{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T07:52:21Z","timestamp":1791532341324,"version":"4.3.4"},"reference-count":67,"publisher":"Oxford University Press (OUP)","issue":"11","funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["ZIA EB000095-04"],"award-info":[{"award-number":["ZIA EB000095-04"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R21AI59666"],"award-info":[{"award-number":["R21AI59666"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["U19 AI135990"],"award-info":[{"award-number":["U19 AI135990"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["75N91019D00024"],"award-info":[{"award-number":["75N91019D00024"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,6,24]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The viral genome of SARS-CoV-2 is packaged by the nucleocapsid (N-)protein into ribonucleoprotein particles (RNPs), 38\u00a0\u00b1\u00a010 of which are contained in each virion. Their architecture has remained unclear due to the pleomorphism of RNPs, the high flexibility of N-protein intrinsically disordered regions, and highly multivalent interactions between viral RNA and N-protein binding sites in both N-terminal (NTD) and C-terminal domain (CTD). Here we explore critical interaction motifs of RNPs by applying a combination of biophysical techniques to ancestral and\u00a0mutant proteins binding different nucleic acids in an in vitro assay for RNP formation, and by examining nucleocapsid\u00a0protein variants in a viral assembly assay. We find that nucleic acid-bound N-protein dimers oligomerize via a recently described protein\u2013protein interface presented by a transient helix in its long disordered linker region between NTD and CTD. The resulting hexameric complexes are stabilized by multivalent protein-nucleic acid interactions that establish crosslinks between dimeric subunits. Assemblies are stabilized by the dimeric CTD of N-protein offering more than one binding site for stem\u2013loop RNA. Our study suggests a model for RNP assembly where N-protein scaffolding at high density on viral RNA is followed by cooperative multimerization through protein\u2013protein interactions in the disordered linker.<\/jats:p>","DOI":"10.1093\/nar\/gkae256","type":"journal-article","created":{"date-parts":[[2024,4,8]],"date-time":"2024-04-08T07:06:25Z","timestamp":1712559985000},"page":"6647-6661","source":"Crossref","is-referenced-by-count":47,"title":["Assembly of SARS-CoV-2 nucleocapsid protein with nucleic acid"],"prefix":"10.1093","volume":"52","author":[{"given":"Huaying","family":"Zhao","sequence":"first","affiliation":[{"name":"Laboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health , Bethesda , MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abdullah M","family":"Syed","sequence":"additional","affiliation":[{"name":"Gladstone Institutes , San Francisco , CA 94158, USA"},{"name":"Innovative Genomics Institute, University of California , Berkeley , CA 94720, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mir M","family":"Khalid","sequence":"additional","affiliation":[{"name":"Gladstone Institutes , San Francisco , CA 94158, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ai","family":"Nguyen","sequence":"additional","affiliation":[{"name":"Laboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health , Bethesda , MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alison","family":"Ciling","sequence":"additional","affiliation":[{"name":"Gladstone Institutes , San Francisco , CA 94158, USA"},{"name":"Innovative Genomics Institute, University of California , Berkeley , CA 94720, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3440-1860","authenticated-orcid":false,"given":"Di","family":"Wu","sequence":"additional","affiliation":[{"name":"Biophysics Core Facility, National Heart, Lung, and Blood Institute, National Institutes of Health , Bethesda , MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wai-Ming","family":"Yau","sequence":"additional","affiliation":[{"name":"Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health , Bethesda , MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sanjana","family":"Srinivasan","sequence":"additional","affiliation":[{"name":"Laboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health , Bethesda , MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominic","family":"Esposito","sequence":"additional","affiliation":[{"name":"Protein Expression Laboratory, Frederick National Laboratory for Cancer Research , Frederick , MD 21702, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jennifer\u00a0A","family":"Doudna","sequence":"additional","affiliation":[{"name":"Gladstone Institutes , San Francisco , CA 94158, USA"},{"name":"Department of Molecular and Cell Biology, University of California , Berkeley , CA 94720, USA"},{"name":"HHMI, University of California , Berkeley , CA 94720, USA"},{"name":"Department of Chemistry, University of California , Berkeley , CA 94720, USA"},{"name":"Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory , Berkeley , CA 94720, USA"},{"name":"California Institute for Quantitative Biosciences (QB3), University of California , Berkeley , CA 94720, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5270-3678","authenticated-orcid":false,"given":"Grzegorz","family":"Piszczek","sequence":"additional","affiliation":[{"name":"Biophysics Core Facility, National Heart, Lung, and Blood Institute, National Institutes of Health , Bethesda , MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Melanie","family":"Ott","sequence":"additional","affiliation":[{"name":"Gladstone Institutes , San Francisco , CA 94158, USA"},{"name":"Department of Medicine, University of California , San Francisco , CA 94143, USA"},{"name":"Chan Zuckerberg Biohub, San Francisco , CA 94158, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8859-6966","authenticated-orcid":false,"given":"Peter","family":"Schuck","sequence":"additional","affiliation":[{"name":"Laboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health , Bethesda , MD 20892, USA"},{"name":"Center for Biomedical Engineering Technology Acceleration, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health , Bethesda , MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2024,4,8]]},"reference":[{"key":"2024062323555045100_B1","doi-asserted-by":"crossref","first-page":"253","DOI":"10.3390\/v11030253","article-title":"Packaging of genomic RNA in positive-sense single-stranded RNA viruses: a complex story","volume":"11","author":"Comas-Garcia","year":"2019","journal-title":"Viruses"},{"key":"2024062323555045100_B2","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.sbi.2011.11.002","article-title":"Nucleic acid packaging in viruses","volume":"22","author":"Speir","year":"2012","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2024062323555045100_B3","doi-asserted-by":"crossref","first-page":"5885","DOI":"10.1038\/s41467-020-19619-7","article-title":"SARS-CoV-2 structure and replication characterized by in situ cryo-electron tomography","volume":"11","author":"Klein","year":"2020","journal-title":"Nat. Commun."},{"key":"2024062323555045100_B4","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1016\/j.cell.2020.09.018","article-title":"Molecular architecture of the SARS-CoV-2 virus","volume":"183","author":"Yao","year":"2020","journal-title":"Cell"},{"key":"2024062323555045100_B5","doi-asserted-by":"crossref","first-page":"1395","DOI":"10.1126\/science.abd3629","article-title":"A molecular pore spans the double membrane of the coronavirus replication organelle","volume":"369","author":"Wolff","year":"2020","journal-title":"Science"},{"key":"2024062323555045100_B6","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1002\/wrna.1326","article-title":"Nucleocapsid proteins: roles beyond viral RNA packaging","volume":"7","author":"Ding","year":"2016","journal-title":"Wiley Interdiscip. Rev. RNA"},{"key":"2024062323555045100_B7","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/j.virol.2019.08.031","article-title":"Coronavirus genomic RNA packaging","volume":"537","author":"Masters","year":"2019","journal-title":"Virology"},{"key":"2024062323555045100_B8","doi-asserted-by":"crossref","first-page":"e02388-23","DOI":"10.1128\/mBio.02371-21","article-title":"Betacoronavirus assembly: clues and perspectives for elucidating SARS-CoV-2 particle formation and egress","volume":"12","author":"Bracquemond","year":"2021","journal-title":"mBio"},{"key":"2024062323555045100_B9","doi-asserted-by":"crossref","first-page":"4629","DOI":"10.1038\/s41467-021-24887-y","article-title":"Correlative multi-scale cryo-imaging unveils SARS-CoV-2 assembly and egress","volume":"12","author":"Mendon\u00e7a","year":"2021","journal-title":"Nat. Commun."},{"key":"2024062323555045100_B10","doi-asserted-by":"crossref","first-page":"237","DOI":"10.4161\/rna.8.2.14991","article-title":"RNA-RNA and RNA-protein interactions in coronavirus replication and transcription","volume":"8","author":"Sola","year":"2011","journal-title":"RNA Biol."},{"key":"2024062323555045100_B11","doi-asserted-by":"crossref","first-page":"166875","DOI":"10.1016\/j.jmb.2021.166875","article-title":"The mechanism of SARS-CoV-2 nucleocapsid protein recognition by the Human 14-3-3 proteins","volume":"433","author":"Tugaeva","year":"2021","journal-title":"J. Mol. Biol."},{"key":"2024062323555045100_B12","doi-asserted-by":"crossref","first-page":"e2024815118","DOI":"10.1073\/pnas.2024815118","article-title":"The total number and mass of SARS-CoV-2 virions","volume":"118","author":"Sender","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2024062323555045100_B13","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1186\/s12985-023-01968-6","article-title":"The SARS-CoV-2 nucleocapsid protein: its role in the viral life cycle, structure and functions, and use as a potential target in the development of vaccines and diagnostics","volume":"20","author":"Wu","year":"2023","journal-title":"Virol. J."},{"key":"2024062323555045100_B14","doi-asserted-by":"crossref","first-page":"e2164219","DOI":"10.1080\/22221751.2022.2164219","article-title":"The role of SARS-CoV-2 nucleocapsid protein in antiviral immunity and vaccine development","volume":"12","author":"Yu","year":"2023","journal-title":"Emerg. Microbes Infect."},{"key":"2024062323555045100_B15","doi-asserted-by":"crossref","first-page":"e02388-23","DOI":"10.1128\/mbio.02388-23","article-title":"Diversity of short linear interaction motifs in SARS-CoV-2 nucleocapsid protein","volume":"14","author":"Schuck","year":"2023","journal-title":"mBio"},{"key":"2024062323555045100_B16","doi-asserted-by":"crossref","first-page":"3331","DOI":"10.1038\/s41467-023-38882-y","article-title":"The preference signature of the SARS-CoV-2 nucleocapsid NTD for its 5\u2032-genomic RNA elements","volume":"14","author":"Korn","year":"2023","journal-title":"Nat. Commun."},{"key":"2024062323555045100_B17","doi-asserted-by":"crossref","first-page":"6041","DOI":"10.1038\/s41467-020-19843-1","article-title":"Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates","volume":"11","author":"Savastano","year":"2020","journal-title":"Nat. Commun."},{"key":"2024062323555045100_B18","doi-asserted-by":"crossref","first-page":"8168","DOI":"10.1093\/nar\/gkac596","article-title":"Double-stranded RNA drives SARS-CoV-2 nucleocapsid protein to undergo phase separation at specific temperatures","volume":"50","author":"Roden","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"2024062323555045100_B19","doi-asserted-by":"crossref","first-page":"101677","DOI":"10.1016\/j.jbc.2022.101677","article-title":"Phase separation by the SARS-CoV-2 nucleocapsid protein: consensus and open questions","volume":"298","author":"Cascarina","year":"2022","journal-title":"J. Biol. Chem."},{"key":"2024062323555045100_B20","doi-asserted-by":"crossref","first-page":"1092","DOI":"10.1016\/j.molcel.2020.11.025","article-title":"Phosphoregulation of phase separation by the SARS-CoV-2 N protein suggests a biophysical basis for its dual functions","volume":"80","author":"Carlson","year":"2020","journal-title":"Mol. Cell"},{"key":"2024062323555045100_B21","doi-asserted-by":"crossref","first-page":"1936","DOI":"10.1038\/s41467-021-21953-3","article-title":"The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA","volume":"12","author":"Cubuk","year":"2021","journal-title":"Nat. Commun."},{"key":"2024062323555045100_B22","doi-asserted-by":"crossref","first-page":"1078","DOI":"10.1016\/j.molcel.2020.11.041","article-title":"Genomic RNA elements drive phase separation of the SARS-CoV-2 nucleocapsid","volume":"80","author":"Iserman","year":"2020","journal-title":"Mol. Cell"},{"key":"2024062323555045100_B23","doi-asserted-by":"crossref","first-page":"929","DOI":"10.3390\/biom12070929","article-title":"NMR reveals specific tracts within the intrinsically disordered regions of the SARS-CoV-2 nucleocapsid protein involved in RNA encountering","volume":"12","author":"Pontoriero","year":"2022","journal-title":"Biomolecules"},{"key":"2024062323555045100_B24","doi-asserted-by":"crossref","first-page":"2609","DOI":"10.1093\/nar\/gkad1215","article-title":"The disordered N-terminal tail of SARS CoV-2 nucleocapsid protein forms a dynamic complex with RNA","volume":"52","author":"Cubuk","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"2024062323555045100_B25","doi-asserted-by":"crossref","first-page":"102560","DOI":"10.1016\/j.jbc.2022.102560","article-title":"Reconstitution of the SARS-CoV-2 ribonucleosome provides insights into genomic RNA packaging and regulation by phosphorylation","volume":"298","author":"Carlson","year":"2022","journal-title":"J. Biol. Chem."},{"key":"2024062323555045100_B26","doi-asserted-by":"crossref","first-page":"eadg6473","DOI":"10.1126\/sciadv.adg6473","article-title":"A conserved oligomerization domain in the disordered linker of coronavirus nucleocapsid proteins","volume":"9","author":"Zhao","year":"2023","journal-title":"Sci. Adv."},{"key":"2024062323555045100_B27","doi-asserted-by":"crossref","first-page":"pgac049","DOI":"10.1093\/pnasnexus\/pgac049","article-title":"Plasticity in structure and assembly of SARS-CoV-2 nucleocapsid protein","volume":"1","author":"Zhao","year":"2022","journal-title":"PNAS Nexus"},{"key":"2024062323555045100_B28","doi-asserted-by":"crossref","DOI":"10.1101\/2023.10.20.23297329","article-title":"Dynamics of SARS-CoV-2 seroprevalence in a large US population over a period of 12 months","author":"Karkanitsa","year":"2023"},{"key":"2024062323555045100_B29","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1007\/978-1-4939-6887-9_5","article-title":"Optimizing expression and solubility of proteins in E. coli using modified Media and induction parameters","volume":"1586","author":"Taylor","year":"2017","journal-title":"Methods Mol. Biol."},{"key":"2024062323555045100_B30","doi-asserted-by":"crossref","first-page":"2309","DOI":"10.1016\/j.bpj.2011.03.004","article-title":"On the distribution of protein refractive index increments","volume":"100","author":"Zhao","year":"2011","journal-title":"Biophys. J."},{"key":"2024062323555045100_B31","doi-asserted-by":"crossref","first-page":"1626","DOI":"10.1126\/science.abl6184","article-title":"Rapid assessment of SARS-CoV-2\u2013evolved variants using virus-like particles","volume":"374","author":"Syed","year":"2021","journal-title":"Science"},{"key":"2024062323555045100_B32","doi-asserted-by":"crossref","first-page":"105362","DOI":"10.1016\/j.jbc.2023.105362","article-title":"Assembly of SARS-CoV-2 ribonucleosomes by truncated N\u2217 variant of the nucleocapsid protein","volume":"299","author":"Adly","year":"2023","journal-title":"J. Biol. Chem."},{"key":"2024062323555045100_B33","volume-title":"Basic Principles of Analytical Ultracentrifugation. CRC Press","author":"Schuck","year":"2015"},{"key":"2024062323555045100_B34","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.ab.2013.05.011","article-title":"Improving the thermal, radial, and temporal accuracy of the analytical ultracentrifuge through external references","volume":"440","author":"Ghirlando","year":"2013","journal-title":"Anal. Biochem."},{"key":"2024062323555045100_B35","doi-asserted-by":"crossref","DOI":"10.1201\/9781315367231","volume-title":"Sedimentation Velocity Analytical Ultracentrifugation: Discrete Species and Size-Distributions of Macromolecules and Particles","author":"Schuck","year":"2016"},{"key":"2024062323555045100_B36","doi-asserted-by":"crossref","first-page":"36397","DOI":"10.1074\/jbc.M507146200","article-title":"Assembly of an RNA-protein complex. Binding of NusB and NusE (S10) proteins to boxA RNA nucleates the formation of the antitermination complex involved in controlling rRNA transcription in Escherichia coli","volume":"280","author":"Greive","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2024062323555045100_B37","doi-asserted-by":"crossref","first-page":"102523","DOI":"10.1016\/j.isci.2021.102523","article-title":"Energetic and structural features of SARS-CoV-2 N-protein co-assemblies with nucleic acids","volume":"24","author":"Zhao","year":"2021","journal-title":"iScience"},{"key":"2024062323555045100_B38","doi-asserted-by":"crossref","first-page":"e1009100","DOI":"10.1371\/journal.ppat.1009100","article-title":"Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein","volume":"16","author":"Dinesh","year":"2020","journal-title":"PLoS Pathog."},{"key":"2024062323555045100_B39","volume-title":"Sedimentation Velocity Analytical Ultracentrifugation: Interacting Systems","author":"Schuck","year":"2017"},{"key":"2024062323555045100_B40","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1073\/pnas.0408399102","article-title":"Studying multiprotein complexes by multi-signal sedimentation velocity analytical ultracentrifugation","volume":"102","author":"Balbo","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2024062323555045100_B41","doi-asserted-by":"crossref","first-page":"2005","DOI":"10.1016\/j.bpj.2009.12.4336","article-title":"Sedimentation patterns of rapidly reversible protein interactions","volume":"98","author":"Schuck","year":"2010","journal-title":"Biophys. J."},{"key":"2024062323555045100_B42","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1017\/S003358350000202X","article-title":"Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity","volume":"11","author":"Record","year":"1978","journal-title":"Q. Rev. Biophys."},{"key":"2024062323555045100_B43","doi-asserted-by":"crossref","first-page":"RP94836","DOI":"10.7554\/eLife.94836.3","article-title":"Modulation of biophysical properties of nucleocapsid protein in the mutant spectrum of SARS-CoV-2","volume":"13","author":"Nguyen","year":"2024","journal-title":"eLife"},{"key":"2024062323555045100_B44","doi-asserted-by":"crossref","first-page":"E97","DOI":"10.1093\/nar\/gkaa632","article-title":"Single molecule mass photometry of nucleic acids","volume":"48","author":"Li","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"2024062323555045100_B45","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1021\/j100821a010","article-title":"Partial specific volumes and refractive index increments in multicomponent systems","volume":"65","author":"Casassa","year":"1961","journal-title":"J. Phys. Chem."},{"key":"2024062323555045100_B46","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.antiviral.2013.12.009","article-title":"The SARS coronavirus nucleocapsid protein - forms and functions","volume":"103","author":"Chang","year":"2014","journal-title":"Antiviral Res."},{"key":"2024062323555045100_B47","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1002\/pro.4221","article-title":"CTD of SARS-CoV-2 N protein is a cryptic domain for binding ATP and nucleic acid that interplay in modulating phase separation","volume":"31","author":"Dang","year":"2022","journal-title":"Protein Sci."},{"key":"2024062323555045100_B48","doi-asserted-by":"crossref","first-page":"102681","DOI":"10.1016\/j.isci.2021.102681","article-title":"Characterization of SARS-CoV-2 nucleocapsid protein reveals multiple functional consequences of the C-terminal domain","volume":"24","author":"Wu","year":"2021","journal-title":"iScience"},{"key":"2024062323555045100_B49","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.bbrc.2020.09.131","article-title":"High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2","volume":"538","author":"Zinzula","year":"2021","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2024062323555045100_B50","doi-asserted-by":"crossref","DOI":"10.2139\/ssrn.4472729","article-title":"SARS-CoV-2 evolution balances conflicting roles of N protein phosphorylation","author":"Syed","year":"2023"},{"key":"2024062323555045100_B51","doi-asserted-by":"crossref","first-page":"e1010627","DOI":"10.1371\/journal.ppat.1010627","article-title":"Nucleocapsid mutations in SARS-CoV-2 augment replication and pathogenesis","volume":"18","author":"Johnson","year":"2022","journal-title":"PLoS Pathog."},{"key":"2024062323555045100_B52","doi-asserted-by":"crossref","first-page":"eabm0808","DOI":"10.1126\/scisignal.abm0808","article-title":"Host protein kinases required for SARS-CoV-2 nucleocapsid phosphorylation and viral replication","volume":"15","author":"Yaron","year":"2022","journal-title":"Sci. Signal."},{"key":"2024062323555045100_B53","doi-asserted-by":"crossref","first-page":"e2113401118","DOI":"10.1073\/pnas.2113401118","article-title":"Targeting the coronavirus nucleocapsid protein through GSK-3 inhibition","volume":"118","author":"Liu","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2024062323555045100_B54","doi-asserted-by":"crossref","first-page":"4555","DOI":"10.1093\/nar\/gkad195","article-title":"A hybrid structure determination approach to investigate the druggability of the nucleocapsid protein of SARS-CoV-2","volume":"51","author":"Padroni","year":"2023","journal-title":"Nucleic Acids Res."},{"key":"2024062323555045100_B55","doi-asserted-by":"crossref","first-page":"167108","DOI":"10.1016\/j.jmb.2021.167108","article-title":"The inherent dynamics and interaction sites of the SARS-CoV-2 nucleocapsid N-terminal region","volume":"433","author":"Redzic","year":"2021","journal-title":"J. Mol. Biol."},{"key":"2024062323555045100_B56","doi-asserted-by":"crossref","first-page":"106843","DOI":"10.1016\/j.bpc.2022.106843","article-title":"Conformational ensemble of the full-length SARS-CoV-2 nucleocapsid (N) protein based on molecular simulations and SAXS data","volume":"288","author":"R\u00f3\u017cycki","year":"2022","journal-title":"Biophys. Chem."},{"key":"2024062323555045100_B57","doi-asserted-by":"crossref","first-page":"pgad333","DOI":"10.1093\/pnasnexus\/pgad333","article-title":"RNA structure and multiple weak interactions balance the interplay between RNA binding and phase separation of SARS-CoV-2 nucleocapsid","volume":"2","author":"Estelle","year":"2023","journal-title":"PNAS Nexus"},{"key":"2024062323555045100_B58","doi-asserted-by":"crossref","first-page":"4280","DOI":"10.1128\/jvi.62.11.4280-4287.1988","article-title":"Interactions between coronavirus nucleocapsid protein and viral RNAs: implications for viral transcription","volume":"62","author":"Baric","year":"1988","journal-title":"J. Virol."},{"key":"2024062323555045100_B59","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1093\/nar\/gkac1179","article-title":"Structural domains of SARS-CoV-2 nucleocapsid protein coordinate to compact long nucleic acid substrates","volume":"51","author":"Morse","year":"2023","journal-title":"Nucleic Acids Res."},{"key":"2024062323555045100_B60","doi-asserted-by":"crossref","first-page":"3917","DOI":"10.1038\/s41467-021-22785-x","article-title":"The architecture of the SARS-CoV-2 RNA genome inside virion","volume":"12","author":"Cao","year":"2021","journal-title":"Nat. Commun."},{"key":"2024062323555045100_B61","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1073\/pnas.1119057109","article-title":"Ionic strength-dependent persistence lengths of single-stranded RNA and DNA","volume":"109","author":"Chen","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2024062323555045100_B62","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1038\/s41467-023-36184-x","article-title":"Visualizing RNA conformational and architectural heterogeneity in solution","volume":"14","author":"Ding","year":"2023","journal-title":"Nat. Commun."},{"key":"2024062323555045100_B63","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1146\/annurev-physchem-040214-121637","article-title":"Mechanisms of virus assembly","volume":"66","author":"Perlmutter","year":"2015","journal-title":"Annu. Rev. Phys. Chem."},{"key":"2024062323555045100_B64","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/S0959-440X(00)00166-4","article-title":"Satellite tobacco mosaic virus RNA: structure and implications for assembly","volume":"11","author":"Larson","year":"2001","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2024062323555045100_B65","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1038\/s41392-023-01385-9","article-title":"Structural characteristics of the SARS-CoV-2 Omicron lineages BA.1 and BA.2 virions","volume":"8","author":"Ma","year":"2023","journal-title":"Signal Transduct. Target. Ther."},{"key":"2024062323555045100_B66","doi-asserted-by":"crossref","first-page":"113575","DOI":"10.1016\/j.ab.2020.113575","article-title":"Measuring the affinity of protein\u2013protein interactions on a single-molecule level by mass photometry","volume":"592","author":"Wu","year":"2020","journal-title":"Anal. Biochem."},{"key":"2024062323555045100_B67","doi-asserted-by":"crossref","first-page":"9513","DOI":"10.1021\/ac302357w","article-title":"Global multi-method analysis of affinities and cooperativity in complex systems of macromolecular interactions","volume":"84","author":"Zhao","year":"2012","journal-title":"Anal. Chem."}],"container-title":["Nucleic Acids Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/nar\/article-pdf\/52\/11\/6647\/58306533\/gkae256.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/nar\/article-pdf\/52\/11\/6647\/58306533\/gkae256.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,11,15]],"date-time":"2024-11-15T16:46:45Z","timestamp":1731689205000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/nar\/article\/52\/11\/6647\/7642063"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,4,8]]},"references-count":67,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2024,4,8]]},"published-print":{"date-parts":[[2024,6,24]]}},"URL":"https:\/\/doi.org\/10.1093\/nar\/gkae256","relation":{},"ISSN":["0305-1048","1362-4962"],"issn-type":[{"value":"0305-1048","type":"print"},{"value":"1362-4962","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2024,6,24]]},"published":{"date-parts":[[2024,4,8]]}}}