메뉴 건너뛰기




Volumn 11, Issue 3, 2015, Pages 1-24

Positive Role of Promyelocytic Leukemia Protein in Type I Interferon Response and Its Regulation by Human Cytomegalovirus

Author keywords

[No Author keywords available]

Indexed keywords

BETA INTERFERON; GAMMA INTERFERON INDUCIBLE PROTEIN 10; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; IE1 PROTEIN; INTERFERON; INTERFERON STIMULATED GENE FACTOR 3; PEPTIDES AND PROTEINS; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN ISG54; STAT1 PROTEIN; STAT2 PROTEIN; UNCLASSIFIED DRUG; HDAC1 PROTEIN, HUMAN; HDAC2 PROTEIN, HUMAN; IE1 PROTEIN, CYTOMEGALOVIRUS; IMMEDIATE EARLY PROTEIN; INTERFERON REGULATORY FACTOR 9; IRF9 PROTEIN, HUMAN; NUCLEAR PROTEIN; PML PROTEIN, HUMAN; STAT1 PROTEIN, HUMAN; STAT2 PROTEIN, HUMAN; TRANSCRIPTION FACTOR; TUMOR SUPPRESSOR PROTEIN;

EID: 84926433175     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004785     Document Type: Article
Times cited : (70)

References (61)
  • 1
    • 0034767753 scopus 로고    scopus 로고
    • Antiviral actions of interferons
    • Samuel CE, Antiviral actions of interferons. Clin Microbiol Rev. 2001;14(4):778–809. 11585785
    • (2001) Clin Microbiol Rev , vol.14 , Issue.4 , pp. 778-809
    • Samuel, C.E.1
  • 2
    • 0029767462 scopus 로고    scopus 로고
    • Cooperation of Stat2 and p300/CBP in signalling induced by interferon-alpha
    • Bhattacharya S, Eckner R, Grossman S, Oldread E, Arany Z, D'Andrea A, et al. Cooperation of Stat2 and p300/CBP in signalling induced by interferon-alpha. Nature. 1996;383(6598):344–7. 8848048
    • (1996) Nature , vol.383 , Issue.6598 , pp. 344-347
    • Bhattacharya, S.1    Eckner, R.2    Grossman, S.3    Oldread, E.4    Arany, Z.5    D'Andrea, A.6
  • 3
    • 0036170183 scopus 로고    scopus 로고
    • IFN-Stimulated transcription through a TBP-free acetyltransferase complex escapes viral shutoff
    • Paulson M, Press C, Smith E, Tanese N, Levy DE, IFN-Stimulated transcription through a TBP-free acetyltransferase complex escapes viral shutoff. Nat Cell Biol. 2002;4(2):140–7. 11802163
    • (2002) Nat Cell Biol , vol.4 , Issue.2 , pp. 140-147
    • Paulson, M.1    Press, C.2    Smith, E.3    Tanese, N.4    Levy, D.E.5
  • 4
    • 0344304443 scopus 로고    scopus 로고
    • Interferon-stimulated transcription and innate antiviral immunity require deacetylase activity and histone deacetylase 1
    • Nusinzon I, Horvath CM, Interferon-stimulated transcription and innate antiviral immunity require deacetylase activity and histone deacetylase 1. Proc Natl Acad Sci U S A. 2003;100(25):14742–7. 14645718
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.25 , pp. 14742-14747
    • Nusinzon, I.1    Horvath, C.M.2
  • 5
    • 3042752799 scopus 로고    scopus 로고
    • Induction of interferon-stimulated gene expression and antiviral responses require protein deacetylase activity
    • Chang HM, Paulson M, Holko M, Rice CM, Williams BR, Marie I, et al. Induction of interferon-stimulated gene expression and antiviral responses require protein deacetylase activity. Proc Natl Acad Sci U S A. 2004;101(26):9578–83. 15210966
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.26 , pp. 9578-9583
    • Chang, H.M.1    Paulson, M.2    Holko, M.3    Rice, C.M.4    Williams, B.R.5    Marie, I.6
  • 6
    • 4644366536 scopus 로고    scopus 로고
    • Histone deacetylase activity is required to recruit RNA polymerase II to the promoters of selected interferon-stimulated early response genes
    • Sakamoto S, Potla R, Larner AC, Histone deacetylase activity is required to recruit RNA polymerase II to the promoters of selected interferon-stimulated early response genes. J Biol Chem. 2004;279(39):40362–7. 15194680
    • (2004) J Biol Chem , vol.279 , Issue.39 , pp. 40362-40367
    • Sakamoto, S.1    Potla, R.2    Larner, A.C.3
  • 7
    • 33645812740 scopus 로고    scopus 로고
    • Positive and negative regulation of the innate antiviral response and beta interferon gene expression by deacetylation
    • Nusinzon I, Horvath CM, Positive and negative regulation of the innate antiviral response and beta interferon gene expression by deacetylation. Mol Cell Biol. 2006;26(8):3106–13. 16581785
    • (2006) Mol Cell Biol , vol.26 , Issue.8 , pp. 3106-3113
    • Nusinzon, I.1    Horvath, C.M.2
  • 8
    • 0036800352 scopus 로고    scopus 로고
    • Chromatin-remodelling factor BRG1 selectively activates a subset of interferon-alpha-inducible genes
    • Huang M, Qian F, Hu Y, Ang C, Li Z, Wen Z, Chromatin-remodelling factor BRG1 selectively activates a subset of interferon-alpha-inducible genes. Nature cell biology. 2002;4(10):774–81. 12244326
    • (2002) Nature cell biology , vol.4 , Issue.10 , pp. 774-781
    • Huang, M.1    Qian, F.2    Hu, Y.3    Ang, C.4    Li, Z.5    Wen, Z.6
  • 9
    • 0028932963 scopus 로고
    • The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML
    • Borden KL, Boddy MN, Lally J, O'Reilly NJ, Martin S, Howe K, et al. The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML. Embo J. 1995;14(7):1532–41. 7729428
    • (1995) Embo J , vol.14 , Issue.7 , pp. 1532-1541
    • Borden, K.L.1    Boddy, M.N.2    Lally, J.3    O'Reilly, N.J.4    Martin, S.5    Howe, K.6
  • 10
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCC/TRIM motif
    • Jensen K, Shiels C, Freemont PS, PML protein isoforms and the RBCC/TRIM motif. Oncogene. 2001;20(49):7223–33. 11704850
    • (2001) Oncogene , vol.20 , Issue.49 , pp. 7223-7233
    • Jensen, K.1    Shiels, C.2    Freemont, P.S.3
  • 11
    • 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, Kamitani T, et al. 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. 1999;147(2):221–34. 10525530
    • (1999) J Cell Biol , vol.147 , Issue.2 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3    Vladimirova, O.V.4    Neff, N.5    Kamitani, T.6
  • 12
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • Bernardi R, Pandolfi PP, Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat Rev Mol Cell Biol. 2007;8(12):1006–16. 17928811
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.12 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 13
    • 53449090838 scopus 로고    scopus 로고
    • Role of nuclear bodies in apoptosis signalling
    • Krieghoff-Henning E, Hofmann TG, Role of nuclear bodies in apoptosis signalling. Biochimica et biophysica acta. 2008;1783(11):2185–94. doi: 10.1016/j.bbamcr.2008.07.002 18680765
    • (2008) Biochimica et biophysica acta , vol.1783 , Issue.11 , pp. 2185-2194
    • Krieghoff-Henning, E.1    Hofmann, T.G.2
  • 14
    • 84905109775 scopus 로고    scopus 로고
    • PML tumour suppression and beyond: therapeutic implications
    • Gamell C, Jan Paul P, Haupt Y, Haupt S, PML tumour suppression and beyond: therapeutic implications. FEBS letters. 2014;588(16):2653–62. doi: 10.1016/j.febslet.2014.02.007 24548562
    • (2014) FEBS letters , vol.588 , Issue.16 , pp. 2653-2662
    • Gamell, C.1    Jan Paul, P.2    Haupt, Y.3    Haupt, S.4
  • 16
    • 0028979594 scopus 로고
    • The acute promyelocytic leukaemia-associated PML gene is induced by interferon
    • Lavau C, Marchio A, Fagioli M, Jansen J, Falini B, Lebon P, et al. The acute promyelocytic leukaemia-associated PML gene is induced by interferon. Oncogene. 1995;11(5):871–6. 7545807
    • (1995) Oncogene , vol.11 , Issue.5 , pp. 871-876
    • Lavau, C.1    Marchio, A.2    Fagioli, M.3    Jansen, J.4    Falini, B.5    Lebon, P.6
  • 17
    • 0026578112 scopus 로고
    • Alternative splicing of PML transcripts predicts coexpression of several carboxy-terminally different protein isoforms
    • Fagioli M, Alcalay M, Pandolfi PP, Venturini L, Mencarelli A, Simeone A, et al. Alternative splicing of PML transcripts predicts coexpression of several carboxy-terminally different protein isoforms. Oncogene. 1992;7(6):1083–91. 1594241
    • (1992) Oncogene , vol.7 , Issue.6 , pp. 1083-1091
    • Fagioli, M.1    Alcalay, M.2    Pandolfi, P.P.3    Venturini, L.4    Mencarelli, A.5    Simeone, A.6
  • 18
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: implications in antiviral defence
    • Everett RD, Chelbi-Alix MK, PML and PML nuclear bodies: implications in antiviral defence. Biochimie. 2007;89(6–7):819–30. 17881113
    • (2007) Biochimie , vol.89 , Issue.6-7 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 19
    • 54549084341 scopus 로고    scopus 로고
    • New insights into the role of the subnuclear structure ND10 for viral infection
    • Tavalai N, Stamminger T, New insights into the role of the subnuclear structure ND10 for viral infection. Biochim Biophys Acta. 2008;1783(11):2207–21. doi: 10.1016/j.bbamcr.2008.08.004 18775455
    • (2008) Biochim Biophys Acta , vol.1783 , Issue.11 , pp. 2207-2221
    • Tavalai, N.1    Stamminger, T.2
  • 20
    • 84885968656 scopus 로고    scopus 로고
    • Virion factors that target Daxx to overcome intrinsic immunity
    • Schreiner S, Wodrich H, Virion factors that target Daxx to overcome intrinsic immunity. J Virol. 2013;87(19):10412–22. doi: 10.1128/JVI.00425-13 23864634
    • (2013) J Virol , vol.87 , Issue.19 , pp. 10412-10422
    • Schreiner, S.1    Wodrich, H.2
  • 22
    • 80053459914 scopus 로고    scopus 로고
    • A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence
    • Boutell C, Cuchet-Lourenco D, Vanni E, Orr A, Glass M, McFarlane S, et al. A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence. PLoS pathogens. 2011;7(9):e1002245. doi: 10.1371/journal.ppat.1002245 21949651
    • (2011) PLoS pathogens , vol.7 , Issue.9
    • Boutell, C.1    Cuchet-Lourenco, D.2    Vanni, E.3    Orr, A.4    Glass, M.5    McFarlane, S.6
  • 23
    • 0030912888 scopus 로고    scopus 로고
    • The major immediate-early proteins IE1 and IE2 of human cytomegalovirus colocalize with and disrupt PML-associated nuclear bodies at very early times in infected permissive cells
    • Ahn JH, Hayward GS, The major immediate-early proteins IE1 and IE2 of human cytomegalovirus colocalize with and disrupt PML-associated nuclear bodies at very early times in infected permissive cells. J Virol. 1997;71(6):4599–613. 9151854
    • (1997) J Virol , vol.71 , Issue.6 , pp. 4599-4613
    • Ahn, J.H.1    Hayward, G.S.2
  • 24
    • 0031877790 scopus 로고    scopus 로고
    • Disruption of PML subnuclear domains by the acidic IE1 protein of human cytomegalovirus is mediated through interaction with PML and may modulate a RING finger-dependent cryptic transactivator function of PML
    • Ahn JH, Brignole EJ, 3rdHayward GS, Disruption of PML subnuclear domains by the acidic IE1 protein of human cytomegalovirus is mediated through interaction with PML and may modulate a RING finger-dependent cryptic transactivator function of PML. Mol Cell Biol. 1998;18(8):4899–913. 9671498
    • (1998) Mol Cell Biol , vol.18 , Issue.8 , pp. 4899-4913
    • Ahn, J.H.1    Brignole, E.J.2    Hayward, G.S.3
  • 25
    • 0031922713 scopus 로고    scopus 로고
    • Disruption of PML-associated nuclear bodies mediated by the human cytomegalovirus major immediate early gene product
    • Wilkinson GW, Kelly C, Sinclair JH, Rickards C, Disruption of PML-associated nuclear bodies mediated by the human cytomegalovirus major immediate early gene product. J Gen Virol. 1998;79 (Pt 5):1233–45. 9603339
    • (1998) J Gen Virol , vol.79 , pp. 1233-1245
    • Wilkinson, G.W.1    Kelly, C.2    Sinclair, J.H.3    Rickards, C.4
  • 26
    • 0030602019 scopus 로고    scopus 로고
    • The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1
    • Korioth F, Maul GG, Plachter B, Stamminger T, Frey J, The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1. Exp Cell Res. 1996;229(1):155–8. 8940259
    • (1996) Exp Cell Res , vol.229 , Issue.1 , pp. 155-158
    • Korioth, F.1    Maul, G.G.2    Plachter, B.3    Stamminger, T.4    Frey, J.5
  • 27
    • 0034663128 scopus 로고    scopus 로고
    • Disruption of PML-associated nuclear bodies by IE1 correlates with efficient early stages of viral gene expression and DNA replication in human cytomegalovirus infection
    • Ahn JH, Hayward GS, Disruption of PML-associated nuclear bodies by IE1 correlates with efficient early stages of viral gene expression and DNA replication in human cytomegalovirus infection. Virology. 2000;274(1):39–55. 10936087
    • (2000) Virology , vol.274 , Issue.1 , pp. 39-55
    • Ahn, J.H.1    Hayward, G.S.2
  • 28
    • 2642574870 scopus 로고    scopus 로고
    • Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells
    • Lee HR, Kim DJ, Lee JM, Choi CY, Ahn BY, Hayward GS, et al. Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells. J Virol. 2004;78(12):6527–42. 15163746
    • (2004) J Virol , vol.78 , Issue.12 , pp. 6527-6542
    • Lee, H.R.1    Kim, D.J.2    Lee, J.M.3    Choi, C.Y.4    Ahn, B.Y.5    Hayward, G.S.6
  • 29
    • 33746840094 scopus 로고    scopus 로고
    • Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections
    • Tavalai N, Papior P, Rechter S, Leis M, Stamminger T, Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections. J Virol. 2006;80(16):8006–18. 16873257
    • (2006) J Virol , vol.80 , Issue.16 , pp. 8006-8018
    • Tavalai, N.1    Papior, P.2    Rechter, S.3    Leis, M.4    Stamminger, T.5
  • 30
    • 37349033209 scopus 로고    scopus 로고
    • Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection
    • Tavalai N, Papior P, Rechter S, Stamminger T, Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection. J Virol. 2008;82(1):126–37. 17942542
    • (2008) J Virol , vol.82 , Issue.1 , pp. 126-137
    • Tavalai, N.1    Papior, P.2    Rechter, S.3    Stamminger, T.4
  • 31
    • 33947410875 scopus 로고    scopus 로고
    • N-terminal determinants of human cytomegalovirus IE1 protein in nuclear targeting and disrupting PML-associated subnuclear structures
    • Lee HR, Huh YH, Kim YE, Lee K, Kim S, Ahn JH, N-terminal determinants of human cytomegalovirus IE1 protein in nuclear targeting and disrupting PML-associated subnuclear structures. Biochem Biophys Res Commun. 2007;356(2):499–504. 17367754
    • (2007) Biochem Biophys Res Commun , vol.356 , Issue.2 , pp. 499-504
    • Lee, H.R.1    Huh, Y.H.2    Kim, Y.E.3    Lee, K.4    Kim, S.5    Ahn, J.H.6
  • 32
    • 33644863208 scopus 로고    scopus 로고
    • A human cytomegalovirus antagonist of type I IFN-dependent signal transducer and activator of transcription signaling
    • Paulus C, Krauss S, Nevels M, A human cytomegalovirus antagonist of type I IFN-dependent signal transducer and activator of transcription signaling. Proc Natl Acad Sci U S A. 2006;103(10):3840–5. 16497831
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.10 , pp. 3840-3845
    • Paulus, C.1    Krauss, S.2    Nevels, M.3
  • 33
    • 55249109587 scopus 로고    scopus 로고
    • Binding STAT2 by the acidic domain of human cytomegalovirus IE1 promotes viral growth and is negatively regulated by SUMO
    • Huh YH, Kim YE, Kim ET, Park JJ, Song MJ, Zhu H, et al. Binding STAT2 by the acidic domain of human cytomegalovirus IE1 promotes viral growth and is negatively regulated by SUMO. J Virol. 2008;82(21):10444–54. doi: 10.1128/JVI.00833-08 18701593
    • (2008) J Virol , vol.82 , Issue.21 , pp. 10444-10454
    • Huh, Y.H.1    Kim, Y.E.2    Kim, E.T.3    Park, J.J.4    Song, M.J.5    Zhu, H.6
  • 34
    • 72849128449 scopus 로고    scopus 로고
    • Physical requirements and functional consequences of complex formation between the cytomegalovirus IE1 protein and human STAT2
    • Krauss S, Kaps J, Czech N, Paulus C, Nevels M, Physical requirements and functional consequences of complex formation between the cytomegalovirus IE1 protein and human STAT2. J Virol. 2009;83(24):12854–70. doi: 10.1128/JVI.01164-09 19812155
    • (2009) J Virol , vol.83 , Issue.24 , pp. 12854-12870
    • Krauss, S.1    Kaps, J.2    Czech, N.3    Paulus, C.4    Nevels, M.5
  • 35
    • 84863291329 scopus 로고    scopus 로고
    • The chromatin-tethering domain of human cytomegalovirus immediate-early (IE) 1 mediates associations of IE1, PML and STAT2 with mitotic chromosomes, but is not essential for viral replication
    • Shin HJ, Kim YE, Kim ET, Ahn JH, The chromatin-tethering domain of human cytomegalovirus immediate-early (IE) 1 mediates associations of IE1, PML and STAT2 with mitotic chromosomes, but is not essential for viral replication. J Gen Virol. 2012;93(Pt 4):716–21. doi: 10.1099/vir.0.037986-0 22158879
    • (2012) J Gen Virol , vol.93 , pp. 716-721
    • Shin, H.J.1    Kim, Y.E.2    Kim, E.T.3    Ahn, J.H.4
  • 36
    • 84912143439 scopus 로고    scopus 로고
    • Crystal structure of cytomegalovirus IE1 protein reveals targeting of TRIM family member PML via coiled-coil interactions
    • Scherer M, Klingl S, Sevvana M, Otto V, Schilling EM, Stump JD, et al. Crystal structure of cytomegalovirus IE1 protein reveals targeting of TRIM family member PML via coiled-coil interactions. PLoS Pathog. 2014;10(11):e1004512. doi: 10.1371/journal.ppat.1004512 25412268
    • (2014) PLoS Pathog , vol.10 , Issue.11
    • Scherer, M.1    Klingl, S.2    Sevvana, M.3    Otto, V.4    Schilling, E.M.5    Stump, J.D.6
  • 37
    • 10344222687 scopus 로고    scopus 로고
    • Human cytomegalovirus immediate-early 1 protein facilitates viral replication by antagonizing histone deacetylation
    • Nevels M, Paulus C, Shenk T, Human cytomegalovirus immediate-early 1 protein facilitates viral replication by antagonizing histone deacetylation. Proc Natl Acad Sci U S A. 2004;101(49):17234–9. 15572445
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.49 , pp. 17234-17239
    • Nevels, M.1    Paulus, C.2    Shenk, T.3
  • 38
    • 79951516890 scopus 로고    scopus 로고
    • PML positively regulates interferon gamma signaling
    • El Bougrini J, Dianoux L, Chelbi-Alix MK, PML positively regulates interferon gamma signaling. Biochimie. 2011;93(3):389–98. doi: 10.1016/j.biochi.2010.11.005 21115099
    • (2011) Biochimie , vol.93 , Issue.3 , pp. 389-398
    • El Bougrini, J.1    Dianoux, L.2    Chelbi-Alix, M.K.3
  • 39
    • 84869231649 scopus 로고    scopus 로고
    • PML promotes MHC class II gene expression by stabilizing the class II transactivator
    • Ulbricht T, Alzrigat M, Horch A, Reuter N, von Mikecz A, Steimle V, et al. PML promotes MHC class II gene expression by stabilizing the class II transactivator. The Journal of cell biology. 2012;199(1):49–63. doi: 10.1083/jcb.201112015 23007646
    • (2012) The Journal of cell biology , vol.199 , Issue.1 , pp. 49-63
    • Ulbricht, T.1    Alzrigat, M.2    Horch, A.3    Reuter, N.4    von Mikecz, A.5    Steimle, V.6
  • 41
    • 84893451810 scopus 로고    scopus 로고
    • ChREBP, a glucose-responsive transcriptional factor, enhances glucose metabolism to support biosynthesis in human cytomegalovirus-infected cells
    • Yu Y, Maguire TG, Alwine JC, ChREBP, a glucose-responsive transcriptional factor, enhances glucose metabolism to support biosynthesis in human cytomegalovirus-infected cells. Proc Natl Acad Sci U S A. 2014;111(5):1951–6. doi: 10.1073/pnas.1310779111 24449882
    • (2014) Proc Natl Acad Sci U S A , vol.111 , Issue.5 , pp. 1951-1956
    • Yu, Y.1    Maguire, T.G.2    Alwine, J.C.3
  • 42
    • 84877896292 scopus 로고    scopus 로고
    • RNAi induces innate immunity through multiple cellular signaling pathways
    • Meng Z, Zhang X, Wu J, Pei R, Xu Y, Yang D, et al. RNAi induces innate immunity through multiple cellular signaling pathways. PLoS One. 2013;8(5):e64708. doi: 10.1371/journal.pone.0064708 23700487
    • (2013) PLoS One , vol.8 , Issue.5
    • Meng, Z.1    Zhang, X.2    Wu, J.3    Pei, R.4    Xu, Y.5    Yang, D.6
  • 43
    • 0035099686 scopus 로고    scopus 로고
    • The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases
    • Wu WS, Vallian S, Seto E, Yang WM, Edmondson D, Roth S, et al. The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases. Mol Cell Biol. 2001;21(7):2259–68. 11259576
    • (2001) Mol Cell Biol , vol.21 , Issue.7 , pp. 2259-2268
    • Wu, W.S.1    Vallian, S.2    Seto, E.3    Yang, W.M.4    Edmondson, D.5    Roth, S.6
  • 44
    • 0031985313 scopus 로고    scopus 로고
    • Defective growth correlates with reduced accumulation of a viral DNA replication protein after low-multiplicity infection by a human cytomegalovirus ie1 mutant
    • Greaves RF, Mocarski ES, Defective growth correlates with reduced accumulation of a viral DNA replication protein after low-multiplicity infection by a human cytomegalovirus ie1 mutant. J Virol. 1998;72(1):366–79. 9420235
    • (1998) J Virol , vol.72 , Issue.1 , pp. 366-379
    • Greaves, R.F.1    Mocarski, E.S.2
  • 45
    • 84867652835 scopus 로고    scopus 로고
    • Requirement for the histone deacetylase Hdac3 for the inflammatory gene expression program in macrophages
    • Chen X, Barozzi I, Termanini A, Prosperini E, Recchiuti A, Dalli J, et al. Requirement for the histone deacetylase Hdac3 for the inflammatory gene expression program in macrophages. Proc Natl Acad Sci U S A. 2012;109(42):E2865–74. doi: 10.1073/pnas.1121131109 22802645
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.42 , pp. 74
    • Chen, X.1    Barozzi, I.2    Termanini, A.3    Prosperini, E.4    Recchiuti, A.5    Dalli, J.6
  • 46
    • 84880081839 scopus 로고    scopus 로고
    • Inhibition of viral pathogenesis and promotion of the septic shock response to bacterial infection by IRF-3 are regulated by the acetylation and phosphorylation of its coactivators
    • Chattopadhyay S, Fensterl V, Zhang Y, Veleeparambil M, Wetzel JL, Sen GC, Inhibition of viral pathogenesis and promotion of the septic shock response to bacterial infection by IRF-3 are regulated by the acetylation and phosphorylation of its coactivators. mBio. 2013;4(2). pii: e00636–12. doi: 10.1128/mBio.00636-12 23532979
    • (2013) mBio , vol.4 , Issue.2 , pp. 12
    • Chattopadhyay, S.1    Fensterl, V.2    Zhang, Y.3    Veleeparambil, M.4    Wetzel, J.L.5    Sen, G.C.6
  • 47
    • 82455175292 scopus 로고    scopus 로고
    • PKC alpha regulates Sendai virus-mediated interferon induction through HDAC6 and beta-catenin
    • Zhu J, Coyne CB, Sarkar SN, PKC alpha regulates Sendai virus-mediated interferon induction through HDAC6 and beta-catenin. EMBO J. 2011;30(23):4838–49. doi: 10.1038/emboj.2011.351 21952047
    • (2011) EMBO J , vol.30 , Issue.23 , pp. 4838-4849
    • Zhu, J.1    Coyne, C.B.2    Sarkar, S.N.3
  • 48
    • 0032569794 scopus 로고    scopus 로고
    • Proto-oncogene PML controls genes devoted to MHC class I antigen presentation
    • Zheng P, Guo Y, Niu Q, Levy DE, Dyck JA, Lu S, et al. Proto-oncogene PML controls genes devoted to MHC class I antigen presentation. Nature. 1998;396(6709):373–6. 9845074
    • (1998) Nature , vol.396 , Issue.6709 , pp. 373-376
    • Zheng, P.1    Guo, Y.2    Niu, Q.3    Levy, D.E.4    Dyck, J.A.5    Lu, S.6
  • 49
    • 0037866466 scopus 로고    scopus 로고
    • The PML gene is not involved in the regulation of MHC class I expression in human cell lines
    • Bruno S, Ghiotto F, Fais F, Fagioli M, Luzi L, Pelicci PG, et al. The PML gene is not involved in the regulation of MHC class I expression in human cell lines. Blood. 2003;101(9):3514–9. 12506025
    • (2003) Blood , vol.101 , Issue.9 , pp. 3514-3519
    • Bruno, S.1    Ghiotto, F.2    Fais, F.3    Fagioli, M.4    Luzi, L.5    Pelicci, P.G.6
  • 50
    • 84880081031 scopus 로고    scopus 로고
    • REST negatively and ISGF3 positively regulate the human STAT1 gene in melanoma
    • Amalraj J, Cutler SJ, Ghazawi I, Boyle GM, Ralph SJ, REST negatively and ISGF3 positively regulate the human STAT1 gene in melanoma. Mol Cancer Ther. 2013;12(7):1288–98. doi: 10.1158/1535-7163.MCT-12-0923 23598529
    • (2013) Mol Cancer Ther , vol.12 , Issue.7 , pp. 1288-1298
    • Amalraj, J.1    Cutler, S.J.2    Ghazawi, I.3    Boyle, G.M.4    Ralph, S.J.5
  • 52
    • 0033306577 scopus 로고    scopus 로고
    • Transcriptional repression by REST: recruitment of Sin3A and histone deacetylase to neuronal genes
    • Huang Y, Myers SJ, Dingledine R, Transcriptional repression by REST: recruitment of Sin3A and histone deacetylase to neuronal genes. Nature neuroscience. 1999;2(10):867–72. 10491605
    • (1999) Nature neuroscience , vol.2 , Issue.10 , pp. 867-872
    • Huang, Y.1    Myers, S.J.2    Dingledine, R.3
  • 53
    • 33845473249 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein functions as a negative regulator of IFN-gamma signaling
    • Choi YH, Bernardi R, Pandolfi PP, Benveniste EN, The promyelocytic leukemia protein functions as a negative regulator of IFN-gamma signaling. Proc Natl Acad Sci U S A. 2006;103(49):18715–20. 17121994
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.49 , pp. 18715-18720
    • Choi, Y.H.1    Bernardi, R.2    Pandolfi, P.P.3    Benveniste, E.N.4
  • 54
    • 84893504479 scopus 로고    scopus 로고
    • Primary macrophages rely on histone deacetylase 1 and 2 expression to induce type I interferon in response to gammaherpesvirus infection
    • Mounce BC, Mboko WP, Kanack AJ, Tarakanova VL, Primary macrophages rely on histone deacetylase 1 and 2 expression to induce type I interferon in response to gammaherpesvirus infection. J Virol. 2014;88(4):2268–78. doi: 10.1128/JVI.03278-13 24335310
    • (2014) J Virol , vol.88 , Issue.4 , pp. 2268-2278
    • Mounce, B.C.1    Mboko, W.P.2    Kanack, A.J.3    Tarakanova, V.L.4
  • 55
    • 0034015319 scopus 로고    scopus 로고
    • High efficiency retroviral vectors that contain no viral coding sequences
    • Yu SS, Kim JM, Kim S, High efficiency retroviral vectors that contain no viral coding sequences. Gene Ther. 2000;7(9):797–804. 10822307
    • (2000) Gene Ther , vol.7 , Issue.9 , pp. 797-804
    • Yu, S.S.1    Kim, J.M.2    Kim, S.3
  • 56
    • 0025931225 scopus 로고
    • A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription
    • Roth MB, Zahler AM, Stolk JA, A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription. J Cell Biol. 1991;115(3):587–96. 1717489
    • (1991) J Cell Biol , vol.115 , Issue.3 , pp. 587-596
    • Roth, M.B.1    Zahler, A.M.2    Stolk, J.A.3
  • 57
    • 36749048614 scopus 로고    scopus 로고
    • Functional interaction of the human cytomegalovirus IE2 protein with histone deacetylase 2 in infected human fibroblasts
    • Park JJ, Kim YE, Pham HT, Kim ET, Chung YH, Ahn JH, Functional interaction of the human cytomegalovirus IE2 protein with histone deacetylase 2 in infected human fibroblasts. J Gen Virol. 2007;88(Pt 12):3214–23. 18024889
    • (2007) J Gen Virol , vol.88 , pp. 3214-3223
    • Park, J.J.1    Kim, Y.E.2    Pham, H.T.3    Kim, E.T.4    Chung, Y.H.5    Ahn, J.H.6
  • 58
    • 80655143462 scopus 로고    scopus 로고
    • Human cytomegalovirus infection causes degradation of Sp100 proteins that suppress viral gene expression
    • Kim YE, Lee JH, Kim ET, Shin HJ, Gu SY, Seol HS, et al. Human cytomegalovirus infection causes degradation of Sp100 proteins that suppress viral gene expression. J Virol. 2011;85(22):11928–37. doi: 10.1128/JVI.00758-11 21880768
    • (2011) J Virol , vol.85 , Issue.22 , pp. 11928-11937
    • Kim, Y.E.1    Lee, J.H.2    Kim, E.T.3    Shin, H.J.4    Gu, S.Y.5    Seol, H.S.6
  • 59
    • 84865658869 scopus 로고    scopus 로고
    • Microarray analysis revealing common and distinct functions of promyelocytic leukemia protein (PML) and tumor necrosis factor alpha (TNFalpha) signaling in endothelial cells
    • Cheng X, Kao HY, Microarray analysis revealing common and distinct functions of promyelocytic leukemia protein (PML) and tumor necrosis factor alpha (TNFalpha) signaling in endothelial cells. BMC Genomics. 2012;13:453. doi: 10.1186/1471-2164-13-453 22947142
    • (2012) BMC Genomics , vol.13 , pp. 453
    • Cheng, X.1    Kao, H.Y.2
  • 60
    • 84904596068 scopus 로고    scopus 로고
    • Analysis of Human Cytomegalovirus-enoded SUMO trgets and temporal regulation of SUMOylation of the immediate-early proteins IE1 and IE2 during infection
    • Kim ET, Kim YE, Kim YJ, Lee MK, Hayward GS, Ahn JH, Analysis of Human Cytomegalovirus-enoded SUMO trgets and temporal regulation of SUMOylation of the immediate-early proteins IE1 and IE2 during infection. PLoS One. 2014;9(7):e103308. doi: 10.1371/journal.pone.0103308 25050850
    • (2014) PLoS One , vol.9 , Issue.7
    • Kim, E.T.1    Kim, Y.E.2    Kim, Y.J.3    Lee, M.K.4    Hayward, G.S.5    Ahn, J.H.6
  • 61
    • 0026532516 scopus 로고
    • A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies
    • Stuurman N, de Graaf A, Floore A, Josso A, Humbel B, de Jong L, et al. A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies. J Cell Sci. 1992;101 (Pt 4):773–84. 1527179
    • (1992) J Cell Sci , vol.101 , pp. 773-784
    • Stuurman, N.1    de Graaf, A.2    Floore, A.3    Josso, A.4    Humbel, B.5    de Jong, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.