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Res."},{"key":"10.1016\/j.ejmech.2023.116069_bib189","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1177\/135965350501000503","article-title":"A randomized, double-blind, placebo-controlled dose-escalation trial of merimepodib (VX-497) and interferon-alpha in previously untreated patients with chronic hepatitis C","volume":"10","author":"McHutchison","year":"2005","journal-title":"Antivir. 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Virol."},{"key":"10.1016\/j.ejmech.2023.116069_bib249","doi-asserted-by":"crossref","first-page":"7713","DOI":"10.1128\/JVI.77.14.7713-7719.2003","article-title":"Activation and inhibition of cellular calcium and tyrosine kinase signaling pathways identify targets of the HBx protein involved in hepatitis B virus replication","volume":"77","author":"Bouchard","year":"2003","journal-title":"J. Virol."},{"key":"10.1016\/j.ejmech.2023.116069_bib250","doi-asserted-by":"crossref","first-page":"2976","DOI":"10.1128\/AAC.00310-06","article-title":"NIM811, a cyclophilin inhibitor, exhibits potent in vitro activity against hepatitis C virus alone or in combination with alpha interferon","volume":"50","author":"Ma","year":"2006","journal-title":"Antimicrob. 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Hepatol."},{"key":"10.1016\/j.ejmech.2023.116069_bib255","doi-asserted-by":"crossref","first-page":"1922","DOI":"10.1073\/pnas.1610197114","article-title":"Quantifying antiviral activity optimizes drug combinations against hepatitis C virus infection","volume":"114","author":"Koizumi","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ejmech.2023.116069_bib256","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0152036","article-title":"Characterization of the anti-HCV activities of the new cyclophilin inhibitor STG-175","volume":"11","author":"Gallay","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.ejmech.2023.116069_bib257","doi-asserted-by":"crossref","first-page":"7165","DOI":"10.4049\/jimmunol.166.12.7165","article-title":"Sanglifehrin A, a novel cyclophilin-binding compound showing immunosuppressive activity with a new mechanism of action","volume":"166","author":"Zenke","year":"2001","journal-title":"J. Immunol."},{"key":"10.1016\/j.ejmech.2023.116069_bib258","doi-asserted-by":"crossref","first-page":"1975","DOI":"10.1128\/AAC.01627-10","article-title":"Preclinical characterization of naturally occurring polyketide cyclophilin inhibitors from the sanglifehrin family","volume":"55","author":"Gregory","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2023.116069_bib259","doi-asserted-by":"crossref","first-page":"3849","DOI":"10.1021\/ja021327y","article-title":"Sanglifehrin-cyclophilin interaction: degradation work, synthetic macrocyclic analogues, X-ray crystal structure, and binding data","volume":"125","author":"Sedrani","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2023.116069_bib260","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.virol.2009.10.043","article-title":"Multiple cyclophilins involved in different cellular pathways mediate HCV replication","volume":"397","author":"Gaither","year":"2010","journal-title":"Virology"},{"key":"10.1016\/j.ejmech.2023.116069_bib261","doi-asserted-by":"crossref","first-page":"5829","DOI":"10.1128\/JVI.02524-06","article-title":"Characterization of hepatitis C virus subgenomic replicon resistance to cyclosporine in vitro","volume":"81","author":"Robida","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.ejmech.2023.116069_bib262","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/j.chembiol.2014.10.023","article-title":"Bioengineering and semisynthesis of an optimized cyclophilin inhibitor for treatment of chronic viral infection","volume":"22","author":"Hansson","year":"2015","journal-title":"Chem. Biol."},{"key":"10.1016\/j.ejmech.2023.116069_bib263","doi-asserted-by":"crossref","first-page":"9473","DOI":"10.1021\/acs.jmedchem.8b00802","article-title":"Discovery of a potent and orally bioavailable cyclophilin inhibitor derived from the sanglifehrin macrocycle","volume":"61","author":"Mackman","year":"2018","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.116069_bib264","doi-asserted-by":"crossref","first-page":"9546","DOI":"10.1021\/acs.jmedchem.5b01064","article-title":"Structure-based discovery of novel cyclophilin A inhibitors for the treatment of hepatitis C virus infections","volume":"58","author":"Yang","year":"2015","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.116069_bib265","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2019.112031","article-title":"Molecular design, synthesis, and biological evaluation of bisamide derivatives as cyclophilin A inhibitors for HCV treatment","volume":"188","author":"Han","year":"2020","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.116069_bib266","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms12777","article-title":"Fragment-based discovery of a new family of non-peptidic small-molecule cyclophilin inhibitors with potent antiviral activities","volume":"7","author":"Ahmed-Belkacem","year":"2016","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ejmech.2023.116069_bib267","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.antiviral.2017.12.010","article-title":"Broad-spectrum antiviral activity of the eIF4A inhibitor silvestrol against corona- and picornaviruses","volume":"150","author":"M\u00fcller","year":"2018","journal-title":"Antivir. Res."},{"key":"10.1016\/j.ejmech.2023.116069_bib268","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.112653","article-title":"Flavaglines as natural products targeting eIF4A and prohibitins: from traditional Chinese medicine to antiviral activity against coronaviruses","volume":"203","author":"Nebigil","year":"2020","journal-title":"Eur. J. Med. 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Biol."},{"key":"10.1016\/j.ejmech.2023.116069_bib271","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1016\/j.chembiol.2006.10.005","article-title":"RNA-mediated sequestration of the RNA helicase eIF4A by Pateamine A inhibits translation initiation","volume":"13","author":"Bordeleau","year":"2006","journal-title":"Chem. Biol."},{"key":"10.1016\/j.ejmech.2023.116069_bib272","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1008250","article-title":"Norovirus infection results in eIF2\u03b1 independent host translation shut-off and remodels the G3BP1 interactome evading stress granule formation","volume":"16","author":"Brocard","year":"2020","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.ejmech.2023.116069_bib273","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/j.bcp.2010.12.025","article-title":"Effects of hippuristanol, an inhibitor of eIF4A, on adult T-cell leukemia","volume":"81","author":"Tsumuraya","year":"2011","journal-title":"Biochem. 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