{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T13:09:19Z","timestamp":1791637759125,"version":"4.3.4"},"reference-count":339,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2021,6,7]],"date-time":"2021-06-07T00:00:00Z","timestamp":1623024000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["19K23841"],"award-info":[{"award-number":["19K23841"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["20K16262"],"award-info":[{"award-number":["20K16262"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["17H05874"],"award-info":[{"award-number":["17H05874"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["17K08655"],"award-info":[{"award-number":["17K08655"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>The host nucleocytoplasmic trafficking system is often hijacked by viruses to accomplish their replication and to suppress the host immune response. Viruses encode many factors that interact with the host nuclear transport receptors (NTRs) and the nucleoporins of the nuclear pore complex (NPC) to access the host nucleus. In this review, we discuss the viral factors and the host factors involved in the nuclear import and export of viral components. As nucleocytoplasmic shuttling is vital for the replication of many viruses, we also review several drugs that target the host nuclear transport machinery and discuss their feasibility for use in antiviral treatment.<\/jats:p>","DOI":"10.3390\/cells10061424","type":"journal-article","created":{"date-parts":[[2021,6,7]],"date-time":"2021-06-07T13:25:43Z","timestamp":1623072343000},"page":"1424","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":32,"title":["How SARS-CoV-2 and Other Viruses Build an Invasion Route to Hijack the Host Nucleocytoplasmic Trafficking System"],"prefix":"10.3390","volume":"10","author":[{"given":"Elma Sakinatus","family":"Sajidah","sequence":"first","affiliation":[{"name":"Division of Nano Life Science in the Graduate School of Frontier Science Initiative, Kanazawa University, Kanazawa 920-1192, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9330-5783","authenticated-orcid":false,"given":"Keesiang","family":"Lim","sequence":"additional","affiliation":[{"name":"WPI-Nano Life Science Institute, Kanazawa University, Kanazawa 920-1192, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard W.","family":"Wong","sequence":"additional","affiliation":[{"name":"Division of Nano Life Science in the Graduate School of Frontier Science Initiative, Kanazawa University, Kanazawa 920-1192, Japan"},{"name":"WPI-Nano Life Science Institute, Kanazawa University, Kanazawa 920-1192, Japan"},{"name":"Cell-Bionomics Research Unit, Institute for Frontier Science Initiative, Kanazawa University, Kanazawa 920-1192, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,6,7]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.jtbi.2018.08.003","article-title":"Immune response and within-host viral evolution: Immune response can accelerate evolution","volume":"456","author":"Korobeinikov","year":"2018","journal-title":"J. Theor. Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1146\/annurev.cellbio.15.1.607","article-title":"Transport between the cell nucleus and the cytoplasm","volume":"15","author":"Kutay","year":"1999","journal-title":"Ann. Rev. Cell Develop. Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1016\/S0092-8674(03)00986-3","article-title":"Cell cycle regulated transport controlled by alterations in the nuclear pore complex","volume":"115","author":"Makhnevych","year":"2003","journal-title":"Cell"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"10841","DOI":"10.1074\/jbc.M110.105890","article-title":"Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis","volume":"285","author":"Nakano","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1038\/nature14587","article-title":"Transcriptional control of autophagy-lysosome function drives pancreatic cancer metabolism","volume":"524","author":"Perera","year":"2015","journal-title":"Nature"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1080\/15548627.2020.1741318","article-title":"Nucleoporin TPR (translocated promoter region, nuclear basket protein) upregulation alters MTOR-HSF1 trails and suppresses autophagy induction in ependymoma","volume":"17","author":"Dewi","year":"2021","journal-title":"Autophagy"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/j.tig.2019.05.006","article-title":"The nuclear pore complex in cell type-specific chromatin structure and gene regulation","volume":"35","author":"Sun","year":"2019","journal-title":"Trends Genet. TIG"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1526","DOI":"10.1016\/j.cell.2016.07.042","article-title":"Nuclear pore permeabilization is a convergent signaling event in effector-triggered immunity","volume":"166","author":"Gu","year":"2016","journal-title":"Cell"},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Lezon, T.R., Sali, A., and Bahar, I. (2009). Global motions of the nuclear pore complex: Insights from elastic network models. PLoS Comput. Biol., 5.","DOI":"10.1371\/journal.pcbi.1000496"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1016\/j.cell.2013.10.055","article-title":"Integrated structural analysis of the human nuclear pore complex scaffold","volume":"155","author":"Bui","year":"2013","journal-title":"Cell"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"7532","DOI":"10.1038\/ncomms8532","article-title":"Structure and gating of the nuclear pore complex","volume":"6","author":"Eibauer","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1016\/j.cell.2012.07.019","article-title":"The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model","volume":"150","author":"Labokha","year":"2012","journal-title":"Cell"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"9512","DOI":"10.1073\/pnas.0603521103","article-title":"Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport","volume":"103","author":"Lim","year":"2006","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1016\/j.cell.2007.06.024","article-title":"A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes","volume":"130","author":"Frey","year":"2007","journal-title":"Cell"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1111\/j.1600-0854.2005.00287.x","article-title":"Translocation through the nuclear pore complex: Selectivity and speed by reduction-of-dimensionality","volume":"6","author":"Peters","year":"2005","journal-title":"Traffic"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.cell.2007.01.044","article-title":"Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex","volume":"129","author":"Patel","year":"2007","journal-title":"Cell"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"120198","DOI":"10.1016\/j.biomaterials.2020.120198","article-title":"Spatiotemporally tracking of nano-biofilaments inside the nuclear pore complex core","volume":"256","author":"Mohamed","year":"2020","journal-title":"Biomaterials"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1083\/jcb.107.4.1279","article-title":"The effects of variations in the number and sequence of targeting signals on nuclear uptake","volume":"107","author":"Dworetzky","year":"1988","journal-title":"J. Cell Biol."},{"key":"ref_19","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 39 nm","volume":"13","author":"Kann","year":"2002","journal-title":"Mol. Biol. Cell"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1042\/BJ20141186","article-title":"Diversification of importin-\u03b1 isoforms in cellular trafficking and disease states","volume":"466","author":"Pumroy","year":"2015","journal-title":"Biochem. J."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/j.tcb.2004.09.004","article-title":"Karyopherins: From nuclear-transport mediators to nuclear-function regulators","volume":"14","author":"Mosammaparast","year":"2004","journal-title":"Trends Cell Biol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1006\/jmbi.2000.3642","article-title":"Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha","volume":"297","author":"Fontes","year":"2000","journal-title":"J. Mol. Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1083\/jcb.143.2.309","article-title":"Determination of the functional domain organization of the importin alpha nuclear import factor","volume":"143","author":"Herold","year":"1998","journal-title":"J. Cell Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/S0092-8674(00)81419-1","article-title":"Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha","volume":"94","author":"Conti","year":"1998","journal-title":"Cell"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/311033a0","article-title":"Sequence requirements for nuclear location of simian virus 40 large-T antigen","volume":"311","author":"Kalderon","year":"1984","journal-title":"Nature"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/0092-8674(91)90245-T","article-title":"Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence","volume":"64","author":"Robbins","year":"1991","journal-title":"Cell"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1038\/20367","article-title":"Structure of importin-beta bound to the IBB domain of importin-alpha","volume":"399","author":"Cingolani","year":"1999","journal-title":"Nature"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/S0092-8674(00)00014-3","article-title":"Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking","volume":"102","author":"Bayliss","year":"2000","journal-title":"Cell"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1016\/S0955-0674(00)00213-1","article-title":"Nucleocytoplasmic transport enters the atomic age","volume":"13","author":"Conti","year":"2001","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1038\/nature03578","article-title":"Structural basis for nuclear import complex dissociation by RanGTP","volume":"435","author":"Lee","year":"2005","journal-title":"Nature"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"5584","DOI":"10.1002\/j.1460-2075.1996.tb00943.x","article-title":"Identification of different roles for RanGDP and RanGTP in nuclear protein import","volume":"15","author":"Kutay","year":"1996","journal-title":"EMBO J."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1083\/jcb.135.3.559","article-title":"RanBP1 stabilizes the interaction of Ran with p97 nuclear protein import","volume":"135","author":"Chi","year":"1996","journal-title":"J. Cell Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1016\/0092-8674(95)90181-7","article-title":"Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins","volume":"83","author":"Rexach","year":"1995","journal-title":"Cell"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1016\/S0092-8674(00)80372-4","article-title":"Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor","volume":"90","author":"Kutay","year":"1997","journal-title":"Cell"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"2587","DOI":"10.1073\/pnas.91.7.2587","article-title":"RanGAP1 induces GTPase activity of nuclear Ras-related Ran","volume":"91","author":"Bischoff","year":"1994","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1073\/pnas.92.5.1749","article-title":"Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport","volume":"92","author":"Bischoff","year":"1995","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1002\/j.1460-2075.1995.tb07049.x","article-title":"Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1","volume":"14","author":"Bischoff","year":"1995","journal-title":"EMBO J."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1038\/366585a0","article-title":"Characterization of proteins that interact with the cell-cycle regulatory protein Ran\/TC4","volume":"366","author":"Coutavas","year":"1993","journal-title":"Nature"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1006\/jmbi.1999.3166","article-title":"Interaction between NTF2 and xFxFG-containing nucleoporins is required to mediate nuclear import of RanGDP","volume":"293","author":"Bayliss","year":"1999","journal-title":"J. Mol. Biol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1038\/354080a0","article-title":"Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1","volume":"354","author":"Bischoff","year":"1991","journal-title":"Nature"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1016\/0092-8674(95)90436-0","article-title":"The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs","volume":"82","author":"Fischer","year":"1995","journal-title":"Cell"},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"K\u0131rl\u0131, K., Karaca, S., Dehne, H.J., Samwer, M., Pan, K.T., Lenz, C., Urlaub, H., and G\u00f6rlich, D. (2015). A deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning. eLife, 4.","DOI":"10.7554\/eLife.11466"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1391","DOI":"10.1083\/jcb.153.7.1391","article-title":"Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export","volume":"153","author":"Lindsay","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"6772","DOI":"10.1128\/MCB.00342-06","article-title":"Nup214 is required for CRM1-dependent nuclear protein export in vivo","volume":"26","author":"Hutten","year":"2006","journal-title":"Mol. Cell. Biol."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Li, Y., Zhou, J., Min, S., Zhang, Y., Zhang, Y., Zhou, Q., Shen, X., Jia, D., Han, J., and Sun, Q. (2019). Distinct RanBP1 nuclear export and cargo dissociation mechanisms between fungi and animals. eLife, 8.","DOI":"10.7554\/eLife.41331"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"3643","DOI":"10.1038\/sj.emboj.7600370","article-title":"Supraphysiological nuclear export signals bind CRM1 independently of RanGTP and arrest at Nup358","volume":"23","author":"Engelsma","year":"2004","journal-title":"EMBO J."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1083\/jcb.145.4.645","article-title":"A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export","volume":"145","author":"Kehlenbach","year":"1999","journal-title":"J. Cell Biol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"8996","DOI":"10.1128\/MCB.20.23.8996-9008.2000","article-title":"TAP (NXF1) belongs to a multigene family of putative RNA export factors with a conserved modular architecture","volume":"20","author":"Herold","year":"2000","journal-title":"Mol. Cell. Biol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"3777","DOI":"10.1091\/mbc.11.11.3777","article-title":"Factors affecting nuclear export of the 60S ribosomal subunit in vivo","volume":"11","author":"Schmidt","year":"2000","journal-title":"Mol. Biol. Cell"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/S0092-8674(00)80829-6","article-title":"PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation","volume":"101","author":"Ohno","year":"2000","journal-title":"Cell"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1016\/S0092-8674(00)80370-0","article-title":"Exportin 1 (Crm1p) is an essential nuclear export factor","volume":"90","author":"Stade","year":"1997","journal-title":"Cell"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/S1097-2765(00)80036-2","article-title":"Identification of a tRNA-specific nuclear export receptor","volume":"1","author":"Kutay","year":"1998","journal-title":"Mol. Cell"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/S0960-9822(98)70130-7","article-title":"Identification of a nuclear export receptor for tRNA","volume":"8","author":"Arts","year":"1998","journal-title":"Curr. Biol. CB"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"3011","DOI":"10.1101\/gad.1158803","article-title":"Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RNAs","volume":"17","author":"Yi","year":"2003","journal-title":"Genes Dev."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"5154","DOI":"10.1073\/pnas.0709167105","article-title":"Mutually exclusive interactions drive handover of mRNA from export adaptors to TAP","volume":"105","author":"Hautbergue","year":"2008","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"5405","DOI":"10.1128\/MCB.22.15.5405-5418.2002","article-title":"Nuclear export of mRNA by TAP\/NXF1 requires two nucleoporin-binding sites but not p15","volume":"22","author":"Braun","year":"2002","journal-title":"Mol. Cell. Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1101\/gad.1616008","article-title":"Definition of global and transcript-specific mRNA export pathways in metazoans","volume":"22","author":"Farny","year":"2008","journal-title":"Genes Dev."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1128\/MCB.21.7.2545-2554.2001","article-title":"NXT1 (p15) is a crucial cellular cofactor in TAP-dependent export of intron-containing RNA in mammalian cells","volume":"21","author":"Guzik","year":"2001","journal-title":"Mol. Cell. Biol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1016\/S1097-2765(00)80065-9","article-title":"TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus","volume":"1","author":"Tabernero","year":"1998","journal-title":"Mol. Cell"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"20979","DOI":"10.1074\/jbc.M302061200","article-title":"Complex formation among the RNA export proteins Nup98, Rae1\/Gle2, and TAP","volume":"278","author":"Blevins","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/S1097-2765(01)00348-3","article-title":"Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP\/p15 mRNA nuclear export factor","volume":"8","author":"Fribourg","year":"2001","journal-title":"Mol. Cell"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1953","DOI":"10.1093\/emboj\/18.7.1953","article-title":"TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleus","volume":"18","author":"Braun","year":"1999","journal-title":"EMBO J."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1111\/tra.12691","article-title":"Mechanisms of nuclear mRNA export: A structural perspective","volume":"20","author":"Xie","year":"2019","journal-title":"Traffic"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1083\/jcb.151.1.1","article-title":"Protein ligands to HuR modulate its interaction with target mRNAs in vivo","volume":"151","author":"Brennan","year":"2000","journal-title":"J. Cell Biol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/S1097-2765(01)00303-3","article-title":"Two closely related human nuclear export factors utilize entirely distinct export pathways","volume":"8","author":"Yang","year":"2001","journal-title":"Mol. Cell"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1261\/rna.060137.116","article-title":"A biochemical framework for eIF4E-dependent mRNA export and nuclear recycling of the export machinery","volume":"23","author":"Volpon","year":"2017","journal-title":"RNA"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"2841","DOI":"10.1093\/emboj\/cdg249","article-title":"Coordinated nuclear export of 60S ribosomal subunits and NMD3 in vertebrates","volume":"22","author":"Trotta","year":"2003","journal-title":"EMBO J."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/978-1-4939-2438-7_1","article-title":"Coronaviruses: An overview of their replication and pathogenesis","volume":"1282","author":"Fehr","year":"2015","journal-title":"Methods Mol. Biol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1128\/MMBR.69.4.635-664.2005","article-title":"Coronavirus pathogenesis and the emerging pathogen severe acute respiratory syndrome coronavirus","volume":"69","author":"Weiss","year":"2005","journal-title":"Microbiol. Mol. Biol. Rev. MMBR"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.medmal.2019.10.004","article-title":"Focus on Middle East respiratory syndrome coronavirus (MERS-CoV)","volume":"50","author":"Bleibtreu","year":"2020","journal-title":"Med. Mal. Infect."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1056\/NEJMoa2001017","article-title":"A Novel Coronavirus from Patients with Pneumonia in China, 2019","volume":"382","author":"Zhu","year":"2020","journal-title":"N. Eng. J. Med."},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Snijder, E.J., Limpens, R., de Wilde, A.H., de Jong, A.W.M., Zevenhoven-Dobbe, J.C., Maier, H.J., Faas, F., Koster, A.J., and B\u00e1rcena, M. (2020). A unifying structural and functional model of the coronavirus replication organelle: Tracking down RNA synthesis. PLoS Biol., 18.","DOI":"10.1101\/2020.03.24.005298"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1395","DOI":"10.1126\/science.abd3629","article-title":"A molecular pore spans the double membrane of the coronavirus replication organelle","volume":"369","author":"Wolff","year":"2020","journal-title":"Science"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1038\/s41586-020-2286-9","article-title":"A SARS-CoV-2 protein interaction map reveals targets for drug repurposing","volume":"583","author":"Gordon","year":"2020","journal-title":"Nature"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"28344","DOI":"10.1073\/pnas.2016650117","article-title":"SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling","volume":"117","author":"Miorin","year":"2020","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.bbrc.2020.11.115","article-title":"Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from the nuclear pore complex","volume":"536","author":"Kato","year":"2021","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_77","doi-asserted-by":"crossref","unstructured":"Addetia, A., Lieberman, N.A.P., Phung, Q., Hsiang, T.Y., Xie, H., Roychoudhury, P., Shrestha, L., Loprieno, M.A., Huang, M.L., and Gale, M. (2021). SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Transport through Interactions with Rae1 and Nup98. mBio, 12.","DOI":"10.1128\/mBio.00065-21"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"108234","DOI":"10.1016\/j.celrep.2020.108234","article-title":"Evasion of Type I Interferon by SARS-CoV-2","volume":"33","author":"Xia","year":"2020","journal-title":"Cell Rep."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"9812","DOI":"10.1128\/JVI.01012-07","article-title":"Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum\/Golgi membrane","volume":"81","author":"Frieman","year":"2007","journal-title":"J. Virol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1128\/JVI.01782-06","article-title":"Severe acute respiratory syndrome coronavirus open reading frame (ORF) 3b, ORF 6, and nucleocapsid proteins function as interferon antagonists","volume":"81","author":"Frieman","year":"2007","journal-title":"J. Virol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1083\/jcb.137.1.27","article-title":"A role for the M9 transport signal of hnRNP A1 in mRNA nuclear export","volume":"137","author":"Izaurralde","year":"1997","journal-title":"J. Cell Biol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"12483","DOI":"10.1093\/nar\/gku953","article-title":"hnRNPA1 couples nuclear export and translation of specific mRNAs downstream of FGF-2\/S6K2 signalling","volume":"42","author":"Roy","year":"2014","journal-title":"Nucl. Acids Res."},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Zhang, K., Miorin, L., Makio, T., Dehghan, I., Gao, S., Xie, Y., Zhong, H., Esparza, M., Kehrer, T., and Kumar, A. (2021). Nsp1 protein of SARS-CoV-2 disrupts the mRNA export machinery to inhibit host gene expression. Sci. Adv., 7.","DOI":"10.1126\/sciadv.abe7386"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1139\/bcb-2018-0394","article-title":"SARS coronavirus protein nsp1 disrupts localization of Nup93 from the nuclear pore complex","volume":"97","author":"Gomez","year":"2019","journal-title":"Biochem. Cell Biol. Biochim. Biol. Cell."},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"Sharma, K., \u00c5kerstr\u00f6m, S., Sharma, A.K., Chow, V.T., Teow, S., Abrenica, B., Booth, S.A., Booth, T.F., Mirazimi, A., and Lal, S.K. (2011). SARS-CoV 9b protein diffuses into nucleus, undergoes active Crm1 mediated nucleocytoplasmic export and triggers apoptosis when retained in the nucleus. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0019436"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"17554","DOI":"10.1038\/srep17554","article-title":"Middle East respiratory syndrome coronavirus ORF4b protein inhibits type I interferon production through both cytoplasmic and nuclear targets","volume":"5","author":"Yang","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Canton, J., Fehr, A.R., Fernandez-Delgado, R., Gutierrez-Alvarez, F.J., Sanchez-Aparicio, M.T., Garc\u00eda-Sastre, A., Perlman, S., Enjuanes, L., and Sola, I. (2018). MERS-CoV 4b protein interferes with the NF-\u03baB-dependent innate immune response during infection. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1006838"},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Schmidt, M.L., and Hoenen, T. (2017). Characterization of the catalytic center of the Ebola virus L polymerase. PLoS Negl. Trop. Dis., 11.","DOI":"10.1371\/journal.pntd.0005996"},{"key":"ref_89","doi-asserted-by":"crossref","unstructured":"Bodmer, B.S., Gre\u00dfler, J., Schmidt, M.L., Holzerland, J., Brandt, J., Braun, S., Groseth, A., and Hoenen, T. (2020). Differences in Viral RNA Synthesis but Not Budding or Entry Contribute to the In Vitro Attenuation of Reston Virus Compared to Ebola Virus. Microorganisms, 8.","DOI":"10.3390\/microorganisms8081215"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"13469","DOI":"10.1128\/JVI.01097-07","article-title":"Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily karyopherin alpha proteins with activated STAT1","volume":"81","author":"Reid","year":"2007","journal-title":"J. Virol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"5156","DOI":"10.1128\/JVI.02349-05","article-title":"Ebola virus VP24 binds karyopherin alpha1 and blocks STAT1 nuclear accumulation","volume":"80","author":"Reid","year":"2006","journal-title":"J. Virol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.chom.2014.07.008","article-title":"Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of phosphorylated STAT1","volume":"16","author":"Xu","year":"2014","journal-title":"Cell Host Microbe"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.virol.2017.06.002","article-title":"Ebolavirus protein VP24 interferes with innate immune responses by inhibiting interferon-\u03bb1 gene expression","volume":"509","author":"He","year":"2017","journal-title":"Virology"},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Zhang, A.P., Bornholdt, Z.A., Liu, T., Abelson, D.M., Lee, D.E., Li, S., Woods, V.L., and Saphire, E.O. (2012). The ebola virus interferon antagonist VP24 directly binds STAT1 and has a novel, pyramidal fold. PLoS Pathog., 8.","DOI":"10.1371\/journal.ppat.1002550"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1083\/jcb.200403057","article-title":"Nucleocytoplasmic shuttling by nucleoporins Nup153 and Nup214 and CRM1-dependent nuclear export control the subcellular distribution of latent Stat1","volume":"165","author":"Marg","year":"2004","journal-title":"J. Cell Biol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"4111","DOI":"10.1093\/emboj\/19.15.4111","article-title":"How Stat1 mediates constitutive gene expression: A complex of unphosphorylated Stat1 and IRF1 supports transcription of the LMP2 gene","volume":"19","author":"Wright","year":"2000","journal-title":"EMBO J."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"S904","DOI":"10.1093\/infdis\/jir323","article-title":"The Ebola virus VP24 protein prevents hnRNP C1\/C2 binding to karyopherin \u03b11 and partially alters its nuclear import","volume":"204","author":"Shabman","year":"2011","journal-title":"J. Infect. Dis."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1128\/MCB.23.2.708-720.2003","article-title":"Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc mRNA in a cell cycle phase-dependent manner","volume":"23","author":"Kim","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"4173","DOI":"10.1073\/pnas.0711222105","article-title":"NFAR-1 and -2 modulate translation and are required for efficient host defense","volume":"105","author":"Pfeifer","year":"2008","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"3254","DOI":"10.1128\/JVI.79.6.3254-3266.2005","article-title":"Functional interaction of heterogeneous nuclear ribonucleoprotein C with poliovirus RNA synthesis initiation complexes","volume":"79","author":"Brunner","year":"2005","journal-title":"J. Virol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1457","DOI":"10.1093\/nar\/27.6.1457","article-title":"hnRNP C and polypyrimidine tract-binding protein specifically interact with the pyrimidine-rich region within the 3\u2032NTR of the HCV RNA genome","volume":"27","author":"Gontarek","year":"1999","journal-title":"Nucl. Acids Res."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/S0168-1702(00)00238-0","article-title":"Heterogeneous nuclear ribonucleoprotein C binds exclusively to the functionally important UUUUU-motifs in the human papillomavirus type-1 AU-rich inhibitory element","volume":"73","author":"Sokolowski","year":"2001","journal-title":"Virus Res."},{"key":"ref_103","doi-asserted-by":"crossref","unstructured":"Miyake, T., Farley, C.M., Neubauer, B.E., Beddow, T.P., Hoenen, T., and Engel, D.A. (2020). ebola virus inclusion body formation and RNA synthesis are controlled by a novel domain of nucleoprotein interacting with VP35. J. Virol., 94.","DOI":"10.1128\/JVI.02100-19"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"S316","DOI":"10.1093\/infdis\/jiv240","article-title":"Importin-\u03b17 Is Involved in the Formation of Ebola Virus Inclusion Bodies but Is Not Essential for Pathogenicity in Mice","volume":"212","author":"Gabriel","year":"2015","journal-title":"J. Infect. Dis."},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Wendt, L., Brandt, J., Bodmer, B.S., Reiche, S., Schmidt, M.L., Traeger, S., and Hoenen, T. (2020). The ebola virus nucleoprotein recruits the nuclear RNA Export Factor NXF1 into inclusion bodies to facilitate viral protein expression. Cells, 9.","DOI":"10.3390\/cells9010187"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"1120","DOI":"10.1002\/eji.201847483","article-title":"Infection with a Brazilian isolate of Zika virus generates RIG-I stimulatory RNA and the viral NS5 protein blocks type I IFN induction and signaling","volume":"48","author":"Hertzog","year":"2018","journal-title":"Eur. J. Immunol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"10438","DOI":"10.1128\/JVI.00986-10","article-title":"The endoplasmic reticulum provides the membrane platform for biogenesis of the flavivirus replication complex","volume":"84","author":"Gillespie","year":"2010","journal-title":"J. Virol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/j.chom.2009.03.007","article-title":"Composition and three-dimensional architecture of the dengue virus replication and assembly sites","volume":"5","author":"Welsch","year":"2009","journal-title":"Cell Host Microbe"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/j.virol.2013.08.006","article-title":"Protein-protein interactions among West Nile non-structural proteins and transmembrane complex formation in mammalian cells","volume":"446","author":"Yu","year":"2013","journal-title":"Virology"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"5408","DOI":"10.1128\/JVI.02188-08","article-title":"NS5 of dengue virus mediates STAT2 binding and degradation","volume":"83","author":"Ashour","year":"2009","journal-title":"J. Virol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"36399","DOI":"10.1074\/jbc.M204977200","article-title":"The interdomain region of dengue NS5 protein that binds to the viral helicase NS3 contains independently functional importin beta 1 and importin alpha\/beta-recognized nuclear localization signals","volume":"277","author":"Brooks","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1111\/j.1600-0854.2007.00579.x","article-title":"Nuclear localization of dengue virus nonstructural protein 5 through its importin alpha\/beta-recognized nuclear localization sequences is integral to viral infection","volume":"8","author":"Pryor","year":"2007","journal-title":"Traffic"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"11642","DOI":"10.1093\/nar\/gku666","article-title":"The methyltransferase domain of dengue virus protein NS5 ensures efficient RNA synthesis initiation and elongation by the polymerase domain","volume":"42","author":"Potisopon","year":"2014","journal-title":"Nucl. Acids Res."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"22621","DOI":"10.1074\/jbc.M113.481382","article-title":"Serotype-specific differences in dengue virus non-structural protein 5 nuclear localization","volume":"288","author":"Hannemann","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Tay, M.Y., Smith, K., Ng, I.H., Chan, K.W., Zhao, Y., Ooi, E.E., Lescar, J., Luo, D., Jans, D.A., and Forwood, J.K. (2016). The C-terminal 18 Amino Acid Region of Dengue Virus NS5 Regulates its Subcellular Localization and Contains a Conserved Arginine Residue Essential for Infectious Virus Production. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005886"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"15589","DOI":"10.1074\/jbc.M808271200","article-title":"CRM1-mediated nuclear export of dengue virus RNA polymerase NS5 modulates interleukin-8 induction and virus production","volume":"284","author":"Rawlinson","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_117","doi-asserted-by":"crossref","unstructured":"De Jes\u00fas-Gonz\u00e1lez, L.A., Cervantes-Salazar, M., Reyes-Ruiz, J.M., Osuna-Ramos, J.F., Farf\u00e1n-Morales, C.N., Palacios-R\u00e1palo, S.N., P\u00e9rez-Olais, J.H., Cordero-Rivera, C.D., Hurtado-Monz\u00f3n, A.M., and Ru\u00edz-Jim\u00e9nez, F. (2020). The nuclear pore complex: A Target for NS3 protease of dengue and zika viruses. Viruses, 12.","DOI":"10.3390\/v12060583"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1007\/s00705-021-05026-w","article-title":"Nuclear localization of non-structural protein 3 (NS3) during dengue virus infection","volume":"166","year":"2021","journal-title":"Arch. Virol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"i657","DOI":"10.1136\/bmj.i657","article-title":"Zika virus is a global public health emergency, declares WHO","volume":"352","author":"Gulland","year":"2016","journal-title":"BMJ"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"242","DOI":"10.15585\/mmwr.mm6509e2","article-title":"Increase in reported prevalence of microcephaly in infants born to women living in areas with confirmed zika virus transmission during the first trimester of pregnancy-brazil, 2015","volume":"65","author":"Henriques","year":"2016","journal-title":"MMWR Morb. Mortal. Wkly. Rep."},{"key":"ref_121","doi-asserted-by":"crossref","unstructured":"Yang, L., Wang, R., Yang, S., Ma, Z., Lin, S., Nan, Y., Li, Q., Tang, Q., and Zhang, Y.J. (2018). Karyopherin alpha 6 is required for replication of porcine reproductive and respiratory syndrome virus and zika virus. J. Virol., 92.","DOI":"10.1128\/JVI.00072-18"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.virol.2019.10.010","article-title":"Zika virus NS5 nuclear accumulation is protective of protein degradation and is required for viral RNA replication","volume":"541","author":"Ji","year":"2020","journal-title":"Virology"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1021\/acsinfecdis.8b00373","article-title":"Zika Virus NS5 forms supramolecular nuclear bodies that sequester importin-\u03b1 and modulate the host immune and pro-inflammatory response in neuronal cells","volume":"5","author":"Ng","year":"2019","journal-title":"ACS Infect. Dis."},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Ye, J., Chen, Z., Li, Y., Zhao, Z., He, W., Zohaib, A., Song, Y., Deng, C., Zhang, B., and Chen, H. (2017). Japanese encephalitis virus NS5 Inhibits Type I Interferon (IFN) production by blocking the nuclear translocation of ifn regulatory factor 3 and NF-\u03baB. J. Virol., 91.","DOI":"10.1128\/JVI.00039-17"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1016\/j.virol.2018.11.009","article-title":"Zika virus NS5 protein antagonizes type I interferon production via blocking TBK1 activation","volume":"527","author":"Lin","year":"2019","journal-title":"Virology"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"2238","DOI":"10.1080\/15548627.2020.1823122","article-title":"Zika virus NS2A protein induces the degradation of KPNA2 (karyopherin subunit alpha 2) via chaperone-mediated autophagy","volume":"16","author":"He","year":"2020","journal-title":"Autophagy"},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Remenyi, R., Gao, Y., Hughes, R.E., Curd, A., Zothner, C., Peckham, M., Merits, A., and Harris, M. (2018). Persistent replication of a chikungunya virus replicon in human cells is associated with presence of stable cytoplasmic granules containing nonstructural protein 3. J. Virol., 92.","DOI":"10.1128\/JVI.00477-18"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"13878","DOI":"10.1128\/JVI.02666-13","article-title":"Chronic joint disease caused by persistent Chikungunya virus infection is controlled by the adaptive immune response","volume":"87","author":"Hawman","year":"2013","journal-title":"J. Virol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1186\/1743-422X-10-269","article-title":"Chikungunya virus capsid protein contains nuclear import and export signals","volume":"10","author":"Thomas","year":"2013","journal-title":"Virol. J."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Jacobs, S.C., Taylor, A., Herrero, L.J., Mahalingam, S., and Fazakerley, J.K. (2017). Mutation of a conserved nuclear export sequence in chikungunya virus capsid protein disrupts host cell nuclear import. Viruses, 9.","DOI":"10.3390\/v9100306"},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Webb, L.G., Veloz, J., Pintado-Silva, J., Zhu, T., Rangel, M.V., Mutetwa, T., Zhang, L., Bernal-Rubio, D., Figueroa, D., and Carrau, L. (2020). Chikungunya virus antagonizes cGAS-STING mediated type-I interferon responses by degrading cGAS. PLoS Pathog., 16.","DOI":"10.1371\/journal.ppat.1008999"},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"G\u00f6ertz, G.P., McNally, K.L., Robertson, S.J., Best, S.M., Pijlman, G.P., and Fros, J.J. (2018). The methyltransferase-like domain of chikungunya virus nsP2 inhibits the interferon response by promoting the nuclear export of STAT1. J. Virol., 92.","DOI":"10.1128\/JVI.01008-18"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"10877","DOI":"10.1128\/JVI.00949-10","article-title":"Chikungunya virus nonstructural protein 2 inhibits type I\/II interferon-stimulated JAK-STAT signaling","volume":"84","author":"Fros","year":"2010","journal-title":"J. Virol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"10394","DOI":"10.1128\/JVI.00884-13","article-title":"The C-terminal domain of chikungunya virus nsP2 independently governs viral RNA replication, cytopathicity, and inhibition of interferon signaling","volume":"87","author":"Fros","year":"2013","journal-title":"J. Virol."},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"Wong, K.Z., and Chu, J.J.H. (2018). The interplay of viral and host factors in chikungunya virus infection: Targets for antiviral strategies. Viruses, 10.","DOI":"10.3390\/v10060294"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1099\/vir.0.071845-0","article-title":"Chikungunya virus non-structural protein 2-mediated host shut-off disables the unfolded protein response","volume":"96","author":"Fros","year":"2015","journal-title":"J. Gen. Virol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"7415","DOI":"10.1073\/pnas.77.12.7415","article-title":"Detection and isolation of type C retrovirus particles from fresh and cultured lymphocytes of a patient with cutaneous T-cell lymphoma","volume":"77","author":"Poiesz","year":"1980","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"868","DOI":"10.1126\/science.6189183","article-title":"Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS)","volume":"220","author":"Chermann","year":"1983","journal-title":"Science"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"2491","DOI":"10.1007\/s00018-018-2772-5","article-title":"Cellular and molecular mechanisms of HIV-1 integration targeting","volume":"75","author":"Engelman","year":"2018","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"9702","DOI":"10.1128\/JVI.01669-15","article-title":"Impact of nucleoporin-mediated chromatin localization and nuclear architecture on HIV integration site selection","volume":"89","author":"Wong","year":"2015","journal-title":"J. Virol."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"13347","DOI":"10.1074\/jbc.273.21.13347","article-title":"Viral protein R regulates docking of the HIV-1 preintegration complex to the nuclear pore complex","volume":"273","author":"Popov","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/j.chom.2008.10.004","article-title":"Genome-scale RNAi screen for host factors required for HIV replication","volume":"4","author":"Zhou","year":"2008","journal-title":"Cell Host Microbe"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.cell.2008.07.032","article-title":"Global analysis of host-pathogen interactions that regulate early-stage HIV-1 replication","volume":"135","author":"Zhou","year":"2008","journal-title":"Cell"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1126\/science.1152725","article-title":"Identification of host proteins required for HIV infection through a functional genomic screen","volume":"319","author":"Brass","year":"2008","journal-title":"Science"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1186\/1742-4690-6-5","article-title":"Microarray study reveals that HIV-1 induces rapid type-I interferon-dependent p53 mRNA up-regulation in human primary CD4+ T cells","volume":"6","author":"Imbeault","year":"2009","journal-title":"Retrovirology"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"4795","DOI":"10.1128\/jvi.74.10.4795-4806.2000","article-title":"Identification of critical amino acid residues in human immunodeficiency virus type 1 IN required for efficient proviral DNA formation at steps prior to integration in dividing and nondividing cells","volume":"74","author":"Tsurutani","year":"2000","journal-title":"J. Virol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1128\/jvi.70.2.1027-1032.1996","article-title":"Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import","volume":"70","author":"Gallay","year":"1996","journal-title":"J. Virol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"4531","DOI":"10.1093\/emboj\/16.15.4531","article-title":"HIV-1 infection of non-dividing cells: Evidence that the amino-terminal basic region of the viral matrix protein is important for Gag processing but not for post-entry nuclear import","volume":"16","author":"Fouchier","year":"1997","journal-title":"EMBO J."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.cell.2007.08.018","article-title":"Structure of full-length HIV-1 CA: A model for the mature capsid lattice","volume":"131","author":"Cheng","year":"2007","journal-title":"Cell"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"3025","DOI":"10.1038\/sj.emboj.7601740","article-title":"HIV-1 DNA Flap formation promotes uncoating of the pre-integration complex at the nuclear pore","volume":"26","author":"Arhel","year":"2007","journal-title":"EMBO J."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"e2019467118","DOI":"10.1073\/pnas.2019467118","article-title":"HIV-1 cores retain their integrity until minutes before uncoating in the nucleus","volume":"118","author":"Li","year":"2021","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"ref_152","doi-asserted-by":"crossref","unstructured":"Francis, A.C., Marin, M., Prellberg, M.J., Palermino-Rowland, K., and Melikyan, G.B. (2020). HIV-1 Uncoating and Nuclear Import Precede the Completion of Reverse Transcription in Cell Lines and in Primary Macrophages. Viruses, 12.","DOI":"10.3390\/v12111234"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1038\/s41564-020-0735-8","article-title":"Nuclear pore blockade reveals that HIV-1 completes reverse transcription and uncoating in the nucleus","volume":"5","author":"Dharan","year":"2020","journal-title":"Nat. Microbiol."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1016\/j.cell.2021.01.025","article-title":"Cone-shaped HIV-1 capsids are transported through intact nuclear pores","volume":"184","author":"Zila","year":"2021","journal-title":"Cell"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"e60821","DOI":"10.7554\/eLife.60821","article-title":"HIV-1 Vpr antagonizes innate immune activation by targeting karyopherin-mediated NF-\u03baB\/IRF3 nuclear transport","volume":"9","author":"Khan","year":"2020","journal-title":"eLife"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/S0014-5793(98)00645-0","article-title":"A peptide derived from the N-terminal region of HIV-1 Vpr promotes nuclear import in permeabilized cells: Elucidation of the NLS region of the Vpr","volume":"429","author":"Karni","year":"1998","journal-title":"FEBS Lett."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"5284","DOI":"10.1128\/JVI.01928-06","article-title":"Novel nuclear import of Vpr promoted by importin alpha is crucial for human immunodeficiency virus type 1 replication in macrophages","volume":"81","author":"Kamata","year":"2007","journal-title":"J. Virol."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"2744","DOI":"10.1016\/j.jmb.2016.05.003","article-title":"Molecular Mechanism of HIV-1 Vpr for Binding to Importin-\u03b1","volume":"428","author":"Miyatake","year":"2016","journal-title":"J. Mol. Biol."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1146\/annurev.micro.52.1.491","article-title":"The HIV-1 Rev protein","volume":"52","author":"Pollard","year":"1998","journal-title":"Ann. Rev. Microbiol."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1006\/jmbi.1997.1420","article-title":"Interactions between HIV Rev and nuclear import and export factors: The Rev nuclear localisation signal mediates specific binding to human importin-beta","volume":"274","author":"Henderson","year":"1997","journal-title":"J. Mol. Biol."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1880","DOI":"10.1126\/science.280.5371.1880","article-title":"HIV-1 regulatory\/accessory genes: Keys to unraveling viral and host cell biology","volume":"280","author":"Emerman","year":"1998","journal-title":"Science"},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"8627","DOI":"10.1128\/JVI.72.11.8627-8635.1998","article-title":"Inhibition of human immunodeficiency virus Rev and human T-cell leukemia virus Rex function, but not Mason-Pfizer monkey virus constitutive transport element activity, by a mutant human nucleoporin targeted to Crm1","volume":"72","author":"Bogerd","year":"1998","journal-title":"J. Virol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1083\/jcb.152.5.895","article-title":"Cofactor requirements for nuclear export of Rev response element (RRE)- and constitutive transport element (CTE)-containing retroviral RNAs. An unexpected role for actin","volume":"152","author":"Hofmann","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1091\/mbc.10.3.649","article-title":"The nucleoporin nup153 plays a critical role in multiple types of nuclear export","volume":"10","author":"Ullman","year":"1999","journal-title":"Mol. Biol. Cell"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1128\/JVI.73.1.120-127.1999","article-title":"Nucleoporins nup98 and nup214 participate in nuclear export of human immunodeficiency virus type 1 Rev","volume":"73","author":"Zolotukhin","year":"1999","journal-title":"J. Virol."},{"key":"ref_166","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":"ref_167","doi-asserted-by":"crossref","first-page":"6645","DOI":"10.1093\/nar\/gku304","article-title":"HIV-1 Rev protein specifies the viral RNA export pathway by suppressing TAP\/NXF1 recruitment","volume":"42","author":"Taniguchi","year":"2014","journal-title":"Nucl. Acids Res."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"5305","DOI":"10.1038\/s41467-018-07753-2","article-title":"Intron-containing RNA from the HIV-1 provirus activates type I interferon and inflammatory cytokines","volume":"9","author":"McCauley","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1038\/s41579-020-00501-8","article-title":"Structural insights into RNA polymerases of negative-sense RNA viruses","volume":"19","author":"Grimes","year":"2021","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"22701","DOI":"10.1074\/jbc.270.39.22701","article-title":"Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import","volume":"270","author":"Jaskunas","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"1850","DOI":"10.1128\/jvi.71.3.1850-1856.1997","article-title":"The NPI-1\/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal","volume":"71","author":"Wang","year":"1997","journal-title":"J. Virol."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1006\/viro.1998.9329","article-title":"A classical bipartite nuclear localization signal on Thogoto and influenza A virus nucleoproteins","volume":"250","author":"Weber","year":"1998","journal-title":"Virology"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1111\/j.1600-0854.2005.00263.x","article-title":"An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein","volume":"6","author":"Cros","year":"2005","journal-title":"Traffic"},{"key":"ref_174","doi-asserted-by":"crossref","unstructured":"Donchet, A., Vassal-Stermann, E., G\u00e9rard, F.C.A., Ruigrok, R.W.H., and Cr\u00e9pin, T. (2020). Differential behaviours and preferential bindings of influenza nucleoproteins on importins-\u03b1. Viruses, 12.","DOI":"10.3390\/v12080834"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1038\/nsmb1212","article-title":"Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit","volume":"14","author":"Tarendeau","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_176","doi-asserted-by":"crossref","unstructured":"Gabriel, G., Herwig, A., and Klenk, H.D. (2008). Interaction of polymerase subunit PB2 and NP with importin alpha1 is a determinant of host range of influenza A virus. PLoS Pathog., 4.","DOI":"10.1371\/journal.ppat.0040011"},{"key":"ref_177","doi-asserted-by":"crossref","unstructured":"Hudjetz, B., and Gabriel, G. (2012). Human-like PB2 627K influenza virus polymerase activity is regulated by importin-\u03b11 and -\u03b17. PLoS Pathog., 8.","DOI":"10.1371\/journal.ppat.1002488"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1016\/j.str.2014.11.015","article-title":"Molecular determinants for nuclear import of influenza A PB2 by importin \u03b1 isoforms 3 and 7","volume":"23","author":"Pumroy","year":"2015","journal-title":"Structure"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"107549","DOI":"10.1016\/j.celrep.2020.107549","article-title":"Cellular Importin-\u03b13 Expression Dynamics in the Lung Regulate Antiviral Response Pathways against Influenza A Virus Infection","volume":"31","author":"Thiele","year":"2020","journal-title":"Cell Rep."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"24727","DOI":"10.1038\/srep24727","article-title":"Structural characterization of recombinant IAV polymerase reveals a stable complex between viral PA-PB1 heterodimer and host RanBP5","volume":"6","author":"Swale","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"3353","DOI":"10.1016\/j.jmb.2020.03.021","article-title":"X-ray structure of the human karyopherin RanBP5, an essential factor for influenza polymerase nuclear trafficking","volume":"432","author":"Swale","year":"2020","journal-title":"J. Mol. Biol."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"20067","DOI":"10.1074\/jbc.M114.569178","article-title":"The nuclear export protein of H5N1 influenza A viruses recruits Matrix 1 (M1) protein to the viral ribonucleoprotein to mediate nuclear export","volume":"289","author":"Brunotte","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"7455","DOI":"10.1128\/JVI.00257-14","article-title":"Characteristics of nucleocytoplasmic transport of H1N1 influenza A virus nuclear export protein","volume":"88","author":"Gao","year":"2014","journal-title":"J. Virol."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"1853","DOI":"10.1073\/pnas.0610977104","article-title":"Influenza virus targets the mRNA export machinery and the nuclear pore complex","volume":"104","author":"Satterly","year":"2007","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"1671","DOI":"10.1038\/s41564-019-0482-x","article-title":"Structural basis for influenza virus NS1 protein block of mRNA nuclear export","volume":"4","author":"Zhang","year":"2019","journal-title":"Nat. Microb."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1016\/S1097-2765(00)80099-4","article-title":"Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3\u2032end formation of cellular pre-mRNAs","volume":"1","author":"Nemeroff","year":"1998","journal-title":"Mol. Cell"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"2273","DOI":"10.1093\/emboj\/18.8.2273","article-title":"Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3\u2032-end processing machinery","volume":"18","author":"Chen","year":"1999","journal-title":"EMBO J."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.cell.2013.02.027","article-title":"The lipid mediator protectin D1 inhibits influenza virus replication and improves severe influenza","volume":"153","author":"Morita","year":"2013","journal-title":"Cell"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1099\/jgv.0.001072","article-title":"ICTV Virus Taxonomy Profile: Papillomaviridae","volume":"99","author":"Chen","year":"2018","journal-title":"J. Gen. Virol."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1056\/NEJMoa021641","article-title":"Epidemiologic classification of human papillomavirus types associated with cervical cancer","volume":"348","author":"Bosch","year":"2003","journal-title":"N. Eng. J. Med."},{"key":"ref_191","doi-asserted-by":"crossref","unstructured":"Aydin, I., Weber, S., Snijder, B., Samperio Ventayol, P., K\u00fchbacher, A., Becker, M., Day, P.M., Schiller, J.T., Kann, M., and Pelkmans, L. (2014). Large scale RNAi reveals the requirement of nuclear envelope breakdown for nuclear import of human papillomaviruses. PLoS Pathog., 10.","DOI":"10.1371\/journal.ppat.1004162"},{"key":"ref_192","doi-asserted-by":"crossref","unstructured":"Pyeon, D., Pearce, S.M., Lank, S.M., Ahlquist, P., and Lambert, P.F. (2009). Establishment of human papillomavirus infection requires cell cycle progression. PLoS Pathog., 5.","DOI":"10.1371\/journal.ppat.1000318"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"13232","DOI":"10.1128\/JVI.77.24.13232-13247.2003","article-title":"Signals that dictate nuclear localization of human papillomavirus type 16 oncoprotein E6 in living cells","volume":"77","author":"Tao","year":"2003","journal-title":"J. Virol."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"2330","DOI":"10.1128\/JVI.77.4.2330-2337.2003","article-title":"Nuclear entry of high-risk human papillomavirus type 16 E6 oncoprotein occurs via several pathways","volume":"77","author":"Moroianu","year":"2003","journal-title":"J. Virol."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"2099","DOI":"10.1099\/vir.0.18961-0","article-title":"Preferential nuclear localization of the human papillomavirus type 16 E6 oncoprotein in cervical carcinoma cells","volume":"84","author":"Masson","year":"2003","journal-title":"J. Gen. Virol."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"7288","DOI":"10.1128\/MCB.18.12.7288","article-title":"Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6","volume":"18","author":"Freedman","year":"1998","journal-title":"Mol. Cell. Biol."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"8773","DOI":"10.1128\/JVI.79.14.8773-8783.2005","article-title":"Involvement of nuclear export in human papillomavirus type 18 E6-mediated ubiquitination and degradation of p53","volume":"79","author":"Stewart","year":"2005","journal-title":"J. Virol."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/j.virol.2008.10.006","article-title":"The human papillomavirus E7 oncoprotein","volume":"384","year":"2009","journal-title":"Virology"},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.virol.2003.08.024","article-title":"The E7 oncoprotein of high-risk human papillomavirus type 16 enters the nucleus via a nonclassical Ran-dependent pathway","volume":"317","author":"Angeline","year":"2003","journal-title":"Virology"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.virol.2008.09.037","article-title":"Identification of the nuclear localization and export signals of high risk HPV16 E7 oncoprotein","volume":"383","author":"Knapp","year":"2009","journal-title":"Virology"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.virol.2013.08.017","article-title":"Nuclear import of high risk HPV16 E7 oncoprotein is mediated by its zinc-binding domain via hydrophobic interactions with Nup62","volume":"446","author":"Eberhard","year":"2013","journal-title":"Virology"},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.virol.2013.11.020","article-title":"Nuclear import of cutaneous beta genus HPV8 E7 oncoprotein is mediated by hydrophobic interactions between its zinc-binding domain and FG nucleoporins","volume":"449","author":"Onder","year":"2014","journal-title":"Virology"},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.virol.2013.04.031","article-title":"Characterization of the transport signals that mediate the nucleocytoplasmic traffic of low risk HPV11 E7","volume":"443","author":"McKee","year":"2013","journal-title":"Virology"},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"13954","DOI":"10.1128\/JVI.78.24.13954-13965.2004","article-title":"Cyclin\/CDK regulates the nucleocytoplasmic localization of the human papillomavirus E1 DNA helicase","volume":"78","author":"Deng","year":"2004","journal-title":"J. Virol."},{"key":"ref_205","doi-asserted-by":"crossref","unstructured":"Egawa, N., Wang, Q., Griffin, H.M., Murakami, I., Jackson, D., Mahmood, R., and Doorbar, J. (2017). HPV16 and 18 genome amplification show different E4-dependence, with 16E4 enhancing E1 nuclear accumulation and replicative efficiency via its cell cycle arrest and kinase activation functions. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006282"},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"5066","DOI":"10.1128\/JVI.02480-06","article-title":"Mitogen-activated protein kinases activate the nuclear localization sequence of human papillomavirus type 11 E1 DNA helicase to promote efficient nuclear import","volume":"81","author":"Yu","year":"2007","journal-title":"J. Virol."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"2899","DOI":"10.1128\/JVI.01850-06","article-title":"Nuclear import of bovine papillomavirus type 1 E1 protein is mediated by multiple alpha importins and is negatively regulated by phosphorylation near a nuclear localization signal","volume":"81","author":"Bian","year":"2007","journal-title":"J. Virol."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"11747","DOI":"10.1128\/JVI.01445-10","article-title":"Nuclear export of human papillomavirus type 31 E1 is regulated by Cdk2 phosphorylation and required for viral genome maintenance","volume":"84","author":"Moody","year":"2010","journal-title":"J. Virol."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"36088","DOI":"10.1074\/jbc.M505138200","article-title":"Nucleo-cytoplasmic shuttling of high risk human Papillomavirus E2 proteins induces apoptosis","volume":"280","author":"Blachon","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.virol.2006.10.018","article-title":"Characterization of the nuclear localization signal of high risk HPV16 E2 protein","volume":"360","author":"Klucevsek","year":"2007","journal-title":"Virology"},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"23958","DOI":"10.1074\/jbc.M200724200","article-title":"Nuclear import strategies of high risk HPV16 L1 major capsid protein","volume":"277","author":"Nelson","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"12179","DOI":"10.1128\/JVI.78.22.12179-12188.2004","article-title":"The l2 minor capsid protein of human papillomavirus type 16 interacts with a network of nuclear import receptors","volume":"78","author":"Darshan","year":"2004","journal-title":"J. Virol."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0163-4453(83)96695-1","article-title":"Post-exposure hepatitis B vaccination of sexual partners of acute viral hepatitis patients","volume":"7","author":"Papaevangelou","year":"1983","journal-title":"J. Infect."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.micpath.2019.01.004","article-title":"Molecular mechanistic insight of hepatitis B virus mediated hepatocellular carcinoma","volume":"128","author":"Chaturvedi","year":"2019","journal-title":"Microb. Pathog."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"1972","DOI":"10.1136\/gutjnl-2015-309809","article-title":"HBV cccDNA: Viral persistence reservoir and key obstacle for a cure of chronic hepatitis B","volume":"64","author":"Nassal","year":"2015","journal-title":"Gut"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1083\/jcb.145.1.45","article-title":"Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex","volume":"145","author":"Kann","year":"1999","journal-title":"J. Cell Biol."},{"key":"ref_217","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. Nat. Acad. Sci. USA"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1128\/JVI.01921-09","article-title":"Production and function of the cytoplasmic deproteinized relaxed circular DNA of hepadnaviruses","volume":"84","author":"Guo","year":"2010","journal-title":"J. Virol."},{"key":"ref_219","doi-asserted-by":"crossref","unstructured":"Schmitz, A., Schwarz, A., Foss, M., Zhou, L., Rabe, B., Hoellenriegel, J., Stoeber, M., Pant\u00e9, N., and Kann, M. (2010). Nucleoporin 153 arrests the nuclear import of hepatitis B virus capsids in the nuclear basket. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1000741"},{"key":"ref_220","doi-asserted-by":"crossref","unstructured":"Li, H.C., Huang, E.Y., Su, P.Y., Wu, S.Y., Yang, C.C., Lin, Y.S., Chang, W.C., and Shih, C. (2010). Nuclear export and import of human hepatitis B virus capsid protein and particles. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1001162"},{"key":"ref_221","doi-asserted-by":"crossref","unstructured":"Nair, S., and Zlotnick, A. (2021). HBV Core protein is in flux between cytoplasmic, nuclear, and nucleolar compartments. mBio, 12.","DOI":"10.1128\/mBio.03514-20"},{"key":"ref_222","doi-asserted-by":"crossref","unstructured":"Chen, C., Wang, J.C., Pierson, E.E., Keifer, D.Z., Delaleau, M., Gallucci, L., Cazenave, C., Kann, M., Jarrold, M.F., and Zlotnick, A. (2016). Importin \u03b2 can bind hepatitis b virus core protein and empty core-like particles and induce structural changes. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005802"},{"key":"ref_223","doi-asserted-by":"crossref","unstructured":"Mitra, B., Wang, J., Kim, E.S., Mao, R., Dong, M., Liu, Y., Zhang, J., and Guo, H. (2019). Hepatitis B Virus Precore Protein p22 Inhibits Alpha Interferon Signaling by Blocking STAT Nuclear Translocation. J. Virol., 93.","DOI":"10.1128\/JVI.00196-19"},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"eaao7298","DOI":"10.1126\/science.aao7298","article-title":"Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes","volume":"360","author":"Dai","year":"2018","journal-title":"Science"},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"6610","DOI":"10.1128\/JVI.02655-08","article-title":"Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN\/Nup214 and the capsid protein pUL25","volume":"83","author":"Pasdeloup","year":"2009","journal-title":"J. Virol."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1128\/JVI.01139-08","article-title":"Herpes simplex virus replication: Roles of viral proteins and nucleoporins in capsid-nucleus attachment","volume":"83","author":"Copeland","year":"2009","journal-title":"J. Virol."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"8998","DOI":"10.1128\/JVI.01209-12","article-title":"A Nuclear localization signal in herpesvirus protein VP1-2 is essential for infection via capsid routing to the nuclear pore","volume":"86","author":"Abaitua","year":"2012","journal-title":"J. Virol."},{"key":"ref_228","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":"ref_229","doi-asserted-by":"crossref","unstructured":"D\u00f6hner, K., Ramos-Nascimento, A., Bialy, D., Anderson, F., Hickford-Martinez, A., Rother, F., Koithan, T., Rudolph, K., Buch, A., and Prank, U. (2018). Importin \u03b11 is required for nuclear import of herpes simplex virus proteins and capsid assembly in fibroblasts and neurons. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1006823"},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"3127","DOI":"10.1099\/0022-1317-75-11-3127","article-title":"Role of the carboxy terminus of herpes simplex virus type 1 DNA polymerase in its interaction with UL42","volume":"75","author":"Marsden","year":"1994","journal-title":"J. Gen. Virol."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1006\/viro.2000.0390","article-title":"The catalytic subunit of herpes simplex virus type 1 DNA polymerase contains a nuclear localization signal in the UL42-binding region","volume":"273","author":"Loregian","year":"2000","journal-title":"Virology"},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"9155","DOI":"10.1021\/bi7002394","article-title":"An importin alpha\/beta-recognized bipartite nuclear localization signal mediates targeting of the human herpes simplex virus type 1 DNA polymerase catalytic subunit pUL30 to the nucleus","volume":"46","author":"Alvisi","year":"2007","journal-title":"Biochemistry"},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"13764","DOI":"10.1021\/bi800869y","article-title":"Nuclear import of HSV-1 DNA polymerase processivity factor UL42 is mediated by a C-terminally located bipartite nuclear localization signal","volume":"47","author":"Alvisi","year":"2008","journal-title":"Biochemistry"},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1111\/dgd.12043","article-title":"Embryonic fibroblasts represent a connecting link between mesenchymal and embryonic stem cells","volume":"55","author":"Yusuf","year":"2013","journal-title":"Dev. Growth Differ."},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1042\/BST0330499","article-title":"The herpes simplex virus ICP27 protein: A multifunctional post-transcriptional regulator of gene expression","volume":"33","author":"Smith","year":"2005","journal-title":"Biochem. Soc. Trans."},{"key":"ref_236","first-page":"5241","article-title":"The many roles of the regulatory protein ICP27 during herpes simplex virus infection","volume":"13","year":"2008","journal-title":"Front. Biosci. J. Virtual Librar."},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"3949","DOI":"10.1128\/JVI.79.7.3949-3961.2005","article-title":"ICP27 recruits Aly\/REF but not TAP\/NXF1 to herpes simplex virus type 1 transcription sites although TAP\/NXF1 is required for ICP27 export","volume":"79","author":"Chen","year":"2005","journal-title":"J. Virol."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.virol.2010.02.023","article-title":"SR proteins SRp20 and 9G8 contribute to efficient export of herpes simplex virus 1 mRNAs","volume":"401","author":"Li","year":"2010","journal-title":"Virology"},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"5769","DOI":"10.1093\/emboj\/20.20.5769","article-title":"Herpes simplex virus ICP27 protein provides viral mRNAs with access to the cellular mRNA export pathway","volume":"20","author":"Koffa","year":"2001","journal-title":"EMBO J."},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"12277","DOI":"10.1074\/jbc.M111.331777","article-title":"Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathways","volume":"287","author":"Malik","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_241","doi-asserted-by":"crossref","unstructured":"Boruchowicz, H., Hawkins, J., Cruz-Palomar, K., and Lipp\u00e9, R. (2020). The XPO6 Exportin Mediates Herpes Simplex Virus 1 gM Nuclear Release Late in Infection. J. Virol., 94.","DOI":"10.1128\/JVI.00753-20"},{"key":"ref_242","doi-asserted-by":"crossref","unstructured":"Walter, G., Richert, Q., Ponnampalam, A., and Sharma, A. (2021). Acute superior mesenteric vein thrombosis in the setting of cytomegalovirus mononucleosis: A case report and review of the literature. Lancet Infect. Dis.","DOI":"10.1016\/S1473-3099(20)30782-9"},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1038\/nrneurol.2016.149","article-title":"HIV-associated opportunistic CNS infections: Pathophysiology, diagnosis and treatment","volume":"12","author":"Bowen","year":"2016","journal-title":"Nat. Rev. Neurol."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"1743","DOI":"10.1099\/vir.0.039214-0","article-title":"Human cytomegalovirus UL97 kinase alters the accumulation of CDK1","volume":"93","author":"Gill","year":"2012","journal-title":"J. Gen. Virol."},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"1756","DOI":"10.1099\/vir.0.040592-0","article-title":"Nuclear import of isoforms of the cytomegalovirus kinase pUL97 is mediated by differential activity of NLS1 and NLS2 both acting through classical importin-\u03b1 binding","volume":"93","author":"Webel","year":"2012","journal-title":"J. Gen. Virol."},{"key":"ref_246","doi-asserted-by":"crossref","unstructured":"Perng, Y.C., Campbell, J.A., Lenschow, D.J., and Yu, D. (2014). Human cytomegalovirus pUL79 is an elongation factor of RNA polymerase II for viral gene transcription. PLoS Pathog., 10.","DOI":"10.1371\/journal.ppat.1004350"},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1007\/s00430-012-0243-4","article-title":"A PY-nuclear localization signal is required for nuclear accumulation of HCMV UL79 protein","volume":"201","author":"Wang","year":"2012","journal-title":"Med. Microbiol. Immunol."},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"8484","DOI":"10.1128\/JVI.00738-10","article-title":"Nucleocytoplasmic shuttling of human cytomegalovirus UL84 is essential for virus growth","volume":"84","author":"Gao","year":"2010","journal-title":"J. Virol."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"3734","DOI":"10.1128\/JVI.77.6.3734-3748.2003","article-title":"A nonconventional nuclear localization signal within the UL84 protein of human cytomegalovirus mediates nuclear import via the importin alpha\/beta pathway","volume":"77","author":"Lischka","year":"2003","journal-title":"J. Virol."},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"10274","DOI":"10.1128\/JVI.00995-06","article-title":"Human cytomegalovirus UL84 protein contains two nuclear export signals and shuttles between the nucleus and the cytoplasm","volume":"80","author":"Lischka","year":"2006","journal-title":"J. Virol."},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"1237","DOI":"10.1093\/nar\/gkl007","article-title":"RNA-binding of the human cytomegalovirus transactivator protein UL69, mediated by arginine-rich motifs, is not required for nuclear export of unspliced RNA","volume":"34","author":"Toth","year":"2006","journal-title":"Nucl. Acids Res."},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"1804","DOI":"10.1128\/JVI.01347-10","article-title":"Characterization of the betaherpesviral pUL69 protein family reveals binding of the cellular mRNA export factor UAP56 as a prerequisite for stimulation of nuclear mRNA export and for efficient viral replication","volume":"85","author":"Zielke","year":"2011","journal-title":"J. Virol."},{"key":"ref_253","first-page":"167","article-title":"Interactions of human cytomegalovirus proteins with the nuclear transport machinery","volume":"325","author":"Stamminger","year":"2008","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"7271","DOI":"10.1093\/emboj\/20.24.7271","article-title":"A novel transferable nuclear export signal mediates CRM1-independent nucleocytoplasmic shuttling of the human cytomegalovirus transactivator protein pUL69","volume":"20","author":"Lischka","year":"2001","journal-title":"EMBO J."},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"8605","DOI":"10.1074\/jbc.M805693200","article-title":"Cyclin-dependent Kinases Phosphorylate the Cytomegalovirus RNA Export Protein pUL69 and Modulate Its Nuclear Localization and Activity","volume":"284","author":"Rechter","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1038\/s41579-019-0249-7","article-title":"Latency and lytic replication in Epstein-Barr virus-associated oncogenesis","volume":"17","year":"2019","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1006\/viro.1999.0054","article-title":"Epstein-barr virus nuclear antigen-1 binds to nuclear transporter karyopherin alpha1\/NPI-1 in addition to karyopherin alpha2\/Rch1","volume":"266","author":"Ito","year":"2000","journal-title":"Virology"},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"1703","DOI":"10.1128\/JVI.02880-14","article-title":"BGLF4 kinase modulates the structure and transport preference of the nuclear pore complex to facilitate nuclear import of Epstein-Barr virus lytic proteins","volume":"89","author":"Chang","year":"2015","journal-title":"J. Virol."},{"key":"ref_259","doi-asserted-by":"crossref","first-page":"11913","DOI":"10.1128\/JVI.01100-08","article-title":"Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production","volume":"82","author":"Lee","year":"2008","journal-title":"J. Virol."},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1128\/JVI.02358-13","article-title":"Human cytomegalovirus UL50 and UL53 recruit viral protein kinase UL97, not protein kinase C, for disruption of nuclear lamina and nuclear egress in infected cells","volume":"88","author":"Sharma","year":"2014","journal-title":"J. Virol."},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"643327","DOI":"10.3389\/fmicb.2021.643327","article-title":"Epstein-Barr Virus Limits the Accumulation of IPO7, an Essential Gene Product","volume":"12","author":"Yang","year":"2021","journal-title":"Front. Microbiol."},{"key":"ref_262","doi-asserted-by":"crossref","first-page":"12405","DOI":"10.1128\/JVI.01415-10","article-title":"Cellular immediate-early gene expression occurs kinetically upstream of Epstein-Barr virus bzlf1 and brlf1 following cross-linking of the B cell antigen receptor in the Akata Burkitt lymphoma cell line","volume":"84","author":"Ye","year":"2010","journal-title":"J. Virol."},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"6872","DOI":"10.1128\/JVI.73.8.6872-6881.1999","article-title":"Association with the cellular export receptor CRM 1 mediates function and intracellular localization of Epstein-Barr virus SM protein, a regulator of gene expression","volume":"73","author":"Boyle","year":"1999","journal-title":"J. Virol."},{"key":"ref_264","doi-asserted-by":"crossref","unstructured":"Funk, C., Ott, M., Raschbichler, V., Nagel, C.H., Binz, A., Sodeik, B., Bauerfeind, R., and Bailer, S.M. (2015). The herpes simplex virus protein pUL31 escorts nucleocapsids to sites of nuclear egress, a process coordinated by its N-terminal domain. PLoS Pathog., 11.","DOI":"10.1371\/journal.ppat.1004957"},{"key":"ref_265","doi-asserted-by":"crossref","first-page":"3713","DOI":"10.1128\/JVI.79.6.3713-3727.2005","article-title":"Characterization and intracellular localization of the Epstein-Barr virus protein BFLF2: Interactions with BFRF1 and with the nuclear lamina","volume":"79","author":"Gonnella","year":"2005","journal-title":"J. Virol."},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"2056","DOI":"10.1099\/vir.0.052571-0","article-title":"The cytomegalovirus egress proteins pUL50 and pUL53 are translocated to the nuclear envelope through two distinct modes of nuclear import","volume":"94","author":"Schmeiser","year":"2013","journal-title":"J. Gen. Virol."},{"key":"ref_267","doi-asserted-by":"crossref","first-page":"1500","DOI":"10.1159\/000495641","article-title":"Characterization of the nucleocytoplasmic transport mechanisms of epstein-barr virus BFLF2","volume":"51","author":"Li","year":"2018","journal-title":"Cell. Physiol. Biochem."},{"key":"ref_268","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.abb.2015.09.024","article-title":"Identification of molecular determinants for the nuclear import of pseudorabies virus UL31","volume":"587","author":"Li","year":"2015","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"2379","DOI":"10.1007\/s00705-016-2910-z","article-title":"Characterization of the nuclear import signal of herpes simplex virus 1 UL31","volume":"161","author":"Cai","year":"2016","journal-title":"Arch. Virol."},{"key":"ref_270","doi-asserted-by":"crossref","first-page":"2002","DOI":"10.1128\/JVI.03143-14","article-title":"Functional characterization of nuclear trafficking signals in pseudorabies virus pUL31","volume":"89","author":"Klupp","year":"2015","journal-title":"J. Virol."},{"key":"ref_271","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1111\/tra.12627","article-title":"Comprehensive analysis of nuclear export of herpes simplex virus type 1 tegument proteins and their Epstein-Barr virus orthologs","volume":"20","author":"Funk","year":"2019","journal-title":"Traffic"},{"key":"ref_272","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/ncomms1158","article-title":"Differential use of importin-\u03b1 isoforms governs cell tropism and host adaptation of influenza virus","volume":"2","author":"Gabriel","year":"2011","journal-title":"Nat. Commun."},{"key":"ref_273","doi-asserted-by":"crossref","unstructured":"Higgs, E.S., Gayedyu-Dennis, D., Fisher, W., Nason, M., Reilly, C., Beavogui, A.H., Aboulhab, J., Nordwall, J., Lobbo, P., and Wachekwa, I. (2021). PREVAIL IV: A Randomized, Double-Blind, Two-Phase, Phase 2 Trial of Remdesivir versus Placebo for Reduction of Ebola Virus RNA in the Semen of Male Survivors. Clin. Infect. Dis.","DOI":"10.1093\/cid\/ciab215"},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"2083","DOI":"10.1016\/S0140-6736(13)61127-7","article-title":"Antiretroviral prophylaxis for HIV infection in injecting drug users in Bangkok, Thailand (the Bangkok Tenofovir Study): A randomised, double-blind, placebo-controlled phase 3 trial","volume":"381","author":"Choopanya","year":"2013","journal-title":"Lancet"},{"key":"ref_275","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1056\/NEJMoa1410649","article-title":"Tenofovir Gel for the Prevention of Herpes Simplex Virus Type 2 Infection","volume":"373","author":"Kharsany","year":"2015","journal-title":"N. Engl. J. Med."},{"key":"ref_276","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1016\/j.chembiol.2008.07.019","article-title":"Design of peptide inhibitors for the importin alpha\/beta nuclear import pathway by activity-based profiling","volume":"15","author":"Kosugi","year":"2008","journal-title":"Chem. Biol."},{"key":"ref_277","doi-asserted-by":"crossref","first-page":"14255","DOI":"10.1074\/jbc.270.24.14255","article-title":"Inhibition of nuclear translocation of transcription factor NF-kappa B by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence","volume":"270","author":"Lin","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"e000386","DOI":"10.1161\/JAHA.113.000386","article-title":"Targeting nuclear import shuttles, importins\/karyopherins alpha by a peptide mimicking the NF\u03baB1\/p50 nuclear localization sequence","volume":"2","author":"Zienkiewicz","year":"2013","journal-title":"J. Am. Heart Assoc."},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/j.antiviral.2013.06.002","article-title":"Nuclear localization of dengue virus (DENV) 1-4 non-structural protein 5; protection against all 4 DENV serotypes by the inhibitor Ivermectin","volume":"99","author":"Tay","year":"2013","journal-title":"Antivir. Res."},{"key":"ref_280","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1042\/BJ20120150","article-title":"Ivermectin is a specific inhibitor of importin \u03b1\/\u03b2-mediated nuclear import able to inhibit replication of HIV-1 and dengue virus","volume":"443","author":"Wagstaff","year":"2012","journal-title":"Biochem. J."},{"key":"ref_281","doi-asserted-by":"crossref","unstructured":"Yang, S.N.Y., Atkinson, S.C., Fraser, J.E., Wang, C., Maher, B., Roman, N., Forwood, J.K., Wagstaff, K.M., Borg, N.A., and Jans, D.A. (2019). Novel flavivirus antiviral that targets the host nuclear transport importin \u03b1\/\u03b21 heterodimer. Cells, 8.","DOI":"10.3390\/cells8030281"},{"key":"ref_282","doi-asserted-by":"crossref","first-page":"104760","DOI":"10.1016\/j.antiviral.2020.104760","article-title":"The broad spectrum antiviral ivermectin targets the host nuclear transport importin \u03b1\/\u03b21 heterodimer","volume":"177","author":"Yang","year":"2020","journal-title":"Antivir. Res."},{"key":"ref_283","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1021\/cb2000296","article-title":"Importazole, a small molecule inhibitor of the transport receptor importin-\u03b2","volume":"6","author":"Soderholm","year":"2011","journal-title":"ACS Chem. Biol."},{"key":"ref_284","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1158\/1535-7163.MCT-15-0052","article-title":"Targeting the Nuclear Import Receptor Kpn\u03b21 as an Anticancer Therapeutic","volume":"15","author":"Chi","year":"2016","journal-title":"Mol. Cancer Ther."},{"key":"ref_285","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1021\/cb100094k","article-title":"Identification of a small molecule inhibitor of importin \u03b2 mediated nuclear import by confocal on-bead screening of tagged one-bead one-compound libraries","volume":"5","author":"Hintersteiner","year":"2010","journal-title":"ACS Chem. Biol."},{"key":"ref_286","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1038\/nsmb1229","article-title":"Structure-based design of a pathway-specific nuclear import inhibitor","volume":"14","author":"Cansizoglu","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_287","doi-asserted-by":"crossref","first-page":"5751","DOI":"10.18632\/aging.102965","article-title":"Molecular anatomy of the subcellular localization and nuclear import mechanism of herpes simplex virus 1 UL6","volume":"12","author":"Cai","year":"2020","journal-title":"Aging"},{"key":"ref_288","doi-asserted-by":"crossref","first-page":"6320","DOI":"10.1016\/S0021-9258(17)37374-X","article-title":"Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression","volume":"269","author":"Nishi","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_289","doi-asserted-by":"crossref","first-page":"9112","DOI":"10.1073\/pnas.96.16.9112","article-title":"Leptomycin B inactivates CRM1\/exportin 1 by covalent modification at a cysteine residue in the central conserved region","volume":"96","author":"Kudo","year":"1999","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"ref_290","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.exphem.2012.09.002","article-title":"Novel selective inhibitors of nuclear export CRM1 antagonists for therapy in mantle cell lymphoma","volume":"41","author":"Zhang","year":"2013","journal-title":"Exp. Hematol."},{"key":"ref_291","doi-asserted-by":"crossref","first-page":"1765","DOI":"10.1182\/blood-2012-04-423160","article-title":"Preclinical activity of a novel CRM1 inhibitor in acute myeloid leukemia","volume":"120","author":"Ranganathan","year":"2012","journal-title":"Blood"},{"key":"ref_292","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.1073\/pnas.1217203110","article-title":"Nuclear export inhibition through covalent conjugation and hydrolysis of Leptomycin B by CRM1","volume":"110","author":"Sun","year":"2013","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"ref_293","doi-asserted-by":"crossref","first-page":"4621","DOI":"10.1182\/blood-2012-05-429506","article-title":"Selective inhibitors of nuclear export show that CRM1\/XPO1 is a target in chronic lymphocytic leukemia","volume":"120","author":"Lapalombella","year":"2012","journal-title":"Blood"},{"key":"ref_294","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1038\/nn.3953","article-title":"Nuclear export inhibitors avert progression in preclinical models of inflammatory demyelination","volume":"18","author":"Haines","year":"2015","journal-title":"Nat. Neurosci."},{"key":"ref_295","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1038\/leu.2013.115","article-title":"CRM1 inhibition induces tumor cell cytotoxicity and impairs osteoclastogenesis in multiple myeloma: Molecular mechanisms and therapeutic implications","volume":"28","author":"Tai","year":"2014","journal-title":"Leukemia"},{"key":"ref_296","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1038\/bjc.1996.415","article-title":"Phase I trial of elactocin","volume":"74","author":"Newlands","year":"1996","journal-title":"Br. J. Cancer"},{"key":"ref_297","doi-asserted-by":"crossref","first-page":"16010","DOI":"10.1038\/sigtrans.2016.10","article-title":"Inhibiting cancer cell hallmark features through nuclear export inhibition","volume":"1","author":"Sun","year":"2016","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_298","doi-asserted-by":"crossref","first-page":"1555","DOI":"10.1016\/j.bbrc.2017.10.016","article-title":"Nuclear import inhibitor N-(4-hydroxyphenyl) retinamide targets Zika virus (ZIKV) nonstructural protein 5 to inhibit ZIKV infection","volume":"493","author":"Wang","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_299","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.antiviral.2017.10.014","article-title":"Antiviral activity of N-(4-hydroxyphenyl) retinamide (4-HPR) against Zika virus","volume":"147","author":"Pitts","year":"2017","journal-title":"Antivir. Res."},{"key":"ref_300","doi-asserted-by":"crossref","first-page":"1780","DOI":"10.1093\/infdis\/jiu319","article-title":"A nuclear transport inhibitor that modulates the unfolded protein response and provides in vivo protection against lethal dengue virus infection","volume":"210","author":"Fraser","year":"2014","journal-title":"J. Infect. Dis."},{"key":"ref_301","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1038\/s41586-020-2443-1","article-title":"Clinical targeting of HIV capsid protein with a long-acting small molecule","volume":"584","author":"Link","year":"2020","journal-title":"Nature"},{"key":"ref_302","doi-asserted-by":"crossref","first-page":"1377","DOI":"10.1038\/s41591-019-0560-x","article-title":"A highly potent long-acting small-molecule HIV-1 capsid inhibitor with efficacy in a humanized mouse model","volume":"25","author":"Yant","year":"2019","journal-title":"Nat. Med."},{"key":"ref_303","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.antiviral.2019.02.003","article-title":"Novel influenza inhibitors designed to target PB1 interactions with host importin RanBP5","volume":"164","author":"Mohl","year":"2019","journal-title":"Antivir. Res."},{"key":"ref_304","doi-asserted-by":"crossref","first-page":"4456","DOI":"10.1039\/C8OB00706C","article-title":"Development of oligonucleotide-based antagonists of Ebola virus protein 24 inhibiting its interaction with karyopherin alpha 1","volume":"16","author":"Tanaka","year":"2018","journal-title":"Org. Biomol. Chem."},{"key":"ref_305","doi-asserted-by":"crossref","first-page":"5155","DOI":"10.1039\/C7OB00012J","article-title":"Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5","volume":"15","author":"Song","year":"2017","journal-title":"Org. Biomol. Chem."},{"key":"ref_306","first-page":"621","article-title":"Randomized placebo-controlled evaluation of intramuscular interferon beta treatment of recurrent human papillomavirus","volume":"97","year":"2001","journal-title":"Obstet. Gynecol."},{"key":"ref_307","doi-asserted-by":"crossref","first-page":"3311","DOI":"10.1038\/emboj.2008.241","article-title":"Interferon-inducible protein, P56, inhibits HPV DNA replication by binding to the viral protein E1","volume":"27","author":"Terenzi","year":"2008","journal-title":"EMBO J."},{"key":"ref_308","doi-asserted-by":"crossref","first-page":"5344","DOI":"10.1128\/AAC.01091-13","article-title":"Preclinical characterization of GLS4, an inhibitor of hepatitis B virus core particle assembly","volume":"57","author":"Wu","year":"2013","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_309","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/S0166-3542(01)00216-9","article-title":"Inhibition of human hepatitis B virus (HBV) by a novel non-nucleosidic compound in a transgenic mouse model","volume":"54","author":"Weber","year":"2002","journal-title":"Antivir. Res."},{"key":"ref_310","doi-asserted-by":"crossref","unstructured":"Brezillon, N., Brunelle, M.N., Massinet, H., Giang, E., Lamant, C., DaSilva, L., Berissi, S., Belghiti, J., Hannoun, L., and Puerstinger, G. (2011). Antiviral activity of Bay 41-4109 on hepatitis B virus in humanized Alb-uPA\/SCID mice. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0025096"},{"key":"ref_311","doi-asserted-by":"crossref","first-page":"2687","DOI":"10.1016\/S0960-894X(00)00544-8","article-title":"Phenylpropenamide derivatives as inhibitors of hepatitis B virus replication","volume":"10","author":"Perni","year":"2000","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_312","doi-asserted-by":"crossref","first-page":"3179","DOI":"10.1128\/AAC.42.12.3179","article-title":"Inhibition of human hepatitis B virus replication by AT-61, a phenylpropenamide derivative, alone and in combination with (-)beta-L-2\u2032,3\u2032-dideoxy-3\u2032-thiacytidine","volume":"42","author":"King","year":"1998","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_313","doi-asserted-by":"crossref","first-page":"3057","DOI":"10.1128\/AAC.46.9.3057-3060.2002","article-title":"Phenylpropenamide derivatives AT-61 and AT-130 inhibit replication of wild-type and lamivudine-resistant strains of hepatitis B virus in vitro","volume":"46","author":"Delaney","year":"2002","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_314","doi-asserted-by":"crossref","first-page":"6931","DOI":"10.1128\/JVI.00582-13","article-title":"Sulfamoylbenzamide derivatives inhibit the assembly of hepatitis B virus nucleocapsids","volume":"87","author":"Campagna","year":"2013","journal-title":"J. Virol."},{"key":"ref_315","doi-asserted-by":"crossref","unstructured":"Berke, J.M., Dehertogh, P., Vergauwen, K., Van Damme, E., Mostmans, W., Vandyck, K., and Pauwels, F. (2017). Capsid Assembly Modulators Have a Dual Mechanism of Action in Primary Human Hepatocytes Infected with Hepatitis B Virus. Antimicrob. Agents Chemother., 61.","DOI":"10.1128\/AAC.00560-17"},{"key":"ref_316","doi-asserted-by":"crossref","unstructured":"Guo, F., Zhao, Q., Sheraz, M., Cheng, J., Qi, Y., Su, Q., Cuconati, A., Wei, L., Du, Y., and Li, W. (2017). HBV core protein allosteric modulators differentially alter cccDNA biosynthesis from de novo infection and intracellular amplification pathways. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006658"},{"key":"ref_317","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/s11901-020-00534-w","article-title":"Targeting Viral cccDNA for Cure of Chronic Hepatitis, B","volume":"19","author":"Ligat","year":"2020","journal-title":"Curr. Hepatol. Rep."},{"key":"ref_318","doi-asserted-by":"crossref","first-page":"104787","DOI":"10.1016\/j.antiviral.2020.104787","article-title":"The FDA-approved drug ivermectin inhibits the replication of SARS-CoV-2 in vitro","volume":"178","author":"Caly","year":"2020","journal-title":"Antivir. Res."},{"key":"ref_319","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.antiviral.2015.12.012","article-title":"Discovery of berberine, abamectin and ivermectin as antivirals against chikungunya and other alphaviruses","volume":"126","author":"Varghese","year":"2016","journal-title":"Antivir. Res."},{"key":"ref_320","doi-asserted-by":"crossref","unstructured":"King, C.R., Tessier, T.M., Dodge, M.J., Weinberg, J.B., and Mymryk, J.S. (2020). Inhibition of Human Adenovirus Replication by the Importin \u03b1\/\u03b21 Nuclear Import Inhibitor Ivermectin. J. Virol., 94.","DOI":"10.1128\/JVI.00710-20"},{"key":"ref_321","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.virol.2014.10.013","article-title":"Role of a nuclear localization signal on the minor capsid proteins VP2 and VP3 in BKPyV nuclear entry","volume":"474","author":"Bennett","year":"2015","journal-title":"Virology"},{"key":"ref_322","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1186\/s13578-021-00568-7","article-title":"Characterization of SARS-CoV-2 proteins reveals Orf6 pathogenicity, subcellular localization, host interactions and attenuation by Selinexor","volume":"11","author":"Lee","year":"2021","journal-title":"Cell Biosci."},{"key":"ref_323","doi-asserted-by":"crossref","first-page":"10228","DOI":"10.1128\/JVI.01774-14","article-title":"Verdinexor, a novel selective inhibitor of nuclear export, reduces influenza a virus replication in vitro and in vivo","volume":"88","author":"Perwitasari","year":"2014","journal-title":"J. Virol."},{"key":"ref_324","doi-asserted-by":"crossref","unstructured":"Perwitasari, O., Johnson, S., Yan, X., Register, E., Crabtree, J., Gabbard, J., Howerth, E., Shacham, S., Carlson, R., and Tamir, S. (2016). Antiviral Efficacy of Verdinexor In Vivo in Two Animal Models of Influenza A Virus Infection. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0167221"},{"key":"ref_325","doi-asserted-by":"crossref","first-page":"1426","DOI":"10.1001\/jama.2021.3071","article-title":"Effect of ivermectin on time to resolution of symptoms among adults with mild COVID-19: A randomized clinical trial","volume":"325","author":"Hurtado","year":"2021","journal-title":"JAMA"},{"key":"ref_326","doi-asserted-by":"crossref","first-page":"3176","DOI":"10.1002\/jmv.26880","article-title":"Effect of a combination of nitazoxanide, ribavirin, and ivermectin plus zinc supplement (MANS.NRIZ study) on the clearance of mild COVID-19","volume":"93","author":"Elalfy","year":"2021","journal-title":"J. Med. Virol."},{"key":"ref_327","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.ijid.2020.11.191","article-title":"A five-day course of ivermectin for the treatment of COVID-19 may reduce the duration of illness","volume":"103","author":"Ahmed","year":"2021","journal-title":"Int. J. Infect. Dis."},{"key":"ref_328","doi-asserted-by":"crossref","first-page":"1757","DOI":"10.1056\/NEJMcp2009249","article-title":"Mild or Moderate Covid-19","volume":"383","author":"Gandhi","year":"2020","journal-title":"N. Engl. J. Med."},{"key":"ref_329","doi-asserted-by":"crossref","unstructured":"Suputtamongkol, Y., Avirutnan, P., Mairiang, D., Angkasekwinai, N., Niwattayakul, K., Yamasmith, E., Saleh-Arong, F.A., Songjaeng, A., Prommool, T., and Tangthawornchaikul, N. (2021). Ivermectin accelerates circulating nonstructural protein 1 (NS1) clearance in adult dengue patients: A combined phase 2\/3 randomized double-blinded placebo controlled trial. Clin. Infect. Dis.","DOI":"10.1093\/cid\/ciaa1332"},{"key":"ref_330","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1086\/343813","article-title":"High circulating levels of the dengue virus nonstructural protein NS1 early in dengue illness correlate with the development of dengue hemorrhagic fever","volume":"186","author":"Libraty","year":"2002","journal-title":"J. Infect. Dis."},{"key":"ref_331","doi-asserted-by":"crossref","first-page":"2712","DOI":"10.1002\/ijc.32344","article-title":"REBACIN\u00ae as a noninvasive clinical intervention for high-risk human papillomavirus persistent infection","volume":"145","author":"Yang","year":"2019","journal-title":"Int. J. Cancer"},{"key":"ref_332","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1002\/ijgo.13385","article-title":"REBACIN\u00ae is an optional intervention for persistent high-risk human papillomavirus infection: A retrospective analysis of 364 patients","volume":"152","author":"Yang","year":"2021","journal-title":"Int. J. Gynaecol. Obstet."},{"key":"ref_333","doi-asserted-by":"crossref","first-page":"1392","DOI":"10.1053\/j.gastro.2018.12.023","article-title":"Antiviral Activity, Safety, and Pharmacokinetics of Capsid Assembly Modulator NVR 3-778 in Patients with Chronic HBV Infection","volume":"156","author":"Yuen","year":"2019","journal-title":"Gastroenterology"},{"key":"ref_334","doi-asserted-by":"crossref","unstructured":"Zhang, H., Wang, F., Zhu, X., Chen, Y., Chen, H., Li, X., Wu, M., Li, C., Liu, J., and Zhang, Y. (2020). Antiviral Activity and Pharmacokinetics of the HBV Capsid Assembly Modulator GLS4 in Patients with Chronic HBV Infection. Clin. Infect. Dis.","DOI":"10.1093\/cid\/ciaa961"},{"key":"ref_335","doi-asserted-by":"crossref","first-page":"100720","DOI":"10.1016\/j.eclinm.2020.100720","article-title":"The effect of early treatment with ivermectin on viral load, symptoms and humoral response in patients with non-severe COVID-19: A pilot, double-blind, placebo-controlled, randomized clinical trial","volume":"32","author":"Chaccour","year":"2021","journal-title":"EClinicalMedicine"},{"key":"ref_336","doi-asserted-by":"crossref","first-page":"5567","DOI":"10.1021\/acsnano.7b00906","article-title":"High-speed atomic force microscopy reveals loss of nuclear pore resilience as a dying code in colorectal cancer cells","volume":"11","author":"Mohamed","year":"2017","journal-title":"ACS Nano"},{"key":"ref_337","doi-asserted-by":"crossref","first-page":"3837","DOI":"10.1021\/acs.jpclett.1c00697","article-title":"High-speed atomic force microscopy reveals spatiotemporal dynamics of histone protein H2A involution by DNA inchworming","volume":"12","author":"Nishide","year":"2021","journal-title":"J. Phys. Chem. Lett."},{"key":"ref_338","doi-asserted-by":"crossref","first-page":"6320","DOI":"10.1021\/acs.nanolett.0c01755","article-title":"High-Speed AFM reveals molecular dynamics of human influenza A hemagglutinin and its interaction with exosomes","volume":"20","author":"Lim","year":"2020","journal-title":"Nano Lett."},{"key":"ref_339","doi-asserted-by":"crossref","first-page":"129313","DOI":"10.1016\/j.bbagen.2019.02.015","article-title":"Direct visualization of avian influenza H5N1 hemagglutinin precursor and its conformational change by high-speed atomic force microscopy","volume":"1864","author":"Lim","year":"2020","journal-title":"Biochim. Biophys. Acta. Gen. 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