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Volumn 10, Issue 9, 2014, Pages

Erratum: The tudor domain protein spindlin1 is involved in intrinsic antiviral defense against incoming Hepatitis B virus and herpes simplex virus type 1 (PLOS Pathogens (2014) 10:9 (e1004343) DOI: 10.1371/journal.ppat.1004343);The Tudor Domain Protein Spindlin1 Is Involved in Intrinsic Antiviral Defense against Incoming Hepatitis B Virus and Herpes Simplex Virus Type 1

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DNA; GENOMIC DNA; HEPATITIS B VIRUS X PROTEIN; HISTONE H4; HISTONE H4K4; LENTIVIRUS VECTOR; PEPTIDES AND PROTEINS; SHORT HAIRPIN RNA; SMALL INTERFERING RNA; SPINDLIN1; UNCLASSIFIED DRUG; VIRUS DNA; ANTIVIRUS AGENT; CELL CYCLE PROTEIN; MESSENGER RNA; MICROTUBULE ASSOCIATED PROTEIN; PHOSPHOPROTEIN; SPINDLIN;

EID: 84907584690     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1009135     Document Type: Erratum
Times cited : (46)

References (55)
  • 1
    • 77949654113 scopus 로고    scopus 로고
    • Mechanisms of HBV-related hepatocarcinogenesis
    • Neuveut C, Wei Y, Buendia MA, (2010) Mechanisms of HBV-related hepatocarcinogenesis. J Hepatol 52: 594–604.
    • (2010) J Hepatol , vol.52 , pp. 594-604
    • Neuveut, C.1    Wei, Y.2    Buendia, M.A.3
  • 2
    • 84875772744 scopus 로고    scopus 로고
    • The PRMT1 methyltransferase is a binding partner of HBx and a negative regulator of hepatitis B virus transcription
    • Benhenda S, Ducroux A, Riviere L, Sobhian B, Ward M, et al. (2013) The PRMT1 methyltransferase is a binding partner of HBx and a negative regulator of hepatitis B virus transcription. J Virol 87: 4360–4371.
    • (2013) J Virol , vol.87 , pp. 4360-4371
    • Benhenda, S.1    Ducroux, A.2    Riviere, L.3    Sobhian, B.4    Ward, M.5
  • 3
    • 1842842127 scopus 로고    scopus 로고
    • LRH-1/hB1F and HNF1 synergistically up-regulate hepatitis B virus gene transcription and DNA replication
    • Cai YN, Zhou Q, Kong YY, Li M, Viollet B, et al. (2003) LRH-1/hB1F and HNF1 synergistically up-regulate hepatitis B virus gene transcription and DNA replication. Cell Res 13: 451–458.
    • (2003) Cell Res , vol.13 , pp. 451-458
    • Cai, Y.N.1    Zhou, Q.2    Kong, Y.Y.3    Li, M.4    Viollet, B.5
  • 4
    • 84855368016 scopus 로고    scopus 로고
    • Inhibition of PP1 Phosphatase Activity by HBx: A Mechanism for the Activation of Hepatitis B Virus Transcription
    • Cougot D, Allemand E, Riviere L, Benhenda S, Duroure K, et al. (2012) Inhibition of PP1 Phosphatase Activity by HBx: A Mechanism for the Activation of Hepatitis B Virus Transcription. Sci Signal 5: ra1.
    • (2012) Sci Signal , vol.5 , pp. ra1
    • Cougot, D.1    Allemand, E.2    Riviere, L.3    Benhenda, S.4    Duroure, K.5
  • 6
    • 33644854241 scopus 로고    scopus 로고
    • Hepatitis B virus replication is regulated by the acetylation status of hepatitis B virus cccDNA-bound H3 and H4 histones
    • Pollicino T, Belloni L, Raffa G, Pediconi N, Squadrito G, et al. (2006) Hepatitis B virus replication is regulated by the acetylation status of hepatitis B virus cccDNA-bound H3 and H4 histones. Gastroenterology 130: 823–837.
    • (2006) Gastroenterology , vol.130 , pp. 823-837
    • Pollicino, T.1    Belloni, L.2    Raffa, G.3    Pediconi, N.4    Squadrito, G.5
  • 7
    • 45249096077 scopus 로고    scopus 로고
    • A concerted action of HNF4alpha and HNF1alpha links hepatitis B virus replication to hepatocyte differentiation
    • Quasdorff M, Hosel M, Odenthal M, Zedler U, Bohne F, et al. (2008) A concerted action of HNF4alpha and HNF1alpha links hepatitis B virus replication to hepatocyte differentiation. Cell Microbiol 10: 1478–1490.
    • (2008) Cell Microbiol , vol.10 , pp. 1478-1490
    • Quasdorff, M.1    Hosel, M.2    Odenthal, M.3    Zedler, U.4    Bohne, F.5
  • 8
    • 33750434272 scopus 로고    scopus 로고
    • PGC-1alpha controls hepatitis B virus through nutritional signals
    • Shlomai A, Paran N, Shaul Y, (2006) PGC-1alpha controls hepatitis B virus through nutritional signals. Proc Natl Acad Sci U S A 103: 16003–16008.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 16003-16008
    • Shlomai, A.1    Paran, N.2    Shaul, Y.3
  • 9
    • 84856514985 scopus 로고    scopus 로고
    • IFN-alpha inhibits HBV transcription and replication in cell culture and in humanized mice by targeting the epigenetic regulation of the nuclear cccDNA minichromosome
    • Belloni L, Allweiss L, Guerrieri F, Pediconi N, Volz T, et al. (2012) IFN-alpha inhibits HBV transcription and replication in cell culture and in humanized mice by targeting the epigenetic regulation of the nuclear cccDNA minichromosome. J Clin Invest 122: 529–537.
    • (2012) J Clin Invest , vol.122 , pp. 529-537
    • Belloni, L.1    Allweiss, L.2    Guerrieri, F.3    Pediconi, N.4    Volz, T.5
  • 10
    • 73949127893 scopus 로고    scopus 로고
    • Nuclear HBx binds the HBV minichromosome and modifies the epigenetic regulation of cccDNA function
    • Belloni L, Pollicino T, De Nicola F, Guerrieri F, Raffa G, et al. (2009) Nuclear HBx binds the HBV minichromosome and modifies the epigenetic regulation of cccDNA function. Proc Natl Acad Sci U S A 106: 19975–19979.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19975-19979
    • Belloni, L.1    Pollicino, T.2    De Nicola, F.3    Guerrieri, F.4    Raffa, G.5
  • 11
    • 0024391379 scopus 로고
    • Transcriptional activation of homologous and heterologous genes by the hepatitis B virus X gene product in cells permissive for viral replication
    • Colgrove R, Simon G, Ganem D, (1989) Transcriptional activation of homologous and heterologous genes by the hepatitis B virus X gene product in cells permissive for viral replication. J Virol 63: 4019–4026.
    • (1989) J Virol , vol.63 , pp. 4019-4026
    • Colgrove, R.1    Simon, G.2    Ganem, D.3
  • 12
    • 17444430845 scopus 로고    scopus 로고
    • The transcriptional transactivation function of HBx protein is important for its augmentation role in hepatitis B virus replication
    • Tang H, Delgermaa L, Huang F, Oishi N, Liu L, et al. (2005) The transcriptional transactivation function of HBx protein is important for its augmentation role in hepatitis B virus replication. J Virol 79: 5548–5556.
    • (2005) J Virol , vol.79 , pp. 5548-5556
    • Tang, H.1    Delgermaa, L.2    Huang, F.3    Oishi, N.4    Liu, L.5
  • 13
    • 79957614798 scopus 로고    scopus 로고
    • Hepatitis B virus X protein is essential to initiate and maintain virus replication after infection
    • Lucifora J, Arzberger S, Durantel D, Belloni L, Strubin M, et al. (2011) Hepatitis B virus X protein is essential to initiate and maintain virus replication after infection. J Hepatol 55: 996–1003.
    • (2011) J Hepatol , vol.55 , pp. 996-1003
    • Lucifora, J.1    Arzberger, S.2    Durantel, D.3    Belloni, L.4    Strubin, M.5
  • 14
    • 33947528120 scopus 로고    scopus 로고
    • The hepatitis B virus X protein functionally interacts with CREB-binding protein/p300 in the regulation of CREB-mediated transcription
    • Cougot D, Wu Y, Cairo S, Caramel J, Renard CA, et al. (2007) The hepatitis B virus X protein functionally interacts with CREB-binding protein/p300 in the regulation of CREB-mediated transcription. J Biol Chem 282: 4277–4287.
    • (2007) J Biol Chem , vol.282 , pp. 4277-4287
    • Cougot, D.1    Wu, Y.2    Cairo, S.3    Caramel, J.4    Renard, C.A.5
  • 15
    • 84870522970 scopus 로고    scopus 로고
    • Hepatitis B virus X protein stimulates gene expression selectively from extrachromosomal DNA templates
    • van Breugel PC, Robert EI, Mueller H, Decorsiere A, Zoulim F, et al. (2012) Hepatitis B virus X protein stimulates gene expression selectively from extrachromosomal DNA templates. Hepatology 56: 2116–2124.
    • (2012) Hepatology , vol.56 , pp. 2116-2124
    • Van Breugel, P.C.1    Robert, E.I.2    Mueller, H.3    Decorsiere, A.4    Zoulim, F.5
  • 16
    • 0031051198 scopus 로고    scopus 로고
    • Spindlin, a major maternal transcript expressed in the mouse during the transition from oocyte to embryo
    • Oh B, Hwang SY, Solter D, Knowles BB, (1997) Spindlin, a major maternal transcript expressed in the mouse during the transition from oocyte to embryo. Development 124: 493–503.
    • (1997) Development , vol.124 , pp. 493-503
    • Oh, B.1    Hwang, S.Y.2    Solter, D.3    Knowles, B.B.4
  • 17
    • 23744444849 scopus 로고    scopus 로고
    • Spindlin1, a novel nuclear protein with a role in the transformation of NIH3T3 cells
    • Gao Y, Yue W, Zhang P, Li L, Xie X, et al. (2005) Spindlin1, a novel nuclear protein with a role in the transformation of NIH3T3 cells. Biochem Biophys Res Commun 335: 343–350.
    • (2005) Biochem Biophys Res Commun , vol.335 , pp. 343-350
    • Gao, Y.1    Yue, W.2    Zhang, P.3    Li, L.4    Xie, X.5
  • 18
    • 40849083563 scopus 로고    scopus 로고
    • Overexpression of SPINDLIN1 induces cellular senescence, multinucleation and apoptosis
    • Yuan H, Zhang P, Qin L, Chen L, Shi S, et al. (2008) Overexpression of SPINDLIN1 induces cellular senescence, multinucleation and apoptosis. Gene 410: 67–74.
    • (2008) Gene , vol.410 , pp. 67-74
    • Yuan, H.1    Zhang, P.2    Qin, L.3    Chen, L.4    Shi, S.5
  • 19
    • 51449120459 scopus 로고    scopus 로고
    • Overexpression of spindlin1 induces metaphase arrest and chromosomal instability
    • Zhang P, Cong B, Yuan H, Chen L, Lv Y, et al. (2008) Overexpression of spindlin1 induces metaphase arrest and chromosomal instability. J Cell Physiol 217: 400–408.
    • (2008) J Cell Physiol , vol.217 , pp. 400-408
    • Zhang, P.1    Cong, B.2    Yuan, H.3    Chen, L.4    Lv, Y.5
  • 20
    • 84868104227 scopus 로고    scopus 로고
    • Distinct mode of methylated lysine-4 of histone H3 recognition by tandem tudor-like domains of Spindlin1
    • Yang N, Wang W, Wang Y, Wang M, Zhao Q, et al. (2012) Distinct mode of methylated lysine-4 of histone H3 recognition by tandem tudor-like domains of Spindlin1. Proc Natl Acad Sci U S A 109: 17954–17959.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 17954-17959
    • Yang, N.1    Wang, W.2    Wang, Y.3    Wang, M.4    Zhao, Q.5
  • 21
    • 33846968157 scopus 로고    scopus 로고
    • Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation
    • Zhao Q, Qin L, Jiang F, Wu B, Yue W, et al. (2007) Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation. J Biol Chem 282: 647–656.
    • (2007) J Biol Chem , vol.282 , pp. 647-656
    • Zhao, Q.1    Qin, L.2    Jiang, F.3    Wu, B.4    Yue, W.5
  • 22
    • 84885848767 scopus 로고    scopus 로고
    • Tudor: a versatile family of histone methylation ‘readers’
    • Lu R, Wang GG, (2013) Tudor: a versatile family of histone methylation ‘readers’. Trends Biochem Sci 38: 546–555.
    • (2013) Trends Biochem Sci , vol.38 , pp. 546-555
    • Lu, R.1    Wang, G.G.2
  • 23
    • 84861980264 scopus 로고    scopus 로고
    • Tudor domain proteins in development
    • Pek JW, Anand A, Kai T, (2012) Tudor domain proteins in development. Development 139: 2255–2266.
    • (2012) Development , vol.139 , pp. 2255-2266
    • Pek, J.W.1    Anand, A.2    Kai, T.3
  • 24
    • 80255133235 scopus 로고    scopus 로고
    • Nucleolar protein Spindlin1 recognizes H3K4 methylation and stimulates the expression of rRNA genes
    • Wang W, Chen Z, Mao Z, Zhang H, Ding X, et al. (2011) Nucleolar protein Spindlin1 recognizes H3K4 methylation and stimulates the expression of rRNA genes. EMBO Rep 12: 1160–1166.
    • (2011) EMBO Rep , vol.12 , pp. 1160-1166
    • Wang, W.1    Chen, Z.2    Mao, Z.3    Zhang, H.4    Ding, X.5
  • 25
    • 84896373575 scopus 로고    scopus 로고
    • Molecular basis underlying histone H3 lysine-arginine methylation pattern readout by Spin/Ssty repeats of Spindlin1
    • Su X, Zhu G, Ding X, Lee SY, Dou Y, et al. (2014) Molecular basis underlying histone H3 lysine-arginine methylation pattern readout by Spin/Ssty repeats of Spindlin1. Genes Dev 28: 622–636.
    • (2014) Genes Dev , vol.28 , pp. 622-636
    • Su, X.1    Zhu, G.2    Ding, X.3    Lee, S.Y.4    Dou, Y.5
  • 26
    • 84880648230 scopus 로고    scopus 로고
    • A tudor domain protein SPINDLIN1 interacts with the mRNA-binding protein SERBP1 and is involved in mouse oocyte meiotic resumption
    • Chew TG, Peaston A, Lim AK, Lorthongpanich C, Knowles BB, et al. (2013) A tudor domain protein SPINDLIN1 interacts with the mRNA-binding protein SERBP1 and is involved in mouse oocyte meiotic resumption. PLoS One 8: e69764.
    • (2013) PLoS One , vol.8 , pp. e69764
    • Chew, T.G.1    Peaston, A.2    Lim, A.K.3    Lorthongpanich, C.4    Knowles, B.B.5
  • 27
    • 80055065839 scopus 로고    scopus 로고
    • Hepatitis C virus reveals a novel early control in acute immune response
    • Arnaud N, Dabo S, Akazawa D, Fukasawa M, Shinkai-Ouchi F, et al. (2011) Hepatitis C virus reveals a novel early control in acute immune response. PLoS Pathog 7: e1002289.
    • (2011) PLoS Pathog , vol.7 , pp. e1002289
    • Arnaud, N.1    Dabo, S.2    Akazawa, D.3    Fukasawa, M.4    Shinkai-Ouchi, F.5
  • 28
    • 0030842540 scopus 로고    scopus 로고
    • Inducible expression of human hepatitis B virus (HBV) in stably transfected hepatoblastoma cells: a novel system for screening potential inhibitors of HBV replication
    • Ladner SK, Otto MJ, Barker CS, Zaifert K, Wang GH, et al. (1997) Inducible expression of human hepatitis B virus (HBV) in stably transfected hepatoblastoma cells: a novel system for screening potential inhibitors of HBV replication. Antimicrob Agents Chemother 41: 1715–1720.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 1715-1720
    • Ladner, S.K.1    Otto, M.J.2    Barker, C.S.3    Zaifert, K.4    Wang, G.H.5
  • 30
    • 26444552110 scopus 로고    scopus 로고
    • Virus infection switches TLR-3-positive human neurons to become strong producers of beta interferon
    • Prehaud C, Megret F, Lafage M, Lafon M, (2005) Virus infection switches TLR-3-positive human neurons to become strong producers of beta interferon. J Virol 79: 12893–12904.
    • (2005) J Virol , vol.79 , pp. 12893-12904
    • Prehaud, C.1    Megret, F.2    Lafage, M.3    Lafon, M.4
  • 31
    • 57049182539 scopus 로고    scopus 로고
    • Hepatic stem-like phenotype and interplay of Wnt/beta-catenin and Myc signaling in aggressive childhood liver cancer
    • Cairo S, Armengol C, De Reynies A, Wei Y, Thomas E, et al. (2008) Hepatic stem-like phenotype and interplay of Wnt/beta-catenin and Myc signaling in aggressive childhood liver cancer. Cancer Cell 14: 471–484.
    • (2008) Cancer Cell , vol.14 , pp. 471-484
    • Cairo, S.1    Armengol, C.2    De Reynies, A.3    Wei, Y.4    Thomas, E.5
  • 32
    • 0025334855 scopus 로고
    • Hepadnavirus envelope proteins regulate covalently closed circular DNA amplification
    • Summers J, Smith PM, Horwich AL, (1990) Hepadnavirus envelope proteins regulate covalently closed circular DNA amplification. J Virol 64: 2819–2824.
    • (1990) J Virol , vol.64 , pp. 2819-2824
    • Summers, J.1    Smith, P.M.2    Horwich, A.L.3
  • 33
    • 57849109058 scopus 로고    scopus 로고
    • Nascent RNA sequencing reveals widespread pausing and divergent initiation at human promoters
    • Core LJ, Waterfall JJ, Lis JT, (2008) Nascent RNA sequencing reveals widespread pausing and divergent initiation at human promoters. Science 322: 1845–1848.
    • (2008) Science , vol.322 , pp. 1845-1848
    • Core, L.J.1    Waterfall, J.J.2    Lis, J.T.3
  • 34
    • 39149132854 scopus 로고    scopus 로고
    • Chromatin control of herpes simplex virus lytic and latent infection
    • Knipe DM, Cliffe A, (2008) Chromatin control of herpes simplex virus lytic and latent infection. Nat Rev Microbiol 6: 211–221.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 211-221
    • Knipe, D.M.1    Cliffe, A.2
  • 35
    • 79959848568 scopus 로고    scopus 로고
    • The intrinsic antiviral defense to incoming HSV-1 genomes includes specific DNA repair proteins and is counteracted by the viral protein ICP0
    • Lilley CE, Chaurushiya MS, Boutell C, Everett RD, Weitzman MD, (2011) The intrinsic antiviral defense to incoming HSV-1 genomes includes specific DNA repair proteins and is counteracted by the viral protein ICP0. PLoS Pathog 7: e1002084.
    • (2011) PLoS Pathog , vol.7 , pp. e1002084
    • Lilley, C.E.1    Chaurushiya, M.S.2    Boutell, C.3    Everett, R.D.4    Weitzman, M.D.5
  • 36
    • 84863378278 scopus 로고    scopus 로고
    • SPINDLIN1 promotes cancer cell proliferation through activation of WNT/TCF-4 signaling
    • Wang JX, Zeng Q, Chen L, Du JC, Yan XL, et al. (2012) SPINDLIN1 promotes cancer cell proliferation through activation of WNT/TCF-4 signaling. Mol Cancer Res 10: 326–335.
    • (2012) Mol Cancer Res , vol.10 , pp. 326-335
    • Wang, J.X.1    Zeng, Q.2    Chen, L.3    Du, J.C.4    Yan, X.L.5
  • 37
    • 77958481159 scopus 로고    scopus 로고
    • Nucleosome-interacting proteins regulated by DNA and histone methylation
    • Bartke T, Vermeulen M, Xhemalce B, Robson SC, Mann M, et al. (2010) Nucleosome-interacting proteins regulated by DNA and histone methylation. Cell 143: 470–484.
    • (2010) Cell , vol.143 , pp. 470-484
    • Bartke, T.1    Vermeulen, M.2    Xhemalce, B.3    Robson, S.C.4    Mann, M.5
  • 38
    • 59349087552 scopus 로고    scopus 로고
    • Importin 8 is a gene silencing factor that targets argonaute proteins to distinct mRNAs
    • Weinmann L, Hock J, Ivacevic T, Ohrt T, Mutze J, et al. (2009) Importin 8 is a gene silencing factor that targets argonaute proteins to distinct mRNAs. Cell 136: 496–507.
    • (2009) Cell , vol.136 , pp. 496-507
    • Weinmann, L.1    Hock, J.2    Ivacevic, T.3    Ohrt, T.4    Mutze, J.5
  • 39
    • 34547512353 scopus 로고    scopus 로고
    • Functional specialization of beta-arrestin interactions revealed by proteomic analysis
    • Xiao K, McClatchy DB, Shukla AK, Zhao Y, Chen M, et al. (2007) Functional specialization of beta-arrestin interactions revealed by proteomic analysis. Proc Natl Acad Sci U S A 104: 12011–12016.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 12011-12016
    • Xiao, K.1    Mcclatchy, D.B.2    Shukla, A.K.3    Zhao, Y.4    Chen, M.5
  • 40
    • 0037413848 scopus 로고    scopus 로고
    • Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3
    • Lemos TA, Passos DO, Nery FC, Kobarg J, (2003) Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3. FEBS Lett 533: 14–20.
    • (2003) FEBS Lett , vol.533 , pp. 14-20
    • Lemos, T.A.1    Passos, D.O.2    Nery, F.C.3    Kobarg, J.4
  • 42
    • 33947513027 scopus 로고    scopus 로고
    • Regulation of histone methylation by demethylimination and demethylation
    • Klose RJ, Zhang Y, (2007) Regulation of histone methylation by demethylimination and demethylation. Nat Rev Mol Cell Biol 8: 307–318.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 307-318
    • Klose, R.J.1    Zhang, Y.2
  • 43
    • 24144462170 scopus 로고    scopus 로고
    • LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription
    • Metzger E, Wissmann M, Yin N, Muller JM, Schneider R, et al. (2005) LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription. Nature 437: 436–439.
    • (2005) Nature , vol.437 , pp. 436-439
    • Metzger, E.1    Wissmann, M.2    Yin, N.3    Muller, J.M.4    Schneider, R.5
  • 44
    • 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, et al. (2012) NOTCH1 nuclear interactome reveals key regulators of its transcriptional activity and oncogenic function. Mol Cell 48: 445–458.
    • (2012) Mol Cell , vol.48 , pp. 445-458
    • Yatim, A.1    Benne, C.2    Sobhian, B.3    Laurent-Chabalier, S.4    Deas, O.5
  • 45
    • 43149084600 scopus 로고    scopus 로고
    • Drosophila STAT is required for directly maintaining HP1 localization and heterochromatin stability
    • Shi S, Larson K, Guo D, Lim SJ, Dutta P, et al. (2008) Drosophila STAT is required for directly maintaining HP1 localization and heterochromatin stability. Nat Cell Biol 10: 489–496.
    • (2008) Nat Cell Biol , vol.10 , pp. 489-496
    • Shi, S.1    Larson, K.2    Guo, D.3    Lim, S.J.4    Dutta, P.5
  • 46
    • 84874035038 scopus 로고    scopus 로고
    • Regulation of alphaherpesvirus infections by the ICP0 family of proteins
    • Boutell C, Everett RD, (2012) Regulation of alphaherpesvirus infections by the ICP0 family of proteins. J Gen Virol 94: 465–481.
    • (2012) J Gen Virol , vol.94 , pp. 465-481
    • Boutell, C.1    Everett, R.D.2
  • 47
    • 0035791019 scopus 로고    scopus 로고
    • Chicken spindlin genes on W and Z chromosomes: transcriptional expression of both genes and dynamic behavior of spindlin in interphase and mitotic cells
    • Itoh Y, Hori T, Saitoh H, Mizuno S, (2001) Chicken spindlin genes on W and Z chromosomes: transcriptional expression of both genes and dynamic behavior of spindlin in interphase and mitotic cells. Chromosome Res 9: 283–299.
    • (2001) Chromosome Res , vol.9 , pp. 283-299
    • Itoh, Y.1    Hori, T.2    Saitoh, H.3    Mizuno, S.4
  • 48
    • 79960942804 scopus 로고    scopus 로고
    • SUMO pathway dependent recruitment of cellular repressors to herpes simplex virus type 1 genomes
    • Cuchet-Lourenco D, Boutell C, Lukashchuk V, Grant K, Sykes A, et al. (2011) SUMO pathway dependent recruitment of cellular repressors to herpes simplex virus type 1 genomes. PLoS Pathog 7: e1002123.
    • (2011) PLoS Pathog , vol.7 , pp. e1002123
    • Cuchet-Lourenco, D.1    Boutell, C.2    Lukashchuk, V.3    Grant, K.4    Sykes, A.5
  • 49
    • 77649338569 scopus 로고    scopus 로고
    • A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses
    • Lilley CE, Chaurushiya MS, Boutell C, Landry S, Suh J, et al. (2010) A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses. Embo J 29: 943–955.
    • (2010) Embo J , vol.29 , pp. 943-955
    • Lilley, C.E.1    Chaurushiya, M.S.2    Boutell, C.3    Landry, S.4    Suh, J.5
  • 50
    • 15444374342 scopus 로고    scopus 로고
    • Arginine methylation of MRE11 by PRMT1 is required for DNA damage checkpoint control
    • Boisvert FM, Dery U, Masson JY, Richard S, (2005) Arginine methylation of MRE11 by PRMT1 is required for DNA damage checkpoint control. Genes Dev 19: 671–676.
    • (2005) Genes Dev , vol.19 , pp. 671-676
    • Boisvert, F.M.1    Dery, U.2    Masson, J.Y.3    Richard, S.4
  • 51
    • 29244456155 scopus 로고    scopus 로고
    • The GAR motif of 53BP1 is arginine methylated by PRMT1 and is necessary for 53BP1 DNA binding activity
    • Boisvert FM, Rhie A, Richard S, Doherty AJ, (2005) The GAR motif of 53BP1 is arginine methylated by PRMT1 and is necessary for 53BP1 DNA binding activity. Cell Cycle 4: 1834–1841.
    • (2005) Cell Cycle , vol.4 , pp. 1834-1841
    • Boisvert, F.M.1    Rhie, A.2    Richard, S.3    Doherty, A.J.4
  • 52
    • 9244252580 scopus 로고    scopus 로고
    • Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks
    • Huyen Y, Zgheib O, Ditullio RA, JrGorgoulis VG, Zacharatos P, et al. (2004) Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks. Nature 432: 406–411.
    • (2004) Nature , vol.432 , pp. 406-411
    • Huyen, Y.1    Zgheib, O.2    Ditullio, R.A.3    Gorgoulis, V.G.4    Zacharatos, P.5
  • 53
    • 15244357567 scopus 로고    scopus 로고
    • Hepatitis B virus X protein stimulates viral genome replication via a DDB1-dependent pathway distinct from that leading to cell death
    • Leupin O, Bontron S, Schaeffer C, Strubin M, (2005) Hepatitis B virus X protein stimulates viral genome replication via a DDB1-dependent pathway distinct from that leading to cell death. J Virol 79: 4238–4245.
    • (2005) J Virol , vol.79 , pp. 4238-4245
    • Leupin, O.1    Bontron, S.2    Schaeffer, C.3    Strubin, M.4
  • 54
    • 0034618437 scopus 로고    scopus 로고
    • Correct binding of viral X protein to UVDDB-p127 cellular protein is critical for efficient infection by hepatitis B viruses
    • Sitterlin D, Bergametti F, Tiollais P, Tennant BC, Transy C, (2000) Correct binding of viral X protein to UVDDB-p127 cellular protein is critical for efficient infection by hepatitis B viruses. Oncogene 19: 4427–4431.
    • (2000) Oncogene , vol.19 , pp. 4427-4431
    • Sitterlin, D.1    Bergametti, F.2    Tiollais, P.3    Tennant, B.C.4    Transy, C.5
  • 55
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy AM, Gaddis NC, Choi JD, Malim MH, (2002) Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418: 646–650.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.