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Volumn 83, Issue 13, 2009, Pages 6641-6651

Homologous recombinational repair factors are recruited and loaded onto the viral DNA genome in Epstein-Barr virus replication compartments

Author keywords

[No Author keywords available]

Indexed keywords

ATM PROTEIN; BROXURIDINE; DNA NUCLEOTIDYLEXOTRANSFERASE; MRE11 PROTEIN; NIBRIN; RAD50 PROTEIN; RAD51 PROTEIN; RAD52 PROTEIN; REPLICATION FACTOR A; REPLICATION PROTEIN A 32; UNCLASSIFIED DRUG; VIRUS DNA; DNA BINDING PROTEIN; MRE11A PROTEIN, HUMAN; RAD51 PROTEIN, HUMAN; RAD52 PROTEIN, HUMAN;

EID: 67449098555     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00049-09     Document Type: Article
Times cited : (70)

References (56)
  • 1
    • 11244269445 scopus 로고    scopus 로고
    • The CDK regulates repair of double-strand breaks by homologous recombination during the cell cycle
    • DOI 10.1038/sj.emboj.7600469
    • Aylon, Y., B. Liefshitz, and M. Kupiec. 2004. The CDK regulates repair of double-strand breaks by homologous recombination during the cell cycle. EMBO J. 23:4868-4875. (Pubitemid 40069716)
    • (2004) EMBO Journal , vol.23 , Issue.24 , pp. 4868-4875
    • Aylon, Y.1    Liefshitz, B.2    Kupiec, M.3
  • 2
    • 0017264404 scopus 로고
    • Concatemeric forms of intracellular herpesvirus DNA
    • Ben-Porat, T., A. S. Kaplan, B. Stehn, and A. S. Rubenstein. 1976. Concatemeric forms of intracellular herpesvirus DNA. Virology 69:547-560.
    • (1976) Virology , vol.69 , pp. 547-560
    • Ben-Porat, T.1    Kaplan, A.S.2    Stehn, B.3    Rubenstein, A.S.4
  • 3
    • 0032556865 scopus 로고    scopus 로고
    • Synergistic actions of Rad51 and Rad52 in recombination and DNA repair
    • DOI 10.1038/34937
    • Benson, F. E., P. Baumann, and S. C. West. 1998. Synergistic actions of Rad51 and Rad52 in recombination and DNA repair. Nature 391:401-404. (Pubitemid 28093516)
    • (1998) Nature , vol.391 , Issue.6665 , pp. 401-404
    • Benson, F.E.1    Baumann, P.2    West, S.C.3
  • 4
    • 3442896884 scopus 로고    scopus 로고
    • Replication Protein a phosphorylation and the cellular response to DNA damage
    • DOI 10.1016/j.dnarep.2004.03.028, PII S1568786404000874
    • Binz, S. K., A. M. Sheehan, and M. S. Wold. 2004. Replication protein A phosphorylation and the cellular response to DNA damage. DNA Repair (Amsterdam) 3:1015-1024. (Pubitemid 39004091)
    • (2004) DNA Repair , vol.3 , Issue.8-9 , pp. 1015-1024
    • Binz, S.K.1    Sheehan, A.M.2    Wold, M.S.3
  • 5
    • 1342302794 scopus 로고    scopus 로고
    • From RPA to BRCA2: Lessons from single-stranded DNA binding by the OB-fold
    • Bochkarev, A., and E. Bochkareva. 2004. From RPA to BRCA2: lessons from single-stranded DNA binding by the OB-fold. Curr. Opin. Struct. Biol. 14:36-42.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 36-42
    • Bochkarev, A.1    Bochkareva, E.2
  • 6
    • 0030848209 scopus 로고    scopus 로고
    • Role of protein-protein interactions in the function of replication protein a (RPA): RPA modulates the activity of DNA polymerase alpha by multiple mechanisms
    • DOI 10.1021/bi970473r
    • Braun, K. A., Y. Lao, Z. He, C. J. Ingles, and M. S. Wold. 1997. Role of protein-protein interactions in the function of replication protein A (RPA): RPA modulates the activity of DNA polymerase alpha by multiple mechanisms. Biochemistry 36:8443-8454. (Pubitemid 27305126)
    • (1997) Biochemistry , vol.36 , Issue.28 , pp. 8443-8454
    • Braun, K.A.1    Lao, Y.2    He, Z.3    Ingles, C.J.4    Wold, M.S.5
  • 7
    • 0034892653 scopus 로고    scopus 로고
    • Mre11 protein complex prevents double-strand break accumulation during chromosomal DNA replication
    • DOI 10.1016/S1097-2765(01)00294-5
    • Costanzo, V., K. Robertson, M. Bibikova, E. Kim, D. Grieco, M. Gottesman, D. Carroll, and J. Gautier. 2001. Mre11 protein complex prevents double-strand break accumulation during chromosomal DNA replication. Mol. Cell 8:137-147. (Pubitemid 32772912)
    • (2001) Molecular Cell , vol.8 , Issue.1 , pp. 137-147
    • Costanzo, V.1    Robertson, K.2    Bibikova, M.3    Kim, E.4    Grieco, D.5    Gottesman, M.6    Carroll, D.7    Gautier, J.8
  • 8
    • 14744274121 scopus 로고    scopus 로고
    • Architecture of replication compartments formed during Epstein-Barr virus lytic replication
    • DOI 10.1128/JVI.79.6.3409-3418.2005
    • Daikoku, T., A. Kudoh, M. Fujita, Y. Sugaya, H. Isomura, N. Shirata, and T. Tsurumi. 2005. Architecture of replication compartments formed during Epstein-Barr virus lytic replication. J. Virol. 79:3409-3418. (Pubitemid 40327929)
    • (2005) Journal of Virology , vol.79 , Issue.6 , pp. 3409-3418
    • Daikoku, T.1    Kudoh, A.2    Fujita, M.3    Sugaya, Y.4    Isomura, H.5    Shirata, N.6    Tsurumi, T.7
  • 9
    • 11144246925 scopus 로고    scopus 로고
    • In vivo dynamics of EBNA1-oriP interaction during latent and lytic replication of Epstein-Barr virus
    • Daikoku, T., A. Kudoh, M. Fujita, Y. Sugaya, H. Isomura, and T. Tsurumi. 2004. In vivo dynamics of EBNA1-oriP interaction during latent and lytic replication of Epstein-Barr virus. J. Biol. Chem. 279:54817-54825.
    • (2004) J. Biol. Chem. , vol.279 , pp. 54817-54825
    • Daikoku, T.1    Kudoh, A.2    Fujita, M.3    Sugaya, Y.4    Isomura, H.5    Tsurumi, T.6
  • 10
    • 33744957331 scopus 로고    scopus 로고
    • Postreplicative mismatch repair factors are recruited to Epstein-Barr virus replication compartments
    • Daikoku, T., A. Kudoh, Y. Sugaya, S. Iwahori, N. Shirata, H. Isomura, and T. Tsurumi. 2006. Postreplicative mismatch repair factors are recruited to Epstein-Barr virus replication compartments. J. Biol. Chem. 281:11422-11430.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11422-11430
    • Daikoku, T.1    Kudoh, A.2    Sugaya, Y.3    Iwahori, S.4    Shirata, N.5    Isomura, H.6    Tsurumi, T.7
  • 11
  • 12
    • 0034141739 scopus 로고    scopus 로고
    • Stability and nuclear distribution of mammalian replication protein A heterotrimeric complex
    • Dimitrova, D. S., and D. M. Gilbert. 2000. Stability and nuclear distribution of mammalian replication protein A heterotrimeric complex. Exp. Cell Res. 254:321-327.
    • (2000) Exp. Cell Res. , vol.254 , pp. 321-327
    • Dimitrova, D.S.1    Gilbert, D.M.2
  • 13
    • 0025365192 scopus 로고
    • Cell-cycle-regulated phosphorylation of DNA replication factor a from human and yeast cells
    • Din, S., S. J. Brill, M. P. Fairman, and B. Stillman. 1990. Cell-cycle-regulated phosphorylation of DNA replication factor A from human and yeast cells. Genes Dev. 4:968-977. (Pubitemid 20188972)
    • (1990) Genes and Development , vol.4 , Issue.6 , pp. 968-977
    • Din, S.1    Brill, S.J.2    Fairman, M.P.3    Stillman, B.4
  • 14
    • 0027358857 scopus 로고
    • Inhibition of DNA replication factor RPA by p53
    • DOI 10.1038/365079a0
    • Dutta, A., J. M. Ruppert, J. C. Aster, and E. Winchester. 1993. Inhibition of DNA replication factor RPA by p53. Nature 365:79-82. (Pubitemid 23305574)
    • (1993) Nature , vol.365 , Issue.6441 , pp. 79-82
    • Dutta, A.1    Ruppert, J.M.2    Aster, J.C.3    Winchester, E.4
  • 15
    • 0026539144 scopus 로고
    • Cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication
    • Dutta, A., and B. Stillman. 1992. cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication. EMBO J. 11:2189-2199.
    • (1992) EMBO J. , vol.11 , pp. 2189-2199
    • Dutta, A.1    Stillman, B.2
  • 16
    • 0025719722 scopus 로고
    • Efficient transcription of the Epstein-Barr virus immediate-early BZLF1 and BRLF1 genes requires protein synthesis
    • Flemington, E. K., A. E. Goldfeld, and S. H. Speck. 1991. Efficient transcription of the Epstein-Barr virus immediate-early BZLF1 and BRLF1 genes requires protein synthesis. J. Virol. 65:7073-7077.
    • (1991) J. Virol. , vol.65 , pp. 7073-7077
    • Flemington, E.K.1    Goldfeld, A.E.2    Speck, S.H.3
  • 17
    • 0038297562 scopus 로고    scopus 로고
    • The mammalian mismatch repair protein MSH2 is required for correct MRE11 and RAD51 relocalization and for efficient cell cycle arrest induced by ionizing radiation in G2 phase
    • DOI 10.1038/sj.onc.1206254
    • Franchitto, A., P. Pichierri, R. Piergentili, M. Crescenzi, M. Bignami, and F. Palitti. 2003. The mammalian mismatch repair protein MSH2 is required for correct MRE11 and RAD51 relocalization and for efficient cell cycle arrest induced by ionizing radiation in G2 phase. Oncogene 22:2110-2120. (Pubitemid 36539561)
    • (2003) Oncogene , vol.22 , Issue.14 , pp. 2110-2120
    • Franchitto, A.1    Pichierri, P.2    Piergentili, R.3    Crescenzi, M.4    Bignami, M.5    Palitti, F.6
  • 18
    • 0037155926 scopus 로고    scopus 로고
    • Nuclear organization of DNA replication initiation proteins in mammalian cells
    • Fujita, M., Y. Ishimi, H. Nakamura, T. Kiyono, and T. Tsurumi. 2002. Nuclear organization of DNA replication initiation proteins in mammalian cells. J. Biol. Chem. 277:10354-10361.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10354-10361
    • Fujita, M.1    Ishimi, Y.2    Nakamura, H.3    Kiyono, T.4    Tsurumi, T.5
  • 19
    • 0029670350 scopus 로고    scopus 로고
    • Inhibition of S-phase entry of human fibroblasts by an antisense oligomer against hCDC47
    • Fujita, M., T. Kiyono, Y. Hayashi, and M. Ishibashi. 1996. Inhibition of S-phase entry of human fibroblasts by an antisense oligomer against hCDC47. Biochem. Biophys. Res. Commun. 219:604-607.
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 604-607
    • Fujita, M.1    Kiyono, T.2    Hayashi, Y.3    Ishibashi, M.4
  • 20
    • 0033520321 scopus 로고    scopus 로고
    • Cell cycle regulation of human CDC6 protein. Intracellular localization, interaction with the human mcm complex, and CDC2 kinase-mediated hyperphosphorylation
    • Fujita, M., C. Yamada, H. Goto, N. Yokoyama, K. Kuzushima, M. Inagaki, and T. Tsurumi. 1999. Cell cycle regulation of human CDC6 protein. Intracellular localization, interaction with the human mcm complex, and CDC2 kinase-mediated hyperphosphorylation. J. Biol. Chem. 274:25927-25932.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25927-25932
    • Fujita, M.1    Yamada, C.2    Goto, H.3    Yokoyama, N.4    Kuzushima, K.5    Inagaki, M.6    Tsurumi, T.7
  • 21
    • 0032403121 scopus 로고    scopus 로고
    • Interaction of human Rad51 recombination protein with single-stranded DNA binding protein, RPA
    • Golub, E. I., R. C. Gupta, T. Haaf, M. S. Wold, and C. M. Radding. 1998. Interaction of human rad51 recombination protein with single-stranded DNA binding protein, RPA. Nucleic Acids Res. 26:5388-5393. (Pubitemid 28542739)
    • (1998) Nucleic Acids Research , vol.26 , Issue.23 , pp. 5388-5393
    • Golub, E.I.1    Gupta, R.C.2    Haaf, T.3    Wold, M.S.4    Radding, C.M.5
  • 22
    • 0029868656 scopus 로고    scopus 로고
    • Proteolytic mapping of human replication protein A: Evidence for multiple structural domains and a conformational change upon interaction with single- Stranded DNA
    • DOI 10.1021/bi9526995
    • Gomes, X. V., L. A. Henricksen, and M. S. Wold. 1996. Proteolytic mapping of human replication protein A: evidence for multiple structural domains and a conformational change upon interaction with single-stranded DNA. Biochemistry 35:5586-5595. (Pubitemid 26136536)
    • (1996) Biochemistry , vol.35 , Issue.17 , pp. 5586-5595
    • Gomes, X.V.1    Henricksen, L.A.2    Wold, M.S.3
  • 23
    • 33746855461 scopus 로고    scopus 로고
    • Regulation of replication protein A functions in DNA mismatch repair by phosphorylation
    • Guo, S., Y. Zhang, F. Yuan, Y. Gao, L. Gu, I. Wong, and G. M. Li. 2006. Regulation of replication protein A functions in DNA mismatch repair by phosphorylation. J. Biol. Chem. 281:21607-21616.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21607-21616
    • Guo, S.1    Zhang, Y.2    Yuan, F.3    Gao, Y.4    Gu, L.5    Wong, I.6    Li, G.M.7
  • 24
    • 0032567041 scopus 로고    scopus 로고
    • The many interfaces of Mre11
    • Haber, J. E. 1998. The many interfaces of Mre11. Cell 95:583-586. (Pubitemid 28544118)
    • (1998) Cell , vol.95 , Issue.5 , pp. 583-586
    • Haber, J.E.1
  • 25
    • 0027311843 scopus 로고
    • Visualization of replication factories attached to a nucleoskeleton
    • DOI 10.1016/0092-8674(93)90235-I
    • Hozak, P., A. B. Hassan, D. A. Jackson, and P. R. Cook. 1993. Visualization of replication factories attached to nucleoskeleton. Cell 73:361-373. (Pubitemid 23123313)
    • (1993) Cell , vol.73 , Issue.2 , pp. 361-373
    • Hozak, P.1    Hassan, A.B.2    Jackson, D.A.3    Cook, P.R.4
  • 26
    • 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
    • DOI 10.1128/JVI.00678-06
    • Kudoh, A., T. Daikoku, Y. Ishimi, Y. Kawaguchi, N. Shirata, S. Iwahori, H. Isomura, and T. Tsurumi. 2006. Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication. J. Virol. 80:10064-10072. (Pubitemid 44522600)
    • (2006) Journal of Virology , vol.80 , Issue.20 , pp. 10064-10072
    • Kudoh, A.1    Daikoku, T.2    Ishimi, Y.3    Kawaguchi, Y.4    Shirata, N.5    Iwahori, S.6    Isomura, H.7    Tsurumi, T.8
  • 27
    • 0346365302 scopus 로고    scopus 로고
    • Inhibition of S-Phase Cyclin-Dependent Kinase Activity Blocks Expression of Epstein-Barr Virus Immediate-Early and Early Genes, Preventing Viral Lytic Replication
    • DOI 10.1128/JVI.78.1.104-115.2004
    • Kudoh, A., T. Daikoku, Y. Sugaya, H. Isomura, M. Fujita, T. Kiyono, Y. Nishiyama, and T. Tsurumi. 2004. Inhibition of S-phase cyclin-dependent kinase activity blocks expression of Epstein-Barr virus immediate-early and early genes, preventing viral lytic replication. J. Virol. 78:104-115. (Pubitemid 37549723)
    • (2004) Journal of Virology , vol.78 , Issue.1 , pp. 104-115
    • Kudoh, A.1    Daikoku, T.2    Sugaya, Y.3    Isomura, H.4    Fujita, M.5    Kiyono, T.6    Nishiyama, Y.7    Tsurumi, T.8
  • 28
    • 0037219580 scopus 로고    scopus 로고
    • Reactivation of lytic replication from B cells latently infected with Epstein-Barr virus occurs with high S-phase cyclin-dependent kinase activity while inhibiting cellular DNA replication
    • DOI 10.1128/JVI.77.2.851-861.2003
    • Kudoh, A., M. Fujita, T. Kiyono, K. Kuzushima, Y. Sugaya, S. Izuta, Y. Nishiyama, and T. Tsurumi. 2003. Reactivation of lytic replication from B cells latently infected with Epstein-Barr virus occurs with high S-phase cyclin- dependent kinase activity while inhibiting cellular DNA replication. J. Virol. 77:851-861. (Pubitemid 36055507)
    • (2003) Journal of Virology , vol.77 , Issue.2 , pp. 851-861
    • Kudoh, A.1    Fujita, M.2    Kiyono, T.3    Kuzushima, K.4    Sugaya, Y.5    Izuta, S.6    Nishiyama, Y.7    Tsurumi, T.8
  • 29
    • 14844336913 scopus 로고    scopus 로고
    • Epstein-Barr virus lytic replication elicits ATM checkpoint signal transduction while providing an Sphase- like cellular environment
    • Kudoh, A., M. Fujita, L. Zhang, N. Shirata, T. Daikoku, Y. Sugaya, H. Isomura, Y. Nishiyama, and T. Tsurumi. 2005. Epstein-Barr virus lytic replication elicits ATM checkpoint signal transduction while providing an Sphase- like cellular environment. J. Biol. Chem. 280:8156-8163.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8156-8163
    • Kudoh, A.1    Fujita, M.2    Zhang, L.3    Shirata, N.4    Daikoku, T.5    Sugaya, Y.6    Isomura, H.7    Nishiyama, Y.8    Tsurumi, T.9
  • 30
    • 25444485251 scopus 로고    scopus 로고
    • Modulation of replication protein A function by its hyperphosphorylation- induced conformational change involving DNA binding domain B
    • Liu, Y., M. Kvaratskhelia, S. Hess, Y. Qu, and Y. Zou. 2005. Modulation of replication protein A function by its hyperphosphorylation-induced conformational change involving DNA binding domain B. J. Biol. Chem. 280:32775-32783.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32775-32783
    • Liu, Y.1    Kvaratskhelia, M.2    Hess, S.3    Qu, Y.4    Zou, Y.5
  • 31
    • 0029870883 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 alkaline nuclease is required for efficient processing of viral DNA replication intermediates
    • Martinez, R., R. T. Sarisky, P. C. Weber, and S. K. Weller. 1996. Herpes simplex virus type 1 alkaline nuclease is required for efficient processing of viral DNA replication intermediates. J. Virol. 70:2075-2085. (Pubitemid 26087564)
    • (1996) Journal of Virology , vol.70 , Issue.4 , pp. 2075-2085
    • Martinez, R.1    Sarisky, R.T.2    Weber, P.C.3    Weller, S.K.4
  • 32
    • 0032556870 scopus 로고    scopus 로고
    • Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein a
    • DOI 10.1038/34950
    • New, J. H., T. Sugiyama, E. Zaitseva, and S. C. Kowalczykowski. 1998. Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A. Nature 391:407-410. (Pubitemid 28093518)
    • (1998) Nature , vol.391 , Issue.6665 , pp. 407-410
    • New, J.H.1    Sugiyama, T.2    Zaitseva, E.3    Kowalczykowski, S.C.4
  • 33
    • 20444375871 scopus 로고    scopus 로고
    • DNA damage induced hyperphosphorylation of replication protein A. 1. Identification of novel sites of phosphorylation in response to DNA damage
    • Nuss, J. E., S. M. Patrick, G. G. Oakley, G. M. Alter, J. G. Robison, K. Dixon, and J. J. Turchi. 2005. DNA damage induced hyperphosphorylation of replication protein A. 1. Identification of novel sites of phosphorylation in response to DNA damage. Biochemistry 44:8428-8437.
    • (2005) Biochemistry , vol.44 , pp. 8428-8437
    • Nuss, J.E.1    Patrick, S.M.2    Oakley, G.G.3    Alter, G.M.4    Robison, J.G.5    Dixon, K.6    Turchi, J.J.7
  • 34
    • 0022895276 scopus 로고
    • The structure of the termini of the Epstein-Barr virus as a marker of clonal cellular proliferation
    • Raab-Traub, N., and K. Flynn. 1986. The structure of the termini of the Epstein-Barr virus as a marker of clonal cellular proliferation. Cell 47:883-889. (Pubitemid 17005061)
    • (1986) Cell , vol.47 , Issue.6 , pp. 883-889
    • Raab-Traub, N.1    Flynn, K.2
  • 35
    • 30444445118 scopus 로고    scopus 로고
    • Interplay between human DNA repair proteins at a unique double-strand break in vivo
    • DOI 10.1038/sj.emboj.7600914, PII 7600914
    • Rodrigue, A., M. Lafrance, M. C. Gauthier, D. McDonald, M. Hendzel, S. C. West, M. Jasin, and J. Y. Masson. 2006. Interplay between human DNA repair proteins at a unique double-strand break in vivo. EMBO J. 25:222-231. (Pubitemid 43077310)
    • (2006) EMBO Journal , vol.25 , Issue.1 , pp. 222-231
    • Rodrigue, A.1    Lafrance, M.2    Gauthier, M.-C.3    McDonald, D.4    Hendzel, M.5    West, S.C.6    Jasin, M.7    Masson, J.-Y.8
  • 36
    • 0025130597 scopus 로고
    • Concatameric replication of Epstein-Barr virus: Structures of the termini in virus-producer and newly transformed cell lines
    • Sato, H., T. Takimoto, S. Tanaka, J. Tanaka, and N. Raab-Traub. 1990. Concatameric replication of Epstein-Barr virus: structure of the termini in virus-producer and newly transformed cell lines. J. Virol. 64:5295-5300. (Pubitemid 20364518)
    • (1990) Journal of Virology , vol.64 , Issue.11 , pp. 5295-5300
    • Sato, H.1    Takimoto, T.2    Tanaka, S.3    Tanaka, J.4    Raab-Traub, N.5
  • 37
    • 0029985571 scopus 로고    scopus 로고
    • Branched structures in the intracellular DNA of herpes simplex virus type 1
    • Severini, A., D. G. Scraba, and D. L. Tyrrell. 1996. Branched structures in the intracellular DNA of herpes simplex virus type 1. J. Virol. 70:3169-3175. (Pubitemid 26121935)
    • (1996) Journal of Virology , vol.70 , Issue.5 , pp. 3169-3175
    • Severini, A.1    Scraba, D.G.2    Tyrrell, D.L.J.3
  • 38
    • 0033104517 scopus 로고    scopus 로고
    • Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates RPA:DNA-PK complexes
    • Shao, R. G., C. X. Cao, H. Zhang, K. W. Kohn, M. S. Wold, and Y. Pommier. 1999. Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates RPA: DNA-PK complexes. EMBO J. 18:1397-1406. (Pubitemid 29110323)
    • (1999) EMBO Journal , vol.18 , Issue.5 , pp. 1397-1406
    • Shao, R.-G.1    Cao, C.-X.2    Zhang, H.3    Kohn, K.W.4    Wold, M.S.5    Pommier, Y.6
  • 39
    • 0026751113 scopus 로고
    • Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein
    • Shinohara, A., H. Ogawa, and T. Ogawa. 1992. Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein. Cell 69:457-470.
    • (1992) Cell , vol.69 , pp. 457-470
    • Shinohara, A.1    Ogawa, H.2    Ogawa, T.3
  • 40
    • 0031902872 scopus 로고    scopus 로고
    • Rad52 forms ring structures and co-operates with RPA in single-strand DNA annealing
    • DOI 10.1046/j.1365-2443.1998.00176.x
    • Shinohara, A., M. Shinohara, T. Ohta, S. Matsuda, and T. Ogawa. 1998. Rad52 forms ring structures and co-operates with RPA in single-strand DNA annealing. Genes Cells 3:145-156. (Pubitemid 28374987)
    • (1998) Genes to Cells , vol.3 , Issue.3 , pp. 145-156
    • Shinohara, A.1    Shinohara, M.2    Ohta, T.3    Matsuda, S.4    Ogawa, T.5
  • 41
    • 0032502760 scopus 로고    scopus 로고
    • Functional analysis of human replication protein A in nucleotide excision repair
    • Stigger, E., R. Drissi, and S. H. Lee. 1998. Functional analysis of human replication protein A in nucleotide excision repair. J. Biol. Chem. 273:9337-9343.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9337-9343
    • Stigger, E.1    Drissi, R.2    Lee, S.H.3
  • 42
    • 0037199924 scopus 로고    scopus 로고
    • Rad52 protein associates with replication protein A (RPA)-single-stranded DNA to accelerate Rad51- mediated displacement of RPA and presynaptic complex formation
    • Sugiyama, T., and S. C. Kowalczykowski. 2002. Rad52 protein associates with replication protein A (RPA)-single-stranded DNA to accelerate Rad51- mediated displacement of RPA and presynaptic complex formation. J. Biol. Chem. 277:31663-31672.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31663-31672
    • Sugiyama, T.1    Kowalczykowski, S.C.2
  • 43
    • 0030849922 scopus 로고    scopus 로고
    • Sp1 binds to the precise locus of end processing within the terminal repeats of Epstein-Barr virus DNA
    • Sun, R., T. A. Spain, S. F. Lin, and G. Miller. 1997. Sp1 binds to the precise locus of end processing within the terminal repeats of Epstein-Barr virus DNA. J. Virol. 71:6136-6143. (Pubitemid 27304955)
    • (1997) Journal of Virology , vol.71 , Issue.8 , pp. 6136-6143
    • Sun, R.1    Spain, T.A.2    Lin, S.-F.3    Miller, G.4
  • 44
    • 0025925178 scopus 로고
    • Formation of intranuclear replication compartments of Epstein-Barr virus with redistribution of BZLF1 and BMRF1 gene products
    • Takagi, S., K. Takada, and T. Sairenji. 1991. Formation of intranuclear replication compartments of Epstein-Barr virus with redistribution of BZLF1 and BMRF1 gene products. Virology 185:309-315.
    • (1991) Virology , vol.185 , pp. 309-315
    • Takagi, S.1    Takada, K.2    Sairenji, T.3
  • 45
    • 11244266124 scopus 로고    scopus 로고
    • Latent and lytic Epstein-Barr virus replication strategies
    • Tsurumi, T., M. Fujita, and A. Kudoh. 2005. Latent and lytic Epstein-Barr virus replication strategies. Rev. Med. Virol. 15:3-15.
    • (2005) Rev. Med. Virol. , vol.15 , pp. 3-15
    • Tsurumi, T.1    Fujita, M.2    Kudoh, A.3
  • 46
    • 1342325347 scopus 로고    scopus 로고
    • Replication protein A (RPA) phosphorylation prevents RPA association with replication centers
    • Vassin, V. M., M. S. Wold, and J. A. Borowiec. 2004. Replication protein A (RPA) phosphorylation prevents RPA association with replication centers. Mol. Cell. Biol. 24:1930-1943.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1930-1943
    • Vassin, V.M.1    Wold, M.S.2    Borowiec, J.A.3
  • 47
    • 34547176640 scopus 로고    scopus 로고
    • Replication blocking lesions present a unique substrate for homologous recombination
    • DOI 10.1038/sj.emboj.7601766, PII 7601766
    • Ward, J. D., L. J. Barber, M. I. Petalcorin, J. Yanowitz, and S. J. Boulton. 2007. Replication blocking lesions present a unique substrate for homologous recombination. EMBO J. 26:3384-3396. (Pubitemid 47123531)
    • (2007) EMBO Journal , vol.26 , Issue.14 , pp. 3384-3396
    • Ward, J.D.1    Barber, L.J.2    Petalcorin, M.I.3    Yanowitz, J.4    Boulton, S.J.5
  • 48
    • 0023681344 scopus 로고
    • Inversion events in the HSV-1 genome are directly mediated by the viral DNA replication machinery and lack sequence specificity
    • DOI 10.1016/0092-8674(88)90200-0
    • Weber, P. C., M. D. Challberg, N. J. Nelson, M. Levine, and J. C. Glorioso. 1988. Inversion events in the HSV-1 genome are directly mediated by the viral DNA replication machinery and lack sequence specificity. Cell 54:369-381. (Pubitemid 18188764)
    • (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
  • 49
    • 33746871757 scopus 로고    scopus 로고
    • Herpes simplex virus type I disrupts the ATR- Dependent DNA-damage response during lytic infection
    • DOI 10.1242/jcs.02981
    • Wilkinson, D. E., and S. K. Weller. 2006. Herpes simplex virus type I disrupts the ATR-dependent DNA-damage response during lytic infection. J. Cell Sci. 119:2695-2703. (Pubitemid 44184006)
    • (2006) Journal of Cell Science , vol.119 , Issue.13 , pp. 2695-2703
    • Wilkinson, D.E.1    Weller, S.K.2
  • 50
    • 18744398124 scopus 로고    scopus 로고
    • Inhibition of the herpes simplex virus type 1 DNA polymerase induces hyperphosphorylation of replication protein a and its accumulation at S-phase-specific sites of DNA damage during infection
    • DOI 10.1128/JVI.79.11.7162-7171.2005
    • Wilkinson, D. E., and S. K. Weller. 2005. Inhibition of the herpes simplex virus type 1 DNA polymerase induces hyperphosphorylation of replication protein A and its accumulation at S-phase-specific sites of DNA damage during infection. J. Virol. 79:7162-7171. (Pubitemid 40677346)
    • (2005) Journal of Virology , vol.79 , Issue.11 , pp. 7162-7171
    • Wilkinson, D.E.1    Weller, S.K.2
  • 51
    • 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
    • DOI 10.1128/JVI.78.9.4783-4796.2004
    • Wilkinson, D. E., and S. K. Weller. 2004. 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. 78:4783-4796. (Pubitemid 38501099)
    • (2004) Journal of Virology , vol.78 , Issue.9 , pp. 4783-4796
    • Wilkinson, D.E.1    Weller, S.K.2
  • 52
    • 0026004036 scopus 로고
    • Epstein-Barr virus-derived plasmids replicate only once per cell cycle and are not amplified after entry into cells
    • Yates, J. L., and N. Guan. 1991. Epstein-Barr virus-derived plasmids replicate only once per cell cycle and are not amplified after entry into cells. J. Virol. 65:483-488.
    • (1991) J. Virol. , vol.65 , pp. 483-488
    • Yates, J.L.1    Guan, N.2
  • 53
    • 0034618613 scopus 로고    scopus 로고
    • Co-expression of human chaperone Hsp70 and Hsdj or Hsp40 co-factor increases solubility of overexpressed target proteins in insect cells
    • Yokoyama, N., M. Hirata, K. Ohtsuka, Y. Nishiyama, K. Fujii, M. Fujita, K. Kuzushima, T. Kiyono, and T. Tsurumi. 2000. Co-expression of human chaperone Hsp70 and Hsdj or Hsp40 co-factor increases solubility of overexpressed target proteins in insect cells. Biochim. Biophys. Acta 1493:119-124.
    • (2000) Biochim. Biophys. Acta , vol.1493 , pp. 119-124
    • Yokoyama, N.1    Hirata, M.2    Ohtsuka, K.3    Nishiyama, Y.4    Fujii, K.5    Fujita, M.6    Kuzushima, K.7    Kiyono, T.8    Tsurumi, T.9
  • 54
    • 0030810633 scopus 로고    scopus 로고
    • Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from HeLa cells
    • Zernik-Kobak, M., K. Vasunia, M. Connelly, C. W. Anderson, and K. Dixon. 1997. Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from HeLa cells. J. Biol. Chem. 272:23896-23904.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23896-23904
    • Zernik-Kobak, M.1    Vasunia, K.2    Connelly, M.3    Anderson, C.W.4    Dixon, K.5
  • 55
    • 0028915144 scopus 로고
    • Structure and role of the terminal repeats of Epstein-Barr virus in processing and packaging of virion DNA
    • Zimmermann, J., and W. Hammerschmidt. 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
  • 56
    • 33745607897 scopus 로고    scopus 로고
    • Functions of human replication protein A (RPA): From DNA replication to DNA damage and stress responses
    • Zou, Y., Y. Liu, X. Wu, and S. M. Shell. 2006. Functions of human replication protein A (RPA): from DNA replication to DNA damage and stress responses. J. Cell. Physiol. 208:267-273.
    • (2006) J. Cell. Physiol. , vol.208 , pp. 267-273
    • Zou, Y.1    Liu, Y.2    Wu, X.3    Shell, S.M.4


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