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Volumn 10, Issue 11, 2014, Pages

Crystal Structure of Cytomegalovirus IE1 Protein Reveals Targeting of TRIM Family Member PML via Coiled-Coil Interactions

Author keywords

[No Author keywords available]

Indexed keywords

CYTOMEGALOVIRUS IE1 PROTEIN; IMMEDIATE EARLY PROTEIN; OLIGONUCLEOTIDE; PROMYELOCYTIC LEUKEMIA PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; CARRIER PROTEIN; IE1 PROTEIN, CYTOMEGALOVIRUS; TRIM5 PROTEIN, HUMAN;

EID: 84912143439     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004512     Document Type: Article
Times cited : (58)

References (85)
  • 1
    • 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.
    • (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
  • 2
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCC/TRIM motif
    • Jensen K, Shiels C, Freemont PS, (2001) PML protein isoforms and the RBCC/TRIM motif. Oncogene 20: 7223–7233.
    • (2001) Oncogene , vol.20 , pp. 7223-7233
    • Jensen, K.1    Shiels, C.2    Freemont, P.S.3
  • 3
    • 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.
    • (2014) J Mol Biol , vol.426 , pp. 1265-1284
    • Rajsbaum, R.1    Garcia-Sastre, A.2    Versteeg, G.A.3
  • 4
    • 84874256730 scopus 로고    scopus 로고
    • The E3-ligase TRIM family of proteins regulates signaling pathways triggered by innate immune pattern-recognition receptors
    • Versteeg GA, Rajsbaum R, Sanchez-Aparicio MT, Maestre AM, Valdiviezo J, et al. (2013) The E3-ligase TRIM family of proteins regulates signaling pathways triggered by innate immune pattern-recognition receptors. Immunity 38: 384–398.
    • (2013) Immunity , vol.38 , pp. 384-398
    • Versteeg, G.A.1    Rajsbaum, R.2    Sanchez-Aparicio, M.T.3    Maestre, A.M.4    Valdiviezo, J.5
  • 5
    • 79952281303 scopus 로고    scopus 로고
    • SUMO E3 ligase activity of TRIM proteins
    • Chu Y, Yang X, (2011) SUMO E3 ligase activity of TRIM proteins. Oncogene 30: 1108–1116.
    • (2011) Oncogene , vol.30 , pp. 1108-1116
    • Chu, Y.1    Yang, X.2
  • 7
    • 0035908032 scopus 로고    scopus 로고
    • Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation
    • Lallemand-Breitenbach V, Zhu J, Puvion F, Koken M, Honore N, et al. (2001) Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation. J Exp Med 193: 1361–1371.
    • (2001) J Exp Med , vol.193 , pp. 1361-1371
    • Lallemand-Breitenbach, V.1    Zhu, J.2    Puvion, F.3    Koken, M.4    Honore, N.5
  • 8
    • 1642512435 scopus 로고    scopus 로고
    • Role of PML and the PML-nuclear body in the control of programmed cell death
    • Bernardi R, Pandolfi PP, (2003) Role of PML and the PML-nuclear body in the control of programmed cell death. Oncogene 22: 9048–9057.
    • (2003) Oncogene , vol.22 , pp. 9048-9057
    • Bernardi, R.1    Pandolfi, P.P.2
  • 9
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • Bernardi R, Pandolfi PP, (2007) Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat Rev Mol Cell Biol 8: 1006–1016.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 10
    • 54549084341 scopus 로고    scopus 로고
    • New insights into the role of the subnuclear structure ND10 for viral infection
    • Tavalai N, Stamminger T, (2008) New insights into the role of the subnuclear structure ND10 for viral infection. Biochim Biophys Acta 1783: 2207–2221.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 2207-2221
    • Tavalai, N.1    Stamminger, T.2
  • 11
    • 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: 819–830.
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 13
    • 9244260598 scopus 로고    scopus 로고
    • Intrinsic immunity: a front-line defense against viral attack
    • Bieniasz PD, (2004) Intrinsic immunity: a front-line defense against viral attack. Nat Immunol 5: 1109–1115.
    • (2004) Nat Immunol , vol.5 , pp. 1109-1115
    • Bieniasz, P.D.1
  • 14
    • 33845968505 scopus 로고    scopus 로고
    • Human Daxx-mediated repression of human cytomegalovirus gene expression correlates with a repressive chromatin structure around the major immediate early promoter
    • Woodhall DL, Groves IJ, Reeves MB, Wilkinson G, Sinclair JH, (2006) Human Daxx-mediated repression of human cytomegalovirus gene expression correlates with a repressive chromatin structure around the major immediate early promoter. J Biol Chem 281: 37652–37660.
    • (2006) J Biol Chem , vol.281 , pp. 37652-37660
    • Woodhall, D.L.1    Groves, I.J.2    Reeves, M.B.3    Wilkinson, G.4    Sinclair, J.H.5
  • 15
    • 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, (2006) Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections. J Virol 80: 8006–8018.
    • (2006) J Virol , vol.80 , pp. 8006-8018
    • Tavalai, N.1    Papior, P.2    Rechter, S.3    Leis, M.4    Stamminger, T.5
  • 16
    • 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, (2008) Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection. J Virol 82: 126–137.
    • (2008) J Virol , vol.82 , pp. 126-137
    • Tavalai, N.1    Papior, P.2    Rechter, S.3    Stamminger, T.4
  • 17
    • 57349108706 scopus 로고    scopus 로고
    • Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection
    • Lukashchuk V, McFarlane S, Everett RD, Preston CM, (2008) Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection. J Virol 82: 12543–12554.
    • (2008) J Virol , vol.82 , pp. 12543-12554
    • Lukashchuk, V.1    McFarlane, S.2    Everett, R.D.3    Preston, C.M.4
  • 18
    • 79959290376 scopus 로고    scopus 로고
    • Human cytomegalovirus immediate-early gene expression is restricted by the nuclear domain 10 component Sp100
    • Adler M, Tavalai N, Muller R, Stamminger T, (2011) Human cytomegalovirus immediate-early gene expression is restricted by the nuclear domain 10 component Sp100. J Gen Virol 92: 1532–1538.
    • (2011) J Gen Virol , vol.92 , pp. 1532-1538
    • Adler, M.1    Tavalai, N.2    Muller, R.3    Stamminger, T.4
  • 19
    • 84873816597 scopus 로고    scopus 로고
    • Components of promyelocytic leukemia nuclear bodies (ND10) act cooperatively to repress herpesvirus infection
    • Glass M, Everett RD, (2013) Components of promyelocytic leukemia nuclear bodies (ND10) act cooperatively to repress herpesvirus infection. J Virol 87: 2174–2185.
    • (2013) J Virol , vol.87 , pp. 2174-2185
    • Glass, M.1    Everett, R.D.2
  • 20
    • 33645757807 scopus 로고    scopus 로고
    • Inactivating a cellular intrinsic immune defense mediated by Daxx is the mechanism through which the human cytomegalovirus pp71 protein stimulates viral immediate-early gene expression
    • Saffert RT, Kalejta RF, (2006) Inactivating a cellular intrinsic immune defense mediated by Daxx is the mechanism through which the human cytomegalovirus pp71 protein stimulates viral immediate-early gene expression. J Virol 80: 3863–3871.
    • (2006) J Virol , vol.80 , pp. 3863-3871
    • Saffert, R.T.1    Kalejta, R.F.2
  • 21
    • 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, et al. (2011) A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence. PLoS Pathog 7: e1002245.
    • (2011) PLoS Pathog , vol.7 , pp. e1002245
    • Boutell, C.1    Cuchet-Lourenco, D.2    Vanni, E.3    Orr, A.4    Glass, M.5
  • 22
    • 84899996201 scopus 로고    scopus 로고
    • The human cytomegalovirus IE1 protein - past and present developments
    • Scherer M, Stamminger T, (2014) The human cytomegalovirus IE1 protein - past and present developments. Future Virology 9: 415–430.
    • (2014) Future Virology , vol.9 , pp. 415-430
    • Scherer, M.1    Stamminger, T.2
  • 23
    • 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, (1998) Disruption of PML-associated nuclear bodies mediated by the human cytomegalovirus major immediate early gene product. J Gen Virol 79 (Pt 5): 1233–1245.
    • (1998) J Gen Virol 79 (Pt , vol.5 , pp. 1233-1245
    • Wilkinson, G.W.1    Kelly, C.2    Sinclair, J.H.3    Rickards, C.4
  • 24
    • 0034755352 scopus 로고    scopus 로고
    • Proteasome-independent disruption of PML oncogenic domains (PODs), but not covalent modification by SUMO-1, is required for human cytomegalovirus immediate-early protein IE1 to inhibit PML-mediated transcriptional repression
    • Xu Y, Ahn JH, Cheng M, apRhys CM, Chiou CJ, et al. (2001) Proteasome-independent disruption of PML oncogenic domains (PODs), but not covalent modification by SUMO-1, is required for human cytomegalovirus immediate-early protein IE1 to inhibit PML-mediated transcriptional repression. J Virol 75: 10683–10695.
    • (2001) J Virol , vol.75 , pp. 10683-10695
    • Xu, Y.1    Ahn, J.H.2    Cheng, M.3    apRhys, C.M.4    Chiou, C.J.5
  • 25
    • 10644231699 scopus 로고    scopus 로고
    • The carboxyl-terminal region of human cytomegalovirus IE1491aa contains an acidic domain that plays a regulatory role and a chromatin-tethering domain that is dispensable during viral replication
    • Reinhardt J, Smith GB, Himmelheber CT, zizkhan-Clifford J, Mocarski ES, (2005) The carboxyl-terminal region of human cytomegalovirus IE1491aa contains an acidic domain that plays a regulatory role and a chromatin-tethering domain that is dispensable during viral replication. J Virol 79: 225–233.
    • (2005) J Virol , vol.79 , pp. 225-233
    • Reinhardt, J.1    Smith, G.B.2    Himmelheber, C.T.3    Zizkhan-Clifford, J.4    Mocarski, E.S.5
  • 26
    • 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, et al. (2007) N-terminal determinants of human cytomegalovirus IE1 protein in nuclear targeting and disrupting PML-associated subnuclear structures. Biochem Biophys Res Commun 356: 499–504.
    • (2007) Biochem Biophys Res Commun , vol.356 , pp. 499-504
    • Lee, H.R.1    Huh, Y.H.2    Kim, Y.E.3    Lee, K.4    Kim, S.5
  • 27
    • 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, (2006) A human cytomegalovirus antagonist of type I IFN-dependent signal transducer and activator of transcription signaling. Proc Natl Acad Sci U S A 103: 3840–3845.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 3840-3845
    • Paulus, C.1    Krauss, S.2    Nevels, M.3
  • 28
    • 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, (2009) Physical requirements and functional consequences of complex formation between the cytomegalovirus IE1 protein and human STAT2. J Virol 83: 12854–12870.
    • (2009) J Virol , vol.83 , pp. 12854-12870
    • Krauss, S.1    Kaps, J.2    Czech, N.3    Paulus, C.4    Nevels, M.5
  • 29
    • 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, et al. (2008) Binding STAT2 by the acidic domain of human cytomegalovirus IE1 promotes viral growth and is negatively regulated by SUMO. J Virol 82: 10444–10454.
    • (2008) J Virol , vol.82 , pp. 10444-10454
    • Huh, Y.H.1    Kim, Y.E.2    Kim, E.T.3    Park, J.J.4    Song, M.J.5
  • 30
    • 0028972538 scopus 로고
    • Disruption of PML-associated nuclear bodies during human cytomegalovirus infection
    • Kelly C, van DR, Wilkinson GW, (1995) Disruption of PML-associated nuclear bodies during human cytomegalovirus infection. J Gen Virol 76 (Pt 11): 2887–2893.
    • (1995) J Gen Virol 76 (Pt , vol.11 , pp. 2887-2893
    • Kelly, C.1    van, D.R.2    Wilkinson, G.W.3
  • 31
    • 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, (1996) The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1. Exp Cell Res 229: 155–158.
    • (1996) Exp Cell Res , vol.229 , pp. 155-158
    • Korioth, F.1    Maul, G.G.2    Plachter, B.3    Stamminger, T.4    Frey, J.5
  • 32
    • 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, (1997) 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 71: 4599–4613.
    • (1997) J Virol , vol.71 , pp. 4599-4613
    • Ahn, J.H.1    Hayward, G.S.2
  • 33
    • 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, (2000) 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 274: 39–55.
    • (2000) Virology , vol.274 , pp. 39-55
    • Ahn, J.H.1    Hayward, G.S.2
  • 34
    • 0344299239 scopus 로고    scopus 로고
    • Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption
    • Muller S, Dejean A, (1999) Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption. J Virol 73: 5137–5143.
    • (1999) J Virol , vol.73 , pp. 5137-5143
    • Muller, S.1    Dejean, A.2
  • 35
    • 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, et al. (2004) 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. Journal of Virology 78: 6527–6542.
    • (2004) Journal of Virology , vol.78 , pp. 6527-6542
    • Lee, H.R.1    Kim, D.J.2    Lee, J.M.3    Choi, C.Y.4    Ahn, B.Y.5
  • 36
    • 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, IIIHayward GS, (1998) 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 18: 4899–4913.
    • (1998) Mol Cell Biol , vol.18 , pp. 4899-4913
    • Ahn, J.H.1    Brignole, E.J.2    Hayward, G.S.3
  • 37
    • 0028970383 scopus 로고
    • CCAAT box-dependent activation of the TATA-less human DNA polymerase alpha promoter by the human cytomegalovirus 72-kilodalton major immediate-early protein
    • Hayhurst GP, Bryant LA, Caswell RC, Walker SM, Sinclair JH, (1995) CCAAT box-dependent activation of the TATA-less human DNA polymerase alpha promoter by the human cytomegalovirus 72-kilodalton major immediate-early protein. J Virol 69: 182–188.
    • (1995) J Virol , vol.69 , pp. 182-188
    • Hayhurst, G.P.1    Bryant, L.A.2    Caswell, R.C.3    Walker, S.M.4    Sinclair, J.H.5
  • 38
    • 0024374201 scopus 로고
    • Expression of the acidic nuclear immediate-early protein (IE1) of human cytomegalovirus in stable cell lines and its preferential association with metaphase chromosomes
    • LaFemina RL, Pizzorno MC, Mosca JD, Hayward GS, (1989) Expression of the acidic nuclear immediate-early protein (IE1) of human cytomegalovirus in stable cell lines and its preferential association with metaphase chromosomes. Virology 172: 584–600.
    • (1989) Virology , vol.172 , pp. 584-600
    • LaFemina, R.L.1    Pizzorno, M.C.2    Mosca, J.D.3    Hayward, G.S.4
  • 39
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztanyi Z, Csizmok V, Tompa P, Simon I, (2005) IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21: 3433–3434.
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 40
  • 41
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield NJ, (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1: 2876–2890.
    • (2006) Nat Protoc , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 42
    • 0036444017 scopus 로고    scopus 로고
    • Generalized Crick equations for modeling noncanonical coiled coils
    • Offer G, Hicks MR, Woolfson DN, (2002) Generalized Crick equations for modeling noncanonical coiled coils. J Struct Biol 137: 41–53.
    • (2002) J Struct Biol , vol.137 , pp. 41-53
    • Offer, G.1    Hicks, M.R.2    Woolfson, D.N.3
  • 43
    • 0343063933 scopus 로고
    • Structure of proteins: packing of alpha-helices and pleated sheets
    • Chothia C, Levitt M, Richardson D, (1977) Structure of proteins: packing of alpha-helices and pleated sheets. Proc Natl Acad Sci U S A 74: 4130–4134.
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 4130-4134
    • Chothia, C.1    Levitt, M.2    Richardson, D.3
  • 45
    • 84901824023 scopus 로고    scopus 로고
    • Structural insights into the TRIM family of ubiquitin E3 ligases
    • Li Y, Wu H, Wu W, Zhuo W, Liu W, et al. (2014) Structural insights into the TRIM family of ubiquitin E3 ligases. Cell Res 24: 762–765.
    • (2014) Cell Res , vol.24 , pp. 762-765
    • Li, Y.1    Wu, H.2    Wu, W.3    Zhuo, W.4    Liu, W.5
  • 46
    • 84903694269 scopus 로고    scopus 로고
    • Structural studies of postentry restriction factors reveal antiparallel dimers that enable avid binding to the HIV-1 capsid lattice
    • Goldstone DC, Walker PA, Calder LJ, Coombs PJ, Kirkpatrick J, et al. (2014) Structural studies of postentry restriction factors reveal antiparallel dimers that enable avid binding to the HIV-1 capsid lattice. Proc Natl Acad Sci U S A 111: 9609–9614.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 9609-9614
    • Goldstone, D.C.1    Walker, P.A.2    Calder, L.J.3    Coombs, P.J.4    Kirkpatrick, J.5
  • 47
    • 84891707336 scopus 로고    scopus 로고
    • Human cytomegalovirus major immediate early 1 protein targets host chromosomes by docking to the acidic pocket on the nucleosome surface
    • Mucke K, Paulus C, Bernhardt K, Gerrer K, Schon K, et al. (2014) Human cytomegalovirus major immediate early 1 protein targets host chromosomes by docking to the acidic pocket on the nucleosome surface. J Virol 88: 1228–1248.
    • (2014) J Virol , vol.88 , pp. 1228-1248
    • Mucke, K.1    Paulus, C.2    Bernhardt, K.3    Gerrer, K.4    Schon, K.5
  • 48
    • 0031878851 scopus 로고    scopus 로고
    • The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms
    • Everett RD, Freemont P, Saitoh H, Dasso M, Orr A, et al. (1998) The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J Virol 72: 6581–6591.
    • (1998) J Virol , vol.72 , pp. 6581-6591
    • Everett, R.D.1    Freemont, P.2    Saitoh, H.3    Dasso, M.4    Orr, A.5
  • 49
    • 84861303373 scopus 로고    scopus 로고
    • Herpesvirus saimiri antagonizes nuclear domain 10-instituted intrinsic immunity via an ORF3-mediated selective degradation of cellular protein Sp100
    • Full F, Reuter N, Zielke K, Stamminger T, Ensser A, (2012) Herpesvirus saimiri antagonizes nuclear domain 10-instituted intrinsic immunity via an ORF3-mediated selective degradation of cellular protein Sp100. J Virol 86: 3541–3553.
    • (2012) J Virol , vol.86 , pp. 3541-3553
    • Full, F.1    Reuter, N.2    Zielke, K.3    Stamminger, T.4    Ensser, A.5
  • 50
    • 84893715483 scopus 로고    scopus 로고
    • Kaposi's sarcoma associated herpesvirus tegument protein ORF75 is essential for viral lytic replication and plays a critical role in the antagonization of ND10-instituted intrinsic immunity
    • Full F, Jungnickl D, Reuter N, Bogner E, Brulois K, et al. (2014) Kaposi's sarcoma associated herpesvirus tegument protein ORF75 is essential for viral lytic replication and plays a critical role in the antagonization of ND10-instituted intrinsic immunity. PLoS Pathog 10: e1003863.
    • (2014) PLoS Pathog , vol.10 , pp. e1003863
    • Full, F.1    Jungnickl, D.2    Reuter, N.3    Bogner, E.4    Brulois, K.5
  • 51
    • 79955079235 scopus 로고    scopus 로고
    • Functional reorganization of promyelocytic leukemia nuclear bodies during BK virus infection
    • Jiang M, Entezami P, Gamez M, Stamminger T, Imperiale MJ, (2011) Functional reorganization of promyelocytic leukemia nuclear bodies during BK virus infection. MBio 2: e00281–10.
    • (2011) MBio , vol.2
    • Jiang, M.1    Entezami, P.2    Gamez, M.3    Stamminger, T.4    Imperiale, M.J.5
  • 52
    • 0034603179 scopus 로고    scopus 로고
    • Differential regulation of sentrinized proteins by a novel sentrin-specific protease
    • Gong L, Millas S, Maul GG, Yeh ET, (2000) Differential regulation of sentrinized proteins by a novel sentrin-specific protease. J Biol Chem 275: 3355–3359.
    • (2000) J Biol Chem , vol.275 , pp. 3355-3359
    • Gong, L.1    Millas, S.2    Maul, G.G.3    Yeh, E.T.4
  • 53
    • 33746824547 scopus 로고    scopus 로고
    • Inhibition of SUMO-independent PML oligomerization by the human cytomegalovirus IE1 protein
    • Kang H, Kim ET, Lee HR, Park JJ, Go YY, et al. (2006) Inhibition of SUMO-independent PML oligomerization by the human cytomegalovirus IE1 protein. J Gen Virol 87: 2181–2190.
    • (2006) J Gen Virol , vol.87 , pp. 2181-2190
    • Kang, H.1    Kim, E.T.2    Lee, H.R.3    Park, J.J.4    Go, Y.Y.5
  • 54
    • 80052490932 scopus 로고    scopus 로고
    • Evidence for a dual antiviral role of the major nuclear domain 10 component Sp100 during the immediate-early and late phases of the human cytomegalovirus replication cycle
    • Tavalai N, Adler M, Scherer M, Riedl Y, Stamminger T, (2011) Evidence for a dual antiviral role of the major nuclear domain 10 component Sp100 during the immediate-early and late phases of the human cytomegalovirus replication cycle. J Virol 85: 9447–9458.
    • (2011) J Virol , vol.85 , pp. 9447-9458
    • Tavalai, N.1    Adler, M.2    Scherer, M.3    Riedl, Y.4    Stamminger, T.5
  • 55
    • 84867564497 scopus 로고    scopus 로고
    • A structural basis for the assembly and functions of a viral polymer that inactivates multiple tumor suppressors
    • Ou HD, Kwiatkowski W, Deerinck TJ, Noske A, Blain KY, et al. (2012) A structural basis for the assembly and functions of a viral polymer that inactivates multiple tumor suppressors. Cell 151: 304–319.
    • (2012) Cell , vol.151 , pp. 304-319
    • Ou, H.D.1    Kwiatkowski, W.2    Deerinck, T.J.3    Noske, A.4    Blain, K.Y.5
  • 56
    • 65549164536 scopus 로고    scopus 로고
    • Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I
    • Gack MU, Albrecht RA, Urano T, Inn KS, Huang IC, et al. (2009) Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I. Cell Host Microbe 5: 439–449.
    • (2009) Cell Host Microbe , vol.5 , pp. 439-449
    • Gack, M.U.1    Albrecht, R.A.2    Urano, T.3    Inn, K.S.4    Huang, I.C.5
  • 57
    • 84891647180 scopus 로고    scopus 로고
    • Identification of cellular proteins that interact with human cytomegalovirus immediate-early protein 1 by protein array assay
    • Martinez FP, Tang Q, (2014) Identification of cellular proteins that interact with human cytomegalovirus immediate-early protein 1 by protein array assay. Viruses 6: 89–105.
    • (2014) Viruses , vol.6 , pp. 89-105
    • Martinez, F.P.1    Tang, Q.2
  • 58
    • 33846298499 scopus 로고    scopus 로고
    • Lysine methylation as a routine rescue strategy for protein crystallization
    • Walter TS, Meier C, Assenberg R, Au KF, Ren J, et al. (2006) Lysine methylation as a routine rescue strategy for protein crystallization. Structure 14: 1617–1622.
    • (2006) Structure , vol.14 , pp. 1617-1622
    • Walter, T.S.1    Meier, C.2    Assenberg, R.3    Au, K.F.4    Ren, J.5
  • 60
    • 0026206788 scopus 로고
    • Sparse matrix sampling: a screening method for crystallization of proteins
    • Jancarik J, Kim S-H, (1991) Sparse matrix sampling: a screening method for crystallization of proteins. J Appl Cryst 24: 409–411.
    • (1991) J Appl Cryst , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.-H.2
  • 61
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW, (1968) Solvent content of protein crystals. J Mol Biol 33: 491–497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 64
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: combining chain tracing with density modification
    • Sheldrick GM, (2010) Experimental phasing with SHELXC/D/E: combining chain tracing with density modification. Acta Crystallogr D Biol Crystallogr 66: 479–485.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 67
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0
    • Bricogne G, Vonrhein C, Flensburg C, Schiltz M, Paciorek W, (2003) Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr D Biol Crystallogr 59: 2023–2030.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 72
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774–797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 73
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL, (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779–815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 74
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl MJ, (1993) Recognition of errors in three-dimensional structures of proteins. Proteins 17: 355–362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 75
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins
    • Wiederstein M, Sippl MJ, (2007) ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res 35: W407–W410.
    • (2007) Nucleic Acids Res , vol.35 , pp. W407-W410
    • Wiederstein, M.1    Sippl, M.J.2
  • 76
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K, (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60: 2256–2268.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 78
  • 80
    • 0343340071 scopus 로고    scopus 로고
    • Covalent modification of the transactivator protein IE2-p86 of human cytomegalovirus by conjugation to the ubiquitin-homologous proteins SUMO-1 and hSMT3b
    • Hofmann H, Floss S, Stamminger T, (2000) Covalent modification of the transactivator protein IE2-p86 of human cytomegalovirus by conjugation to the ubiquitin-homologous proteins SUMO-1 and hSMT3b. J Virol 74: 2510–2524.
    • (2000) J Virol , vol.74 , pp. 2510-2524
    • Hofmann, H.1    Floss, S.2    Stamminger, T.3
  • 81
    • 0036091745 scopus 로고    scopus 로고
    • Functional interaction between the pp71 protein of human cytomegalovirus and the PML-interacting protein human Daxx
    • Hofmann H, Sindre H, Stamminger T, (2002) Functional interaction between the pp71 protein of human cytomegalovirus and the PML-interacting protein human Daxx. J Virol 76: 5769–5783.
    • (2002) J Virol , vol.76 , pp. 5769-5783
    • Hofmann, H.1    Sindre, H.2    Stamminger, T.3
  • 82
    • 84877940759 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier (SUMO) pathway-mediated enhancement of human cytomegalovirus replication correlates with a recruitment of SUMO-1/3 proteins to viral replication compartments
    • Scherer M, Reuter N, Wagenknecht N, Otto V, Sticht H, et al. (2013) Small ubiquitin-related modifier (SUMO) pathway-mediated enhancement of human cytomegalovirus replication correlates with a recruitment of SUMO-1/3 proteins to viral replication compartments. J Gen Virol 94: 1373–1384.
    • (2013) J Gen Virol , vol.94 , pp. 1373-1384
    • Scherer, M.1    Reuter, N.2    Wagenknecht, N.3    Otto, V.4    Sticht, H.5
  • 83
    • 33645053126 scopus 로고    scopus 로고
    • Two-step red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli
    • Tischer BK, von EJ, Kaufer B, Osterrieder N, (2006) Two-step red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli. Biotechniques 40: 191–197.
    • (2006) Biotechniques , vol.40 , pp. 191-197
    • Tischer, B.K.1    von, E.J.2    Kaufer, B.3    Osterrieder, N.4
  • 84
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL, (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97: 6640–6645.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2


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