{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T03:28:58Z","timestamp":1787887738367,"version":"build-2784847793"},"reference-count":76,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2021,2,18]],"date-time":"2021-02-18T00:00:00Z","timestamp":1613606400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100002854","name":"ESF","doi-asserted-by":"publisher","award":["POWR.03.02.00-00-I028\/17-00"],"award-info":[{"award-number":["POWR.03.02.00-00-I028\/17-00"]}],"id":[{"id":"10.13039\/100002854","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004281","name":"Narodowe Centrum Nauki","doi-asserted-by":"publisher","award":["2016\/23\/B\/NZ6\/02536"],"award-info":[{"award-number":["2016\/23\/B\/NZ6\/02536"]}],"id":[{"id":"10.13039\/501100004281","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Adenovirus infections tend to be mild, but they may pose a serious threat for young and immunocompromised individuals. The treatment is complicated because there are no approved safe and specific drugs for adenovirus infections. Here, we present evidence that 17-(Allylamino)-17-demethoxygeldanamycin (17-AAG), an inhibitor of Hsp90 chaperone, decreases the rate of human adenovirus 5 (HAdV-5) replication in cell cultures by 95%. 17-AAG inhibited the transcription of early and late genes of HAdV-5, replication of viral DNA, and expression of viral proteins. 6 h after infection, Hsp90 inhibition results in a 6.3-fold reduction of the newly synthesized E1A protein level without a decrease in the E1A mRNA level. However, the Hsp90 inhibition does not increase the decay rate of the E1A protein that was constitutively expressed in the cell before exposure to the inhibitor. The co-immunoprecipitation proved that E1A protein interacted with Hsp90. Altogether, the presented results show, for the first time. that Hsp90 chaperones newly synthesized, but not mature, E1A protein. Because E1A serves as a transcriptional co-activator of adenovirus early genes, the anti-adenoviral activity of the Hsp90 inhibitor might be explained by the decreased E1A level.<\/jats:p>","DOI":"10.3390\/ijms22042020","type":"journal-article","created":{"date-parts":[[2021,2,18]],"date-time":"2021-02-18T20:56:21Z","timestamp":1613681781000},"page":"2020","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Heat Shock Protein 90 Chaperones E1A Early Protein of Adenovirus 5 and Is Essential for Replication of the Virus"],"prefix":"10.3390","volume":"22","author":[{"given":"Iga","family":"Dalidowska","sequence":"first","affiliation":[{"name":"Department of Experimental Pharmacology, Mossakowski Medical Research Institute, Polish Academy of Sciences, Pawinskiego 5, 02-106 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olga","family":"Gazi","sequence":"additional","affiliation":[{"name":"Chair and Department of Medical Microbiology, Medical University of Warsaw, 02-091 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1697-8164","authenticated-orcid":false,"given":"Dorota","family":"Sulejczak","sequence":"additional","affiliation":[{"name":"Department of Experimental Pharmacology, Mossakowski Medical Research Institute, Polish Academy of Sciences, Pawinskiego 5, 02-106 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maciej","family":"Przybylski","sequence":"additional","affiliation":[{"name":"Chair and Department of Medical Microbiology, Medical University of Warsaw, 02-091 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1169-4517","authenticated-orcid":false,"given":"Pawel","family":"Bieganowski","sequence":"additional","affiliation":[{"name":"Department of Experimental Pharmacology, Mossakowski Medical Research Institute, Polish Academy of Sciences, Pawinskiego 5, 02-106 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,2,18]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1016\/j.bbamcr.2011.08.013","article-title":"Approaches for defining the Hsp90-dependent proteome","volume":"1823","author":"Hartson","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_2","first-page":"2802","article-title":"Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies","volume":"4","author":"Lai","year":"1984","journal-title":"Mol. Cell Biol."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Echeverria, P.C., Bernthaler, A., Dupuis, P., Mayer, B., and Picard, D. (2011). An interaction network predicted from public data as a discovery tool: Application to the Hsp90 molecular chaperone machine. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0026044"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1007\/s002800050817","article-title":"The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin","volume":"42","author":"Schulte","year":"1998","journal-title":"Cancer Chemother Pharm."},{"key":"ref_5","first-page":"48","article-title":"Heat shock protein 90 targeting therapy: State of the art and future perspective","volume":"14","author":"Tatokoro","year":"2015","journal-title":"EXCLI J."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"253","DOI":"10.2174\/1568009619666191202101330","article-title":"Old and New Approaches to Target the Hsp90 Chaperone","volume":"20","author":"Sanchez","year":"2020","journal-title":"Curr. Cancer Drug Targets"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"3269","DOI":"10.1007\/s00705-017-3511-1","article-title":"HSP90: A promising broad-spectrum antiviral drug target","volume":"162","author":"Wang","year":"2017","journal-title":"Arch. Virol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1016\/j.bbamcr.2011.11.007","article-title":"Broad action of Hsp90 as a host chaperone required for viral replication","volume":"1823","author":"Geller","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"13122","DOI":"10.1128\/JVI.78.23.13122-13131.2004","article-title":"Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function","volume":"78","author":"Hu","year":"2004","journal-title":"J. Virol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"10126","DOI":"10.1128\/JVI.01671-13","article-title":"Hsp90 inhibitor 17-DMAG decreases expression of conserved herpesvirus protein kinases and reduces virus production in Epstein-Barr virus-infected cells","volume":"87","author":"Sun","year":"2013","journal-title":"J. Virol."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Tsou, Y.L., Lin, Y.W., Chang, H.W., Lin, H.Y., Shao, H.Y., Yu, S.L., Liu, C.C., Chitra, E., Sia, C., and Chow, Y.H. (2013). Heat shock protein 90: Role in enterovirus 71 entry and assembly and potential target for therapy. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0077133"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Bukong, T.N., Momen-Heravi, F., Kodys, K., Bala, S., and Szabo, G. (2014). Exosomes from hepatitis C infected patients transmit HCV infection and contain replication competent viral RNA in complex with Ago2-miR122-HSP90. PLoS Pathog., 10.","DOI":"10.1371\/journal.ppat.1004424"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2892","DOI":"10.1016\/j.bbrc.2018.08.065","article-title":"Heat shock protein 70 and heat shock protein 90 synergistically increase hepatitis B viral capsid assembly","volume":"503","author":"Seo","year":"2018","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"10740","DOI":"10.1128\/JVI.79.16.10740-10749.2005","article-title":"Herpes simplex virus type 1 DNA polymerase requires the mammalian chaperone hsp90 for proper localization to the nucleus","volume":"79","author":"Burch","year":"2005","journal-title":"J. Virol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"13640","DOI":"10.1128\/JVI.02006-13","article-title":"HSP90 protects the human T-cell leukemia virus type 1 (HTLV-1) tax oncoprotein from proteasomal degradation to support NF-kappaB activation and HTLV-1 replication","volume":"87","author":"Gao","year":"2013","journal-title":"J. Virol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"15227","DOI":"10.1074\/jbc.273.24.15227","article-title":"Active participation of Hsp90 in the biogenesis of the trimeric reovirus cell attachment protein sigma1","volume":"273","author":"Gilmore","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1038\/s41598-018-37249-4","article-title":"Molecular Evolution of Human Adenovirus (HAdV) Species C","volume":"9","author":"Dhingra","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_18","first-page":"195","article-title":"Adenovirus","volume":"343","author":"Smith","year":"2010","journal-title":"Curr. Top Microbiol. Immunol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1812","DOI":"10.1038\/srep01812","article-title":"Molecular evolution of human adenoviruses","volume":"3","author":"Robinson","year":"2013","journal-title":"Sci. Rep."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1128\/CMR.00052-07","article-title":"Adenoviruses in immunocompromised hosts","volume":"21","author":"Echavarria","year":"2008","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1128\/CMR.00116-13","article-title":"Adenovirus infections in immunocompetent and immunocompromised patients","volume":"27","author":"Lion","year":"2014","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"8834","DOI":"10.1128\/JVI.76.17.8834-8841.2002","article-title":"Adenovirus type 37 uses sialic acid as a cellular receptor on Chang C cells","volume":"76","author":"Arnberg","year":"2002","journal-title":"J. Virol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"7909","DOI":"10.1128\/JVI.72.10.7909-7915.1998","article-title":"The coxsackievirus-adenovirus receptor protein can function as a cellular attachment protein for adenovirus serotypes from subgroups A, C, D, E, and F","volume":"72","author":"Roelvink","year":"1998","journal-title":"J. Virol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1320","DOI":"10.1126\/science.275.5304.1320","article-title":"Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5","volume":"275","author":"Bergelson","year":"1997","journal-title":"Science"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1408","DOI":"10.1038\/nm952","article-title":"CD46 is a cellular receptor for group B adenoviruses","volume":"9","author":"Gaggar","year":"2003","journal-title":"Nat. Med."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/0092-8674(93)90231-E","article-title":"Integrins alpha v beta 3 and alpha v beta 5 promote adenovirus internalization but not virus attachment","volume":"73","author":"Wickham","year":"1993","journal-title":"Cell"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1128\/jvi.55.2.442-449.1985","article-title":"Role of vesicles during adenovirus 2 internalization into HeLa cells","volume":"55","author":"Svensson","year":"1985","journal-title":"J. Virol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1016\/0092-8674(93)90382-Z","article-title":"Stepwise dismantling of adenovirus 2 during entry into cells","volume":"75","author":"Greber","year":"1993","journal-title":"Cell"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1016\/0022-2836(78)90048-7","article-title":"Regulation of the appearance of cytoplasmic RNAs from region 1 of the adenovirus 2 genome","volume":"126","author":"Spector","year":"1978","journal-title":"J. Mol. Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1139\/o88-068","article-title":"Transactivation by the adenovirus E1A gene","volume":"66","author":"Nevins","year":"1988","journal-title":"Biochem. Cell Biol."},{"key":"ref_31","first-page":"187","article-title":"Adenovirus DNA replication: Protein priming, jumping back and the role of the DNA binding protein DBP","volume":"272","author":"Brenkman","year":"2003","journal-title":"Curr. Top Microbiol. Immunol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"13492","DOI":"10.1016\/S0021-9258(18)33474-4","article-title":"DNA sequence analysis of the region encoding the terminal protein and the hypothetical N-gene product of adenovirus type 2","volume":"257","author":"Alestrom","year":"1982","journal-title":"J. Biol. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"6725","DOI":"10.1073\/pnas.1603872113","article-title":"The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1gamma sumoylation and poly-SUMO chain elongation","volume":"113","author":"Sohn","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.2741\/1604","article-title":"Functions of the adenovirus E4 proteins and their impact on viral vectors","volume":"10","author":"Weitzman","year":"2005","journal-title":"Front. Biosci."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"7836","DOI":"10.1038\/sj.onc.1204861","article-title":"Regulation of the cell cycle and apoptosis by the oncogenes of adenovirus","volume":"20","author":"White","year":"2001","journal-title":"Oncogene"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1080\/08830180490265556","article-title":"Functions and mechanisms of action of the adenovirus E3 proteins","volume":"23","author":"Lichtenstein","year":"2004","journal-title":"Int. Rev. Immunol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"7096","DOI":"10.1128\/JVI.00107-10","article-title":"Adenovirus late-phase infection is controlled by a novel L4 promoter","volume":"84","author":"Morris","year":"2010","journal-title":"J. Virol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"5006","DOI":"10.2741\/3059","article-title":"Temporal regulation of adenovirus major late alternative RNA splicing","volume":"13","author":"Akusjarvi","year":"2008","journal-title":"Front. Biosci."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1128\/JVI.01675-13","article-title":"Adenovirus death protein (ADP) is required for lytic infection of human lymphocytes","volume":"88","author":"Murali","year":"2014","journal-title":"J. Virol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2296","DOI":"10.1128\/jvi.70.4.2296-2306.1996","article-title":"The adenovirus death protein (E3-11.6K) is required at very late stages of infection for efficient cell lysis and release of adenovirus from infected cells","volume":"70","author":"Tollefson","year":"1996","journal-title":"J. Virol."},{"key":"ref_41","first-page":"2884","article-title":"Selective induction of human heat shock gene transcription by the adenovirus E1A gene products, including the 12S E1A product","volume":"7","author":"Simon","year":"1987","journal-title":"Mol. Cell. Biol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/0042-6822(91)90015-4","article-title":"Association of HSP70 with the adenovirus type 5 fiber protein in infected HEp-2 cells","volume":"180","author":"Macejak","year":"1991","journal-title":"Virology"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1016\/0014-4827(92)90290-O","article-title":"Adenovirus capsid proteins interact with HSP70 proteins after penetration in human or rodent cells","volume":"201","author":"Niewiarowska","year":"1992","journal-title":"Exp. Cell. Res."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1006\/viro.1997.8597","article-title":"Cloning and sequencing of the cellular-viral junctions from the human adenovirus type 5 transformed 293 cell line","volume":"233","author":"Louis","year":"1997","journal-title":"Virology"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"2027","DOI":"10.1002\/j.1460-2075.1987.tb02467.x","article-title":"Differential splicing yields novel adenovirus 5 E1A mRNAs that encode 30 kd and 35 kd proteins","volume":"6","author":"Stephens","year":"1987","journal-title":"EMBO J."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"4308","DOI":"10.1038\/s41598-018-22639-5","article-title":"Hsp90 interacts with multiple dengue virus 2 proteins","volume":"8","author":"Srisutthisamphan","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.virusres.2016.08.009","article-title":"Heat shock protein 90 is essential for replication of porcine circovirus type 2 in PK-15 cells","volume":"224","author":"Liu","year":"2016","journal-title":"Virus Res."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Mohl, B.P., and Roy, P. (2019). Hsp90 Chaperones Bluetongue Virus Proteins and Prevents Proteasomal Degradation. J. Virol., 93.","DOI":"10.1128\/JVI.00898-19"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"27123","DOI":"10.1038\/srep27123","article-title":"The co-chaperone Cdc37 regulates the rabies virus phosphoprotein stability by targeting to Hsp90AA1 machinery","volume":"6","author":"Xu","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.virol.2010.11.005","article-title":"Heat shock protein 90 facilitates formation of the HBV capsid via interacting with the HBV core protein dimers","volume":"410","author":"Shim","year":"2011","journal-title":"Virology"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"26130","DOI":"10.18632\/oncotarget.25452","article-title":"Heat shock protein 90 inhibitors augment endogenous wild-type p53 expression but down-regulate the adenovirally-induced expression by inhibiting a proteasome activity","volume":"9","author":"Chai","year":"2018","journal-title":"Oncotarget"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1016\/0092-8674(79)90333-7","article-title":"Pre-early adenovirus 5 gene product regulates synthesis of early viral messenger RNAs","volume":"17","author":"Berk","year":"1979","journal-title":"Cell"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/0092-8674(80)90138-5","article-title":"Control of adenovirus early gene expression: A class of immediate early products","volume":"21","author":"Lewis","year":"1980","journal-title":"Cell"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.antiviral.2018.09.011","article-title":"Inhibition of adenovirus infection by mifepristone","volume":"159","author":"Bunuales","year":"2018","journal-title":"Antiviral. Res."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1038\/s41598-018-37290-3","article-title":"Repositioning salicylanilide anthelmintic drugs to treat adenovirus infections","volume":"9","author":"Pachon","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1016\/S0042-6822(03)00431-8","article-title":"DNA synthesis-dependent relief of repression of transcription from the adenovirus type 2 IVa(2) promoter by a cellular protein","volume":"314","author":"Huang","year":"2003","journal-title":"Virology"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1782","DOI":"10.1128\/JVI.78.4.1782-1791.2004","article-title":"Activation of the early-late switch in adenovirus type 5 major late transcription unit expression by L4 gene products","volume":"78","author":"Farley","year":"2004","journal-title":"J. Virol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"3049","DOI":"10.1128\/JVI.02455-08","article-title":"Adenovirus serotype 5 L4-22K and L4-33K proteins have distinct functions in regulating late gene expression","volume":"83","author":"Morris","year":"2009","journal-title":"J. Virol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1146\/annurev.ge.20.120186.000401","article-title":"Adenovirus promoters and E1A transactivation","volume":"20","author":"Berk","year":"1986","journal-title":"Annu. Rev. Genet."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"4067","DOI":"10.1093\/nar\/13.11.4067","article-title":"Cis and trans activation of adenovirus IVa2 gene transcription","volume":"13","author":"Natarajan","year":"1985","journal-title":"Nucleic. Acids. Res."},{"key":"ref_61","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 alpha\/beta1 Nuclear Import Inhibitor Ivermectin. J. Virol., 94.","DOI":"10.1128\/JVI.00710-20"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1177\/095632020501600206","article-title":"Geldanamycin, a potent and specific inhibitor of Hsp90, inhibits gene expression and replication of human cytomegalovirus","volume":"16","author":"Basha","year":"2005","journal-title":"Antivir. Chem. Chemother."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"198200","DOI":"10.1016\/j.virusres.2020.198200","article-title":"Hsp90 function is required for stable transcription of the baculovirus transactivator ie-1 gene","volume":"291","author":"Katsuma","year":"2021","journal-title":"Virus Res."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"161","DOI":"10.3851\/IMP1479","article-title":"Combination therapy for hepatitis C virus with heat-shock protein 90 inhibitor 17-AAG and proteasome inhibitor MG132","volume":"20","author":"Ujino","year":"2010","journal-title":"Antivir. Chem. Chemother."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1128\/JVI.01783-14","article-title":"Interactome analysis of the human respiratory syncytial virus RNA polymerase complex identifies protein chaperones as important cofactors that promote L-protein stability and RNA synthesis","volume":"89","author":"Munday","year":"2015","journal-title":"J. Virol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/j.virol.2008.04.040","article-title":"Hsp90 inhibitors reduce influenza virus replication in cell culture","volume":"377","author":"Chase","year":"2008","journal-title":"Virology"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1007\/s10637-010-9493-4","article-title":"A Phase II trial of 17-allylamino, 17-demethoxygeldanamycin (17-AAG, tanespimycin) in patients with metastatic melanoma","volume":"30","author":"Pacey","year":"2012","journal-title":"Invest New Drugs"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1775","DOI":"10.1158\/1078-0432.CCR-06-1863","article-title":"Phase I trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer","volume":"13","author":"Solit","year":"2007","journal-title":"Clin. Cancer Res."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1016\/j.bbamcr.2010.03.002","article-title":"Mutations that increase both Hsp90 ATPase activity in vitro and Hsp90 drug resistance in vivo","volume":"1803","author":"Zurawska","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Baker, A.T., Aguirre-Hernandez, C., Hallden, G., and Parker, A.L. (2018). Designer Oncolytic Adenovirus: Coming of Age. Cancers (Basel), 10.","DOI":"10.20944\/preprints201805.0273.v1"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"8636","DOI":"10.1002\/jcp.27850","article-title":"Oncolytic adenovirus: A tool for cancer therapy in combination with other therapeutic approaches","volume":"234","author":"Goradel","year":"2019","journal-title":"J. Cell Physiol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1016\/j.urology.2006.04.021","article-title":"Oncolytic viral therapy by bladder instillation using an E1A, E1B double-restricted adenovirus in an orthotopic bladder cancer model","volume":"68","author":"Wang","year":"2006","journal-title":"Urology"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"3571","DOI":"10.1002\/1873-3468.13576","article-title":"Adenovirus persistence, reactivation, and clinical management","volume":"593","author":"Lion","year":"2019","journal-title":"FEBS Lett."},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Pennington, M.R., Saha, A., Painter, D.F., Gavazzi, C., Ismail, A.M., Zhou, X., Chodosh, J., and Rajaiya, J. (2019). Disparate Entry of Adenoviruses Dictates Differential Innate Immune Responses on the Ocular Surface. Microorganisms, 7.","DOI":"10.3390\/microorganisms7090351"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Kosulin, K. (2019). Intestinal HAdV Infection: Tissue Specificity, Persistence, and Implications for Antiviral Therapy. Viruses, 11.","DOI":"10.3390\/v11090804"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1093\/oxfordjournals.aje.a118408","article-title":"A simple method of estimating fifty per cent endpoints","volume":"27","author":"Reed","year":"1938","journal-title":"Am. J. Epidemiol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/4\/2020\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T05:25:47Z","timestamp":1760160347000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/4\/2020"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,2,18]]},"references-count":76,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2021,2]]}},"alternative-id":["ijms22042020"],"URL":"https:\/\/doi.org\/10.3390\/ijms22042020","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,2,18]]}}}