{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,31]],"date-time":"2025-12-31T18:45:24Z","timestamp":1767206724272,"version":"build-2238731810"},"reference-count":61,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2021,12,6]],"date-time":"2021-12-06T00:00:00Z","timestamp":1638748800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000928","name":"Welch Foundation","doi-asserted-by":"publisher","award":["AH-0033"],"award-info":[{"award-number":["AH-0033"]}],"id":[{"id":"10.13039\/100000928","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001823","name":"Ministry of Education Youth and Sports","doi-asserted-by":"publisher","award":["LTAUSA17061"],"award-info":[{"award-number":["LTAUSA17061"]}],"id":[{"id":"10.13039\/501100001823","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.mdpi.com"],"crossmark-restriction":true},"short-container-title":["Viruses"],"abstract":"<jats:p>Fullerene derivatives with hydrophilic substituents have been shown to exhibit a range of biological activities, including antiviral ones. For a long time, the anti-HIV activity of fullerene derivatives was believed to be due to their binding into the hydrophobic pocket of HIV-1 protease, thereby blocking its activity. Recent work, however, brought new evidence of a novel, protease-independent mechanism of fullerene derivatives\u2019 action. We studied in more detail the mechanism of the anti-HIV-1 activity of N,N-dimethyl[70]fulleropyrrolidinium iodide fullerene derivatives. By using a combination of in vitro and cell-based approaches, we showed that these C70 derivatives inhibited neither HIV-1 protease nor HIV-1 maturation. Instead, our data indicate effects of fullerene C70 derivatives on viral genomic RNA packaging and HIV-1 cDNA synthesis during reverse transcription\u2014without impairing reverse transcriptase activity though. Molecularly, this could be explained by a strong binding affinity of these fullerene derivatives to HIV-1 nucleocapsid domain, preventing its proper interaction with viral genomic RNA, thereby blocking reverse transcription and HIV-1 infectivity. Moreover, the fullerene derivatives\u2019 oxidative activity and fluorescence quenching, which could be one of the reasons for the inconsistency among reported anti-HIV-1 mechanisms, are discussed herein.<\/jats:p>","DOI":"10.3390\/v13122451","type":"journal-article","created":{"date-parts":[[2021,12,7]],"date-time":"2021-12-07T03:21:05Z","timestamp":1638847265000},"page":"2451","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Fullerene Derivatives Prevent Packaging of Viral Genomic RNA into HIV-1 Particles by Binding Nucleocapsid Protein"],"prefix":"10.3390","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0497-4924","authenticated-orcid":false,"given":"Ivana","family":"K\u0159\u00ed\u017eov\u00e1","sequence":"first","affiliation":[{"name":"Department of Biotechnology, University of Chemistry and Technology Prague, Technick\u00e1 5, 166 28 Prague, Czech Republic"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0430-766X","authenticated-orcid":false,"given":"Al\u017eb\u011bta","family":"Dost\u00e1lkov\u00e1","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, University of Chemistry and Technology Prague, Technick\u00e1 5, 166 28 Prague, Czech Republic"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2954-9462","authenticated-orcid":false,"given":"Edison","family":"Castro","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Texas at El Paso, 500 West University, El Paso, TX 79902, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jan","family":"Prchal","sequence":"additional","affiliation":[{"name":"Laboratory of NMR Spectroscopy, University of Chemistry and Technology, 166 28 Prague, Czech Republic"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6255-5579","authenticated-orcid":false,"given":"Romana","family":"Hadravov\u00e1","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, University of Chemistry and Technology Prague, Technick\u00e1 5, 166 28 Prague, Czech Republic"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Filip","family":"Kaufman","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, University of Chemistry and Technology Prague, Technick\u00e1 5, 166 28 Prague, Czech Republic"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5430-5270","authenticated-orcid":false,"given":"Richard","family":"Hrabal","sequence":"additional","affiliation":[{"name":"Laboratory of NMR Spectroscopy, University of Chemistry and Technology, 166 28 Prague, Czech Republic"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5698-4366","authenticated-orcid":false,"given":"Tom\u00e1\u0161","family":"Ruml","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Microbiology, University of Chemistry and Technology Prague, Technick\u00e1 5, 166 28 Prague, Czech Republic"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Manuel","family":"Llano","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, University of Texas at El Paso, 500 West University, El Paso, TX 79902, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Luis","family":"Echegoyen","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Texas at El Paso, 500 West University, El Paso, TX 79902, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5645-8227","authenticated-orcid":false,"given":"Michaela","family":"Rumlov\u00e1","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, University of Chemistry and Technology Prague, Technick\u00e1 5, 166 28 Prague, Czech Republic"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2021,12,6]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1038\/nsmb785","article-title":"The stoichiometry of Gag protein in HIV-1","volume":"11","author":"Briggs","year":"2004","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1038\/35030177","article-title":"Image reconstructions of helical assemblies of the HIV-1 CA protein","volume":"407","author":"Li","year":"2000","journal-title":"Nature"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1038\/nature09640","article-title":"Atomic-level modelling of the HIV capsid","volume":"469","author":"Pornillos","year":"2011","journal-title":"Nature"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1434","DOI":"10.1126\/science.aah4972","article-title":"The structure and flexibility of conical HIV-1 capsids determined within intact virions","volume":"354","author":"Mattei","year":"2016","journal-title":"Science"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1126\/science.283.5398.80","article-title":"Assembly and analysis of conical models for the HIV-1 core","volume":"283","author":"Ganser","year":"1999","journal-title":"Science"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1038\/nrmicro3503","article-title":"HIV-1 capsid: The multifaceted key player in HIV-1 infection","volume":"13","author":"Campbell","year":"2015","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1038\/nature12769","article-title":"HIV-1 evades innate immune recognition through specific cofactor recruitment","volume":"503","author":"Rasaiyaah","year":"2013","journal-title":"Nature"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/j.chom.2018.03.009","article-title":"Single HIV-1 Imaging Reveals Progression of Infection through CA-Dependent Steps of Docking at the Nuclear Pore, Uncoating, and Nuclear Transport","volume":"23","author":"Francis","year":"2018","journal-title":"Cell Host Microbe."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Burdick, R.C., Delviks-Frankenberry, K.A., Chen, J., Janaka, S.K., Sastri, J., Hu, W.S., and Pathak, V.K. (2017). Dynamics and regulation of nuclear import and nuclear movements of HIV-1 complexes. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006570"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"7818","DOI":"10.1128\/JVI.00325-11","article-title":"The requirement for nucleoporin NUP153 during human immunodeficiency virus type 1 infection is determined by the viral capsid","volume":"85","author":"Matreyek","year":"2011","journal-title":"J. Virol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.coviro.2013.11.003","article-title":"A model for cofactor use during HIV-1 reverse transcription and nuclear entry","volume":"4","author":"Hilditch","year":"2014","journal-title":"Curr. Opin. Virol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"9975","DOI":"10.1073\/pnas.1014522108","article-title":"Complementary assays reveal a relationship between HIV-1 uncoating and reverse transcription","volume":"108","author":"Hulme","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"E7169","DOI":"10.1073\/pnas.1706245114","article-title":"Early cytoplasmic uncoating is associated with infectivity of HIV-1","volume":"114","author":"Mamede","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"13613","DOI":"10.1128\/JVI.02219-14","article-title":"HIV-1 uncoating is facilitated by dynein and kinesin 1","volume":"88","author":"Lukic","year":"2014","journal-title":"J. Virol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1128\/JVI.01228-12","article-title":"Inhibition of reverse transcriptase activity increases stability of the HIV-1 core","volume":"87","author":"Yang","year":"2013","journal-title":"J. Virol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1186\/s12977-016-0292-7","article-title":"HIV-1 capsid uncoating initiates after the first strand transfer of reverse transcription","volume":"13","author":"Cosnefroy","year":"2016","journal-title":"Retrovirology"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1007\/s12250-019-00095-3","article-title":"Multiple Roles of HIV-1 Capsid during the Virus Replication Cycle","volume":"34","author":"Novikova","year":"2019","journal-title":"Virologica. Sinica."},{"key":"ref_18","first-page":"53","article-title":"Nucleocapsid Protein: A Desirable Target for Future Therapies Against HIV-1","volume":"389","author":"Mori","year":"2015","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"270","DOI":"10.2174\/1570162X14999160224103555","article-title":"HIV-1 Capsid Inhibitors as Antiretroviral Agents","volume":"14","author":"Valente","year":"2016","journal-title":"Curr. HIV Res."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1016\/j.biotechadv.2017.12.016","article-title":"In vitro methods for testing antiviral drugs","volume":"36","author":"Rumlova","year":"2018","journal-title":"Biotechnol. Adv."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1097\/COH.0000000000000472","article-title":"Inhibitors of the HIV-1 capsid, a target of opportunity","volume":"13","author":"Carnes","year":"2018","journal-title":"Curr. Opin. HIV AIDS"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1038\/318162a0","article-title":"C60: Buckminsterfullerene","volume":"318","author":"Kroto","year":"1985","journal-title":"Nature"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1272\/jnms.79.248","article-title":"Water-soluble fullerene derivatives for drug discovery","volume":"79","author":"Nakamura","year":"2012","journal-title":"J. Nippon Med. Sch."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"6523","DOI":"10.1039\/C7TB00855D","article-title":"Fullerenes in Biology and Medicine","volume":"5","author":"Castro","year":"2017","journal-title":"J. Mater. Chem. B"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"127675","DOI":"10.1016\/j.bmcl.2020.127675","article-title":"Fullerene derivatives as dual inhibitors of HIV-1 reverse transcriptase and protease","volume":"31","author":"Yasuno","year":"2021","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1016\/j.ejmech.2003.09.005","article-title":"Fullerene derivatives: An attractive tool for biological applications","volume":"38","author":"Bosi","year":"2003","journal-title":"Eur. J. Med. Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1016\/j.drudis.2019.01.013","article-title":"Fullerene-based delivery systems","volume":"24","author":"Kazemzadeh","year":"2019","journal-title":"Drug Discov. Today"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1016\/j.bmcl.2004.12.030","article-title":"Human immunodeficiency virus-reverse transcriptase inhibition and hepatitis C virus RNA-dependent RNA polymerase inhibition activities of fullerene derivatives","volume":"15","author":"Mashino","year":"2005","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"4565","DOI":"10.1016\/j.bmcl.2016.08.086","article-title":"Novel fullerene derivatives as dual inhibitors of Hepatitis C virus NS5B polymerase and NS3\/4A protease","volume":"26","author":"Kataoka","year":"2016","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_30","first-page":"50","article-title":"Synthesis of giant globular multivalent glycofullerenes as potent inhibitors in a model of Ebola virus infection","volume":"8","author":"Sigwalt","year":"2015","journal-title":"Nat. Chem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1021\/bm3016658","article-title":"Glycofullerenes Inhibit Viral Infection","volume":"14","author":"Luczkowiak","year":"2013","journal-title":"Biomacromolecules"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"3226","DOI":"10.1016\/j.bmcl.2015.05.086","article-title":"The human immunodeficiency virus-reverse transcriptase inhibition activity of novel pyridine\/pyridinium-type fullerene derivatives","volume":"25","author":"Yasuno","year":"2015","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"6506","DOI":"10.1021\/ja00068a005","article-title":"Inhibition of the Hiv-1 Protease by Fullerene Derivatives-Model-Building Studies and Experimental-Verification","volume":"115","author":"Friedman","year":"1993","journal-title":"J. Am. Chem. Soc."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"6510","DOI":"10.1021\/ja00068a006","article-title":"Synthesis of a Fullerene Derivative for the Inhibition of HIV Enzymes","volume":"115","author":"Sijbesma","year":"1993","journal-title":"J. Am. Chem. Soc."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"5731","DOI":"10.1128\/AAC.00341-16","article-title":"Fullerene Derivatives Strongly Inhibit HIV-1 Replication by Affecting Virus Maturation without Impairing Protease Activity","volume":"60","author":"Martinez","year":"2016","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"10963","DOI":"10.1021\/acs.jmedchem.6b00994","article-title":"Characterization of New Cationic N,N-Dimethyl[70]fulleropyrrolidinium Iodide Derivatives as Potent HIV-1 Maturation Inhibitors","volume":"59","author":"Castro","year":"2016","journal-title":"J. Med. Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"6496","DOI":"10.1021\/jo00125a040","article-title":"1,3-Dipolar Cycloaddition of N-Methylazomethine Ylide to C70","volume":"60","author":"Wilson","year":"1995","journal-title":"J. Org. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"31426","DOI":"10.1021\/acsami.6b10668","article-title":"Improved Performance and Stability of Inverted Planar Perovskite Solar Cells Using Fulleropyrrolidine Layers","volume":"8","author":"Tian","year":"2016","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Dostalkova, A., Skach, K., Kaufman, F., Krizova, I., Hadravova, R., Flegel, M., Ruml, T., Hrabal, R., and Rumlova, M. (2020). PF74 and Its Novel Derivatives Stabilize Hexameric Lattice of HIV-1 Mature-like Particles. Molecules, 25.","DOI":"10.3390\/molecules25081895"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1988","DOI":"10.1128\/JVI.06638-11","article-title":"The G-Patch Domain of Mason-Pfizer Monkey Virus Is a Part of Reverse Transcriptase","volume":"86","author":"Ruml","year":"2012","journal-title":"J. Virol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.virol.2018.06.001","article-title":"Conserved cysteines in Mason-Pfizer monkey virus capsid protein are essential for infectious mature particle formation","volume":"521","author":"Pichalova","year":"2018","journal-title":"Virology"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.virol.2008.07.021","article-title":"The effect of point mutations within the N-terminal domain of Mason-Pfizer monkey virus capsid protein on virus core assembly and infectivity","volume":"380","author":"Wildova","year":"2008","journal-title":"Virology"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"38803","DOI":"10.1074\/jbc.M306967200","article-title":"dUTPase and nucleocapsid polypeptides of the Mason-Pfizer monkey virus form a fusion protein in the virion with homotrimeric organization and low catalytic efficiency","volume":"278","author":"Erdei","year":"2003","journal-title":"J. Bio. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1007\/978-1-59745-170-3_5","article-title":"Real-time PCR analysis of HIV-1 replication post-entry events","volume":"485","author":"Mbisa","year":"2009","journal-title":"Methods Mol. Biol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"e00106-18","DOI":"10.1128\/JVI.00106-18","article-title":"Mutations in the basic region of the Mason-Pfizer monkey virus nucleocapsid protein affect reverse transcription, gRNA packaging and the site of viral assembly","volume":"92","author":"Dostalkova","year":"2018","journal-title":"J. Virol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1007\/978-1-62703-670-2_4","article-title":"The cyclosporin A washout assay to detect HIV-1 uncoating in infected cells","volume":"1087","author":"Hulme","year":"2014","journal-title":"Methods Mol. Biol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"4593","DOI":"10.1128\/JVI.03197-15","article-title":"Nucleic Acid Binding by Mason-Pfizer Monkey Virus CA Promotes Virus Assembly and Genome Packaging","volume":"90","author":"Fuzik","year":"2016","journal-title":"J. Virol."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Korb, O., St\u00fctzle, T., and Exner, T.E. (2006, January 4\u20137). PLANTS: Application of Ant Colony Optimization to Structure-Based Drug Design. Proceedings of the Ant Colony Optimization and Swarm Intelligence, Berlin, Heidelberg.","DOI":"10.1007\/11839088_22"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J. Comput. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1177\/095632020801900301","article-title":"Bevirimat: A novel maturation inhibitor for the treatment of HIV-1 infection","volume":"19","author":"Martin","year":"2008","journal-title":"Antivir. Chem. Chemother"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1186\/1742-4690-11-37","article-title":"HIV-1 protease-induced apoptosis","volume":"11","author":"Rumlova","year":"2014","journal-title":"Retrovirology"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.virol.2015.08.029","article-title":"FAITH-Fast Assembly Inhibitor Test for HIV","volume":"486","author":"Hadravova","year":"2015","journal-title":"Virology"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"17076","DOI":"10.1038\/s41598-019-53483-w","article-title":"A simple, high-throughput stabilization assay to test HIV-1 uncoating inhibitors","volume":"9","author":"Dostalkova","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/nsmb964","article-title":"A peptide inhibitor of HIV-1 assembly in vitro","volume":"12","author":"Sticht","year":"2005","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"5667","DOI":"10.1128\/JVI.76.11.5667-5677.2002","article-title":"Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication","volume":"76","author":"Forshey","year":"2002","journal-title":"J. Virol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1128\/JVI.03043-14","article-title":"Identification of Capsid Mutations That Alter the Rate of HIV-1 Uncoating in Infected Cells","volume":"89","author":"Hulme","year":"2015","journal-title":"J. Virol."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Blair, W.S., Pickford, C., Irving, S.L., Brown, D.G., Anderson, M., Bazin, R., Cao, J., Ciaramella, G., Isaacson, J., and Jackson, L. (2010). HIV capsid is a tractable target for small molecule therapeutic intervention. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1001220"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1128\/JVI.01406-10","article-title":"Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization","volume":"85","author":"Shi","year":"2011","journal-title":"J. Virol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"e00845-18","DOI":"10.1128\/JVI.00845-18","article-title":"PF74 Reinforces the HIV-1 Capsid to Impair Reverse Transcription-Induced Uncoating","volume":"92","author":"Rankovic","year":"2018","journal-title":"J. Virol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1006\/jmbi.2000.3979","article-title":"NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the psi-RNA packaging signal. Implications for genome recognition","volume":"301","author":"Amarasinghe","year":"2000","journal-title":"J. Mol. Biol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1126\/science.279.5349.384","article-title":"Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element","volume":"279","author":"Wu","year":"1998","journal-title":"Science"}],"updated-by":[{"DOI":"10.3390\/v14061187","type":"correction","label":"Correction","source":"publisher","updated":{"date-parts":[[2021,12,6]],"date-time":"2021-12-06T00:00:00Z","timestamp":1638748800000}}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/13\/12\/2451\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,8,3]],"date-time":"2025-08-03T22:19:18Z","timestamp":1754259558000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/13\/12\/2451"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,12,6]]},"references-count":61,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2021,12]]}},"alternative-id":["v13122451"],"URL":"https:\/\/doi.org\/10.3390\/v13122451","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,12,6]]}}}