{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,22]],"date-time":"2026-01-22T09:11:09Z","timestamp":1769073069342,"version":"3.49.0"},"reference-count":60,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2015,6,1]],"date-time":"2015-06-01T00:00:00Z","timestamp":1433116800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["CIHR MOP 111270"],"award-info":[{"award-number":["CIHR MOP 111270"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["NSERC RGPAS 412254-11"],"award-info":[{"award-number":["NSERC RGPAS 412254-11"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["RGPIN 227926-11"],"award-info":[{"award-number":["RGPIN 227926-11"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Opinion in Virology"],"published-print":{"date-parts":[[2015,6]]},"DOI":"10.1016\/j.coviro.2015.03.017","type":"journal-article","created":{"date-parts":[[2015,4,3]],"date-time":"2015-04-03T22:21:59Z","timestamp":1428099719000},"page":"59-65","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":16,"special_numbering":"C","title":["Old foes, new understandings: nuclear entry of small non-enveloped DNA viruses"],"prefix":"10.1016","volume":"12","author":[{"given":"Nikta","family":"Fay","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nelly","family":"Pant\u00e9","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.coviro.2015.03.017_bib0305","doi-asserted-by":"crossref","first-page":"a000562","DOI":"10.1101\/cshperspect.a000562","article-title":"The nuclear pore complex and nuclear transport","volume":"2","author":"Wente","year":"2010","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"10.1016\/j.coviro.2015.03.017_sbref0310","doi-asserted-by":"crossref","first-page":"1634","DOI":"10.1016\/j.bbamcr.2010.12.009","article-title":"How viruses access the nucleus","volume":"1813","author":"Cohen","year":"2011","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.coviro.2015.03.017_bib0315","doi-asserted-by":"crossref","first-page":"2176","DOI":"10.1016\/j.bbamcr.2011.03.019","article-title":"Regulation of nucleocytoplasmic trafficking of viral proteins: an integral role in pathogenesis?","volume":"1813","author":"Fulcher","year":"2011","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.coviro.2015.03.017_sbref0320","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.antiviral.2012.06.008","article-title":"Nuclear trafficking of proteins from RNA viruses: potential target for antivirals?","volume":"95","author":"Caly","year":"2012","journal-title":"Antiviral Res"},{"key":"10.1016\/j.coviro.2015.03.017_bib0325","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1091\/mbc.01-06-0308","article-title":"Nuclear pore complex is able to transport macromolecules with diameters of about 39nm","volume":"13","author":"Pante","year":"2002","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.coviro.2015.03.017_bib0330","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.jsb.2011.11.006","article-title":"Nuclear transport of baculovirus: revealing the nuclear pore complex passage","volume":"177","author":"Au","year":"2012","journal-title":"J Struct Biol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0335","doi-asserted-by":"crossref","first-page":"2483","DOI":"10.3390\/v5102483","article-title":"Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes","volume":"5","author":"Matreyek","year":"2013","journal-title":"Viruses"},{"key":"10.1016\/j.coviro.2015.03.017_bib0340","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.virusres.2013.09.003","article-title":"New insights in the role of nucleoporins: a bridge leading to concerted steps from HIV-1 nuclear entry until integration","volume":"178","author":"Di Nunzio","year":"2013","journal-title":"Virus Res"},{"key":"10.1016\/j.coviro.2015.03.017_bib0345","doi-asserted-by":"crossref","first-page":"2424","DOI":"10.3390\/v5102424","article-title":"Transport of the influenza virus genome from nucleus to nucleus","volume":"5","author":"Hutchinson","year":"2013","journal-title":"Viruses"},{"key":"10.1016\/j.coviro.2015.03.017_bib0350","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.virusres.2006.09.013","article-title":"Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes","volume":"124","author":"Boulo","year":"2007","journal-title":"Virus Res"},{"key":"10.1016\/j.coviro.2015.03.017_bib0355","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1038\/nrmicro3367","article-title":"At the centre: influenza A virus ribonucleoproteins","volume":"13","author":"Eisfeld","year":"2015","journal-title":"Nat Rev Microbiol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0360","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1002\/jmr.1120","article-title":"Nuclear delivery mechanism of herpes simplex virus type 1 genome","volume":"24","author":"Liashkovich","year":"2011","journal-title":"J Mol Recognit"},{"key":"10.1016\/j.coviro.2015.03.017_bib0365","doi-asserted-by":"crossref","first-page":"4922","DOI":"10.1128\/MCB.20.13.4922-4931.2000","article-title":"Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro","volume":"20","author":"Ojala","year":"2000","journal-title":"Mol Cell Biol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0370","doi-asserted-by":"crossref","first-page":"1092","DOI":"10.1038\/ncb1201-1092","article-title":"Import of adenovirus DNA involves the nuclear pore complex receptor CAN\/Nup214 and histone H1","volume":"3","author":"Trotman","year":"2001","journal-title":"Nat Cell Biol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0375","doi-asserted-by":"crossref","first-page":"9849","DOI":"10.1073\/pnas.1730940100","article-title":"Nuclear import of hepatitis B virus capsids and release of the viral genome","volume":"100","author":"Rabe","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.coviro.2015.03.017_bib0380","doi-asserted-by":"crossref","first-page":"2410","DOI":"10.3390\/v5102410","article-title":"Viruses challenge selectivity barrier of nuclear pores","volume":"5","author":"Labokha","year":"2013","journal-title":"Viruses"},{"key":"10.1016\/j.coviro.2015.03.017_bib0385","doi-asserted-by":"crossref","first-page":"526","DOI":"10.4161\/nucl.21979","article-title":"Virus strategies for passing the nuclear envelope barrier","volume":"3","author":"Kobiler","year":"2012","journal-title":"Nucleus"},{"key":"10.1016\/j.coviro.2015.03.017_bib0390","doi-asserted-by":"crossref","first-page":"2019","DOI":"10.3390\/v5082019","article-title":"Viral subversion of the nuclear pore complex","volume":"5","author":"Le Sage","year":"2013","journal-title":"Viruses"},{"key":"10.1016\/j.coviro.2015.03.017_bib0395","doi-asserted-by":"crossref","first-page":"5998","DOI":"10.1093\/emboj\/16.19.5998","article-title":"The role of the nuclear pore complex in adenovirus DNA entry","volume":"16","author":"Greber","year":"1997","journal-title":"EMBO J"},{"key":"10.1016\/j.coviro.2015.03.017_sbref0400","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.chom.2011.08.010","article-title":"Kinesin-1-mediated capsid disassembly and disruption of the nuclear pore complex promote virus infection","volume":"10","author":"Strunze","year":"2011","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.coviro.2015.03.017_bib0405","doi-asserted-by":"crossref","first-page":"41594","DOI":"10.1074\/jbc.M104514200","article-title":"The docking of kinesins, KIF5B and KIF5C, to Ran-binding protein 2 (RanBP2) is mediated via a novel RanBP2 domain","volume":"276","author":"Cai","year":"2001","journal-title":"J Biol Chem"},{"key":"10.1016\/j.coviro.2015.03.017_bib0410","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1038\/embor.2009.29","article-title":"RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system","volume":"10","author":"Cho","year":"2009","journal-title":"EMBO Rep"},{"key":"10.1016\/j.coviro.2015.03.017_bib0415","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1083\/jcb.201008064","article-title":"HIV-1 remodels the nuclear pore complex","volume":"193","author":"Monette","year":"2011","journal-title":"J Cell Biol"},{"key":"10.1016\/j.coviro.2015.03.017_sbref0420","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/B978-0-12-394310-1.00003-5","article-title":"Effect of viral infection on the nuclear envelope and nuclear pore complex","volume":"299","author":"Cohen","year":"2012","journal-title":"Int Rev Cell Mol Biol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0425","doi-asserted-by":"crossref","first-page":"2474","DOI":"10.1128\/JVI.79.4.2474-2483.2005","article-title":"Adenovirus protein VII functions throughout early phase and interacts with cellular proteins SET and pp32","volume":"79","author":"Xue","year":"2005","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0430","doi-asserted-by":"crossref","first-page":"9608","DOI":"10.1128\/JVI.00850-06","article-title":"Adenovirus core protein pVII is translocated into the nucleus by multiple import receptor pathways","volume":"80","author":"Wodrich","year":"2006","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0435","doi-asserted-by":"crossref","first-page":"1313","DOI":"10.1111\/j.1600-0854.2007.00618.x","article-title":"A role for transportin in the nuclear import of adenovirus core proteins and DNA","volume":"8","author":"Hindley","year":"2007","journal-title":"Traffic"},{"key":"10.1016\/j.coviro.2015.03.017_bib0440","doi-asserted-by":"crossref","first-page":"1414","DOI":"10.1111\/j.1600-0854.2009.00968.x","article-title":"Transportin mediates nuclear entry of DNA in vertebrate systems","volume":"10","author":"Lachish-Zalait","year":"2009","journal-title":"Traffic"},{"key":"10.1016\/j.coviro.2015.03.017_bib0445","doi-asserted-by":"crossref","first-page":"4298","DOI":"10.1074\/jbc.275.6.4298","article-title":"Nuclear import of adenovirus DNA in vitro involves the nuclear protein import pathway and hsc70","volume":"275","author":"Saphire","year":"2000","journal-title":"J Biol Chem"},{"key":"10.1016\/j.coviro.2015.03.017_bib0450","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1111\/tra.12021","article-title":"Importin-7 mediates nuclear trafficking of DNA in mammalian cells","volume":"14","author":"Dhanoya","year":"2013","journal-title":"Traffic"},{"key":"10.1016\/j.coviro.2015.03.017_bib0455","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1006\/mthe.2001.0457","article-title":"Infection of purified nuclei by adeno-associated virus 2","volume":"4","author":"Hansen","year":"2001","journal-title":"Mol Ther"},{"key":"10.1016\/j.coviro.2015.03.017_bib0460","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.ymeth.2010.02.001","article-title":"Microinjection of Xenopus laevis oocytes as a system for studying nuclear transport of viruses","volume":"51","author":"Au","year":"2010","journal-title":"Methods"},{"key":"10.1016\/j.coviro.2015.03.017_bib0465","doi-asserted-by":"crossref","first-page":"3243","DOI":"10.1099\/vir.0.80967-0","article-title":"Pushing the envelope: microinjection of Minute virus of mice into Xenopus oocytes causes damage to the nuclear envelope","volume":"86","author":"Cohen","year":"2005","journal-title":"J Gen Virol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0470","doi-asserted-by":"crossref","first-page":"3209","DOI":"10.1099\/vir.0.82232-0","article-title":"Parvoviral nuclear import: bypassing the host nuclear-transport machinery","volume":"87","author":"Cohen","year":"2006","journal-title":"J Gen Virol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0475","doi-asserted-by":"crossref","first-page":"4863","DOI":"10.1128\/JVI.01999-10","article-title":"Nuclear envelope disruption involving host caspases plays a role in the parvovirus replication cycle","volume":"85","author":"Cohen","year":"2011","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.03.017_sbref0480","doi-asserted-by":"crossref","first-page":"e1003671","DOI":"10.1371\/journal.ppat.1003671","article-title":"Parvoviruses cause nuclear envelope breakdown by activating key enzymes of mitosis","volume":"9","author":"Porwal","year":"2013","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.coviro.2015.03.017_bib0485","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1083\/jcb.200703002","article-title":"An in vitro nuclear disassembly system reveals a role for the RanGTPase system and microtubule-dependent steps in nuclear envelope breakdown","volume":"178","author":"Muhlhausser","year":"2007","journal-title":"J Cell Biol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0490","doi-asserted-by":"crossref","first-page":"6522","DOI":"10.1128\/JVI.02061-08","article-title":"Integrase interacts with nucleoporin NUP153 to mediate the nuclear import of human immunodeficiency virus type 1","volume":"83","author":"Woodward","year":"2009","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0495","doi-asserted-by":"crossref","first-page":"2721","DOI":"10.1083\/jcb.109.6.2721","article-title":"Endocytosis of simian virus 40 into the endoplasmic reticulum","volume":"109","author":"Kartenbeck","year":"1989","journal-title":"J Cell Biol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0500","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1016\/j.cell.2007.09.038","article-title":"Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells","volume":"131","author":"Schelhaas","year":"2007","journal-title":"Cell"},{"key":"10.1016\/j.coviro.2015.03.017_bib0505","doi-asserted-by":"crossref","first-page":"a013250","DOI":"10.1101\/cshperspect.a013250","article-title":"How viruses use the endoplasmic reticulum for entry, replication, and assembly","volume":"5","author":"Inoue","year":"2013","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"10.1016\/j.coviro.2015.03.017_sbref0510","doi-asserted-by":"crossref","first-page":"e1002037","DOI":"10.1371\/journal.ppat.1002037","article-title":"A large and intact viral particle penetrates the endoplasmic reticulum membrane to reach the cytosol","volume":"7","author":"Inoue","year":"2011","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.coviro.2015.03.017_sbref0515","doi-asserted-by":"crossref","first-page":"1305","DOI":"10.1038\/ncb2339","article-title":"BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol","volume":"13","author":"Geiger","year":"2011","journal-title":"Nat Cell Biol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0520","doi-asserted-by":"crossref","first-page":"330","DOI":"10.3389\/fmicb.2014.00330","article-title":"ERAD and how viruses exploit it","volume":"5","author":"Byun","year":"2014","journal-title":"Front Microbiol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0525","doi-asserted-by":"crossref","first-page":"e1004007","DOI":"10.1371\/journal.ppat.1004007","article-title":"A cytosolic chaperone complexes with dynamic membrane J-proteins and mobilizes a nonenveloped virus out of the endoplasmic reticulum","volume":"10","author":"Walczak","year":"2014","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.coviro.2015.03.017_bib0530","doi-asserted-by":"crossref","first-page":"2510","DOI":"10.1074\/jbc.M112.428425","article-title":"The viroporin activity of the minor structural proteins VP2 and VP3 is required for SV40 propagation","volume":"288","author":"Giorda","year":"2013","journal-title":"J Biol Chem"},{"key":"10.1016\/j.coviro.2015.03.017_bib0535","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1073\/pnas.93.1.96","article-title":"Association with capsid proteins promotes nuclear targeting of simian virus 40 DNA","volume":"93","author":"Nakanishi","year":"1996","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.coviro.2015.03.017_bib0540","doi-asserted-by":"crossref","first-page":"9368","DOI":"10.1128\/JVI.76.18.9368-9377.2002","article-title":"Interaction of the Vp3 nuclear localization signal with the importin alpha 2\/beta heterodimer directs nuclear entry of infecting simian virus 40","volume":"76","author":"Nakanishi","year":"2002","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0545","doi-asserted-by":"crossref","first-page":"3778","DOI":"10.1128\/JVI.02664-06","article-title":"Minor capsid proteins of simian virus 40 are dispensable for nucleocapsid assembly and cell entry but are required for nuclear entry of the viral genome","volume":"81","author":"Nakanishi","year":"2007","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0550","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1186\/1743-422X-9-158","article-title":"Disassociation of the SV40 genome from capsid proteins prior to nuclear entry","volume":"9","author":"Kuksin","year":"2012","journal-title":"Virol J"},{"key":"10.1016\/j.coviro.2015.03.017_bib0555","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1128\/JVI.6.1.87-93.1970","article-title":"Morphological aspects of the uptake of simian virus 40 by permissive cells","volume":"6","author":"Hummeler","year":"1970","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0560","doi-asserted-by":"crossref","first-page":"620","DOI":"10.1128\/JVI.19.2.620-636.1976","article-title":"Early events in polyoma virus infection: attachment, penetration, and nuclear entry","volume":"19","author":"Mackay","year":"1976","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.03.017_sbref0565","doi-asserted-by":"crossref","first-page":"320","DOI":"10.4161\/nucl.2.4.16371","article-title":"Simian virus 40 induces lamin A\/C fluctuations and nuclear envelope deformation during cell entry","volume":"2","author":"Butin-Israeli","year":"2007","journal-title":"Nucleus"},{"key":"10.1016\/j.coviro.2015.03.017_bib0570","doi-asserted-by":"crossref","first-page":"3431","DOI":"10.1128\/JVI.01735-09","article-title":"Simian virus 40 infection triggers a balanced network that includes apoptotic, survival, and stress pathways","volume":"84","author":"Butin-Israeli","year":"2010","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0575","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1126\/science.1063957","article-title":"Dynamic disruptions in nuclear envelope architecture and integrity induced by HIV-1 Vpr","volume":"294","author":"de Noronha","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.03.017_bib0580","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.1126\/science.1066729","article-title":"Virology HIV\u2014breaking the rules for nuclear entry","volume":"294","author":"Segura-Totten","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.coviro.2015.03.017_bib0585","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/j.ceb.2012.01.009","article-title":"Trafficking to uncharted territory of the nuclear envelope","volume":"24","author":"Burns","year":"2012","journal-title":"Curr Opin Cell Biol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0590","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1016\/j.tcb.2012.07.003","article-title":"Alternative nuclear transport for cellular protein quality control","volume":"22","author":"Rose","year":"2012","journal-title":"Trends Cell Biol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0595","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1128\/JVI.4.1.75-93.1969","article-title":"Herpes-type virus of the frog renal adenocarcinoma. I. Virus development in tumor transplants maintained at low temperature","volume":"4","author":"Stackpole","year":"1969","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2015.03.017_bib0600","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1016\/j.cell.2012.03.032","article-title":"Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling","volume":"149","author":"Speese","year":"2012","journal-title":"Cell"}],"container-title":["Current Opinion in Virology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1879625715000486?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1879625715000486?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2020,8,31]],"date-time":"2020-08-31T08:37:08Z","timestamp":1598863028000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1879625715000486"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,6]]},"references-count":60,"alternative-id":["S1879625715000486"],"URL":"https:\/\/doi.org\/10.1016\/j.coviro.2015.03.017","relation":{},"ISSN":["1879-6257"],"issn-type":[{"value":"1879-6257","type":"print"}],"subject":[],"published":{"date-parts":[[2015,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Old foes, new understandings: nuclear entry of small non-enveloped DNA viruses","name":"articletitle","label":"Article Title"},{"value":"Current Opinion in Virology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.coviro.2015.03.017","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2015 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}