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Volumn 111, Issue 1, 2014, Pages 243-248

Nucleolin is important for Epstein-Barr virus nuclear antigen 1-mediated episome binding, maintenance, and transcription

Author keywords

Chromatin; Lymphoma; Nasopharyngeal carcinoma; Oncogenic herpesvirus

Indexed keywords

ADENOSINE TRIPHOSPHATE; EPSTEIN BARR VIRUS ANTIGEN 1; NUCLEOLIN; SHORT HAIRPIN RNA; VIRUS DNA; VIRUS RNA;

EID: 84891934686     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1321800111     Document Type: Article
Times cited : (42)

References (44)
  • 1
    • 34250010253 scopus 로고    scopus 로고
    • Epstein-Barr virus and its replication
    • ed Knipe DaHP (Lippincott, Williams, and Wilkins, Philadelphia), 5th Ed
    • Kieff E, Rickinson AB (2007) Epstein-Barr virus and its replication. Fields Virology, ed Knipe DaHP (Lippincott, Williams, and Wilkins, Philadelphia), 5th Ed, Vol 2, pp 2603-2700.
    • (2007) Fields Virology , vol.2 , pp. 2603-2700
    • Kieff, E.1    Rickinson, A.B.2
  • 2
    • 0034698034 scopus 로고    scopus 로고
    • Two domains of the epstein-barr virus origin DNA-binding protein, EBNA1, orchestrate sequencespecific DNA binding
    • Cruickshank J, Shire K, Davidson AR, Edwards AM, Frappier L (2000) Two domains of the epstein-barr virus origin DNA-binding protein, EBNA1, orchestrate sequencespecific DNA binding. J Biol Chem 275(29): 22273-22277.
    • (2000) J Biol Chem , vol.275 , Issue.29 , pp. 22273-22277
    • Cruickshank, J.1    Shire, K.2    Davidson, A.R.3    Edwards, A.M.4    Frappier, L.5
  • 3
    • 0021993827 scopus 로고
    • A vector that replicates as a plasmid and can be efficiently selected in B-lymphoblasts transformed by Epstein-Barr virus
    • Sugden B, Marsh K, Yates J (1985) A vector that replicates as a plasmid and can be efficiently selected in B-lymphoblasts transformed by Epstein-Barr virus. Mol Cell Biol 5(2): 410-413.
    • (1985) Mol Cell Biol , vol.5 , Issue.2 , pp. 410-413
    • Sugden, B.1    Marsh, K.2    Yates, J.3
  • 4
    • 0021988550 scopus 로고
    • Stable replication of plasmids derived from Epstein-Barr virus in various mammalian cells
    • Yates JL, Warren N, Sugden B (1985) Stable replication of plasmids derived from Epstein-Barr virus in various mammalian cells. Nature 313(6005): 812-815.
    • (1985) Nature , vol.313 , Issue.6005 , pp. 812-815
    • Yates, J.L.1    Warren, N.2    Sugden, B.3
  • 5
    • 84876439615 scopus 로고    scopus 로고
    • EBNA1 and host factors in Epstein-Barr virus latent DNA replication
    • Frappier L (2012) EBNA1 and host factors in Epstein-Barr virus latent DNA replication. Curr Opin Virol 2(6): 733-739.
    • (2012) Curr Opin Virol , vol.2 , Issue.6 , pp. 733-739
    • Frappier, L.1
  • 6
    • 0026004036 scopus 로고
    • Epstein-Barr virus-derived plasmids replicate only once per cell cycle and are not amplified after entry into cells
    • Yates JL, Guan N (1991) Epstein-Barr virus-derived plasmids replicate only once per cell cycle and are not amplified after entry into cells. J Virol 65(1): 483-488.
    • (1991) J Virol , vol.65 , Issue.1 , pp. 483-488
    • Yates, J.L.1    Guan, N.2
  • 7
    • 0037634447 scopus 로고    scopus 로고
    • The spacing between adjacent binding sites in the family of repeats affects the functions of Epstein-Barr nuclear antigen 1 in transcription activation and stable plasmid maintenance
    • Hebner C, Lasanen J, Battle S, Aiyar A (2003) The spacing between adjacent binding sites in the family of repeats affects the functions of Epstein-Barr nuclear antigen 1 in transcription activation and stable plasmid maintenance. Virology 311(2): 263-274.
    • (2003) Virology , vol.311 , Issue.2 , pp. 263-274
    • Hebner, C.1    Lasanen, J.2    Battle, S.3    Aiyar, A.4
  • 8
    • 0022134525 scopus 로고
    • Sequence-specific DNA binding of the Epstein-Barr virus nuclear antigen (EBNA-1) to clustered sites in the plasmid maintenance region
    • Rawlins DR, Milman G, Hayward SD, Hayward GS (1985) Sequence-specific DNA binding of the Epstein-Barr virus nuclear antigen (EBNA-1) to clustered sites in the plasmid maintenance region. Cell 42(3): 859-868.
    • (1985) Cell , vol.42 , Issue.3 , pp. 859-868
    • Rawlins, D.R.1    Milman, G.2    Hayward, S.D.3    Hayward, G.S.4
  • 9
    • 84867026753 scopus 로고    scopus 로고
    • Contributions of Epstein-Barr nuclear antigen 1 (EBNA1) to cell immortalization and survival
    • Frappier L (2012) Contributions of Epstein-Barr nuclear antigen 1 (EBNA1) to cell immortalization and survival. Viruses 4(9): 1537-1547.
    • (2012) Viruses , vol.4 , Issue.9 , pp. 1537-1547
    • Frappier, L.1
  • 10
    • 0034252499 scopus 로고    scopus 로고
    • The DNA segregation mechanism of Epstein- Barr virus nuclear antigen 1
    • Wu H, Ceccarelli DF, Frappier L (2000) The DNA segregation mechanism of Epstein- Barr virus nuclear antigen 1. EMBO Rep 1(2): 140-144.
    • (2000) EMBO Rep , vol.1 , Issue.2 , pp. 140-144
    • Wu, H.1    Ceccarelli, D.F.2    Frappier, L.3
  • 11
    • 33749039167 scopus 로고    scopus 로고
    • Transcriptional activation by EBV nuclear antigen 1 is essential for the expression of EBV's transforming genes
    • Altmann M, et al. (2006) Transcriptional activation by EBV nuclear antigen 1 is essential for the expression of EBV's transforming genes. Proc Natl Acad Sci USA 103(38): 14188-14193.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.38 , pp. 14188-14193
    • Altmann, M.1
  • 12
    • 0034122511 scopus 로고    scopus 로고
    • Functional analyses of the EBNA1 origin DNA binding protein of Epstein-Barr virus
    • Ceccarelli DF, Frappier L (2000) Functional analyses of the EBNA1 origin DNA binding protein of Epstein-Barr virus. J Virol 74(11): 4939-4948.
    • (2000) J Virol , vol.74 , Issue.11 , pp. 4939-4948
    • Ceccarelli, D.F.1    Frappier, L.2
  • 13
    • 67650901947 scopus 로고    scopus 로고
    • Zinc coordination is required for and regulates transcription activation by Epstein-Barr nuclear antigen 1
    • Aras S, Singh G, Johnston K, Foster T, Aiyar A (2009) Zinc coordination is required for and regulates transcription activation by Epstein-Barr nuclear antigen 1. PLoS Pathog 5(6):e1000469.
    • (2009) PLoS Pathog , vol.5 , Issue.6
    • Aras, S.1    Singh, G.2    Johnston, K.3    Foster, T.4    Aiyar, A.5
  • 14
    • 34249934410 scopus 로고    scopus 로고
    • Chromatin profiling of Epstein-Barr virus latency control region
    • Day L, et al. (2007) Chromatin profiling of Epstein-Barr virus latency control region. J Virol 81(12): 6389-6401.
    • (2007) J Virol , vol.81 , Issue.12 , pp. 6389-6401
    • Day, L.1
  • 15
    • 57349095971 scopus 로고    scopus 로고
    • The EBNA1 protein of Epstein-Barr virus functionally interacts with Brd4
    • Lin A, Wang S, Nguyen T, Shire K, Frappier L (2008) The EBNA1 protein of Epstein-Barr virus functionally interacts with Brd4. J Virol 82(24): 12009-12019.
    • (2008) J Virol , vol.82 , Issue.24 , pp. 12009-12019
    • Lin, A.1    Wang, S.2    Nguyen, T.3    Shire, K.4    Frappier, L.5
  • 16
    • 70350277265 scopus 로고    scopus 로고
    • Nucleosome assembly proteins bind to Epstein-Barr virus nuclear antigen 1 and affect its functions in DNA replication and transcriptional activation
    • Wang S, Frappier L (2009) Nucleosome assembly proteins bind to Epstein-Barr virus nuclear antigen 1 and affect its functions in DNA replication and transcriptional activation. J Virol 83(22): 11704-11714.
    • (2009) J Virol , vol.83 , Issue.22 , pp. 11704-11714
    • Wang, S.1    Frappier, L.2
  • 17
    • 0025265082 scopus 로고
    • Identification of major nucleolar proteins as candidate mitotic substrates of cdc2 kinase
    • Peter M, Nakagawa J, Dorée M, Labbé JC, Nigg EA (1990) Identification of major nucleolar proteins as candidate mitotic substrates of cdc2 kinase. Cell 60(5): 791-801.
    • (1990) Cell , vol.60 , Issue.5 , pp. 791-801
    • Peter, M.1    Nakagawa, J.2    Dorée, M.3    Labbé, J.C.4    Nigg, E.A.5
  • 18
    • 33646164896 scopus 로고    scopus 로고
    • Nucleolin is a histone chaperone with FACT-like activity and assists remodeling of nucleosomes
    • Angelov D, et al. (2006) Nucleolin is a histone chaperone with FACT-like activity and assists remodeling of nucleosomes. EMBO J 25(8): 1669-1679.
    • (2006) EMBO J , vol.25 , Issue.8 , pp. 1669-1679
    • Angelov, D.1
  • 19
    • 79960091417 scopus 로고    scopus 로고
    • Nucleolin: The most abundant multifunctional phosphoprotein of nucleolus
    • Tajrishi MM, Tuteja R, Tuteja N (2011) Nucleolin: The most abundant multifunctional phosphoprotein of nucleolus. Commun Integr Biol 4(3): 267-275.
    • (2011) Commun Integr Biol , vol.4 , Issue.3 , pp. 267-275
    • Tajrishi, M.M.1    Tuteja, R.2    Tuteja, N.3
  • 20
    • 0032921853 scopus 로고    scopus 로고
    • Structure and functions of nucleolin
    • Ginisty H, Sicard H, Roger B, Bouvet P (1999) Structure and functions of nucleolin. J Cell Sci 112(Pt 6): 761-772.
    • (1999) J Cell Sci , vol.112 , Issue.PART 6 , pp. 761-772
    • Ginisty, H.1    Sicard, H.2    Roger, B.3    Bouvet, P.4
  • 21
    • 0038585032 scopus 로고    scopus 로고
    • Deletion and site-specific mutagenesis of nucleolin's carboxy GAR domain
    • Pellar GJ, DiMario PJ (2003) Deletion and site-specific mutagenesis of nucleolin's carboxy GAR domain. Chromosoma 111(7): 461-469.
    • (2003) Chromosoma , vol.111 , Issue.7 , pp. 461-469
    • Pellar, G.J.1    Dimario, P.J.2
  • 22
    • 33846681638 scopus 로고    scopus 로고
    • Nucleolin: A multiFACeTed protein
    • Mongelard F, Bouvet P (2007) Nucleolin: A multiFACeTed protein. Trends Cell Biol 17(2): 80-86.
    • (2007) Trends Cell Biol , vol.17 , Issue.2 , pp. 80-86
    • Mongelard, F.1    Bouvet, P.2
  • 23
    • 33746277552 scopus 로고    scopus 로고
    • Structure and function of the nucleolus in the spotlight
    • Raska I, Shaw PJ, Cmarko D (2006) Structure and function of the nucleolus in the spotlight. Curr Opin Cell Biol 18(3): 325-334.
    • (2006) Curr Opin Cell Biol , vol.18 , Issue.3 , pp. 325-334
    • Raska, I.1    Shaw, P.J.2    Cmarko, D.3
  • 24
    • 0034635474 scopus 로고    scopus 로고
    • Nucleolin, a novel partner for the Myb transcription factor family that regulates their activity
    • Ying GG, et al. (2000) Nucleolin, a novel partner for the Myb transcription factor family that regulates their activity. J Biol Chem 275(6): 4152-4158.
    • (2000) J Biol Chem , vol.275 , Issue.6 , pp. 4152-4158
    • Ying, G.G.1
  • 25
    • 0030887616 scopus 로고    scopus 로고
    • Nucleolin is one component of the B cell-specific transcription factor and switch region binding protein, LR1
    • Hanakahi LA, Dempsey LA, Li MJ, Maizels N (1997) Nucleolin is one component of the B cell-specific transcription factor and switch region binding protein, LR1. Proc Natl Acad Sci USA 94(8): 3605-3610.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.8 , pp. 3605-3610
    • Hanakahi, L.A.1    Dempsey, L.A.2    Li, M.J.3    Maizels, N.4
  • 26
    • 0037152165 scopus 로고    scopus 로고
    • Nucleolin as activator of human papillomavirus type 18 oncogene transcription in cervical cancer
    • Grinstein E, et al. (2002) Nucleolin as activator of human papillomavirus type 18 oncogene transcription in cervical cancer. J Exp Med 196(8): 1067-1078.
    • (2002) J Exp Med , vol.196 , Issue.8 , pp. 1067-1078
    • Grinstein, E.1
  • 27
    • 0029962298 scopus 로고    scopus 로고
    • C23 interacts with B23, a putative nucleolar- localization-signal-binding protein
    • Li YP, Busch RK, Valdez BC, Busch H (1996) C23 interacts with B23, a putative nucleolar- localization-signal-binding protein. Eur J Biochem 237(1): 153-158.
    • (1996) Eur J Biochem , vol.237 , Issue.1 , pp. 153-158
    • Li, Y.P.1    Busch, R.K.2    Valdez, B.C.3    Busch, H.4
  • 28
    • 47549091537 scopus 로고    scopus 로고
    • Playing both sides: Nucleophosmin between tumor suppression and oncogenesis
    • Di Fiore PP (2008) Playing both sides: Nucleophosmin between tumor suppression and oncogenesis. J Cell Biol 182(1): 7-9.
    • (2008) J Cell Biol , vol.182 , Issue.1 , pp. 7-9
    • Di Fiore, P.P.1
  • 29
    • 84855992367 scopus 로고    scopus 로고
    • EGCG debilitates the persistence of EBV latency by reducing the DNA binding potency of nuclear antigen 1
    • Chen YL, Tsai HL, Peng CW (2012) EGCG debilitates the persistence of EBV latency by reducing the DNA binding potency of nuclear antigen 1. Biochem Biophys Res Commun 417(3): 1093-1099.
    • (2012) Biochem Biophys Res Commun , vol.417 , Issue.3 , pp. 1093-1099
    • Chen, Y.L.1    Tsai, H.L.2    Peng, C.W.3
  • 30
    • 0015499229 scopus 로고
    • Separation of Epstein-Barr virus DNA from large chromosomal DNA in non-virus-producing cells
    • Nonoyama M, Pagano JS (1972) Separation of Epstein-Barr virus DNA from large chromosomal DNA in non-virus-producing cells. Nat New Biol 238(84): 169-171.
    • (1972) Nat New Biol , vol.238 , Issue.84 , pp. 169-171
    • Nonoyama, M.1    Pagano, J.S.2
  • 31
    • 84886634930 scopus 로고
    • Covalently closed circular duplex DNA of Epstein-Barr virus in a human lymphoid cell line
    • Lindahl T, et al. (1976) Covalently closed circular duplex DNA of Epstein-Barr virus in a human lymphoid cell line. J Mol Biol 102(3): 511-530.
    • (1976) J Mol Biol , vol.102 , Issue.3 , pp. 511-530
    • Lindahl, T.1
  • 32
    • 0028924512 scopus 로고
    • The murine nucleolin protein is an inducible DNA and ATP binding protein which is readily detected in nuclear extracts of lipopolysaccharide- treated splenocytes
    • Miranda GA, Chokler I, Aguilera RJ (1995) The murine nucleolin protein is an inducible DNA and ATP binding protein which is readily detected in nuclear extracts of lipopolysaccharide- treated splenocytes. Exp Cell Res 217(2): 294-308.
    • (1995) Exp Cell Res , vol.217 , Issue.2 , pp. 294-308
    • Miranda, G.A.1    Chokler, I.2    Aguilera, R.J.3
  • 33
    • 0034067252 scopus 로고    scopus 로고
    • Synthesis and activity of pyrrolidinyl- and thiazolidinyl-dipeptide derivatives as inhibitors of the Tc80 prolyl oligopeptidase from Trypanosoma cruzi
    • Joyeau R, et al. (2000) Synthesis and activity of pyrrolidinyl- and thiazolidinyl-dipeptide derivatives as inhibitors of the Tc80 prolyl oligopeptidase from Trypanosoma cruzi. Eur J Med Chem 35(2): 257-266.
    • (2000) Eur J Med Chem , vol.35 , Issue.2 , pp. 257-266
    • Joyeau, R.1
  • 34
    • 0033966236 scopus 로고    scopus 로고
    • Reversal activity of the naturally occurring chemosensitizer malagashanine in Plasmodium malaria
    • Rafatro H, et al. (2000) Reversal activity of the naturally occurring chemosensitizer malagashanine in Plasmodium malaria. Biochem Pharmacol 59(9): 1053-1061.
    • (2000) Biochem Pharmacol , vol.59 , Issue.9 , pp. 1053-1061
    • Rafatro, H.1
  • 36
    • 0242331744 scopus 로고    scopus 로고
    • Telomere repeat binding factors TRF1, TRF2, and hRAP1 modulate replication of Epstein-Barr virus OriP
    • Deng Z, Atanasiu C, Burg JS, Broccoli D, Lieberman PM (2003) Telomere repeat binding factors TRF1, TRF2, and hRAP1 modulate replication of Epstein-Barr virus OriP. J Virol 77(22): 11992-12001.
    • (2003) J Virol , vol.77 , Issue.22 , pp. 11992-12001
    • Deng, Z.1    Atanasiu, C.2    Burg, J.S.3    Broccoli, D.4    Lieberman, P.M.5
  • 37
    • 84863617583 scopus 로고    scopus 로고
    • Epstein-Barr nuclear antigen 1 (EBNA1)-dependent recruitment of origin recognition complex (Orc) on oriP of Epstein-Barr virus with purified proteins: Stimulation by Cdc6 through its direct interaction with EBNA1
    • Moriyama K, Yoshizawa-Sugata N, Obuse C, Tsurimoto T, Masai H (2012) Epstein-Barr nuclear antigen 1 (EBNA1)-dependent recruitment of origin recognition complex (Orc) on oriP of Epstein-Barr virus with purified proteins: Stimulation by Cdc6 through its direct interaction with EBNA1. J Biol Chem 287(28): 23977-23994.
    • (2012) J Biol Chem , vol.287 , Issue.28 , pp. 23977-23994
    • Moriyama, K.1    Yoshizawa-Sugata, N.2    Obuse, C.3    Tsurimoto, T.4    Masai, H.5
  • 38
    • 73449097872 scopus 로고    scopus 로고
    • EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replication
    • Sarkari F, et al. (2009) EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replication. PLoS Pathog 5(10):e1000624.
    • (2009) PLoS Pathog , vol.5 , Issue.10
    • Sarkari, F.1
  • 39
    • 75449116596 scopus 로고    scopus 로고
    • Nucleolin is required for efficient nuclear egress of herpes simplex virus type 1 nucleocapsids
    • Sagou K, Uema M, Kawaguchi Y (2010) Nucleolin is required for efficient nuclear egress of herpes simplex virus type 1 nucleocapsids. J Virol 84(4): 2110-2121.
    • (2010) J Virol , vol.84 , Issue.4 , pp. 2110-2121
    • Sagou, K.1    Uema, M.2    Kawaguchi, Y.3
  • 40
    • 75449093392 scopus 로고    scopus 로고
    • Nucleolin associates with the human cytomegalovirus DNA polymerase accessory subunit UL44 and is necessary for efficient viral replication
    • Strang BL, Boulant S, Coen DM (2010) Nucleolin associates with the human cytomegalovirus DNA polymerase accessory subunit UL44 and is necessary for efficient viral replication. J Virol 84(4): 1771-1784.
    • (2010) J Virol , vol.84 , Issue.4 , pp. 1771-1784
    • Strang, B.L.1    Boulant, S.2    Coen, D.M.3
  • 41
    • 33746782535 scopus 로고    scopus 로고
    • Cell cycle-controlled interaction of nucleolin with the retinoblastoma protein and cancerous cell transformation
    • Grinstein E, et al. (2006) Cell cycle-controlled interaction of nucleolin with the retinoblastoma protein and cancerous cell transformation. J Biol Chem 281(31): 22223-22235.
    • (2006) J Biol Chem , vol.281 , Issue.31 , pp. 22223-22235
    • Grinstein, E.1
  • 42
    • 84867239122 scopus 로고    scopus 로고
    • The requirement of c-Jun N-terminal kinase 2 in regulation of hypoxia-inducing factor-1α mRNA stability
    • Zhang D, et al. (2012) The requirement of c-Jun N-terminal kinase 2 in regulation of hypoxia-inducing factor-1α mRNA stability. J Biol Chem 287(41): 34361-34371.
    • (2012) J Biol Chem , vol.287 , Issue.41 , pp. 34361-34371
    • Zhang, D.1
  • 43
    • 84881054800 scopus 로고    scopus 로고
    • Nucleolin inhibits Fas ligand binding and suppresses Fas-mediated apoptosis in vivo via a surface nucleolin-Fas complex
    • Wise JF, et al. (2013) Nucleolin inhibits Fas ligand binding and suppresses Fas-mediated apoptosis in vivo via a surface nucleolin-Fas complex. Blood 121(23): 4729-4739.
    • (2013) Blood , vol.121 , Issue.23 , pp. 4729-4739
    • Wise, J.F.1
  • 44
    • 84879585408 scopus 로고    scopus 로고
    • In vivo NCL targeting affects breast cancer aggressiveness through miRNA regulation
    • Pichiorri F, et al. (2013) In vivo NCL targeting affects breast cancer aggressiveness through miRNA regulation. J Exp Med 210(5): 951-968.
    • (2013) J Exp Med , vol.210 , Issue.5 , pp. 951-968
    • Pichiorri, F.1


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