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Volumn 84, Issue 24, 2010, Pages 12589-12598

Tetrameric ring formation of Epstein-Barr virus polymerase processivity factor is crucial for viral replication

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE; DNA POLYMERASE PROCESSIVITY FACTOR BMRF1; MUTANT PROTEIN; UNCLASSIFIED DRUG; VIRUS DNA;

EID: 78649392657     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01394-10     Document Type: Article
Times cited : (14)

References (47)
  • 1
    • 69449088939 scopus 로고    scopus 로고
    • Distinctive effects of the Epstein-Barr virus family of repeats on viral latent gene promoter activity and B-lymphocyte transformation
    • Ali, A. K., S. Saito, S. Shibata, K. Takada, and T. Kanda. 2009. Distinctive effects of the Epstein-Barr virus family of repeats on viral latent gene promoter activity and B-lymphocyte transformation. J. Virol. 83:9163-9174.
    • (2009) J. Virol. , vol.83 , pp. 9163-9174
    • Ali, A.K.1    Saito, S.2    Shibata, S.3    Takada, K.4    Kanda, T.5
  • 2
    • 69449102907 scopus 로고    scopus 로고
    • The flexible loop of the human cytomegalovirus DNA polymerase processivity factor ppUL44 is required for efficient DNA binding and replication in cells
    • Alvisi, G., D. M. Roth, D. Camozzi, G. S. Pari, A. Loregian, A. Ripalti, and D. A. Jans. 2009. The flexible loop of the human cytomegalovirus DNA polymerase processivity factor ppUL44 is required for efficient DNA binding and replication in cells. J. Virol. 83:9567-9576.
    • (2009) J. Virol. , vol.83 , pp. 9567-9576
    • Alvisi, G.1    Roth, D.M.2    Camozzi, D.3    Pari, G.S.4    Loregian, A.5    Ripalti, A.6    Jans, D.A.7
  • 3
    • 0035110865 scopus 로고    scopus 로고
    • The ring-type polymerase sliding clamp family
    • Bruck, I., and M. O'Donnell. 2001. The ring-type polymerase sliding clamp family. Genome Biol. 2:REVIEWS3001.
    • (2001) Genome Biol. , vol.2
    • Bruck, I.1    O'Donnell, M.2
  • 4
    • 0029123595 scopus 로고
    • Functional analysis of EA-D of Epstein-Barr virus
    • Chen, L. W., L. S. Lin, Y. S. Chang, and S. T. Liu. 1995. Functional analysis of EA-D of Epstein-Barr virus. Virology 211:593-597.
    • (1995) Virology , vol.211 , pp. 593-597
    • Chen, L.W.1    Lin, L.S.2    Chang, Y.S.3    Liu, S.T.4
  • 5
    • 0021959359 scopus 로고
    • Interaction of Epstein-Barr virus DNA polymerase and 5′- triphosphates of several antiviral nucleoside analogs
    • Chiou, J. F., and Y. C. Cheng. 1985. Interaction of Epstein-Barr virus DNA polymerase and 5′-triphosphates of several antiviral nucleoside analogs. Antimicrob. Agents Chemother. 27:416-418.
    • (1985) Antimicrob. Agents Chemother. , vol.27 , pp. 416-418
    • Chiou, J.F.1    Cheng, Y.C.2
  • 6
    • 0022344091 scopus 로고
    • A second Epstein-Barr virus early antigen gene in BamHI fragment M encodes a 48- To 50-kilodalton nuclear protein
    • Cho, M. S., G. Milman, and S. D. Hayward. 1985. A second Epstein-Barr virus early antigen gene in BamHI fragment M encodes a 48- to 50-kilodalton nuclear protein. J. Virol. 56:860-866.
    • (1985) J. Virol. , vol.56 , pp. 860-866
    • Cho, M.S.1    Milman, G.2    Hayward, S.D.3
  • 7
    • 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
  • 8
    • 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
  • 10
    • 0004250845 scopus 로고    scopus 로고
    • Lippincott Williams & Wilkins. 4th ed. Lippincott Williams & Wilkins, Philadelphia, PA
    • Fields, B. N., D. M. Knipe, P. M. Howley, D. E. Griffin, and Lippincott Williams & Wilkins. 2002. Fields virology, 4th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2002) Fields Virology
    • Fields, B.N.1    Knipe, D.M.2    Howley, P.M.3    Griffin, D.E.4
  • 11
    • 0028915139 scopus 로고
    • Replication of Epstein-Barr virus oriLyt: Lack of a dedicated virally encoded origin-binding protein and dependence on Zta in cotransfection assays
    • Fixman, E. D., G. S. Hayward, and S. D. Hayward. 1995. Replication of Epstein-Barr virus oriLyt: lack of a dedicated virally encoded origin-binding protein and dependence on Zta in cotransfection assays. J. Virol. 69:2998-3006.
    • (1995) J. Virol. , vol.69 , pp. 2998-3006
    • Fixman, E.D.1    Hayward, G.S.2    Hayward, S.D.3
  • 12
    • 0026708186 scopus 로고
    • Trans-acting requirements for replication of Epstein-Barr virus ori-Lyt
    • Fixman, E. D., G. S. Hayward, and S. D. Hayward. 1992. trans-acting requirements for replication of Epstein-Barr virus ori-Lyt. J. Virol. 66:5030-5039.
    • (1992) J. Virol. , vol.66 , pp. 5030-5039
    • Fixman, E.D.1    Hayward, G.S.2    Hayward, S.D.3
  • 13
    • 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
  • 14
    • 0031713687 scopus 로고    scopus 로고
    • In vitro processing of herpes simplex virus type 1 DNA replication intermediates by the viral alkaline nuclease, UL12
    • Goldstein, J. N., and S. K. Weller. 1998. In vitro processing of herpes simplex virus type 1 DNA replication intermediates by the viral alkaline nuclease, UL12. J. Virol. 72:8772-8781.
    • (1998) J. Virol. , vol.72 , pp. 8772-8781
    • Goldstein, J.N.1    Weller, S.K.2
  • 15
    • 0030592544 scopus 로고    scopus 로고
    • Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA
    • Gulbis, J. M., Z. Kelman, J. Hurwitz, M. O'Donnell, and J. Kuriyan. 1996. Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA. Cell 87:297-306.
    • (1996) Cell , vol.87 , pp. 297-306
    • Gulbis, J.M.1    Kelman, Z.2    Hurwitz, J.3    O'Donnell, M.4    Kuriyan, J.5
  • 16
    • 0023698910 scopus 로고
    • Identification and characterization of oriLyt, a lytic origin of DNA replication of Epstein-Barr virus
    • DOI 10.1016/0092-8674(88)90028-1
    • Hammerschmidt, W., and B. Sugden. 1988. Identification and characterization of oriLyt, a lytic origin of DNA replication of Epstein-Barr virus. Cell 55:427-433. (Pubitemid 18261432)
    • (1988) Cell , vol.55 , Issue.3 , pp. 427-433
    • Hammerschmidt, W.1    Sugden, B.2
  • 17
    • 38849116422 scopus 로고    scopus 로고
    • Noncanonical TATA sequence in the UL44 late promoter of human cytomegalovirus is required for the accumulation of late viral transcripts
    • DOI 10.1128/JVI.01917-07
    • Isomura, H., M. F. Stinski, A. Kudoh, T. Murata, S. Nakayama, Y. Sato, S. Iwahori, and T. Tsurumi. 2008. Noncanonical TATA sequence in the UL44 late promoter of human cytomegalovirus is required for the accumulation of late viral transcripts. J. Virol. 82:1638-1646. (Pubitemid 351206915)
    • (2008) Journal of Virology , vol.82 , Issue.4 , pp. 1638-1646
    • Isomura, H.1    Stinski, M.F.2    Kudoh, A.3    Murata, T.4    Nakayama, S.5    Sato, Y.6    Iwahori, S.7    Tsurumi, T.8
  • 18
    • 37849008194 scopus 로고    scopus 로고
    • A cis element between the TATA box and the transcription start site of the major immediate-early promoter of human cytomegalovirus determines efficiency of viral replication
    • Isomura, H., M. F. Stinski, A. Kudoh, S. Nakayama, T. Murata, Y. Sato, S. Iwahori, and T. Tsurumi. 2008. A cis element between the TATA box and the transcription start site of the major immediate-early promoter of human cytomegalovirus determines efficiency of viral replication. J. Virol. 82:849-858.
    • (2008) J. Virol. , vol.82 , pp. 849-858
    • Isomura, H.1    Stinski, M.F.2    Kudoh, A.3    Nakayama, S.4    Murata, T.5    Sato, Y.6    Iwahori, S.7    Tsurumi, T.8
  • 19
    • 8644230155 scopus 로고    scopus 로고
    • Role of the proximal enhancer of the major immediate-early promoter in human cytomegalovirus replication
    • Isomura, H., T. Tsurumi, and M. F. Stinski. 2004. Role of the proximal enhancer of the major immediate-early promoter in human cytomegalovirus replication. J. Virol. 78:12788-12799.
    • (2004) J. Virol. , vol.78 , pp. 12788-12799
    • Isomura, H.1    Tsurumi, T.2    Stinski, M.F.3
  • 20
    • 0021819988 scopus 로고
    • Purification of Epstein-Barr virus DNA polymerase from P3HR-1 cells
    • Kallin, B., L. Sternas, A. K. Saemundssen, J. Luka, H. Jornvall, B. Eriksson, P. Z. Tao, M. T. Nilsson, and G. Klein. 1985. Purification of Epstein-Barr virus DNA polymerase from P3HR-1 cells. J. Virol. 54:561-568. (Pubitemid 15050971)
    • (1985) Journal of Virology , vol.54 , Issue.2 , pp. 561-568
    • Kallin, B.1    Sternas, L.2    Saemundssen, A.K.3
  • 21
    • 0028795649 scopus 로고
    • Bipartite DNA-binding region of the Epstein-Barr virus BMRF1 product essential for DNA polymerase accessory function
    • Kiehl, A., and D. I. Dorsky. 1995. Bipartite DNA-binding region of the Epstein-Barr virus BMRF1 product essential for DNA polymerase accessory function. J. Virol. 69:1669-1677.
    • (1995) J. Virol. , vol.69 , pp. 1669-1677
    • Kiehl, A.1    Dorsky, D.I.2
  • 22
    • 0025784487 scopus 로고
    • Cooperation of EBV DNA polymerase and EA-D(BMRF1) in vitro and colocalization in nuclei of infected cells
    • Kiehl, A., and D. I. Dorsky. 1991. Cooperation of EBV DNA polymerase and EA-D(BMRF1) in vitro and colocalization in nuclei of infected cells. Virology 184:330-340.
    • (1991) Virology , vol.184 , pp. 330-340
    • Kiehl, A.1    Dorsky, D.I.2
  • 23
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna, T. S., X. P. Kong, S. Gary, P. M. Burgers, and J. Kuriyan. 1994. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell 79:1233-1243.
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 24
    • 0023270119 scopus 로고
    • Association of Epstein-Barr virus early antigen diffuse component and virus-specified DNA polymerase activity
    • Li, J. S., B. S. Zhou, G. E. Dutschman, S. P. Grill, R. S. Tan, and Y. C. Cheng. 1987. Association of Epstein-Barr virus early antigen diffuse component and virus-specified DNA polymerase activity. J. Virol. 61:2947-2949.
    • (1987) J. Virol. , vol.61 , pp. 2947-2949
    • Li, J.S.1    Zhou, B.S.2    Dutschman, G.E.3    Grill, S.P.4    Tan, R.S.5    Cheng, Y.C.6
  • 25
    • 34547891497 scopus 로고    scopus 로고
    • Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: Implications for the processivity mechanism
    • Loregian, A., E. Sinigalia, B. Mercorelli, G. Palu, and D. M. Coen. 2007. Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism. Nucleic Acids Res. 35:4779-4791.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4779-4791
    • Loregian, A.1    Sinigalia, E.2    Mercorelli, B.3    Palu, G.4    Coen, D.M.5
  • 26
    • 4644264523 scopus 로고    scopus 로고
    • The Epstein-Barr virus polymerase accessory factor BMRF1 adopts a ring-shaped structure as visualized by electron microscopy
    • Makhov, A. M., D. Subramanian, E. Holley-Guthrie, S. C. Kenney, and J. D. Griffith. 2004. The Epstein-Barr virus polymerase accessory factor BMRF1 adopts a ring-shaped structure as visualized by electron microscopy. J. Biol. Chem. 279:40358-40361.
    • (2004) J. Biol. Chem. , vol.279 , pp. 40358-40361
    • Makhov, A.M.1    Subramanian, D.2    Holley-Guthrie, E.3    Kenney, S.C.4    Griffith, J.D.5
  • 27
    • 0030042028 scopus 로고    scopus 로고
    • The product of a 1.9-kb mRNA which overlaps the HSV-1 alkaline nuclease gene (UL12) cannot relieve the growth defects of a null mutant
    • Martinez, R., L. Shao, J. C. Bronstein, P. C. Weber, and S. K. Weller. 1996. The product of a 1.9-kb mRNA which overlaps the HSV-1 alkaline nuclease gene (UL12) cannot relieve the growth defects of a null mutant. Virology 215:152-164.
    • (1996) Virology , vol.215 , pp. 152-164
    • Martinez, R.1    Shao, L.2    Bronstein, J.C.3    Weber, P.C.4    Weller, S.K.5
  • 28
    • 0037377527 scopus 로고    scopus 로고
    • Intermolecular ion pairs maintain the toroidal structure of Pyrococcus furiosus PCNA
    • DOI 10.1110/ps.0234503
    • Matsumiya, S., S. Ishino, Y. Ishino, and K. Morikawa. 2003. Intermolecular ion pairs maintain the toroidal structure of Pyrococcus furiosus PCNA. Protein Sci. 12:823-831. (Pubitemid 36348469)
    • (2003) Protein Science , vol.12 , Issue.4 , pp. 823-831
    • Matsumiya, S.1    Ishino, S.2    Ishino, Y.3    Morikawa, K.4
  • 29
    • 0034628915 scopus 로고    scopus 로고
    • Crystal structure of the DNA polymerase processivity factor of T4 bacteriophage
    • Moarefi, I., D. Jeruzalmi, J. Turner, M. O'Donnell, and J. Kuriyan. 2000. Crystal structure of the DNA polymerase processivity factor of T4 bacteriophage. J. Mol. Biol. 296:1215-1223.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1215-1223
    • Moarefi, I.1    Jeruzalmi, D.2    Turner, J.3    O'Donnell, M.4    Kuriyan, J.5
  • 33
    • 69249096140 scopus 로고    scopus 로고
    • Epstein-Barr virus polymerase processivity factor enhances BALF2 promoter transcription as a coactivator for the BZLF1 immediate-early protein
    • Nakayama, S., T. Murata, K. Murayama, Y. Yasui, Y. Sato, A. Kudoh, S. Iwahori, H. Isomura, T. Kanda, and T. Tsurumi. 2009. Epstein-Barr virus polymerase processivity factor enhances BALF2 promoter transcription as a coactivator for the BZLF1 immediate-early protein. J. Biol. Chem. 284:21557-21568.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21557-21568
    • Nakayama, S.1    Murata, T.2    Murayama, K.3    Yasui, Y.4    Sato, Y.5    Kudoh, A.6    Iwahori, S.7    Isomura, H.8    Kanda, T.9    Tsurumi, T.10
  • 34
    • 33646442894 scopus 로고    scopus 로고
    • The Epstein-Barr virus BMRF1 gene is essential for lytic virus replication
    • Neuhierl, B., and H. J. Delecluse. 2006. The Epstein-Barr virus BMRF1 gene is essential for lytic virus replication. J. Virol. 80:5078-5081.
    • (2006) J. Virol. , vol.80 , pp. 5078-5081
    • Neuhierl, B.1    Delecluse, H.J.2
  • 35
    • 0037069336 scopus 로고    scopus 로고
    • Glycoprotein gp110 of Epstein-Barr virus determines viral tropism and efficiency of infection
    • Neuhierl, B., R. Feederle, W. Hammerschmidt, and H. J. Delecluse. 2002. Glycoprotein gp110 of Epstein-Barr virus determines viral tropism and efficiency of infection. Proc. Natl. Acad. Sci. U. S. A. 99:15036-15041.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 15036-15041
    • Neuhierl, B.1    Feederle, R.2    Hammerschmidt, W.3    Delecluse, H.J.4
  • 36
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukaryotic vector
    • Niwa, H., K. Yamamura, and J. Miyazaki. 1991. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 108:193-199.
    • (1991) Gene , vol.108 , pp. 193-199
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 37
    • 0347627532 scopus 로고    scopus 로고
    • The herpes simplex virus processivity factor, UL42, binds DNA as a monomer
    • Randell, J. C., and D. M. Coen. 2004. The herpes simplex virus processivity factor, UL42, binds DNA as a monomer. J. Mol. Biol. 335:409-413.
    • (2004) J. Mol. Biol. , vol.335 , pp. 409-413
    • Randell, J.C.1    Coen, D.M.2
  • 38
    • 24644512131 scopus 로고    scopus 로고
    • Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesis
    • Randell, J. C., G. Komazin, C. Jiang, C. B. Hwang, and D. M. Coen. 2005. Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesis. J. Virol. 79:12025-12034.
    • (2005) J. Virol. , vol.79 , pp. 12025-12034
    • Randell, J.C.1    Komazin, G.2    Jiang, C.3    Hwang, C.B.4    Coen, D.M.5
  • 39
    • 0028269715 scopus 로고
    • Study of the structure of replicative intermediates of HSV-1 DNA by pulsed-field gel electrophoresis
    • Severini, A., A. R. Morgan, D. R. Tovell, and D. L. Tyrrell. 1994. Study of the structure of replicative intermediates of HSV-1 DNA by pulsed-field gel electrophoresis. Virology 200:428-435.
    • (1994) Virology , vol.200 , pp. 428-435
    • Severini, A.1    Morgan, A.R.2    Tovell, D.R.3    Tyrrell, D.L.4
  • 40
    • 0032692565 scopus 로고    scopus 로고
    • Building a replisome from interacting pieces: Sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex
    • Shamoo, Y., and T. A. Steitz. 1999. Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex. Cell 99:155-166.
    • (1999) Cell , vol.99 , pp. 155-166
    • Shamoo, Y.1    Steitz, T.A.2
  • 41
    • 0028111669 scopus 로고
    • Isolation of Epstein-Barr virus (EBV)-negative cell clones from the EBV-positive Burkitt's lymphoma (BL) line Akata: Malignant phenotypes of BL cells are dependent on EBV
    • Shimizu, N., A. Tanabe-Tochikura, Y. Kuroiwa, and K. Takada. 1994. Isolation of Epstein-Barr virus (EBV)-negative cell clones from the EBV-positive Burkitt's lymphoma (BL) line Akata: malignant phenotypes of BL cells are dependent on EBV. J. Virol. 68:6069-6073.
    • (1994) J. Virol. , vol.68 , pp. 6069-6073
    • Shimizu, N.1    Tanabe-Tochikura, A.2    Kuroiwa, Y.3    Takada, K.4
  • 42
    • 0027478992 scopus 로고
    • Purification and characterization of the DNA-binding activity of the Epstein-Barr virus DNA polymerase accessory protein BMRF1 gene products, as expressed in insect cells by using the baculovirus system
    • Tsurumi, T. 1993. Purification and characterization of the DNA-binding activity of the Epstein-Barr virus DNA polymerase accessory protein BMRF1 gene products, as expressed in insect cells by using the baculovirus system. J. Virol. 67:1681-1687. (Pubitemid 23067680)
    • (1993) Journal of Virology , vol.67 , Issue.3 , pp. 1681-1687
    • Tsurumi, T.1
  • 43
    • 0027448643 scopus 로고
    • Functional interaction between Epstein-Barr virus DNA polymerase catalytic subunit and its accessory subunit in vitro
    • Tsurumi, T., T. Daikoku, R. Kurachi, and Y. Nishiyama. 1993. Functional interaction between Epstein-Barr virus DNA polymerase catalytic subunit and its accessory subunit in vitro. J. Virol. 67:7648-7653. (Pubitemid 23343898)
    • (1993) Journal of Virology , vol.67 , Issue.12 , pp. 7648-7653
    • Tsurumi, T.1    Daikoku, T.2    Kurachi, R.3    Nishiyama, Y.4
  • 44
    • 0028334980 scopus 로고
    • Further characterization of the interaction between the Epstein-Barr virus DNA polymerase catalytic subunit and its accessory subunit with regard to the 3′-to-5′ exonucleolytic activity and stability of initiation complex at primer terminus
    • Tsurumi, T., T. Daikoku, and Y. Nishiyama. 1994. Further characterization of the interaction between the Epstein-Barr virus DNA polymerase catalytic subunit and its accessory subunit with regard to the 3′-to-5′ exonucleolytic activity and stability of initiation complex at primer terminus. J. Virol. 68:3354-3363.
    • (1994) J. Virol. , vol.68 , pp. 3354-3363
    • Tsurumi, T.1    Daikoku, T.2    Nishiyama, Y.3
  • 45
    • 0030586695 scopus 로고    scopus 로고
    • Epstein-Barr virus single-stranded DNA-binding protein: Purification, characterization, and action on DNA synthesis by the viral DNA polymerase
    • DOI 10.1006/viro.1996.0432
    • Tsurumi, T., A. Kobayashi, K. Tamai, H. Yamada, T. Daikoku, Y. Yamashita, and Y. Nishiyama. 1996. Epstein-Barr virus single-stranded DNA-binding protein: purification, characterization, and action on DNA synthesis by the viral DNA polymerase. Virology 222:352-364. (Pubitemid 26279180)
    • (1996) Virology , vol.222 , Issue.2 , pp. 352-364
    • Tsurumi, T.1    Kobayashi, A.2    Tamai, K.3    Yamada, H.4    Daikoku, T.5    Yamashita, Y.6    Nishiyama, Y.7
  • 47
    • 0029931715 scopus 로고    scopus 로고
    • Functional and physical interactions between the Epstein-Barr virus (EBV) proteins BZLF1 and BMRF1: Effects on EBV transcription and lytic replication
    • Zhang, Q., Y. Hong, D. Dorsky, E. Holley-Guthrie, S. Zalani, N. A. Elshiekh, A. Kiehl, T. Le, and S. Kenney. 1996. Functional and physical interactions between the Epstein-Barr virus (EBV) proteins BZLF1 and BMRF1: effects on EBV transcription and lytic replication. J. Virol. 70:5131-5142. (Pubitemid 26240684)
    • (1996) Journal of Virology , vol.70 , Issue.8 , pp. 5131-5142
    • Zhang, Q.1    Hong, Y.2    Dorsky, D.3    Holley-Guthrie, E.4    Zalani, S.5    Elshiekh, N.A.6    Kiehl, A.7    Le, T.8    Kenney, S.9


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