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Volumn 12, Issue 1, 2016, Pages

EBNA3C Directs Recruitment of RBPJ (CBF1) to Chromatin during the Process of Gene Repression in EBV Infected B Cells

Author keywords

[No Author keywords available]

Indexed keywords

EPSTEIN BARR NUCLEAR PROTEIN EBNA3C; NOTCH RECEPTOR; RECOMBINATION SIGNAL BINDING PROTEIN J; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; VIRUS PROTEIN; CHROMATIN; EBNA-3C, EPSTEIN-BARR VIRUS; EPSTEIN BARR VIRUS ANTIGEN; IMMUNOGLOBULIN J RECOMBINATION SIGNAL SEQUENCE BINDING PROTEIN; RBPJ PROTEIN, HUMAN;

EID: 84956815097     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1005383     Document Type: Article
Times cited : (21)

References (99)
  • 1
    • 4944266319 scopus 로고    scopus 로고
    • Epstein–Barr virus: 40 years on
    • Young LS, Rickinson AB, Epstein–Barr virus: 40 years on. Nat Rev Cancer. 2004;4: 757–768. doi: 10.1038/nrc1452 15510157
    • (2004) Nat Rev Cancer , vol.4 , pp. 757-768
    • Young, L.S.1    Rickinson, A.B.2
  • 2
    • 33645745240 scopus 로고    scopus 로고
    • Spectrum of Epstein-Barr virus-associated diseases
    • Kutok JL, Wang F, Spectrum of Epstein-Barr virus-associated diseases. Annu Rev Pathol. 2006;1: 375–404. doi: 10.1146/annurev.pathol.1.110304.100209 18039120
    • (2006) Annu Rev Pathol , vol.1 , pp. 375-404
    • Kutok, J.L.1    Wang, F.2
  • 3
    • 77649188072 scopus 로고    scopus 로고
    • Cellular factors associated with latency and spontaneous Epstein-Barr virus reactivation in B-lymphoblastoid cell lines
    • Davies ML, Xu S, Lyons-Weiler J, Rosendorff A, Webber SA, Wasil LR, et al. Cellular factors associated with latency and spontaneous Epstein-Barr virus reactivation in B-lymphoblastoid cell lines. Virology. 2010;400: 53–67. doi: 10.1016/j.virol.2010.01.002 20153012
    • (2010) Virology , vol.400 , pp. 53-67
    • Davies, M.L.1    Xu, S.2    Lyons-Weiler, J.3    Rosendorff, A.4    Webber, S.A.5    Wasil, L.R.6
  • 4
    • 18144395736 scopus 로고    scopus 로고
    • Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of the 20S proteasome and are degraded by 20S proteasomes in vitro, but are very stable in latently infected B cells
    • Touitou R, O'Nions J, Heaney J, Allday MJ, Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of the 20S proteasome and are degraded by 20S proteasomes in vitro, but are very stable in latently infected B cells. J Gen Virol. 2005;86: 1269–1277. doi: 10.1099/vir.0.80763–0 15831937
    • (2005) J Gen Virol , vol.86 , pp. 1269-1277
    • Touitou, R.1    O'Nions, J.2    Heaney, J.3    Allday, M.J.4
  • 5
    • 70049083050 scopus 로고    scopus 로고
    • Differential gene expression patterns of EBV infected EBNA-3A positive and negative human B lymphocytes
    • Hertle ML, Popp C, Petermann S, Maier S, Kremmer E, Lang R, et al. Differential gene expression patterns of EBV infected EBNA-3A positive and negative human B lymphocytes. PLoS Pathog. 2009;5: e1000506. doi: 10.1371/journal.ppat.1000506 19578441
    • (2009) PLoS Pathog , vol.5 , pp. 1000506
    • Hertle, M.L.1    Popp, C.2    Petermann, S.3    Maier, S.4    Kremmer, E.5    Lang, R.6
  • 6
    • 78649746843 scopus 로고    scopus 로고
    • Extensive Co-Operation between the Epstein-Barr Virus EBNA3 Proteins in the Manipulation of Host Gene Expression and Epigenetic Chromatin Modification
    • White RE, Kremmer E, Allday MJ, Masucci MG, Extensive Co-Operation between the Epstein-Barr Virus EBNA3 Proteins in the Manipulation of Host Gene Expression and Epigenetic Chromatin Modification. PLoS ONE. 2010;5: e13979. doi: 10.1371/journal.pone.0013979.t001 21085583
    • (2010) PLoS ONE , vol.5 , pp. 13979
    • White, R.E.1    Kremmer, E.2    Allday, M.J.3    Masucci, M.G.4
  • 7
    • 78651099289 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C regulated genes in lymphoblastoid cell lines
    • Zhao B, Mar JC, Maruo S, Lee S, Gewurz BE, Johannsen E, et al. Epstein-Barr virus nuclear antigen 3C regulated genes in lymphoblastoid cell lines. Proc Natl Acad Sci USA. 2011;108: 337–342. doi: 10.1073/pnas.1017419108 21173222
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 337-342
    • Zhao, B.1    Mar, J.C.2    Maruo, S.3    Lee, S.4    Gewurz, B.E.5    Johannsen, E.6
  • 8
    • 0028903431 scopus 로고
    • Epstein-Barr virus nuclear protein 3C modulates transcription through interaction with the sequence-specific DNA-binding protein J kappa
    • Robertson ES, Grossman S, Johannsen E, Miller C, Lin J, Tomkinson B, et al. Epstein-Barr virus nuclear protein 3C modulates transcription through interaction with the sequence-specific DNA-binding protein J kappa. Journal of Virology. 1995;69: 3108–3116. 7707539
    • (1995) Journal of Virology , vol.69 , pp. 3108-3116
    • Robertson, E.S.1    Grossman, S.2    Johannsen, E.3    Miller, C.4    Lin, J.5    Tomkinson, B.6
  • 9
    • 0029990265 scopus 로고    scopus 로고
    • The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B, and 3C interact with RBPJ(kappa)
    • Robertson ES, Lin J, Kieff E, The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B, and 3C interact with RBPJ(kappa). Journal of Virology. 1996;70: 3068–3074. 8627785
    • (1996) Journal of Virology , vol.70 , pp. 3068-3074
    • Robertson, E.S.1    Lin, J.2    Kieff, E.3
  • 10
    • 0030589480 scopus 로고    scopus 로고
    • Epstein-Barr nuclear antigen-3 and -4 interact with RBP-2N, a major isoform of RBP-J kappa in B lymphocytes
    • Krauer KG, Kienzle N, Young DB, Sculley TB, Epstein-Barr nuclear antigen-3 and -4 interact with RBP-2N, a major isoform of RBP-J kappa in B lymphocytes. Virology. 1996;226: 346–353. doi: 10.1006/viro.1996.0662 8955054
    • (1996) Virology , vol.226 , pp. 346-353
    • Krauer, K.G.1    Kienzle, N.2    Young, D.B.3    Sculley, T.B.4
  • 11
    • 0029974216 scopus 로고    scopus 로고
    • A conserved domain of the Epstein-Barr virus nuclear antigens 3A and 3C binds to a discrete domain of Jkappa
    • Zhao B, Marshall DR, Sample CE, A conserved domain of the Epstein-Barr virus nuclear antigens 3A and 3C binds to a discrete domain of Jkappa. Journal of Virology. 1996;70: 4228–4236. 8676443
    • (1996) Journal of Virology , vol.70 , pp. 4228-4236
    • Zhao, B.1    Marshall, D.R.2    Sample, C.E.3
  • 12
    • 0029013590 scopus 로고
    • Epstein-Barr virus nuclear antigen 3C is a transcriptional regulator
    • Marshall D, Sample C, Epstein-Barr virus nuclear antigen 3C is a transcriptional regulator. Journal of Virology. 1995;69: 3624–3630. 7745710
    • (1995) Journal of Virology , vol.69 , pp. 3624-3630
    • Marshall, D.1    Sample, C.2
  • 13
    • 33747623018 scopus 로고    scopus 로고
    • Notch signalling: a simple pathway becomes complex
    • Bray SJ, Notch signalling: a simple pathway becomes complex. Nat Rev Mol Cell Biol. Nature Publishing Group; 2006;7: 678–689. doi: 10.1038/nrm2009 16921404
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 678-689
    • Bray, S.J.1
  • 14
    • 84879870498 scopus 로고    scopus 로고
    • Notch signaling at a glance
    • Hori K, Sen A, Artavanis-Tsakonas S, Notch signaling at a glance. J Cell Sci. The Company of Biologists Ltd; 2013;126: 2135–2140. doi: 10.1242/jcs.127308 23729744
    • (2013) J Cell Sci , vol.126 , pp. 2135-2140
    • Hori, K.1    Sen, A.2    Artavanis-Tsakonas, S.3
  • 15
    • 2642601104 scopus 로고    scopus 로고
    • The mammalian transcriptional repressor RBP (CBF1) targets TFIID and TFIIA to prevent activated transcription
    • Olave I, Reinberg D, Vales LD, The mammalian transcriptional repressor RBP (CBF1) targets TFIID and TFIIA to prevent activated transcription. Genes Dev. Cold Spring Harbor Laboratory Press; 1998;12: 1621–1637. 9620850
    • (1998) Genes Dev , vol.12 , pp. 1621-1637
    • Olave, I.1    Reinberg, D.2    Vales, L.D.3
  • 16
    • 0032145527 scopus 로고    scopus 로고
    • A histone deacetylase corepressor complex regulates the Notch signal transduction pathway
    • Kao HY, Ordentlich P, Koyano-Nakagawa N, Tang Z, Downes M, Kintner CR, et al. A histone deacetylase corepressor complex regulates the Notch signal transduction pathway. Genes Dev. Cold Spring Harbor Laboratory Press; 1998;12: 2269–2277. 9694793
    • (1998) Genes Dev , vol.12 , pp. 2269-2277
    • Kao, H.Y.1    Ordentlich, P.2    Koyano-Nakagawa, N.3    Tang, Z.4    Downes, M.5    Kintner, C.R.6
  • 17
    • 0033524444 scopus 로고    scopus 로고
    • CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex
    • Hsieh JJ, Zhou S, Chen L, Young DB, Hayward SD, CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex. Proc Natl Acad Sci USA. National Academy of Sciences; 1999;96: 23–28. 9874765
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 23-28
    • Hsieh, J.J.1    Zhou, S.2    Chen, L.3    Young, D.B.4    Hayward, S.D.5
  • 18
    • 18644368822 scopus 로고    scopus 로고
    • SHARP is a novel component of the Notch/RBP-Jkappa signalling pathway
    • Oswald F, Kostezka U, Astrahantseff K, Bourteele S, Dillinger K, Zechner U, et al. SHARP is a novel component of the Notch/RBP-Jkappa signalling pathway. EMBO J. European Molecular Biology Organization; 2002;21: 5417–5426. doi: 10.1093/emboj/cdf549 12374742
    • (2002) EMBO J , vol.21 , pp. 5417-5426
    • Oswald, F.1    Kostezka, U.2    Astrahantseff, K.3    Bourteele, S.4    Dillinger, K.5    Zechner, U.6
  • 19
    • 27944491856 scopus 로고    scopus 로고
    • RBP-Jkappa/SHARP recruits CtIP/CtBP corepressors to silence Notch target genes
    • Oswald F, Winkler M, Cao Y, Astrahantseff K, Bourteele S, Knöchel W, et al. RBP-Jkappa/SHARP recruits CtIP/CtBP corepressors to silence Notch target genes. Mol Cell Biol. American Society for Microbiology; 2005;25: 10379–10390. doi: 10.1128/MCB.25.23.10379–10390.2005 16287852
    • (2005) Mol Cell Biol , vol.25 , pp. 10379-10390
    • Oswald, F.1    Winkler, M.2    Cao, Y.3    Astrahantseff, K.4    Bourteele, S.5    Knöchel, W.6
  • 20
    • 0031983193 scopus 로고    scopus 로고
    • LIM protein KyoT2 negatively regulates transcription by association with the RBP-J DNA-binding protein
    • Taniguchi Y, Furukawa T, Tun T, Han H, Honjo T, LIM protein KyoT2 negatively regulates transcription by association with the RBP-J DNA-binding protein. Mol Cell Biol. American Society for Microbiology (ASM); 1998;18: 644–654. 9418910
    • (1998) Mol Cell Biol , vol.18 , pp. 644-654
    • Taniguchi, Y.1    Furukawa, T.2    Tun, T.3    Han, H.4    Honjo, T.5
  • 21
    • 0034671686 scopus 로고    scopus 로고
    • Notch signaling: from the outside in
    • Mumm JS, Kopan R, Notch signaling: from the outside in. Dev Biol. 2000;228: 151–165. doi: 10.1006/dbio.2000.9960 11112321
    • (2000) Dev Biol , vol.228 , pp. 151-165
    • Mumm, J.S.1    Kopan, R.2
  • 22
    • 0036727125 scopus 로고    scopus 로고
    • Gamma-secretase-mediated proteolysis in cell-surface-receptor signalling
    • Fortini ME, Gamma-secretase-mediated proteolysis in cell-surface-receptor signalling. Nat Rev Mol Cell Biol. Nature Publishing Group; 2002;3: 673–684. doi: 10.1038/nrm910 12209127
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 673-684
    • Fortini, M.E.1
  • 23
    • 0041355557 scopus 로고    scopus 로고
    • Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration
    • Selkoe D, Kopan R, Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration. Annu Rev Neurosci. Annual Reviews 4139 El Camino Way, P.O. Box 10139, Palo Alto, CA 94303–0139, USA; 2003;26: 565–597. doi: 10.1146/annurev.neuro.26.041002.131334 12730322
    • (2003) Annu Rev Neurosci , vol.26 , pp. 565-597
    • Selkoe, D.1    Kopan, R.2
  • 24
    • 0029583607 scopus 로고
    • Physical interaction between a novel domain of the receptor Notch and the transcription factor RBP-J kappa/Su(H)
    • Tamura K, Taniguchi Y, Minoguchi S, Sakai T, Tun T, Furukawa T, et al. Physical interaction between a novel domain of the receptor Notch and the transcription factor RBP-J kappa/Su(H). Curr Biol. 1995;5: 1416–1423. 8749394
    • (1995) Curr Biol , vol.5 , pp. 1416-1423
    • Tamura, K.1    Taniguchi, Y.2    Minoguchi, S.3    Sakai, T.4    Tun, T.5    Furukawa, T.6
  • 25
    • 0027291722 scopus 로고
    • Control of cell fate in C. elegans by a GLP-1 peptide consisting primarily of ankyrin repeats
    • Roehl H, Kimble J, Control of cell fate in C. elegans by a GLP-1 peptide consisting primarily of ankyrin repeats. Nature. Nature Publishing Group; 1993;364: 632–635. doi: 10.1038/364632a0 8350921
    • (1993) Nature , vol.364 , pp. 632-635
    • Roehl, H.1    Kimble, J.2
  • 26
    • 0030782174 scopus 로고    scopus 로고
    • Involvement of RBP-J in biological functions of mouse Notch1 and its derivatives
    • Kato H, Taniguchi Y, Kurooka H, Minoguchi S, Sakai T, Nomura-Okazaki S, et al. Involvement of RBP-J in biological functions of mouse Notch1 and its derivatives. Development. 1997;124: 4133–4141. 9374409
    • (1997) Development , vol.124 , pp. 4133-4141
    • Kato, H.1    Taniguchi, Y.2    Kurooka, H.3    Minoguchi, S.4    Sakai, T.5    Nomura-Okazaki, S.6
  • 27
    • 0032403190 scopus 로고    scopus 로고
    • Roles of the ankyrin repeats and C-terminal region of the mouse notch1 intracellular region
    • Kurooka H, Kuroda K, Honjo T, Roles of the ankyrin repeats and C-terminal region of the mouse notch1 intracellular region. Nucleic Acids Research. Oxford University Press; 1998;26: 5448–5455. 9826771
    • (1998) Nucleic Acids Research , vol.26 , pp. 5448-5455
    • Kurooka, H.1    Kuroda, K.2    Honjo, T.3
  • 28
    • 0034682337 scopus 로고    scopus 로고
    • LAG-3 is a putative transcriptional activator in the C. elegans Notch pathway
    • Petcherski AG, Kimble J, LAG-3 is a putative transcriptional activator in the C. elegans Notch pathway. Nature. Nature Publishing Group; 2000;405: 364–368. doi: 10.1038/35012645
    • (2000) Nature. Nature Publishing Group , vol.405 , pp. 364-368
    • Petcherski, A.G.1    Kimble, J.2
  • 29
    • 0034729722 scopus 로고    scopus 로고
    • Mastermind is a putative activator for Notch
    • Petcherski AG, Kimble J, Mastermind is a putative activator for Notch. Curr Biol. 2000;10: R471–3. 10898989
    • (2000) Curr Biol , vol.10 , pp. 471-473
    • Petcherski, A.G.1    Kimble, J.2
  • 30
    • 0033662392 scopus 로고    scopus 로고
    • MAML1, a human homologue of Drosophila mastermind, is a transcriptional co-activator for NOTCH receptors
    • Wu L, Aster JC, Blacklow SC, Lake R, Artavanis-Tsakonas S, Griffin JD, MAML1, a human homologue of Drosophila mastermind, is a transcriptional co-activator for NOTCH receptors. Nat Genet. 2000;26: 484–489. doi: 10.1038/82644 11101851
    • (2000) Nat Genet , vol.26 , pp. 484-489
    • Wu, L.1    Aster, J.C.2    Blacklow, S.C.3    Lake, R.4    Artavanis-Tsakonas, S.5    Griffin, J.D.6
  • 31
    • 0028124316 scopus 로고
    • The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the J kappa recombination signal binding protein
    • Grossman SR, Johannsen E, Tong X, Yalamanchili R, Kieff E, The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the J kappa recombination signal binding protein. Proc Natl Acad Sci USA. 1994;91: 7568–7572. 8052621
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7568-7572
    • Grossman, S.R.1    Johannsen, E.2    Tong, X.3    Yalamanchili, R.4    Kieff, E.5
  • 32
    • 0028133036 scopus 로고
    • Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa
    • Henkel T, Ling PD, Hayward SD, Peterson MG, Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa. Science. 1994;265: 92–95. 8016657
    • (1994) Science , vol.265 , pp. 92-95
    • Henkel, T.1    Ling, P.D.2    Hayward, S.D.3    Peterson, M.G.4
  • 33
    • 0028171081 scopus 로고
    • The human J kappa recombination signal sequence binding protein (RBP-J kappa) targets the Epstein-Barr virus EBNA2 protein to its DNA responsive elements
    • Waltzer L, Logeat F, Brou C, Israel A, Sergeant A, Manet E, The human J kappa recombination signal sequence binding protein (RBP-J kappa) targets the Epstein-Barr virus EBNA2 protein to its DNA responsive elements. EMBO J. European Molecular Biology Organization; 1994;13: 5633–5638. 7988560
    • (1994) EMBO J , vol.13 , pp. 5633-5638
    • Waltzer, L.1    Logeat, F.2    Brou, C.3    Israel, A.4    Sergeant, A.5    Manet, E.6
  • 34
    • 0028063483 scopus 로고
    • Epstein-Barr virus nuclear antigen 2 exerts its transactivating function through interaction with recombination signal binding protein RBP-J kappa, the homologue of Drosophila Suppressor of Hairless
    • Zimber-Strobl U, Strobl LJ, Meitinger C, Hinrichs R, Sakai T, Furukawa T, et al. Epstein-Barr virus nuclear antigen 2 exerts its transactivating function through interaction with recombination signal binding protein RBP-J kappa, the homologue of Drosophila Suppressor of Hairless. EMBO J. European Molecular Biology Organization; 1994;13: 4973–4982. 7957063
    • (1994) EMBO J , vol.13 , pp. 4973-4982
    • Zimber-Strobl, U.1    Strobl, L.J.2    Meitinger, C.3    Hinrichs, R.4    Sakai, T.5    Furukawa, T.6
  • 35
    • 0035200379 scopus 로고    scopus 로고
    • EBNA2 and Notch signalling in Epstein-Barr virus mediated immortalization of B lymphocytes
    • Zimber-Strobl U, Strobl LJ, EBNA2 and Notch signalling in Epstein-Barr virus mediated immortalization of B lymphocytes. Semin Cancer Biol. 2001;11: 423–434. doi: 10.1006/scbi.2001.0409 11669604
    • (2001) Semin Cancer Biol , vol.11 , pp. 423-434
    • Zimber-Strobl, U.1    Strobl, L.J.2
  • 36
    • 0029948549 scopus 로고    scopus 로고
    • EBNA-2 and EBNA-3C extensively and mutually exclusively associate with RBPJkappa in Epstein-Barr virus-transformed B lymphocytes
    • Johannsen E, Miller CL, Grossman SR, Kieff E, EBNA-2 and EBNA-3C extensively and mutually exclusively associate with RBPJkappa in Epstein-Barr virus-transformed B lymphocytes. Journal of Virology. American Society for Microbiology (ASM); 1996;70: 4179–4183. 8648764
    • (1996) Journal of Virology , vol.70 , pp. 4179-4183
    • Johannsen, E.1    Miller, C.L.2    Grossman, S.R.3    Kieff, E.4
  • 37
    • 0029843985 scopus 로고    scopus 로고
    • Epstein-Barr virus EBNA3A and EBNA3C proteins both repress RBP-J kappa-EBNA2-activated transcription by inhibiting the binding of RBP-J kappa to DNA
    • Waltzer L, Perricaudet M, Sergeant A, Manet E, Epstein-Barr virus EBNA3A and EBNA3C proteins both repress RBP-J kappa-EBNA2-activated transcription by inhibiting the binding of RBP-J kappa to DNA. Journal of Virology. 1996;70: 5909–5915. 8709211
    • (1996) Journal of Virology , vol.70 , pp. 5909-5915
    • Waltzer, L.1    Perricaudet, M.2    Sergeant, A.3    Manet, E.4
  • 38
    • 0028076871 scopus 로고
    • The Epstein-Barr virus determined nuclear antigens EBNA-3A, -3B, and -3C repress EBNA-2-mediated transactivation of the viral terminal protein 1 gene promoter
    • Le Roux A, Kerdiles B, Walls D, Dedieu JF, Perricaudet M, The Epstein-Barr virus determined nuclear antigens EBNA-3A, -3B, and -3C repress EBNA-2-mediated transactivation of the viral terminal protein 1 gene promoter. Virology. 1994;205: 596–602. doi: 10.1006/viro.1994.1687 7975264
    • (1994) Virology , vol.205 , pp. 596-602
    • Le Roux, A.1    Kerdiles, B.2    Walls, D.3    Dedieu, J.F.4    Perricaudet, M.5
  • 39
    • 0030821170 scopus 로고    scopus 로고
    • Epstein-Barr virus EBNA3C represses Cp, the major promoter for EBNA expression, but has no effect on the promoter of the cell gene CD21
    • Radkov SA, Bain M, Farrell PJ, West M, Rowe M, Allday MJ, Epstein-Barr virus EBNA3C represses Cp, the major promoter for EBNA expression, but has no effect on the promoter of the cell gene CD21. Journal of Virology. 1997;71: 8552–8562. 9343213
    • (1997) Journal of Virology , vol.71 , pp. 8552-8562
    • Radkov, S.A.1    Bain, M.2    Farrell, P.J.3    West, M.4    Rowe, M.5    Allday, M.J.6
  • 40
    • 63149180521 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear protein EBNA3C residues critical for maintaining lymphoblastoid cell growth
    • Maruo S, Wu Y, Ito T, Kanda T, Kieff ED, Takada K, Epstein-Barr virus nuclear protein EBNA3C residues critical for maintaining lymphoblastoid cell growth. Proc Natl Acad Sci USA. 2009;106: 4419–4424. doi: 10.1073/pnas.0813134106 19237563
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4419-4424
    • Maruo, S.1    Wu, Y.2    Ito, T.3    Kanda, T.4    Kieff, E.D.5    Takada, K.6
  • 41
    • 70450237781 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear protein 3C domains necessary for lymphoblastoid cell growth: interaction with RBP-Jkappa regulates TCL1
    • Lee S, Sakakibara S, Maruo S, Zhao B, Calderwood MA, Holthaus AM, et al. Epstein-Barr virus nuclear protein 3C domains necessary for lymphoblastoid cell growth: interaction with RBP-Jkappa regulates TCL1. Journal of Virology. American Society for Microbiology; 2009;83: 12368–12377. doi: 10.1128/JVI.01403-09 19776126
    • (2009) Journal of Virology , vol.83 , pp. 12368-12377
    • Lee, S.1    Sakakibara, S.2    Maruo, S.3    Zhao, B.4    Calderwood, M.A.5    Holthaus, A.M.6
  • 42
    • 79955532721 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear protein 3C binds to the N-terminal (NTD) and beta trefoil domains (BTD) of RBP/CSL; only the NTD interaction is essential for lymphoblastoid cell growth
    • Calderwood MA, Lee S, Holthaus AM, Blacklow SC, Kieff E, Johannsen E, Epstein-Barr virus nuclear protein 3C binds to the N-terminal (NTD) and beta trefoil domains (BTD) of RBP/CSL; only the NTD interaction is essential for lymphoblastoid cell growth. Virology. 2011;414: 19–25. doi: 10.1016/j.virol.2011.02.018 21440926
    • (2011) Virology , vol.414 , pp. 19-25
    • Calderwood, M.A.1    Lee, S.2    Holthaus, A.M.3    Blacklow, S.C.4    Kieff, E.5    Johannsen, E.6
  • 43
    • 3342964330 scopus 로고    scopus 로고
    • Viral interactions with the Notch pathway
    • Hayward SD, Viral interactions with the Notch pathway. Semin Cancer Biol. 2004;14: 387–396. doi: 10.1016/j.semcancer.2004.04.018 15288264
    • (2004) Semin Cancer Biol , vol.14 , pp. 387-396
    • Hayward, S.D.1
  • 44
    • 33744793492 scopus 로고    scopus 로고
    • Notch and Wnt signaling: mimicry and manipulation by gamma herpesviruses
    • Hayward SD, Liu J, Fujimuro M, Notch and Wnt signaling: mimicry and manipulation by gamma herpesviruses. Sci STKE. Science Signaling; 2006;2006: re4–re4. doi: 10.1126/stke.3352006re4 16705130
    • (2006) Sci STKE , vol.2006 , pp. 4
    • Hayward, S.D.1    Liu, J.2    Fujimuro, M.3
  • 45
    • 84884692313 scopus 로고    scopus 로고
    • Inactivation of Intergenic Enhancers by EBNA3A Initiates and Maintains Polycomb Signatures across a Chromatin Domain Encoding CXCL10 and CXCL9
    • Harth-Hertle ML, Scholz BA, Erhard F, Glaser LV, Dölken L, Zimmer R, et al. Inactivation of Intergenic Enhancers by EBNA3A Initiates and Maintains Polycomb Signatures across a Chromatin Domain Encoding CXCL10 and CXCL9. PLoS Pathog. 2013;9: e1003638. doi: 10.1371/journal.ppat.1003638 24068939
    • (2013) PLoS Pathog , vol.9 , pp. 1003638
    • Harth-Hertle, M.L.1    Scholz, B.A.2    Erhard, F.3    Glaser, L.V.4    Dölken, L.5    Zimmer, R.6
  • 46
    • 0029960796 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C is a powerful repressor of transcription when tethered to DNA
    • Bain M, Watson RJ, Farrell PJ, Allday MJ, Epstein-Barr virus nuclear antigen 3C is a powerful repressor of transcription when tethered to DNA. Journal of Virology. 1996;70: 2481–2489. 8642676
    • (1996) Journal of Virology , vol.70 , pp. 2481-2489
    • Bain, M.1    Watson, R.J.2    Farrell, P.J.3    Allday, M.J.4
  • 47
    • 0031964949 scopus 로고    scopus 로고
    • Transcriptional repression by the Epstein-Barr virus EBNA3A protein tethered to DNA does not require RBP-Jkappa
    • Bourillot PY, Waltzer L, Sergeant A, Manet E, Transcriptional repression by the Epstein-Barr virus EBNA3A protein tethered to DNA does not require RBP-Jkappa. J Gen Virol. 1998;79 (Pt 2): 363–370. 9472621
    • (1998) J Gen Virol , vol.79 , pp. 363-370
    • Bourillot, P.Y.1    Waltzer, L.2    Sergeant, A.3    Manet, E.4
  • 48
    • 0032991714 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C interacts with histone deacetylase to repress transcription
    • Radkov SA, Touitou R, Brehm A, Rowe M, West M, Kouzarides T, et al. Epstein-Barr virus nuclear antigen 3C interacts with histone deacetylase to repress transcription. Journal of Virology. 1999;73: 5688–5697. 10364319
    • (1999) Journal of Virology , vol.73 , pp. 5688-5697
    • Radkov, S.A.1    Touitou, R.2    Brehm, A.3    Rowe, M.4    West, M.5    Kouzarides, T.6
  • 49
    • 0037378585 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C recruits histone deacetylase activity and associates with the corepressors mSin3A and NCoR in human B-cell lines
    • Knight JS, Lan K, Subramanian C, Robertson ES, Epstein-Barr virus nuclear antigen 3C recruits histone deacetylase activity and associates with the corepressors mSin3A and NCoR in human B-cell lines. Journal of Virology. 2003;77: 4261–4272. 12634383
    • (2003) Journal of Virology , vol.77 , pp. 4261-4272
    • Knight, J.S.1    Lan, K.2    Subramanian, C.3    Robertson, E.S.4
  • 50
    • 0034910721 scopus 로고    scopus 로고
    • Physical and functional interactions between the corepressor CtBP and the Epstein-Barr virus nuclear antigen EBNA3C
    • Touitou R, Hickabottom M, Parker G, Crook T, Allday MJ, Physical and functional interactions between the corepressor CtBP and the Epstein-Barr virus nuclear antigen EBNA3C. Journal of Virology. American Society for Microbiology; 2001;75: 7749–7755. doi: 10.1128/JVI.75.16.7749–7755.2001 11462050
    • (2001) Journal of Virology , vol.75 , pp. 7749-7755
    • Touitou, R.1    Hickabottom, M.2    Parker, G.3    Crook, T.4    Allday, M.J.5
  • 51
    • 84861304914 scopus 로고    scopus 로고
    • Downregulation of Integrin Receptor-Signaling Genes by Epstein-Barr Virus EBNA 3C via Promoter-Proximal and -Distal Binding Elements
    • McClellan MJ, Khasnis S, Wood CD, Palermo RD, Schlick SN, Kanhere AS, et al. Downregulation of Integrin Receptor-Signaling Genes by Epstein-Barr Virus EBNA 3C via Promoter-Proximal and -Distal Binding Elements. Journal of Virology. 2012;86: 5165–5178. doi: 10.1128/JVI.07161-11 22357270
    • (2012) Journal of Virology , vol.86 , pp. 5165-5178
    • McClellan, M.J.1    Khasnis, S.2    Wood, C.D.3    Palermo, R.D.4    Schlick, S.N.5    Kanhere, A.S.6
  • 52
    • 84874772161 scopus 로고    scopus 로고
    • Induction of p16(INK4a) is the major barrier to proliferation when Epstein-Barr virus (EBV) transforms primary B cells into lymphoblastoid cell lines
    • Skalska L, White RE, Parker GA, Sinclair AJ, Paschos K, Allday MJ, Induction of p16(INK4a) is the major barrier to proliferation when Epstein-Barr virus (EBV) transforms primary B cells into lymphoblastoid cell lines. PLoS Pathog. 2013;9: e1003187. doi: 10.1371/journal.ppat.1003187 23436997
    • (2013) PLoS Pathog , vol.9 , pp. 1003187
    • Skalska, L.1    White, R.E.2    Parker, G.A.3    Sinclair, A.J.4    Paschos, K.5    Allday, M.J.6
  • 53
    • 84884685804 scopus 로고    scopus 로고
    • Modulation of enhancer looping and differential gene targeting by epstein-barr virus transcription factors directs cellular reprogramming
    • McClellan MJ, Wood CD, Ojeniyi O, Cooper TJ, Kanhere A, Arvey A, et al. Modulation of enhancer looping and differential gene targeting by epstein-barr virus transcription factors directs cellular reprogramming. PLoS Pathog. 2013;9: e1003636. doi: 10.1371/journal.ppat.1003636 24068937
    • (2013) PLoS Pathog , vol.9 , pp. 1003636
    • McClellan, M.J.1    Wood, C.D.2    Ojeniyi, O.3    Cooper, T.J.4    Kanhere, A.5    Arvey, A.6
  • 54
    • 38349057842 scopus 로고    scopus 로고
    • Two Epstein–Barr virus (EBV) oncoproteins cooperate to repress expression of the proapoptotic tumour-suppressor Bim: clues to the pathogenesis of Burkitt's lymphoma
    • Anderton E, Yee J, Smith P, Crook T, White RE, Allday MJ, Two Epstein–Barr virus (EBV) oncoproteins cooperate to repress expression of the proapoptotic tumour-suppressor Bim: clues to the pathogenesis of Burkitt's lymphoma. Oncogene. 2007;27: 421–433. doi: 10.1038/sj.onc.1210668 17653091
    • (2007) Oncogene , vol.27 , pp. 421-433
    • Anderton, E.1    Yee, J.2    Smith, P.3    Crook, T.4    White, R.E.5    Allday, M.J.6
  • 55
    • 77954664053 scopus 로고    scopus 로고
    • Epigenetic Repression of p16INK4A by Latent Epstein-Barr Virus Requires the Interaction of EBNA3A and EBNA3C with CtBP
    • Skalska L, White RE, Allday MJ, Speck SH, Epigenetic Repression of p16INK4A by Latent Epstein-Barr Virus Requires the Interaction of EBNA3A and EBNA3C with CtBP. PLoS Pathog. 2010;6: e1000951. doi: 10.1371/journal.ppat.1000951.g010 20548956
    • (2010) PLoS Pathog , vol.6 , pp. 1000951
    • Skalska, L.1    White, R.E.2    Allday, M.J.3    Speck, S.H.4
  • 56
    • 84938790848 scopus 로고    scopus 로고
    • Epstein-Barr Virus Proteins EBNA3A and EBNA3C Together Induce Expression of the Oncogenic MicroRNA Cluster miR-221/miR-222 and Ablate Expression of Its Target p57KIP2
    • Bazot Q, Paschos K, Skalska L, Kalchschmidt JS, Parker GA, Allday MJ, Flemington EK, Epstein-Barr Virus Proteins EBNA3A and EBNA3C Together Induce Expression of the Oncogenic MicroRNA Cluster miR-221/miR-222 and Ablate Expression of Its Target p57KIP2. PLoS Pathog. Public Library of Science; 2015;11: e1005031. doi: 10.1371/journal.ppat.1005031 26153983
    • (2015) PLoS Pathog , vol.11 , pp. 1005031
    • Bazot, Q.1    Paschos, K.2    Skalska, L.3    Kalchschmidt, J.S.4    Parker, G.A.5    Allday, M.J.6    Flemington, E.K.7
  • 57
    • 84867288340 scopus 로고    scopus 로고
    • BIM promoter directly targeted by EBNA3C in polycomb-mediated repression by EBV
    • Paschos K, Parker GA, Watanatanasup E, White RE, Allday MJ, BIM promoter directly targeted by EBNA3C in polycomb-mediated repression by EBV. Nucleic Acids Research. 2012;40: 7233–7246. doi: 10.1093/nar/gks391 22584624
    • (2012) Nucleic Acids Research , vol.40 , pp. 7233-7246
    • Paschos, K.1    Parker, G.A.2    Watanatanasup, E.3    White, R.E.4    Allday, M.J.5
  • 58
    • 0017329178 scopus 로고
    • Establishment in continuous culture of a new type of lymphocyte from a “Burkitt like” malignant lymphoma (line D.G.-75)
    • Ben-Bassat H, Goldblum N, Mitrani S, Goldblum T, Yoffey JM, Cohen MM, et al. Establishment in continuous culture of a new type of lymphocyte from a “Burkitt like” malignant lymphoma (line D.G.-75). Int J Cancer. 1977;19: 27–33. 188769
    • (1977) Int J Cancer , vol.19 , pp. 27-33
    • Ben-Bassat, H.1    Goldblum, N.2    Mitrani, S.3    Goldblum, T.4    Yoffey, J.M.5    Cohen, M.M.6
  • 59
    • 0027456839 scopus 로고
    • Epstein-Barr virus (EBV) nuclear antigen 6 induces expression of the EBV latent membrane protein and an activated phenotype in Raji cells
    • Allday MJ, Crawford DH, Thomas JA, Epstein-Barr virus (EBV) nuclear antigen 6 induces expression of the EBV latent membrane protein and an activated phenotype in Raji cells. J Gen Virol. 1993;74 (Pt 3): 361–369. 8383171
    • (1993) J Gen Virol , vol.74 , pp. 361-369
    • Allday, M.J.1    Crawford, D.H.2    Thomas, J.A.3
  • 60
    • 21644471586 scopus 로고    scopus 로고
    • A somatic knockout of CBF1 in a human B-cell line reveals that induction of CD21 and CCR7 by EBNA-2 is strictly CBF1 dependent and that downregulation of immunoglobulin M is partially CBF1 independent
    • Maier S, Santak M, Mantik A, Grabusic K, Kremmer E, Hammerschmidt W, et al. A somatic knockout of CBF1 in a human B-cell line reveals that induction of CD21 and CCR7 by EBNA-2 is strictly CBF1 dependent and that downregulation of immunoglobulin M is partially CBF1 independent. Journal of Virology. American Society for Microbiology; 2005;79: 8784–8792. doi: 10.1128/JVI.79.14.8784–8792.2005 15994772
    • (2005) Journal of Virology , vol.79 , pp. 8784-8792
    • Maier, S.1    Santak, M.2    Mantik, A.3    Grabusic, K.4    Kremmer, E.5    Hammerschmidt, W.6
  • 61
    • 84869096429 scopus 로고    scopus 로고
    • NOTCH1 nuclear interactome reveals key regulators of its transcriptional activity and oncogenic function
    • Yatim A, Benne C, Sobhian B, Laurent-Chabalier S, Deas O, Judde J-G, et al. NOTCH1 nuclear interactome reveals key regulators of its transcriptional activity and oncogenic function. Mol Cell. 2012;48: 445–458. doi: 10.1016/j.molcel.2012.08.022 23022380
    • (2012) Mol Cell , vol.48 , pp. 445-458
    • Yatim, A.1    Benne, C.2    Sobhian, B.3    Laurent-Chabalier, S.4    Deas, O.5    Judde, J.-G.6
  • 62
    • 34249886282 scopus 로고    scopus 로고
    • Notch activation stimulates transient and selective binding of Su(H)/CSL to target enhancers
    • Krejcí A, Bray S, Notch activation stimulates transient and selective binding of Su(H)/CSL to target enhancers. Genes Dev. 2007;21: 1322–1327. doi: 10.1101/gad.424607 17545467
    • (2007) Genes Dev , vol.21 , pp. 1322-1327
    • Krejcí, A.1    Bray, S.2
  • 64
    • 79956348321 scopus 로고    scopus 로고
    • EBV nuclear antigen EBNALP dismisses transcription repressors NCoR and RBPJ from enhancers and EBNA2 increases NCoR-deficient RBPJ DNA binding
    • Portal D, Zhao B, Calderwood MA, Sommermann T, Johannsen E, Kieff E, EBV nuclear antigen EBNALP dismisses transcription repressors NCoR and RBPJ from enhancers and EBNA2 increases NCoR-deficient RBPJ DNA binding. Proc Natl Acad Sci USA. National Acad Sciences; 2011;108: 7808–7813. doi: 10.1073/pnas.1104991108 21518914
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 7808-7813
    • Portal, D.1    Zhao, B.2    Calderwood, M.A.3    Sommermann, T.4    Johannsen, E.5    Kieff, E.6
  • 65
    • 0036190875 scopus 로고    scopus 로고
    • PROMO: detection of known transcription regulatory elements using species-tailored searches
    • Messeguer X, Escudero R, Farré D, Núñez O, Martínez J, Albà MM, PROMO: detection of known transcription regulatory elements using species-tailored searches. Bioinformatics. 2002;18: 333–334. 11847087
    • (2002) Bioinformatics , vol.18 , pp. 333-334
    • Messeguer, X.1    Escudero, R.2    Farré, D.3    Núñez, O.4    Martínez, J.5    Albà, M.M.6
  • 66
    • 0042622245 scopus 로고    scopus 로고
    • Identification of patterns in biological sequences at the ALGGEN server: PROMO and MALGEN
    • Farré D, Roset R, Huerta M, Adsuara JE, Roselló L, Albà MM, et al. Identification of patterns in biological sequences at the ALGGEN server: PROMO and MALGEN. Nucleic Acids Research. Oxford University Press; 2003;31: 3651–3653. 12824386
    • (2003) Nucleic Acids Research , vol.31 , pp. 3651-3653
    • Farré, D.1    Roset, R.2    Huerta, M.3    Adsuara, J.E.4    Roselló, L.5    Albà, M.M.6
  • 67
    • 84891940137 scopus 로고    scopus 로고
    • Epstein-Barr Virus Nuclear Antigen 3C binds to BATF/IRF4 or SPI1/IRF4 composite sites and recruits Sin3A to repress CDKN2A
    • Jiang S, Willox B, Zhou H, Holthaus AM, Wang A, Shi TT, et al. Epstein-Barr Virus Nuclear Antigen 3C binds to BATF/IRF4 or SPI1/IRF4 composite sites and recruits Sin3A to repress CDKN2A. Proc Natl Acad Sci USA. 2013. doi: 10.1073/pnas.1321704111
    • (2013) Proc Natl Acad Sci USA
    • Jiang, S.1    Willox, B.2    Zhou, H.3    Holthaus, A.M.4    Wang, A.5    Shi, T.T.6
  • 68
    • 84920973039 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3A partially coincides with EBNA3C genome-wide and is tethered to DNA through BATF complexes
    • Schmidt SCS, Jiang S, Zhou H, Willox B, Holthaus AM, Kharchenko PV, et al. Epstein-Barr virus nuclear antigen 3A partially coincides with EBNA3C genome-wide and is tethered to DNA through BATF complexes. Proc Natl Acad Sci USA. National Acad Sciences; 2014;: 201422580. doi: 10.1073/pnas.1422580112
    • (2014) Proc Natl Acad Sci USA , pp. 201422580
    • Schmidt, S.C.S.1    Jiang, S.2    Zhou, H.3    Willox, B.4    Holthaus, A.M.5    Kharchenko, P.V.6
  • 69
    • 84861322316 scopus 로고    scopus 로고
    • Carboxyl-terminal amino acids 1052 to 1082 of the latency-associated nuclear antigen (LANA) interact with RBP-Jκ and are responsible for LANA-mediated RTA repression
    • Jin Y, He Z, Liang D, Zhang Q, Zhang H, Deng Q, et al. Carboxyl-terminal amino acids 1052 to 1082 of the latency-associated nuclear antigen (LANA) interact with RBP-Jκ and are responsible for LANA-mediated RTA repression. Journal of Virology. American Society for Microbiology; 2012;86: 4956–4969. doi: 10.1128/JVI.06788-11 22379075
    • (2012) Journal of Virology , vol.86 , pp. 4956-4969
    • Jin, Y.1    He, Z.2    Liang, D.3    Zhang, Q.4    Zhang, H.5    Deng, Q.6
  • 70
    • 84897470888 scopus 로고    scopus 로고
    • RBPJ, the major transcriptional effector of Notch signaling, remains associated with chromatin throughout mitosis, suggesting a role in mitotic bookmarking
    • Lake RJ, Tsai P-F, Choi I, Won K-J, Fan H-Y, Fortini M, RBPJ, the major transcriptional effector of Notch signaling, remains associated with chromatin throughout mitosis, suggesting a role in mitotic bookmarking. PLoS Genet. Public Library of Science; 2014;10: e1004204. doi: 10.1371/journal.pgen.1004204
    • (2014) PLoS Genet. Public Library of Science , vol.10 , pp. 1004204
    • Lake, R.J.1    Tsai, P.-F.2    Choi, I.3    Won, K.-J.4    Fan, H.-Y.5    Fortini, M.6
  • 71
    • 84946836475 scopus 로고    scopus 로고
    • Histone acetyltransferases and histone deacetylases in B- and T-cell development, physiology and malignancy
    • Haery L, Thompson RC, Gilmore TD, Histone acetyltransferases and histone deacetylases in B- and T-cell development, physiology and malignancy. Genes Cancer. Impact Journals, LLC; 2015;6: 184–213. 26124919
    • (2015) Genes Cancer , vol.6 , pp. 184-213
    • Haery, L.1    Thompson, R.C.2    Gilmore, T.D.3
  • 72
    • 33947302685 scopus 로고    scopus 로고
    • The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases
    • Iwase S, Lan F, Bayliss P, la Torre-Ubieta de L, Huarte M, Qi HH, et al. The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases. Cell. 2007;128: 1077–1088. doi: 10.1016/j.cell.2007.02.017 17320160
    • (2007) Cell , vol.128 , pp. 1077-1088
    • Iwase, S.1    Lan, F.2    Bayliss, P.3    la Torre-Ubieta de, L.4    Huarte, M.5    Qi, H.H.6
  • 73
    • 33947245128 scopus 로고    scopus 로고
    • RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3
    • Christensen J, Agger K, Cloos PAC, Pasini D, Rose S, Sennels L, et al. RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3. Cell. 2007;128: 1063–1076. doi: 10.1016/j.cell.2007.02.003 17320161
    • (2007) Cell , vol.128 , pp. 1063-1076
    • Christensen, J.1    Agger, K.2    Cloos, P.A.C.3    Pasini, D.4    Rose, S.5    Sennels, L.6
  • 74
    • 33847401344 scopus 로고    scopus 로고
    • The retinoblastoma binding protein RBP2 is an H3K4 demethylase
    • Klose RJ, Yan Q, Tothova Z, Yamane K, Erdjument-Bromage H, Tempst P, et al. The retinoblastoma binding protein RBP2 is an H3K4 demethylase. Cell. 2007;128: 889–900. doi: 10.1016/j.cell.2007.02.013 17320163
    • (2007) Cell , vol.128 , pp. 889-900
    • Klose, R.J.1    Yan, Q.2    Tothova, Z.3    Yamane, K.4    Erdjument-Bromage, H.5    Tempst, P.6
  • 75
    • 33847383585 scopus 로고    scopus 로고
    • Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein
    • Lee MG, Norman J, Shilatifard A, Shiekhattar R, Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein. Cell. 2007;128: 877–887. doi: 10.1016/j.cell.2007.02.004 17320162
    • (2007) Cell , vol.128 , pp. 877-887
    • Lee, M.G.1    Norman, J.2    Shilatifard, A.3    Shiekhattar, R.4
  • 76
    • 34249900454 scopus 로고    scopus 로고
    • The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation
    • Tahiliani M, Mei P, Fang R, Leonor T, Rutenberg M, Shimizu F, et al. The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation. Nature. Nature Publishing Group; 2007;447: 601–605. doi: 10.1038/nature05823
    • (2007) Nature. Nature Publishing Group , vol.447 , pp. 601-605
    • Tahiliani, M.1    Mei, P.2    Fang, R.3    Leonor, T.4    Rutenberg, M.5    Shimizu, F.6
  • 77
    • 84860215207 scopus 로고    scopus 로고
    • Molecular mechanisms and potential functions of histone demethylases
    • Kooistra SM, Helin K, Molecular mechanisms and potential functions of histone demethylases. Nat Rev Mol Cell Biol. Nature Publishing Group; 2012;13: 297–311. doi: 10.1038/nrm3327 22473470
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 297-311
    • Kooistra, S.M.1    Helin, K.2
  • 79
    • 78650722823 scopus 로고    scopus 로고
    • Physiological roles of class I HDAC complex and histone demethylase
    • Hayakawa T, Nakayama J-I, Physiological roles of class I HDAC complex and histone demethylase. J Biomed Biotechnol. Hindawi Publishing Corporation; 2011;2011: 129383–10. doi: 10.1155/2011/129383 21049000
    • (2011) J Biomed Biotechnol , vol.2011 , pp. 129310-129383
    • Hayakawa, T.1    Nakayama, J.-I.2
  • 80
    • 33746407708 scopus 로고    scopus 로고
    • Recruitment of PRC1 function at the initiation of X inactivation independent of PRC2 and silencing
    • Schoeftner S, Sengupta AK, Kubicek S, Mechtler K, Spahn L, Koseki H, et al. Recruitment of PRC1 function at the initiation of X inactivation independent of PRC2 and silencing. EMBO J. EMBO Press; 2006;25: 3110–3122. doi: 10.1038/sj.emboj.7601187 16763550
    • (2006) EMBO J , vol.25 , pp. 3110-3122
    • Schoeftner, S.1    Sengupta, A.K.2    Kubicek, S.3    Mechtler, K.4    Spahn, L.5    Koseki, H.6
  • 81
    • 34248169728 scopus 로고    scopus 로고
    • The polycomb group protein Suz12 is required for embryonic stem cell differentiation
    • Pasini D, Bracken AP, Hansen JB, Capillo M, Helin K, The polycomb group protein Suz12 is required for embryonic stem cell differentiation. Mol Cell Biol. American Society for Microbiology; 2007;27: 3769–3779. doi: 10.1128/MCB.01432-06 17339329
    • (2007) Mol Cell Biol , vol.27 , pp. 3769-3779
    • Pasini, D.1    Bracken, A.P.2    Hansen, J.B.3    Capillo, M.4    Helin, K.5
  • 82
    • 84857367297 scopus 로고    scopus 로고
    • RYBP-PRC1 complexes mediate H2A ubiquitylation at polycomb target sites independently of PRC2 and H3K27me3
    • Tavares L, Dimitrova E, Oxley D, Webster J, Poot R, Demmers J, et al. RYBP-PRC1 complexes mediate H2A ubiquitylation at polycomb target sites independently of PRC2 and H3K27me3. Cell. 2012;148: 664–678. doi: 10.1016/j.cell.2011.12.029 22325148
    • (2012) Cell , vol.148 , pp. 664-678
    • Tavares, L.1    Dimitrova, E.2    Oxley, D.3    Webster, J.4    Poot, R.5    Demmers, J.6
  • 83
    • 84863012512 scopus 로고    scopus 로고
    • Direct recruitment of polycomb repressive complex 1 to chromatin by core binding transcription factors
    • Yu M, Mazor T, Huang H, Huang H-T, Kathrein KL, Woo AJ, et al. Direct recruitment of polycomb repressive complex 1 to chromatin by core binding transcription factors. Mol Cell. 2012;45: 330–343. doi: 10.1016/j.molcel.2011.11.032 22325351
    • (2012) Mol Cell , vol.45 , pp. 330-343
    • Yu, M.1    Mazor, T.2    Huang, H.3    Huang, H.-T.4    Kathrein, K.L.5    Woo, A.J.6
  • 84
    • 84902127230 scopus 로고    scopus 로고
    • Variant PRC1 complex-dependent H2A ubiquitylation drives PRC2 recruitment and polycomb domain formation
    • Blackledge NP, Farcas AM, Kondo T, King HW, McGouran JF, Hanssen LLP, et al. Variant PRC1 complex-dependent H2A ubiquitylation drives PRC2 recruitment and polycomb domain formation. Cell. 2014;157: 1445–1459. doi: 10.1016/j.cell.2014.05.004 24856970
    • (2014) Cell , vol.157 , pp. 1445-1459
    • Blackledge, N.P.1    Farcas, A.M.2    Kondo, T.3    King, H.W.4    McGouran, J.F.5    Hanssen, L.L.P.6
  • 85
    • 84902333500 scopus 로고    scopus 로고
    • Targeting polycomb to pericentric heterochromatin in embryonic stem cells reveals a role for H2AK119u1 in PRC2 recruitment
    • Cooper S, Dienstbier M, Hassan R, Schermelleh L, Sharif J, Blackledge NP, et al. Targeting polycomb to pericentric heterochromatin in embryonic stem cells reveals a role for H2AK119u1 in PRC2 recruitment. Cell Rep. 2014;7: 1456–1470. doi: 10.1016/j.celrep.2014.04.012 24857660
    • (2014) Cell Rep , vol.7 , pp. 1456-1470
    • Cooper, S.1    Dienstbier, M.2    Hassan, R.3    Schermelleh, L.4    Sharif, J.5    Blackledge, N.P.6
  • 86
    • 84901987800 scopus 로고    scopus 로고
    • Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression
    • Kalb R, Latwiel S, Baymaz HI, Jansen PWTC, Müller CW, Vermeulen M, et al. Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression. Nat Struct Mol Biol. Nature Publishing Group; 2014;21: 569–571. doi: 10.1038/nsmb.2833 24837194
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 569-571
    • Kalb, R.1    Latwiel, S.2    Baymaz, H.I.3    Jansen, P.W.T.C.4    Müller, C.W.5    Vermeulen, M.6
  • 87
    • 33646865180 scopus 로고    scopus 로고
    • Control of developmental regulators by Polycomb in human embryonic stem cells
    • Lee TI, Jenner RG, Boyer LA, Guenther MG, Levine SS, Kumar RM, et al. Control of developmental regulators by Polycomb in human embryonic stem cells. Cell. 2006;125: 301–313. doi: 10.1016/j.cell.2006.02.043 16630818
    • (2006) Cell , vol.125 , pp. 301-313
    • Lee, T.I.1    Jenner, R.G.2    Boyer, L.A.3    Guenther, M.G.4    Levine, S.S.5    Kumar, R.M.6
  • 88
    • 34248358308 scopus 로고    scopus 로고
    • Hyperconserved CpG domains underlie Polycomb-binding sites
    • Tanay A, O'Donnell AH, Damelin M, Bestor TH, Hyperconserved CpG domains underlie Polycomb-binding sites. Proc Natl Acad Sci USA. National Acad Sciences; 2007;104: 5521–5526. doi: 10.1073/pnas.0609746104 17376869
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 5521-5526
    • Tanay, A.1    O'Donnell, A.H.2    Damelin, M.3    Bestor, T.H.4
  • 90
  • 91
    • 34848825691 scopus 로고    scopus 로고
    • Polycomb response elements mediate the formation of chromosome higher-order structures in the bithorax complex
    • Lanzuolo C, Roure V, Dekker J, Bantignies F, Orlando V, Polycomb response elements mediate the formation of chromosome higher-order structures in the bithorax complex. Nat Cell Biol. Nature Publishing Group; 2007;9: 1167–1174. doi: 10.1038/ncb1637 17828248
    • (2007) Nat Cell Biol , vol.9 , pp. 1167-1174
    • Lanzuolo, C.1    Roure, V.2    Dekker, J.3    Bantignies, F.4    Orlando, V.5
  • 93
    • 46449119367 scopus 로고    scopus 로고
    • A novel 6C assay uncovers Polycomb-mediated higher order chromatin conformations
    • Tiwari VK, Cope L, McGarvey KM, Ohm JE, Baylin SB, A novel 6C assay uncovers Polycomb-mediated higher order chromatin conformations. Genome Res. Cold Spring Harbor Lab; 2008;18: 1171–1179. doi: 10.1101/gr.073452.107 18502945
    • (2008) Genome Res , vol.18 , pp. 1171-1179
    • Tiwari, V.K.1    Cope, L.2    McGarvey, K.M.3    Ohm, J.E.4    Baylin, S.B.5
  • 94
    • 84892474589 scopus 로고    scopus 로고
    • Polycomb silencing: from linear chromatin domains to 3D chromosome folding
    • Cheutin T, Cavalli G, Polycomb silencing: from linear chromatin domains to 3D chromosome folding. Curr Opin Genet Dev. 2014;25: 30–37. doi: 10.1016/j.gde.2013.11.016 24434548
    • (2014) Curr Opin Genet Dev , vol.25 , pp. 30-37
    • Cheutin, T.1    Cavalli, G.2
  • 95
    • 80052603592 scopus 로고    scopus 로고
    • Epstein-Barr virus exploits intrinsic B-lymphocyte transcription programs to achieve immortal cell growth
    • Zhao B, Zou J, Wang H, Johannsen E, Peng C-W, Quackenbush J, et al. Epstein-Barr virus exploits intrinsic B-lymphocyte transcription programs to achieve immortal cell growth. Proc Natl Acad Sci USA. National Acad Sciences; 2011;108: 14902–14907. doi: 10.1073/pnas.1108892108 21746931
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 14902-14907
    • Zhao, B.1    Zou, J.2    Wang, H.3    Johannsen, E.4    Peng, C.-W.5    Quackenbush, J.6
  • 96
    • 0037033108 scopus 로고    scopus 로고
    • Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A cooperate to bind the co-repressor carboxyl-terminal-binding protein (CtBP)
    • Hickabottom M, Parker GA, Freemont P, Crook T, Allday MJ, Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A cooperate to bind the co-repressor carboxyl-terminal-binding protein (CtBP). J Biol Chem. 2002;277: 47197–47204. doi: 10.1074/jbc.M208116200 12372828
    • (2002) J Biol Chem , vol.277 , pp. 47197-47204
    • Hickabottom, M.1    Parker, G.A.2    Freemont, P.3    Crook, T.4    Allday, M.J.5
  • 97
    • 0032493274 scopus 로고    scopus 로고
    • Propagation and recovery of intact, infectious Epstein-Barr virus from prokaryotic to human cells
    • Delecluse HJ, Hilsendegen T, Pich D, Zeidler R, Hammerschmidt W, Propagation and recovery of intact, infectious Epstein-Barr virus from prokaryotic to human cells. Proc Natl Acad Sci USA. 1998;95: 8245–8250. 9653172
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8245-8250
    • Delecluse, H.J.1    Hilsendegen, T.2    Pich, D.3    Zeidler, R.4    Hammerschmidt, W.5
  • 98
    • 0347382541 scopus 로고    scopus 로고
    • Generation and precise modification of a herpesvirus saimiri bacterial artificial chromosome demonstrates that the terminal repeats are required for both virus production and episomal persistence
    • White RE, Calderwood MA, Whitehouse A, Generation and precise modification of a herpesvirus saimiri bacterial artificial chromosome demonstrates that the terminal repeats are required for both virus production and episomal persistence. J Gen Virol. 2003;84: 3393–3403. 14645920
    • (2003) J Gen Virol , vol.84 , pp. 3393-3403
    • White, R.E.1    Calderwood, M.A.2    Whitehouse, A.3
  • 99
    • 0033119460 scopus 로고    scopus 로고
    • Long-term stability of large insert genomic DNA episomal shuttle vectors in human cells
    • Wade-Martins R, Frampton J, James MR, Long-term stability of large insert genomic DNA episomal shuttle vectors in human cells. Nucleic Acids Research. Oxford University Press; 1999;27: 1674–1682. 10075999
    • (1999) Nucleic Acids Research , vol.27 , pp. 1674-1682
    • Wade-Martins, R.1    Frampton, J.2    James, M.R.3


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