{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T22:24:56Z","timestamp":1790720696522,"version":"4.1.0"},"reference-count":220,"publisher":"Elsevier BV","issue":"22","license":[{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,10,29]],"date-time":"2026-10-29T00:00:00Z","timestamp":1793232000000},"content-version":"am","delay-in-days":362,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100004330","name":"GlaxoSmithKline","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100004330","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institutes of Health National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01AI150275"],"award-info":[{"award-number":["R01AI150275"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institutes of Health National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01AI183884"],"award-info":[{"award-number":["R01AI183884"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institutes of Health National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01AI143295"],"award-info":[{"award-number":["R01AI143295"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100019650","name":"Vir Biotechnology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100019650","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012007","name":"Rockefeller University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012007","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004343","name":"Stavros Niarchos Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004343","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2025,11]]},"DOI":"10.1016\/j.jmb.2025.169182","type":"journal-article","created":{"date-parts":[[2025,4,30]],"date-time":"2025-04-30T23:03:44Z","timestamp":1746054224000},"page":"169182","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"title":["Hepatitis B Virus Nucleocapsid Assembly"],"prefix":"10.1016","volume":"437","author":[{"given":"Xupeng","family":"Hong","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William M.","family":"Schneider","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charles M.","family":"Rice","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2025.169182_b0005","unstructured":"WHO. Hepatitis B. World Health Organization; 2024."},{"key":"10.1016\/j.jmb.2025.169182_b0010","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1016\/0092-8674(92)90599-8","article-title":"The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis","volume":"71","author":"Wang","year":"1992","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2025.169182_b0015","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1128\/jvi.36.3.829-836.1980","article-title":"Virus of Pekin ducks with structural and biological relatedness to human hepatitis B virus","volume":"36","author":"Mason","year":"1980","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0020","doi-asserted-by":"crossref","first-page":"4533","DOI":"10.1073\/pnas.75.9.4533","article-title":"A virus similar to human hepatitis B virus associated with hepatitis and hepatoma in woodchucks","volume":"75","author":"Summers","year":"1978","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0025","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/j.chom.2017.07.019","article-title":"Deciphering the origin and evolution of hepatitis B viruses by means of a family of non-enveloped fish viruses","volume":"22","author":"Lauber","year":"2017","journal-title":"Cell Host Microbe."},{"key":"10.1016\/j.jmb.2025.169182_b0030","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2022373118","article-title":"Conservation of the HBV RNA element epsilon in nackednaviruses reveals ancient origin of protein-primed reverse transcription","volume":"118","author":"Beck","year":"2021","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0035","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/0092-8674(78)90245-3","article-title":"High frequency of aberrant expression of Moloney murine leukemia virus in clonal infections","volume":"14","author":"Shields","year":"1978","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2025.169182_b0040","doi-asserted-by":"crossref","first-page":"5757","DOI":"10.1128\/jvi.64.12.5757-5763.1990","article-title":"Role of the gag polyprotein precursor in packaging and maturation of Rous sarcoma virus genomic RNA","volume":"64","author":"Oertle","year":"1990","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0045","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1128\/jvi.70.2.880-886.1996","article-title":"trans-acting proteins involved in RNA encapsidation and viral assembly in human immunodeficiency virus type 1","volume":"70","author":"Kaye","year":"1996","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0050","doi-asserted-by":"crossref","first-page":"5969","DOI":"10.1128\/jvi.68.9.5969-5981.1994","article-title":"Efficiency and selectivity of RNA packaging by Rous sarcoma virus Gag deletion mutants","volume":"68","author":"Sakalian","year":"1994","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0055","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1038\/344552a0","article-title":"Polymerase gene products of hepatitis B viruses are required for genomic RNA packaging as well as for reverse transcription","volume":"344","author":"Hirsch","year":"1990","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2025.169182_b0060","doi-asserted-by":"crossref","first-page":"5324","DOI":"10.1128\/jvi.64.11.5324-5332.1990","article-title":"The P gene product of hepatitis B virus is required as a structural component for genomic RNA encapsidation","volume":"64","author":"Bartenschlager","year":"1990","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0065","doi-asserted-by":"crossref","first-page":"3413","DOI":"10.1002\/j.1460-2075.1992.tb05420.x","article-title":"Hepadnaviral assembly is initiated by polymerase binding to the encapsidation signal in the viral RNA genome","volume":"11","author":"Bartenschlager","year":"1992","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2025.169182_b0070","doi-asserted-by":"crossref","first-page":"3254","DOI":"10.1128\/jvi.67.6.3254-3263.1993","article-title":"An RNA stem-loop structure directs hepatitis B virus genomic RNA encapsidation","volume":"67","author":"Pollack","year":"1993","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0075","doi-asserted-by":"crossref","first-page":"5579","DOI":"10.1128\/jvi.68.9.5579-5587.1994","article-title":"Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis","volume":"68","author":"Pollack","year":"1994","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0080","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1002\/j.1460-2075.1990.tb07540.x","article-title":"A short cis\u2010acting sequence is required for hepatitis B virus pregenome encapsidation and sufficient for packaging of foreign RNA","volume":"9","author":"Junker-Niepmann","year":"1990","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2025.169182_b0085","doi-asserted-by":"crossref","first-page":"11447","DOI":"10.1128\/JVI.74.24.11447-11455.2000","article-title":"In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90","volume":"74","author":"Hu","year":"2000","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0090","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1128\/JVI.76.1.269-279.2002","article-title":"In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins","volume":"76","author":"Hu","year":"2002","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0095","doi-asserted-by":"crossref","first-page":"5134","DOI":"10.1128\/JVI.07137-11","article-title":"In vitro epsilon RNA-dependent protein priming activity of human hepatitis B virus polymerase","volume":"86","author":"Jones","year":"2012","journal-title":"J Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0100","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1010362","article-title":"Relaxing the restricted structural dynamics in the human hepatitis B virus RNA encapsidation signal enables replication initiation in vitro","volume":"18","author":"D\u00f6rnbrack","year":"2022","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0105","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1016\/S1097-2765(01)80009-5","article-title":"The crystal structure of the human hepatitis B virus capsid","volume":"3","author":"Wynne","year":"1999","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2025.169182_b0110","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1016\/0092-8674(94)90142-2","article-title":"Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy","volume":"77","author":"Crowther","year":"1994","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2025.169182_b0115","doi-asserted-by":"crossref","first-page":"48","DOI":"10.3748\/wjg.v13.i1.48","article-title":"Hepatitis B virus replication","volume":"13","author":"Beck","year":"2007","journal-title":"World J. Gastroenterol.: WJG"},{"key":"10.1016\/j.jmb.2025.169182_b0120","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a021386","article-title":"Hepadnavirus genome replication and persistence","volume":"5","author":"Hu","year":"2015","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"10.1016\/j.jmb.2025.169182_b0125","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.antiviral.2015.06.020","article-title":"Core protein: a pleiotropic keystone in the HBV lifecycle","volume":"121","author":"Zlotnick","year":"2015","journal-title":"Antiviral Res."},{"key":"10.1016\/j.jmb.2025.169182_b0130","doi-asserted-by":"crossref","first-page":"1577","DOI":"10.3390\/biomedicines9111577","article-title":"The hepatitis B virus nucleocapsid\u2014dynamic compartment for infectious virus production and new antiviral target","volume":"9","author":"Niklasch","year":"2021","journal-title":"Biomedicines"},{"key":"10.1016\/j.jmb.2025.169182_b0135","doi-asserted-by":"crossref","first-page":"642","DOI":"10.3390\/v15030642","article-title":"Hepatitis B virus capsid: the core in productive entry and covalently closed circular DNA formation","volume":"15","author":"Mendenhall","year":"2023","journal-title":"Viruses"},{"key":"10.1016\/j.jmb.2025.169182_b0140","doi-asserted-by":"crossref","first-page":"1759","DOI":"10.1002\/hep.21896","article-title":"Hepatitis B virus infection initiates with a large surface protein\u2013dependent binding to heparan sulfate proteoglycans","volume":"46","author":"Schulze","year":"2007","journal-title":"Hepatology"},{"key":"10.1016\/j.jmb.2025.169182_b0145","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.00049","article-title":"Sodium taurocholate cotransporting polypeptide is a functional receptor for human hepatitis B and D virus","volume":"1","author":"Yan","year":"2012","journal-title":"Elife"},{"key":"10.1016\/j.jmb.2025.169182_b0150","doi-asserted-by":"crossref","DOI":"10.1111\/cmi.13205","article-title":"Hepatitis B virus entry into HepG2\u2010NTCP cells requires clathrin\u2010mediated endocytosis","volume":"22","author":"Herrscher","year":"2020","journal-title":"Cell. Microbiol."},{"key":"10.1016\/j.jmb.2025.169182_b0155","doi-asserted-by":"crossref","first-page":"6415","DOI":"10.1128\/JVI.00393-13","article-title":"Regulation of hepatitis B virus infection by Rab5, Rab7, and the endolysosomal compartment","volume":"87","author":"Macovei","year":"2013","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0160","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.64507","article-title":"A fusion peptide in preS1 and the human protein disulfide isomerase ERp57 are involved in hepatitis B virus membrane fusion process","volume":"10","author":"P\u00e9rez-Vargas","year":"2021","journal-title":"Elife"},{"key":"10.1016\/j.jmb.2025.169182_b0165","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1006\/viro.1996.8376","article-title":"pH-independent uptake of hepatitis B virus in primary human hepatocytes","volume":"229","author":"Hagelstein","year":"1997","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2025.169182_b0170","doi-asserted-by":"crossref","first-page":"13057","DOI":"10.1128\/JVI.01495-07","article-title":"Entry of hepatitis delta virus requires the conserved cysteine residues of the hepatitis B virus envelope protein antigenic loop and is blocked by inhibitors of thiol-disulfide exchange","volume":"81","author":"Abou-Jaoud\u00e9","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0175","article-title":"Cryo-EM structures of human hepatitis B and woodchuck hepatitis virus small spherical subviral particles","volume":"8","author":"Liu","year":"2022","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jmb.2025.169182_b0180","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1000741","article-title":"Nucleoporin 153 arrests the nuclear import of hepatitis B virus capsids in the nuclear basket","volume":"6","author":"Schmitz","year":"2010","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0185","doi-asserted-by":"crossref","first-page":"9849","DOI":"10.1073\/pnas.1730940100","article-title":"Nuclear import of hepatitis B virus capsids and release of the viral genome","volume":"100","author":"Rabe","year":"2003","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0190","doi-asserted-by":"crossref","first-page":"8000","DOI":"10.3748\/wjg.v19.i44.8000","article-title":"Identification and characterization of a novel bipartite nuclear localization signal in the hepatitis B virus polymerase","volume":"19","author":"Lupberger","year":"2013","journal-title":"World J. Gastroenterol.: WJG"},{"key":"10.1016\/j.jmb.2025.169182_b0195","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1128\/jvi.68.1.6-13.1994","article-title":"Reverse transcription in hepatitis B viruses is primed by a tyrosine residue of the polymerase","volume":"68","author":"Zoulim","year":"1994","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0200","doi-asserted-by":"crossref","first-page":"8437","DOI":"10.1128\/jvi.68.12.8437-8442.1994","article-title":"Role of RNA in enzymatic activity of the reverse transcriptase of hepatitis B viruses","volume":"68","author":"Wang","year":"1994","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0205","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1016\/0092-8674(86)90602-1","article-title":"Formation of the pool of covalently closed circular viral DNA in hepadnavirus-infected cells","volume":"47","author":"Tuttleman","year":"1986","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2025.169182_b0210","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/0042-6822(90)90206-7","article-title":"In hepatocytes infected with duck hepatitis B virus, the template for viral RNA synthesis is amplified by an intracellular pathway","volume":"175","author":"Wu","year":"1990","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2025.169182_b0215","doi-asserted-by":"crossref","first-page":"6164","DOI":"10.1128\/JVI.02721-06","article-title":"Formation of hepatitis B virus covalently closed circular DNA: removal of genome-linked protein","volume":"81","author":"Gao","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0220","doi-asserted-by":"crossref","first-page":"12472","DOI":"10.1128\/JVI.01123-07","article-title":"Characterization of the intracellular deproteinized relaxed circular DNA of hepatitis B virus: an intermediate of covalently closed circular DNA formation","volume":"81","author":"Guo","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0225","doi-asserted-by":"crossref","first-page":"2129","DOI":"10.1073\/pnas.0308478100","article-title":"Expansion and contraction of the hepatitis B virus transcriptional template in infected chimpanzees","volume":"101","author":"Wieland","year":"2004","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0230","doi-asserted-by":"crossref","first-page":"794","DOI":"10.1016\/j.jhep.2020.11.003","article-title":"Transition to HBeAg-negative chronic hepatitis B virus infection is associated with reduced cccDNA transcriptional activity","volume":"74","author":"Suslov","year":"2021","journal-title":"J. Hepatol."},{"key":"10.1016\/j.jmb.2025.169182_b0235","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1128\/JVI.75.1.311-322.2001","article-title":"Kinetics of hepadnavirus loss from the liver during inhibition of viral DNA synthesis","volume":"75","author":"Zhu","year":"2001","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0240","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1001082","article-title":"Generation of covalently closed circular DNA of hepatitis B viruses via intracellular recycling is regulated in a virus specific manner","volume":"6","author":"K\u00f6ck","year":"2010","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0245","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1010739","article-title":"Constrained evolution of overlapping genes in viral host adaptation: acquisition of glycosylation motifs in hepadnaviral precore\/core genes","volume":"18","author":"Hong","year":"2022","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0250","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1002255","article-title":"Secretion of genome-free hepatitis B virus\u2013single strand blocking model for virion morphogenesis of para-retrovirus","volume":"7","author":"Ning","year":"2011","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0255","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01695-20","article-title":"Characterization of hepatitis B precore\/core-related antigens","volume":"95","author":"Hong","year":"2021","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0260","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1111\/jvh.12361","article-title":"Genome\u2010free hepatitis B virion levels in patient sera as a potential marker to monitor response to antiviral therapy","volume":"22","author":"Luckenbaugh","year":"2015","journal-title":"J. Viral Hepat."},{"key":"10.1016\/j.jmb.2025.169182_b0265","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00272-18","article-title":"Common and distinct capsid and surface protein requirements for secretion of complete and genome-free hepatitis B virions","volume":"92","author":"Ning","year":"2018","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0270","doi-asserted-by":"crossref","first-page":"5435","DOI":"10.1128\/jvi.65.10.5435-5439.1991","article-title":"Infection initiated by the RNA pregenome of a DNA virus","volume":"65","author":"Huang","year":"1991","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0275","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.adg6265","article-title":"An RNA-based system to study hepatitis B virus replication and evaluate antivirals","volume":"9","author":"Yu","year":"2023","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jmb.2025.169182_b0280","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.01150-22","article-title":"Pregenomic RNA Launch Hepatitis B virus replication system facilitates the mechanistic study of antiviral agents and drug-resistant variants on covalently closed circular DNA Synthesis","volume":"96","author":"Zhao","year":"2022","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0285","doi-asserted-by":"crossref","first-page":"6141","DOI":"10.1128\/jvi.64.12.6141-6147.1990","article-title":"The arginine-rich domain of hepatitis B virus precore and core proteins contains a signal for nuclear transport","volume":"64","author":"Yeh","year":"1990","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0290","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1001162","article-title":"Nuclear export and import of human hepatitis B virus capsid protein and particles","volume":"6","author":"Li","year":"2010","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0295","doi-asserted-by":"crossref","first-page":"5830","DOI":"10.1128\/JVI.00394-16","article-title":"Cell-free hepatitis B virus capsid assembly dependent on the core protein C-terminal domain and regulated by phosphorylation","volume":"90","author":"Ludgate","year":"2016","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0300","doi-asserted-by":"crossref","DOI":"10.1093\/emboj\/21.5.876","article-title":"The morphogenic linker peptide of HBV capsid protein forms a mobile array on the interior surface","author":"Watts","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2025.169182_b0305","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1007085","article-title":"Multiple roles of core protein linker in hepatitis B virus replication","volume":"14","author":"Liu","year":"2018","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0310","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1009230","article-title":"Multiple roles of PP2A binding motif in hepatitis B virus core linker and PP2A in regulating core phosphorylation state and viral replication","volume":"17","author":"Xi","year":"2021","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0315","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.00399-22","article-title":"Region-specific hepatitis B virus genome exposure from nucleocapsid modulated by capsid linker sequence and inhibitor: implications for uncoating","volume":"96","author":"Xi","year":"2022","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0320","doi-asserted-by":"crossref","first-page":"12950","DOI":"10.1128\/JVI.77.24.12950-12960.2003","article-title":"Stability and morphology comparisons of self-assembled virus-like particles from wild-type and mutant human hepatitis B virus capsid proteins","volume":"77","author":"Newman","year":"2003","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0325","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.1021\/acs.biochem.4c00077","article-title":"Guanidine hydrochloride-induced hepatitis B virus capsid disassembly hysteresis","volume":"63","author":"Khaykelson","year":"2024","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2025.169182_b0330","doi-asserted-by":"crossref","first-page":"11494","DOI":"10.1128\/JVI.01912-13","article-title":"Maturation-associated destabilization of hepatitis B virus nucleocapsid","volume":"87","author":"Cui","year":"2013","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0335","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1006\/jmbi.1997.1068","article-title":"Quasi-equivalent viruses: a paradigm for protein assemblies","volume":"269","author":"Johnson","year":"1997","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2025.169182_b0340","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1016\/j.molcel.2006.04.025","article-title":"Native hepatitis B virions and capsids visualized by electron cryomicroscopy","volume":"22","author":"Dryden","year":"2006","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2025.169182_b0345","doi-asserted-by":"crossref","first-page":"4307","DOI":"10.1128\/jvi.67.7.4307-4315.1993","article-title":"An intramolecular disulfide bridge between Cys-7 and Cys61 determines the structure of the secretory core gene product (e antigen) of hepatitis B virus","volume":"67","author":"Nassal","year":"1993","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0350","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1016\/S0021-9258(18)54079-5","article-title":"Structure of hepatitis B virus core and e-antigen. A single precore amino acid prevents nucleocapsid assembly","volume":"268","author":"Sch\u00f6del","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2025.169182_b0355","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1016\/0022-2836(92)90101-O","article-title":"Topological analysis of the hepatitis B virus core particle by cysteine-cysteine cross-linking","volume":"225","author":"Nassal","year":"1992","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2025.169182_b0360","doi-asserted-by":"crossref","first-page":"5393","DOI":"10.1128\/jvi.66.9.5393-5398.1992","article-title":"Cys residues of the hepatitis B virus capsid protein are not essential for the assembly of viral core particles but can influence their stability","volume":"66","author":"Zhou","year":"1992","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0365","doi-asserted-by":"crossref","first-page":"1314","DOI":"10.1016\/j.str.2018.06.012","article-title":"Structures of hepatitis b virus core-and e-antigen immune complexes suggest multi-point inhibition","volume":"26","author":"Eren","year":"2018","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2025.169182_b0370","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1016\/j.jmb.2010.03.026","article-title":"Molecular basis for the high degree of antigenic cross-reactivity between hepatitis B virus capsids (HBcAg) and dimeric capsid-related protein (HBeAg): insights into the enigmatic nature of the e-antigen","volume":"398","author":"Watts","year":"2010","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2025.169182_b0375","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.jmb.2011.03.049","article-title":"Role of the propeptide in controlling conformation and assembly state of hepatitis B virus e-antigen","volume":"409","author":"Watts","year":"2011","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2025.169182_b0380","doi-asserted-by":"crossref","DOI":"10.1128\/mbio.03501-22","article-title":"Characterization of intracellular precore-derived proteins and their functions in hepatitis B virus-infected human hepatocytes","volume":"14","author":"Hong","year":"2023","journal-title":"MBio"},{"key":"10.1016\/j.jmb.2025.169182_b0385","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1128\/jvi.71.1.345-353.1997","article-title":"Posttranscriptional regulation of hepatitis B virus replication by the precore protein","volume":"71","author":"Scaglioni","year":"1997","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0390","doi-asserted-by":"crossref","first-page":"1736","DOI":"10.1021\/bi801814y","article-title":"A mutant hepatitis B virus core protein mimics inhibitors of icosahedral capsid self-assembly","volume":"48","author":"Bourne","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2025.169182_b0395","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1128\/JVI.02033-09","article-title":"Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly","volume":"84","author":"Packianathan","year":"2010","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0400","doi-asserted-by":"crossref","first-page":"2735","DOI":"10.1016\/j.cell.2024.04.008","article-title":"Deep mutational scanning of hepatitis B virus reveals a mechanism for cis-preferential reverse transcription","volume":"187","author":"Yu","year":"2024","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2025.169182_b0405","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.virol.2008.06.021","article-title":"Characterization of the contribution of spliced RNAs of hepatitis B virus to DNA synthesis in transfected cultures of Huh7 and HepG2 cells","volume":"379","author":"Abraham","year":"2008","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2025.169182_b0410","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1111\/jvh.13702","article-title":"Secreted hepatitis B virus splice variants differ by HBV genotype and across phases of chronic hepatitis B infection","volume":"29","author":"Maslac","year":"2022","journal-title":"J. Viral Hepat."},{"key":"10.1016\/j.jmb.2025.169182_b0415","doi-asserted-by":"crossref","first-page":"1836","DOI":"10.1128\/jvi.65.4.1836-1842.1991","article-title":"Naturally occurring missense mutation in the polymerase gene terminating hepatitis B virus replication","volume":"65","author":"Blum","year":"1991","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0420","doi-asserted-by":"crossref","first-page":"5539","DOI":"10.1128\/jvi.65.10.5539-5543.1991","article-title":"Defective hepatitis B virus particles are generated by packaging and reverse transcription of spliced viral RNAs in vivo","volume":"65","author":"Terre","year":"1991","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0425","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/0042-6822(90)90005-C","article-title":"Encapsidation of truncated human hepatitis B virus genomes through trans-complementation of the core protein and polymerase","volume":"176","author":"Chiang","year":"1990","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2025.169182_b0430","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/S0042-6822(03)00142-9","article-title":"The duck hepatitis B virus polymerase and core proteins accumulate in different patterns from their common mRNA","volume":"311","author":"Yao","year":"2003","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2025.169182_b0435","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1074\/jbc.M208895200","article-title":"Kinetics of synthesis and turnover of the duck hepatitis B virus reverse transcriptase","volume":"278","author":"Yao","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2025.169182_b0440","doi-asserted-by":"crossref","first-page":"3353","DOI":"10.1099\/vir.0.80297-0","article-title":"Detection and characterization of cytoplasmic hepatitis B virus reverse transcriptase","volume":"85","author":"Cao","year":"2004","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0445","doi-asserted-by":"crossref","first-page":"8705","DOI":"10.1128\/JVI.01229-16","article-title":"Hepatitis B virus polymerase localizes to the mitochondria, and its terminal protein domain contains the mitochondrial targeting signal","volume":"90","author":"Unchwaniwala","year":"2016","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0450","doi-asserted-by":"crossref","first-page":"6124","DOI":"10.1093\/nar\/gkm628","article-title":"Chaperone activation of the hepadnaviral reverse transcriptase for template RNA binding is established by the Hsp70 and stimulated by the Hsp90 system","volume":"35","author":"Stahl","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2025.169182_b0455","doi-asserted-by":"crossref","first-page":"e4421","DOI":"10.1002\/pro.4421","article-title":"Predicted structure of the hepatitis B virus polymerase reveals an ancient conserved protein fold","volume":"31","author":"Tajwar","year":"2022","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0460","doi-asserted-by":"crossref","first-page":"13354","DOI":"10.1128\/JVI.01196-07","article-title":"Chaperones activate hepadnavirus reverse transcriptase by transiently exposing a C-proximal region in the terminal protein domain that contributes to \u03b5 RNA binding","volume":"81","author":"Stahl","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0465","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1038\/296677a0","article-title":"Electron microscopy of hepatitis B core antigen synthesized in E. coli","volume":"296","author":"Cohen","year":"1982","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2025.169182_b0470","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1128\/jvi.59.1.176-180.1986","article-title":"Expression of hepatitis B virus core antigen gene in Saccharomyces cerevisiae: synthesis of two polypeptides translated from different initiation codons","volume":"59","author":"Miyanohara","year":"1986","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0475","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/0042-6822(90)90247-O","article-title":"Expression of hepatitis B virus core and precore antigens in insect cells and characterization of a core-associated kinase activity","volume":"176","author":"Lanford","year":"1990","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2025.169182_b0480","doi-asserted-by":"crossref","first-page":"3086","DOI":"10.1128\/jvi.66.5.3086-3092.1992","article-title":"Characterization of hepatitis B virus capsid particle assembly in Xenopus oocytes","volume":"66","author":"Zhou","year":"1992","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0485","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1128\/jvi.17.3.885-893.1976","article-title":"Demonstration of subpopulations of Dane particles","volume":"17","author":"Kaplan","year":"1976","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0490","doi-asserted-by":"crossref","first-page":"4919","DOI":"10.1021\/bi00015a003","article-title":"Hepatitis core antigen produced in Escherichia coli: subunit composition, conformation analysis, and in vitro capsid assembly","volume":"34","author":"Wingfield","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2025.169182_b0495","doi-asserted-by":"crossref","first-page":"7174","DOI":"10.1128\/JVI.00586-10","article-title":"Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity","volume":"84","author":"Porterfield","year":"2010","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0500","article-title":"3.5 \u00c5 cryoEM structure of hepatitis B virus core assembled from full-length core protein","volume":"8","author":"Yu","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jmb.2025.169182_b0505","doi-asserted-by":"crossref","first-page":"15821","DOI":"10.1073\/pnas.0504874102","article-title":"A structural model for maturation of the hepatitis B virus core","volume":"102","author":"Roseman","year":"2005","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0510","doi-asserted-by":"crossref","DOI":"10.1002\/anie.202201083","article-title":"Fast magic-angle-spinning NMR reveals the evasive hepatitis\u2005B virus capsid C-terminal domain","volume":"61","author":"Callon","year":"2022","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.jmb.2025.169182_b0515","doi-asserted-by":"crossref","first-page":"3319","DOI":"10.1128\/jvi.64.7.3319-3330.1990","article-title":"Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein","volume":"64","author":"Birnbaum","year":"1990","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0520","doi-asserted-by":"crossref","first-page":"955","DOI":"10.1128\/jvi.61.4.955-961.1987","article-title":"In vivo phosphorylation and protein analysis of hepatitis B virus core antigen","volume":"61","author":"Roossinck","year":"1987","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0525","doi-asserted-by":"crossref","first-page":"2327","DOI":"10.1128\/jvi.65.5.2327-2331.1991","article-title":"Phosphorylation of hepatitis B virus precore and core proteins","volume":"65","author":"Yeh","year":"1991","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0530","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1128\/jvi.69.2.1025-1029.1995","article-title":"Phosphorylation and nuclear localization of the hepatitis B virus core protein: significance of serine in the three repeated SPRRR motifs","volume":"69","author":"Liao","year":"1995","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0535","doi-asserted-by":"crossref","first-page":"8754","DOI":"10.1128\/JVI.01343-14","article-title":"Phosphoacceptors threonine 162 and serines 170 and 178 within the carboxyl-terminal RRRS\/T motif of the hepatitis B virus core protein make multiple contributions to hepatitis B virus replication","volume":"88","author":"Jung","year":"2014","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0540","doi-asserted-by":"crossref","first-page":"8124","DOI":"10.1128\/JVI.76.16.8124-8137.2002","article-title":"Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein","volume":"76","author":"Daub","year":"2002","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0545","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1083\/jcb.125.1.99","article-title":"A eukaryotic cytosolic chaperonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle","volume":"125","author":"Lingappa","year":"1994","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jmb.2025.169182_b0550","doi-asserted-by":"crossref","first-page":"67","DOI":"10.3389\/fmolb.2019.00067","article-title":"Combining cell-free protein synthesis and NMR into a tool to study capsid assembly modulation","volume":"6","author":"Wang","year":"2019","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.jmb.2025.169182_b0555","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2022464118","article-title":"A pocket-factor\u2013triggered conformational switch in the hepatitis B virus capsid","volume":"118","author":"Lecoq","year":"2021","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0560","doi-asserted-by":"crossref","first-page":"4578","DOI":"10.1128\/jvi.64.9.4578-4581.1990","article-title":"Preferred translation of human hepatitis B virus polymerase from core protein-but not from precore protein-specific transcript","volume":"64","author":"Ou","year":"1990","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0565","series-title":"Methods in Enzymology","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/S0076-6879(96)75013-9","article-title":"Expression and characterization of hepadnavirus reverse transcriptases","author":"Hu","year":"1996"},{"key":"10.1016\/j.jmb.2025.169182_b0570","doi-asserted-by":"crossref","first-page":"1060","DOI":"10.1073\/pnas.93.3.1060","article-title":"Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase","volume":"93","author":"Hu","year":"1996","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0575","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1093\/emboj\/16.1.59","article-title":"Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids","volume":"16","author":"Hu","year":"1997","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2025.169182_b0580","doi-asserted-by":"crossref","first-page":"13122","DOI":"10.1128\/JVI.78.23.13122-13131.2004","article-title":"Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function","volume":"78","author":"Hu","year":"2004","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0585","doi-asserted-by":"crossref","first-page":"2141","DOI":"10.1128\/JVI.80.5.2141-2150.2006","article-title":"Hepatitis B virus reverse transcriptase and \u03b5 RNA sequences required for specific interaction in vitro","volume":"80","author":"Hu","year":"2006","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0590","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1128\/jvi.70.1.585-589.1996","article-title":"Specific hepatitis B virus minus-strand DNA synthesis requires only the 5'encapsidation signal and the 3'-proximal direct repeat DR1","volume":"70","author":"Rieger","year":"1996","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0595","doi-asserted-by":"crossref","first-page":"4431","DOI":"10.1128\/jvi.69.7.4431-4439.1995","article-title":"Nucleotide priming and reverse transcriptase activity of hepatitis B virus polymerase expressed in insect cells","volume":"69","author":"Lanford","year":"1995","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0600","doi-asserted-by":"crossref","first-page":"2996","DOI":"10.1128\/jvi.71.4.2996-3004.1997","article-title":"Transcomplementation of nucleotide priming and reverse transcription between independently expressed TP and RT domains of the hepatitis B virus reverse transcriptase","volume":"71","author":"Lanford","year":"1997","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0605","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1099\/0022-1317-79-5-1121","article-title":"In vitro activity of hepatitis B virus polymerase: requirement for distinct metal ions and the viral epsilon stem-loop","volume":"79","author":"Urban","year":"1998","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0610","doi-asserted-by":"crossref","first-page":"7410","DOI":"10.1128\/JVI.75.16.7410-7419.2001","article-title":"Reconstitution of a functional duck hepatitis B virus replication initiation complex from separate reverse transcriptase domains expressed in Escherichia coli","volume":"75","author":"Beck","year":"2001","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0615","doi-asserted-by":"crossref","first-page":"4471","DOI":"10.1128\/JVI.77.8.4471-4480.2003","article-title":"Heat shock protein 90-independent activation of truncated hepadnavirus reverse transcriptase","volume":"77","author":"Wang","year":"2003","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0620","doi-asserted-by":"crossref","first-page":"36128","DOI":"10.1074\/jbc.M301069200","article-title":"Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein","volume":"278","author":"Beck","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2025.169182_b0625","doi-asserted-by":"crossref","first-page":"3967","DOI":"10.1093\/nar\/21.17.3967","article-title":"The encapsidation signal on the hepatitis B virus RNA pregenome forms a stem-loop structure that is critical for its function","volume":"21","author":"Knaus","year":"1993","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2025.169182_b0630","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1008945","article-title":"Biogenesis and molecular characteristics of serum hepatitis B virus RNA","volume":"16","author":"Shen","year":"2020","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0635","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.00760-23","article-title":"Conditional replication and secretion of hepatitis B virus genome uncover the truncated 3\u2032 terminus of encapsidated viral pregenomic RNA","volume":"97","author":"Shen","year":"2023","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0640","doi-asserted-by":"crossref","first-page":"2179","DOI":"10.1128\/JVI.78.5.2179-2186.2004","article-title":"Underrepresentation of the 3\u2032 region of the capsid pregenomic RNA of duck hepatitis B virus","volume":"78","author":"Ostrow","year":"2004","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0645","doi-asserted-by":"crossref","first-page":"1357","DOI":"10.1016\/0092-8674(90)90431-D","article-title":"Translational inactivation of RNA function: discrimination against a subset of genomic transcripts during HBV nucleocapsid assembly","volume":"63","author":"Nassal","year":"1990","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2025.169182_b0650","doi-asserted-by":"crossref","first-page":"3067","DOI":"10.1128\/jvi.69.5.3067-3073.1995","article-title":"Mutations in the epsilon sequences of human hepatitis B virus affect both RNA encapsidation and reverse transcription","volume":"69","author":"Fallows","year":"1995","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0655","doi-asserted-by":"crossref","first-page":"3909","DOI":"10.1093\/nar\/23.19.3909","article-title":"Distinct requirements for primary sequence in the 5\u2032-and 3\u2032-part of a bulge in the hepatitis B virus RNA encapsidation signal revealed by a combined in vivo selection\/in vitro amplification system","volume":"23","author":"Rieger","year":"1995","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2025.169182_b0660","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1006\/viro.1994.1247","article-title":"The stem-loop structure of the cis-encapsidation signal is highly conserved in naturally occurring hepatitis B virus variants","volume":"200","author":"Laskus","year":"1994","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2025.169182_b0665","doi-asserted-by":"crossref","first-page":"2764","DOI":"10.1128\/jvi.70.5.2764-2773.1996","article-title":"A bulged region of the hepatitis B virus RNA encapsidation signal contains the replication origin for discontinuous first-strand DNA synthesis","volume":"70","author":"Nassal","year":"1996","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0670","doi-asserted-by":"crossref","first-page":"7120","DOI":"10.1038\/s41598-017-07657-z","article-title":"Few basepairing-independent motifs in the apical half of the avian HBV \u03b5 RNA stem-loop determine site-specific initiation of protein-priming","volume":"7","author":"Gajer","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jmb.2025.169182_b0675","doi-asserted-by":"crossref","first-page":"9761","DOI":"10.1080\/07391102.2021.1934544","article-title":"Structural insights of the conserved \u201cpriming loop\u201d of hepatitis B virus pre-genomic RNA","volume":"40","author":"LeBlanc","year":"2022","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.jmb.2025.169182_b0680","doi-asserted-by":"crossref","first-page":"4803","DOI":"10.1093\/nar\/gkf603","article-title":"The apical stem\u2013loop of the hepatitis B virus encapsidation signal folds into a stable tri\u2013loop with two underlying pyrimidine bulges","volume":"30","author":"Flodell","year":"2002","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2025.169182_b0685","doi-asserted-by":"crossref","first-page":"4449","DOI":"10.1093\/nar\/gkl582","article-title":"Solution structure of the apical stem\u2013loop of the human hepatitis B virus encapsidation signal","volume":"34","author":"Flodell","year":"2006","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2025.169182_b0690","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2022.167633","article-title":"Conformational dynamics of the hepatitis B virus pre-genomic RNA on multiple time scales: Implications for viral replication","volume":"434","author":"Olenginski","year":"2022","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2025.169182_b0695","doi-asserted-by":"crossref","first-page":"5741","DOI":"10.1128\/jvi.70.9.5741-5750.1996","article-title":"Evidence for activation of the hepatitis B virus polymerase by binding of its RNA template","volume":"70","author":"Tavis","year":"1996","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0700","doi-asserted-by":"crossref","first-page":"5789","DOI":"10.1128\/JVI.72.7.5789-5796.1998","article-title":"The duck hepatitis B virus polymerase is activated by its RNA packaging signal, \u025b","volume":"72","author":"Tavis","year":"1998","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0705","doi-asserted-by":"crossref","first-page":"6265","DOI":"10.1128\/MCB.18.11.6265","article-title":"Formation of a functional hepatitis B virus replication initiation complex involves a major structural alteration in the RNA template","volume":"18","author":"Beck","year":"1998","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.jmb.2025.169182_b0710","first-page":"1","article-title":"Accurate structure prediction of biomolecular interactions with AlphaFold 3","author":"Abramson","year":"2024","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2025.169182_b0715","doi-asserted-by":"crossref","first-page":"5502","DOI":"10.1128\/JVI.74.12.5502-5508.2000","article-title":"Evidence that the 5\u2032-end cap structure is essential for encapsidation of hepatitis B virus pregenomic RNA","volume":"74","author":"Jeong","year":"2000","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0720","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1128\/JVI.01232-09","article-title":"Incorporation of eukaryotic translation initiation factor eIF4E into viral nucleocapsids via interaction with hepatitis B virus polymerase","volume":"84","author":"Kim","year":"2010","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0725","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1038\/s41577-020-0288-3","article-title":"RIG-I-like receptors: their regulation and roles in RNA sensing","volume":"20","author":"Rehwinkel","year":"2020","journal-title":"Nature Rev. Immunol."},{"key":"10.1016\/j.jmb.2025.169182_b0730","doi-asserted-by":"crossref","first-page":"624","DOI":"10.1038\/ni.2048","article-title":"IFIT1 is an antiviral protein that recognizes 5\u2032-triphosphate RNA","volume":"12","author":"Pichlmair","year":"2011","journal-title":"Nature Immunol."},{"key":"10.1016\/j.jmb.2025.169182_b0735","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1038\/nature11783","article-title":"Structural basis for viral 5\u2032-PPP-RNA recognition by human IFIT proteins","volume":"494","author":"Abbas","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2025.169182_b0740","doi-asserted-by":"crossref","first-page":"9913","DOI":"10.1073\/pnas.0504273102","article-title":"Interferon prevents formation of replication-competent hepatitis B virus RNA-containing nucleocapsids","volume":"102","author":"Wieland","year":"2005","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0745","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.immuni.2014.12.016","article-title":"The RNA sensor RIG-I dually functions as an innate sensor and direct antiviral factor for hepatitis B virus","volume":"42","author":"Sato","year":"2015","journal-title":"Immunity"},{"key":"10.1016\/j.jmb.2025.169182_b0750","doi-asserted-by":"crossref","first-page":"2084","DOI":"10.1128\/jvi.68.4.2084-2090.1994","article-title":"Two regions of an avian hepadnavirus RNA pregenome are required in cis for encapsidation","volume":"68","author":"Calvert","year":"1994","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0755","doi-asserted-by":"crossref","first-page":"3309","DOI":"10.1128\/jvi.65.6.3309-3316.1991","article-title":"cis-acting sequences required for encapsidation of duck hepatitis B virus pregenomic RNA","volume":"65","author":"Hirsch","year":"1991","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0760","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1038\/s42003-021-02897-2","article-title":"In vitro functional analysis of gRNA sites regulating assembly of hepatitis B virus","volume":"4","author":"Patel","year":"2021","journal-title":"Commun. Biol."},{"key":"10.1016\/j.jmb.2025.169182_b0765","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/nmicrobiol.2017.98","article-title":"HBV RNA pre-genome encodes specific motifs that mediate interactions with the viral core protein that promote nucleocapsid assembly","volume":"2","author":"Patel","year":"2017","journal-title":"Nature Microbiol."},{"key":"10.1016\/j.jmb.2025.169182_b0770","doi-asserted-by":"crossref","first-page":"1564","DOI":"10.1128\/JVI.02852-13","article-title":"Comparative analysis of hepatitis B virus polymerase sequences required for viral RNA binding, RNA packaging, and protein priming","volume":"88","author":"Jones","year":"2014","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0775","doi-asserted-by":"crossref","first-page":"3617","DOI":"10.1128\/jvi.65.7.3617-3624.1991","article-title":"Pregenomic RNA encapsidation analysis of eleven missense and nonsense polymerase mutants of human hepatitis B virus","volume":"65","author":"Roychoudhury","year":"1991","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0780","doi-asserted-by":"crossref","first-page":"8032","DOI":"10.1128\/JVI.00332-09","article-title":"Four conserved cysteine residues of the hepatitis B virus polymerase are critical for RNA pregenome encapsidation","volume":"83","author":"Kim","year":"2009","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0785","doi-asserted-by":"crossref","first-page":"4107","DOI":"10.1128\/jvi.66.7.4107-4116.1992","article-title":"The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsidation and productive viral positive-strand DNA synthesis but not for virus assembly","volume":"66","author":"Nassal","year":"1992","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0790","doi-asserted-by":"crossref","first-page":"1871","DOI":"10.1128\/JVI.79.3.1871-1887.2005","article-title":"Exposure of RNA templates and encapsidation of spliced viral RNA are influenced by the arginine-rich domain of human hepatitis B virus core antigen (HBcAg 165-173)","volume":"79","author":"Le Pogam","year":"2005","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0795","doi-asserted-by":"crossref","first-page":"13812","DOI":"10.1128\/JVI.78.24.13812-13818.2004","article-title":"Hepatitis B virus nucleocapsids formed by carboxy-terminally mutated core proteins contain spliced viral genomes but lack full-size DNA","volume":"78","author":"K\u00f6ck","year":"2004","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0800","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1006\/viro.1999.9798","article-title":"Roles of the three major phosphorylation sites of hepatitis B virus core protein in viral replication","volume":"259","author":"Lan","year":"1999","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2025.169182_b0805","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.02139-17","article-title":"Hepatitis B virus core protein dephosphorylation occurs during pregenomic RNA encapsidation","volume":"92","author":"Zhao","year":"2018","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0810","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1008669","article-title":"Protein phosphatase 1 catalyzes HBV core protein dephosphorylation and is co-packaged with viral pregenomic RNA into nucleocapsids","volume":"16","author":"Hu","year":"2020","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0815","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1007488","article-title":"Hepatitis B virus core protein phosphorylation: identification of the SRPK1 target sites and impact of their occupancy on RNA binding and capsid structure","volume":"14","author":"Heger-Stevic","year":"2018","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0820","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00092-17","article-title":"Capsid Phosphorylation State and Hepadnavirus Virion Secretion","volume":"91","author":"Ning","year":"2017","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0825","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1012905","article-title":"HBV polymerase recruits the phosphatase PP1 to dephosphorylate HBc-Ser170 to complete encapsidation","volume":"21","author":"Hsieh","year":"2025","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0830","doi-asserted-by":"crossref","first-page":"11329","DOI":"10.1073\/pnas.1321424111","article-title":"Encapsidated hepatitis B virus reverse transcriptase is poised on an ordered RNA lattice","volume":"111","author":"Wang","year":"2014","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0835","doi-asserted-by":"crossref","first-page":"4377","DOI":"10.1093\/nar\/gkh772","article-title":"SELEX-derived aptamers of the duck hepatitis B virus RNA encapsidation signal distinguish critical and non-critical residues for productive initiation of reverse transcription","volume":"32","author":"Hu","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2025.169182_b0840","doi-asserted-by":"crossref","first-page":"11577","DOI":"10.1128\/JVI.01414-07","article-title":"The topology of hepatitis B virus pregenomic RNA promotes its replication","volume":"81","author":"Abraham","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0845","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/j.virol.2006.08.036","article-title":"Complementarity between epsilon and phi sequences in pregenomic RNA influences hepatitis B virus replication efficiency","volume":"359","author":"Oropeza","year":"2007","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2025.169182_b0850","doi-asserted-by":"crossref","first-page":"12237","DOI":"10.1128\/JVI.01218-12","article-title":"Cyclin-dependent kinase 2 phosphorylates s\/t-p sites in the hepadnavirus core protein C-terminal domain and is incorporated into viral capsids","volume":"86","author":"Ludgate","year":"2012","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0855","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00230-21","article-title":"Regulation of HBV Replication by Cyclin Docking Motifs in Core Protein","volume":"95","author":"Liu","year":"2021","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0860","doi-asserted-by":"crossref","first-page":"1750","DOI":"10.1002\/hep.29236","article-title":"Polo\u2010like\u2010kinase 1 is a proviral host factor for hepatitis B virus replication","volume":"66","author":"Diab","year":"2017","journal-title":"Hepatology"},{"key":"10.1016\/j.jmb.2025.169182_b0865","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1042\/BJ20060347","article-title":"Phosphorylation of hepatitis B virus Cp at Ser87 facilitates core assembly","volume":"398","author":"Kang","year":"2006","journal-title":"Biochem. J."},{"key":"10.1016\/j.jmb.2025.169182_b0870","doi-asserted-by":"crossref","first-page":"7993","DOI":"10.1128\/jvi.68.12.7993-8000.1994","article-title":"Effect of core protein phosphorylation by protein kinase C on encapsidation of RNA within core particles of hepatitis B virus","volume":"68","author":"Kann","year":"1994","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0875","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2201927119","article-title":"Autophagic membranes participate in hepatitis B virus nucleocapsid assembly, precore and core protein trafficking, and viral release","volume":"119","author":"Chu","year":"2022","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0880","doi-asserted-by":"crossref","first-page":"6803","DOI":"10.1128\/jvi.70.10.6803-6809.1996","article-title":"A host factor that binds near the termini of hepatitis B virus pregenomic RNA","volume":"70","author":"Perri","year":"1996","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0885","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1242\/jcs.00261","article-title":"hRUL138, a novel human RNA-binding RING-H2 ubiquitin-protein ligase","volume":"116","author":"Kreft","year":"2003","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0890","first-page":"1","article-title":"RBM24 stabilizes hepatitis B virus pregenomic RNA but inhibits core protein translation by targeting the terminal redundancy sequence","volume":"7","author":"Yao","year":"2018","journal-title":"Emerg. Microbes Infect."},{"key":"10.1016\/j.jmb.2025.169182_b0895","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.02161-18","article-title":"RNA-binding motif protein 24 (RBM24) is involved in pregenomic RNA packaging by mediating interaction between hepatitis B virus polymerase and the epsilon element","volume":"93","author":"Yao","year":"2019","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0900","doi-asserted-by":"crossref","DOI":"10.1016\/j.antiviral.2022.105249","article-title":"RNA-Binding motif protein 38 (RBM38) mediates HBV pgRNA packaging into the nucleocapsid","volume":"198","author":"Yao","year":"2022","journal-title":"Antiviral Res."},{"key":"10.1016\/j.jmb.2025.169182_b0905","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1038\/s41392-023-01573-7","article-title":"RNA binding protein TIAR modulates HBV replication by tipping the balance of pgRNA translation","volume":"8","author":"Zhang","year":"2023","journal-title":"Signal Transduct. Target. Ther."},{"key":"10.1016\/j.jmb.2025.169182_b0910","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1002\/hep.30329","article-title":"PAPD5\/7 are host factors that are required for hepatitis B virus RNA stabilization","volume":"69","author":"Mueller","year":"2019","journal-title":"Hepatology"},{"key":"10.1016\/j.jmb.2025.169182_b0915","article-title":"N6-methyladenosine modification of the 5\u2032 epsilon structure of the HBV pregenome RNA regulates its encapsidation by the viral core protein","volume":"119","author":"Kim","year":"2022","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0920","doi-asserted-by":"crossref","first-page":"8829","DOI":"10.1073\/pnas.1808319115","article-title":"N6-methyladenosine modification of hepatitis B virus RNA differentially regulates the viral life cycle","volume":"115","author":"Imam","year":"2018","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmb.2025.169182_b0925","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1128\/JVI.77.1.416-422.2003","article-title":"Mapping of amino acid side chains on the surface of hepatitis B virus capsids required for envelopment and virion formation","volume":"77","author":"Ponsel","year":"2003","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0930","doi-asserted-by":"crossref","first-page":"4165","DOI":"10.1128\/JVI.74.9.4165-4173.2000","article-title":"Intrahepatic induction of alpha\/beta interferon eliminates viral RNA-containing capsids in hepatitis B virus transgenic mice","volume":"74","author":"Wieland","year":"2000","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0935","doi-asserted-by":"crossref","first-page":"9332","DOI":"10.1128\/JVI.00918-10","article-title":"Interferons accelerate decay of replication-competent nucleocapsids of hepatitis B virus","volume":"84","author":"Xu","year":"2010","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0940","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1006296","article-title":"Interferon-inducible ribonuclease ISG20 inhibits hepatitis B virus replication through directly binding to the epsilon stem-loop structure of viral RNA","volume":"13","author":"Liu","year":"2017","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0945","doi-asserted-by":"crossref","first-page":"651","DOI":"10.3390\/v11070651","article-title":"Effects of Moloney leukemia virus 10 protein on hepatitis B virus infection and viral replication","volume":"11","author":"Puray-Chavez","year":"2019","journal-title":"Viruses"},{"key":"10.1016\/j.jmb.2025.169182_b0950","doi-asserted-by":"crossref","first-page":"19804","DOI":"10.1074\/jbc.RA119.009435","article-title":"The MOV10 helicase restricts hepatitis B virus replication by inhibiting viral reverse transcription","volume":"294","author":"Liu","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2025.169182_b0955","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003494","article-title":"Inhibition of hepatitis B virus replication by the host zinc finger antiviral protein","volume":"9","author":"Mao","year":"2013","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0960","doi-asserted-by":"crossref","first-page":"1829","DOI":"10.1126\/science.1092066","article-title":"Inhibition of hepatitis B virus replication by APOBEC3G","volume":"303","author":"Turelli","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.jmb.2025.169182_b0965","doi-asserted-by":"crossref","first-page":"6852","DOI":"10.1128\/JVI.00465-08","article-title":"Reverse transcriptase- and RNA packaging signal-dependent incorporation of APOBEC3G into hepatitis B virus nucleocapsids","volume":"82","author":"Nguyen","year":"2008","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0970","doi-asserted-by":"crossref","first-page":"4465","DOI":"10.1128\/JVI.02510-06","article-title":"Deamination-independent inhibition of hepatitis B virus reverse transcription by APOBEC3G","volume":"81","author":"Nguyen","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0975","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.02190-17","article-title":"Asymmetric modification of hepatitis B virus (HBV) genomes by an endogenous cytidine deaminase inside HBV cores informs a model of reverse transcription","volume":"92","author":"Nair","year":"2018","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0980","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1000928","article-title":"Massive APOBEC3 editing of hepatitis B viral DNA in cirrhosis","volume":"6","author":"Vartanian","year":"2010","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b0985","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00444-21","article-title":"RNA helicase DDX17 inhibits hepatitis B virus replication by blocking viral pregenomic RNA encapsidation","volume":"95","author":"Mao","year":"2021","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0990","doi-asserted-by":"crossref","first-page":"5815","DOI":"10.1128\/JVI.00011-09","article-title":"DDX3 DEAD-Box RNA helicase inhibits hepatitis B virus reverse transcription by incorporation into nucleocapsids","volume":"83","author":"Wang","year":"2009","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b0995","article-title":"Characterization of the host factors required for hepadnavirus covalently closed circular (ccc) DNA formation","volume":"7","author":"Guo","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.jmb.2025.169182_b1000","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1010633","article-title":"Host cell-dependent late entry step as determinant of hepatitis B virus infection","volume":"18","author":"Hong","year":"2022","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2025.169182_b1005","doi-asserted-by":"crossref","first-page":"6158","DOI":"10.1128\/jvi.69.10.6158-6169.1995","article-title":"High-level hepatitis B virus replication in transgenic mice","volume":"69","author":"Guidotti","year":"1995","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b1010","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1006\/viro.1996.0260","article-title":"Homologous and heterologous complementation of HBV and WHV capsid and polymerase functions in RNA encapsidation","volume":"219","author":"Ziermann","year":"1996","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2025.169182_b1015","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1099\/0022-1317-71-4-959","article-title":"Trans-complementation of the C gene of human and the P gene of woodchuck hepadnaviruses","volume":"71","author":"Okamoto","year":"1990","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b1020","doi-asserted-by":"crossref","first-page":"6931","DOI":"10.1128\/JVI.00582-13","article-title":"Sulfamoylbenzamide derivatives inhibit the assembly of hepatitis B virus nucleocapsids","volume":"87","author":"Campagna","year":"2013","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b1025","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1016\/0042-6822(92)90763-F","article-title":"Evidence for involvement of a ribosomal leaky scanning mechanism in the translation of the hepatitis B virus pol gene from the viral pregenome RNA","volume":"188","author":"Lin","year":"1992","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2025.169182_b1030","doi-asserted-by":"crossref","first-page":"4886","DOI":"10.1128\/jvi.67.8.4886-4895.1993","article-title":"Translation of the hepatitis B virus P gene by ribosomal scanning as an alternative to internal initiation","volume":"67","author":"Fouillot","year":"1993","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b1035","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1093\/nar\/gki251","article-title":"Translation of the first upstream ORF in the hepatitis B virus pregenomic RNA modulates translation at the core and polymerase initiation codons","volume":"33","author":"Chen","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2025.169182_b1040","doi-asserted-by":"crossref","first-page":"11751","DOI":"10.1128\/JVI.78.21.11751-11757.2004","article-title":"Translation of duck hepatitis B virus reverse transcriptase by ribosomal shunting","volume":"78","author":"Sen","year":"2004","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b1045","doi-asserted-by":"crossref","first-page":"6343","DOI":"10.1128\/JVI.00101-11","article-title":"RNA elements directing translation of the duck hepatitis B Virus polymerase via ribosomal shunting","volume":"85","author":"Cao","year":"2011","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b1050","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1016\/j.virol.2006.02.026","article-title":"Suppression of mRNA accumulation by the duck hepatitis B virus reverse transcriptase","volume":"350","author":"Cao","year":"2006","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2025.169182_b1055","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.virol.2007.11.010","article-title":"Hepatitis B virus polymerase suppresses translation of pregenomic RNA via a mechanism involving its interaction with 5\u2032 stem\u2013loop structure","volume":"373","author":"Ryu","year":"2008","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2025.169182_b1060","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1038\/s41575-022-00700-z","article-title":"Nomenclature of HBV core protein-targeting antivirals","volume":"19","author":"Zoulim","year":"2022","journal-title":"Nature Rev. Gastroenterol. Hepatol."},{"key":"10.1016\/j.jmb.2025.169182_b1065","doi-asserted-by":"crossref","DOI":"10.1016\/j.antiviral.2021.105080","article-title":"Identification of hepatitis B virus core protein residues critical for capsid assembly, pgRNA encapsidation and resistance to capsid assembly modulators","volume":"191","author":"Luo","year":"2021","journal-title":"Antiviral Res."},{"key":"10.1016\/j.jmb.2025.169182_b1070","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1021\/cb100275b","article-title":"Trapping of hepatitis B virus capsid assembly intermediates by phenylpropenamide assembly accelerators","volume":"5","author":"Katen","year":"2010","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.jmb.2025.169182_b1075","doi-asserted-by":"crossref","first-page":"2305","DOI":"10.1128\/JVI.02147-07","article-title":"Inhibition of hepadnavirus reverse transcriptase-\u03b5 RNA interaction by porphyrin compounds","volume":"82","author":"Lin","year":"2008","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b1080","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1080\/22221751.2021.1919034","article-title":"Hepatitis B virus nucleocapsid uncoating: biological consequences and regulation by cellular nucleases","author":"Hu","year":"2021","journal-title":"Emerg. Microbes Infect."},{"key":"10.1016\/j.jmb.2025.169182_b1085","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1128\/jvi.23.2.368-376.1977","article-title":"Structure of hepatitis B Dane particle DNA and nature of the endogenous DNA polymerase reaction","volume":"23","author":"Landers","year":"1977","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2025.169182_b1090","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1038\/s41564-020-0678-0","article-title":"Core components of DNA lagging strand synthesis machinery are essential for hepatitis B virus cccDNA formation","volume":"5","author":"Wei","year":"2020","journal-title":"Nature Microbiol."},{"key":"10.1016\/j.jmb.2025.169182_b1095","doi-asserted-by":"crossref","DOI":"10.1016\/j.jhepr.2022.100534","article-title":"Conversion of hepatitis B virus relaxed circular to covalently closed circular DNA is supported in murine cells","author":"Wei","year":"2022","journal-title":"JHEP Rep."},{"key":"10.1016\/j.jmb.2025.169182_b1100","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.1126\/science.1072266","article-title":"Chemical synthesis of poliovirus cDNA: generation of infectious virus in the absence of natural template","volume":"297","author":"Cello","year":"2002","journal-title":"Science"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283625002487?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283625002487?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,25]],"date-time":"2026-05-25T08:08:57Z","timestamp":1779696537000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283625002487"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,11]]},"references-count":220,"journal-issue":{"issue":"22","published-print":{"date-parts":[[2025,11]]}},"alternative-id":["S0022283625002487"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2025.169182","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2025,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Hepatitis B Virus Nucleocapsid Assembly","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2025.169182","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"169182"}}