메뉴 건너뛰기




Volumn 88, Issue 11, 2014, Pages 6076-6092

Sp100 isoform-specific regulation of human adenovirus 5 gene expression

Author keywords

[No Author keywords available]

Indexed keywords

DAXX PROTEIN; HETEROCHROMATIN PROTEIN 1; MEMBRANE PROTEIN; PROTEIN ATRX; PROTEIN SP100; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84899888123     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00469-14     Document Type: Article
Times cited : (42)

References (119)
  • 1
    • 0027095906 scopus 로고
    • IFN enhance expression of Sp100, an autoantigen in primary biliary cirrhosis
    • Guldner HH, Szostecki C, Grotzinger T, Will H. 1992. IFN enhance expression of Sp100, an autoantigen in primary biliary cirrhosis. J. Immunol. 149:4067-4073.
    • (1992) J. Immunol. , vol.149 , pp. 4067-4073
    • Guldner, H.H.1    Szostecki, C.2    Grotzinger, T.3    Will, H.4
  • 2
    • 0029894340 scopus 로고    scopus 로고
    • Interferonmodulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML)
    • Grotzinger T, Sternsdorf T, Jensen K, Will H. 1996. Interferonmodulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML). Eur. J. Biochem. 238:554-560. http://dx. doi. org/10. 1111/j. 1432-1033. 1996. 0554z. x.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 554-560
    • Grotzinger, T.1    Sternsdorf, T.2    Jensen, K.3    Will, H.4
  • 3
    • 0032560469 scopus 로고    scopus 로고
    • Chromatin components as part of a putative transcriptional repressing complex
    • Lehming N, Le Saux A, Schuller J, Ptashne M. 1998. Chromatin components as part of a putative transcriptional repressing complex. Proc. Natl. Acad. Sci. USA. 95:7322-7326. http://dx. doi. org/10. 1073/pnas. 95. 13. 7322.
    • (1998) Proc. Natl. Acad. Sci. USA. , vol.95 , pp. 7322-7326
    • Lehming, N.1    Le Saux, A.2    Schuller, J.3    Ptashne, M.4
  • 4
    • 0025633966 scopus 로고
    • Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis
    • Szostecki C, Guldner HH, Netter HJ, Will H. 1990. Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis. J. Immunol. 145:4338-4347.
    • (1990) J. Immunol. , vol.145 , pp. 4338-4347
    • Szostecki, C.1    Guldner, H.H.2    Netter, H.J.3    Will, H.4
  • 5
    • 0023142958 scopus 로고
    • Autoimmune sera recognize a 100 kD nuclear protein antigen (sp-100)
    • Szostecki C, Krippner H, Penner E, Bautz FA. 1987. Autoimmune sera recognize a 100 kD nuclear protein antigen (sp-100). Clin. Exp. Immunol. 68:108-116.
    • (1987) Clin. Exp. Immunol. , vol.68 , pp. 108-116
    • Szostecki, C.1    Krippner, H.2    Penner, E.3    Bautz, F.A.4
  • 6
    • 0026713520 scopus 로고
    • Autoantibodies to the nuclear Sp100 protein in primary biliary cirrhosis and associated diseases: epitope specificity and immunoglobulin class distribution
    • Szostecki C, Will H, Netter HJ, Guldner HH. 1992. Autoantibodies to the nuclear Sp100 protein in primary biliary cirrhosis and associated diseases: epitope specificity and immunoglobulin class distribution. Scand. J. Immunol. 36:555-564. http://dx. doi. org/10. 1111/j. 1365-3083. 1992. tb03224. x.
    • (1992) Scand. J. Immunol. , vol.36 , pp. 555-564
    • Szostecki, C.1    Will, H.2    Netter, H.J.3    Guldner, H.H.4
  • 7
    • 0026513504 scopus 로고
    • Genomic variability and alternative splicing generate multiple PML/RAR alpha transcripts that encode aberrant PML proteins and PML/RAR alpha isoforms in acute promyelocytic leukaemia
    • Pandolfi PP, Alcalay M, Fagioli M, Zangrilli D, Mencarelli A, Diverio D, Biondi A, Lo Coco F, Rambaldi A, Grignani F. 1992. Genomic variability and alternative splicing generate multiple PML/RAR alpha transcripts that encode aberrant PML proteins and PML/RAR alpha isoforms in acute promyelocytic leukaemia. EMBO J. 11:1397-1407.
    • (1992) EMBO J. , vol.11 , pp. 1397-1407
    • Pandolfi, P.P.1    Alcalay, M.2    Fagioli, M.3    Zangrilli, D.4    Mencarelli, A.5    Diverio, D.6    Biondi, A.7    Lo Coco, F.8    Rambaldi, A.9    Grignani, F.10
  • 9
    • 0027520499 scopus 로고
    • Nuclear dot antigens may specify transcriptional domains in the nucleus
    • Xie K, Lambie EJ, Snyder M. 1993. Nuclear dot antigens may specify transcriptional domains in the nucleus. Mol. Cell. Biol. 13:6170-6179.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6170-6179
    • Xie, K.1    Lambie, E.J.2    Snyder, M.3
  • 10
    • 0029845262 scopus 로고    scopus 로고
    • LYSP100-associated nuclear domains (LANDs): description of a new class of subnuclear structures and their relationship to PML nuclear bodies
    • Dent AL, Yewdell J, Puvion-Dutilleul F, Koken MH, de The H, Staudt LM. 1996. LYSP100-associated nuclear domains (LANDs): description of a new class of subnuclear structures and their relationship to PML nuclear bodies. Blood 88:1423-1426.
    • (1996) Blood , vol.88 , pp. 1423-1426
    • Dent, A.L.1    Yewdell, J.2    Puvion-Dutilleul, F.3    Koken, M.H.4    de The, H.5    Staudt, L.M.6
  • 11
    • 0035028618 scopus 로고    scopus 로고
    • Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role ofSUMOmodification
    • Seeler JS, Marchio A, Losson R, Desterro JM, Hay RT, Chambon P, Dejean A. 2001. Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role ofSUMOmodification. Mol. Cell. Biol. 21:3314-3324. http://dx. doi. org/10. 1128/MCB. 21. 10. 3314-3324. 2001.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3314-3324
    • Seeler, J.S.1    Marchio, A.2    Losson, R.3    Desterro, J.M.4    Hay, R.T.5    Chambon, P.6    Dejean, A.7
  • 12
    • 0032999287 scopus 로고    scopus 로고
    • Splice variants of the nuclear dot-associated Sp100 protein contain homologies to HMG-1 and a human nuclear phosphoprotein-box motif
    • Guldner HH, Szostecki C, Schroder P, Matschl U, Jensen K, Luders C, Will H, Sternsdorf T. 1999. Splice variants of the nuclear dot-associated Sp100 protein contain homologies to HMG-1 and a human nuclear phosphoprotein-box motif. J. Cell Sci. 112:733-747.
    • (1999) J. Cell Sci. , vol.112 , pp. 733-747
    • Guldner, H.H.1    Szostecki, C.2    Schroder, P.3    Matschl, U.4    Jensen, K.5    Luders, C.6    Will, H.7    Sternsdorf, T.8
  • 13
    • 0033617169 scopus 로고    scopus 로고
    • The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers
    • Sternsdorf T, Jensen K, Reich B, Will H. 1999. The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J. Biol. Chem. 274:12555-12566. http://dx. doi. org/10. 1074/jbc. 274. 18. 12555.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12555-12566
    • Sternsdorf, T.1    Jensen, K.2    Reich, B.3    Will, H.4
  • 14
    • 0034957535 scopus 로고    scopus 로고
    • The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation
    • Bottomley MJ, Collard MW, Huggenvik JI, Liu Z, Gibson TJ, Sattler M. 2001. The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation. Nat. Struct. Biol. 8:626-633. http://dx. doi. org/10. 1038/89675.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 626-633
    • Bottomley, M.J.1    Collard, M.W.2    Huggenvik, J.I.3    Liu, Z.4    Gibson, T.J.5    Sattler, M.6
  • 15
    • 33746406755 scopus 로고    scopus 로고
    • SP100B, a repressor of gene expression preferentially binds to DNA with unmethylated CpGs
    • Isaac A, Wilcox KW, Taylor JL. 2006. SP100B, a repressor of gene expression preferentially binds to DNA with unmethylated CpGs. J. Cell. Biochem. 98:1106-1122. http://dx. doi. org/10. 1002/jcb. 20841.
    • (2006) J. Cell. Biochem. , vol.98 , pp. 1106-1122
    • Isaac, A.1    Wilcox, K.W.2    Taylor, J.L.3
  • 17
    • 55949118684 scopus 로고    scopus 로고
    • PHD fingers in human diseases: disorders arising from misinterpreting epigenetic marks
    • Baker LA, Allis CD, Wang GG. 2008. PHD fingers in human diseases: disorders arising from misinterpreting epigenetic marks. Mutat. Res. 647:3-12. http://dx. doi. org/10. 1016/j. mrfmmm. 2008. 07. 004.
    • (2008) Mutat. Res. , vol.647 , pp. 3-12
    • Baker, L.A.1    Allis, C.D.2    Wang, G.G.3
  • 18
    • 0032560477 scopus 로고    scopus 로고
    • Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment
    • Seeler JS, Marchio A, Sitterlin D, Transy C, Dejean A. 1998. Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment. Proc. Natl. Acad. Sci. USA. 95:7316-7321. http://dx. doi. org/10. 1073/pnas. 95. 13. 7316.
    • (1998) Proc. Natl. Acad. Sci. USA. , vol.95 , pp. 7316-7321
    • Seeler, J.S.1    Marchio, A.2    Sitterlin, D.3    Transy, C.4    Dejean, A.5
  • 19
    • 0035861985 scopus 로고    scopus 로고
    • A consensus DNA recognition motif for two KDWK transcription factors identifies flexiblelength, CpG-methylation sensitive cognate binding sites in the majority of human promoters
    • Burnett E, Christensen J, Tattersall P. 2001. A consensus DNA recognition motif for two KDWK transcription factors identifies flexiblelength, CpG-methylation sensitive cognate binding sites in the majority of human promoters. J. Mol. Biol. 314:1029-1039. http://dx. doi. org/10. 1006/jmbi. 2000. 5198.
    • (2001) J. Mol. Biol. , vol.314 , pp. 1029-1039
    • Burnett, E.1    Christensen, J.2    Tattersall, P.3
  • 20
    • 84877124213 scopus 로고    scopus 로고
    • Sp100A promotes chromatin decondensation at a cytomegalovirus-promoter-regulated transcription site
    • Newhart A, Negorev DG, Rafalska-Metcalf IU, Yang T, Maul GG, Janicki SM. 2013. Sp100A promotes chromatin decondensation at a cytomegalovirus-promoter-regulated transcription site. Mol. Biol. Cell 24:1454-1468. http://dx. doi. org/10. 1091/mbc. E12-09-0669.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1454-1468
    • Newhart, A.1    Negorev, D.G.2    Rafalska-Metcalf, I.U.3    Yang, T.4    Maul, G.G.5    Janicki, S.M.6
  • 21
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1
    • Sternsdorf T, Jensen K, Will H. 1997. Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J. Cell Biol. 139:1621-1634. http://dx. doi. org/10. 1083/jcb. 139. 7. 1621.
    • (1997) J. Cell Biol. , vol.139 , pp. 1621-1634
    • Sternsdorf, T.1    Jensen, K.2    Will, H.3
  • 22
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitinrelated modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Muller S, Matunis MJ, Dejean A. 1998. Conjugation with the ubiquitinrelated modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17:61-70. http://dx. doi. org/10. 1093/emboj/17. 1. 61.
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 23
    • 0026019835 scopus 로고
    • Identification of a novel nuclear domain
    • Ascoli CA, Maul GG. 1991. Identification of a novel nuclear domain. J. Cell Biol. 112:785-795. http://dx. doi. org/10. 1083/jcb. 112. 5. 785.
    • (1991) J. Cell Biol. , vol.112 , pp. 785-795
    • Ascoli, C.A.1    Maul, G.G.2
  • 24
    • 0026502780 scopus 로고
    • Characterization of a fusion cDNA (RARA/myl) transcribed from the t(15;17) translocation breakpoint in acute promyelocytic leukemia
    • Chang KS, Stass SA, Chu DT, Deaven LL, Trujillo JM, Freireich EJ. 1992. Characterization of a fusion cDNA (RARA/myl) transcribed from the t(15;17) translocation breakpoint in acute promyelocytic leukemia. Mol. Cell. Biol. 12:800-810.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 800-810
    • Chang, K.S.1    Stass, S.A.2    Chu, D.T.3    Deaven, L.L.4    Trujillo, J.M.5    Freireich, E.J.6
  • 25
    • 0025780876 scopus 로고
    • Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML
    • Kakizuka A, Miller WH, Jr, Umesono K, Warrell RP, Jr, Frankel SR, Murty VV, Dmitrovsky E, Evans RM. 1991. Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML. Cell 66:663-674. http://dx. doi. org/10. 1016/0092-8674(91)90112-C.
    • (1991) Cell , vol.66 , pp. 663-674
    • Kakizuka, A.1    Miller Jr., W.H.2    Umesono, K.3    Warrell Jr., R.P.4    Frankel, S.R.5    Murty, V.V.6    Dmitrovsky, E.7    Evans, R.M.8
  • 26
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyteretinoic acid receptor oncoprotein
    • Dyck JA, Maul GG, Miller WH, Jr, Chen JD, Kakizuka A, Evans RM. 1994. A novel macromolecular structure is a target of the promyelocyteretinoic acid receptor oncoprotein. Cell 76:333-343. http://dx. doi. org/10. 1016/0092-8674(94)90340-9.
    • (1994) Cell , vol.76 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller Jr., W.H.3    Chen, J.D.4    Kakizuka, A.5    Evans, R.M.6
  • 27
    • 0025875679 scopus 로고
    • The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR
    • de The H, Lavau C, Marchio A, Chomienne C, Degos L, Dejean A. 1991. The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 66:675-684. http://dx. doi. org/10. 1016/0092-8674 (91)90113-D.
    • (1991) Cell , vol.66 , pp. 675-684
    • de The, H.1    Lavau, C.2    Marchio, A.3    Chomienne, C.4    Degos, L.5    Dejean, A.6
  • 28
    • 0026583943 scopus 로고
    • Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins
    • Kastner P, Perez A, Lutz Y, Rochette-Egly C, Gaub MP, Durand B, Lanotte M, Berger R, Chambon P. 1992. Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins. EMBO J. 11:629-642.
    • (1992) EMBO J. , vol.11 , pp. 629-642
    • Kastner, P.1    Perez, A.2    Lutz, Y.3    Rochette-Egly, C.4    Gaub, M.P.5    Durand, B.6    Lanotte, M.7    Berger, R.8    Chambon, P.9
  • 29
    • 0026729132 scopus 로고
    • A previously uncharacterized gene, PML, is fused to the retinoic acid receptor alpha gene in acute promyelocytic leukaemia
    • Goddard AD, Borrow J, Solomon E. 1992. A previously uncharacterized gene, PML, is fused to the retinoic acid receptor alpha gene in acute promyelocytic leukaemia. Leukemia 6(Suppl 3):117S-119S.
    • (1992) Leukemia , vol.6 , Issue.SUPPL. 3
    • Goddard, A.D.1    Borrow, J.2    Solomon, E.3
  • 31
    • 0033561797 scopus 로고    scopus 로고
    • Deconstructing a disease: RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia
    • Melnick A, Licht JD. 1999. Deconstructing a disease: RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia. Blood 93:3167-3215.
    • (1999) Blood , vol.93 , pp. 3167-3215
    • Melnick, A.1    Licht, J.D.2
  • 33
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells
    • Weis K, Rambaud S, Lavau C, Jansen J, Carvalho T, Carmo-Fonseca M, Lamond A, Dejean A. 1994. Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells. Cell 76:345-356. http://dx. doi. org/10. 1016/0092-8674(94)90341-7.
    • (1994) Cell , vol.76 , pp. 345-356
    • Weis, K.1    Rambaud, S.2    Lavau, C.3    Jansen, J.4    Carvalho, T.5    Carmo-Fonseca, M.6    Lamond, A.7    Dejean, A.8
  • 34
    • 0029145206 scopus 로고
    • Two nuclear dot-associated proteins, PML and Sp100, are often coautoimmunogenic in patients with primary biliary cirrhosis
    • Sternsdorf T, Guldner HH, Szostecki C, Grotzinger T, Will H. 1995. Two nuclear dot-associated proteins, PML and Sp100, are often coautoimmunogenic in patients with primary biliary cirrhosis. Scand. J. Immunol. 42:257-268. http://dx. doi. org/10. 1111/j. 1365-3083. 1995. tb03652. x.
    • (1995) Scand. J. Immunol. , vol.42 , pp. 257-268
    • Sternsdorf, T.1    Guldner, H.H.2    Szostecki, C.3    Grotzinger, T.4    Will, H.5
  • 35
    • 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. http://dx. doi. org/10. 1016/j. bbamcr. 2008. 08. 004.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2207-2221
    • Tavalai, N.1    Stamminger, T.2
  • 37
    • 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. http://dx. doi. org/10. 1016/j. biochi. 2007. 01. 004.
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 38
    • 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. http://dx. doi. org/10. 1089/jir. 2010. 0111.
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 145-158
    • Geoffroy, M.C.1    Chelbi-Alix, M.K.2
  • 39
    • 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, Yeh ET, Strauss JF, 3rd, Maul GG. 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. http://dx. doi. org/10. 1083/jcb. 147. 2. 221.
    • (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    Kamitani, T.6    Yeh, E.T.7    Strauss III, J.F.8    Maul, G.G.9
  • 40
    • 33750447586 scopus 로고    scopus 로고
    • The mechanisms of PML-nuclear body formation
    • Shen TH, Lin HK, Scaglioni PP, Yung TM, Pandolfi PP. 2006. The mechanisms of PML-nuclear body formation. Mol. Cell 24:331-339. http://dx. doi. org/10. 1016/j. molcel. 2006. 09. 013.
    • (2006) Mol. Cell , vol.24 , pp. 331-339
    • Shen, T.H.1    Lin, H.K.2    Scaglioni, P.P.3    Yung, T.M.4    Pandolfi, P.P.5
  • 41
    • 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. http://dx. doi. org/10. 1038/nrm2277.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 43
    • 0029736651 scopus 로고    scopus 로고
    • PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia
    • Boddy MN, Howe K, Etkin LD, Solomon E, Freemont PS. 1996. PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene 13:971-982.
    • (1996) Oncogene , vol.13 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 45
    • 0041837510 scopus 로고    scopus 로고
    • Nuclear and unclear functions of SUMO
    • Seeler JS, Dejean A. 2003. Nuclear and unclear functions of SUMO. Nat. Rev. Mol. Cell Biol. 4:690-699. http://dx. doi. org/10. 1038/nrm1200.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 690-699
    • Seeler, J.S.1    Dejean, A.2
  • 47
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: a history of modification
    • Hay RT. 2005. SUMO: a history of modification. Mol. Cell 18:1-12. http://dx. doi. org/10. 1016/j. molcel. 2005. 03. 012.
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 48
    • 77957808656 scopus 로고    scopus 로고
    • SUMO modification of E1B-55K oncoprotein regulates isoformspecific binding to the tumour suppressor protein PML
    • Wimmer P, Schreiner S, Everett RD, Sirma H, Groitl P, Dobner T. 2010. SUMO modification of E1B-55K oncoprotein regulates isoformspecific binding to the tumour suppressor protein PML. Oncogene 29: 5511-5522. http://dx. doi. org/10. 1038/onc. 2010. 284.
    • (2010) Oncogene , vol.29 , pp. 5511-5522
    • Wimmer, P.1    Schreiner, S.2    Everett, R.D.3    Sirma, H.4    Groitl, P.5    Dobner, T.6
  • 49
    • 84856862707 scopus 로고    scopus 로고
    • Human pathogens and the host cell SUMOylation system
    • Wimmer P, Schreiner S, Dobner T. 2012. Human pathogens and the host cell SUMOylation system. J. Virol. 86:642-654. http://dx. doi. org/10. 1128/JVI. 06227-11.
    • (2012) J. Virol. , vol.86 , pp. 642-654
    • Wimmer, P.1    Schreiner, S.2    Dobner, T.3
  • 50
    • 84875906959 scopus 로고    scopus 로고
    • Cross-talk between phosphorylation and SUMOylation regulates transforming activities of an adenoviral oncoprotein
    • Wimmer P, Blanchette P, Schreiner S, Ching W, Groitl P, Berscheminski J, Branton PE, Will H, Dobner T. 2013. Cross-talk between phosphorylation and SUMOylation regulates transforming activities of an adenoviral oncoprotein. Oncogene 32:1626-1637. http://dx. doi. org/10. 1038/onc. 2012. 187.
    • (2013) Oncogene , vol.32 , pp. 1626-1637
    • Wimmer, P.1    Blanchette, P.2    Schreiner, S.3    Ching, W.4    Groitl, P.5    Berscheminski, J.6    Branton, P.E.7    Will, H.8    Dobner, T.9
  • 51
    • 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 Thé H. 1998. Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein. J. Virol. 72:1043-1051.
    • (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 Thé, H.5
  • 52
    • 84871958784 scopus 로고    scopus 로고
    • The adenoviral oncogene E1A-13S interacts with a specific isoform of the tumor suppressor PML to enhance viral transcription
    • Berscheminski J, Groitl P, Dobner T, Wimmer P, Schreiner S. 2013. The adenoviral oncogene E1A-13S interacts with a specific isoform of the tumor suppressor PML to enhance viral transcription. J. Virol. 87:965-977. http://dx. doi. org/10. 1128/JVI. 02023-12.
    • (2013) J. Virol. , vol.87 , pp. 965-977
    • Berscheminski, J.1    Groitl, P.2    Dobner, T.3    Wimmer, P.4    Schreiner, S.5
  • 53
    • 70249111471 scopus 로고    scopus 로고
    • Detection of protein SUMOylation in vivo
    • Tatham MH, Rodriguez MS, Xirodimas DP, Hay RT. 2009. Detection of protein SUMOylation in vivo. Nat. Protoc. 4:1363-1371. http://dx. doi. org/10. 1038/nprot. 2009. 128.
    • (2009) Nat. Protoc. , vol.4 , pp. 1363-1371
    • Tatham, M.H.1    Rodriguez, M.S.2    Xirodimas, D.P.3    Hay, R.T.4
  • 55
    • 40149085109 scopus 로고    scopus 로고
    • Replication of ICP0-null mutant herpes simplex virus type 1 is restricted by both PML and Sp100
    • Everett RD, Parada C, Gripon P, Sirma H, Orr A. 2008. Replication of ICP0-null mutant herpes simplex virus type 1 is restricted by both PML and Sp100. J. Virol. 82:2661-2672. http://dx. doi. org/10. 1128/JVI. 02308-07.
    • (2008) J. Virol. , vol.82 , pp. 2661-2672
    • Everett, R.D.1    Parada, C.2    Gripon, P.3    Sirma, H.4    Orr, A.5
  • 57
    • 84876038069 scopus 로고    scopus 로고
    • Control of human adenovirus type 5 (Ad5) gene expression by cellular Daxx/ATRX chromatin-associated complexes
    • Schreiner S, Bürck C, Glass M, Groitl P, Wimmer P, Kinkley S, Mund A, Everett RD, Dobner T. 2013. Control of human adenovirus type 5 (Ad5) gene expression by cellular Daxx/ATRX chromatin-associated complexes. Nucleic Acids Res. 41:3532-3550. http://dx. doi. org/10. 1093/nar/gkt064.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 3532-3550
    • Schreiner, S.1    Bürck, C.2    Glass, M.3    Groitl, P.4    Wimmer, P.5    Kinkley, S.6    Mund, A.7    Everett, R.D.8    Dobner, T.9
  • 58
    • 0032999287 scopus 로고    scopus 로고
    • Splice variants of the nuclear dot-associated Sp100 protein contain homologies to HMG-1 and a human nuclear phosphoprotein-box motif
    • Guldner HH, Szostecki C, Schroder P, Matschl U, Jensen K, Luders C, Will H, Sternsdorf T. 1999. Splice variants of the nuclear dot-associated Sp100 protein contain homologies to HMG-1 and a human nuclear phosphoprotein-box motif. J. Cell Sci. 112:733-747.
    • (1999) J. Cell Sci. , vol.112 , pp. 733-747
    • Guldner, H.H.1    Szostecki, C.2    Schroder, P.3    Matschl, U.4    Jensen, K.5    Luders, C.6    Will, H.7    Sternsdorf, T.8
  • 59
    • 84864389662 scopus 로고    scopus 로고
    • Functional cooperation between human adenovirus type 5 early region 4, open reading frame 6 protein, and cellular homeobox protein HoxB7
    • Muller D, Schreiner S, Schmid M, Groitl P, Winkler M, Dobner T. 2012. Functional cooperation between human adenovirus type 5 early region 4, open reading frame 6 protein, and cellular homeobox protein HoxB7. J. Virol. 86:8296-8308. http://dx. doi. org/10. 1128/JVI. 00222-12.
    • (2012) J. Virol. , vol.86 , pp. 8296-8308
    • Muller, D.1    Schreiner, S.2    Schmid, M.3    Groitl, P.4    Winkler, M.5    Dobner, T.6
  • 60
    • 34547448548 scopus 로고    scopus 로고
    • Construction of adenovirus type 5 early region 1 and 4 virus mutants
    • Groitl P, Dobner T. 2007. Construction of adenovirus type 5 early region 1 and 4 virus mutants. Methods Mol. Med. 130:29-39.
    • (2007) Methods Mol. Med. , vol.130 , pp. 29-39
    • Groitl, P.1    Dobner, T.2
  • 61
    • 69449108528 scopus 로고    scopus 로고
    • A 49-kilodalton isoform of the adenovirus type 5 early region 1B 55-kilodalton protein is sufficient to support virus replication
    • Kindsmuller K, Schreiner S, Leinenkugel F, Groitl P, Kremmer E, Dobner T. 2009. A 49-kilodalton isoform of the adenovirus type 5 early region 1B 55-kilodalton protein is sufficient to support virus replication. J. Virol. 83:9045-9056. http://dx. doi. org/10. 1128/JVI. 00728-09.
    • (2009) J. Virol. , vol.83 , pp. 9045-9056
    • Kindsmuller, K.1    Schreiner, S.2    Leinenkugel, F.3    Groitl, P.4    Kremmer, E.5    Dobner, T.6
  • 64
    • 0020501764 scopus 로고
    • Monoclonal antibodies which recognize native and denatured forms of the adenovirus DNAbinding protein
    • Reich NC, Sarnow P, Duprey E, Levine AJ. 1983. Monoclonal antibodies which recognize native and denatured forms of the adenovirus DNAbinding protein. Virology 128:480-484. http://dx. doi. org/10. 1016/0042-6822(83)90274-X.
    • (1983) Virology , vol.128 , pp. 480-484
    • Reich, N.C.1    Sarnow, P.2    Duprey, E.3    Levine, A.J.4
  • 65
    • 0019951019 scopus 로고
    • A monoclonal antibody detecting the adenovirus type 5-E1b-58Kd tumor antigen: characterization of the E1b-58Kd tumor antigen in adenovirus-infected and-transformed cells
    • Sarnow P, Sullivan CA, Levine AJ. 1982. A monoclonal antibody detecting the adenovirus type 5-E1b-58Kd tumor antigen: characterization of the E1b-58Kd tumor antigen in adenovirus-infected and-transformed cells. Virology 120:510-517. http://dx. doi. org/10. 1016/0042-6822(82) 90054-X.
    • (1982) Virology , vol.120 , pp. 510-517
    • Sarnow, P.1    Sullivan, C.A.2    Levine, A.J.3
  • 66
    • 0025267802 scopus 로고
    • The adenovirus E4 17-kilodalton protein complexes with the cellular transcription factor E2F, altering its DNA-binding properties and stimulating E1Aindependent accumulation of E2 mRNA
    • Marton MJ, Baim SB, Ornelles DA, Shenk T. 1990. The adenovirus E4 17-kilodalton protein complexes with the cellular transcription factor E2F, altering its DNA-binding properties and stimulating E1Aindependent accumulation of E2 mRNA. J. Virol. 64:2345-2359.
    • (1990) J. Virol. , vol.64 , pp. 2345-2359
    • Marton, M.J.1    Baim, S.B.2    Ornelles, D.A.3    Shenk, T.4
  • 67
    • 0033531251 scopus 로고    scopus 로고
    • The adenovirus E4orf6 protein contributes to malignant transformation by antagonizing E1Ainduced accumulation of the tumor suppressor protein p53
    • Nevels M, Spruss T, Wolf H, Dobner T. 1999. The adenovirus E4orf6 protein contributes to malignant transformation by antagonizing E1Ainduced accumulation of the tumor suppressor protein p53. Oncogene 18:9-17. http://dx. doi. org/10. 1038/sj. onc. 1202284.
    • (1999) Oncogene , vol.18 , pp. 9-17
    • Nevels, M.1    Spruss, T.2    Wolf, H.3    Dobner, T.4
  • 68
    • 34249852362 scopus 로고    scopus 로고
    • Intranuclear targeting and nuclear export of the adenovirus E1B-55K protein are regulated by SUMO1 conjugation
    • Kindsmuller K, Groitl P, Hartl B, Blanchette P, Hauber J, Dobner T. 2007. Intranuclear targeting and nuclear export of the adenovirus E1B-55K protein are regulated by SUMO1 conjugation. Proc. Natl. Acad. Sci. USA. 104:6684-6689. http://dx. doi. org/10. 1073/pnas. 0702158104.
    • (2007) Proc. Natl. Acad. Sci. USA. , vol.104 , pp. 6684-6689
    • Kindsmuller, K.1    Groitl, P.2    Hartl, B.3    Blanchette, P.4    Hauber, J.5    Dobner, T.6
  • 69
    • 84875906959 scopus 로고    scopus 로고
    • Cross-talk between phosphorylation and SUMOylation regulates transforming activities of an adenoviral oncoprotein
    • Wimmer P, Blanchette P, Schreiner S, Ching W, Groitl P, Berscheminski J, Branton PE, Will H, Dobner T. 2013. Cross-talk between phosphorylation and SUMOylation regulates transforming activities of an adenoviral oncoprotein. Oncogene 32:1626-1637. http://dx. doi. org/10. 1038/onc. 2012. 187.
    • (2013) Oncogene , vol.32 , pp. 1626-1637
    • Wimmer, P.1    Blanchette, P.2    Schreiner, S.3    Ching, W.4    Groitl, P.5    Berscheminski, J.6    Branton, P.E.7    Will, H.8    Dobner, T.9
  • 70
    • 12444320379 scopus 로고    scopus 로고
    • Blockage of CRM1-dependent nuclear export of the adenovirus type 5 early region 1B 55-kDa protein augments oncogenic transformation of primary rat cells
    • Endter C, Hartl B, Spruss T, Hauber J, Dobner T. 2005. Blockage of CRM1-dependent nuclear export of the adenovirus type 5 early region 1B 55-kDa protein augments oncogenic transformation of primary rat cells. Oncogene 24:55-64. http://dx. doi. org/10. 1038/sj. onc. 1208170.
    • (2005) Oncogene , vol.24 , pp. 55-64
    • Endter, C.1    Hartl, B.2    Spruss, T.3    Hauber, J.4    Dobner, T.5
  • 71
    • 0033571214 scopus 로고    scopus 로고
    • SUMO-1 modification activates the transcriptional response of p53
    • Rodriguez MS, Desterro JM, Lain S, Midgley CA, Lane DP, Hay RT. 1999. SUMO-1 modification activates the transcriptional response of p53. EMBO J. 18:6455-6461. http://dx. doi. org/10. 1093/emboj/18. 22. 6455.
    • (1999) EMBO J. , vol.18 , pp. 6455-6461
    • Rodriguez, M.S.1    Desterro, J.M.2    Lain, S.3    Midgley, C.A.4    Lane, D.P.5    Hay, R.T.6
  • 72
    • 77953736164 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of Daxx by the viral E1B-55K protein in human adenovirus-infected cells
    • Schreiner S, Wimmer P, Sirma H, Everett RD, Blanchette P, Groitl P, Dobner T. 2010. Proteasome-dependent degradation of Daxx by the viral E1B-55K protein in human adenovirus-infected cells. J. Virol. 84: 7029-7038. http://dx. doi. org/10. 1128/JVI. 00074-10.
    • (2010) J. Virol. , vol.84 , pp. 7029-7038
    • Schreiner, S.1    Wimmer, P.2    Sirma, H.3    Everett, R.D.4    Blanchette, P.5    Groitl, P.6    Dobner, T.7
  • 74
    • 0030052130 scopus 로고    scopus 로고
    • Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure
    • Doucas V, Ishov AM, Romo A, Juguilon H, Weitzman MD, Evans RM, Maul GG. 1996. Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure. Genes Dev. 10:196-207. http://dx. doi. org/10. 1101/gad. 10. 2. 196.
    • (1996) Genes Dev. , vol.10 , pp. 196-207
    • Doucas, V.1    Ishov, A.M.2    Romo, A.3    Juguilon, H.4    Weitzman, M.D.5    Evans, R.M.6    Maul, G.G.7
  • 75
    • 84888268767 scopus 로고    scopus 로고
    • SPOC1-mediated antiviral host cell response is antagonized early in human adenovirus type 5 infection
    • Schreiner S, Kinkley S, Bürck C, Mund A, Wimmer P, Schubert T, Groitl P, Will H, Dobner T. 2013. SPOC1-mediated antiviral host cell response is antagonized early in human adenovirus type 5 infection. PLoS Pathog. 9:e1003775. http://dx. doi. org/10. 1371/journal. ppat. 1003775.
    • (2013) PLoS Pathog. , vol.9
    • Schreiner, S.1    Kinkley, S.2    Bürck, C.3    Mund, A.4    Wimmer, P.5    Schubert, T.6    Groitl, P.7    Will, H.8    Dobner, T.9
  • 76
    • 77955922552 scopus 로고    scopus 로고
    • Identification of a molecular recognition feature in the E1A oncoprotein that binds the SUMO conjugase UBC9 and likely interferes with polySUMOylation
    • Yousef AF, Fonseca GJ, Pelka P, Ablack JN, Walsh C, Dick FA, Bazett-Jones DP, Shaw GS, Mymryk JS. 2010. Identification of a molecular recognition feature in the E1A oncoprotein that binds the SUMO conjugase UBC9 and likely interferes with polySUMOylation. Oncogene 29:4693-4704. http://dx. doi. org/10. 1038/onc. 2010. 226.
    • (2010) Oncogene , vol.29 , pp. 4693-4704
    • Yousef, A.F.1    Fonseca, G.J.2    Pelka, P.3    Ablack, J.N.4    Walsh, C.5    Dick, F.A.6    Bazett-Jones, D.P.7    Shaw, G.S.8    Mymryk, J.S.9
  • 77
    • 19844383887 scopus 로고    scopus 로고
    • Viral oncoproteins E1A and E7 and cellular LxCxE proteins repress SUMO modification of the retinoblastoma tumor suppressor
    • Ledl A, Schmidt D, Muller S. 2005. Viral oncoproteins E1A and E7 and cellular LxCxE proteins repress SUMO modification of the retinoblastoma tumor suppressor. Oncogene 24:3810-3818. http://dx. doi. org/10. 1038/sj. onc. 1208539.
    • (2005) Oncogene , vol.24 , pp. 3810-3818
    • Ledl, A.1    Schmidt, D.2    Muller, S.3
  • 79
    • 0026537862 scopus 로고
    • A pitfall of using a second plasmid to determine transfection efficiency
    • Farr A, Roman A. 1992. A pitfall of using a second plasmid to determine transfection efficiency. Nucleic Acids Res. 20:920. http://dx. doi. org/10. 1093/nar/20. 4. 920.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 920
    • Farr, A.1    Roman, A.2
  • 80
    • 0033793393 scopus 로고    scopus 로고
    • Pitfall of an internal control plasmid: response of Renilla luciferase (pRLTK) plasmid to dihydrotestosterone and dexamethasone
    • Ibrahim NM, Marinovic AC, Price SR, Young LG, Frohlich O. 2000. Pitfall of an internal control plasmid: response of Renilla luciferase (pRLTK) plasmid to dihydrotestosterone and dexamethasone. Biotechniques 29:782-784.
    • (2000) Biotechniques , vol.29 , pp. 782-784
    • Ibrahim, N.M.1    Marinovic, A.C.2    Price, S.R.3    Young, L.G.4    Frohlich, O.5
  • 81
    • 1842732155 scopus 로고    scopus 로고
    • Androgen responsiveness of Renilla luciferase reporter vectors is promoter, transgene, and cell line dependent
    • Mulholland DJ, Cox M, Read J, Rennie P, Nelson C. 2004. Androgen responsiveness of Renilla luciferase reporter vectors is promoter, transgene, and cell line dependent. Prostate 59:115-119. http://dx. doi. org/10. 1002/pros. 20059.
    • (2004) Prostate , vol.59 , pp. 115-119
    • Mulholland, D.J.1    Cox, M.2    Read, J.3    Rennie, P.4    Nelson, C.5
  • 82
    • 21244435488 scopus 로고    scopus 로고
    • Enhanced green fluorescent protein as an alternative control reporter to Renilla luciferase
    • Vesuna F, Winnard P, Jr, Raman V. 2005. Enhanced green fluorescent protein as an alternative control reporter to Renilla luciferase. Anal. Biochem. 342:345-347. http://dx. doi. org/10. 1016/j. ab. 2005. 04. 047.
    • (2005) Anal. Biochem. , vol.342 , pp. 345-347
    • Vesuna, F.1    Winnard Jr., P.2    Raman, V.3
  • 84
    • 0000800331 scopus 로고    scopus 로고
    • Adenoviridae: the viruses and their replication
    • Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), 4th ed, Lippincott Williams& Wilkins, Philadelphia, PA.
    • Shenk T. 2001. Adenoviridae: the viruses and their replication, p 2265-. 2300. In Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), Fields virology, 4th ed. Lippincott Williams& Wilkins, Philadelphia, PA.
    • (2001) Fields virology , pp. 2265-2300
    • Shenk, T.1
  • 85
    • 0029032354 scopus 로고
    • Adenovirus infection induces rearrangements in the intranuclear distribution of the nuclear body-associated PML protein
    • Puvion-Dutilleul F, Chelbi-Alix MK, Koken M, Quignon F, Puvion E, de The H. 1995. Adenovirus infection induces rearrangements in the intranuclear distribution of the nuclear body-associated PML protein. Exp. Cell Res. 218:9-16. http://dx. doi. org/10. 1006/excr. 1995. 1125.
    • (1995) Exp. Cell Res. , vol.218 , pp. 9-16
    • Puvion-Dutilleul, F.1    Chelbi-Alix, M.K.2    Koken, M.3    Quignon, F.4    Puvion, E.5    de The, H.6
  • 86
    • 33644768122 scopus 로고    scopus 로고
    • Interaction of the adenovirus type 5 E4 Orf3 protein with promyelocytic leukemia protein isoform II is required for ND10 disruption
    • Hoppe A, Beech SJ, Dimmock J, Leppard KN. 2006. Interaction of the adenovirus type 5 E4 Orf3 protein with promyelocytic leukemia protein isoform II is required for ND10 disruption. J. Virol. 80:3042-3049. http://dx. doi. org/10. 1128/JVI. 80. 6. 3042-3049. 2006.
    • (2006) J. Virol. , vol.80 , pp. 3042-3049
    • Hoppe, A.1    Beech, S.J.2    Dimmock, J.3    Leppard, K.N.4
  • 88
    • 59849108860 scopus 로고    scopus 로고
    • Adenovirus type 5 E4 Orf3 protein targets promyelocytic leukaemia (PML) protein nuclear domains for disruption via a sequence inPMLisoform II that is predicted as a protein interaction site by bioinformatic analysis
    • Leppard KN, Emmott E, Cortese MS, Rich T. 2009. Adenovirus type 5 E4 Orf3 protein targets promyelocytic leukaemia (PML) protein nuclear domains for disruption via a sequence inPMLisoform II that is predicted as a protein interaction site by bioinformatic analysis. J. Gen. Virol. 90: 95-104. http://dx. doi. org/10. 1099/vir. 0. 005512-0.
    • (2009) J. Gen. Virol. , vol.90 , pp. 95-104
    • Leppard, K.N.1    Emmott, E.2    Cortese, M.S.3    Rich, T.4
  • 90
    • 0032900876 scopus 로고    scopus 로고
    • The adenovirus type 5 E1b 55K and E4 Orf3 proteins associate in infected cells and affect ND10 components
    • Leppard KN, Everett RD. 1999. The adenovirus type 5 E1b 55K and E4 Orf3 proteins associate in infected cells and affect ND10 components. J. Gen. Virol. 80:997-1008.
    • (1999) J. Gen. Virol. , vol.80 , pp. 997-1008
    • Leppard, K.N.1    Everett, R.D.2
  • 91
    • 18744362169 scopus 로고    scopus 로고
    • Serotype-specific reorganization of the Mre11 complex by adenoviral E4orf3 proteins
    • Stracker TH, Lee DV, Carson CT, Araujo FD, Ornelles DA, Weitzman MD. 2005. Serotype-specific reorganization of the Mre11 complex by adenoviral E4orf3 proteins. J. Virol. 79:6664-6673. http://dx. doi. org/10. 1128/JVI. 79. 11. 6664-6673. 2005.
    • (2005) J. Virol. , vol.79 , pp. 6664-6673
    • Stracker, T.H.1    Lee, D.V.2    Carson, C.T.3    Araujo, F.D.4    Ornelles, D.A.5    Weitzman, M.D.6
  • 92
    • 0035969103 scopus 로고    scopus 로고
    • DNA viruses and viral proteins that interact with PML nuclear bodies
    • Everett RD. 2001. DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 20:7266-7273. http://dx. doi. org/10. 1038/sj. onc. 1204759.
    • (2001) Oncogene , vol.20 , pp. 7266-7273
    • Everett, R.D.1
  • 93
    • 77957808656 scopus 로고    scopus 로고
    • SUMO modification of E1B-55K oncoprotein regulates isoformspecific binding to the tumour suppressor protein PML
    • Wimmer P, Schreiner S, Everett RD, Sirma H, Groitl P, Dobner T. 2010. SUMO modification of E1B-55K oncoprotein regulates isoformspecific binding to the tumour suppressor protein PML. Oncogene 29: 5511-5522. http://dx. doi. org/10. 1038/onc. 2010. 284.
    • (2010) Oncogene , vol.29 , pp. 5511-5522
    • Wimmer, P.1    Schreiner, S.2    Everett, R.D.3    Sirma, H.4    Groitl, P.5    Dobner, T.6
  • 94
    • 0345471390 scopus 로고    scopus 로고
    • Adenovirus type 5 E4orf3 protein relieves p53 inhibition by E1B-55-kilodalton protein
    • König C, Roth J, Dobbelstein M. 1999. Adenovirus type 5 E4orf3 protein relieves p53 inhibition by E1B-55-kilodalton protein. J. Virol. 73:2253-2262.
    • (1999) J. Virol. , vol.73 , pp. 2253-2262
    • König, C.1    Roth, J.2    Dobbelstein, M.3
  • 95
    • 78049525016 scopus 로고    scopus 로고
    • Adenovirus E1B 55-kilodalton protein is a p53-SUMO1 E3 ligase that represses p53 and stimulates its nuclear export through interactions with promyelocytic leukemia nuclear bodies
    • Pennella MA, Liu Y, Woo JL, Kim CA, Berk AJ. 2010. Adenovirus E1B 55-kilodalton protein is a p53-SUMO1 E3 ligase that represses p53 and stimulates its nuclear export through interactions with promyelocytic leukemia nuclear bodies. J. Virol. 84:12210-12225. http://dx. doi. org/10. 1128/JVI. 01442-10.
    • (2010) J. Virol. , vol.84 , pp. 12210-12225
    • Pennella, M.A.1    Liu, Y.2    Woo, J.L.3    Kim, C.A.4    Berk, A.J.5
  • 96
    • 42049098813 scopus 로고    scopus 로고
    • The adenovirus E1B-55K oncoprotein induces SUMO modification of p53
    • Muller S, Dobner T. 2008. The adenovirus E1B-55K oncoprotein induces SUMO modification of p53. Cell Cycle 7:754-758. http://dx. doi. org/10. 4161/cc. 7. 6. 5495.
    • (2008) Cell Cycle , vol.7 , pp. 754-758
    • Muller, S.1    Dobner, T.2
  • 97
    • 0037311411 scopus 로고    scopus 로고
    • Nuclear matrix localization and SUMO-1 modification of adenovirus type 5 E1b 55K protein are controlled by E4 Orf6 protein
    • Lethbridge KJ, Scott GE, Leppard KN. 2003. Nuclear matrix localization and SUMO-1 modification of adenovirus type 5 E1b 55K protein are controlled by E4 Orf6 protein. J. Gen. Virol. 84:259-268. http://dx. doi. org/10. 1099/vir. 0. 18820-0.
    • (2003) J. Gen. Virol. , vol.84 , pp. 259-268
    • Lethbridge, K.J.1    Scott, G.E.2    Leppard, K.N.3
  • 98
    • 6344234804 scopus 로고    scopus 로고
    • Both BC-box motifs of adenovirus protein E4orf6 are required to efficiently assemble an E3 ligase complex that degrades p53
    • Blanchette P, Cheng CY, Yan Q, Ketner G, Ornelles DA, Dobner T, Conaway RC, Conaway JW, Branton PE. 2004. Both BC-box motifs of adenovirus protein E4orf6 are required to efficiently assemble an E3 ligase complex that degrades p53. Mol. Cell. Biol. 24:9619-9629. http://dx. doi. org/10. 1128/MCB. 24. 21. 9619-9629. 2004.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9619-9629
    • Blanchette, P.1    Cheng, C.Y.2    Yan, Q.3    Ketner, G.4    Ornelles, D.A.5    Dobner, T.6    Conaway, R.C.7    Conaway, J.W.8    Branton, P.E.9
  • 101
    • 0021345625 scopus 로고
    • Adenovirus early region 1B 58, 000-dalton tumor antigen is physically associated with an early region 4 25, 000-dalton protein in productively infected cells
    • Sarnow P, Hearing P, Anderson CW, Halbert DN, Shenk T, Levine AJ. 1984. Adenovirus early region 1B 58, 000-dalton tumor antigen is physically associated with an early region 4 25, 000-dalton protein in productively infected cells. J. Virol. 49:692-700.
    • (1984) J. Virol. , vol.49 , pp. 692-700
    • Sarnow, P.1    Hearing, P.2    Anderson, C.W.3    Halbert, D.N.4    Shenk, T.5    Levine, A.J.6
  • 102
    • 0020079972 scopus 로고
    • Adenovirus E1b-58kd tumor antigen and SV40 large tumor antigen are physically associated with the same 54 kd cellular protein in transformed cells
    • Sarnow P, Ho YS, Williams J, Levine AJ. 1982. Adenovirus E1b-58kd tumor antigen and SV40 large tumor antigen are physically associated with the same 54 kd cellular protein in transformed cells. Cell 28:387-394. http://dx. doi. org/10. 1016/0092-8674(82)90356-7.
    • (1982) Cell , vol.28 , pp. 387-394
    • Sarnow, P.1    Ho, Y.S.2    Williams, J.3    Levine, A.J.4
  • 103
    • 0028352769 scopus 로고
    • The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0
    • Maul GG, Everett RD. 1994. The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0. J. Gen. Virol. 75:1223-1233. http://dx. doi. org/10. 1099/0022-1317-75-6-1223.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1223-1233
    • Maul, G.G.1    Everett, R.D.2
  • 104
    • 0030895008 scopus 로고    scopus 로고
    • A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein
    • Everett RD, Meredith M, Orr A, Cross A, Kathoria M, Parkinson J. 1997. A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein. EMBO J. 16:1519-1530. http://dx. doi. org/10. 1093/emboj/16. 7. 1519.
    • (1997) EMBO J. , vol.16 , pp. 1519-1530
    • Everett, R.D.1    Meredith, M.2    Orr, A.3    Cross, A.4    Kathoria, M.5    Parkinson, J.6
  • 105
    • 0027769358 scopus 로고
    • Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0)
    • Maul GG, Guldner HH, Spivack JG. 1993. Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0). J. Gen. Virol. 74:2679-2690. http://dx. doi. org/10. 1099/0022-1317-74-12-2679.
    • (1993) J. Gen. Virol. , vol.74 , pp. 2679-2690
    • Maul, G.G.1    Guldner, H.H.2    Spivack, J.G.3
  • 106
    • 0035121442 scopus 로고    scopus 로고
    • Interactions of herpes simplex virus type 1 with ND10 and recruitment of PML to replication compartments
    • Burkham J, Coen DM, Hwang CB, Weller SK. 2001. Interactions of herpes simplex virus type 1 with ND10 and recruitment of PML to replication compartments. J. Virol. 75:2353-2367. http://dx. doi. org/10. 1128/JVI. 75. 5. 2353-2367. 2001.
    • (2001) J. Virol. , vol.75 , pp. 2353-2367
    • Burkham, J.1    Coen, D.M.2    Hwang, C.B.3    Weller, S.K.4
  • 107
    • 0031743484 scopus 로고    scopus 로고
    • ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication com-partments in the presence of viral DNA polymerase
    • Burkham J, Coen DM, Weller SK. 1998. ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication com-partments in the presence of viral DNA polymerase. J. Virol. 72:10100-10107.
    • (1998) J. Virol. , vol.72 , pp. 10100-10107
    • Burkham, J.1    Coen, D.M.2    Weller, S.K.3
  • 108
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasomedependent degradation of the nuclear bodies-associated PML and Sp100 proteins
    • Chelbi-Alix MK, de The H. 1999. Herpes virus induced proteasomedependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene 18:935-941. http://dx. doi. org/10. 1038/sj. onc. 1202366.
    • (1999) Oncogene , vol.18 , pp. 935-941
    • Chelbi-Alix, M.K.1    de The, H.2
  • 109
    • 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, Kathoria M, Parkinson J. 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    Kathoria, M.6    Parkinson, J.7
  • 110
    • 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
  • 111
    • 0033779805 scopus 로고    scopus 로고
    • Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins
    • Parkinson J, Everett RD. 2000. Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins. J. Virol. 74:10006-10017. http://dx. doi. org/10. 1128/JVI. 74. 21. 10006-10017. 2000.
    • (2000) J. Virol. , vol.74 , pp. 10006-10017
    • Parkinson, J.1    Everett, R.D.2
  • 112
    • 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, Ling PD, Lee CH, Ahn JH. 2011. Human cytomegalovirus infection causes degradation of Sp100 proteins that suppress viral gene expression. J. Virol. 85:11928-11937. http://dx. doi. org/10. 1128/JVI. 00758-11.
    • (2011) J. Virol. , vol.85 , 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    Ling, P.D.7    Lee, C.H.8    Ahn, J.H.9
  • 113
    • 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. http://dx. doi. org/10. 1128/JVI. 06992-11.
    • (2012) J. Virol. , vol.86 , pp. 3541-3553
    • Full, F.1    Reuter, N.2    Zielke, K.3    Stamminger, T.4    Ensser, A.5
  • 114
    • 33746809411 scopus 로고    scopus 로고
    • Differential role of Sp100 isoforms in interferon-mediated repression of herpes simplex virus type 1 immediate-early protein expression
    • Negorev DG, Vladimirova OV, Ivanov A, Rauscher F, 3rd, Maul GG. 2006. Differential role of Sp100 isoforms in interferon-mediated repression of herpes simplex virus type 1 immediate-early protein expression. J. Virol. 80:8019-8029. http://dx. doi. org/10. 1128/JVI. 02164-05.
    • (2006) J. Virol. , vol.80 , pp. 8019-8029
    • Negorev, D.G.1    Vladimirova, O.V.2    Ivanov, A.3    Rauscher III, F.4    Maul, G.G.5
  • 115
    • 84866324649 scopus 로고    scopus 로고
    • DNA viruses and the cellular DNA-damage response
    • Turnell AS, Grand RJ. 2012. DNA viruses and the cellular DNA-damage response. J. Gen. Virol. 93:2076-2097. http://dx. doi. org/10. 1099/vir. 0. 044412-0.
    • (2012) J. Gen. Virol. , vol.93 , pp. 2076-2097
    • Turnell, A.S.1    Grand, R.J.2
  • 116
    • 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. http://dx. doi. org/10. 1128/JVI. 00870-11.
    • (2011) J. Virol. , vol.85 , pp. 9447-9458
    • Tavalai, N.1    Adler, M.2    Scherer, M.3    Riedl, Y.4    Stamminger, T.5
  • 117
    • 71949105212 scopus 로고    scopus 로고
    • The emerging role of HP1 in the DNA damage response
    • Dinant C, Luijsterburg MS. 2009. The emerging role of HP1 in the DNA damage response. Mol. Cell. Biol. 29:6335-6340. http://dx. doi. org/10. 1128/MCB. 01048-09.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 6335-6340
    • Dinant, C.1    Luijsterburg, M.S.2
  • 118
    • 79955507697 scopus 로고    scopus 로고
    • HP1alpha recruitment toDNAdamage by p150CAF-1 promotes homologous recombination repair
    • Baldeyron C, Soria G, Roche D, Cook AJ, Almouzni G. 2011. HP1alpha recruitment toDNAdamage by p150CAF-1 promotes homologous recombination repair. J. Cell Biol. 193:81-95. http://dx. doi. org/10. 1083/jcb. 201101030.
    • (2011) J. Cell Biol. , vol.193 , pp. 81-95
    • Baldeyron, C.1    Soria, G.2    Roche, D.3    Cook, A.J.4    Almouzni, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.