{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T04:49:02Z","timestamp":1787028542675,"version":"build-2736575974"},"reference-count":220,"publisher":"MDPI AG","issue":"13","license":[{"start":{"date-parts":[[2024,6,28]],"date-time":"2024-06-28T00:00:00Z","timestamp":1719532800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004837","name":"Ministerio de Ciencia, Innovaci\u00f3n y Universidades","doi-asserted-by":"publisher","award":["RYC2021-032674-I"],"award-info":[{"award-number":["RYC2021-032674-I"]}],"id":[{"id":"10.13039\/501100004837","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004837","name":"Ministerio de Ciencia, Innovaci\u00f3n y Universidades","doi-asserted-by":"publisher","award":["PID2022-136725OB-I00"],"award-info":[{"award-number":["PID2022-136725OB-I00"]}],"id":[{"id":"10.13039\/501100004837","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004837","name":"Ministerio de Ciencia, Innovaci\u00f3n y Universidades","doi-asserted-by":"publisher","award":["PID2022-140647NA-100"],"award-info":[{"award-number":["PID2022-140647NA-100"]}],"id":[{"id":"10.13039\/501100004837","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011033","name":"Agencia Estatal de Investigaci\u00f3n","doi-asserted-by":"publisher","award":["RYC2021-032674-I"],"award-info":[{"award-number":["RYC2021-032674-I"]}],"id":[{"id":"10.13039\/501100011033","id-type":"DOI","asserted-by":"publisher"}]},{"name":"\u00abNextGenerationEU\u00bb\/PRTR\u00bb","award":["RYC2021-032674-I"],"award-info":[{"award-number":["RYC2021-032674-I"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The human immunodeficiency virus type 1 (HIV-1) capsid is a protein core formed by multiple copies of the viral capsid (CA) protein. Inside the capsid, HIV-1 harbours all the viral components required for replication, including the genomic RNA and viral enzymes reverse transcriptase (RT) and integrase (IN). Upon infection, the RT transforms the genomic RNA into a double-stranded DNA molecule that is subsequently integrated into the host chromosome by IN. For this to happen, the viral capsid must open and release the viral DNA, in a process known as uncoating. Capsid plays a key role during the initial stages of HIV-1 replication; therefore, its stability is intimately related to infection efficiency, and untimely uncoating results in reverse transcription defects. How and where uncoating takes place and its relationship with reverse transcription is not fully understood, but the recent development of novel biochemical and cellular approaches has provided unprecedented detail on these processes. In this review, we present the latest findings on the intricate link between capsid stability, reverse transcription and uncoating, the different models proposed over the years for capsid uncoating, and the role played by other cellular factors on these processes.<\/jats:p>","DOI":"10.3390\/ijms25137167","type":"journal-article","created":{"date-parts":[[2024,7,2]],"date-time":"2024-07-02T12:58:42Z","timestamp":1719925122000},"page":"7167","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["May I Help You with Your Coat? HIV-1 Capsid Uncoating and Reverse Transcription"],"prefix":"10.3390","volume":"25","author":[{"ORCID":"https:\/\/orcid.org\/0009-0000-3762-6240","authenticated-orcid":false,"given":"Laura","family":"Arribas","sequence":"first","affiliation":[{"name":"Instituto Universitario de Investigaciones Biom\u00e9dicas y Sanitarias (IUIBS), Universidad de Las Palmas de Gran Canaria, 35016 Las Palmas de Gran Canaria, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1251-6640","authenticated-orcid":false,"given":"Luis","family":"Men\u00e9ndez-Arias","sequence":"additional","affiliation":[{"name":"Centro de Biolog\u00eda Molecular \u201cSevero Ochoa\u201d (Consejo Superior de Investigaciones Cient\u00edficas & Universidad Aut\u00f3noma de Madrid), 28049 Madrid, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0548-7690","authenticated-orcid":false,"given":"Gilberto","family":"Betancor","sequence":"additional","affiliation":[{"name":"Instituto Universitario de Investigaciones Biom\u00e9dicas y Sanitarias (IUIBS), Universidad de Las Palmas de Gran Canaria, 35016 Las Palmas de Gran Canaria, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,6,28]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1099\/jgv.0.001497","article-title":"ICTV Virus Taxonomy Profile: Caulimoviridae","volume":"101","author":"Teycheney","year":"2020","journal-title":"J. Gen Virol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1099\/jgv.0.001415","article-title":"ICTV Virus Taxonomy Profile: Hepadnaviridae","volume":"101","author":"Magnius","year":"2020","journal-title":"J. Gen. Virol."},{"key":"ref_3","unstructured":"(2024, April 15). Available online: https:\/\/www.who.int\/data\/gho\/data\/themes\/hiv-aids#:~:text=Global%20situation%20and%20trends%3A,at%20the%20end%20of%202022."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Wainberg, M.A., and Jeang, K.T. (2008). 25 years of HIV-1 research\u2014Progress and perspectives. BMC Med., 6.","DOI":"10.1186\/1741-7015-6-31"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Marceau, T., and Braibant, M. (2024). Role of Viral Envelope Proteins in Determining Susceptibility of Viruses to IFITM Proteins. Viruses, 16.","DOI":"10.3390\/v16020254"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1707","DOI":"10.1093\/emboj\/cdg143","article-title":"Structural organization of authentic, mature HIV-1 virions and cores","volume":"22","author":"Briggs","year":"2003","journal-title":"EMBO J."},{"key":"ref_7","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_8","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1016\/j.cell.2009.04.063","article-title":"X-ray structures of the hexameric building block of the HIV capsid","volume":"137","author":"Pornillos","year":"2009","journal-title":"Cell"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1016\/j.cell.2009.10.010","article-title":"Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function","volume":"139","author":"Byeon","year":"2009","journal-title":"Cell"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1038\/nature11169","article-title":"Structure of the immature retroviral capsid at 8 A resolution by cryo-electron microscopy","volume":"487","author":"Bharat","year":"2012","journal-title":"Nature"},{"key":"ref_11","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_12","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1146\/annurev.biochem.67.1.1","article-title":"HIV-1: Fifteen proteins and an RNA","volume":"67","author":"Frankel","year":"1998","journal-title":"Annu. Rev. Biochem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1016\/0092-8674(93)90637-6","article-title":"Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B","volume":"73","author":"Luban","year":"1993","journal-title":"Cell"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1038\/372359a0","article-title":"Specific incorporation of cyclophilin A into HIV-1 virions","volume":"372","author":"Franke","year":"1994","journal-title":"Nature"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1126\/science.abb4808","article-title":"Structural and mechanistic bases for a potent HIV-1 capsid inhibitor","volume":"370","author":"Bester","year":"2020","journal-title":"Science"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"5821","DOI":"10.1128\/jvi.69.9.5821-5823.1995","article-title":"Cyclophilin binding to the human immunodeficiency virus type 1 Gag polyprotein is mimicked by an anti-cyclosporine antibody","volume":"69","author":"Franke","year":"1995","journal-title":"J. Virol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.coviro.2021.03.005","article-title":"Integrative structural biology of HIV-1 capsid protein assemblies: Combining experiment and computation","volume":"48","author":"Perilla","year":"2021","journal-title":"Curr. Opin. Virol."},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Zhuang, S., and Torbett, B.E. (2021). Interactions of HIV-1 Capsid with Host Factors and Their Implications for Developing Novel Therapeutics. Viruses, 13.","DOI":"10.3390\/v13030417"},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Krebs, A.S., Mendonca, L.M., and Zhang, P. (2021). Structural Analysis of Retrovirus Assembly and Maturation. Viruses, 14.","DOI":"10.3390\/v14010054"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1126\/science.277.5322.112","article-title":"Positive effects of combined antiretroviral therapy on CD4+ T cell homeostasis and function in advanced HIV disease","volume":"277","author":"Autran","year":"1997","journal-title":"Science"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Singh, A.K., Kumar, A., Arora, S., Kumar, R., Verma, A., Khalilullah, H., Jaremko, M., Emwas, A.H., and Kumar, P. (2024). Current insights and molecular docking studies of HIV-1 reverse transcriptase inhibitors. Chem. Biol. Drug Des., 103.","DOI":"10.1111\/cbdd.14372"},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Singh, A.K., and Das, K. (2022). Insights into HIV-1 Reverse Transcriptase (RT) Inhibition and Drug Resistance from Thirty Years of Structural Studies. Viruses, 14.","DOI":"10.3390\/v14051027"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.tips.2021.10.004","article-title":"Update and latest advances in antiretroviral therapy","volume":"43","author":"Delgado","year":"2022","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1126\/science.1377403","article-title":"Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor","volume":"256","author":"Kohlstaedt","year":"1992","journal-title":"Science"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Mouhand, A., Pasi, M., Catala, M., Zargarian, L., Belfetmi, A., Barraud, P., Mauffret, O., and Tisne, C. (2020). Overview of the Nucleic-Acid Binding Properties of the HIV-1 Nucleocapsid Protein in Its Different Maturation States. Viruses, 12.","DOI":"10.3390\/v12101109"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"700","DOI":"10.4161\/rna.7.6.13685","article-title":"Nucleic acid chaperone activity of retroviral Gag proteins","volume":"7","author":"Rein","year":"2010","journal-title":"RNA Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"866","DOI":"10.1016\/j.jmb.2011.12.034","article-title":"Nucleocapsid protein annealing of a primer-template enhances (+)-strand DNA synthesis and fidelity by HIV-1 reverse transcriptase","volume":"415","author":"Kim","year":"2012","journal-title":"J. Mol. Biol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/S0079-6603(05)80006-6","article-title":"Nucleic acid chaperone activity of HIV-1 nucleocapsid protein: Critical role in reverse transcription and molecular mechanism","volume":"80","author":"Levin","year":"2005","journal-title":"Prog. Nucleic Acid Res. Mol. Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1038\/s41586-018-0055-9","article-title":"Architecture of an HIV-1 reverse transcriptase initiation complex","volume":"557","author":"Larsen","year":"2018","journal-title":"Nature"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"7308","DOI":"10.1073\/pnas.1814170116","article-title":"Structure of HIV-1 RT\/dsRNA initiation complex prior to nucleotide incorporation","volume":"116","author":"Das","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.virusres.2016.12.019","article-title":"Viral reverse transcriptases","volume":"234","author":"Alvarez","year":"2017","journal-title":"Virus Res."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.sbi.2020.07.005","article-title":"Advances in understanding the initiation of HIV-1 reverse transcription","volume":"65","author":"Krupkin","year":"2020","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1002\/j.1460-2075.1996.tb00426.x","article-title":"Specific initiation and switch to elongation of human immunodeficiency virus type 1 reverse transcription require the post-transcriptional modifications of primer tRNA3Lys","volume":"15","author":"Isel","year":"1996","journal-title":"EMBO J."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"7178","DOI":"10.1002\/j.1460-2075.1996.tb01109.x","article-title":"Binding and kinetic properties of HIV-1 reverse transcriptase markedly differ during initiation and elongation of reverse transcription","volume":"15","author":"Lanchy","year":"1996","journal-title":"EMBO J."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1126\/science.aaa9266","article-title":"RNA structure. Structure of the HIV-1 RNA packaging signal","volume":"348","author":"Keane","year":"2015","journal-title":"Science"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"8697","DOI":"10.1038\/s41598-019-45079-1","article-title":"LC\/MS analysis and deep sequencing reveal the accurate RNA composition in the HIV-1 virion","volume":"9","author":"Simonova","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1038\/nsmb.1687","article-title":"A sequence similar to tRNA 3 Lys gene is embedded in HIV-1 U3-R and promotes minus-strand transfer","volume":"17","author":"DiChiacchio","year":"2010","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1752","DOI":"10.1016\/j.biocel.2004.02.016","article-title":"\u2018Binding, bending and bonding\u2019: Polypurine tract-primed initiation of plus-strand DNA synthesis in human immunodeficiency virus","volume":"36","author":"Rausch","year":"2004","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1074\/jbc.M117.798256","article-title":"Mechanism of polypurine tract primer generation by HIV-1 reverse transcriptase","volume":"293","author":"Figiel","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2259","DOI":"10.1093\/nar\/gkv077","article-title":"Effects of HIV-1 reverse transcriptase connection subdomain mutations on polypurine tract removal and initiation of (+)-strand DNA synthesis","volume":"43","author":"Betancor","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Alvarez, M., Sapena-Ventura, E., Luczkowiak, J., Martin-Alonso, S., and Menendez-Arias, L. (2021). Analysis and Molecular Determinants of HIV RNase H Cleavage Specificity at the PPT\/U3 Junction. Viruses, 13.","DOI":"10.3390\/v13010131"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/S0021-9258(19)69935-7","article-title":"The terminal redundancy of the retrovirus genome facilitates chain elongation by reverse transcriptase","volume":"256","author":"Swanstrom","year":"1981","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1128\/jvi.66.1.367-373.1992","article-title":"Incomplete removal of the RNA primer for minus-strand DNA synthesis by human immunodeficiency virus type 1 reverse transcriptase","volume":"66","author":"Pullen","year":"1992","journal-title":"J. Virol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"15071","DOI":"10.1016\/S0021-9258(18)42147-3","article-title":"Specificity of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H in removal of the minus-strand primer, tRNA(Lys3)","volume":"267","author":"Smith","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"28384","DOI":"10.1074\/jbc.273.43.28384","article-title":"The nature of human immunodeficiency virus type 1 strand transfers","volume":"273","author":"Yu","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"e0067622","DOI":"10.1128\/jvi.00676-22","article-title":"Mutations in the 3\u2032-PPT Lead to HIV-1 Replication without Integration","volume":"96","author":"Richetta","year":"2022","journal-title":"J. Virol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1089\/aid.1993.9.817","article-title":"Characterization of HIV replication complexes early after cell-to-cell infection","volume":"9","author":"Karageorgos","year":"1993","journal-title":"AIDS Res. Hum. Retroviruses"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"6125","DOI":"10.1073\/pnas.90.13.6125","article-title":"Association of integrase, matrix, and reverse transcriptase antigens of human immunodeficiency virus type 1 with viral nucleic acids following acute infection","volume":"90","author":"Bukrinsky","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1910","DOI":"10.1128\/jvi.65.4.1910-1915.1991","article-title":"Determination of viral proteins present in the human immunodeficiency virus type 1 preintegration complex","volume":"65","author":"Farnet","year":"1991","journal-title":"J. Virol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"5382","DOI":"10.1128\/jvi.71.7.5382-5390.1997","article-title":"Human immunodeficiency virus type 1 preintegration complexes: Studies of organization and composition","volume":"71","author":"Miller","year":"1997","journal-title":"J. Virol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"3626","DOI":"10.1128\/JVI.75.8.3626-3635.2001","article-title":"Characterization of intracellular reverse transcription complexes of human immunodeficiency virus type 1","volume":"75","author":"Fassati","year":"2001","journal-title":"J. Virol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1016\/S0960-9822(95)00209-0","article-title":"Target DNA capture by HIV-1 integration complexes","volume":"5","author":"Miller","year":"1995","journal-title":"Curr. Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"3565","DOI":"10.1093\/emboj\/20.13.3565","article-title":"Human immunodeficiency virus type 1 integrase: Arrangement of protein domains in active cDNA complexes","volume":"20","author":"Gao","year":"2001","journal-title":"EMBO J."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"8196","DOI":"10.1128\/JVI.77.15.8196-8206.2003","article-title":"Structural analyses of purified human immunodeficiency virus type 1 intracellular reverse transcription complexes","volume":"77","author":"Nermut","year":"2003","journal-title":"J. Virol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"5067","DOI":"10.1128\/jvi.66.8.5067-5074.1992","article-title":"Viral DNA carried by human immunodeficiency virus type 1 virions","volume":"66","author":"Lori","year":"1992","journal-title":"J. Virol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"4893","DOI":"10.1128\/jvi.66.8.4893-4900.1992","article-title":"Partial reverse transcripts in virions from human immunodeficiency and murine leukemia viruses","volume":"66","author":"Trono","year":"1992","journal-title":"J. Virol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"2809","DOI":"10.1128\/jvi.70.5.2809-2824.1996","article-title":"Endogenous reverse transcription of human immunodeficiency virus type 1 in physiological microenviroments: An important stage for viral infection of nondividing cells","volume":"70","author":"Zhang","year":"1996","journal-title":"J. Virol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/S1386-6532(02)00121-X","article-title":"The first strand transfer reaction of HIV-1 reverse transcription is more efficient in infected cells than in cell-free natural endogenous reverse transcription reactions","volume":"26","author":"Hooker","year":"2003","journal-title":"J. Clin. Virol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1425","DOI":"10.1128\/JVI.01808-07","article-title":"Cell factors stimulate human immunodeficiency virus type 1 reverse transcription in vitro","volume":"82","author":"Warrilow","year":"2008","journal-title":"J. Virol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"8645","DOI":"10.1128\/jvi.70.12.8645-8652.1996","article-title":"The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycle","volume":"70","author":"Reicin","year":"1996","journal-title":"J. Virol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"9357","DOI":"10.1128\/JVI.75.19.9357-9366.2001","article-title":"Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells","volume":"75","author":"Tang","year":"2001","journal-title":"J. Virol."},{"key":"ref_62","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_63","doi-asserted-by":"crossref","first-page":"848","DOI":"10.1038\/nature02343","article-title":"The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys","volume":"427","author":"Stremlau","year":"2004","journal-title":"Nature"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1038\/s41579-019-0225-2","article-title":"Restriction of HIV-1 and other retroviruses by TRIM5","volume":"17","author":"Pornillos","year":"2019","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"18372","DOI":"10.1073\/pnas.1210903109","article-title":"Structural insight into HIV-1 capsid recognition by rhesus TRIM5alpha","volume":"109","author":"Yang","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1038\/s41467-020-15106-1","article-title":"TRIM5alpha self-assembly and compartmentalization of the HIV-1 viral capsid","volume":"11","author":"Yu","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1073\/pnas.1013426108","article-title":"Hexagonal assembly of a restricting TRIM5alpha protein","volume":"108","author":"Chandrasekaran","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Zhao, G., Ke, D., Vu, T., Ahn, J., Shah, V.B., Yang, R., Aiken, C., Charlton, L.M., Gronenborn, A.M., and Zhang, P. (2011). Rhesus TRIM5alpha disrupts the HIV-1 capsid at the inter-hexamer interfaces. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002009"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1083\/jcb.200203150","article-title":"Visualization of the intracellular behavior of HIV in living cells","volume":"159","author":"McDonald","year":"2002","journal-title":"J. Cell Biol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1126\/science.1240933","article-title":"Cyclic GMP-AMP synthase is an innate immune sensor of HIV and other retroviruses","volume":"341","author":"Gao","year":"2013","journal-title":"Science"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1126\/science.1243640","article-title":"IFI16 DNA sensor is required for death of lymphoid CD4 T cells abortively infected with HIV","volume":"343","author":"Monroe","year":"2014","journal-title":"Science"},{"key":"ref_72","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_73","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_74","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_75","doi-asserted-by":"crossref","first-page":"e0073223","DOI":"10.1128\/jvi.00732-23","article-title":"Emerging role of cyclophilin A in HIV-1 infection: From producer cell to the target cell nucleus","volume":"97","author":"Padron","year":"2023","journal-title":"J. Virol."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Schaller, T., Ocwieja, K.E., Rasaiyaah, J., Price, A.J., Brady, T.L., Roth, S.L., Hue, S., Fletcher, A.J., Lee, K., and KewalRamani, V.N. (2011). HIV-1 capsid-cyclophilin interactions determine nuclear import pathway, integration targeting and replication efficiency. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002439"},{"key":"ref_77","doi-asserted-by":"crossref","unstructured":"Price, A.J., Fletcher, A.J., Schaller, T., Elliott, T., Lee, K., KewalRamani, V.N., Chin, J.W., Towers, G.J., and James, L.C. (2012). CPSF6 defines a conserved capsid interface that modulates HIV-1 replication. PLoS Pathog., 8.","DOI":"10.2210\/pdb4b4n\/pdb"},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Matreyek, K.A., Yucel, S.S., Li, X., and Engelman, A. (2013). Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003693"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"18625","DOI":"10.1073\/pnas.1419945112","article-title":"Structural basis of HIV-1 capsid recognition by PF74 and CPSF6","volume":"111","author":"Bhattacharya","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1234","DOI":"10.1016\/j.str.2019.04.015","article-title":"MxB Restricts HIV-1 by Targeting the Tri-hexamer Interface of the Viral Capsid","volume":"27","author":"Smaga","year":"2019","journal-title":"Structure"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"e2202815120","DOI":"10.1073\/pnas.2202815120","article-title":"The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores","volume":"120","author":"Shen","year":"2023","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"6660","DOI":"10.1038\/ncomms7660","article-title":"HIV-1 capsids bind and exploit the kinesin-1 adaptor FEZ1 for inward movement to the nucleus","volume":"6","author":"Malikov","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"2373","DOI":"10.1016\/j.celrep.2019.07.079","article-title":"FEZ1 Is Recruited to a Conserved Cofactor Site on Capsid to Promote HIV-1 Trafficking","volume":"28","author":"Huang","year":"2019","journal-title":"Cell Rep."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1038\/s41586-018-0396-4","article-title":"Inositol phosphates are assembly co-factors for HIV-1","volume":"560","author":"Dick","year":"2018","journal-title":"Nature"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1038\/nature02777","article-title":"Cyclophilin A retrotransposition into TRIM5 explains owl monkey resistance to HIV-1","volume":"430","author":"Sayah","year":"2004","journal-title":"Nature"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1038\/nature12162","article-title":"Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics","volume":"497","author":"Zhao","year":"2013","journal-title":"Nature"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"e4792","DOI":"10.1002\/pro.4792","article-title":"USCF ChimeraX: Tools for structure building and analysis","volume":"32","author":"Meng","year":"2023","journal-title":"Protein Sci."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S0092-8674(00)80828-4","article-title":"HIV-1 genome nuclear import is mediated by a central DNA flap","volume":"101","author":"Zennou","year":"2000","journal-title":"Cell"},{"key":"ref_89","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_90","doi-asserted-by":"crossref","unstructured":"Price, A.J., Jacques, D.A., McEwan, W.A., Fletcher, A.J., Essig, S., Chin, J.W., Halambage, U.D., Aiken, C., and James, L.C. (2014). Host cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassembly. PLoS Pathog., 10.","DOI":"10.1371\/journal.ppat.1004459"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"3570","DOI":"10.1128\/JVI.01295-10","article-title":"LEDGF dominant interference proteins demonstrate prenuclear exposure of HIV-1 integrase and synergize with LEDGF depletion to destroy viral infectivity","volume":"85","author":"Meehan","year":"2011","journal-title":"J. Virol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"5350","DOI":"10.1128\/JVI.00476-15","article-title":"Complementary Assays Reveal a Low Level of CA Associated with Viral Complexes in the Nuclei of HIV-1-Infected Cells","volume":"89","author":"Hulme","year":"2015","journal-title":"J. Virol."},{"key":"ref_93","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_94","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1186\/1742-4690-10-70","article-title":"Evidence for biphasic uncoating during HIV-1 infection from a novel imaging assay","volume":"10","author":"Xu","year":"2013","journal-title":"Retrovirology"},{"key":"ref_95","doi-asserted-by":"crossref","unstructured":"Eschbach, J.E., Puray-Chavez, M., Mohammed, S., Wang, Q., Xia, M., Huang, L.C., Shan, L., and Kutluay, S.B. (2024). HIV-1 capsid stability and reverse transcription are finely balanced to minimize sensing of reverse transcription products via the cGAS-STING pathway. mBio, 15.","DOI":"10.1128\/mbio.00348-24"},{"key":"ref_96","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_97","doi-asserted-by":"crossref","unstructured":"Francis, A.C., and Melikyan, G.B. (2018). Live-Cell Imaging of Early Steps of Single HIV-1 Infection. Viruses, 10.","DOI":"10.3390\/v10050275"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"3505","DOI":"10.1038\/s41467-020-17256-8","article-title":"HIV-1 replication complexes accumulate in nuclear speckles and integrate into speckle-associated genomic domains","volume":"11","author":"Francis","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_99","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_100","doi-asserted-by":"crossref","first-page":"1840","DOI":"10.1038\/s41564-019-0575-6","article-title":"Transportin-1 binds to the HIV-1 capsid via a nuclear localization signal and triggers uncoating","volume":"4","author":"Fernandez","year":"2019","journal-title":"Nat. Microbiol."},{"key":"ref_101","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_102","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_103","doi-asserted-by":"crossref","first-page":"5486","DOI":"10.1073\/pnas.1920631117","article-title":"HIV-1 uncoats in the nucleus near sites of integration","volume":"117","author":"Burdick","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_104","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. Natl. Acad. Sci. USA"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"e64776","DOI":"10.7554\/eLife.64776","article-title":"HIV-1 uncoating by release of viral cDNA from capsid-like structures in the nucleus of infected cells","volume":"10","author":"Muller","year":"2021","journal-title":"eLife"},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Schifferdecker, S., Zila, V., Muller, T.G., Sakin, V., Anders-Osswein, M., Laketa, V., Krausslich, H.G., and Muller, B. (2022). Direct Capsid Labeling of Infectious HIV-1 by Genetic Code Expansion Allows Detection of Largely Complete Nuclear Capsids and Suggests Nuclear Entry of HIV-1 Complexes via Common Routes. mBio, 13.","DOI":"10.1128\/mbio.01959-22"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"108201","DOI":"10.1016\/j.celrep.2020.108201","article-title":"Nuclear Import of the HIV-1 Core Precedes Reverse Transcription and Uncoating","volume":"32","author":"Selyutina","year":"2020","journal-title":"Cell Rep."},{"key":"ref_108","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_109","doi-asserted-by":"crossref","first-page":"2928","DOI":"10.1021\/acsnano.3c07678","article-title":"HIV-1 Capsid Uncoating Is a Multistep Process That Proceeds through Defect Formation Followed by Disassembly of the Capsid Lattice","volume":"18","author":"Gifford","year":"2024","journal-title":"ACS Nano"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/s41594-023-00925-9","article-title":"Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels","volume":"30","author":"Shen","year":"2023","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1038\/s41586-023-06966-w","article-title":"HIV-1 capsids enter the FG phase of nuclear pores like a transport receptor","volume":"626","author":"Fu","year":"2024","journal-title":"Nature"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1038\/nature15381","article-title":"In situ structural analysis of the human nuclear pore complex","volume":"526","author":"Kosinski","year":"2015","journal-title":"Nature"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1146\/annurev-biochem-062917-011901","article-title":"The Structure of the Nuclear Pore Complex (An Update)","volume":"88","author":"Lin","year":"2019","journal-title":"Annu. Rev. Biochem."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"e2313737121","DOI":"10.1073\/pnas.2313737121","article-title":"HIV-1 capsid shape, orientation, and entropic elasticity regulate translocation into the nuclear pore complex","volume":"121","author":"Hudait","year":"2024","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_115","first-page":"10-1128","article-title":"Remodeling of the Core Leads HIV-1 Preintegration Complex into the Nucleus of Human Lymphocytes","volume":"94","author":"Gazi","year":"2020","journal-title":"J. Virol."},{"key":"ref_116","doi-asserted-by":"crossref","unstructured":"Francis, A.C., Cereseto, A., Singh, P.K., Shi, J., Poeschla, E., Engelman, A.N., Aiken, C., and Melikyan, G.B. (2022). Localization and functions of native and eGFP-tagged capsid proteins in HIV-1 particles. PLoS Pathog., 18.","DOI":"10.1371\/journal.ppat.1010754"},{"key":"ref_117","doi-asserted-by":"crossref","unstructured":"Guedan, A., Donaldson, C.D., Caroe, E.R., Cosnefroy, O., Taylor, I.A., and Bishop, K.N. (2021). HIV-1 requires capsid remodelling at the nuclear pore for nuclear entry and integration. PLoS Pathog., 17.","DOI":"10.1101\/2021.03.18.436028"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1038\/s41586-023-06969-7","article-title":"The HIV capsid mimics karyopherin engagement of FG-nucleoporins","volume":"626","author":"Dickson","year":"2024","journal-title":"Nature"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"3782","DOI":"10.1038\/s41467-023-39146-5","article-title":"The HIV-1 capsid core is an opportunistic nuclear import receptor","volume":"14","author":"Xue","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"e41800","DOI":"10.7554\/eLife.41800","article-title":"HIV-1 nuclear import in macrophages is regulated by CPSF6-capsid interactions at the nuclear pore complex","volume":"8","author":"Bejarano","year":"2019","journal-title":"eLife"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"e04114","DOI":"10.7554\/eLife.04114","article-title":"Quantitative microscopy of functional HIV post-entry complexes reveals association of replication with the viral capsid","volume":"3","author":"Peng","year":"2014","journal-title":"eLife"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"10-1128","DOI":"10.1128\/JVI.00034-17","article-title":"Imaging HIV-1 Genomic DNA from Entry through Productive Infection","volume":"91","author":"Stultz","year":"2017","journal-title":"J. Virol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"113941","DOI":"10.1016\/j.celrep.2024.113941","article-title":"Spatial resolution of HIV-1 post-entry steps in resting CD4 T cells","volume":"43","author":"Ananth","year":"2024","journal-title":"Cell Rep."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"10714","DOI":"10.1038\/ncomms10714","article-title":"Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site","volume":"7","author":"Liu","year":"2016","journal-title":"Nat. Commun."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1186\/s12977-019-0471-4","article-title":"Functional analysis of the secondary HIV-1 capsid binding site in the host protein cyclophilin A","volume":"16","author":"Peng","year":"2019","journal-title":"Retrovirology"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"E10707","DOI":"10.1073\/pnas.1712033114","article-title":"Bicaudal D2 facilitates the cytoplasmic trafficking and nuclear import of HIV-1 genomes during infection","volume":"114","author":"Dharan","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"10-1128","DOI":"10.1128\/JVI.00358-18","article-title":"HIV-1 Engages a Dynein-Dynactin-BICD2 Complex for Infection and Transport to the Nucleus","volume":"92","author":"Carnes","year":"2018","journal-title":"J. Virol."},{"key":"ref_128","doi-asserted-by":"crossref","unstructured":"Dharan, A., Talley, S., Tripathi, A., Mamede, J.I., Majetschak, M., Hope, T.J., and Campbell, E.M. (2016). KIF5B and Nup358 Cooperatively Mediate the Nuclear Import of HIV-1 during Infection. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005700"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1038\/s41564-021-00868-1","article-title":"Sec24C is an HIV-1 host dependency factor crucial for virus replication","volume":"6","author":"Rebensburg","year":"2021","journal-title":"Nat. Microbiol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1016\/j.chom.2018.08.002","article-title":"Capsid-CPSF6 Interaction Licenses Nuclear HIV-1 Trafficking to Sites of Viral DNA Integration","volume":"24","author":"Achuthan","year":"2018","journal-title":"Cell Host Microbe"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1038\/nature00939","article-title":"Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein","volume":"418","author":"Sheehy","year":"2002","journal-title":"Nature"},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Huthoff, H., Autore, F., Gallois-Montbrun, S., Fraternali, F., and Malim, M.H. (2009). RNA-dependent oligomerization of APOBEC3G is required for restriction of HIV-1. PLoS Pathog., 5.","DOI":"10.1371\/journal.ppat.1000330"},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Apolonia, L., Schulz, R., Curk, T., Rocha, P., Swanson, C.M., Schaller, T., Ule, J., and Malim, M.H. (2015). Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1. PLoS Pathog., 11.","DOI":"10.1371\/journal.ppat.1004609"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"5000","DOI":"10.1128\/JVI.02237-06","article-title":"APOBEC3G multimers are recruited to the plasma membrane for packaging into human immunodeficiency virus type 1 virus-like particles in an RNA-dependent process requiring the NC basic linker","volume":"81","author":"Burnett","year":"2007","journal-title":"J. Virol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"35822","DOI":"10.1074\/jbc.M405761200","article-title":"Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs","volume":"279","author":"Svarovskaia","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.virol.2015.03.012","article-title":"APOBECs and virus restriction","volume":"479\u2013480","author":"Harris","year":"2015","journal-title":"Virology"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"8780","DOI":"10.1073\/pnas.0603313103","article-title":"Cellular inhibitors of long interspersed element 1 and Alu retrotransposition","volume":"103","author":"Bogerd","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Vartanian, J.P., Henry, M., Marchio, A., Suspene, R., Aynaud, M.M., Guetard, D., Cervantes-Gonzalez, M., Battiston, C., Mazzaferro, V., and Pineau, P. (2010). Massive APOBEC3 editing of hepatitis B viral DNA in cirrhosis. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1000928"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1404","DOI":"10.1038\/nm945","article-title":"The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif","volume":"9","author":"Sheehy","year":"2003","journal-title":"Nat. Med."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1016\/S0092-8674(03)00423-9","article-title":"DNA deamination mediates innate immunity to retroviral infection","volume":"113","author":"Harris","year":"2003","journal-title":"Cell"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1038\/nature01709","article-title":"Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts","volume":"424","author":"Mangeat","year":"2003","journal-title":"Nature"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1038\/nature01707","article-title":"The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA","volume":"424","author":"Zhang","year":"2003","journal-title":"Nature"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1128\/JVI.80.3.1067-1076.2006","article-title":"Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors","volume":"80","author":"Cullen","year":"2006","journal-title":"J. Virol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"184","DOI":"10.2174\/1570162X16666180817115830","article-title":"Host Restriction Factors and Human Immunodeficiency Virus (HIV-1): A Dynamic Interplay Involving All Phases of the Viral Life Cycle","volume":"16","author":"Durbano","year":"2018","journal-title":"Curr. HIV Res."},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"Bishop, K.N., Verma, M., Kim, E.Y., Wolinsky, S.M., and Malim, M.H. (2008). APOBEC3G inhibits elongation of HIV-1 reverse transcripts. PLoS Pathog., 4.","DOI":"10.1371\/journal.ppat.1000231"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1038\/nchem.1795","article-title":"Oligomerization transforms human APOBEC3G from an efficient enzyme to a slowly dissociating nucleic acid-binding protein","volume":"6","author":"Chaurasiya","year":"2014","journal-title":"Nat. Chem."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1038\/s41467-017-00501-y","article-title":"Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G","volume":"8","author":"Morse","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"3777","DOI":"10.1128\/JVI.06594-11","article-title":"The cellular antiviral protein APOBEC3G interacts with HIV-1 reverse transcriptase and inhibits its function during viral replication","volume":"86","author":"Wang","year":"2012","journal-title":"J. Virol."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1038\/s41564-017-0063-9","article-title":"Deep sequencing of HIV-1 reverse transcripts reveals the multifaceted antiviral functions of APOBEC3G","volume":"3","author":"Pollpeter","year":"2018","journal-title":"Nat. Microbiol."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"8450","DOI":"10.1128\/JVI.00839-06","article-title":"Antiviral potency of APOBEC proteins does not correlate with cytidine deamination","volume":"80","author":"Bishop","year":"2006","journal-title":"J. Virol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"2587","DOI":"10.1074\/jbc.M607298200","article-title":"APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G","volume":"282","author":"Holmes","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1508","DOI":"10.1128\/JVI.02587-12","article-title":"Suppression of HIV-1 infection by APOBEC3 proteins in primary human CD4(+) T cells is associated with inhibition of processive reverse transcription as well as excessive cytidine deamination","volume":"87","author":"Gillick","year":"2013","journal-title":"J. Virol."},{"key":"ref_153","doi-asserted-by":"crossref","unstructured":"Meissner, M.E., Willkomm, N.A., Lucas, J., Arndt, W.G., Aitken, S.F., Julik, E.J., Baliga, S., and Mansky, L.M. (2022). Differential Activity of APOBEC3F, APOBEC3G, and APOBEC3H in the Restriction of HIV-2. J. Mol. Biol., 434.","DOI":"10.1016\/j.jmb.2021.167355"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1339","DOI":"10.1016\/j.jmb.2019.02.015","article-title":"APOBEC3 Host Restriction Factors of HIV-1 Can Change the Template Switching Frequency of Reverse Transcriptase","volume":"431","author":"Adolph","year":"2019","journal-title":"J. Mol. Biol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1186\/s12977-015-0174-4","article-title":"SAMHD1 specifically restricts retroviruses through its RNase activity","volume":"12","author":"Choi","year":"2015","journal-title":"Retrovirology"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1038\/nature10623","article-title":"HIV-1 restriction factor SAMHD1 is a deoxynucleoside triphosphate triphosphohydrolase","volume":"480","author":"Goldstone","year":"2011","journal-title":"Nature"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1038\/nature10195","article-title":"Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein","volume":"474","author":"Hrecka","year":"2011","journal-title":"Nature"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1038\/ni.2236","article-title":"SAMHD1 restricts the replication of human immunodeficiency virus type 1 by depleting the intracellular pool of deoxynucleoside triphosphates","volume":"13","author":"Lahouassa","year":"2012","journal-title":"Nat. Immunol."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1038\/s41467-021-21023-8","article-title":"Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification","volume":"12","author":"Yu","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1016\/j.chom.2013.03.005","article-title":"The retroviral restriction ability of SAMHD1, but not its deoxynucleotide triphosphohydrolase activity, is regulated by phosphorylation","volume":"13","author":"White","year":"2013","journal-title":"Cell Host Microbe"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1038\/nm.3626","article-title":"The ribonuclease activity of SAMHD1 is required for HIV-1 restriction","volume":"20","author":"Ryoo","year":"2014","journal-title":"Nat. Med."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"108748","DOI":"10.1016\/j.jmgm.2024.108748","article-title":"Molecular dynamics investigation of DNA fragments bound to the anti-HIV protein SAMHD1 reveals alterations in allosteric communications","volume":"129","author":"Thapa","year":"2024","journal-title":"J. Mol. Graph. Model."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"4479","DOI":"10.1128\/JVI.79.7.4479-4491.2005","article-title":"Human immunodeficiency virus type 1-induced macrophage gene expression includes the p21 gene, a target for viral regulation","volume":"79","author":"Vazquez","year":"2005","journal-title":"J. Virol."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"12253","DOI":"10.1128\/JVI.01395-09","article-title":"The CDK inhibitor p21Cip1\/WAF1 is induced by FcgammaR activation and restricts the replication of human immunodeficiency virus type 1 and related primate lentiviruses in human macrophages","volume":"83","author":"Bergamaschi","year":"2009","journal-title":"J. Virol."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"5381","DOI":"10.1038\/sj.onc.1202923","article-title":"Control of E2F activity by p21Waf1\/Cip1","volume":"18","author":"Delavaine","year":"1999","journal-title":"Oncogene"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"E3997","DOI":"10.1073\/pnas.1306719110","article-title":"p21-mediated RNR2 repression restricts HIV-1 replication in macrophages by inhibiting dNTP biosynthesis pathway","volume":"110","author":"Allouch","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_167","first-page":"6607","article-title":"Transcription of the E2F-1 gene is rendered cell cycle dependent by E2F DNA-binding sites within its promoter","volume":"14","author":"Neuman","year":"1994","journal-title":"Mol. Cell. Biol."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"E1322","DOI":"10.1073\/pnas.1322059111","article-title":"p21 regulates the HIV-1 restriction factor SAMHD1","volume":"111","author":"Pauls","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1186\/s12985-018-0959-x","article-title":"Inhibition of HIV early replication by the p53 and its downstream gene p21","volume":"15","author":"Shi","year":"2018","journal-title":"Virol. J."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1172\/JCI44539","article-title":"CD4+ T cells from elite controllers resist HIV-1 infection by selective upregulation of p21","volume":"121","author":"Chen","year":"2011","journal-title":"J. Clin. Investig."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1186\/s12977-020-00522-4","article-title":"Increased expression of CDKN1A\/p21 in HIV-1 controllers is correlated with upregulation of ZC3H12A\/MCPIP1","volume":"17","author":"Cortes","year":"2020","journal-title":"Retrovirology"},{"key":"ref_172","doi-asserted-by":"crossref","unstructured":"Maillet, S., Fernandez, J., Decourcelle, M., El Koulali, K., Blanchet, F.P., Arhel, N.J., Maarifi, G., and Nisole, S. (2020). Daxx Inhibits HIV-1 Reverse Transcription and Uncoating in a SUMO-Dependent Manner. Viruses, 12.","DOI":"10.3390\/v12060636"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.bbrc.2008.06.017","article-title":"Daxx interacts with HIV-1 integrase and inhibits lentiviral gene expression","volume":"373","author":"Huang","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_174","doi-asserted-by":"crossref","unstructured":"Dutrieux, J., Maarifi, G., Portilho, D.M., Arhel, N.J., Chelbi-Alix, M.K., and Nisole, S. (2015). PML\/TRIM19-Dependent Inhibition of Retroviral Reverse-Transcription by Daxx. PLoS Pathog., 11.","DOI":"10.1371\/journal.ppat.1005280"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1128\/MMBR.00059-12","article-title":"The unexpected roles of eukaryotic translation elongation factors in RNA virus replication and pathogenesis","volume":"77","author":"Li","year":"2013","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"9587","DOI":"10.1073\/pnas.1204673109","article-title":"Eukaryotic elongation factor 1 complex subunits are critical HIV-1 reverse transcription cofactors","volume":"109","author":"Warren","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"10-1128","DOI":"10.1128\/mBio.00316-18","article-title":"HIV-1 Uncoating and Reverse Transcription Require eEF1A Binding to Surface-Exposed Acidic Residues of the Reverse Transcriptase Thumb Domain","volume":"9","author":"Rawle","year":"2018","journal-title":"mBio"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1186\/1742-4690-9-53","article-title":"Endogenous MOV10 inhibits the retrotransposition of endogenous retroelements but not the replication of exogenous retroviruses","volume":"9","author":"Swanson","year":"2012","journal-title":"Retrovirology"},{"key":"ref_179","doi-asserted-by":"crossref","unstructured":"Guan, Y., Gao, H., Leu, N.A., Vourekas, A., Alexiou, P., Maragkakis, M., Kang, Z., Mourelatos, Z., Liang, G., and Wang, P.J. (2023). The MOV10 RNA helicase is a dosage-dependent host restriction factor for LINE1 retrotransposition in mice. PLoS Genet., 19.","DOI":"10.1371\/journal.pgen.1010566"},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"10241","DOI":"10.1128\/JVI.00585-10","article-title":"P body-associated protein Mov10 inhibits HIV-1 replication at multiple stages","volume":"84","author":"Burdick","year":"2010","journal-title":"J. Virol."},{"key":"ref_181","doi-asserted-by":"crossref","unstructured":"Furtak, V., Mulky, A., Rawlings, S.A., Kozhaya, L., Lee, K., Kewalramani, V.N., and Unutmaz, D. (2010). Perturbation of the P-body component Mov10 inhibits HIV-1 infectivity. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0009081"},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"1220","DOI":"10.1074\/jbc.M111.309831","article-title":"Identification of molecular determinants from Moloney leukemia virus 10 homolog (MOV10) protein for virion packaging and anti-HIV-1 activity","volume":"287","author":"Abudu","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"14346","DOI":"10.1074\/jbc.M110.109314","article-title":"Moloney leukemia virus 10 (MOV10) protein inhibits retrovirus replication","volume":"285","author":"Wang","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/j.molcel.2007.04.016","article-title":"RNA helicase A interacts with RISC in human cells and functions in RISC loading","volume":"26","author":"Robb","year":"2007","journal-title":"Mol. Cell"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"12625","DOI":"10.1074\/jbc.M510596200","article-title":"Association of RNA helicase a with human immunodeficiency virus type 1 particles","volume":"281","author":"Roy","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"1686","DOI":"10.1093\/nar\/gkp1075","article-title":"RNA helicase A modulates translation of HIV-1 and infectivity of progeny virions","volume":"38","author":"Bolinger","year":"2010","journal-title":"Nucleic Acids Res"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"1847","DOI":"10.1128\/JVI.02010-10","article-title":"Coordinate roles of Gag and RNA helicase A in promoting the annealing of formula to HIV-1 RNA","volume":"85","author":"Xing","year":"2011","journal-title":"J. Virol."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"2418","DOI":"10.1016\/j.jmb.2016.04.011","article-title":"DHX9\/RHA Binding to the PBS-Segment of the Genomic RNA during HIV-1 Assembly Bolsters Virion Infectivity","volume":"428","author":"Boeras","year":"2016","journal-title":"J. Mol. Biol."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"11473","DOI":"10.1074\/jbc.RA119.007679","article-title":"Virion-associated, host-derived DHX9\/RNA helicase A enhances the processivity of HIV-1 reverse transcriptase on genomic RNA","volume":"294","author":"Brady","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1021\/cb300648v","article-title":"Drugging topoisomerases: Lessons and challenges","volume":"8","author":"Pommier","year":"2013","journal-title":"ACS Chem. Biol."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"8442","DOI":"10.1073\/pnas.1430827100","article-title":"Human topoisomerase I promotes HIV-1 proviral DNA synthesis: Implications for the species specificity and cellular tropism of HIV-1 infection","volume":"100","author":"Shoya","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"5694","DOI":"10.1073\/pnas.92.12.5694","article-title":"Human immunodeficiency virus type 1 reverse transcriptase: Enhancement of activity by interaction with cellular topoisomerase I","volume":"92","author":"Takahashi","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1016\/S0006-291X(02)00503-X","article-title":"Topoisomerase I and ATP activate cDNA synthesis of human immunodeficiency virus type 1","volume":"294","author":"Takahashi","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1016\/j.bbrc.2003.12.042","article-title":"Topoisomerase I dissociates human immunodeficiency virus type 1 reverse transcriptase from genomic RNAs","volume":"313","author":"Takahashi","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.antiviral.2016.11.001","article-title":"An analog of camptothecin inactive against Topoisomerase I is broadly neutralizing of HIV-1 through inhibition of Vif-dependent APOBEC3G degradation","volume":"136","author":"Bennett","year":"2016","journal-title":"Antiviral Res."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"10-1128","DOI":"10.1128\/mBio.02820-20","article-title":"The Host Cell Metabolite Inositol Hexakisphosphate Promotes Efficient Endogenous HIV-1 Reverse Transcription by Stabilizing the Viral Capsid","volume":"11","author":"Jennings","year":"2020","journal-title":"mBio"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"eabc8420","DOI":"10.1126\/science.abc8420","article-title":"Reconstitution and visualization of HIV-1 capsid-dependent replication and integration in vitro","volume":"370","author":"Christensen","year":"2020","journal-title":"Science"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"eadn7033","DOI":"10.1126\/sciadv.adn7033","article-title":"HIV-1 uncoating requires long double-stranded reverse transcription products","volume":"10","author":"Burdick","year":"2024","journal-title":"Sci. Adv."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.virol.2005.02.028","article-title":"Uncoating of HIV-1 requires cellular activation","volume":"337","author":"Auewarakul","year":"2005","journal-title":"Virology"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1038\/nature19098","article-title":"HIV-1 uses dynamic capsid pores to import nucleotides and fuel encapsidated DNA synthesis","volume":"536","author":"Jacques","year":"2016","journal-title":"Nature"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1038\/s41594-022-00887-4","article-title":"HIV-1 is dependent on its immature lattice to recruit IP6 for mature capsid assembly","volume":"30","author":"Renner","year":"2023","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_202","doi-asserted-by":"crossref","unstructured":"Renner, N., Mallery, D.L., Faysal, K.M.R., Peng, W., Jacques, D.A., Bocking, T., and James, L.C. (2021). A lysine ring in HIV capsid pores coordinates IP6 to drive mature capsid assembly. PLoS Pathog., 17.","DOI":"10.1371\/journal.ppat.1009164"},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"e35335","DOI":"10.7554\/eLife.35335","article-title":"IP6 is an HIV pocket factor that prevents capsid collapse and promotes DNA synthesis","volume":"7","author":"Mallery","year":"2018","journal-title":"eLife"},{"key":"ref_204","doi-asserted-by":"crossref","unstructured":"Sowd, G.A., Shi, J., Fulmer, A., and Aiken, C. (2023). HIV-1 capsid stability enables inositol phosphate-independent infection of target cells and promotes integration into genes. PLoS Pathog., 19.","DOI":"10.1371\/journal.ppat.1011423"},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"10-1128","DOI":"10.1128\/JVI.00166-21","article-title":"HIV-1 uncoating occurs via a series of rapid biomechanical changes in the core related to individual stages of reverse transcription","volume":"95","author":"Rankovic","year":"2021","journal-title":"J. Virol."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"e56275","DOI":"10.15252\/embr.202256275","article-title":"IP6-stabilised HIV capsids evade cGAS\/STING-mediated host immune sensing","volume":"24","author":"Papa","year":"2023","journal-title":"EMBO Rep."},{"key":"ref_207","doi-asserted-by":"crossref","unstructured":"Xu, C., Fischer, D.K., Rankovic, S., Li, W., Dick, R.A., Runge, B., Zadorozhnyi, R., Ahn, J., Aiken, C., and Polenova, T. (2020). Permeability of the HIV-1 capsid to metabolites modulates viral DNA synthesis. PLoS Biol., 18.","DOI":"10.1101\/2020.04.30.071217"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"3712","DOI":"10.1128\/JVI.80.8.3712-3720.2006","article-title":"Evidence for a functional link between uncoating of the human immunodeficiency virus type 1 core and nuclear import of the viral preintegration complex","volume":"80","author":"Dismuke","year":"2006","journal-title":"J. Virol."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"1502","DOI":"10.1371\/journal.ppat.0030156","article-title":"Evidence for direct involvement of the capsid protein in HIV infection of nondividing cells","volume":"3","author":"Yamashita","year":"2007","journal-title":"PLoS Pathog."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"a006882","DOI":"10.1101\/cshperspect.a006882","article-title":"HIV-1 reverse transcription","volume":"2","author":"Hu","year":"2012","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1186\/1742-4690-9-65","article-title":"Virus-producing cells determine the host protein profiles of HIV-1 virion cores","volume":"9","author":"Santos","year":"2012","journal-title":"Retrovirology"},{"key":"ref_212","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_213","doi-asserted-by":"crossref","first-page":"10-1128","DOI":"10.1128\/JVI.00289-17","article-title":"Reverse Transcription Mechanically Initiates HIV-1 Capsid Disassembly","volume":"91","author":"Rankovic","year":"2017","journal-title":"J. Virol."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"10-1128","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_215","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_216","doi-asserted-by":"crossref","unstructured":"Francis, A.C., Marin, M., Shi, J., Aiken, C., and Melikyan, G.B. (2016). Time-Resolved Imaging of Single HIV-1 Uncoating In Vitro and in Living Cells. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005709"},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1186\/1742-4690-3-4","article-title":"Intracytoplasmic maturation of the human immunodeficiency virus type 1 reverse transcription complexes determines their capacity to integrate into chromatin","volume":"3","author":"Iordanskiy","year":"2006","journal-title":"Retrovirology"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1186\/1742-4690-3-38","article-title":"Wild-type and central DNA flap defective HIV-1 lentiviral vector genomes: Intracellular visualization at ultrastructural resolution levels","volume":"3","author":"Arhel","year":"2006","journal-title":"Retrovirology"},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"e105247","DOI":"10.15252\/embj.2020105247","article-title":"Clustering and reverse transcription of HIV-1 genomes in nuclear niches of macrophages","volume":"40","author":"Rensen","year":"2021","journal-title":"EMBO J."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"E4780","DOI":"10.1073\/pnas.1315996110","article-title":"Nuclear import of APOBEC3F-labeled HIV-1 preintegration complexes","volume":"110","author":"Burdick","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/13\/7167\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T15:07:29Z","timestamp":1760108849000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/13\/7167"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,6,28]]},"references-count":220,"journal-issue":{"issue":"13","published-online":{"date-parts":[[2024,7]]}},"alternative-id":["ijms25137167"],"URL":"https:\/\/doi.org\/10.3390\/ijms25137167","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,6,28]]}}}