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Volumn 11, Issue 5, 2015, Pages

Selective Recruitment of Nuclear Factors to Productively Replicating Herpes Simplex Virus Genomes

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; CYCLIN C; CYCLIN DEPENDENT KINASE 7; CYCLIN DEPENDENT KINASE 8; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; DNA TOPOISOMERASE; FACILITATES CHROMATIN TRANSCRIPTION; HISTONE DEACETYLASE; INFECTED CELL POLYPEPTIDE 4; INFECTED CELL PROTEIN 8; MINICHROMOSOME MAINTENANCE PROTEIN 2; MINICHROMOSOME MAINTENANCE PROTEIN 3; MINICHROMOSOME MAINTENANCE PROTEIN 4; MINICHROMOSOME MAINTENANCE PROTEIN 5; MINICHROMOSOME MAINTENANCE PROTEIN 6; MINICHROMOSOME MAINTENANCE PROTEIN 7; NUCLEAR FACTOR; PROTEIN SERINE THREONINE KINASE; PROTEIN UL30; PROTEIN UL5; PROTEIN UL52; PROTEIN UL8; PROTEIN UL9; RNA POLYMERASE II; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR IID; TRANSCRIPTION FACTOR IIH; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; UNINDEXED DRUG; URACIL DNA GLYCOSIDASE; MESSENGER RNA; NUCLEAR PROTEIN; VIRAL PROTEIN;

EID: 84930346957     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004939     Document Type: Article
Times cited : (90)

References (88)
  • 1
    • 0023899276 scopus 로고
    • The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1
    • McGeoch DJ, Dalrymple MA, Davison AJ, Dolan A, Frame MC, et al. (1988) The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. J Gen Virol 69: 1531–1574. 2839594
    • (1988) J Gen Virol , vol.69 , pp. 1531-1574
    • McGeoch, D.J.1    Dalrymple, M.A.2    Davison, A.J.3    Dolan, A.4    Frame, M.C.5
  • 2
    • 0023056480 scopus 로고
    • Complete DNA sequence of the short repeat region in the genome of herpes simplex virus type 1
    • McGeoch DJ, Dolan A, Donald S, Brauer DH, (1986) Complete DNA sequence of the short repeat region in the genome of herpes simplex virus type 1. Nucleic Acids Res 14: 1727–1745. 3005980
    • (1986) Nucleic Acids Res , vol.14 , pp. 1727-1745
    • McGeoch, D.J.1    Dolan, A.2    Donald, S.3    Brauer, D.H.4
  • 3
    • 0020701819 scopus 로고
    • Molecular genetics of herpes simplex virus. VIII. further characterization of a temperature-sensitive mutant defective in release of viral DNA and in other stages of the viral reproductive cycle
    • Batterson W, Furlong D, Roizman B, (1983) Molecular genetics of herpes simplex virus. VIII. further characterization of a temperature-sensitive mutant defective in release of viral DNA and in other stages of the viral reproductive cycle. J Virol 45: 397–407. 6296445
    • (1983) J Virol , vol.45 , pp. 397-407
    • Batterson, W.1    Furlong, D.2    Roizman, B.3
  • 4
    • 0034091334 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro
    • Ojala PM, Sodeik B, Ebersold MW, Kutay U, Helenius A, (2000) Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro. Mol Cell Biol 20: 4922–4931. 10848617
    • (2000) Mol Cell Biol , vol.20 , pp. 4922-4931
    • Ojala, P.M.1    Sodeik, B.2    Ebersold, M.W.3    Kutay, U.4    Helenius, A.5
  • 5
    • 31644431670 scopus 로고    scopus 로고
    • The genome of HSV-1 translocates through the nuclear pore as a condensed rod-like structure
    • Shahin V, Hafezi W, Oberleithner H, Ludwig Y, Windoffer B, et al. (2006) The genome of HSV-1 translocates through the nuclear pore as a condensed rod-like structure. J Cell Sci 119: 23–30. 16339172
    • (2006) J Cell Sci , vol.119 , pp. 23-30
    • Shahin, V.1    Hafezi, W.2    Oberleithner, H.3    Ludwig, Y.4    Windoffer, B.5
  • 6
    • 0032143446 scopus 로고    scopus 로고
    • Nuclear domain 10, the site of DNA virus transcription and replication
    • Maul GG, (1998) Nuclear domain 10, the site of DNA virus transcription and replication. Bioessays 20: 660–667. 9780840
    • (1998) Bioessays , vol.20 , pp. 660-667
    • Maul, G.G.1
  • 7
    • 84921957488 scopus 로고    scopus 로고
    • Structure of the herpes simplex virus 1 genome: manipulation of nicks and gaps can abrogate infectivity and alter the cellular DNA damage response
    • Smith S, Reuven N, Mohni KN, Schumacher AJ, Weller SK, (2014) Structure of the herpes simplex virus 1 genome: manipulation of nicks and gaps can abrogate infectivity and alter the cellular DNA damage response. J Virol 88: 10146–10156. doi: 10.1128/JVI.01723-14 24965466
    • (2014) J Virol , vol.88 , pp. 10146-10156
    • Smith, S.1    Reuven, N.2    Mohni, K.N.3    Schumacher, A.J.4    Weller, S.K.5
  • 8
    • 0035969103 scopus 로고    scopus 로고
    • DNA viruses and viral proteins that interact with PML nuclear bodies
    • Everett RD, (2001) DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 20: 7266–7273. 11704855
    • (2001) Oncogene , vol.20 , pp. 7266-7273
    • Everett, R.D.1
  • 9
    • 0037903355 scopus 로고    scopus 로고
    • Herpes simplex virus replication compartments can form by coalescence of smaller compartments
    • Taylor TJ, McNamee EE, Day C, Knipe DM, (2003) Herpes simplex virus replication compartments can form by coalescence of smaller compartments. Virology 309: 232–247. 12758171
    • (2003) Virology , vol.309 , pp. 232-247
    • Taylor, T.J.1    McNamee, E.E.2    Day, C.3    Knipe, D.M.4
  • 10
    • 0020615188 scopus 로고
    • Characterization of the herpes simplex virion-associated factor responsible for the induction of alpha genes
    • Batterson W, Roizman B, (1983) Characterization of the herpes simplex virion-associated factor responsible for the induction of alpha genes. J Virol 46: 371–377. 6302308
    • (1983) J Virol , vol.46 , pp. 371-377
    • Batterson, W.1    Roizman, B.2
  • 11
    • 0021659654 scopus 로고
    • Identification of herpes simplex virus DNA sequences which encode a trans-acting polypeptide responsible for stimulation of immediate early transcription
    • Campbell ME, Palfreyman JW, Preston CM, (1984) Identification of herpes simplex virus DNA sequences which encode a trans-acting polypeptide responsible for stimulation of immediate early transcription. J Mol Biol 180: 1–19. 6096556
    • (1984) J Mol Biol , vol.180 , pp. 1-19
    • Campbell, M.E.1    Palfreyman, J.W.2    Preston, C.M.3
  • 12
    • 0019190731 scopus 로고
    • A herpes simplex virus type 1 function continuously required for early and late virus RNA synthesis
    • Watson RJ, Clements JB, (1980) A herpes simplex virus type 1 function continuously required for early and late virus RNA synthesis. Nature 285: 329–330. 6246451
    • (1980) Nature , vol.285 , pp. 329-330
    • Watson, R.J.1    Clements, J.B.2
  • 13
    • 0016156837 scopus 로고
    • Transcription of herpes simplex type 1 DNA in nuclei isolated from infected HEp-2 and KB cells
    • Alwine JC, Steinhart WL, Hill CW, (1974) Transcription of herpes simplex type 1 DNA in nuclei isolated from infected HEp-2 and KB cells. Virology 60: 302–307. 4366499
    • (1974) Virology , vol.60 , pp. 302-307
    • Alwine, J.C.1    Steinhart, W.L.2    Hill, C.W.3
  • 14
    • 0037333386 scopus 로고    scopus 로고
    • Recruitment of herpes simplex virus type 1 transcriptional regulatory protein ICP4 into foci juxtaposed to ND10 in live, infected cells
    • Everett RD, Sourvinos G, Orr A, (2003) Recruitment of herpes simplex virus type 1 transcriptional regulatory protein ICP4 into foci juxtaposed to ND10 in live, infected cells. J Virol 77: 3680–3689. 12610143
    • (2003) J Virol , vol.77 , pp. 3680-3689
    • Everett, R.D.1    Sourvinos, G.2    Orr, A.3
  • 15
    • 0842304512 scopus 로고    scopus 로고
    • Formation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexes
    • Everett RD, Sourvinos G, Leiper C, Clements JB, Orr A, (2004) Formation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexes. J Virol 78: 1903–1917. 14747555
    • (2004) J Virol , vol.78 , pp. 1903-1917
    • Everett, R.D.1    Sourvinos, G.2    Leiper, C.3    Clements, J.B.4    Orr, A.5
  • 16
    • 17044458937 scopus 로고    scopus 로고
    • Compartmentalization of VP16 in cells infected with recombinant herpes simplex virus expressing VP16-green fluorescent protein fusion proteins
    • La Boissiere S, Izeta A, Malcomber S, O'Hare P, (2004) Compartmentalization of VP16 in cells infected with recombinant herpes simplex virus expressing VP16-green fluorescent protein fusion proteins. J Virol 78: 8002–8014. 15254172
    • (2004) J Virol , vol.78 , pp. 8002-8014
    • La Boissiere, S.1    Izeta, A.2    Malcomber, S.3    O'Hare, P.4
  • 17
    • 0016162063 scopus 로고
    • Regulation of herpesvirus macromolecular synthesis. I. Cascade regulation of the synthesis of three groups of viral proteins
    • Honess RW, Roizman B, (1974) Regulation of herpesvirus macromolecular synthesis. I. Cascade regulation of the synthesis of three groups of viral proteins. J Virol 14: 8–19. 4365321
    • (1974) J Virol , vol.14 , pp. 8-19
    • Honess, R.W.1    Roizman, B.2
  • 18
    • 0342284520 scopus 로고
    • Regulation of herpesvirus macromolecular synthesis: sequential transition of polypeptide synthesis requires functional viral polypeptides
    • Honess RW, Roizman B, (1975) Regulation of herpesvirus macromolecular synthesis: sequential transition of polypeptide synthesis requires functional viral polypeptides. Proc Natl Acad Sci U S A 72: 1276–1280. 165503
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 1276-1280
    • Honess, R.W.1    Roizman, B.2
  • 19
    • 0022919477 scopus 로고
    • A method for identifying the viral genes required for herpesvirus DNA replication
    • Challberg MD, (1986) A method for identifying the viral genes required for herpesvirus DNA replication. Proc Natl Acad Sci U S A 83: 9094–9098. 3024166
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 9094-9098
    • Challberg, M.D.1
  • 20
    • 84866103520 scopus 로고    scopus 로고
    • Herpes simplex viruses: mechanisms of DNA replication
    • Weller SK, Coen DM, (2012) Herpes simplex viruses: mechanisms of DNA replication. Cold Spring Harb Perspect Biol 4: a013011. doi: 10.1101/cshperspect.a013011 22952399
    • (2012) Cold Spring Harb Perspect Biol , vol.4 , pp. 13011
    • Weller, S.K.1    Coen, D.M.2
  • 21
    • 84858240360 scopus 로고    scopus 로고
    • Procapsid assembly, maturation, nuclear exit: dynamic steps in the production of infectious herpesvirions
    • Cardone G, Heymann JB, Cheng N, Trus BL, Steven AC, (2012) Procapsid assembly, maturation, nuclear exit: dynamic steps in the production of infectious herpesvirions. Adv Exp Med Biol 726: 423–439. doi: 10.1007/978-1-4614-0980-9_19 22297525
    • (2012) Adv Exp Med Biol , vol.726 , pp. 423-439
    • Cardone, G.1    Heymann, J.B.2    Cheng, N.3    Trus, B.L.4    Steven, A.C.5
  • 22
    • 84885971731 scopus 로고    scopus 로고
    • Tracking viral genomes in host cells at single-molecule resolution
    • Wang IH, Suomalainen M, Andriasyan V, Kilcher S, Mercer J, et al. (2013) Tracking viral genomes in host cells at single-molecule resolution. Cell Host Microbe 14: 468–480. doi: 10.1016/j.chom.2013.09.004 24139403
    • (2013) Cell Host Microbe , vol.14 , pp. 468-480
    • Wang, I.H.1    Suomalainen, M.2    Andriasyan, V.3    Kilcher, S.4    Mercer, J.5
  • 23
    • 84887081781 scopus 로고    scopus 로고
    • Identification of proteins at active, stalled, and collapsed replication forks using isolation of proteins on nascent DNA (iPOND) coupled with mass spectrometry
    • Sirbu BM, McDonald WH, Dungrawala H, Badu-Nkansah A, Kavanaugh GM, et al. (2013) Identification of proteins at active, stalled, and collapsed replication forks using isolation of proteins on nascent DNA (iPOND) coupled with mass spectrometry. J Biol Chem 288: 31458–31467. doi: 10.1074/jbc.M113.511337 24047897
    • (2013) J Biol Chem , vol.288 , pp. 31458-31467
    • Sirbu, B.M.1    McDonald, W.H.2    Dungrawala, H.3    Badu-Nkansah, A.4    Kavanaugh, G.M.5
  • 24
    • 79959629469 scopus 로고    scopus 로고
    • Analysis of protein dynamics at active, stalled, and collapsed replication forks
    • Sirbu BM, Couch FB, Feigerle JT, Bhaskara S, Hiebert SW, et al. (2011) Analysis of protein dynamics at active, stalled, and collapsed replication forks. Genes Dev 25: 1320–1327. doi: 10.1101/gad.2053211 21685366
    • (2011) Genes Dev , vol.25 , pp. 1320-1327
    • Sirbu, B.M.1    Couch, F.B.2    Feigerle, J.T.3    Bhaskara, S.4    Hiebert, S.W.5
  • 25
    • 84861741887 scopus 로고    scopus 로고
    • Monitoring the spatiotemporal dynamics of proteins at replication forks and in assembled chromatin using isolation of proteins on nascent DNA
    • Sirbu BM, Couch FB, Cortez D, (2012) Monitoring the spatiotemporal dynamics of proteins at replication forks and in assembled chromatin using isolation of proteins on nascent DNA. Nat Protoc 7: 594–605. doi: 10.1038/nprot.2012.010 22383038
    • (2012) Nat Protoc , vol.7 , pp. 594-605
    • Sirbu, B.M.1    Couch, F.B.2    Cortez, D.3
  • 26
    • 84876955256 scopus 로고    scopus 로고
    • A proteomic characterization of factors enriched at nascent DNA molecules
    • Lopez-Contreras AJ, Ruppen I, Nieto-Soler M, Murga M, Rodriguez-Acebes S, et al. (2013) A proteomic characterization of factors enriched at nascent DNA molecules. Cell Rep 3: 1105–1116. doi: 10.1016/j.celrep.2013.03.009 23545495
    • (2013) Cell Rep , vol.3 , pp. 1105-1116
    • Lopez-Contreras, A.J.1    Ruppen, I.2    Nieto-Soler, M.3    Murga, M.4    Rodriguez-Acebes, S.5
  • 27
    • 84921718845 scopus 로고    scopus 로고
    • Purification of proteins on newly synthesized DNA using iPOND
    • Dungrawala H, Cortez D, (2015) Purification of proteins on newly synthesized DNA using iPOND. Methods Mol Biol 1228: 123–131. doi: 10.1007/978-1-4939-1680-1_10 25311126
    • (2015) Methods Mol Biol , vol.1228 , pp. 123-131
    • Dungrawala, H.1    Cortez, D.2
  • 28
    • 84903192816 scopus 로고    scopus 로고
    • Identification of a large protein network involved in epigenetic transmission in replicating DNA of embryonic stem cells
    • Aranda S, Rutishauser D, Ernfors P, (2014) Identification of a large protein network involved in epigenetic transmission in replicating DNA of embryonic stem cells. Nucleic Acids Res 42: 6972–6986. doi: 10.1093/nar/gku374 24852249
    • (2014) Nucleic Acids Res , vol.42 , pp. 6972-6986
    • Aranda, S.1    Rutishauser, D.2    Ernfors, P.3
  • 29
    • 35148893559 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 genomes are associated with ND10 nuclear substructures in quiescently infected human fibroblasts
    • Everett RD, Murray J, Orr A, Preston CM, (2007) Herpes simplex virus type 1 genomes are associated with ND10 nuclear substructures in quiescently infected human fibroblasts. J Virol 81: 10991–11004. 17670833
    • (2007) J Virol , vol.81 , pp. 10991-11004
    • Everett, R.D.1    Murray, J.2    Orr, A.3    Preston, C.M.4
  • 30
    • 0344995285 scopus 로고    scopus 로고
    • Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0
    • Hobbs WE, DeLuca NA, (1999) Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0. Journal of Virology 73: 8245–8255. 10482575
    • (1999) Journal of Virology , vol.73 , pp. 8245-8255
    • Hobbs, W.E.1    DeLuca, N.A.2
  • 31
    • 0032863957 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein Vmw110 inhibits progression of cells through mitosis and from G(1) into S phase of the cell cycle
    • Lomonte P, Everett RD, (1999) Herpes simplex virus type 1 immediate-early protein Vmw110 inhibits progression of cells through mitosis and from G(1) into S phase of the cell cycle. J Virol 73: 9456–9467. 10516054
    • (1999) J Virol , vol.73 , pp. 9456-9467
    • Lomonte, P.1    Everett, R.D.2
  • 32
    • 0032520689 scopus 로고    scopus 로고
    • Regulation of expression of nuclear and mitochondrial forms of human uracil-DNA glycosylase
    • Haug T, Skorpen F, Aas PA, Malm V, Skjelbred C, et al. (1998) Regulation of expression of nuclear and mitochondrial forms of human uracil-DNA glycosylase. Nucleic Acids Res 26: 1449–1457. 9490791
    • (1998) Nucleic Acids Res , vol.26 , pp. 1449-1457
    • Haug, T.1    Skorpen, F.2    Aas, P.A.3    Malm, V.4    Skjelbred, C.5
  • 33
    • 84885454866 scopus 로고    scopus 로고
    • A rapid and efficient method to purify proteins at replication forks under native conditions
    • Leung KH, Abou El Hassan M, Bremner R, (2013) A rapid and efficient method to purify proteins at replication forks under native conditions. Biotechniques 55: 204–206. doi: 10.2144/000114089 24107252
    • (2013) Biotechniques , vol.55 , pp. 204-206
    • Leung, K.H.1    Abou El Hassan, M.2    Bremner, R.3
  • 34
    • 84885393420 scopus 로고    scopus 로고
    • Temporal association of herpes simplex virus ICP4 with cellular complexes functioning at multiple steps in PolII transcription
    • Wagner LM, DeLuca NA, (2013) Temporal association of herpes simplex virus ICP4 with cellular complexes functioning at multiple steps in PolII transcription. PLoS One 8: e78242. doi: 10.1371/journal.pone.0078242 24147125
    • (2013) PLoS One , vol.8 , pp. 78242
    • Wagner, L.M.1    DeLuca, N.A.2
  • 35
    • 79958102996 scopus 로고    scopus 로고
    • Herpes simplex virus 1 ICP4 forms complexes with TFIID and mediator in virus-infected cells
    • Lester JT, DeLuca NA, (2011) Herpes simplex virus 1 ICP4 forms complexes with TFIID and mediator in virus-infected cells. J Virol 85: 5733–5744. doi: 10.1128/JVI.00385-11 21450820
    • (2011) J Virol , vol.85 , pp. 5733-5744
    • Lester, J.T.1    DeLuca, N.A.2
  • 36
    • 84881475940 scopus 로고    scopus 로고
    • The CRAPome: a contaminant repository for affinity purification-mass spectrometry data
    • Mellacheruvu D, Wright Z, Couzens AL, Lambert JP, St-Denis NA, et al. (2013) The CRAPome: a contaminant repository for affinity purification-mass spectrometry data. Nat Methods 10: 730–736. doi: 10.1038/nmeth.2557 23921808
    • (2013) Nat Methods , vol.10 , pp. 730-736
    • Mellacheruvu, D.1    Wright, Z.2    Couzens, A.L.3    Lambert, J.P.4    St-Denis, N.A.5
  • 37
    • 0019136475 scopus 로고
    • The structure of herpes simplex virus type 1 DNA as probed by micrococcal nuclease digestion
    • Leinbach SS, Summers WC, (1980) The structure of herpes simplex virus type 1 DNA as probed by micrococcal nuclease digestion. J Gen Virol 51: 45–59. 6257837
    • (1980) J Gen Virol , vol.51 , pp. 45-59
    • Leinbach, S.S.1    Summers, W.C.2
  • 38
    • 0018462188 scopus 로고
    • Random cleavage of intranuclear herpes simplex virus DNA by micrococcal nuclease
    • Mouttet ME, Guetard D, Bechet JM, (1979) Random cleavage of intranuclear herpes simplex virus DNA by micrococcal nuclease. FEBS Lett 100: 107–109. 220083
    • (1979) FEBS Lett , vol.100 , pp. 107-109
    • Mouttet, M.E.1    Guetard, D.2    Bechet, J.M.3
  • 39
    • 41149097014 scopus 로고    scopus 로고
    • Temporal association of the herpes simplex virus genome with histone proteins during a lytic infection
    • Oh J, Fraser NW, (2008) Temporal association of the herpes simplex virus genome with histone proteins during a lytic infection. J Virol 82: 3530–3537. 18160436
    • (2008) J Virol , vol.82 , pp. 3530-3537
    • Oh, J.1    Fraser, N.W.2
  • 40
    • 4444250828 scopus 로고    scopus 로고
    • During lytic infection herpes simplex virus type 1 is associated with histones bearing modifications that correlate with active transcription
    • Kent JR, Zeng PY, Atanasiu D, Gardner J, Fraser NW, et al. (2004) During lytic infection herpes simplex virus type 1 is associated with histones bearing modifications that correlate with active transcription. J Virol 78: 10178–10186. 15331750
    • (2004) J Virol , vol.78 , pp. 10178-10186
    • Kent, J.R.1    Zeng, P.Y.2    Atanasiu, D.3    Gardner, J.4    Fraser, N.W.5
  • 41
    • 33744921070 scopus 로고    scopus 로고
    • Trimethylation of histone H3 lysine 4 by Set1 in the lytic infection of human herpes simplex virus 1
    • Huang J, Kent JR, Placek B, Whelan KA, Hollow CM, et al. (2006) Trimethylation of histone H3 lysine 4 by Set1 in the lytic infection of human herpes simplex virus 1. J Virol 80: 5740–5746. 16731913
    • (2006) J Virol , vol.80 , pp. 5740-5746
    • Huang, J.1    Kent, J.R.2    Placek, B.3    Whelan, K.A.4    Hollow, C.M.5
  • 42
    • 0024555760 scopus 로고
    • During latency, herpes simplex virus type 1 DNA is associated with nucleosomes in a chromatin structure
    • Deshmane SL, Fraser NW, (1989) During latency, herpes simplex virus type 1 DNA is associated with nucleosomes in a chromatin structure. J Virol 63: 943–947. 2536115
    • (1989) J Virol , vol.63 , pp. 943-947
    • Deshmane, S.L.1    Fraser, N.W.2
  • 43
    • 78649491469 scopus 로고    scopus 로고
    • Dissecting the transcriptional functions of human DNA topoisomerase I by selective inhibitors: implications for physiological and therapeutic modulation of enzyme activity
    • Capranico G, Marinello J, Baranello L, (2010) Dissecting the transcriptional functions of human DNA topoisomerase I by selective inhibitors: implications for physiological and therapeutic modulation of enzyme activity. Biochim Biophys Acta 1806: 240–250. doi: 10.1016/j.bbcan.2010.06.003 20600630
    • (2010) Biochim Biophys Acta , vol.1806 , pp. 240-250
    • Capranico, G.1    Marinello, J.2    Baranello, L.3
  • 44
    • 0026062090 scopus 로고
    • Localization of p53, retinoblastoma and host replication proteins at sites of viral replication in herpes-infected cells
    • Wilcock D, Lane DP, (1991) Localization of p53, retinoblastoma and host replication proteins at sites of viral replication in herpes-infected cells. Nature 349: 429–431. 1671528
    • (1991) Nature , vol.349 , pp. 429-431
    • Wilcock, D.1    Lane, D.P.2
  • 45
    • 2442653990 scopus 로고    scopus 로고
    • Proteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8
    • Taylor TJ, Knipe DM, (2004) Proteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8. J Virol 78: 5856–5866. 15140983
    • (2004) J Virol , vol.78 , pp. 5856-5866
    • Taylor, T.J.1    Knipe, D.M.2
  • 47
    • 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, Tatsumi Y, Fujita M, et al. (2005) Activation of ataxia telangiectasia-mutated DNA damage checkpoint signal transduction elicited by herpes simplex virus infection. J Biol Chem 280: 30336–30341. 15964848
    • (2005) J Biol Chem , vol.280 , pp. 30336-30341
    • Shirata, N.1    Kudoh, A.2    Daikoku, T.3    Tatsumi, Y.4    Fujita, M.5
  • 48
    • 33847686708 scopus 로고    scopus 로고
    • Using or abusing: viruses and the cellular DNA damage response
    • Lilley CE, Schwartz RA, Weitzman MD, (2007) Using or abusing: viruses and the cellular DNA damage response. Trends Microbiol 15: 119–126. 17275307
    • (2007) Trends Microbiol , vol.15 , pp. 119-126
    • Lilley, C.E.1    Schwartz, R.A.2    Weitzman, M.D.3
  • 49
    • 77649338569 scopus 로고    scopus 로고
    • A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses
    • Lilley CE, Chaurushiya MS, Boutell C, Landry S, Suh J, et al. (2010) A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses. EMBO J 29: 943–955. doi: 10.1038/emboj.2009.400 20075863
    • (2010) EMBO J , vol.29 , pp. 943-955
    • Lilley, C.E.1    Chaurushiya, M.S.2    Boutell, C.3    Landry, S.4    Suh, J.5
  • 50
    • 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, (1999) 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: 650–657. 9847370
    • (1999) J Virol , vol.73 , pp. 650-657
    • Parkinson, J.1    Lees-Miller, S.P.2    Everett, R.D.3
  • 51
    • 79959848568 scopus 로고    scopus 로고
    • The intrinsic antiviral defense to incoming HSV-1 genomes includes specific DNA repair proteins and is counteracted by the viral protein ICP0
    • Lilley CE, Chaurushiya MS, Boutell C, Everett RD, Weitzman MD, (2011) The intrinsic antiviral defense to incoming HSV-1 genomes includes specific DNA repair proteins and is counteracted by the viral protein ICP0. PLoS Pathog 7: e1002084. doi: 10.1371/journal.ppat.1002084 21698222
    • (2011) PLoS Pathog , vol.7 , pp. 1002084
    • Lilley, C.E.1    Chaurushiya, M.S.2    Boutell, C.3    Everett, R.D.4    Weitzman, M.D.5
  • 52
    • 0142182192 scopus 로고    scopus 로고
    • The role of DNA recombination in herpes simplex virus DNA replication
    • Wilkinson DE, Weller SK, (2003) The role of DNA recombination in herpes simplex virus DNA replication. IUBMB Life 55: 451–458. 14609200
    • (2003) IUBMB Life , vol.55 , pp. 451-458
    • Wilkinson, D.E.1    Weller, S.K.2
  • 53
    • 84866057096 scopus 로고    scopus 로고
    • The HSV-1 exonuclease, UL12, stimulates recombination by a single strand annealing mechanism
    • Schumacher AJ, Mohni KN, Kan Y, Hendrickson EA, Stark JM, et al. (2012) The HSV-1 exonuclease, UL12, stimulates recombination by a single strand annealing mechanism. PLoS Pathog 8: e1002862. doi: 10.1371/journal.ppat.1002862 22912580
    • (2012) PLoS Pathog , vol.8 , pp. 1002862
    • Schumacher, A.J.1    Mohni, K.N.2    Kan, Y.3    Hendrickson, E.A.4    Stark, J.M.5
  • 54
    • 78649441078 scopus 로고    scopus 로고
    • Physical interaction between the herpes simplex virus type 1 exonuclease, UL12, and the DNA double-strand break-sensing MRN complex
    • Balasubramanian N, Bai P, Buchek G, Korza G, Weller SK, (2010) Physical interaction between the herpes simplex virus type 1 exonuclease, UL12, and the DNA double-strand break-sensing MRN complex. J Virol 84: 12504–12514. doi: 10.1128/JVI.01506-10 20943970
    • (2010) J Virol , vol.84 , pp. 12504-12514
    • Balasubramanian, N.1    Bai, P.2    Buchek, G.3    Korza, G.4    Weller, S.K.5
  • 55
    • 20544465434 scopus 로고    scopus 로고
    • SMC proteins and chromosome mechanics: from bacteria to humans
    • Hirano T, (2005) SMC proteins and chromosome mechanics: from bacteria to humans. Philos Trans R Soc Lond B Biol Sci 360: 507–514. 15897176
    • (2005) Philos Trans R Soc Lond B Biol Sci , vol.360 , pp. 507-514
    • Hirano, T.1
  • 56
    • 84880696794 scopus 로고    scopus 로고
    • Cohesin: functions beyond sister chromatid cohesion
    • Mehta GD, Kumar R, Srivastava S, Ghosh SK, (2013) Cohesin: functions beyond sister chromatid cohesion. FEBS Lett 587: 2299–2312. doi: 10.1016/j.febslet.2013.06.035 23831059
    • (2013) FEBS Lett , vol.587 , pp. 2299-2312
    • Mehta, G.D.1    Kumar, R.2    Srivastava, S.3    Ghosh, S.K.4
  • 57
    • 84892474330 scopus 로고    scopus 로고
    • Epigenetic deregulation of the LMP1/LMP2 locus of Epstein-Barr virus by mutation of a single CTCF-cohesin binding site
    • Chen HS, Martin KA, Lu F, Lupey LN, Mueller JM, et al. (2014) Epigenetic deregulation of the LMP1/LMP2 locus of Epstein-Barr virus by mutation of a single CTCF-cohesin binding site. J Virol 88: 1703–1713. doi: 10.1128/JVI.02209-13 24257606
    • (2014) J Virol , vol.88 , pp. 1703-1713
    • Chen, H.S.1    Martin, K.A.2    Lu, F.3    Lupey, L.N.4    Mueller, J.M.5
  • 58
    • 79956191128 scopus 로고    scopus 로고
    • Occupancy of chromatin organizers in the Epstein-Barr virus genome
    • Holdorf MM, Cooper SB, Yamamoto KR, Miranda JJ, (2011) Occupancy of chromatin organizers in the Epstein-Barr virus genome. Virology 415: 1–5. doi: 10.1016/j.virol.2011.04.004 21550623
    • (2011) Virology , vol.415 , pp. 1-5
    • Holdorf, M.M.1    Cooper, S.B.2    Yamamoto, K.R.3    Miranda, J.J.4
  • 59
    • 81255164924 scopus 로고    scopus 로고
    • DNA mismatch repair proteins are required for efficient herpes simplex virus 1 replication
    • Mohni KN, Mastrocola AS, Bai P, Weller SK, Heinen CD, (2011) DNA mismatch repair proteins are required for efficient herpes simplex virus 1 replication. J Virol 85: 12241–12253. doi: 10.1128/JVI.05487-11 21957315
    • (2011) J Virol , vol.85 , pp. 12241-12253
    • Mohni, K.N.1    Mastrocola, A.S.2    Bai, P.3    Weller, S.K.4    Heinen, C.D.5
  • 60
    • 0024520122 scopus 로고
    • Gene UL2 of herpes simplex virus type 1 encodes a uracil-DNA glycosylase
    • Mullaney J, Moss HW, McGeoch DJ, (1989) Gene UL2 of herpes simplex virus type 1 encodes a uracil-DNA glycosylase. J Gen Virol 70 (Pt 2): 449–454. 2567340
    • (1989) J Gen Virol , vol.70 , pp. 449-454
    • Mullaney, J.1    Moss, H.W.2    McGeoch, D.J.3
  • 61
    • 81255208061 scopus 로고    scopus 로고
    • The many roles of the highly interactive HSV protein ICP27, a key regulator of infection
    • Sandri-Goldin RM, (2011) The many roles of the highly interactive HSV protein ICP27, a key regulator of infection. Future Microbiol 6: 1261–1277. doi: 10.2217/fmb.11.119 22082288
    • (2011) Future Microbiol , vol.6 , pp. 1261-1277
    • Sandri-Goldin, R.M.1
  • 62
    • 15244351309 scopus 로고    scopus 로고
    • ICP27 recruits Aly/REF but not TAP/NXF1 to herpes simplex virus type 1 transcription sites although TAP/NXF1 is required for ICP27 export
    • Chen IH, Li L, Silva L, Sandri-Goldin RM, (2005) ICP27 recruits Aly/REF but not TAP/NXF1 to herpes simplex virus type 1 transcription sites although TAP/NXF1 is required for ICP27 export. J Virol 79: 3949–3961. 15767397
    • (2005) J Virol , vol.79 , pp. 3949-3961
    • Chen, I.H.1    Li, L.2    Silva, L.3    Sandri-Goldin, R.M.4
  • 63
    • 0036892520 scopus 로고    scopus 로고
    • ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway
    • Chen IH, Sciabica KS, Sandri-Goldin RM, (2002) ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway. J Virol 76: 12877–12889. 12438613
    • (2002) J Virol , vol.76 , pp. 12877-12889
    • Chen, I.H.1    Sciabica, K.S.2    Sandri-Goldin, R.M.3
  • 64
    • 55449092922 scopus 로고    scopus 로고
    • Recruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intronless mRNA nuclear export and virus replication
    • Boyne JR, Colgan KJ, Whitehouse A, (2008) Recruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intronless mRNA nuclear export and virus replication. PLoS Pathog 4: e1000194. doi: 10.1371/journal.ppat.1000194 18974867
    • (2008) PLoS Pathog , vol.4 , pp. 1000194
    • Boyne, J.R.1    Colgan, K.J.2    Whitehouse, A.3
  • 65
    • 84860725581 scopus 로고    scopus 로고
    • Functional coupling of transcription and splicing
    • Montes M, Becerra S, Sanchez-Alvarez M, Sune C, (2012) Functional coupling of transcription and splicing. Gene 501: 104–117. doi: 10.1016/j.gene.2012.04.006 22537677
    • (2012) Gene , vol.501 , pp. 104-117
    • Montes, M.1    Becerra, S.2    Sanchez-Alvarez, M.3    Sune, C.4
  • 66
    • 44649196386 scopus 로고    scopus 로고
    • Functional integration of transcriptional and RNA processing machineries
    • Pandit S, Wang D, Fu XD, (2008) Functional integration of transcriptional and RNA processing machineries. Curr Opin Cell Biol 20: 260–265. doi: 10.1016/j.ceb.2008.03.001 18436438
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 260-265
    • Pandit, S.1    Wang, D.2    Fu, X.D.3
  • 67
    • 46449087802 scopus 로고    scopus 로고
    • Biogenesis of mRNPs: integrating different processes in the eukaryotic nucleus
    • Luna R, Gaillard H, Gonzalez-Aguilera C, Aguilera A, (2008) Biogenesis of mRNPs: integrating different processes in the eukaryotic nucleus. Chromosoma 117: 319–331. doi: 10.1007/s00412-008-0158-4 18427828
    • (2008) Chromosoma , vol.117 , pp. 319-331
    • Luna, R.1    Gaillard, H.2    Gonzalez-Aguilera, C.3    Aguilera, A.4
  • 69
    • 28144460300 scopus 로고    scopus 로고
    • A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex
    • Jin J, Cai Y, Yao T, Gottschalk AJ, Florens L, et al. (2005) A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex. J Biol Chem 280: 41207–41212. 16230350
    • (2005) J Biol Chem , vol.280 , pp. 41207-41212
    • Jin, J.1    Cai, Y.2    Yao, T.3    Gottschalk, A.J.4    Florens, L.5
  • 70
    • 0032578762 scopus 로고    scopus 로고
    • Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex
    • Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL, (1998) Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex. Nature 395: 917–921. 9804427
    • (1998) Nature , vol.395 , pp. 917-921
    • Tong, J.K.1    Hassig, C.A.2    Schnitzler, G.R.3    Kingston, R.E.4    Schreiber, S.L.5
  • 71
    • 85023631515 scopus 로고    scopus 로고
    • HMGA proteins as modulators of chromatin structure during transcriptional activation
    • Ozturk N, Singh I, Mehta A, Braun T, Barreto G, (2014) HMGA proteins as modulators of chromatin structure during transcriptional activation. Front Cell Dev Biol 2: 5. doi: 10.3389/fcell.2014.00005 25364713
    • (2014) Front Cell Dev Biol , vol.2 , pp. 5
    • Ozturk, N.1    Singh, I.2    Mehta, A.3    Braun, T.4    Barreto, G.5
  • 72
    • 36849066365 scopus 로고    scopus 로고
    • A YY1-INO80 complex regulates genomic stability through homologous recombination-based repair
    • Wu S, Shi Y, Mulligan P, Gay F, Landry J, et al. (2007) A YY1-INO80 complex regulates genomic stability through homologous recombination-based repair. Nat Struct Mol Biol 14: 1165–1172. 18026119
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1165-1172
    • Wu, S.1    Shi, Y.2    Mulligan, P.3    Gay, F.4    Landry, J.5
  • 73
    • 84894048601 scopus 로고    scopus 로고
    • Histone chaperone FACT regulates homologous recombination by chromatin remodeling through interaction with RNF20
    • Oliveira DV, Kato A, Nakamura K, Ikura T, Okada M, et al. (2014) Histone chaperone FACT regulates homologous recombination by chromatin remodeling through interaction with RNF20. J Cell Sci 127: 763–772. doi: 10.1242/jcs.135855 24357716
    • (2014) J Cell Sci , vol.127 , pp. 763-772
    • Oliveira, D.V.1    Kato, A.2    Nakamura, K.3    Ikura, T.4    Okada, M.5
  • 74
    • 0031947054 scopus 로고    scopus 로고
    • The high mobility group protein 1 is a coactivator of herpes simplex virus ICP4 in vitro
    • Carrozza MJ, DeLuca N, (1998) The high mobility group protein 1 is a coactivator of herpes simplex virus ICP4 in vitro. J Virol 72: 6752–6757. 9658123
    • (1998) J Virol , vol.72 , pp. 6752-6757
    • Carrozza, M.J.1    DeLuca, N.2
  • 75
    • 0043244876 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage
    • Kettenberger H, Armache KJ, Cramer P, (2003) Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage. Cell 114: 347–357. 12914699
    • (2003) Cell , vol.114 , pp. 347-357
    • Kettenberger, H.1    Armache, K.J.2    Cramer, P.3
  • 76
    • 84887161037 scopus 로고    scopus 로고
    • Control of transcriptional elongation
    • Kwak H, Lis JT, (2013) Control of transcriptional elongation. Annu Rev Genet 47: 483–508. doi: 10.1146/annurev-genet-110711-155440 24050178
    • (2013) Annu Rev Genet , vol.47 , pp. 483-508
    • Kwak, H.1    Lis, J.T.2
  • 77
    • 84922281026 scopus 로고    scopus 로고
    • TRIM28 regulates RNA polymerase II promoter-proximal pausing and pause release
    • Bunch H, Zheng X, Burkholder A, Dillon ST, Motola S, et al. (2014) TRIM28 regulates RNA polymerase II promoter-proximal pausing and pause release. Nat Struct Mol Biol 21: 876–883. doi: 10.1038/nsmb.2878 25173174
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 876-883
    • Bunch, H.1    Zheng, X.2    Burkholder, A.3    Dillon, S.T.4    Motola, S.5
  • 78
    • 0025996912 scopus 로고
    • Cooperative interaction of an initiator-binding transcription initiation factor and the helix-loop-helix activator USF
    • Roy AL, Meisterernst M, Pognonec P, Roeder RG, (1991) Cooperative interaction of an initiator-binding transcription initiation factor and the helix-loop-helix activator USF. Nature 354: 245–248. 1961251
    • (1991) Nature , vol.354 , pp. 245-248
    • Roy, A.L.1    Meisterernst, M.2    Pognonec, P.3    Roeder, R.G.4
  • 79
    • 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, (1997) 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: 1133–1139. 8995634
    • (1997) J Virol , vol.71 , pp. 1133-1139
    • Leopardi, R.1    Ward, P.L.2    Ogle, W.O.3    Roizman, B.4
  • 80
    • 77249089491 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 infected cell protein 22
    • Lin FS, Ding Q, Guo H, Zheng AC, (2010) The herpes simplex virus type 1 infected cell protein 22. Virol Sin 25: 1–7. doi: 10.1007/s12250-010-3080-x 20960278
    • (2010) Virol Sin , vol.25 , pp. 1-7
    • Lin, F.S.1    Ding, Q.2    Guo, H.3    Zheng, A.C.4
  • 81
    • 33745155714 scopus 로고    scopus 로고
    • Construction and characterization of bacterial artificial chromosomes containing HSV-1 strains 17 and KOS
    • Gierasch WW, Zimmerman DL, Ward SL, Vanheyningen TK, Romine JD, et al. (2006) Construction and characterization of bacterial artificial chromosomes containing HSV-1 strains 17 and KOS. J Virol Methods 135: 197–206. 16647145
    • (2006) J Virol Methods , vol.135 , pp. 197-206
    • Gierasch, W.W.1    Zimmerman, D.L.2    Ward, S.L.3    Vanheyningen, T.K.4    Romine, J.D.5
  • 82
    • 33645053126 scopus 로고    scopus 로고
    • Two-step red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli
    • Tischer BK, von Einem J, Kaufer B, Osterrieder N, (2006) Two-step red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli. Biotechniques 40: 191–197. 16526409
    • (2006) Biotechniques , vol.40 , pp. 191-197
    • Tischer, B.K.1    von Einem, J.2    Kaufer, B.3    Osterrieder, N.4
  • 83
    • 79955159135 scopus 로고    scopus 로고
    • En passant mutagenesis: a two step markerless red recombination system
    • Tischer BK, Smith GA, Osterrieder N, (2010) En passant mutagenesis: a two step markerless red recombination system. Methods Mol Biol 634: 421–430. doi: 10.1007/978-1-60761-652-8_30 20677001
    • (2010) Methods Mol Biol , vol.634 , pp. 421-430
    • Tischer, B.K.1    Smith, G.A.2    Osterrieder, N.3
  • 84
    • 0029143375 scopus 로고
    • Functional interactions between herpes simplex virus immediate-early proteins during infection: gene expression as a consequence of ICP27 and different domains of ICP4
    • Samaniego LA, Webb AL, DeLuca NA, (1995) Functional interactions between herpes simplex virus immediate-early proteins during infection: gene expression as a consequence of ICP27 and different domains of ICP4. J Virol 69: 5705–5715. 7637016
    • (1995) J Virol , vol.69 , pp. 5705-5715
    • Samaniego, L.A.1    Webb, A.L.2    DeLuca, N.A.3
  • 85
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern EM, (1975) Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol 98: 503–517. 1195397
    • (1975) J Mol Biol , vol.98 , pp. 503-517
    • Southern, E.M.1
  • 86
    • 84863998594 scopus 로고    scopus 로고
    • The N terminus and C terminus of herpes simplex virus 1 ICP4 cooperate to activate viral gene expression
    • Wagner LM, Lester JT, Sivrich FL, DeLuca NA, (2012) The N terminus and C terminus of herpes simplex virus 1 ICP4 cooperate to activate viral gene expression. J Virol 86: 6862–6874. doi: 10.1128/JVI.00651-12 22496239
    • (2012) J Virol , vol.86 , pp. 6862-6874
    • Wagner, L.M.1    Lester, J.T.2    Sivrich, F.L.3    DeLuca, N.A.4
  • 87
    • 84858022403 scopus 로고    scopus 로고
    • Quantitative proteomic and genetic analyses of the schizophrenia susceptibility factor dysbindin identify novel roles of the biogenesis of lysosome-related organelles complex 1
    • Gokhale A, Larimore J, Werner E, So L, Moreno-De-Luca A, et al. (2012) Quantitative proteomic and genetic analyses of the schizophrenia susceptibility factor dysbindin identify novel roles of the biogenesis of lysosome-related organelles complex 1. J Neurosci 32: 3697–3711. doi: 10.1523/JNEUROSCI.5640-11.2012 22423091
    • (2012) J Neurosci , vol.32 , pp. 3697-3711
    • Gokhale, A.1    Larimore, J.2    Werner, E.3    So, L.4    Moreno-De-Luca, A.5
  • 88
    • 84901309807 scopus 로고    scopus 로고
    • Transcription of the herpes simplex virus 1 genome during productive and quiescent infection of neuronal and nonneuronal cells
    • Harkness JM, Kader M, DeLuca NA, (2014) Transcription of the herpes simplex virus 1 genome during productive and quiescent infection of neuronal and nonneuronal cells. J Virol 88: 6847–6861. doi: 10.1128/JVI.00516-14 24719411
    • (2014) J Virol , vol.88 , pp. 6847-6861
    • Harkness, J.M.1    Kader, M.2    DeLuca, N.A.3


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