{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,13]],"date-time":"2026-04-13T13:43:19Z","timestamp":1776087799346,"version":"3.50.1"},"reference-count":48,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2024,11,1]],"date-time":"2024-11-01T00:00:00Z","timestamp":1730419200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,11,1]],"date-time":"2024-11-01T00:00:00Z","timestamp":1730419200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,10,12]],"date-time":"2023-10-12T00:00:00Z","timestamp":1697068800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100012166","name":"National Key Research and Development Program of China","doi-asserted-by":"publisher","award":["2022YFA1303600"],"award-info":[{"award-number":["2022YFA1303600"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Genes & Diseases"],"published-print":{"date-parts":[[2024,11]]},"DOI":"10.1016\/j.gendis.2023.101142","type":"journal-article","created":{"date-parts":[[2023,10,14]],"date-time":"2023-10-14T06:56:47Z","timestamp":1697266607000},"page":"101142","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":4,"title":["The proteasome activator subunit PSME1 promotes HBV replication by inhibiting the degradation of HBV core protein"],"prefix":"10.1016","volume":"11","author":[{"given":"Yu","family":"Liu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jiaxin","family":"Yang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yanyan","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Qiqi","family":"Zeng","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yao","family":"Fan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ailong","family":"Huang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hui","family":"Fan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"1","key":"10.1016\/j.gendis.2023.101142_bib1","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1002\/hep.32314","article-title":"Getting to HBV cure: the promising paths forward","volume":"76","author":"Fung","year":"2022","journal-title":"Hepatology"},{"issue":"1","key":"10.1016\/j.gendis.2023.101142_bib2","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1128\/MMBR.64.1.51-68.2000","article-title":"Hepatitis B virus biology","volume":"64","author":"Seeger","year":"2000","journal-title":"Microbiol Mol Biol Rev"},{"issue":"4","key":"10.1016\/j.gendis.2023.101142_bib3","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1016\/j.tim.2018.01.009","article-title":"Hepatitis B virus","volume":"26","author":"Shih","year":"2018","journal-title":"Trends Microbiol"},{"issue":"6","key":"10.1016\/j.gendis.2023.101142_bib4","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/S2468-1253(18)30056-6","article-title":"Global prevalence, treatment, and prevention of hepatitis B virus infection in 2016: a modelling study","volume":"3","author":"Collaborators","year":"2018","journal-title":"Lancet Gastroenterol Hepatol"},{"issue":"10381","key":"10.1016\/j.gendis.2023.101142_bib5","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1016\/S0140-6736(22)01468-4","article-title":"Hepatitis B","volume":"401","author":"Jeng","year":"2023","journal-title":"Lancet."},{"issue":"4","key":"10.1016\/j.gendis.2023.101142_bib6","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1016\/j.jhep.2009.10.033","article-title":"Mechanisms of HBV-related hepatocarcinogenesis","volume":"52","author":"Neuveut","year":"2010","journal-title":"J Hepatol"},{"issue":"5","key":"10.1016\/j.gendis.2023.101142_bib7","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1111\/apt.17105","article-title":"Review article: novel biomarkers in hepatitis B infection","volume":"56","author":"Lok","year":"2022","journal-title":"Aliment Pharmacol Ther"},{"issue":"12","key":"10.1016\/j.gendis.2023.101142_bib8","doi-asserted-by":"crossref","first-page":"1972","DOI":"10.1136\/gutjnl-2015-309809","article-title":"HBV cccDNA: viral persistence reservoir and key obstacle for a cure of chronic hepatitis B","volume":"64","author":"Nassal","year":"2015","journal-title":"Gut"},{"issue":"1","key":"10.1016\/j.gendis.2023.101142_bib9","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.virol.2010.07.005","article-title":"Proximity between the cap and 5\u2032 epsilon stem-loop structure is critical for the suppression of pgRNA translation by the hepatitis B viral polymerase","volume":"406","author":"Ryu","year":"2010","journal-title":"Virology"},{"issue":"1","key":"10.1016\/j.gendis.2023.101142_bib10","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-loop structure","volume":"373","author":"Ryu","year":"2008","journal-title":"Virology"},{"issue":"7","key":"10.1016\/j.gendis.2023.101142_bib11","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"},{"issue":"47","key":"10.1016\/j.gendis.2023.101142_bib12","doi-asserted-by":"crossref","first-page":"28584","DOI":"10.1074\/jbc.M115.678441","article-title":"Hepatitis B virus core protein phosphorylation sites affect capsid stability and transient exposure of the C-terminal domain","volume":"290","author":"Selzer","year":"2015","journal-title":"J Biol Chem"},{"issue":"4","key":"10.1016\/j.gendis.2023.101142_bib13","doi-asserted-by":"crossref","first-page":"1641","DOI":"10.1128\/JVI.01671-06","article-title":"Regulation of hepadnavirus reverse transcription by dynamic nucleocapsid phosphorylation","volume":"81","author":"Basagoudanavar","year":"2007","journal-title":"J Virol"},{"key":"10.1016\/j.gendis.2023.101142_bib14","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.antiviral.2017.11.015","article-title":"The diverse functions of the hepatitis B core\/capsid protein (HBc) in the viral life cycle: implications for the development of HBc-targeting antivirals","volume":"149","author":"Diab","year":"2018","journal-title":"Antivir Res"},{"issue":"17","key":"10.1016\/j.gendis.2023.101142_bib15","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 USA"},{"issue":"3","key":"10.1016\/j.gendis.2023.101142_bib16","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1016\/j.jhep.2021.05.013","article-title":"Covalently closed circular DNA: the ultimate therapeutic target for curing HBV infections","volume":"75","author":"Martinez","year":"2021","journal-title":"J Hepatol"},{"issue":"3","key":"10.1016\/j.gendis.2023.101142_bib17","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1038\/nprot.2016.018","article-title":"Spatially resolved proteomic mapping in living cells with the engineered peroxidase APEX2","volume":"11","author":"Hung","year":"2016","journal-title":"Nat Protoc"},{"issue":"1","key":"10.1016\/j.gendis.2023.101142_bib18","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/s41467-020-20367-x","article-title":"Spatiotemporal profiling of cytosolic signaling complexes in living cells by selective proximity proteomics","volume":"12","author":"Ke","year":"2021","journal-title":"Nat Commun"},{"issue":"1","key":"10.1016\/j.gendis.2023.101142_bib19","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1038\/nmeth.3179","article-title":"Directed evolution of APEX2 for electron microscopy and proximity labeling","volume":"12","author":"Lam","year":"2015","journal-title":"Nat Methods"},{"issue":"34","key":"10.1016\/j.gendis.2023.101142_bib20","doi-asserted-by":"crossref","first-page":"11763","DOI":"10.1002\/anie.201905949","article-title":"Expanding APEX2 substrates for proximity-dependent labeling of nucleic acids and proteins in living cells","volume":"58","author":"Zhou","year":"2019","journal-title":"Angew Chem Int Ed Engl"},{"issue":"2","key":"10.1016\/j.gendis.2023.101142_bib21","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1152\/physrev.00027.2001","article-title":"The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction","volume":"82","author":"Glickman","year":"2002","journal-title":"Physiol Rev"},{"issue":"9","key":"10.1016\/j.gendis.2023.101142_bib22","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1007\/s00018-011-0657-y","article-title":"The role of the proteasome in the generation of MHC class I ligands and immune responses","volume":"68","author":"Sijts","year":"2011","journal-title":"Cell Mol Life Sci"},{"issue":"4","key":"10.1016\/j.gendis.2023.101142_bib23","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1002\/eji.201041040","article-title":"PA28 and the proteasome immunosubunits play a central and independent role in the production of MHC class I-binding peptides in vivo","volume":"41","author":"de Graaf","year":"2011","journal-title":"Eur J Immunol"},{"issue":"15","key":"10.1016\/j.gendis.2023.101142_bib24","doi-asserted-by":"crossref","first-page":"10515","DOI":"10.1016\/S0021-9258(19)50047-3","article-title":"Identification, purification, and characterization of a protein activator (PA28) of the 20 S proteasome (macropain)","volume":"267","author":"Ma","year":"1992","journal-title":"J Biol Chem"},{"issue":"34","key":"10.1016\/j.gendis.2023.101142_bib25","doi-asserted-by":"crossref","first-page":"13791","DOI":"10.1073\/pnas.1300013110","article-title":"Proteasome activator complex PA28 identified as an accessible target in prostate cancer by in vivo selection of human antibodies","volume":"110","author":"S\u00e1nchez-Mart\u00edn","year":"2013","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.gendis.2023.101142_bib26","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1186\/s13046-016-0309-z","article-title":"Overexpression of proteasomal activator PA28\u03b1 serves as a prognostic factor in oral squamous cell carcinoma","volume":"35","author":"Feng","year":"2016","journal-title":"J Exp Clin Cancer Res"},{"key":"10.1016\/j.gendis.2023.101142_bib27","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1038\/s41408-020-00393-0","article-title":"Downregulation of PA28\u03b1 induces proteasome remodeling and results in resistance to proteasome inhibitors in multiple myeloma","volume":"10","author":"Gu","year":"2020","journal-title":"Blood Cancer J"},{"issue":"2","key":"10.1016\/j.gendis.2023.101142_bib28","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/j.bbrc.2010.05.104","article-title":"Studies on immunoproteasome in human liver. Part I: absence in fetuses, presence in normal subjects, and increased levels in chronic active hepatitis and cirrhosis","volume":"397","author":"Vasuri","year":"2010","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.gendis.2023.101142_bib29","article-title":"Proteomic characterization of the natural history of chronic HBV infection revealed by tandem mass tag-based quantitative proteomics approach","volume":"15","author":"Xun","year":"2022","journal-title":"Mater Today Bio"},{"key":"10.1016\/j.gendis.2023.101142_bib30","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1038\/s41419-022-04852-3","article-title":"PRKDC promotes hepatitis B virus transcription through enhancing the binding of RNA Pol II to cccDNA","volume":"13","author":"Fan","year":"2022","journal-title":"Cell Death Dis"},{"issue":"11","key":"10.1016\/j.gendis.2023.101142_bib31","doi-asserted-by":"crossref","first-page":"2039","DOI":"10.1016\/j.jmb.2015.03.005","article-title":"Bimolecular fluorescence complementation (BiFC) analysis: advances and recent applications for genome-wide interaction studies","volume":"427","author":"Miller","year":"2015","journal-title":"J Mol Biol"},{"issue":"5","key":"10.1016\/j.gendis.2023.101142_bib32","doi-asserted-by":"crossref","first-page":"285","DOI":"10.2144\/000113943","article-title":"Bimolecular fluorescence complementation (BiFC): a 5-year update and future perspectives","volume":"53","author":"Kodama","year":"2012","journal-title":"Biotechniques"},{"key":"10.1016\/j.gendis.2023.101142_bib33","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1146\/annurev.biophys.37.032807.125842","article-title":"Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells","volume":"37","author":"Kerppola","year":"2008","journal-title":"Annu Rev Biophys"},{"issue":"9","key":"10.1016\/j.gendis.2023.101142_bib34","doi-asserted-by":"crossref","first-page":"998","DOI":"10.1093\/abbs\/gmaa073","article-title":"Strategies to improve the fluorescent signal of the tripartite sfGFP system","volume":"52","author":"Shen","year":"2020","journal-title":"Acta Biochim Biophys Sin"},{"key":"10.1016\/j.gendis.2023.101142_bib35","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":"Antivir Res"},{"issue":"12","key":"10.1016\/j.gendis.2023.101142_bib36","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"},{"issue":"5","key":"10.1016\/j.gendis.2023.101142_bib37","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.gendis.2023.101142_bib38","doi-asserted-by":"crossref","first-page":"m2200","DOI":"10.1136\/bmj.m2200","article-title":"Hepatitis B virus persistence and reactivation","volume":"370","author":"Shi","year":"2020","journal-title":"BMJ"},{"issue":"2","key":"10.1016\/j.gendis.2023.101142_bib39","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005438","article-title":"Transcriptome-wide analysis of hepatitis B virus-mediated changes to normal hepatocyte gene expression","volume":"12","author":"Lamontagne","year":"2016","journal-title":"PLoS Pathog"},{"issue":"1","key":"10.1016\/j.gendis.2023.101142_bib40","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.jhep.2021.02.009","article-title":"Translatomic profiling reveals novel self-restricting virus-host interactions during HBV infection","volume":"75","author":"Yuan","year":"2021","journal-title":"J Hepatol"},{"key":"10.1016\/j.gendis.2023.101142_bib41","article-title":"Multi-omics analyses reveal metabolic alterations regulated by hepatitis B virus core protein in hepatocellular carcinoma cells","volume":"7","author":"Xie","year":"2017","journal-title":"Sci Rep"},{"issue":"11","key":"10.1016\/j.gendis.2023.101142_bib42","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1008593","article-title":"Hepatitis B virus core protein nuclear interactome identifies SRSF10 as a host RNA-binding protein restricting HBV RNA production","volume":"16","author":"Chabrolles","year":"2020","journal-title":"PLoS Pathog"},{"issue":"6","key":"10.1016\/j.gendis.2023.101142_bib43","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1016\/j.jiph.2021.03.009","article-title":"Quantitative proteomics analysis reveals unique but overlapping protein signatures in HIV infections","volume":"14","author":"Al-Mozaini","year":"2021","journal-title":"J Infect Public Health"},{"issue":"3","key":"10.1016\/j.gendis.2023.101142_bib44","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0173259","article-title":"PA28 modulates antigen processing and viral replication during coxsackievirus B3 infection","volume":"12","author":"Respondek","year":"2017","journal-title":"PLoS One"},{"issue":"11","key":"10.1016\/j.gendis.2023.101142_bib45","doi-asserted-by":"crossref","first-page":"2197","DOI":"10.1074\/mcp.RA118.000735","article-title":"Comprehensive proteomics identification of IFN-\u03bb3-regulated antiviral proteins in HBV-transfected cells","volume":"17","author":"Makjaroen","year":"2018","journal-title":"Mol Cell Proteomics"},{"issue":"7","key":"10.1016\/j.gendis.2023.101142_bib46","doi-asserted-by":"crossref","first-page":"2144","DOI":"10.1053\/j.gastro.2008.02.063","article-title":"Proteasome activation by hepatitis C core protein is reversed by ethanol-induced oxidative stress","volume":"134","author":"Osna","year":"2008","journal-title":"Gastroenterology"},{"issue":"3","key":"10.1016\/j.gendis.2023.101142_bib47","first-page":"577","article-title":"Proteomic identification of down-regulation of oncoprotein DJ-1 and proteasome activator subunit 1 in hepatitis B virus-infected well-differentiated hepatocellular carcinoma","volume":"31","author":"Zhang","year":"2007","journal-title":"Int J Oncol"},{"issue":"12","key":"10.1016\/j.gendis.2023.101142_bib48","doi-asserted-by":"crossref","first-page":"3961","DOI":"10.1096\/fj.201600698R","article-title":"LC3\/GABARAP family proteins: autophagy-(un)related functions","volume":"30","author":"Schaaf","year":"2016","journal-title":"FASEB J"}],"container-title":["Genes & Diseases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2352304223004257?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2352304223004257?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,9,15]],"date-time":"2024-09-15T11:36:54Z","timestamp":1726400214000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2352304223004257"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,11]]},"references-count":48,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2024,11]]}},"alternative-id":["S2352304223004257"],"URL":"https:\/\/doi.org\/10.1016\/j.gendis.2023.101142","relation":{},"ISSN":["2352-3042"],"issn-type":[{"value":"2352-3042","type":"print"}],"subject":[],"published":{"date-parts":[[2024,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The proteasome activator subunit PSME1 promotes HBV replication by inhibiting the degradation of HBV core protein","name":"articletitle","label":"Article Title"},{"value":"Genes & Diseases","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.gendis.2023.101142","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 The Authors. Publishing services by Elsevier B.V. on behalf of KeAi Communications Co., Ltd.","name":"copyright","label":"Copyright"}],"article-number":"101142"}}