virus particles
    • Wang JT, Yang PW, Lee CP, Han CH, Tsai CH, Chen MR: Detection of Epstein-Barr virus BGLF4 protein kinase in virus replication compartments and virus particles. J. Gen. Virol. 86(Pt 12), 3215-3225 (2005).
    • (2005) J. Gen. Virol , vol.86 , Issue.PART 12 , pp. 3215-3225
    • Wang, J.T.1    Yang, P.W.2    Lee, C.P.3    Han, C.H.4    Tsai, C.H.5    Chen, M.R.6
  • 257
    • 33749463157 scopus 로고    scopus 로고
    • Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication
    • Kudoh A, Daikoku T, Ishimi Y et al.: Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication. J. Virol. 80(20), 10064-10072 (2006).
    • (2006) J. Virol , vol.80 , Issue.20 , pp. 10064-10072
    • Kudoh, A.1    Daikoku, T.2    Ishimi, Y.3
  • 258
    • 11144246925 scopus 로고    scopus 로고
    • In vivo dynamics of EBNA1-OriP interaction during latent and lytic replication of Epstein-Barr virus
    • Daikoku T, Kudoh A, Fujita M, Sugaya Y, Isomura H, Tsurumi T: In vivo dynamics of EBNA1-OriP interaction during latent and lytic replication of Epstein-Barr virus. J. Biol. Chem. 279(52), 54817-54825 (2004).
    • (2004) J. Biol. Chem , vol.279 , Issue.52 , pp. 54817-54825
    • Daikoku, T.1    Kudoh, A.2    Fujita, M.3    Sugaya, Y.4    Isomura, H.5    Tsurumi, T.6
  • 259
    • 65349113014 scopus 로고    scopus 로고
    • Protein array identification of substrates of the Epstein-Barr virus protein kinase BGLF4
    • Zhu J, Liao G, Shan L et al.: Protein array identification of substrates of the Epstein-Barr virus protein kinase BGLF4. J. Virol. 83(10), 5219-5231 (2009).
    • (2009) J. Virol , vol.83 , Issue.10 , pp. 5219-5231
    • Zhu, J.1    Liao, G.2    Shan, L.3
  • 260
    • 33846508516 scopus 로고    scopus 로고
    • Characterization of the uracil-DNA glycosylase activity of Epstein-Barr virus BKRF3 and its role in lytic viral DNA replication
    • Lu CC, Huang HT, Wang JT et al.: Characterization of the uracil-DNA glycosylase activity of Epstein-Barr virus BKRF3 and its role in lytic viral DNA replication. J. Virol. 81(3), 1195-1208 (2007).
    • (2007) J. Virol , vol.81 , Issue.3 , pp. 1195-1208
    • Lu, C.C.1    Huang, H.T.2    Wang, J.T.3
  • 261
    • 0028291733 scopus 로고
    • Evidence that the herpes simplex virus type 1 uracil DNA glycosylase is required for efficient viral replication and latency in the murine nervous system
    • Pyles RB, Thompson RL: Evidence that the herpes simplex virus type 1 uracil DNA glycosylase is required for efficient viral replication and latency in the murine nervous system. J. Virol. 68(8), 4963-4972 (1994).
    • (1994) J. Virol , vol.68 , Issue.8 , pp. 4963-4972
    • Pyles, R.B.1    Thompson, R.L.2
  • 262
    • 0034909237 scopus 로고    scopus 로고
    • Requirement for uracil-DNA glycosylase during the transition to late-phase cytomegalovirus DNA replication
    • Courcelle CT, Courcelle J, Prichard MN, Mocarski ES: Requirement for uracil-DNA glycosylase during the transition to late-phase cytomegalovirus DNA replication. J. Virol. 75(16), 7592-7601 (2001).
    • (2001) J. Virol , vol.75 , Issue.16 , pp. 7592-7601
    • Courcelle, C.T.1    Courcelle, J.2    Prichard, M.N.3    Mocarski, E.S.4
  • 263
    • 0027076385 scopus 로고
    • Uracil in OriS of herpes simplex 1 alters its specific recognition by origin binding protein (OBP): Does virus induced uracil-DNA glycosylase play a key role in viral reactivation and replication?
    • Focher F, Verri A, Verzeletti S, Mazzarello P, Spadari S: Uracil in OriS of herpes simplex 1 alters its specific recognition by origin binding protein (OBP): does virus induced uracil-DNA glycosylase play a key role in viral reactivation and replication? Chromosoma 102(1 Suppl.), S67-S71 (1992).
    • (1992) Chromosoma , vol.102 , Issue.1 SUPPL.
    • Focher, F.1    Verri, A.2    Verzeletti, S.3    Mazzarello, P.4    Spadari, S.5
  • 264
    • 67650531087 scopus 로고    scopus 로고
    • Reconstitution of uracil DNA glycosylase-initiated base excision repair in herpes simplex virus-1
    • Bogani F, Chua CN, Boehmer PE: Reconstitution of uracil DNA glycosylase-initiated base excision repair in herpes simplex virus-1. J. Biol. Chem. 284(25), 16784-16790 (2009).
    • (2009) J. Biol. Chem , vol.284 , Issue.25 , pp. 16784-16790
    • Bogani, F.1    Chua, C.N.2    Boehmer, P.E.3
  • 265
    • 23944485244 scopus 로고    scopus 로고
    • Human cytomegalovirus uracil DNA glycosylase associates with ppUL44 and accelerates the accumulation of viral DNA
    • Prichard MN, Lawlor H, Duke GM et al.: Human cytomegalovirus uracil DNA glycosylase associates with ppUL44 and accelerates the accumulation of viral DNA. Virol. J. 2, 55 (2005).
    • (2005) Virol. J , vol.2 , pp. 55
    • Prichard, M.N.1    Lawlor, H.2    Duke, G.M.3
  • 266
    • 47049099550 scopus 로고    scopus 로고
    • Characterization of human cytomegalovirus uracil DNA glycosylase (UL114) and its interaction with polymerase processivity factor (UL44)
    • Ranneberg-Nilsen T, Dale HA, Luna L et al.: Characterization of human cytomegalovirus uracil DNA glycosylase (UL114) and its interaction with polymerase processivity factor (UL44). J. Mol. Biol. 381(2), 276-288 (2008).
    • (2008) J. Mol. Biol , vol.381 , Issue.2 , pp. 276-288
    • Ranneberg-Nilsen, T.1    Dale, H.A.2    Luna, L.3


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