메뉴 건너뛰기




Volumn 78, Issue 17, 2004, Pages 9412-9422

Epstein-Barr virus (EBV) SM protein induces and recruits cellular Sp110b to stabilize mRNAs and enhance EBV lytic gene expression

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; MESSENGER RNA; NUCLEAR BODY PROTEIN; PROTEIN SM; SMALL INTERFERING RNA; SP110 PROTEIN; SP110B PROTEIN; STAT1 PROTEIN; UNCLASSIFIED DRUG; VIRUS DNA; VIRUS PROTEIN;

EID: 4143100267     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.17.9412-9422.2004     Document Type: Article
Times cited : (55)

References (47)
  • 1
    • 0032798394 scopus 로고    scopus 로고
    • The Epstein-Barr virus BZLF1 protein interacts physically and functionally with the histone acetylase CREB-binding protein
    • Adamson, A. L., and S. Kenney. 1999. The Epstein-Barr virus BZLF1 protein interacts physically and functionally with the histone acetylase CREB-binding protein. J. Virol. 73:6551-6558.
    • (1999) J. Virol. , vol.73 , pp. 6551-6558
    • Adamson, A.L.1    Kenney, S.2
  • 2
    • 0030839829 scopus 로고    scopus 로고
    • Gene identification using the yeast two-hybrid system
    • Bai, C., and S. J. Elledge. 1997. Gene identification using the yeast two-hybrid system. Methods Enzymol. 283:141-156.
    • (1997) Methods Enzymol. , vol.283 , pp. 141-156
    • Bai, C.1    Elledge, S.J.2
  • 3
    • 0034467855 scopus 로고    scopus 로고
    • Lytic but not latent replication of Epstein-Barr virus is associated with PML and induces sequential release of nuclear domain 10 proteins
    • Bell, P., P. M. Lieberman, and G. G. Maul. 2000. Lytic but not latent replication of Epstein-Barr virus is associated with PML and induces sequential release of nuclear domain 10 proteins. J. Virol. 74:11800-11810.
    • (2000) J. Virol. , vol.74 , pp. 11800-11810
    • Bell, P.1    Lieberman, P.M.2    Maul, G.G.3
  • 4
    • 0033860185 scopus 로고    scopus 로고
    • Sp110 localizes to the PML-Sp100 nuclear body and may function as a nuclear hormone receptor transcriptional coactivator
    • Bloch, D. B., A. Nakajima, T. Gulick, J. D. Chiche, D. Orth, S. M. de La Monte, and K. D. Bloch. 2000. Sp110 localizes to the PML-Sp100 nuclear body and may function as a nuclear hormone receptor transcriptional coactivator. Mol. Cell. Biol. 20:6138-6146.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6138-6146
    • Bloch, D.B.1    Nakajima, A.2    Gulick, T.3    Chiche, J.D.4    Orth, D.5    De La Monte, S.M.6    Bloch, K.D.7
  • 5
    • 0036284985 scopus 로고    scopus 로고
    • Alternate replication in B cells and epithelial cells switches tropism of Epstein-Barr virus
    • Borza, C. M., and L. M. Hutt-Fletcher. 2002. Alternate replication in B cells and epithelial cells switches tropism of Epstein-Barr virus. Nat. Med. 8:594-599.
    • (2002) Nat. Med. , vol.8 , pp. 594-599
    • Borza, C.M.1    Hutt-Fletcher, L.M.2
  • 7
    • 0032798214 scopus 로고    scopus 로고
    • Association with the cellular export receptor CRM 1 mediates function and intracellular localization of Epstein-Barr virus SM protein, a regulator of gene expression
    • Boyle, S. M., V. Ruvolo, A. K. Gupta, and S. Swaminathan. 1999. Association with the cellular export receptor CRM 1 mediates function and intracellular localization of Epstein-Barr virus SM protein, a regulator of gene expression. J. Virol. 73:6872-6881.
    • (1999) J. Virol. , vol.73 , pp. 6872-6881
    • Boyle, S.M.1    Ruvolo, V.2    Gupta, A.K.3    Swaminathan, S.4
  • 9
    • 0037941647 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein mediates interferon-based anti-herpes simplex virus 1 effects
    • Chee, A. V., P. Lopez, P. P. Pandolfi, and B. Roizman. 2003. Promyelocytic leukemia protein mediates interferon-based anti-herpes simplex virus 1 effects. J. Virol. 77:7101-7105.
    • (2003) J. Virol. , vol.77 , pp. 7101-7105
    • Chee, A.V.1    Lopez, P.2    Pandolfi, P.P.3    Roizman, B.4
  • 10
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins
    • Chelbi-Alix, M. K., and H. de The. 1999. Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene 18:935-941.
    • (1999) Oncogene , vol.18 , pp. 935-941
    • Chelbi-Alix, M.K.1    De The, H.2
  • 11
    • 0035910046 scopus 로고    scopus 로고
    • Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus
    • Chin, K. C., and P. Cresswell. 2001. Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus. Proc. Natl. Acad. Sci. USA 98:15125-15130.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15125-15130
    • Chin, K.C.1    Cresswell, P.2
  • 12
    • 0022382345 scopus 로고
    • Localization of the coding region for an Epstein-Barr virus early antigen and inducible expression of this 60-kilodalton nuclear protein in transfected fibroblast cell lines
    • Cho, M. S., K. T. Jeang, and S. D. Hayward. 1985. Localization of the coding region for an Epstein-Barr virus early antigen and inducible expression of this 60-kilodalton nuclear protein in transfected fibroblast cell lines. J. Virol. 56:852-859.
    • (1985) J. Virol. , vol.56 , pp. 852-859
    • Cho, M.S.1    Jeang, K.T.2    Hayward, S.D.3
  • 13
    • 0030052130 scopus 로고    scopus 로고
    • Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure
    • Doucas, V., A. M. Ishov, A. Romo, H. Juguilon, M. D. Weitzman, R. M. Evans, and G. G. Maul. 1996. Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure. Genes Dev. 10:196-207.
    • (1996) Genes Dev. , vol.10 , pp. 196-207
    • Doucas, V.1    Ishov, A.M.2    Romo, A.3    Juguilon, H.4    Weitzman, M.D.5    Evans, R.M.6    Maul, G.G.7
  • 14
    • 0035969103 scopus 로고    scopus 로고
    • DNA viruses and viral proteins that interact with PML nuclear bodies
    • Everett, R. D. 2001. DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 20:7266-7273.
    • (2001) Oncogene , vol.20 , pp. 7266-7273
    • Everett, R.D.1
  • 15
    • 0031878851 scopus 로고    scopus 로고
    • The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms
    • Everett, R. D., P. Freemont, H. Saitoh, M. Dasso, A, Orr, M. Kathoria, and J. Parkinson. 1998. The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J. Virol. 72:6581-6591.
    • (1998) J. Virol. , vol.72 , pp. 6581-6591
    • Everett, R.D.1    Freemont, P.2    Saitoh, H.3    Dasso, M.4    Orr, A.5    Kathoria, M.6    Parkinson, J.7
  • 16
    • 0028039189 scopus 로고
    • HSV-1 IE protein Vmw110 causes redistribution of PML
    • Everett, R. D., and G. G. Maul. 1994. HSV-1 IE protein Vmw110 causes redistribution of PML. EMBO J. 13:5062-5069.
    • (1994) EMBO J. , vol.13 , pp. 5062-5069
    • Everett, R.D.1    Maul, G.G.2
  • 17
    • 0032127876 scopus 로고    scopus 로고
    • The APECED polyglandular autoimmune syndrome protein, AIRE-1, contains the SAND domain and is probably a transcription factor
    • Gibson, T. J., C. Ramu, C. Gemund, and R. Aasland. 1998. The APECED polyglandular autoimmune syndrome protein, AIRE-1, contains the SAND domain and is probably a transcription factor. Trends Biochem. Sci. 23:242-244.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 242-244
    • Gibson, T.J.1    Ramu, C.2    Gemund, C.3    Aasland, R.4
  • 18
    • 0029894340 scopus 로고    scopus 로고
    • Interferon-modulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML)
    • Grotzinger, T., T. Sternsdorf, K. Jensen, and H. Will. 1996. Interferon-modulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML). Eur. J. Biochem. 238:554-560.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 554-560
    • Grotzinger, T.1    Sternsdorf, T.2    Jensen, K.3    Will, H.4
  • 19
  • 20
    • 0027095906 scopus 로고
    • IFN enhance expression of Sp100, an autoantigen in primary biliary cirrhosis
    • Guldner, H. H., C. Szostecki, T. Grotzinger, and H. Will. 1992. IFN enhance expression of Sp100, an autoantigen in primary biliary cirrhosis. J. Immunol. 149:4067-4073.
    • (1992) J. Immunol. , vol.149 , pp. 4067-4073
    • Guldner, H.H.1    Szostecki, C.2    Grotzinger, T.3    Will, H.4
  • 21
    • 0037414768 scopus 로고    scopus 로고
    • A novel nuclear export signal and a REF interaction domain both promote mRNA export by the Epstein-Barr virus EB2 protein
    • Hiriart, E., G. Farjot, H. Gruffat, M. V. Nguyen, A. Sergeant, and E. Manet. 2003. A novel nuclear export signal and a REF interaction domain both promote mRNA export by the Epstein-Barr virus EB2 protein. J. Biol. Chem. 278:335-342.
    • (2003) J. Biol. Chem. , vol.278 , pp. 335-342
    • Hiriart, E.1    Farjot, G.2    Gruffat, H.3    Nguyen, M.V.4    Sergeant, A.5    Manet, E.6
  • 22
    • 0025269031 scopus 로고
    • Intervening sequences increase efficiency of RNA 3′ processing and accumulation of cytoplasmic RNA
    • Huang, M. T., and C. M. Gorman. 1990. Intervening sequences increase efficiency of RNA 3′ processing and accumulation of cytoplasmic RNA. Nucleic Acids Res. 18:937-947.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 937-947
    • Huang, M.T.1    Gorman, C.M.2
  • 23
    • 0029838230 scopus 로고    scopus 로고
    • The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition
    • Ishov, A. M., and G. G. Maul. 1996. The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition. J. Cell Biol. 134:815-826.
    • (1996) J. Cell Biol. , vol.134 , pp. 815-826
    • Ishov, A.M.1    Maul, G.G.2
  • 24
    • 0036310441 scopus 로고    scopus 로고
    • Daxx-mediated accumulation of human cytomegalovirus tegument protein pp71 at ND10 facilitates initiation of viral infection at these nuclear domains
    • Ishov, A. M., O. V. Vladimirova, and G. G. Maul. 2002. Daxx-mediated accumulation of human cytomegalovirus tegument protein pp71 at ND10 facilitates initiation of viral infection at these nuclear domains. J. Virol. 76:7705-7712.
    • (2002) J. Virol. , vol.76 , pp. 7705-7712
    • Ishov, A.M.1    Vladimirova, O.V.2    Maul, G.G.3
  • 25
    • 0027361282 scopus 로고
    • Molecular cloning of two new interferon-induced, highly related nuclear phosphoproteins
    • Kadereit, S., D. R. Gewert, J. Galabru, A. G. Hovanessian, and E. F. Meurs. 1993. Molecular cloning of two new interferon-induced, highly related nuclear phosphoproteins. J. Biol. Chem. 268:24432-24441.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24432-24441
    • Kadereit, S.1    Gewert, D.R.2    Galabru, J.3    Hovanessian, A.G.4    Meurs, E.F.5
  • 26
    • 0030602019 scopus 로고    scopus 로고
    • The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1
    • Korioth, F., G. G. Maul, B. Plachter, T. Stamminger, and J. Frey. 1996. The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1. Exp. Cell Res. 229:155-158.
    • (1996) Exp. Cell Res. , vol.229 , pp. 155-158
    • Korioth, F.1    Maul, G.G.2    Plachter, B.3    Stamminger, T.4    Frey, J.5
  • 27
    • 0032574737 scopus 로고    scopus 로고
    • Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body
    • LaMorte, V. J., J. A. Dyck, R. L. Ochs, and R. M. Evans. 1998. Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body. Proc. Natl. Acad. Sci. USA 95:4991-4996.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4991-4996
    • LaMorte, V.J.1    Dyck, J.A.2    Ochs, R.L.3    Evans, R.M.4
  • 29
    • 0033592896 scopus 로고    scopus 로고
    • Splicing is required for rapid and efficient mRNA export in metazoans
    • Luo, M. J., and R. Reed. 1999. Splicing is required for rapid and efficient mRNA export in metazoans. Proc. Natl. Acad. Sci. USA 96:14937-14942.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14937-14942
    • Luo, M.J.1    Reed, R.2
  • 30
    • 0032143446 scopus 로고    scopus 로고
    • Nuclear domain 10, the site of DNA virus transcription and replication
    • Maul, G. G. 1998. Nuclear domain 10, the site of DNA virus transcription and replication. Bioessays 20:660-667.
    • (1998) Bioessays , vol.20 , pp. 660-667
    • Maul, G.G.1
  • 31
    • 0028352769 scopus 로고
    • The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0
    • Maul, G. G., and R. D. Everett. 1994. The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0. J. Gen. Virol. 75:1223-1233.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1223-1233
    • Maul, G.G.1    Everett, R.D.2
  • 32
    • 0029862620 scopus 로고    scopus 로고
    • Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1
    • Maul, G. G., A. M. Ishov, and R. D. Everett. 1996. Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1. Virology 217:67-75.
    • (1996) Virology , vol.217 , pp. 67-75
    • Maul, G.G.1    Ishov, A.M.2    Everett, R.D.3
  • 33
    • 0016835245 scopus 로고
    • Establishment and characterization of an Epstein-Barr virus (EBV)-negative lymphoblastoid B cell line (BJA-B) from an exceptional EBV-genome-negative African Burkitt's lymphoma
    • Menezes, J., W. Liebold, G. Klein, and G. Clements. 1975. Establishment and characterization of an Epstein-Barr virus (EBV)-negative lymphoblastoid B cell line (BJA-B) from an exceptional EBV-genome-negative African Burkitt's lymphoma. Biomedicine 22:276-284.
    • (1975) Biomedicine , vol.22 , pp. 276-284
    • Menezes, J.1    Liebold, W.2    Klein, G.3    Clements, G.4
  • 35
    • 0031862729 scopus 로고    scopus 로고
    • Cytomegalovirus activates interferon immediate-early response gene expression and an interferon regulatory factor 3-containing interferon- stimulated response element-binding complex
    • Navarro, L., K. Mowen, S. Rodems, B. Weaver, N. Reich, D. Spector, and M. David. 1998. Cytomegalovirus activates interferon immediate-early response gene expression and an interferon regulatory factor 3-containing interferon-stimulated response element-binding complex. Mol. Cell. Biol. 18:3796-3802.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3796-3802
    • Navarro, L.1    Mowen, K.2    Rodems, S.3    Weaver, B.4    Reich, N.5    Spector, D.6    David, M.7
  • 36
    • 0020447692 scopus 로고
    • Non-immortalizing P3J-HR1 Epstein Barr virus: A deletion mutant of its transforming parent
    • Rabson, M., L. Gradoville, L. Heston, and G. Miller. 1982. Non-immortalizing P3J-HR1 Epstein Barr virus: a deletion mutant of its transforming parent, Jijoye. J. Virol. 48:834-844.
    • (1982) Jijoye. J. Virol. , vol.48 , pp. 834-844
    • Rabson, M.1    Gradoville, L.2    Heston, L.3    Miller, G.4
  • 37
    • 0034979001 scopus 로고    scopus 로고
    • Epstein-Barr virus SM protein interacts with mRNA in vivo and mediates a gene-specific increase in cytoplasmic mRNA
    • Ruvolo, V., A. K. Gupta, and S. Swaminathan. 2001. Epstein-Barr virus SM protein interacts with mRNA in vivo and mediates a gene-specific increase in cytoplasmic mRNA. J. Virol. 75:6033-6041.
    • (2001) J. Virol. , vol.75 , pp. 6033-6041
    • Ruvolo, V.1    Gupta, A.K.2    Swaminathan, S.3
  • 38
    • 0037334420 scopus 로고    scopus 로고
    • The Epstein-Barr virus SM protein induces STAT1 and interferon-stimulated gene expression
    • Ruvolo, V., L. Navarro, C. E. Sample, M. David, S. Sung, and S. Swaminathan. 2003. The Epstein-Barr virus SM protein induces STAT1 and interferon-stimulated gene expression. J. Virol. 77:3690-3701.
    • (2003) J. Virol. , vol.77 , pp. 3690-3701
    • Ruvolo, V.1    Navarro, L.2    Sample, C.E.3    David, M.4    Sung, S.5    Swaminathan, S.6
  • 39
    • 0346365296 scopus 로고    scopus 로고
    • Functional analysis of Epstein-Barr virus SM protein: Identification of amino acids essential for structure, transactivation, splicing inhibition, and virion production
    • Ruvolo, V., L. Sun, K. Howard, S. Sung, H. J. Delecluse, W. Hammerschmidt, and S. Swaminathan. 2004. Functional analysis of Epstein-Barr virus SM protein: identification of amino acids essential for structure, transactivation, splicing inhibition, and virion production. J. Virol. 78:340-352.
    • (2004) J. Virol. , vol.78 , pp. 340-352
    • Ruvolo, V.1    Sun, L.2    Howard, K.3    Sung, S.4    Delecluse, H.J.5    Hammerschmidt, W.6    Swaminathan, S.7
  • 40
    • 0032555233 scopus 로고    scopus 로고
    • The Epstein-Barr virus nuclear protein SM is both a posttranscriptional inhibitor and activator of gene expression
    • Ruvolo, V., E. Wang, S. Boyle, and S. Swaminathan. 1998. The Epstein-Barr virus nuclear protein SM is both a posttranscriptional inhibitor and activator of gene expression. Proc. Natl. Acad. Sci. USA 95:8852-8857.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8852-8857
    • Ruvolo, V.1    Wang, E.2    Boyle, S.3    Swaminathan, S.4
  • 41
    • 0032560477 scopus 로고    scopus 로고
    • Interaction of SP100 with HP1 proteins: A link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment
    • Seeler, J. S., A. Marchio, D. Sitterlin, C. Transy, and A. Dejean. 1998. Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment. Proc Natl. Acad. Sci. USA 95:7316-7321.
    • (1998) Proc Natl. Acad. Sci. USA , vol.95 , pp. 7316-7321
    • Seeler, J.S.1    Marchio, A.2    Sitterlin, D.3    Transy, C.4    Dejean, A.5
  • 42
    • 0031743482 scopus 로고    scopus 로고
    • Mta has properties of an RNA export protein and increases cytoplasmic accumulation of Epstein-Barr virus replication gene mRNA
    • Semmes, O. J., L. Chen, R. T. Sarisky, Z. Gao, L. Zhong, and S. D. Hayward. 1998. Mta has properties of an RNA export protein and increases cytoplasmic accumulation of Epstein-Barr virus replication gene mRNA. J. Virol. 72:9526-9534.
    • (1998) J. Virol. , vol.72 , pp. 9526-9534
    • Semmes, O.J.1    Chen, L.2    Sarisky, R.T.3    Gao, Z.4    Zhong, L.5    Hayward, S.D.6
  • 43
    • 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
  • 44
    • 0025726282 scopus 로고
    • An Epstein-Barr virus-producer line Akata: Establishment of the cell line and analysis of viral DNA
    • Takada, K., K. Horinouchi, Y. Ono, T. Aya, T. Osato, M. Takahashi, and S. Hayasaka. 1991. An Epstein-Barr virus-producer line Akata: establishment of the cell line and analysis of viral DNA. Virus Genes 5:147-156.
    • (1991) Virus Genes , vol.5 , pp. 147-156
    • Takada, K.1    Horinouchi, K.2    Ono, Y.3    Aya, T.4    Osato, T.5    Takahashi, M.6    Hayasaka, S.7
  • 45
    • 0024590981 scopus 로고
    • Synchronous and sequential activation of latently infected Epstein-Barr virus genomes
    • Takada, K., and Y. Ono. 1989. Synchronous and sequential activation of latently infected Epstein-Barr virus genomes. J. Virol. 63:445-449.
    • (1989) J. Virol. , vol.63 , pp. 445-449
    • Takada, K.1    Ono, Y.2
  • 46
    • 0142123224 scopus 로고    scopus 로고
    • Modulation of retinoid signaling by a cytoplasmic viral protein via sequestration of Sp110b, a potent transcriptional corepressor of retinoic acid receptor, from the nucleus
    • Watashi, K., M. Hijikata, A. Tagawa, T. Doi, H. Marusawa, and K. Shimotohno. 2003. Modulation of retinoid signaling by a cytoplasmic viral protein via sequestration of Sp110b, a potent transcriptional corepressor of retinoic acid receptor, from the nucleus. Mol. Cell. Biol. 23:7498-7509.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7498-7509
    • Watashi, K.1    Hijikata, M.2    Tagawa, A.3    Doi, T.4    Marusawa, H.5    Shimotohno, K.6
  • 47
    • 0035152285 scopus 로고    scopus 로고
    • Origin-independent assembly of Kaposi's sarcoma-associated herpesvirus DNA replication compartments in transient cotransfection assays and association with the open reading frame-K8 protein and cellular PML
    • Wu, F. Y., J. H. Ahn, D. J. Alcendor, W. J. Jang, J. Xiao, S. D. Hayward, and G. S. Hayward. 2001. Origin-independent assembly of Kaposi's sarcoma-associated herpesvirus DNA replication compartments in transient cotransfection assays and association with the open reading frame-K8 protein and cellular PML. J. Virol. 75:1487-1506.
    • (2001) J. Virol. , vol.75 , pp. 1487-1506
    • Wu, F.Y.1    Ahn, J.H.2    Alcendor, D.J.3    Jang, W.J.4    Xiao, J.5    Hayward, S.D.6    Hayward, G.S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.