{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T16:32:01Z","timestamp":1790785921844,"version":"4.1.0"},"reference-count":49,"publisher":"Elsevier BV","issue":"14","license":[{"start":{"date-parts":[[2021,7,1]],"date-time":"2021-07-01T00:00:00Z","timestamp":1625097600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,7,1]],"date-time":"2021-07-01T00:00:00Z","timestamp":1625097600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,7,20]],"date-time":"2022-07-20T00:00:00Z","timestamp":1658275200000},"content-version":"vor","delay-in-days":384,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100009612","name":"Oregon State University","doi-asserted-by":"publisher","award":["MCB 2034446"],"award-info":[{"award-number":["MCB 2034446"]}],"id":[{"id":"10.13039\/100009612","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100009612","name":"Oregon State University","doi-asserted-by":"publisher","award":["1S10OD018518"],"award-info":[{"award-number":["1S10OD018518"]}],"id":[{"id":"10.13039\/100009612","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["MCB 2034446"],"award-info":[{"award-number":["MCB 2034446"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["1S10OD018518"],"award-info":[{"award-number":["1S10OD018518"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["MCB 2034446"],"award-info":[{"award-number":["MCB 2034446"]}],"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":["1S10OD018518"],"award-info":[{"award-number":["1S10OD018518"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000937","name":"M.J. Murdock Charitable Trust","doi-asserted-by":"publisher","award":["MCB 2034446"],"award-info":[{"award-number":["MCB 2034446"]}],"id":[{"id":"10.13039\/100000937","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000937","name":"M.J. Murdock Charitable Trust","doi-asserted-by":"publisher","award":["1S10OD018518"],"award-info":[{"award-number":["1S10OD018518"]}],"id":[{"id":"10.13039\/100000937","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Journal"],"published-print":{"date-parts":[[2021,7]]},"DOI":"10.1016\/j.bpj.2021.03.023","type":"journal-article","created":{"date-parts":[[2021,3,29]],"date-time":"2021-03-29T19:50:16Z","timestamp":1617047416000},"page":"2890-2901","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":49,"title":["Multivalent binding of the partially disordered SARS-CoV-2 nucleocapsid phosphoprotein dimer to RNA"],"prefix":"10.1016","volume":"120","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6461-4154","authenticated-orcid":false,"given":"Heather M.","family":"Forsythe","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5886-9567","authenticated-orcid":false,"given":"Joaquin","family":"Rodriguez Galvan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhen","family":"Yu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8131-6896","authenticated-orcid":false,"given":"Seth","family":"Pinckney","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6858-0086","authenticated-orcid":false,"given":"Patrick","family":"Reardon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3928-2757","authenticated-orcid":false,"given":"Richard B.","family":"Cooley","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9756-2637","authenticated-orcid":false,"given":"Phillip","family":"Zhu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7905-8250","authenticated-orcid":false,"given":"Amber D.","family":"Rolland","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James S.","family":"Prell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4892-5259","authenticated-orcid":false,"given":"Elisar","family":"Barbar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpj.2021.03.023_bib1","series-title":"WHO Coronavirus Disease (COVID-19) Dashboard","year":"2020"},{"key":"10.1016\/j.bpj.2021.03.023_bib2","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1001\/jama.2020.12603","article-title":"Persistent symptoms in patients after acute COVID-19","volume":"324","author":"Carf\u00ec","year":"2020","journal-title":"JAMA"},{"key":"10.1016\/j.bpj.2021.03.023_bib3","doi-asserted-by":"crossref","first-page":"m3026","DOI":"10.1136\/bmj.m3026","article-title":"Management of post-acute covid-19 in primary care","volume":"370","author":"Greenhalgh","year":"2020","journal-title":"BMJ"},{"key":"10.1016\/j.bpj.2021.03.023_bib4","doi-asserted-by":"crossref","first-page":"e01925-19","DOI":"10.1128\/JVI.01925-19","article-title":"Nucleocapsid protein recruitment to replication-transcription complexes plays a crucial role in coronaviral life cycle","volume":"94","author":"Cong","year":"2020","journal-title":"J.\u00a0Virol"},{"key":"10.1016\/j.bpj.2021.03.023_bib5","doi-asserted-by":"crossref","first-page":"2991","DOI":"10.3390\/v6082991","article-title":"The coronavirus nucleocapsid is a multifunctional protein","volume":"6","author":"McBride","year":"2014","journal-title":"Viruses"},{"key":"10.1016\/j.bpj.2021.03.023_bib6","doi-asserted-by":"crossref","first-page":"e105938","DOI":"10.15252\/embj.2020105938","article-title":"Structures of the SARS-CoV-2 nucleocapsid and their perspectives for drug design","volume":"39","author":"Peng","year":"2020","journal-title":"EMBO J"},{"key":"10.1016\/j.bpj.2021.03.023_bib7","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1016\/j.apsb.2020.04.009","article-title":"Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites","volume":"10","author":"Kang","year":"2020","journal-title":"Acta Pharm. Sin. B"},{"key":"10.1016\/j.bpj.2021.03.023_bib8","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1038\/s41586-020-2286-9","article-title":"A SARS-CoV-2 protein interaction map reveals targets for drug repurposing","volume":"583","author":"Gordon","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.bpj.2021.03.023_bib9","first-page":"2837670","article-title":"Attenuated subcomponent vaccine design targeting the SARS-CoV-2 nucleocapsid phosphoprotein RNA binding domain: in\u00a0silico analysis","volume":"2020","author":"Chukwudozie","year":"2020","journal-title":"J.\u00a0Immunol. Res"},{"key":"10.1016\/j.bpj.2021.03.023_bib10","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1016\/j.bbrc.2020.04.136","article-title":"Biochemical characterization of SARS-CoV-2 nucleocapsid protein","volume":"527","author":"Zeng","year":"2020","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1016\/j.bpj.2021.03.023_bib11","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":"10.1016\/j.bpj.2021.03.023_bib12","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1016\/j.jmb.2007.02.069","article-title":"Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA","volume":"368","author":"Chen","year":"2007","journal-title":"J.\u00a0Mol. Biol"},{"key":"10.1016\/j.bpj.2021.03.023_bib13","doi-asserted-by":"crossref","first-page":"3913","DOI":"10.1128\/JVI.02236-06","article-title":"Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein","volume":"81","author":"Saikatendu","year":"2007","journal-title":"J.\u00a0Virol"},{"key":"10.1016\/j.bpj.2021.03.023_bib14","doi-asserted-by":"crossref","first-page":"2174","DOI":"10.1016\/j.csbj.2020.08.006","article-title":"Structural insights into the mechanism of RNA recognition by the N-terminal RNA-binding domain of the SARS-CoV-2 nucleocapsid phosphoprotein","volume":"18","author":"Khan","year":"2020","journal-title":"Comput. Struct. Biotechnol. J"},{"key":"10.1016\/j.bpj.2021.03.023_bib15","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":"10.1016\/j.bpj.2021.03.023_bib16","doi-asserted-by":"crossref","first-page":"1884","DOI":"10.1016\/j.csbj.2020.07.005","article-title":"Genus-specific pattern of intrinsically disordered central regions in the nucleocapsid protein of coronaviruses","volume":"18","author":"Barik","year":"2020","journal-title":"Comput. Struct. Biotechnol. J"},{"key":"10.1016\/j.bpj.2021.03.023_bib17","doi-asserted-by":"crossref","first-page":"5229","DOI":"10.1074\/jbc.M805747200","article-title":"Glycogen synthase kinase-3 regulates the phosphorylation of severe acute respiratory syndrome coronavirus nucleocapsid protein and viral replication","volume":"284","author":"Wu","year":"2009","journal-title":"J.\u00a0Biol. Chem"},{"key":"10.1016\/j.bpj.2021.03.023_bib18","doi-asserted-by":"crossref","first-page":"5740","DOI":"10.1038\/s41598-017-06062-w","article-title":"Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers","volume":"7","author":"Cong","year":"2017","journal-title":"Sci. Rep"},{"key":"10.1016\/j.bpj.2021.03.023_bib19","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.bpc.2004.06.008","article-title":"In\u00a0vitro biochemical and thermodynamic characterization of nucleocapsid protein of SARS","volume":"112","author":"Luo","year":"2004","journal-title":"Biophys. Chem"},{"key":"10.1016\/j.bpj.2021.03.023_bib20","doi-asserted-by":"crossref","first-page":"e57309","DOI":"10.7554\/eLife.57309","article-title":"SARS-CoV-2 (COVID-19) by the numbers","volume":"9","author":"Bar-On","year":"2020","journal-title":"eLife"},{"key":"10.1016\/j.bpj.2021.03.023_bib21","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1186\/s43556-020-00001-4","article-title":"Structural characterization of the C-terminal domain of SARS-CoV-2 nucleocapsid protein","volume":"1","author":"Zhou","year":"2020","journal-title":"Mol. Biomed"},{"key":"10.1016\/j.bpj.2021.03.023_bib22","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1016\/j.jmb.2007.11.093","article-title":"Solution structure of the c-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAIL-NMR method","volume":"380","author":"Takeda","year":"2008","journal-title":"J.\u00a0Mol. Biol"},{"key":"10.1016\/j.bpj.2021.03.023_bib23","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":"10.1016\/j.bpj.2021.03.023_bib24","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.coviro.2020.05.006","article-title":"Structure, dynamics and phase separation of measles virus RNA replication machinery","volume":"41","author":"Guseva","year":"2020","journal-title":"Curr. Opin. Virol"},{"key":"10.1016\/j.bpj.2021.03.023_bib25","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1038\/s41556-019-0300-y","article-title":"A lipid-based partitioning mechanism for selective incorporation of proteins into membranes of HIV particles","volume":"21","author":"Sengupta","year":"2019","journal-title":"Nat. Cell Biol"},{"key":"10.1016\/j.bpj.2021.03.023_bib26","doi-asserted-by":"crossref","first-page":"eaaz7095","DOI":"10.1126\/sciadv.aaz7095","article-title":"Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly","volume":"6","author":"Guseva","year":"2020","journal-title":"Sci. Adv"},{"key":"10.1016\/j.bpj.2021.03.023_bib27","doi-asserted-by":"crossref","first-page":"107520","DOI":"10.1016\/j.celrep.2020.03.084","article-title":"Pan-retroviral nucleocapsid-mediated phase separation regulates genomic RNA positioning and trafficking","volume":"31","author":"Monette","year":"2020","journal-title":"Cell Rep"},{"key":"10.1016\/j.bpj.2021.03.023_bib28","doi-asserted-by":"crossref","first-page":"e106478","DOI":"10.15252\/embj.2020106478","article-title":"SARS-CoV-2 nucleocapsid protein phase-separates with RNA and with human hnRNPs","volume":"39","author":"Perdikari","year":"2020","journal-title":"EMBO J"},{"key":"10.1016\/j.bpj.2021.03.023_bib29","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":"10.1016\/j.bpj.2021.03.023_bib30","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1038\/s41467-020-20768-y","article-title":"The SARS-CoV-2 Nucleocapsid phosphoprotein forms mutually exclusive condensates with RNA and the membrane-associated M protein","volume":"12","author":"Lu","year":"2021","journal-title":"Nat. Commun"},{"key":"10.1016\/j.bpj.2021.03.023_bib31","article-title":"The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA","author":"Cubuk","year":"2020","journal-title":"bioRxiv"},{"key":"10.1016\/j.bpj.2021.03.023_bib32","doi-asserted-by":"crossref","first-page":"1143","DOI":"10.1038\/s41422-020-00408-2","article-title":"Liquid-liquid phase separation by SARS-CoV-2 nucleocapsid protein and RNA","volume":"30","author":"Chen","year":"2020","journal-title":"Cell Res"},{"key":"10.1016\/j.bpj.2021.03.023_bib33","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.chroma.2014.02.030","article-title":"Purification of protein complexes of defined subunit stoichiometry using a set of orthogonal, tag-cleaving proteases","volume":"1337","author":"Frey","year":"2014","journal-title":"J.\u00a0Chromatogr. A"},{"key":"10.1016\/j.bpj.2021.03.023_bib34","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\u00a0N protein suggests a biophysical basis for its dual functions","volume":"80","author":"Carlson","year":"2020","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bpj.2021.03.023_bib35","series-title":"Analytical Ultracentrifugation in Biochemistry and Polymer Science","first-page":"90","article-title":"Computer-aided interpretation of analytical sedimentation data for proteins","author":"Laue","year":"1992"},{"key":"10.1016\/j.bpj.2021.03.023_bib36","doi-asserted-by":"crossref","first-page":"1606","DOI":"10.1016\/S0006-3495(00)76713-0","article-title":"Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling","volume":"78","author":"Schuck","year":"2000","journal-title":"Biophys. J"},{"key":"10.1016\/j.bpj.2021.03.023_bib37","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S0091-679X(07)84006-4","article-title":"Analytical ultracentrifugation: sedimentation velocity and sedimentation equilibrium","volume":"84","author":"Cole","year":"2008","journal-title":"Methods Cell Biol"},{"key":"10.1016\/j.bpj.2021.03.023_bib38","doi-asserted-by":"crossref","first-page":"9557","DOI":"10.1021\/ac1022953","article-title":"Collision cross sections of proteins and their complexes: a calibration framework and database for gas-phase structural biology","volume":"82","author":"Bush","year":"2010","journal-title":"Anal. Chem"},{"key":"10.1016\/j.bpj.2021.03.023_bib39","doi-asserted-by":"crossref","first-page":"1181","DOI":"10.1002\/rcm.6211","article-title":"Traveling-wave ion mobility mass spectrometry of protein complexes: accurate calibrated collision cross-sections of human insulin oligomers","volume":"26","author":"Salbo","year":"2012","journal-title":"Rapid Commun. Mass Spectrom"},{"key":"10.1016\/j.bpj.2021.03.023_bib40","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1016\/j.bbapap.2012.11.013","article-title":"Native ion mobility-mass spectrometry and related methods in structural biology","volume":"1834","author":"Konijnenberg","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpj.2021.03.023_bib41","doi-asserted-by":"crossref","first-page":"5107","DOI":"10.1021\/acs.analchem.7b00673","article-title":"Extended protein ions are formed by the chain ejection model in chemical supercharging electrospray ionization","volume":"89","author":"Donor","year":"2017","journal-title":"Anal. Chem"},{"key":"10.1016\/j.bpj.2021.03.023_bib42","doi-asserted-by":"crossref","first-page":"4959","DOI":"10.1016\/j.jmb.2019.10.011","article-title":"The LC8-RavP ensemble structure evinces A role for LC8 in regulating lyssavirus polymerase functionality","volume":"431","author":"Jespersen","year":"2019","journal-title":"J.\u00a0Mol. Biol"},{"key":"10.1016\/j.bpj.2021.03.023_bib43","doi-asserted-by":"crossref","first-page":"6059","DOI":"10.1021\/bi036155b","article-title":"Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein","volume":"43","author":"Huang","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2021.03.023_bib44","doi-asserted-by":"crossref","first-page":"1890","DOI":"10.1002\/pro.3909","article-title":"Architecture and self-assembly of the SARS-CoV-2 nucleocapsid protein","volume":"29","author":"Ye","year":"2020","journal-title":"Protein Sci"},{"key":"10.1016\/j.bpj.2021.03.023_bib45","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":"10.1016\/j.bpj.2021.03.023_bib46","article-title":"Autoproteolytic products of the SARS-CoV-2 nucleocapsid protein are primed for antibody evasion and virus proliferation","author":"Lutomski","year":"2020","journal-title":"bioRxiv"},{"key":"10.1016\/j.bpj.2021.03.023_bib47","article-title":"The nucleocapsid protein of zoonotic betacoronaviruses is an attractive target for antiviral drug discovery","author":"Lang","year":"2020","journal-title":"Life Sci"},{"key":"10.1016\/j.bpj.2021.03.023_bib48","article-title":"Computational guided identification of novel potent inhibitors of N-terminal domain of nucleocapsid protein of severe acute respiratory syndrome coronavirus 2","author":"Dhankhar","year":"2020","journal-title":"J.\u00a0Biomol. Struct. Dyn"},{"key":"10.1016\/j.bpj.2021.03.023_bib49","article-title":"Targeting SARS-CoV-2 nucleocapsid oligomerization: insights from molecular docking and molecular dynamics simulations","author":"Ahamad","year":"2020","journal-title":"J.\u00a0Biomol. Struct. Dyn"}],"container-title":["Biophysical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349521002538?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349521002538?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,13]],"date-time":"2025-09-13T16:53:07Z","timestamp":1757782387000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006349521002538"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,7]]},"references-count":49,"journal-issue":{"issue":"14","published-print":{"date-parts":[[2021,7]]}},"alternative-id":["S0006349521002538"],"URL":"https:\/\/doi.org\/10.1016\/j.bpj.2021.03.023","relation":{},"ISSN":["0006-3495"],"issn-type":[{"value":"0006-3495","type":"print"}],"subject":[],"published":{"date-parts":[[2021,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Multivalent binding of the partially disordered SARS-CoV-2 nucleocapsid phosphoprotein dimer to RNA","name":"articletitle","label":"Article Title"},{"value":"Biophysical Journal","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bpj.2021.03.023","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Biophysical Society.","name":"copyright","label":"Copyright"}]}}