{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T11:36:46Z","timestamp":1791200206938,"version":"4.2.0"},"reference-count":156,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2009,12,15]],"date-time":"2009-12-15T00:00:00Z","timestamp":1260835200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>In recent studies we and others have identified the cellular proteins PML, hDaxx, and Sp100, which form a subnuclear structure known as nuclear domain 10 (ND10) or PML nuclear bodies (PML-NBs), as host restriction factors that counteract herpesviral infections by inhibiting viral replication at different stages. The antiviral function of ND10, however, is antagonized by viral regulatory proteins (e.g., ICP0 of herpes simplex virus; IE1 of human cytomegalovirus) which induce either a modification or disruption of ND10. This review will summarize the current knowledge on how viral replication is inhibited by ND10 proteins. Furthermore, herpesviral strategies to defeat this host defense mechanism are discussed.<\/jats:p>","DOI":"10.3390\/v1031240","type":"journal-article","created":{"date-parts":[[2009,12,15]],"date-time":"2009-12-15T11:34:56Z","timestamp":1260876896000},"page":"1240-1264","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":80,"title":["Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies"],"prefix":"10.3390","volume":"1","author":[{"given":"Nina","family":"Tavalai","sequence":"first","affiliation":[{"name":"Institute for Clinical and Molecular Virology, University of Erlangen-Nuremberg, Schlossgarten 4, 91054 Erlangen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Stamminger","sequence":"additional","affiliation":[{"name":"Institute for Clinical and Molecular Virology, University of Erlangen-Nuremberg, Schlossgarten 4, 91054 Erlangen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2009,12,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1038\/ni1125","article-title":"Intrinsic immunity: a front-line defense against viral attack","volume":"5","author":"Bieniasz","year":"2004","journal-title":"Nat. Immunol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"7234","DOI":"10.1038\/sj.onc.1204764","article-title":"Cellular proteins localized at and interacting within ND10\/PML nuclear bodies\/PODs suggest functions of a nuclear depot","volume":"20","author":"Negorev","year":"2001","journal-title":"Oncogene"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1242\/jcs.101.4.773","article-title":"A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies","volume":"101","author":"Stuurman","year":"1992","journal-title":"J. Cell Sci."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1083\/jcb.112.5.785","article-title":"Identification of a novel nuclear domain","volume":"112","author":"Ascoli","year":"1991","journal-title":"J. Cell Biol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1111\/j.1462-5822.2005.00677.x","article-title":"Interactions between DNA viruses, ND10 and the DNA damage response","volume":"8","author":"Everett","year":"2006","journal-title":"Cell Microbiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1002\/bies.20089","article-title":"PML nuclear bodies: dynamic sensors of DNA damage and cellular stress","volume":"26","author":"Dellaire","year":"2004","journal-title":"Bioessays"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1864","DOI":"10.4161\/cc.6.15.4560","article-title":"Beyond repair foci: subnuclear domains and the cellular response to DNA damage","volume":"6","author":"Dellaire","year":"2007","journal-title":"Cell Cycle"},{"key":"ref_8","first-page":"743-755","article-title":"Nuclear redistribution of BRCA1 during viral infection","volume":"9","author":"Maul","year":"1998","journal-title":"Cell Growth Differ."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1146\/annurev.micro.57.030502.090836","article-title":"Aggresomes and pericentriolar sites of virus assembly: cellular defense or viral design?","volume":"61","author":"Wileman","year":"2007","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"4905","DOI":"10.1091\/mbc.e05-01-0019","article-title":"Nuclear aggresomes form by fusion of PML-associated aggregates","volume":"16","author":"Fu","year":"2005","journal-title":"Mol. Biol. Cell"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"4338","DOI":"10.4049\/jimmunol.145.12.4338","article-title":"Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis","volume":"145","author":"Szostecki","year":"1990","journal-title":"J. Immunol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2748","DOI":"10.1182\/blood.V95.9.2748.009k31a_2748_2752","article-title":"Role of SUMO-1-modified PML in nuclear body formation","volume":"95","author":"Zhong","year":"2000","journal-title":"Blood"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1083\/jcb.147.2.221","article-title":"PML is critical for ND10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1","volume":"147","author":"Ishov","year":"1999","journal-title":"J. Cell Biol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"7995","DOI":"10.1128\/JVI.00734-06","article-title":"PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0","volume":"80","author":"Everett","year":"2006","journal-title":"J. Virol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"8006","DOI":"10.1128\/JVI.00743-06","article-title":"Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections","volume":"80","author":"Tavalai","year":"2006","journal-title":"J. Virol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"663-674","DOI":"10.1016\/0092-8674(91)90112-C","article-title":"Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML","volume":"66","author":"Kakizuka","year":"1991","journal-title":"Cell"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"7223","DOI":"10.1038\/sj.onc.1204765","article-title":"PML protein isoforms and the RBCC\/TRIM motif","volume":"20","author":"Jensen","year":"2001","journal-title":"Oncogene"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1074\/jbc.271.1.130","article-title":"Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene, PML","volume":"271","author":"Le","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"6515","DOI":"10.1093\/nar\/gkp633","article-title":"Herpesvirus protein ICP27 switches PML isoform by altering mRNA splicing","volume":"37","author":"Nojima","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"e2277","DOI":"10.1371\/journal.pone.0002277","article-title":"A role for cytoplasmic PML in cellular resistance to viral infection","volume":"3","author":"McNally","year":"2008","journal-title":"PLoS ONE"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"4581","DOI":"10.1242\/jcs.112.24.4581","article-title":"Cell cycle regulation of PML modification and ND10 composition","volume":"112","author":"Everett","year":"1999","journal-title":"J. Cell Sci."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"3117","DOI":"10.1074\/jbc.273.6.3117","article-title":"Covalent modification of PML by the sentrin family of ubiquitin-like proteins","volume":"273","author":"Kamitani","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1093\/emboj\/17.1.61","article-title":"Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus","volume":"17","author":"Muller","year":"1998","journal-title":"EMBO J."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"26675","DOI":"10.1074\/jbc.273.41.26675","article-title":"Identification of three major sentrinization sites in PML","volume":"273","author":"Kamitani","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/j.molcel.2006.09.013","article-title":"The mechanisms of PML-nuclear body formation","volume":"24","author":"Shen","year":"2006","journal-title":"Mol. Cell"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/j.molcel.2006.10.019","article-title":"Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors","volume":"24","author":"Lin","year":"2006","journal-title":"Mol. Cell"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"3702","DOI":"10.1093\/emboj\/18.13.3702","article-title":"The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx","volume":"18","author":"Hollenbach","year":"1999","journal-title":"EMBO J."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1289-1298","DOI":"10.1089\/dna.1997.16.1289","article-title":"Cloning and expression of primate Daxx cDNAs and mapping of the human gene to chromosome 6p21.3 in the MHC region","volume":"16","author":"Kiriakidou","year":"1997","journal-title":"DNA Cell Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1784","DOI":"10.1128\/MCB.20.5.1784-1796.2000","article-title":"Sequestration and inhibition of Daxx-mediated transcriptional repression by PML","volume":"20","author":"Li","year":"2000","journal-title":"Mol. Cell Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"2029","DOI":"10.1242\/jcs.111.14.2029","article-title":"Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fas-mediated cell death","volume":"111","author":"Pluta","year":"1998","journal-title":"J. Cell Sci."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.tcb.2005.12.002","article-title":"Daxx: death or survival protein?","volume":"16","author":"Salomoni","year":"2006","journal-title":"Trends Cell Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1038\/sj.onc.1203385","article-title":"EAP1\/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes","volume":"19","author":"Li","year":"2000","journal-title":"Oncogene"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1016\/j.jmb.2007.02.047","article-title":"Inhibition of NF-kappaB acetylation and its transcriptional activity by Daxx","volume":"368","author":"Park","year":"2007","journal-title":"J. Mol. Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1242\/jcs.00234","article-title":"RNAi reveals anti-apoptotic and transcriptionally repressive activities of DAXX","volume":"116","author":"Michaelson","year":"2003","journal-title":"J. Cell Sci."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"10164","DOI":"10.1074\/jbc.M409161200","article-title":"Daxx mediates the small ubiquitin-like modifier-dependent transcriptional repression of Smad4","volume":"280","author":"Chang","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"5356","DOI":"10.1093\/nar\/gkg741","article-title":"Identification of Daxx interacting with p73, one of the p53 family, and its regulation of p53 activity by competitive interaction with PML","volume":"31","author":"Kim","year":"2003","journal-title":"Nucleic Acids Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"10529","DOI":"10.1128\/MCB.24.24.10529-10541.2004","article-title":"Negative modulation of androgen receptor transcriptional activity by Daxx","volume":"24","author":"Lin","year":"2004","journal-title":"Mol. Cell Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"3319","DOI":"10.1242\/jcs.115.16.3319","article-title":"Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek","volume":"115","author":"Hollenbach","year":"2002","journal-title":"J. Cell Sci."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2985","DOI":"10.4049\/jimmunol.172.5.2985","article-title":"Physical and functional interactions between Daxx and DNA methyltransferase 1-associated protein, DMAP1","volume":"172","author":"Muromoto","year":"2004","journal-title":"J. Immunol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"3807","DOI":"10.1242\/jcs.01230","article-title":"Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI\/SNF protein ATRX","volume":"117","author":"Ishov","year":"2004","journal-title":"J. Cell Sci."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"10635","DOI":"10.1073\/pnas.1937626100","article-title":"The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodies","volume":"100","author":"Xue","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"25446","DOI":"10.1074\/jbc.M200633200","article-title":"Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration","volume":"277","author":"Lin","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1182\/blood.V88.4.1423.bloodjournal8841423","article-title":"LYSP100-associated nuclear domains (LANDs): description of a new class of subnuclear structures and their relationship to PML nuclear bodies","volume":"88","author":"Dent","year":"1996","journal-title":"Blood"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"3314","DOI":"10.1128\/MCB.21.10.3314-3324.2001","article-title":"Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modification","volume":"21","author":"Seeler","year":"2001","journal-title":"Mol. Cell Biol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"7316","DOI":"10.1073\/pnas.95.13.7316","article-title":"Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment","volume":"95","author":"Seeler","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1242\/jcs.112.5.733","article-title":"Splice variants of the nuclear dot-associated Sp100 protein contain homologies to HMG-1 and a human nuclear phosphoprotein-box motif","volume":"112","author":"Guldner","year":"1999","journal-title":"J. Cell Sci."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1038\/89675","article-title":"The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation","volume":"8","author":"Bottomley","year":"2001","journal-title":"Nat. Struct. Biol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1002\/jcb.20434","article-title":"SP100B is a repressor of gene expression","volume":"95","author":"Wilcox","year":"2005","journal-title":"J. Cell Biochem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1002\/jcb.20841","article-title":"SP100B, a repressor of gene expression preferentially binds to DNA with unmethylated CpGs","volume":"98","author":"Isaac","year":"2006","journal-title":"J. Cell Biochem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/S0006-291X(02)00699-X","article-title":"Modification of Daxx by small ubiquitin-related modifier-1","volume":"295","author":"Jang","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1621","DOI":"10.1083\/jcb.139.7.1621","article-title":"Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1\/SUMO-1","volume":"139","author":"Sternsdorf","year":"1997","journal-title":"J. Cell Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"12555","DOI":"10.1074\/jbc.274.18.12555","article-title":"The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers","volume":"274","author":"Sternsdorf","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/S0092-8674(02)00626-8","article-title":"The role of PML in tumor suppression","volume":"108","author":"Salomoni","year":"2002","journal-title":"Cell"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2819","DOI":"10.1038\/sj.onc.1207533","article-title":"PML nuclear bodies and apoptosis","volume":"23","author":"Takahashi","year":"2004","journal-title":"Oncogene"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"9048","DOI":"10.1038\/sj.onc.1207106","article-title":"Role of PML and the PML-nuclear body in the control of programmed cell death","volume":"22","author":"Bernardi","year":"2003","journal-title":"Oncogene"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1002\/jcb.240590410","article-title":"Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress","volume":"59","author":"Maul","year":"1995","journal-title":"J. Cell Biochem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"3358","DOI":"10.1093\/emboj\/cdf341","article-title":"Deconstructing PML-induced premature senescence","volume":"21","author":"Bischof","year":"2002","journal-title":"EMBO J."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1361","DOI":"10.1084\/jem.193.12.1361","article-title":"et al. Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML\/retinoic acid receptor alpha degradation","volume":"193","author":"Zhu","year":"2001","journal-title":"J. Exp. Med."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"E85-E90","DOI":"10.1038\/35010583","article-title":"The transcriptional role of PML and the nuclear body","volume":"2","author":"Zhong","year":"2000","journal-title":"Nat. Cell Biol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"5259","DOI":"10.1128\/MCB.22.15.5259-5269.2002","article-title":"Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies","volume":"22","author":"Borden","year":"2002","journal-title":"Mol. Cell Biol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1006","DOI":"10.1038\/nrm2277","article-title":"Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies","volume":"8","author":"Bernardi","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1139\/o02-079","article-title":"The promyelocytic leukemia nuclear body: sites of activity?","volume":"80","author":"Eskiw","year":"2002","journal-title":"Biochem. Cell Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1083\/jcb.148.2.283","article-title":"Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA","volume":"148","author":"Boisvert","year":"2000","journal-title":"J. Cell Biol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1397","DOI":"10.1042\/BST0351397","article-title":"Daxx mediates SUMO-dependent transcriptional control and subnuclear compartmentalization","volume":"35","author":"Shih","year":"2007","journal-title":"Biochem. Soc. Trans."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"2259","DOI":"10.1128\/MCB.21.7.2259-2268.2001","article-title":"The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases","volume":"21","author":"Wu","year":"2001","journal-title":"Mol. Cell Biol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"998","DOI":"10.1101\/gad.1632208","article-title":"Daxx represses RelB target promoters via DNA methyltransferase recruitment and DNA hypermethylation","volume":"22","author":"Puto","year":"2008","journal-title":"Genes Dev."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1126\/science.1065173","article-title":"Methyltransferase recruitment and DNA hypermethylation of target promoters by an oncogenic transcription factor","volume":"295","author":"Raker","year":"2002","journal-title":"Science"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1016\/S1097-2765(01)00257-X","article-title":"Role of PML and PML-RARalpha in Mad-mediated transcriptional repression","volume":"7","author":"Khan","year":"2001","journal-title":"Mol. Cell"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1016\/j.yexcr.2005.12.005","article-title":"PML-associated repressor of transcription (PAROT), a novel KRAB-zinc finger repressor, is regulated through association with PML nuclear bodies","volume":"312","author":"Fleischer","year":"2006","journal-title":"Exp. Cell Res."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1288","DOI":"10.1128\/MCB.26.4.1288-1296.2006","article-title":"Recruitment of the histone methyltransferase SUV39H1 and its role in the oncogenic properties of the leukemia-associated PML-retinoic acid receptor fusion protein","volume":"26","author":"Carbone","year":"2006","journal-title":"Mol. Cell Biol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1016\/j.ccr.2007.04.009","article-title":"et al. Role of the polycomb repressive complex 2 in acute promyelocytic leukemia","volume":"11","author":"Villa","year":"2007","journal-title":"Cancer Cell"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1083\/jcb.152.5.1099","article-title":"The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body","volume":"152","author":"Boisvert","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"4991","DOI":"10.1073\/pnas.95.9.4991","article-title":"Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body","volume":"95","author":"LaMorte","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"7266","DOI":"10.1038\/sj.onc.1204759","article-title":"DNA viruses and viral proteins that interact with PML nuclear bodies","volume":"20","author":"Everett","year":"2001","journal-title":"Oncogene"},{"key":"ref_75","first-page":"295","article-title":"Viruses as hijackers of PML nuclear bodies","volume":"51","author":"Moller","year":"2003","journal-title":"Arch. Immunol. Ther. Exp. (Warsz.)"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1002\/(SICI)1521-1878(199808)20:8<660::AID-BIES9>3.0.CO;2-M","article-title":"Nuclear domain 10, the site of DNA virus transcription and replication","volume":"20","author":"Maul","year":"1998","journal-title":"Bioessays"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"7274","DOI":"10.1038\/sj.onc.1204854","article-title":"Role and fate of PML nuclear bodies in response to interferon and viral infections","volume":"20","author":"Regad","year":"2001","journal-title":"Oncogene"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1016\/j.biochi.2007.01.004","article-title":"PML and PML nuclear bodies: implications in antiviral defence","volume":"89","author":"Everett","year":"2007","journal-title":"Biochimie"},{"key":"ref_79","first-page":"2027","article-title":"Induction of the PML protein by interferons in normal and APL cells","volume":"9","author":"Pelicano","year":"1995","journal-title":"Leukemia"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"4067","DOI":"10.4049\/jimmunol.149.12.4067","article-title":"IFN enhance expression of Sp100, an autoantigen in primary biliary cirrhosis","volume":"149","author":"Guldner","year":"1992","journal-title":"J. Immunol."},{"key":"ref_81","first-page":"2565","article-title":"Transcriptional induction of the PML growth suppressor gene by interferons is mediated through an ISRE and a GAS element","volume":"11","author":"Stadler","year":"1995","journal-title":"Oncogene"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"25253","DOI":"10.1074\/jbc.271.41.25253","article-title":"The interferon (IFN)-stimulated gene Sp100 promoter contains an IFN-gamma activation site and an imperfect IFN-stimulated response element which mediate type I IFN inducibility","volume":"271","author":"Grotzinger","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"11133","DOI":"10.1158\/0008-5472.CAN-07-1342","article-title":"Direct transcriptional activation of promyelocytic leukemia protein by IFN regulatory factor 3 induces the p53-dependent growth inhibition of cancer cells","volume":"67","author":"Kim","year":"2007","journal-title":"Cancer Res."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1111\/j.1432-1033.1996.0554z.x","article-title":"Interferon-modulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML)","volume":"238","author":"Grotzinger","year":"1996","journal-title":"Eur. J. Biochem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"2679","DOI":"10.1099\/0022-1317-74-12-2679","article-title":"Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0)","volume":"74","author":"Maul","year":"1993","journal-title":"J. Gen. Virol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1083\/jcb.134.4.815","article-title":"The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition","volume":"134","author":"Ishov","year":"1996","journal-title":"J. Cell Biol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1006\/viro.1996.0094","article-title":"Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1","volume":"217","author":"Maul","year":"1996","journal-title":"Virology"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"5062","DOI":"10.1002\/j.1460-2075.1994.tb06835.x","article-title":"HSV-1 IE protein Vmw110 causes redistribution of PML","volume":"13","author":"Everett","year":"1994","journal-title":"EMBO J."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1099\/0022-1317-75-6-1223","article-title":"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","volume":"75","author":"Maul","year":"1994","journal-title":"J. Gen. Virol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1002\/1521-1878(200008)22:8<761::AID-BIES10>3.0.CO;2-A","article-title":"ICP0, a regulator of herpes simplex virus during lytic and latent infection","volume":"22","author":"Everett","year":"2000","journal-title":"Bioessays"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1038\/sj.onc.1202366","article-title":"Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins","volume":"18","year":"1999","journal-title":"Oncogene"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"6581","DOI":"10.1128\/JVI.72.8.6581-6591.1998","article-title":"The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms","volume":"72","author":"Everett","year":"1998","journal-title":"J. Virol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"5137","DOI":"10.1128\/JVI.73.6.5137-5143.1999","article-title":"Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption","volume":"73","author":"Muller","year":"1999","journal-title":"J. Virol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"10006","DOI":"10.1128\/JVI.74.21.10006-10017.2000","article-title":"Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins","volume":"74","author":"Parkinson","year":"2000","journal-title":"J. Virol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1128\/JVI.76.2.841-850.2002","article-title":"Herpes simplex virus type 1 immediate-early protein ICP0 and is isolated RING finger domain act as ubiquitin E3 ligases in vitro","volume":"76","author":"Boutell","year":"2002","journal-title":"J. Virol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"8963","DOI":"10.1073\/pnas.1533420100","article-title":"The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a","volume":"100","author":"Gu","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"295-304","DOI":"10.1006\/viro.2001.1280","article-title":"The immediate-early protein, ICP0, is essential for the resistance of herpes simplex virus to interferon-alpha\/beta","volume":"293","author":"Harle","year":"2002","journal-title":"Virology"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"2052","DOI":"10.1128\/JVI.74.4.2052-2056.2000","article-title":"Herpes simplex virus ICP0 mutants are hypersensitive to interferon","volume":"74","author":"Mossman","year":"2000","journal-title":"J. Virol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1186\/1743-422X-3-44","article-title":"ICP0 antagonizes Stat 1-dependent repression of herpes simplex virus: implications for the regulation of viral latency","volume":"3","author":"Halford","year":"2006","journal-title":"Virol. J."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"7101","DOI":"10.1128\/JVI.77.12.7101-7105.2003","article-title":"Promyelocytic leukemia protein mediates interferon-based anti-herpes simplex virus 1 effects","volume":"77","author":"Chee","year":"2003","journal-title":"J. Virol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"11411","DOI":"10.1128\/JVI.78.20.11411-11415.2004","article-title":"Visualization by live-cell microscopy of disruption of ND10 during herpes simplex virus type 1 infection","volume":"78","author":"Everett","year":"2004","journal-title":"J. Virol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"9355","DOI":"10.1128\/JVI.76.18.9355-9367.2002","article-title":"Overexpression of promyelocytic leukemia protein precludes the dispersal of ND10 structures and has no effect on accumulation of infectious herpes simplex virus 1 or its proteins","volume":"76","author":"Lopez","year":"2002","journal-title":"J. Virol."},{"key":"ref_103","doi-asserted-by":"crossref","unstructured":"Everett, R.D., Parada, C., Gripon, P., Sirma, H., and Orr, A. (2007). Replication of ICP0 null mutant herpes simplex virus type 1 is restricted by both PML and Sp100. J. Virol.","DOI":"10.1128\/JVI.02308-07"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"5168","DOI":"10.1128\/JVI.02083-08","article-title":"Differential functions of interferon-upregulated Sp100 isoforms: herpes simplex virus type 1 promoter-based immediate-early gene suppression and PML protection from ICP0-mediated degradation","volume":"83","author":"Negorev","year":"2009","journal-title":"J. Virol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"8019-8029","DOI":"10.1128\/JVI.02164-05","article-title":"Differential role of Sp100 isoforms in interferon-mediated repression of herpes simplex virus type 1 immediate-early protein expression","volume":"80","author":"Negorev","year":"2006","journal-title":"J. Virol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1128\/CMR.9.3.361","article-title":"Varicella-zoster virus","volume":"9","author":"Arvin","year":"1996","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"4262","DOI":"10.1128\/JVI.00021-09","article-title":"Components of nuclear domain 10 bodies regulate varicella-zoster virus replication","volume":"83","author":"Kyratsous","year":"2009","journal-title":"J. Virol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"7303","DOI":"10.1128\/jvi.66.12.7303-7308.1992","article-title":"Varicella-zoster virus open reading frame 61 protein is functionally homologous to herpes simplex virus type 1 ICP0","volume":"66","author":"Moriuchi","year":"1992","journal-title":"J. Virol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"4290","DOI":"10.1128\/jvi.67.7.4290-4295.1993","article-title":"Varicella-zoster virus (VZV) open reading frame 61 protein transactivates VZV gene promoters and enhances the infectivity of VZV DNA","volume":"67","author":"Moriuchi","year":"1993","journal-title":"J. Virol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"10637","DOI":"10.1128\/JVI.01144-09","article-title":"Complementation of a Herpes Simplex Virus ICP0 null mutant by Varicella Zoster Virus ORF61p","volume":"83","author":"Kyratsous","year":"2009","journal-title":"J. Virol."},{"key":"ref_111","unstructured":"Knipe, D.M., Howley, P., Griffin, D.E., Lamb, R.A., Martin, M.A., Roizman, B., and Straus, S.E. (2007). Lippincott-Williams and Wilkins. [5th ed]."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"4599","DOI":"10.1128\/jvi.71.6.4599-4613.1997","article-title":"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","volume":"71","author":"Ahn","year":"1997","journal-title":"J. Virol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1083\/jcb.138.1.5","article-title":"Human cytomegalovirus immediate early interaction with host nuclear structures: definition of an immediate transcript environment","volume":"138","author":"Ishov","year":"1997","journal-title":"J. Cell Biol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1099\/0022-1317-79-5-1233","article-title":"Disruption of PML-associated nuclear bodies mediated by the human cytomegalovirus major immediate early gene product","volume":"79","author":"Wilkinson","year":"1998","journal-title":"J. Gen. Virol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1006\/excr.1996.0353","article-title":"The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1","volume":"229","author":"Korioth","year":"1996","journal-title":"Exp. Cell Res."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"4899-4913","DOI":"10.1128\/MCB.18.8.4899","article-title":"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","volume":"18","author":"Ahn","year":"1998","journal-title":"Mol. Cell Biol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"6527","DOI":"10.1128\/JVI.78.12.6527-6542.2004","article-title":"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","volume":"78","author":"Lee","year":"2004","journal-title":"J. Virol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"10683","DOI":"10.1128\/JVI.75.22.10683-10695.2001","article-title":"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","volume":"75","author":"Xu","year":"2001","journal-title":"J. Virol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"2181","DOI":"10.1099\/vir.0.81787-0","article-title":"Inhibition of SUMO-independent PML oligomerization by the human cytomegalovirus IE1 protein","volume":"87","author":"Kang","year":"2006","journal-title":"J. Gen. Virol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1006\/viro.2000.0448","article-title":"Disruption of PML-associated nuclear bodies by IE1 correlates with efficient early stages of viral gene expression and DNA replication in human cytomegalovirus infection","volume":"274","author":"Ahn","year":"2000","journal-title":"Virology"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"5769","DOI":"10.1128\/JVI.76.11.5769-5783.2002","article-title":"Functional interaction between the pp71 protein of human cytomegalovirus and the PML-interacting protein human Daxx","volume":"76","author":"Hofmann","year":"2002","journal-title":"J. Virol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"7705","DOI":"10.1128\/JVI.76.15.7705-7712.2002","article-title":"Daxx-mediated accumulation of human cytomegalovirus tegument protein pp71 at ND10 facilitates initiation of viral infection at these nuclear domains","volume":"76","author":"Ishov","year":"2002","journal-title":"J. Virol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1601","DOI":"10.1099\/0022-1317-83-7-1601","article-title":"Activity and intracellular localization of the human cytomegalovirus protein pp71","volume":"83","author":"Marshall","year":"2002","journal-title":"J. Gen. Virol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"7792","DOI":"10.1128\/JVI.79.12.7792-7802.2005","article-title":"Interaction between the human cytomegalovirus UL82 gene product (pp71) and hDaxx regulates immediate-early gene expression and viral replication","volume":"79","author":"Cantrell","year":"2005","journal-title":"J. Virol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"37652","DOI":"10.1074\/jbc.M604273200","article-title":"Human Daxx-mediated repression of human cytomegalovirus gene expression correlates with a repressive chromatin structure around the major immediate early promoter","volume":"281","author":"Woodhall","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"3863","DOI":"10.1128\/JVI.80.8.3863-3871.2006","article-title":"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","volume":"80","author":"Saffert","year":"2006","journal-title":"J. Virol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.1099\/vir.0.81566-0","article-title":"Role of the cellular protein hDaxx in human cytomegalovirus immediate-early gene expression","volume":"87","author":"Preston","year":"2006","journal-title":"J. Gen. Virol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"6188","DOI":"10.1128\/JVI.02676-05","article-title":"Human cytomegalovirus (HCMV) UL82 gene product (pp71) relieves hDaxx-mediated repression of HCMV replication","volume":"80","author":"Cantrell","year":"2006","journal-title":"J. Virol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1128\/JVI.01685-07","article-title":"Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection","volume":"82","author":"Tavalai","year":"2008","journal-title":"J. Virol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.virol.2007.05.037","article-title":"Proteasome-dependent, ubiquitin-independent degradation of Daxx by the viral pp71 protein in human cytomegalovirus-infected cells","volume":"367","author":"Hwang","year":"2007","journal-title":"Virology"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1016\/j.febslet.2008.01.040","article-title":"Proteasome inhibitor MG132 blocks viral DNA replication and assembly of human cytomegalovirus","volume":"582","author":"Kaspari","year":"2008","journal-title":"FEBS Lett."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"6591","DOI":"10.1128\/JVI.02639-08","article-title":"Human cytomegalovirus protein pp71 induces Daxx SUMOylation","volume":"83","author":"Hwang","year":"2009","journal-title":"J. Virol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"12543","DOI":"10.1128\/JVI.01215-08","article-title":"Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection","volume":"82","author":"Lukashchuk","year":"2008","journal-title":"J. Virol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"14506","DOI":"10.1073\/pnas.97.26.14506","article-title":"UL82 virion protein activates expression of immediate early viral genes in human cytomegalovirus-infected cells","volume":"97","author":"Bresnahan","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"9109","DOI":"10.1128\/JVI.00827-07","article-title":"Human cytomegalovirus gene expression is silenced by Daxx-mediated intrinsic immune defense in model latent infections established in vitro","volume":"81","author":"Saffert","year":"2007","journal-title":"J. Virol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"2935","DOI":"10.1099\/vir.0.83019-0","article-title":"Knockdown of hDaxx in normally non-permissive undifferentiated cells does not permit human cytomegalovirus immediate-early gene expression","volume":"88","author":"Groves","year":"2007","journal-title":"J. Gen. Virol."},{"key":"ref_137","unstructured":"Sinclair, J. (2009). Chromatin structure regulates human cytomegalovirus gene expression during latency, reactivation and lytic infection. Biochim. Biophys Acta."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.2741\/3311","article-title":"PML nuclear bodies as sites of epigenetic regulation","volume":"14","author":"Torok","year":"2009","journal-title":"Front Biosci."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"2364","DOI":"10.1099\/vir.0.012526-0","article-title":"Lytic infection of permissive cells with human cytomegalovirus is regulated by an intrinsic 'pre-immediate-early' repression of viral gene expression mediated by histone post-translational modification","volume":"90","author":"Groves","year":"2009","journal-title":"J. Gen. Virol."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"9525","DOI":"10.1128\/JVI.00946-08","article-title":"Dynamic histone H3 acetylation and methylation at human cytomegalovirus promoters during replication in fibroblasts","volume":"82","author":"Shenk","year":"2008","journal-title":"J. Virol."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/S1044579X0200086X","article-title":"Epstein-Barr virus in the pathogenesis of NPC","volume":"12","year":"2002","journal-title":"Semin. Cancer Biol"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"11800","DOI":"10.1128\/JVI.74.24.11800-11810.2000","article-title":"Lytic but not latent replication of epstein-barr virus is associated with PML and induces sequential release of nuclear domain 10 proteins","volume":"74","author":"Bell","year":"2000","journal-title":"J. Virol."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1099\/vir.0.81589-0","article-title":"Epstein-Barr virus origin of lytic replication mediates association of replicating episomes with promyelocytic leukaemia protein nuclear bodies and replication compartments","volume":"87","author":"Amon","year":"2006","journal-title":"J. Gen. Virol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"2388","DOI":"10.1128\/JVI.75.5.2388-2399.2001","article-title":"Epstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies","volume":"75","author":"Adamson","year":"2001","journal-title":"J. Virol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"10334","DOI":"10.1128\/JVI.75.21.10334-10347.2001","article-title":"Identification of acidic and aromatic residues in the Zta activation domain essential for Epstein-Barr virus reactivation","volume":"75","author":"Deng","year":"2001","journal-title":"J. Virol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"4492","DOI":"10.1128\/JVI.79.7.4492-4505.2005","article-title":"The Epstein-Barr virus EBNA-LP protein preferentially coactivates EBNA2-mediated stimulation of latent membrane proteins expressed from the viral divergent promoter","volume":"79","author":"Peng","year":"2005","journal-title":"J. Virol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"2562","DOI":"10.1128\/jvi.70.4.2562-2568.1996","article-title":"The Epstein-Barr virus-encoded nuclear antigen EBNA-5 accumulates in PML-containing bodies","volume":"70","author":"Szekely","year":"1996","journal-title":"J. Virol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"3565","DOI":"10.1038\/sj.emboj.7600820","article-title":"Mediation of Epstein-Barr virus EBNA-LP transcriptional coactivation by Sp100","volume":"24","author":"Ling","year":"2005","journal-title":"EMBO J."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"7322","DOI":"10.1073\/pnas.95.13.7322","article-title":"Chromatin components as part of a putative transcriptional repressing complex","volume":"95","author":"Lehming","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1089\/jir.2008.0023","article-title":"Regulation of Sp100A subnuclear localization and transcriptional function by EBNA-LP and interferon","volume":"28","author":"Echendu","year":"2008","journal-title":"J. Interferon Cytokine Res."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"e1000170","DOI":"10.1371\/journal.ppat.1000170","article-title":"Epstein-Barr nuclear antigen 1 contributes to nasopharyngeal carcinoma through disruption of PML nuclear bodies","volume":"4","author":"Sivachandran","year":"2008","journal-title":"PLoS Pathog."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1128\/JVI.75.3.1487-1506.2001","article-title":"Origin-independent assembly of Kaposi's sarcoma-associated herpesvirus DNA replication compartments in transient cotransfection assays and association with the ORF-K8 protein and cellular PML","volume":"75","author":"Wu","year":"2001","journal-title":"J. Virol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1006\/viro.2001.1005","article-title":"Human-herpesvirus-8-encoded K8 protein colocalizes with the promyelocytic leukemia protein (PML) bodies and recruits p53 to the PML bodies","volume":"286","author":"Katano","year":"2001","journal-title":"Virology"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"8849","DOI":"10.1128\/JVI.00339-09","article-title":"Kaposi's sarcoma-associated herpesvirus protein LANA2 disrupts PML oncogenic domains and inhibits PML-mediated transcriptional repression of the survivin gene","volume":"83","author":"Gallego","year":"2009","journal-title":"J. Virol."},{"key":"ref_155","doi-asserted-by":"crossref","unstructured":"Ling, P.D., Tan, J., Sewatanon, J., and Peng, R. (2008). The murine gammaherpesvirus 68 open reading frame 75c tegument protein induces the degradation of PML and is essential for production of infectious virus. J. Virol.","DOI":"10.1128\/JVI.02752-07"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"e2781","DOI":"10.1371\/journal.pone.0002781","article-title":"Multiple functions for ORF75c in murid herpesvirus-4 infection","volume":"3","author":"Gaspar","year":"2008","journal-title":"PLoS ONE"}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/1\/3\/1240\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T22:12:00Z","timestamp":1760220720000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/1\/3\/1240"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,12,15]]},"references-count":156,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2009,12]]}},"alternative-id":["v1031240"],"URL":"https:\/\/doi.org\/10.3390\/v1031240","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2009,12,15]]}}}