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Volumn 11, Issue 11, 2015, Pages

PML/TRIM19-Dependent Inhibition of Retroviral Reverse-Transcription by Daxx

Author keywords

[No Author keywords available]

Indexed keywords

DAXX PROTEIN; MESSENGER RNA; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN S 100; SUMO PROTEIN; TRIPARTITE MOTIF PROTEIN 19; UNCLASSIFIED DRUG; VIRUS RNA; DAXX PROTEIN, HUMAN; NUCLEAR PROTEIN; PML PROTEIN, HUMAN; PROTEIN BINDING; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TRANSCRIPTION FACTOR; TUMOR SUPPRESSOR PROTEIN;

EID: 84948977407     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1005280     Document Type: Article
Times cited : (50)

References (60)
  • 1
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys
    • Stremlau M, Owens CM, Perron MJ, Kiessling M, Autissier P, et al. (2004) The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. Nature 427: 848–853. 14985764
    • (2004) Nature , vol.427 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3    Kiessling, M.4    Autissier, P.5
  • 3
    • 3242670402 scopus 로고    scopus 로고
    • The human and African green monkey TRIM5alpha genes encode Ref1 and Lv1 retroviral restriction factor activities
    • Keckesova Z, Ylinen LM, Towers GJ, (2004) The human and African green monkey TRIM5alpha genes encode Ref1 and Lv1 retroviral restriction factor activities. Proc Natl Acad Sci U S A 101: 10780–10785. 15249687
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10780-10785
    • Keckesova, Z.1    Ylinen, L.M.2    Towers, G.J.3
  • 4
    • 3242720240 scopus 로고    scopus 로고
    • Trim5alpha protein restricts both HIV-1 and murine leukemia virus
    • Yap MW, Nisole S, Lynch C, Stoye JP, (2004) Trim5alpha protein restricts both HIV-1 and murine leukemia virus. Proc Natl Acad Sci U S A 101: 10786–10791. 15249690
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10786-10791
    • Yap, M.W.1    Nisole, S.2    Lynch, C.3    Stoye, J.P.4
  • 5
    • 17744371839 scopus 로고    scopus 로고
    • The tripartite motif family identifies cell compartments
    • Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, et al. (2001) The tripartite motif family identifies cell compartments. EMBO J 20: 2140–2151. 11331580
    • (2001) EMBO J , vol.20 , pp. 2140-2151
    • Reymond, A.1    Meroni, G.2    Fantozzi, A.3    Merla, G.4    Cairo, S.5
  • 6
    • 84894515095 scopus 로고    scopus 로고
    • TRIMmunity: the roles of the TRIM E3-ubiquitin ligase family in innate antiviral immunity
    • Rajsbaum R, Garcia-Sastre A, Versteeg GA, (2014) TRIMmunity: the roles of the TRIM E3-ubiquitin ligase family in innate antiviral immunity. J Mol Biol 426: 1265–1284. doi: 10.1016/j.jmb.2013.12.005 24333484
    • (2014) J Mol Biol , vol.426 , pp. 1265-1284
    • Rajsbaum, R.1    Garcia-Sastre, A.2    Versteeg, G.A.3
  • 7
    • 0029015347 scopus 로고
    • Molecular cloning of a new interferon-induced factor that represses human immunodeficiency virus type 1 long terminal repeat expression
    • Tissot C, Mechti N, (1995) Molecular cloning of a new interferon-induced factor that represses human immunodeficiency virus type 1 long terminal repeat expression. J Biol Chem 270: 14891–14898. 7797467
    • (1995) J Biol Chem , vol.270 , pp. 14891-14898
    • Tissot, C.1    Mechti, N.2
  • 8
    • 40349094838 scopus 로고    scopus 로고
    • The interferon response inhibits HIV particle production by induction of TRIM22
    • Barr SD, Smiley JR, Bushman FD, (2008) The interferon response inhibits HIV particle production by induction of TRIM22. PLoS Pathog 4: e1000007. doi: 10.1371/journal.ppat.1000007 18389079
    • (2008) PLoS Pathog , vol.4 , pp. 1000007
    • Barr, S.D.1    Smiley, J.R.2    Bushman, F.D.3
  • 9
    • 40349116307 scopus 로고    scopus 로고
    • TRIM E3 ligases interfere with early and late stages of the retroviral life cycle
    • Uchil PD, Quinlan BD, Chan WT, Luna JM, Mothes W, (2008) TRIM E3 ligases interfere with early and late stages of the retroviral life cycle. PLoS Pathog 4: e16. doi: 10.1371/journal.ppat.0040016 18248090
    • (2008) PLoS Pathog , vol.4 , pp. 16
    • Uchil, P.D.1    Quinlan, B.D.2    Chan, W.T.3    Luna, J.M.4    Mothes, W.5
  • 10
    • 27244444559 scopus 로고    scopus 로고
    • TRIM family proteins: retroviral restriction and antiviral defence
    • Nisole S, Stoye JP, Saib A, (2005) TRIM family proteins: retroviral restriction and antiviral defence. Nat Rev Microbiol 3: 799–808. 16175175
    • (2005) Nat Rev Microbiol , vol.3 , pp. 799-808
    • Nisole, S.1    Stoye, J.P.2    Saib, A.3
  • 11
    • 68949189335 scopus 로고    scopus 로고
    • Tripartite motif-containing 22 inhibits the activity of hepatitis B virus core promoter, which is dependent on nuclear-located RING domain
    • Gao B, Duan Z, Xu W, Xiong S, (2009) Tripartite motif-containing 22 inhibits the activity of hepatitis B virus core promoter, which is dependent on nuclear-located RING domain. Hepatology 50: 424–433. doi: 10.1002/hep.23011 19585648
    • (2009) Hepatology , vol.50 , pp. 424-433
    • Gao, B.1    Duan, Z.2    Xu, W.3    Xiong, S.4
  • 12
    • 63449090704 scopus 로고    scopus 로고
    • TRIM22 E3 ubiquitin ligase activity is required to mediate antiviral activity against encephalomyocarditis virus
    • Eldin P, Papon L, Oteiza A, Brocchi E, Lawson TG, et al. (2009) TRIM22 E3 ubiquitin ligase activity is required to mediate antiviral activity against encephalomyocarditis virus. J Gen Virol 90: 536–545. doi: 10.1099/vir.0.006288-0 19218198
    • (2009) J Gen Virol , vol.90 , pp. 536-545
    • Eldin, P.1    Papon, L.2    Oteiza, A.3    Brocchi, E.4    Lawson, T.G.5
  • 13
    • 84875797273 scopus 로고    scopus 로고
    • TRIM22 inhibits influenza A virus infection by targeting the viral nucleoprotein for degradation
    • Di Pietro A, Kajaste-Rudnitski A, Oteiza A, Nicora L, Towers GJ, et al. (2013) TRIM22 inhibits influenza A virus infection by targeting the viral nucleoprotein for degradation. J Virol 87: 4523–4533. doi: 10.1128/JVI.02548-12 23408607
    • (2013) J Virol , vol.87 , pp. 4523-4533
    • Di Pietro, A.1    Kajaste-Rudnitski, A.2    Oteiza, A.3    Nicora, L.4    Towers, G.J.5
  • 14
    • 0035796503 scopus 로고    scopus 로고
    • PML mediates the interferon-induced antiviral state against a complex retrovirus via its association with the viral transactivator
    • Regad T, Saib A, Lallemand-Breitenbach V, Pandolfi PP, de The H, et al. (2001) PML mediates the interferon-induced antiviral state against a complex retrovirus via its association with the viral transactivator. Embo J 20: 3495–3505. 11432836
    • (2001) Embo J , vol.20 , pp. 3495-3505
    • Regad, T.1    Saib, A.2    Lallemand-Breitenbach, V.3    Pandolfi, P.P.4    de The, H.5
  • 15
    • 33748636239 scopus 로고    scopus 로고
    • Cross talk between PML and p53 during poliovirus infection: implications for antiviral defense
    • Pampin M, Simonin Y, Blondel B, Percherancier Y, Chelbi-Alix MK, (2006) Cross talk between PML and p53 during poliovirus infection: implications for antiviral defense. J Virol 80: 8582–8592. 16912307
    • (2006) J Virol , vol.80 , pp. 8582-8592
    • Pampin, M.1    Simonin, Y.2    Blondel, B.3    Percherancier, Y.4    Chelbi-Alix, M.K.5
  • 16
    • 0031907092 scopus 로고    scopus 로고
    • Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein
    • Chelbi-Alix MK, Quignon F, Pelicano L, Koken MHM, de The H, (1998) Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein. J Virol 72: 1043–1051. 9444998
    • (1998) J Virol , vol.72 , pp. 1043-1051
    • Chelbi-Alix, M.K.1    Quignon, F.2    Pelicano, L.3    Koken, M.H.M.4    de The, H.5
  • 17
    • 77957192176 scopus 로고    scopus 로고
    • Resistance to rabies virus infection conferred by the PMLIV isoform
    • Blondel D, Kheddache S, Lahaye X, Dianoux L, Chelbi-Alix MK, (2010) Resistance to rabies virus infection conferred by the PMLIV isoform. J Virol 84: 10719–10726. doi: 10.1128/JVI.01286-10 20702643
    • (2010) J Virol , vol.84 , pp. 10719-10726
    • Blondel, D.1    Kheddache, S.2    Lahaye, X.3    Dianoux, L.4    Chelbi-Alix, M.K.5
  • 18
    • 84855836014 scopus 로고    scopus 로고
    • Promyelocytic leukemia isoform IV confers resistance to encephalomyocarditis virus via the sequestration of 3D polymerase in nuclear bodies
    • Maroui MA, Pampin M, Chelbi-Alix MK, (2011) Promyelocytic leukemia isoform IV confers resistance to encephalomyocarditis virus via the sequestration of 3D polymerase in nuclear bodies. J Virol 85: 13164–13173. doi: 10.1128/JVI.05808-11 21994459
    • (2011) J Virol , vol.85 , pp. 13164-13173
    • Maroui, M.A.1    Pampin, M.2    Chelbi-Alix, M.K.3
  • 19
    • 84891687081 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein is a cell-intrinsic factor inhibiting parvovirus DNA replication
    • Mitchell AM, Hirsch ML, Li C, Samulski RJ, (2014) Promyelocytic leukemia protein is a cell-intrinsic factor inhibiting parvovirus DNA replication. J Virol 88: 925–936. doi: 10.1128/JVI.02922-13 24198403
    • (2014) J Virol , vol.88 , pp. 925-936
    • Mitchell, A.M.1    Hirsch, M.L.2    Li, C.3    Samulski, R.J.4
  • 20
    • 84897687732 scopus 로고    scopus 로고
    • Implication of PMLIV in both intrinsic and innate immunity
    • El Asmi F, Maroui MA, Dutrieux J, Blondel D, Nisole S, et al. (2014) Implication of PMLIV in both intrinsic and innate immunity. PLoS Pathog 10: e1003975. doi: 10.1371/journal.ppat.1003975 24586174
    • (2014) PLoS Pathog , vol.10 , pp. 1003975
    • El Asmi, F.1    Maroui, M.A.2    Dutrieux, J.3    Blondel, D.4    Nisole, S.5
  • 21
    • 0034973563 scopus 로고    scopus 로고
    • Cytoplasmic recruitment of INI1 and PML on incoming HIV preintegration complexes: interference with early steps of viral replication
    • Turelli P, Doucas V, Craig E, Mangeat B, Klages N, et al. (2001) Cytoplasmic recruitment of INI1 and PML on incoming HIV preintegration complexes: interference with early steps of viral replication. Mol Cell 7: 1245–1254. 11430827
    • (2001) Mol Cell , vol.7 , pp. 1245-1254
    • Turelli, P.1    Doucas, V.2    Craig, E.3    Mangeat, B.4    Klages, N.5
  • 22
    • 0344089327 scopus 로고    scopus 로고
    • As(2)O(3) enhances retroviral reverse transcription and counteracts Ref1 antiviral activity
    • Berthoux L, Towers GJ, Gurer C, Salomoni P, Pandolfi PP, et al. (2003) As(2)O(3) enhances retroviral reverse transcription and counteracts Ref1 antiviral activity. J Virol 77: 3167–3180. 12584341
    • (2003) J Virol , vol.77 , pp. 3167-3180
    • Berthoux, L.1    Towers, G.J.2    Gurer, C.3    Salomoni, P.4    Pandolfi, P.P.5
  • 24
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1
    • Ishov AM, Sotnikov AG, Negorev D, Vladimirova OV, Neff N, et al. (1999) PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1. J Cell Biol 147: 221–234. 10525530
    • (1999) J Cell Biol , vol.147 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3    Vladimirova, O.V.4    Neff, N.5
  • 26
    • 54249103056 scopus 로고    scopus 로고
    • Regulation of apoptosis by PML and the PML-NBs
    • Bernardi R, Papa A, Pandolfi PP, (2008) Regulation of apoptosis by PML and the PML-NBs. Oncogene 27: 6299–6312. doi: 10.1038/onc.2008.305 18931695
    • (2008) Oncogene , vol.27 , pp. 6299-6312
    • Bernardi, R.1    Papa, A.2    Pandolfi, P.P.3
  • 27
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: implications in antiviral defence
    • Everett RD, Chelbi-Alix MK, (2007) PML and PML nuclear bodies: implications in antiviral defence. Biochimie 89(6–7): 819–830. 17343971
    • (2007) Biochimie , vol.89 , Issue.6-7 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 28
    • 78651471295 scopus 로고    scopus 로고
    • Role of promyelocytic leukemia protein in host antiviral defense
    • Geoffroy MC, Chelbi-Alix MK, (2011) Role of promyelocytic leukemia protein in host antiviral defense. J Interferon Cytokine Res 31: 145–158. doi: 10.1089/jir.2010.0111 21198351
    • (2011) J Interferon Cytokine Res , vol.31 , pp. 145-158
    • Geoffroy, M.C.1    Chelbi-Alix, M.K.2
  • 30
    • 43049096803 scopus 로고    scopus 로고
    • Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway
    • Lallemand-Breitenbach V, Jeanne M, Benhenda S, Nasr R, Lei M, et al. (2008) Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway. Nat Cell Biol 10: 547–555. doi: 10.1038/ncb1717 18408733
    • (2008) Nat Cell Biol , vol.10 , pp. 547-555
    • Lallemand-Breitenbach, V.1    Jeanne, M.2    Benhenda, S.3    Nasr, R.4    Lei, M.5
  • 31
    • 43049093756 scopus 로고    scopus 로고
    • RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
    • Tatham MH, Geoffroy MC, Shen L, Plechanovova A, Hattersley N, et al. (2008) RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol 10(5): 538–546. doi: 10.1038/ncb1716 18408734
    • (2008) Nat Cell Biol , vol.10 , Issue.5 , pp. 538-546
    • Tatham, M.H.1    Geoffroy, M.C.2    Shen, L.3    Plechanovova, A.4    Hattersley, N.5
  • 32
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Muller S, Matunis MJ, Dejean A, (1998) Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. Embo J 17: 61–70. 9427741
    • (1998) Embo J , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 33
    • 60649088334 scopus 로고    scopus 로고
    • Ginkgolic acid inhibits protein SUMOylation by blocking formation of the E1-SUMO intermediate
    • Fukuda I, Ito A, Hirai G, Nishimura S, Kawasaki H, et al. (2009) Ginkgolic acid inhibits protein SUMOylation by blocking formation of the E1-SUMO intermediate. Chem Biol 16: 133–140. doi: 10.1016/j.chembiol.2009.01.009 19246003
    • (2009) Chem Biol , vol.16 , pp. 133-140
    • Fukuda, I.1    Ito, A.2    Hirai, G.3    Nishimura, S.4    Kawasaki, H.5
  • 34
    • 2442554169 scopus 로고    scopus 로고
    • Identification of autonomous IAP LTR retrotransposons mobile in mammalian cells
    • Dewannieux M, Dupressoir A, Harper F, Pierron G, Heidmann T, (2004) Identification of autonomous IAP LTR retrotransposons mobile in mammalian cells. Nat Genet 36: 534–539. 15107856
    • (2004) Nat Genet , vol.36 , pp. 534-539
    • Dewannieux, M.1    Dupressoir, A.2    Harper, F.3    Pierron, G.4    Heidmann, T.5
  • 35
    • 8744304935 scopus 로고    scopus 로고
    • An active murine transposon family pair: retrotransposition of "master" MusD copies and ETn trans-mobilization
    • Ribet D, Dewannieux M, Heidmann T, (2004) An active murine transposon family pair: retrotransposition of "master" MusD copies and ETn trans-mobilization. Genome Res 14: 2261–2267. 15479948
    • (2004) Genome Res , vol.14 , pp. 2261-2267
    • Ribet, D.1    Dewannieux, M.2    Heidmann, T.3
  • 36
    • 2642670320 scopus 로고    scopus 로고
    • An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm
    • Borden KL, Campbell Dwyer EJ, Salvato MS, (1998) An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm. J Virol 72: 758–766. 9420283
    • (1998) J Virol , vol.72 , pp. 758-766
    • Borden, K.L.1    Campbell, D.E.J.2    Salvato, M.S.3
  • 37
    • 18744379736 scopus 로고    scopus 로고
    • Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies
    • Blondel D, Regad T, Poisson N, Pavie B, Harper F, et al. (2002) Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies. Oncogene 21: 7957–7970. 12439746
    • (2002) Oncogene , vol.21 , pp. 7957-7970
    • Blondel, D.1    Regad, T.2    Poisson, N.3    Pavie, B.4    Harper, F.5
  • 38
    • 84895552537 scopus 로고    scopus 로고
    • Cytoplasmic PML: from molecular regulation to biological functions
    • Jin G, Gao Y, Lin HK, (2014) Cytoplasmic PML: from molecular regulation to biological functions. J Cell Biochem 115: 812–818. doi: 10.1002/jcb.24727 24288198
    • (2014) J Cell Biochem , vol.115 , pp. 812-818
    • Jin, G.1    Gao, Y.2    Lin, H.K.3
  • 39
    • 79957798908 scopus 로고    scopus 로고
    • The nuclear bodies inside out: PML conquers the cytoplasm
    • Carracedo A, Ito K, Pandolfi PP, (2011) The nuclear bodies inside out: PML conquers the cytoplasm. Curr Opin Cell Biol 23: 360–366. doi: 10.1016/j.ceb.2011.03.011 21501958
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 360-366
    • Carracedo, A.1    Ito, K.2    Pandolfi, P.P.3
  • 40
    • 4544256756 scopus 로고    scopus 로고
    • Cytoplasmic PML function in TGF-beta signalling
    • Lin HK, Bergmann S, Pandolfi PP, (2004) Cytoplasmic PML function in TGF-beta signalling. Nature 431: 205–211. 15356634
    • (2004) Nature , vol.431 , pp. 205-211
    • Lin, H.K.1    Bergmann, S.2    Pandolfi, P.P.3
  • 41
    • 48449083440 scopus 로고    scopus 로고
    • A role for cytoplasmic PML in cellular resistance to viral infection
    • McNally BA, Trgovcich J, Maul GG, Liu Y, Zheng P, (2008) A role for cytoplasmic PML in cellular resistance to viral infection. PLoS One 3: e2277. doi: 10.1371/journal.pone.0002277 18509536
    • (2008) PLoS One , vol.3 , pp. 2277
    • McNally, B.A.1    Trgovcich, J.2    Maul, G.G.3    Liu, Y.4    Zheng, P.5
  • 42
    • 0033952527 scopus 로고    scopus 로고
    • Sequestration and inhibition of Daxx-mediated transcriptional repression by PML
    • Li H, Leo C, Zhu J, Wu X, O'Neil J, et al. (2000) Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol Cell Biol 20: 1784–1796. 10669754
    • (2000) Mol Cell Biol , vol.20 , pp. 1784-1796
    • Li, H.1    Leo, C.2    Zhu, J.3    Wu, X.4    O'Neil, J.5
  • 43
    • 33750491062 scopus 로고    scopus 로고
    • Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors
    • Lin DY, Huang YS, Jeng JC, Kuo HY, Chang CC, et al. (2006) Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol Cell 24: 341–354. 17081986
    • (2006) Mol Cell , vol.24 , pp. 341-354
    • Lin, D.Y.1    Huang, Y.S.2    Jeng, J.C.3    Kuo, H.Y.4    Chang, C.C.5
  • 44
    • 52049097494 scopus 로고    scopus 로고
    • PML NBs (ND10) and Daxx: from nuclear structure to protein function
    • Lindsay CR, Morozov VM, Ishov AM, (2008) PML NBs (ND10) and Daxx: from nuclear structure to protein function. Front Biosci 13: 7132–7142. 18508722
    • (2008) Front Biosci , vol.13 , pp. 7132-7142
    • Lindsay, C.R.1    Morozov, V.M.2    Ishov, A.M.3
  • 45
    • 0031587883 scopus 로고    scopus 로고
    • Daxx, a novel Fas-binding protein that activates JNK and apoptosis
    • Yang X, Khosravi-Far R, Chang HY, Baltimore D, (1997) Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell 89: 1067–1076. 9215629
    • (1997) Cell , vol.89 , pp. 1067-1076
    • Yang, X.1    Khosravi-Far, R.2    Chang, H.Y.3    Baltimore, D.4
  • 46
    • 84885968656 scopus 로고    scopus 로고
    • Virion factors that target Daxx to overcome intrinsic immunity
    • Schreiner S, Wodrich H, (2013) Virion factors that target Daxx to overcome intrinsic immunity. J Virol 87: 10412–10422. doi: 10.1128/JVI.00425-13 23864634
    • (2013) J Virol , vol.87 , pp. 10412-10422
    • Schreiner, S.1    Wodrich, H.2
  • 47
    • 84873853378 scopus 로고    scopus 로고
    • Retroviral DNA methylation and epigenetic repression are mediated by the antiviral host protein Daxx
    • Shalginskikh N, Poleshko A, Skalka AM, Katz RA, (2013) Retroviral DNA methylation and epigenetic repression are mediated by the antiviral host protein Daxx. J Virol 87: 2137–2150. doi: 10.1128/JVI.02026-12 23221555
    • (2013) J Virol , vol.87 , pp. 2137-2150
    • Shalginskikh, N.1    Poleshko, A.2    Skalka, A.M.3    Katz, R.A.4
  • 48
    • 16244383862 scopus 로고    scopus 로고
    • The cellular protein daxx interacts with avian sarcoma virus integrase and viral DNA to repress viral transcription
    • Greger JG, Katz RA, Ishov AM, Maul GG, Skalka AM, (2005) The cellular protein daxx interacts with avian sarcoma virus integrase and viral DNA to repress viral transcription. J Virol 79: 4610–4618. 15795247
    • (2005) J Virol , vol.79 , pp. 4610-4618
    • Greger, J.G.1    Katz, R.A.2    Ishov, A.M.3    Maul, G.G.4    Skalka, A.M.5
  • 49
    • 11144231031 scopus 로고    scopus 로고
    • Covalent modification of human immunodeficiency virus type 1 p6 by SUMO-1
    • Gurer C, Berthoux L, Luban J, (2005) Covalent modification of human immunodeficiency virus type 1 p6 by SUMO-1. J Virol 79: 910–917. 15613319
    • (2005) J Virol , vol.79 , pp. 910-917
    • Gurer, C.1    Berthoux, L.2    Luban, J.3
  • 50
    • 79958018867 scopus 로고    scopus 로고
    • Impairment of human immunodeficiency virus type-1 integrase SUMOylation correlates with an early replication defect
    • Zamborlini A, Coiffic A, Beauclair G, Delelis O, Paris J, et al. (2011) Impairment of human immunodeficiency virus type-1 integrase SUMOylation correlates with an early replication defect. J Biol Chem 286: 21013–21022. doi: 10.1074/jbc.M110.189274 21454548
    • (2011) J Biol Chem , vol.286 , pp. 21013-21022
    • Zamborlini, A.1    Coiffic, A.2    Beauclair, G.3    Delelis, O.4    Paris, J.5
  • 51
    • 46049097750 scopus 로고    scopus 로고
    • Daxx interacts with HIV-1 integrase and inhibits lentiviral gene expression
    • Huang L, Xu GL, Zhang JQ, Tian L, Xue JL, et al. (2008) Daxx interacts with HIV-1 integrase and inhibits lentiviral gene expression. Biochem Biophys Res Commun 373: 241–245. doi: 10.1016/j.bbrc.2008.06.017 18558084
    • (2008) Biochem Biophys Res Commun , vol.373 , pp. 241-245
    • Huang, L.1    Xu, G.L.2    Zhang, J.Q.3    Tian, L.4    Xue, J.L.5
  • 52
    • 78049250225 scopus 로고    scopus 로고
    • Reverse Transcriptase and Cellular Factors: Regulators of HIV-1 Reverse Transcription
    • Warren K, Warrilow D, Meredith L, Harrich D, (2009) Reverse Transcriptase and Cellular Factors: Regulators of HIV-1 Reverse Transcription. Viruses 1: 873–894. doi: 10.3390/v1030873 21994574
    • (2009) Viruses , vol.1 , pp. 873-894
    • Warren, K.1    Warrilow, D.2    Meredith, L.3    Harrich, D.4
  • 53
    • 84882896267 scopus 로고    scopus 로고
    • Cyclic GMP-AMP synthase is an innate immune sensor of HIV and other retroviruses
    • Gao D, Wu J, Wu YT, Du F, Aroh C, et al. (2013) Cyclic GMP-AMP synthase is an innate immune sensor of HIV and other retroviruses. Science 341: 903–906. doi: 10.1126/science.1240933 23929945
    • (2013) Science , vol.341 , pp. 903-906
    • Gao, D.1    Wu, J.2    Wu, Y.T.3    Du, F.4    Aroh, C.5
  • 54
    • 84888002403 scopus 로고    scopus 로고
    • IFI16 senses DNA forms of the lentiviral replication cycle and controls HIV-1 replication
    • Jakobsen MR, Bak RO, Andersen A, Berg RK, Jensen SB, et al. (2013) IFI16 senses DNA forms of the lentiviral replication cycle and controls HIV-1 replication. Proc Natl Acad Sci U S A 110: E4571–4580. doi: 10.1073/pnas.1311669110 24154727
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 4571-4580
    • Jakobsen, M.R.1    Bak, R.O.2    Andersen, A.3    Berg, R.K.4    Jensen, S.B.5
  • 55
    • 77956497003 scopus 로고    scopus 로고
    • A cryptic sensor for HIV-1 activates antiviral innate immunity in dendritic cells
    • Manel N, Hogstad B, Wang Y, Levy DE, Unutmaz D, et al. (2010) A cryptic sensor for HIV-1 activates antiviral innate immunity in dendritic cells. Nature 467: 214–217. doi: 10.1038/nature09337 20829794
    • (2010) Nature , vol.467 , pp. 214-217
    • Manel, N.1    Hogstad, B.2    Wang, Y.3    Levy, D.E.4    Unutmaz, D.5
  • 56
    • 84888054227 scopus 로고    scopus 로고
    • HIV-1 evades innate immune recognition through specific cofactor recruitment
    • Rasaiyaah J, Tan CP, Fletcher AJ, Price AJ, Blondeau C, et al. (2013) HIV-1 evades innate immune recognition through specific cofactor recruitment. Nature 503: 402–405. doi: 10.1038/nature12769 24196705
    • (2013) Nature , vol.503 , pp. 402-405
    • Rasaiyaah, J.1    Tan, C.P.2    Fletcher, A.J.3    Price, A.J.4    Blondeau, C.5
  • 57
    • 84890215093 scopus 로고    scopus 로고
    • The capsids of HIV-1 and HIV-2 determine immune detection of the viral cDNA by the innate sensor cGAS in dendritic cells
    • Lahaye X, Satoh T, Gentili M, Cerboni S, Conrad C, et al. (2013) The capsids of HIV-1 and HIV-2 determine immune detection of the viral cDNA by the innate sensor cGAS in dendritic cells. Immunity 39: 1132–1142. doi: 10.1016/j.immuni.2013.11.002 24269171
    • (2013) Immunity , vol.39 , pp. 1132-1142
    • Lahaye, X.1    Satoh, T.2    Gentili, M.3    Cerboni, S.4    Conrad, C.5
  • 58
    • 4444317361 scopus 로고    scopus 로고
    • Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX
    • Ishov AM, Vladimirova OV, Maul GG, (2004) Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX. J Cell Sci 117: 3807–3820. 15252119
    • (2004) J Cell Sci , vol.117 , pp. 3807-3820
    • Ishov, A.M.1    Vladimirova, O.V.2    Maul, G.G.3
  • 59
    • 60049097867 scopus 로고    scopus 로고
    • Arsenic trioxide inhibits hepatitis C virus RNA replication through modulation of the glutathione redox system and oxidative stress
    • Kuroki M, Ariumi Y, Ikeda M, Dansako H, Wakita T, et al. (2009) Arsenic trioxide inhibits hepatitis C virus RNA replication through modulation of the glutathione redox system and oxidative stress. J Virol 83: 2338–2348. doi: 10.1128/JVI.01840-08 19109388
    • (2009) J Virol , vol.83 , pp. 2338-2348
    • Kuroki, M.1    Ariumi, Y.2    Ikeda, M.3    Dansako, H.4    Wakita, T.5
  • 60
    • 84892598770 scopus 로고    scopus 로고
    • Dynamics of histone H3.3 deposition in proliferating and senescent cells reveals a DAXX-dependent targeting to PML-NBs important for pericentromeric heterochromatin organization
    • Corpet A, Olbrich T, Gwerder M, Fink D, Stucki M, (2014) Dynamics of histone H3.3 deposition in proliferating and senescent cells reveals a DAXX-dependent targeting to PML-NBs important for pericentromeric heterochromatin organization. Cell Cycle 13: 249–267. doi: 10.4161/cc.26988 24200965
    • (2014) Cell Cycle , vol.13 , pp. 249-267
    • Corpet, A.1    Olbrich, T.2    Gwerder, M.3    Fink, D.4    Stucki, M.5


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