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Volumn 88, Issue 9, 2014, Pages 4962-4975

Epstein-Barr virus BALF3 has nuclease activity and mediates mature virion production during the lytic cycle

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BALF3 PROTEIN; ENDONUCLEASE; MAGNESIUM; MANGANESE; NUCLEASE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84897495549     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00063-14     Document Type: Article
Times cited : (23)

References (90)
  • 1
    • 0015499229 scopus 로고
    • Separation of Epstein-Barr virus DNA from large chromosomal DNA in non-virus-producing cells
    • Nonoyama M, Pagano JS. 1972. Separation of Epstein-Barr virus DNA from large chromosomal DNA in non-virus-producing cells. Nat. New Biol. 238:169-171. http://dx.doi.org/10.1038/newbio238169a0.
    • (1972) Nat. New Biol. , vol.238 , pp. 169-171
    • Nonoyama, M.1    Pagano, J.S.2
  • 2
    • 0016308511 scopus 로고
    • Plasmid DNA as a possible state of Epstein-Barr virus genomes in nonproductive cells
    • Nonoyama M, Tanaka A. 1975. Plasmid DNA as a possible state of Epstein-Barr virus genomes in nonproductive cells. Cold Spring Harbor Symp. Quant. Biol. 39:807-810.
    • (1975) Cold Spring Harbor Symp. Quant. Biol. , vol.39 , pp. 807-810
    • Nonoyama, M.1    Tanaka, A.2
  • 3
    • 0004445838 scopus 로고
    • Epstein-Barr virus genomes with properties of circular DNA molecules in carrier cells
    • Adams A, Lindahl T. 1975. Epstein-Barr virus genomes with properties of circular DNA molecules in carrier cells. Proc. Natl. Acad. Sci. U. S. A. 72:1477-1481. http://dx.doi.org/10.1073/pnas.72.4.1477.
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , pp. 1477-1481
    • Adams, A.1    Lindahl, T.2
  • 4
    • 0344622126 scopus 로고
    • A cis-acting element from the Epstein-Barr viral genome that permits stable replication of recombinant plasmids in latently infected cells
    • Yates J, Warren N, Reisman D, Sugden B. 1984. A cis-acting element from the Epstein-Barr viral genome that permits stable replication of recombinant plasmids in latently infected cells. Proc. Natl. Acad. Sci. U. S. A. 81:3806-3810. http://dx.doi.org/10.1073/pnas.81.12.3806.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 3806-3810
    • Yates, J.1    Warren, N.2    Reisman, D.3    Sugden, B.4
  • 5
    • 0021988550 scopus 로고
    • Stable replication of plasmids derived from Epstein-Barr virus in various mammalian cells
    • Yates JL, Warren N, Sugden B. 1985. Stable replication of plasmids derived from Epstein-Barr virus in various mammalian cells. Nature 313: 812-815. http://dx.doi.org/10.1038/313812a0.
    • (1985) Nature , vol.313 , pp. 812-815
    • Yates, J.L.1    Warren, N.2    Sugden, B.3
  • 6
    • 0023183647 scopus 로고
    • Replication of latent Epstein-Barr virus genomes in Raji cells
    • Adams A. 1987. Replication of latent Epstein-Barr virus genomes in Raji cells. J. Virol. 61:1743-1746.
    • (1987) J. Virol. , vol.61 , pp. 1743-1746
    • Adams, A.1
  • 7
    • 0035881485 scopus 로고    scopus 로고
    • Human origin recognition complex binds to the region of the latent origin of DNA replication of Epstein-Barr virus
    • Schepers A, Ritzi M, Bousset K, Kremmer E, Yates JL, Harwood J, Diffley JF, Hammerschmidt W. 2001. Human origin recognition complex binds to the region of the latent origin of DNA replication of Epstein-Barr virus. EMBO J. 20:4588-4602. http://dx.doi.org/10.1093/emboj/20.16.4588.
    • (2001) EMBO J. , vol.20 , pp. 4588-4602
    • Schepers, A.1    Ritzi, M.2    Bousset, K.3    Kremmer, E.4    Yates, J.L.5    Harwood, J.6    Diffley, J.F.7    Hammerschmidt, W.8
  • 8
    • 0035964363 scopus 로고    scopus 로고
    • Human DNA replication initiation factors, ORC and MCM, associate with oriP of Epstein-Barr virus
    • Chaudhuri B, Xu H, Todorov I, Dutta A, Yates JL. 2001. Human DNA replication initiation factors, ORC and MCM, associate with oriP of Epstein-Barr virus. Proc. Natl. Acad. Sci. U. S. A. 98:10085-10089. http://dx.doi.org/10.1073/pnas.181347998.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10085-10089
    • Chaudhuri, B.1    Xu, H.2    Todorov, I.3    Dutta, A.4    Yates, J.L.5
  • 10
    • 84863617583 scopus 로고    scopus 로고
    • Epstein-Barr nuclear antigen 1 (EBNA1)-dependent recruitment of origin recognition complex (Orc) on oriP of Epstein-Barr virus with purified proteins: stimulation by Cdc6 through its direct interaction with EBNA1
    • Moriyama K, Yoshizawa-Sugata N, Obuse C, Tsurimoto T, Masai H. 2012. Epstein-Barr nuclear antigen 1 (EBNA1)-dependent recruitment of origin recognition complex (Orc) on oriP of Epstein-Barr virus with purified proteins: stimulation by Cdc6 through its direct interaction with EBNA1. J. Biol. Chem. 287:23977-23994. http://dx.doi.org/10.1074/jbc.M112.368456.
    • (2012) J. Biol. Chem. , vol.287 , pp. 23977-23994
    • Moriyama, K.1    Yoshizawa-Sugata, N.2    Obuse, C.3    Tsurimoto, T.4    Masai, H.5
  • 11
    • 0023698910 scopus 로고
    • Identification and characterization of oriLyt, a lytic origin of DNA replication of Epstein-Barr virus
    • Hammerschmidt W, Sugden B. 1988. Identification and characterization of oriLyt, a lytic origin of DNA replication of Epstein-Barr virus. Cell 55:427-433. http://dx.doi.org/10.1016/0092-8674(88)90028-1.
    • (1988) Cell , vol.55 , pp. 427-433
    • Hammerschmidt, W.1    Sugden, B.2
  • 12
    • 0024375760 scopus 로고
    • Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes
    • Hammerschmidt W, Sugden B. 1989. Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes. Nature 340: 393-397. http://dx.doi.org/10.1038/340393a0.
    • (1989) Nature , vol.340 , pp. 393-397
    • Hammerschmidt, W.1    Sugden, B.2
  • 13
    • 0025049916 scopus 로고
    • Herpes simplex virus type 1 UL28 gene product is important for the formation of mature capsids
    • Addison C, Rixon FJ, Preston VG. 1990. Herpes simplex virus type 1 UL28 gene product is important for the formation of mature capsids. J. Gen. Virol. 71:2377-2384. http://dx.doi.org/10.1099/0022-1317-71-10-2377.
    • (1990) J. Gen. Virol. , vol.71 , pp. 2377-2384
    • Addison, C.1    Rixon, F.J.2    Preston, V.G.3
  • 14
    • 0027194739 scopus 로고
    • Characterization of a temperature-sensitive mutant of the UL15 open reading frame of herpes simplex virus 1
    • Poon AP, Roizman B. 1993. Characterization of a temperature-sensitive mutant of the UL15 open reading frame of herpes simplex virus 1. J. Virol. 67:4497-4503.
    • (1993) J. Virol. , vol.67 , pp. 4497-4503
    • Poon, A.P.1    Roizman, B.2
  • 15
    • 0027313477 scopus 로고
    • Identification of the gene product encoded by ORF UL56 of the human cytomegalovirus genome
    • Bogner E, Reschke M, Reis B, Mockenhaupt T, Radsak K. 1993. Identification of the gene product encoded by ORF UL56 of the human cytomegalovirus genome. Virology 196:290-293. http://dx.doi.org/10.1006/viro.1993.1477.
    • (1993) Virology , vol.196 , pp. 290-293
    • Bogner, E.1    Reschke, M.2    Reis, B.3    Mockenhaupt, T.4    Radsak, K.5
  • 16
    • 35348921131 scopus 로고    scopus 로고
    • The varicella-zoster virus DNA encapsidation genes: identification and characterization of the putative terminase subunits
    • Visalli RJ, Nicolosi DM, Irven KL, Goshorn B, Khan T, Visalli MA. 2007. The varicella-zoster virus DNA encapsidation genes: identification and characterization of the putative terminase subunits. Virus Res. 129: 200-211. http://dx.doi.org/10.1016/j.virusres.2007.07.015.
    • (2007) Virus Res. , vol.129 , pp. 200-211
    • Visalli, R.J.1    Nicolosi, D.M.2    Irven, K.L.3    Goshorn, B.4    Khan, T.5    Visalli, M.A.6
  • 18
    • 0027204661 scopus 로고
    • Herpes simplex virus type 1 DNA cleavage and encapsidation require the product of the UL28 gene: isolation and characterization of two UL28 deletion mutants
    • Tengelsen LA, Pederson NE, Shaver PR, Wathen MW, Homa FL. 1993. Herpes simplex virus type 1 DNA cleavage and encapsidation require the product of the UL28 gene: isolation and characterization of two UL28 deletion mutants. J. Virol. 67:3470-3480.
    • (1993) J. Virol. , vol.67 , pp. 3470-3480
    • Tengelsen, L.A.1    Pederson, N.E.2    Shaver, P.R.3    Wathen, M.W.4    Homa, F.L.5
  • 19
    • 0036510764 scopus 로고    scopus 로고
    • ATPase activity of the terminase subunit pUL56 of human cytomegalovirus
    • Hwang JS, Bogner E. 2002. ATPase activity of the terminase subunit pUL56 of human cytomegalovirus. J. Biol. Chem. 277:6943-6948. http://dx.doi.org/10.1074/jbc.M108984200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6943-6948
    • Hwang, J.S.1    Bogner, E.2
  • 20
    • 0031936307 scopus 로고    scopus 로고
    • The gene product of human cytomegalovirus open reading frame UL56 binds the pac motif and has specific nuclease activity
    • Bogner E, Radsak K, Stinski MF. 1998. The gene product of human cytomegalovirus open reading frame UL56 binds the pac motif and has specific nuclease activity. J. Virol. 72:2259-2264.
    • (1998) J. Virol. , vol.72 , pp. 2259-2264
    • Bogner, E.1    Radsak, K.2    Stinski, M.F.3
  • 21
    • 0028125245 scopus 로고
    • The herpes simplex virus 1 UL15 gene encodes two proteins and is required for cleavage of genomic viral DNA
    • Baines JD, Poon AP, Rovnak J, Roizman B. 1994. The herpes simplex virus 1 UL15 gene encodes two proteins and is required for cleavage of genomic viral DNA. J. Virol. 68:8118-8124.
    • (1994) J. Virol. , vol.68 , pp. 8118-8124
    • Baines, J.D.1    Poon, A.P.2    Rovnak, J.3    Roizman, B.4
  • 22
    • 0036529667 scopus 로고    scopus 로고
    • The terminase subunits pUL56 and pUL89 of human cytomegalovirus are DNA-metabolizing proteins with toroidal structure
    • Scheffczik H, Savva CG, Holzenburg A, Kolesnikova L, Bogner E. 2002. The terminase subunits pUL56 and pUL89 of human cytomegalovirus are DNA-metabolizing proteins with toroidal structure. Nucleic Acids Res. 30:1695-1703. http://dx.doi.org/10.1093/nar/30.7.1695.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1695-1703
    • Scheffczik, H.1    Savva, C.G.2    Holzenburg, A.3    Kolesnikova, L.4    Bogner, E.5
  • 23
    • 77952919201 scopus 로고    scopus 로고
    • Short hairpin RNAs specific to human cytomegalovirus terminase subunit pUL89 prevent viral maturation
    • Thoma C, Bogner E. 2010. Short hairpin RNAs specific to human cytomegalovirus terminase subunit pUL89 prevent viral maturation. Antivir. Ther. 15:391-400. http://dx.doi.org/10.3851/IMP1536.
    • (2010) Antivir. Ther. , vol.15 , pp. 391-400
    • Thoma, C.1    Bogner, E.2
  • 24
    • 0036239144 scopus 로고    scopus 로고
    • DNA cleavage and packaging proteins encoded by genes U(L)28, U(L)15, and U(L)33 of herpes simplex virus type 1 form a complex in infected cells
    • Beard PM, Taus NS, Baines JD. 2002. DNA cleavage and packaging proteins encoded by genes U(L)28, U(L)15, and U(L)33 of herpes simplex virus type 1 form a complex in infected cells. J. Virol. 76:4785-4791. http://dx.doi.org/10.1128/JVI.76.10.4785-4791.2002.
    • (2002) J. Virol. , vol.76 , pp. 4785-4791
    • Beard, P.M.1    Taus, N.S.2    Baines, J.D.3
  • 25
    • 33744931114 scopus 로고    scopus 로고
    • The putative terminase subunit of herpes simplex virus 1 encoded by UL28 is necessary and sufficient to mediate interaction between pUL15 and pUL33
    • Yang K, Baines JD. 2006. The putative terminase subunit of herpes simplex virus 1 encoded by UL28 is necessary and sufficient to mediate interaction between pUL15 and pUL33. J. Virol. 80:5733-5739. http://dx.doi.org/10.1128/JVI.00125-06.
    • (2006) J. Virol. , vol.80 , pp. 5733-5739
    • Yang, K.1    Baines, J.D.2
  • 26
    • 33845461933 scopus 로고    scopus 로고
    • Linker insertion mutations in the herpes simplex virus type 1 UL28 gene: effects on UL28 interaction with UL15 and UL33 and identification of a second-site mutation in the UL15 gene that suppresses a lethal UL28 mutation
    • Jacobson JG, Yang K, Baines JD, Homa FL. 2006. Linker insertion mutations in the herpes simplex virus type 1 UL28 gene: effects on UL28 interaction with UL15 and UL33 and identification of a second-site mutation in the UL15 gene that suppresses a lethal UL28 mutation. J. Virol. 80:12312-12323. http://dx.doi.org/10.1128/JVI.01766-06.
    • (2006) J. Virol. , vol.80 , pp. 12312-12323
    • Jacobson, J.G.1    Yang, K.2    Baines, J.D.3    Homa, F.L.4
  • 27
    • 69249214019 scopus 로고    scopus 로고
    • Characterization of the varicella-zoster virus ORF25 gene product: pORF25 interacts with multiple DNA encapsidation proteins
    • Visalli RJ, Knepper J, Goshorn B, Vanover K, Burnside DM, Irven K, McGauley R, Visalli M. 2009. Characterization of the varicella-zoster virus ORF25 gene product: pORF25 interacts with multiple DNA encapsidation proteins. Virus Res. 144:58-64. http://dx.doi.org/10.1016/j.virusres.2009.03.019.
    • (2009) Virus Res. , vol.144 , pp. 58-64
    • Visalli, R.J.1    Knepper, J.2    Goshorn, B.3    Vanover, K.4    Burnside, D.M.5    Irven, K.6    McGauley, R.7    Visalli, M.8
  • 28
  • 29
    • 0018095112 scopus 로고
    • Structure of the joint region and the termini of the DNA of herpes simplex virus type 1
    • Wagner MJ, Summers WC. 1978. Structure of the joint region and the termini of the DNA of herpes simplex virus type 1. J. Virol. 27:374-387.
    • (1978) J. Virol. , vol.27 , pp. 374-387
    • Wagner, M.J.1    Summers, W.C.2
  • 32
    • 0016790290 scopus 로고
    • Anatomy of herpes simplex virus DNA. II. Size, composition, and arrangement of inverted terminal repetitions
    • Wadsworth S, Jacob RJ, Roizman B. 1975. Anatomy of herpes simplex virus DNA. II. Size, composition, and arrangement of inverted terminal repetitions. J. Virol. 15:1487-1497.
    • (1975) J. Virol. , vol.15 , pp. 1487-1497
    • Wadsworth, S.1    Jacob, R.J.2    Roizman, B.3
  • 34
    • 0022006793 scopus 로고
    • Signals for site-specific cleavage of HSV DNA: maturation involves two separate cleavage events at sites distal to the recognition sequences
    • Varmuza SL, Smiley JR. 1985. Signals for site-specific cleavage of HSV DNA: maturation involves two separate cleavage events at sites distal to the recognition sequences. Cell 41:793-802. http://dx.doi.org/10.1016/S0092-8674(85)80060-X.
    • (1985) Cell , vol.41 , pp. 793-802
    • Varmuza, S.L.1    Smiley, J.R.2
  • 35
    • 0022521898 scopus 로고
    • Functional domains within the a sequence involved in the cleavage-packaging of herpes simplex virus DNA
    • Deiss LP, Chou J, Frenkel N. 1986. Functional domains within the a sequence involved in the cleavage-packaging of herpes simplex virus DNA. J. Virol. 59:605-618.
    • (1986) J. Virol. , vol.59 , pp. 605-618
    • Deiss, L.P.1    Chou, J.2    Frenkel, N.3
  • 36
    • 0022636662 scopus 로고
    • Herpes simplex virus amplicon: cleavage of concatemeric DNA is linked to packaging and involves amplification of the terminally reiterated a sequence
    • Deiss LP, Frenkel N. 1986. Herpes simplex virus amplicon: cleavage of concatemeric DNA is linked to packaging and involves amplification of the terminally reiterated a sequence. J. Virol. 57:933-941.
    • (1986) J. Virol. , vol.57 , pp. 933-941
    • Deiss, L.P.1    Frenkel, N.2
  • 37
    • 0023390688 scopus 로고
    • Structure and variability of the a sequence in the genome of human cytomegalovirus (Towne strain)
    • Mocarski ES, Liu AC, Spaete RR. 1987. Structure and variability of the a sequence in the genome of human cytomegalovirus (Towne strain). J. Gen. Virol. 68:2223-2230. http://dx.doi.org/10.1099/0022-1317-68-8-2223.
    • (1987) J. Gen. Virol. , vol.68 , pp. 2223-2230
    • Mocarski, E.S.1    Liu, A.C.2    Spaete, R.R.3
  • 38
    • 0021346401 scopus 로고
    • Heterogeneity in subregions of the terminal repeats of herpes simplex virus type 2 DNA
    • van den Berg FM, van Ooyen AJ, Volkers H, Walboomers JM. 1984. Heterogeneity in subregions of the terminal repeats of herpes simplex virus type 2 DNA. Intervirology 21:96-103. http://dx.doi.org/10.1159/000149507.
    • (1984) Intervirology , vol.21 , pp. 96-103
    • van den Berg, F.M.1    van Ooyen, A.J.2    Volkers, H.3    Walboomers, J.M.4
  • 39
    • 0021893583 scopus 로고
    • The a sequence of the cytomegalovirus genome functions as a cleavage/packaging signal for herpes simplex virus defective genomes
    • Spaete RR, Mocarski ES. 1985. The a sequence of the cytomegalovirus genome functions as a cleavage/packaging signal for herpes simplex virus defective genomes. J. Virol. 54:817-824.
    • (1985) J. Virol. , vol.54 , pp. 817-824
    • Spaete, R.R.1    Mocarski, E.S.2
  • 40
    • 0022374025 scopus 로고
    • Analysis of the genomic termini of tupaia herpesvirus DNA by restriction mapping and nucleotide sequencing
    • Albrecht M, Darai G, Flugel RM. 1985. Analysis of the genomic termini of tupaia herpesvirus DNA by restriction mapping and nucleotide sequencing. J. Virol. 56:466-474.
    • (1985) J. Virol. , vol.56 , pp. 466-474
    • Albrecht, M.1    Darai, G.2    Flugel, R.M.3
  • 41
    • 0021723832 scopus 로고
    • Structure of the genome termini of varicella-zoster virus
    • Davison AJ. 1984. Structure of the genome termini of varicella-zoster virus. J. Gen. Virol. 65:1969-1977. http://dx.doi.org/10.1099/0022-1317-65-11-1969.
    • (1984) J. Gen. Virol. , vol.65 , pp. 1969-1977
    • Davison, A.J.1
  • 43
    • 0023845901 scopus 로고
    • Replication of the murine cytomegalovirus genome: structure and role of the termini in the generation and cleavage of concatenates
    • Marks JR, Spector DH. 1988. Replication of the murine cytomegalovirus genome: structure and role of the termini in the generation and cleavage of concatenates. Virology 162:98-107. http://dx.doi.org/10.1016/0042-6822(88)90398-4.
    • (1988) Virology , vol.162 , pp. 98-107
    • Marks, J.R.1    Spector, D.H.2
  • 44
    • 0023833517 scopus 로고
    • Specificity of cleavage in replicative-form DNA of bovine herpesvirus 1
    • Hammerschmidt W, Ludwig H, Buhk HJ. 1988. Specificity of cleavage in replicative-form DNA of bovine herpesvirus 1. J. Virol. 62:1355-1363.
    • (1988) J. Virol. , vol.62 , pp. 1355-1363
    • Hammerschmidt, W.1    Ludwig, H.2    Buhk, H.J.3
  • 46
    • 0031963626 scopus 로고    scopus 로고
    • Sequences within the herpesvirus-conserved pac1 and pac2 motifs are required for cleavage and packaging of the murine cytomegalovirus genome
    • McVoy MA, Nixon DE, Adler SP, Mocarski ES. 1998. Sequences within the herpesvirus-conserved pac1 and pac2 motifs are required for cleavage and packaging of the murine cytomegalovirus genome. J. Virol. 72:48-56.
    • (1998) J. Virol. , vol.72 , pp. 48-56
    • McVoy, M.A.1    Nixon, D.E.2    Adler, S.P.3    Mocarski, E.S.4
  • 47
    • 0035853056 scopus 로고    scopus 로고
    • Herpes simplex virus DNA packaging sequences adopt novel structures that are specifically recognized by a component of the cleavage and packaging machinery
    • Adelman K, Salmon B, Baines JD. 2001. Herpes simplex virus DNA packaging sequences adopt novel structures that are specifically recognized by a component of the cleavage and packaging machinery. Proc. Natl. Acad. Sci. U. S. A. 98:3086-3091. http://dx.doi.org/10.1073/pnas.061555698.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 3086-3091
    • Adelman, K.1    Salmon, B.2    Baines, J.D.3
  • 48
    • 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. 1995. Structure and role of the terminal repeats of Epstein-Barr virus in processing and packaging of virion DNA. J. Virol. 69:3147-3155.
    • (1995) J. Virol. , vol.69 , pp. 3147-3155
    • Zimmermann, J.1    Hammerschmidt, W.2
  • 49
    • 19944396158 scopus 로고    scopus 로고
    • Defective infectious particles and rare packaged genomes produced by cells carrying terminal-repeat-negative Epstein-Barr virus
    • Feederle R, Shannon-Lowe C, Baldwin G, Delecluse HJ. 2005. Defective infectious particles and rare packaged genomes produced by cells carrying terminal-repeat-negative Epstein-Barr virus. J. Virol. 79:7641-7647. http://dx.doi.org/10.1128/JVI.79.12.7641-7647.2005.
    • (2005) J. Virol. , vol.79 , pp. 7641-7647
    • Feederle, R.1    Shannon-Lowe, C.2    Baldwin, G.3    Delecluse, H.J.4
  • 50
    • 84873823633 scopus 로고    scopus 로고
    • An Epstein-Barr virus mutant produces immunogenic defective particles devoid of viral DNA
    • Pavlova S, Feederle R, Gartner K, Fuchs W, Granzow H, Delecluse HJ. 2013. An Epstein-Barr virus mutant produces immunogenic defective particles devoid of viral DNA. J. Virol. 87:2011-2022. http://dx.doi.org/10.1128/JVI.02533-12.
    • (2013) J. Virol. , vol.87 , pp. 2011-2022
    • Pavlova, S.1    Feederle, R.2    Gartner, K.3    Fuchs, W.4    Granzow, H.5    Delecluse, H.J.6
  • 52
    • 0032824654 scopus 로고    scopus 로고
    • Requirement for cell-to-cell contact in Epstein-Barr virus infection of nasopharyngeal carcinoma cells and keratinocytes
    • Chang Y, Tung CH, Huang YT, Lu J, Chen JY, Tsai CH. 1999. Requirement for cell-to-cell contact in Epstein-Barr virus infection of nasopharyngeal carcinoma cells and keratinocytes. J. Virol. 73:8857-8866.
    • (1999) J. Virol. , vol.73 , pp. 8857-8866
    • Chang, Y.1    Tung, C.H.2    Huang, Y.T.3    Lu, J.4    Chen, J.Y.5    Tsai, C.H.6
  • 53
    • 0034467912 scopus 로고    scopus 로고
    • A baculovirus superinfection system: efficient vehicle for gene transfer into Drosophila S2 cells
    • Lee DF, Chen CC, Hsu TA, Juang JL. 2000. A baculovirus superinfection system: efficient vehicle for gene transfer into Drosophila S2 cells. J. Virol. 74:11873-11880. http://dx.doi.org/10.1128/JVI.74.24.11873-11880.2000.
    • (2000) J. Virol. , vol.74 , pp. 11873-11880
    • Lee, D.F.1    Chen, C.C.2    Hsu, T.A.3    Juang, J.L.4
  • 55
    • 0029037293 scopus 로고
    • Characterization of Epstein-Barr virus DNase and its interaction with the major DNA binding protein
    • Lin SF, Hsu TY, Liu MY, Lin LS, Yang HL, Chen JY, Yang CS. 1995. Characterization of Epstein-Barr virus DNase and its interaction with the major DNA binding protein. Virology 208:712-722. http://dx.doi.org/10.1006/viro.1995.1203.
    • (1995) Virology , vol.208 , pp. 712-722
    • Lin, S.F.1    Hsu, T.Y.2    Liu, M.Y.3    Lin, L.S.4    Yang, H.L.5    Chen, J.Y.6    Yang, C.S.7
  • 56
    • 79952521991 scopus 로고    scopus 로고
    • Epstein-Barr virus (EBV) Rta-mediated EBV and Kaposi's sarcomaassociated herpesvirus lytic reactivations in 293 cells
    • Chen YJ, Tsai WH, Chen YL, Ko YC, Chou SP, Chen JY, Lin SF. 2011. Epstein-Barr virus (EBV) Rta-mediated EBV and Kaposi's sarcomaassociated herpesvirus lytic reactivations in 293 cells. PLoS One 6:e17809. http://dx.doi.org/10.1371/journal.pone.0017809.
    • (2011) PLoS One , vol.6
    • Chen, Y.J.1    Tsai, W.H.2    Chen, Y.L.3    Ko, Y.C.4    Chou, S.P.5    Chen, J.Y.6    Lin, S.F.7
  • 57
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and IκB proteins: new discoveries and insights
    • Baldwin AS, Jr. 1996. The NF-κB and IκB proteins: new discoveries and insights. Annu. Rev. Immunol. 14:649-681. http://dx.doi.org/10.1146/annurev.immunol.14.1.649.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649-681
    • Baldwin Jr., A.S.1
  • 58
    • 0036152167 scopus 로고    scopus 로고
    • Chromosomal integration of Epstein-Barr virus genomes in nasopharyngeal carcinoma cells
    • Chang Y, Cheng SD, Tsai CH. 2002. Chromosomal integration of Epstein-Barr virus genomes in nasopharyngeal carcinoma cells. Head Neck 24:143-150. http://dx.doi.org/10.1002/hed.10039.
    • (2002) Head Neck , vol.24 , pp. 143-150
    • Chang, Y.1    Cheng, S.D.2    Tsai, C.H.3
  • 59
    • 0001139633 scopus 로고
    • A study of malignant tumours in Nigeria by shortterm tissue culture
    • Pulvertaft RJV. 1965. A study of malignant tumours in Nigeria by shortterm tissue culture. J. Clin. Pathol. 18:261-273. http://dx.doi.org/10.1136/jcp.18.3.261.
    • (1965) J. Clin. Pathol. , vol.18 , pp. 261-273
    • Pulvertaft, R.J.V.1
  • 60
    • 0021346191 scopus 로고
    • Detection of circular and linear herpesvirus DNA molecules in mammalian cells by gel electrophoresis
    • Gardella T, Medveczky P, Sairenji T, Mulder C. 1984. Detection of circular and linear herpesvirus DNA molecules in mammalian cells by gel electrophoresis. J. Virol. 50:248-254.
    • (1984) J. Virol. , vol.50 , pp. 248-254
    • Gardella, T.1    Medveczky, P.2    Sairenji, T.3    Mulder, C.4
  • 61
    • 0015289418 scopus 로고
    • Epstein-Barr virus: transformation, cytopathic changes, and viral antigens in squirrel monkey and marmoset leukocytes
    • Miller G, Shope T, Lisco H, Stitt D, Lipman M. 1972. Epstein-Barr virus: transformation, cytopathic changes, and viral antigens in squirrel monkey and marmoset leukocytes. Proc. Natl. Acad. Sci. U. S. A. 69:383-387. http://dx.doi.org/10.1073/pnas.69.2.383.
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 383-387
    • Miller, G.1    Shope, T.2    Lisco, H.3    Stitt, D.4    Lipman, M.5
  • 63
    • 49949098917 scopus 로고    scopus 로고
    • Putative functional domains of human cytomegalovirus pUL56 involved in dimerization and benzimidazole D-ribonucleoside activity
    • Champier G, Couvreux A, Hantz S, Rametti A, Mazeron MC, Bouaziz S, Denis F, Alain S. 2008. Putative functional domains of human cytomegalovirus pUL56 involved in dimerization and benzimidazole D-ribonucleoside activity. Antivir. Ther. 13:643-654.
    • (2008) Antivir. Ther. , vol.13 , pp. 643-654
    • Champier, G.1    Couvreux, A.2    Hantz, S.3    Rametti, A.4    Mazeron, M.C.5    Bouaziz, S.6    Denis, F.7    Alain, S.8
  • 64
    • 0037337054 scopus 로고    scopus 로고
    • Identification of the ATP-binding site in the terminase subunit pUL56 of human cytomegalovirus
    • Scholz B, Rechter S, Drach JC, Townsend LB, Bogner E. 2003. Identification of the ATP-binding site in the terminase subunit pUL56 of human cytomegalovirus. Nucleic Acids Res. 31:1426-1433. http://dx.doi.org/10.1093/nar/gkg229.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1426-1433
    • Scholz, B.1    Rechter, S.2    Drach, J.C.3    Townsend, L.B.4    Bogner, E.5
  • 65
    • 31944444727 scopus 로고    scopus 로고
    • Genome-wide transcription program and expression of the Rta responsive gene of Epstein-Barr virus
    • Lu CC, Jeng YY, Tsai CH, Liu MY, Yeh SW, Hsu TY, Chen MR. 2006. Genome-wide transcription program and expression of the Rta responsive gene of Epstein-Barr virus. Virology 345:358-372. http://dx.doi.org/10.1016/j.virol.2005.09.064.
    • (2006) Virology , vol.345 , pp. 358-372
    • Lu, C.C.1    Jeng, Y.Y.2    Tsai, C.H.3    Liu, M.Y.4    Yeh, S.W.5    Hsu, T.Y.6    Chen, M.R.7
  • 66
    • 0019828909 scopus 로고
    • Molecular cloning of the complete Epstein-Barr virus genome as a set of overlapping restriction endonuclease fragments
    • Arrand JR, Rymo L, Walsh JE, Bjorck E, Lindahl T, Griffin BE. 1981. Molecular cloning of the complete Epstein-Barr virus genome as a set of overlapping restriction endonuclease fragments. Nucleic Acids Res. 9:2999-3014. http://dx.doi.org/10.1093/nar/9.13.2999.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 2999-3014
    • Arrand, J.R.1    Rymo, L.2    Walsh, J.E.3    Bjorck, E.4    Lindahl, T.5    Griffin, B.E.6
  • 67
    • 0018084923 scopus 로고
    • Enzymatic breakage of the cohesive end site of phage λ DNA: terminase (ter) reaction
    • Becker A, Gold M. 1978. Enzymatic breakage of the cohesive end site of phage λ DNA: terminase (ter) reaction. Proc. Natl. Acad. Sci. U. S. A. 75:4199-4203. http://dx.doi.org/10.1073/pnas.75.9.4199.
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 4199-4203
    • Becker, A.1    Gold, M.2
  • 68
    • 0027463091 scopus 로고
    • Physical and kinetic characterization of the DNA packaging enzyme from bacteriophage λ
    • Tomka MA, Catalano CE. 1993. Physical and kinetic characterization of the DNA packaging enzyme from bacteriophage λ. J. Biol. Chem. 268: 3056-3065.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3056-3065
    • Tomka, M.A.1    Catalano, C.E.2
  • 69
    • 0023788430 scopus 로고
    • Mechanism of cos DNA cleavage by bacteriophage λ terminase: multiple roles of ATP
    • Higgins RR, Lucko HJ, Becker A. 1988. Mechanism of cos DNA cleavage by bacteriophage λ terminase: multiple roles of ATP. Cell 54:765-775. http://dx.doi.org/10.1016/S0092-8674(88)91021-5.
    • (1988) Cell , vol.54 , pp. 765-775
    • Higgins, R.R.1    Lucko, H.J.2    Becker, A.3
  • 70
    • 0027146278 scopus 로고
    • The role of cosB, the binding site for terminase, the DNA packaging enzyme of bacteriophage λ, in the nicking reaction
    • Cue D, Feiss M. 1993. The role of cosB, the binding site for terminase, the DNA packaging enzyme of bacteriophage λ, in the nicking reaction. J. Mol. Biol. 234:594-609. http://dx.doi.org/10.1006/jmbi.1993.1614.
    • (1993) J. Mol. Biol. , vol.234 , pp. 594-609
    • Cue, D.1    Feiss, M.2
  • 71
    • 0028560406 scopus 로고
    • Chromosome end formation in phage λ, catalyzed by terminase, is controlled by twoDNAelements of cos, cosN and R3, and by ATP
    • Higgins RR, Becker A. 1994. Chromosome end formation in phage λ, catalyzed by terminase, is controlled by twoDNAelements of cos, cosN and R3, and by ATP. EMBO J. 13:6152-6161.
    • (1994) EMBO J. , vol.13 , pp. 6152-6161
    • Higgins, R.R.1    Becker, A.2
  • 72
    • 0029129293 scopus 로고
    • Interaction of terminase, the DNA packaging enzyme of phage λ, with its cosDNAsubstrate
    • Higgins RR, Becker A. 1995. Interaction of terminase, the DNA packaging enzyme of phage λ, with its cosDNAsubstrate. J. Mol. Biol. 252:31-46. http://dx.doi.org/10.1006/jmbi.1995.0473.
    • (1995) J. Mol. Biol. , vol.252 , pp. 31-46
    • Higgins, R.R.1    Becker, A.2
  • 73
    • 0025362781 scopus 로고
    • Bacteriophage lambda DNA: the beginning of the end
    • Becker A, Murialdo H. 1990. Bacteriophage lambda DNA: the beginning of the end. J. Bacteriol. 172:2819-2824.
    • (1990) J. Bacteriol. , vol.172 , pp. 2819-2824
    • Becker, A.1    Murialdo, H.2
  • 74
    • 0001607723 scopus 로고
    • Distantly related sequences in the α-and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ, Gay NJ. 1982. Distantly related sequences in the α-and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 76
    • 0036207969 scopus 로고    scopus 로고
    • Human cytomegalovirus terminase as a target for antiviral chemotherapy
    • Bogner E. 2002. Human cytomegalovirus terminase as a target for antiviral chemotherapy. Rev. Med. Virol. 12:115-127. http://dx.doi.org/10.1002/rmv.344.
    • (2002) Rev. Med. Virol. , vol.12 , pp. 115-127
    • Bogner, E.1
  • 77
    • 1842737691 scopus 로고    scopus 로고
    • Insights into the structure of human cytomegalovirus large terminase subunit pUL56
    • Savva CG, Holzenburg A, Bogner E. 2004. Insights into the structure of human cytomegalovirus large terminase subunit pUL56. FEBS Lett. 563: 135-140. http://dx.doi.org/10.1016/S0014-5793(04)00283-2.
    • (2004) FEBS Lett. , vol.563 , pp. 135-140
    • Savva, C.G.1    Holzenburg, A.2    Bogner, E.3
  • 78
    • 23044460704 scopus 로고    scopus 로고
    • Binding of two zinc finger nuclease monomers to two specific sites is required for effective double-strand DNA cleavage
    • Mani M, Smith J, Kandavelou K, Berg JM, Chandrasegaran S. 2005. Binding of two zinc finger nuclease monomers to two specific sites is required for effective double-strand DNA cleavage. Biochem. Biophys. Res. Commun. 334:1191-1197. http://dx.doi.org/10.1016/j.bbrc.2005.07.021.
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 1191-1197
    • Mani, M.1    Smith, J.2    Kandavelou, K.3    Berg, J.M.4    Chandrasegaran, S.5
  • 79
    • 0034283804 scopus 로고    scopus 로고
    • Requirements for double-strand cleavage by chimeric restriction enzymes with zinc finger DNA-recognition domains
    • Smith J, Bibikova M, Whitby FG, Reddy AR, Chandrasegaran S, Carroll D. 2000. Requirements for double-strand cleavage by chimeric restriction enzymes with zinc finger DNA-recognition domains. Nucleic Acids Res. 28:3361-3369. http://dx.doi.org/10.1093/nar/28.17.3361.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3361-3369
    • Smith, J.1    Bibikova, M.2    Whitby, F.G.3    Reddy, A.R.4    Chandrasegaran, S.5    Carroll, D.6
  • 80
    • 0027217224 scopus 로고
    • A novel terminase activity associated with the DNA packaging protein gp17 of bacteriophage T4
    • Bhattacharyya SP, Rao VB. 1993. A novel terminase activity associated with the DNA packaging protein gp17 of bacteriophage T4. Virology 196: 34-44. http://dx.doi.org/10.1006/viro.1993.1452.
    • (1993) Virology , vol.196 , pp. 34-44
    • Bhattacharyya, S.P.1    Rao, V.B.2
  • 81
    • 0019751751 scopus 로고
    • Interactions between the maturation protein gp17 and the single-stranded DNA binding protein gp32 initiate DNA packaging and compete with initiation of secondary DNA replication forks in phage T4
    • Mosig G, Ghosal D, Bock S. 1981. Interactions between the maturation protein gp17 and the single-stranded DNA binding protein gp32 initiate DNA packaging and compete with initiation of secondary DNA replication forks in phage T4. Prog. Clin. Biol. Res. 64:139-150.
    • (1981) Prog. Clin. Biol. Res. , vol.64 , pp. 139-150
    • Mosig, G.1    Ghosal, D.2    Bock, S.3
  • 83
    • 34249946267 scopus 로고    scopus 로고
    • Putative terminase subunits of herpes simplex virus 1 form a complex in the cytoplasm and interact with portal protein in the nucleus
    • Yang K, Homa F, Baines JD. 2007. Putative terminase subunits of herpes simplex virus 1 form a complex in the cytoplasm and interact with portal protein in the nucleus. J. Virol. 81:6419-6433. http://dx.doi.org/10.1128/JVI.00047-07.
    • (2007) J. Virol. , vol.81 , pp. 6419-6433
    • Yang, K.1    Homa, F.2    Baines, J.D.3
  • 84
    • 0033828844 scopus 로고    scopus 로고
    • The potential terminase subunit of human cytomegalovirus, pUL56, is translocated into the nucleus by its own nuclear localization signal and interacts with importin β
    • Giesen K, Radsak K, Bogner E. 2000. The potential terminase subunit of human cytomegalovirus, pUL56, is translocated into the nucleus by its own nuclear localization signal and interacts with importin β. J. Gen. Virol. 81:2231-2244.
    • (2000) J. Gen. Virol. , vol.81 , pp. 2231-2244
    • Giesen, K.1    Radsak, K.2    Bogner, E.3
  • 85
    • 0042389525 scopus 로고    scopus 로고
    • Point mutations in exon I of the herpes simplex virus putative terminase subunit, UL15, indicate that the most conserved residues are essential for cleavage and packaging
    • Przech AJ, Yu D, Weller SK. 2003. Point mutations in exon I of the herpes simplex virus putative terminase subunit, UL15, indicate that the most conserved residues are essential for cleavage and packaging. J. Virol. 77: 9613-9621. http://dx.doi.org/10.1128/JVI.77.17.9613-9621.2003.
    • (2003) J. Virol. , vol.77 , pp. 9613-9621
    • Przech, A.J.1    Yu, D.2    Weller, S.K.3
  • 86
    • 0017195384 scopus 로고
    • Differential effect of phosphonoacetic acid on the expression of Epstein-Barr viral antigens and virus production
    • Nyormoi O, Thorley-Lawson DA, Elkington J, Strominger JL. 1976. Differential effect of phosphonoacetic acid on the expression of Epstein-Barr viral antigens and virus production. Proc. Natl. Acad. Sci. U. S. A. 73:1745-1748. http://dx.doi.org/10.1073/pnas.73.5.1745.
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 1745-1748
    • Nyormoi, O.1    Thorley-Lawson, D.A.2    Elkington, J.3    Strominger, J.L.4
  • 87
    • 0017265399 scopus 로고
    • Inhibition of Epstein-Barr virus DNA synthesis and late gene expression by phosphonoacetic acid
    • Summers WC, Klein G. 1976. Inhibition of Epstein-Barr virus DNA synthesis and late gene expression by phosphonoacetic acid. J. Virol. 18: 151-155.
    • (1976) J. Virol. , vol.18 , pp. 151-155
    • Summers, W.C.1    Klein, G.2
  • 88
    • 0025902185 scopus 로고
    • Characterization of two monoclonal antibodies to Epstein-Barr virus diffuse early antigen which react to two different epitopes and have different biological function
    • Tsai CH, Williams MV, Glaser R. 1991. Characterization of two monoclonal antibodies to Epstein-Barr virus diffuse early antigen which react to two different epitopes and have different biological function. J. Virol. Methods 33:47-52.
    • (1991) J. Virol. Methods , vol.33 , pp. 47-52
    • Tsai, C.H.1    Williams, M.V.2    Glaser, R.3
  • 89
    • 33745244290 scopus 로고    scopus 로고
    • Herpes simplex virus capsid structure: DNA packaging protein UL25 is located on the external surface of the capsid near the vertices
    • Newcomb WW, Homa FL, Brown JC. 2006. Herpes simplex virus capsid structure: DNA packaging protein UL25 is located on the external surface of the capsid near the vertices. J. Virol. 80:6286-6294. http://dx.doi.org/10.1128/JVI.02648-05.
    • (2006) J. Virol. , vol.80 , pp. 6286-6294
    • Newcomb, W.W.1    Homa, F.L.2    Brown, J.C.3
  • 90
    • 34548158174 scopus 로고    scopus 로고
    • A putative leucine zipper within the herpes simplex virus type 1 UL6 protein is required for portal ring formation
    • Nellissery JK, Szczepaniak R, Lamberti C, Weller SK. 2007. A putative leucine zipper within the herpes simplex virus type 1 UL6 protein is required for portal ring formation. J. Virol. 81:8868-8877. http://dx.doi.org/10.1128/JVI.00739-07.
    • (2007) J. Virol. , vol.81 , pp. 8868-8877
    • Nellissery, J.K.1    Szczepaniak, R.2    Lamberti, C.3    Weller, S.K.4


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