{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T10:30:48Z","timestamp":1787567448537,"version":"build-2736575974"},"reference-count":107,"publisher":"eLife Sciences Publications, Ltd","license":[{"start":{"date-parts":[[2025,12,30]],"date-time":"2025-12-30T00:00:00Z","timestamp":1767052800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/publicdomain\/zero\/1.0\/"},{"start":{"date-parts":[[2025,12,30]],"date-time":"2025-12-30T00:00:00Z","timestamp":1767052800000},"content-version":"am","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/publicdomain\/zero\/1.0\/"},{"start":{"date-parts":[[2025,12,30]],"date-time":"2025-12-30T00:00:00Z","timestamp":1767052800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/publicdomain\/zero\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["ZIA EB000099-02"],"award-info":[{"award-number":["ZIA EB000099-02"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"award":["ZIA EB000099-02"],"award-info":[{"award-number":["ZIA EB000099-02"]}],"id":[{"id":"https:\/\/ror.org\/01cwqze88","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":["elifesciences.org"],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:p>Previously, we showed that the genetic diversity of SARS-CoV-2 nucleocapsid (N) protein explores a wide range of biophysical properties facilitated by non-local impact of point mutations to its intrinsically disordered regions (Nguyen et al., 2024). This includes modulation of self-association, such as the creation of a de novo binding interface through the P13L mutation characteristic of Omicron variants. In the present work, we focus on the key function of N condensing viral RNA into ribonucleoprotein particles (RNPs) for viral assembly. Lacking high-resolution structural information, biochemical and biophysical approaches have revealed architectural principles of RNPs, which involve cooperative interactions of several protein-protein and protein-RNA interfaces, initiated through oligomerization of conserved transient helices in the central disordered linker of N. Here, we study the impact of defining N-protein mutations in variants of concern on RNP formation, using biophysical tools, a virus-like particle assay, and reverse genetics experiments. We find convergent evolution in repeated, independent introduction of amino acid substitutions strengthening existing binding interfaces, compensating for other substitutions that promote viral replication but decrease RNP stability. Furthermore, we show that the P13L mutation of Omicron variants enhances RNP assembly and increases viral fitness. Overall, our data reveal RNP complexes to be highly variable not only in sequence and conformations but also in thermodynamic and kinetic stability, with its pleomorphism affecting basic architectural principles. We hypothesize that the formation of polydisperse, fuzzy N-RNA clusters with multiple distributed weak binding interfaces optimizes reversible RNA condensation, while supporting host adaptation and allowing for a large sequence space to be explored.<\/jats:p>","DOI":"10.7554\/elife.108922","type":"journal-article","created":{"date-parts":[[2025,10,15]],"date-time":"2025-10-15T16:30:26Z","timestamp":1760545826000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.108922","source":"Crossref","is-referenced-by-count":0,"title":["Evolution of a fuzzy ribonucleoprotein complex in viral assembly"],"prefix":"10.7554","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8827-6639","authenticated-orcid":true,"given":"Huaying","family":"Zhao","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00372qc85","id-type":"ROR","asserted-by":"publisher"}],"name":"Laboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"conceptualization","vocabulary":"credit"},{"role":"data-curation","vocabulary":"credit"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"investigation","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"resources","vocabulary":"credit"},{"role":"supervision","vocabulary":"credit"},{"role":"writing-original-draft","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"given":"Tiansheng","family":"Li","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/043z4tv69","id-type":"ROR","asserted-by":"publisher"}],"name":"Cellular Biology Section, Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"investigation","vocabulary":"credit"},{"role":"resources","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"given":"Sergio A","family":"Hassan","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/043z4tv69","id-type":"ROR","asserted-by":"publisher"}],"name":"Bioinformatics and Computational Biosciences Branch, National Institute of Allergy and Infectious Diseases, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"data-curation","vocabulary":"credit"},{"role":"investigation","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"resources","vocabulary":"credit"},{"role":"visualization","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"given":"Ai","family":"Nguyen","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00372qc85","id-type":"ROR","asserted-by":"publisher"}],"name":"Laboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"investigation","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"resources","vocabulary":"credit"},{"role":"validation","vocabulary":"credit"}]},{"given":"Siddhartha AK","family":"Datta","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00372qc85","id-type":"ROR","asserted-by":"publisher"}],"name":"Laboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"investigation","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"resources","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"given":"Guofeng","family":"Zhang","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00372qc85","id-type":"ROR","asserted-by":"publisher"}],"name":"Electron Microscopy Unit, Trans-NIH Shared Resource on Biomedical Engineering and Physical Science, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"investigation","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"visualization","vocabulary":"credit"}]},{"given":"Camden","family":"Trent","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00372qc85","id-type":"ROR","asserted-by":"publisher"}],"name":"Laboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"investigation","vocabulary":"credit"}]},{"given":"Agata M","family":"Czaja","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00372qc85","id-type":"ROR","asserted-by":"publisher"}],"name":"Laboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"investigation","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"}]},{"given":"Di","family":"Wu","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/012pb6c26","id-type":"ROR","asserted-by":"publisher"}],"name":"Biophysics Core Facility, National Heart, Lung, and Blood Institute, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"investigation","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"resources","vocabulary":"credit"}]},{"given":"Maria A","family":"Aronova","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00372qc85","id-type":"ROR","asserted-by":"publisher"}],"name":"Laboratory of Cellular Imaging and Macromolecular Biophysics, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"data-curation","vocabulary":"credit"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"resources","vocabulary":"credit"},{"role":"visualization","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"given":"Kin Kui","family":"Lai","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05bjen692","id-type":"ROR","asserted-by":"publisher"}],"name":"HIV Dynamics and Replication Program, Center for Cancer Research, National Cancer Institute","place":["Frederick, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"investigation","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"resources","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5270-3678","authenticated-orcid":true,"given":"Grzegorz","family":"Piszczek","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/012pb6c26","id-type":"ROR","asserted-by":"publisher"}],"name":"Biophysics Core Facility, National Heart, Lung, and Blood Institute, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"methodology","vocabulary":"credit"},{"role":"resources","vocabulary":"credit"},{"role":"supervision","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"given":"Richard","family":"Leapman","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00372qc85","id-type":"ROR","asserted-by":"publisher"}],"name":"Laboratory of Cellular Imaging and Macromolecular Biophysics, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"methodology","vocabulary":"credit"},{"role":"resources","vocabulary":"credit"},{"role":"supervision","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"given":"Jonathan W","family":"Yewdell","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/043z4tv69","id-type":"ROR","asserted-by":"publisher"}],"name":"Cellular Biology Section, Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"methodology","vocabulary":"credit"},{"role":"resources","vocabulary":"credit"},{"role":"supervision","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8859-6966","authenticated-orcid":true,"given":"Peter","family":"Schuck","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00372qc85","id-type":"ROR","asserted-by":"publisher"}],"name":"Laboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health","place":["Bethesda, United States"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"corresponding-author","vocabulary":"crossref"},{"role":"conceptualization","vocabulary":"credit"},{"role":"funding-acquisition","vocabulary":"credit"},{"role":"investigation","vocabulary":"credit"},{"role":"software","vocabulary":"credit"},{"role":"supervision","vocabulary":"credit"},{"role":"visualization","vocabulary":"credit"},{"role":"writing-original-draft","vocabulary":"credit"}]}],"member":"4374","published-online":{"date-parts":[[2025,12,30]]},"reference":[{"key":"bib1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2023.105362","type":"journal-article","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":"The Journal of Biological Chemistry"},{"key":"bib2","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1016\/j.cell.2018.12.035","type":"journal-article","article-title":"Considerations and challenges in studying liquid-liquid phase separation and biomolecular condensates","volume":"176","author":"Alberti","year":"2019","journal-title":"Cell"},{"key":"bib3","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2304302120","type":"journal-article","article-title":"Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2","volume":"120","author":"Alderson","year":"2023","journal-title":"PNAS"},{"key":"bib4","doi-asserted-by":"publisher","DOI":"10.1101\/2023.08.06.552128","type":"preprint","article-title":"Conserved molecular recognition by an intrinsically disordered region in the absence of sequence conservation","volume-title":"bioRxiv","author":"Alston","year":"2023"},{"key":"bib5","doi-asserted-by":"publisher","first-page":"4562","DOI":"10.1016\/j.csbj.2022.08.015","type":"journal-article","article-title":"Evolutionary progression of collective mutations in Omicron sub-lineages towards efficient RBD-hACE2: Allosteric communications between and within viral and human proteins","volume":"20","author":"Barozi","year":"2022","journal-title":"Computational and Structural Biotechnology Journal"},{"key":"bib6","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.abm4034","type":"journal-article","article-title":"The intrinsically disordered SARS-CoV-2 nucleoprotein in dynamic complex with its viral partner nsp3a","volume":"8","author":"Bessa","year":"2022","journal-title":"Science Advances"},{"key":"bib7","doi-asserted-by":"publisher","DOI":"10.1093\/ve\/vead055","type":"journal-article","article-title":"Fitness effects of mutations to SARS-CoV-2 proteins","volume":"9","author":"Bloom","year":"2023","journal-title":"Virus Evolution"},{"key":"bib8","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.aax2323","type":"journal-article","article-title":"A specific phosphorylation-dependent conformational switch in SARS-CoV-2 nucleocapsid protein inhibits RNA binding","volume":"10","author":"Botova","year":"2024","journal-title":"Science Advances"},{"key":"bib9","doi-asserted-by":"publisher","first-page":"4597","DOI":"10.1016\/j.cell.2023.08.026","type":"journal-article","article-title":"SARS-CoV-2 variants evolve convergent strategies to remodel the host response","volume":"186","author":"Bouhaddou","year":"2023","journal-title":"Cell"},{"key":"bib10","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3390\/ijms21239045","type":"journal-article","article-title":"Liquid-liquid phase separation by intrinsically disordered protein regions of viruses: roles in viral life cycle and control of virus-host interactions","volume":"21","author":"Brocca","year":"2020","journal-title":"International Journal of Molecular Sciences"},{"key":"bib11","doi-asserted-by":"publisher","first-page":"441","DOI":"10.1016\/j.sbi.2011.02.005","type":"journal-article","article-title":"Evolution and disorder","volume":"21","author":"Brown","year":"2011","journal-title":"Current Opinion in Structural Biology"},{"key":"bib12","doi-asserted-by":"publisher","first-page":"1092","DOI":"10.1016\/j.molcel.2020.11.025","type":"journal-article","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":"Molecular Cell"},{"key":"bib13","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2022.102560","type":"journal-article","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":"The Journal of Biological Chemistry"},{"key":"bib14","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1007\/s11373-005-9035-9","type":"journal-article","article-title":"Modular organization of SARS coronavirus nucleocapsid protein","volume":"13","author":"Chang","year":"2006","journal-title":"Journal of Biomedical Science"},{"key":"bib15","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-21953-3","type":"journal-article","article-title":"The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA","volume":"12","author":"Cubuk","year":"2021","journal-title":"Nature Communications"},{"key":"bib16","doi-asserted-by":"publisher","first-page":"2609","DOI":"10.1093\/nar\/gkad1215","type":"journal-article","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 Research"},{"key":"bib17","doi-asserted-by":"publisher","DOI":"10.1016\/j.xcrp.2025.102695","type":"journal-article","article-title":"The dimerization domain of SARS-CoV-2 nucleocapsid protein is partially disordered and forms a dynamic high-affinity dimer","volume":"6","author":"Cubuk","year":"2025","journal-title":"Cell Reports. Physical Science"},{"key":"bib18","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1016\/j.tibs.2010.10.002","type":"journal-article","article-title":"How viruses hijack cell regulation","volume":"36","author":"Davey","year":"2011","journal-title":"Trends in Biochemical Sciences"},{"key":"bib19","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1186\/s12964-015-0120-z","type":"journal-article","article-title":"Short linear motifs - Ex nihilo evolution of protein regulation Short linear motifs - The unexplored frontier of the eukaryotic proteome","volume":"01","author":"Davey","year":"2015","journal-title":"Cell Communication and Signaling"},{"key":"bib20","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-024-55024-0","type":"journal-article","article-title":"A core network in the SARS-CoV-2 nucleocapsid NTD mediates structural integrity and selective RNA-binding","volume":"15","author":"Dhamotharan","year":"2024","journal-title":"Nature Communications"},{"key":"bib21","doi-asserted-by":"publisher","first-page":"2821","DOI":"10.1039\/c5mb00301f","type":"journal-article","article-title":"Fuzziness endows viral motif-mimicry","volume":"11","author":"Duro","year":"2015","journal-title":"Molecular bioSystems"},{"key":"bib22","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1038\/nrm1589","type":"journal-article","article-title":"Intrinsically unstructured proteins and their functions","volume":"6","author":"Dyson","year":"2005","journal-title":"Nature Reviews. Molecular Cell Biology"},{"key":"bib23","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1002\/gch2.1018","type":"journal-article","article-title":"Data, disease and diplomacy: GISAID\u2019s innovative contribution to global health","volume":"1","author":"Elbe","year":"2017","journal-title":"Global Challenges"},{"key":"bib24","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2021.693204","type":"journal-article","article-title":"Molecular evolution of the influenza a virus non-structural protein 1 in interspecies transmission and adaptation","volume":"12","author":"Evseev","year":"2021","journal-title":"Frontiers in Microbiology"},{"key":"bib25","doi-asserted-by":"publisher","DOI":"10.3390\/vaccines12080887","type":"journal-article","article-title":"Subsequent waves of convergent evolution in SARS-CoV-2 genes and proteins","volume":"12","author":"Focosi","year":"2024","journal-title":"Vaccines"},{"key":"bib26","doi-asserted-by":"publisher","first-page":"2278","DOI":"10.1016\/j.jmb.2018.02.015","type":"journal-article","article-title":"Fuzziness in protein interactions-a historical perspective","volume":"430","author":"Fuxreiter","year":"2018","journal-title":"Journal of Molecular Biology"},{"key":"bib27","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1016\/j.ab.2013.05.011","type":"journal-article","article-title":"Improving the thermal, radial, and temporal accuracy of the analytical ultracentrifuge through external references","volume":"440","author":"Ghirlando","year":"2013","journal-title":"Analytical Biochemistry"},{"key":"bib28","doi-asserted-by":"publisher","DOI":"10.1002\/pro.4968","type":"journal-article","article-title":"Protein structure-function continuum model: Emerging nexuses between specificity, evolution, and structure","volume":"33","author":"Gupta","year":"2024","journal-title":"Protein Science"},{"key":"bib29","doi-asserted-by":"publisher","first-page":"255","DOI":"10.1007\/s12104-021-10014-x","type":"journal-article","article-title":"1H, 13C and 15N Backbone chemical shift assignments of the n-terminal and central intrinsically disordered domains of SARS-CoV-2 nucleoprotein","volume":"15","author":"Guseva","year":"2021","journal-title":"Biomolecular NMR Assignments"},{"key":"bib30","doi-asserted-by":"publisher","first-page":"4121","DOI":"10.1093\/bioinformatics\/bty407","type":"journal-article","article-title":"Nextstrain: real-time tracking of pathogen evolution","volume":"34","author":"Hadfield","year":"2018","journal-title":"Bioinformatics"},{"key":"bib31","doi-asserted-by":"publisher","first-page":"1729","DOI":"10.1016\/j.celrep.2014.04.052","type":"journal-article","article-title":"Use of host-like peptide motifs in viral proteins is a prevalent strategy in host-virus interactions","volume":"7","author":"Hagai","year":"2014","journal-title":"Cell Reports"},{"key":"bib32","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1038\/s41580-023-00673-0","type":"journal-article","article-title":"The molecular basis for cellular function of intrinsically disordered protein regions","volume":"25","author":"Holehouse","year":"2024","journal-title":"Nature Reviews. Molecular Cell Biology"},{"key":"bib33","doi-asserted-by":"publisher","first-page":"1078","DOI":"10.1016\/j.molcel.2020.11.041","type":"journal-article","article-title":"Genomic RNA elements drive phase separation of the SARS-CoV-2 Nucleocapsid","volume":"80","author":"Iserman","year":"2020","journal-title":"Molecular Cell"},{"key":"bib34","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.3001425","type":"journal-article","article-title":"SARS-CoV-2 nucleocapsid protein forms condensates with viral genomic RNA","volume":"19","author":"Jack","year":"2021","journal-title":"PLOS Biology"},{"key":"bib35","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1010627","type":"journal-article","article-title":"Nucleocapsid mutations in SARS-CoV-2 augment replication and pathogenesis","volume":"18","author":"Johnson","year":"2022","journal-title":"PLOS Pathogens"},{"key":"bib36","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2024.107828","type":"journal-article","article-title":"N terminus of SARS-CoV-2 nonstructural protein 3 interrupts RNA-driven phase separation of N protein by displacing RNA","volume":"300","author":"Ke","year":"2024","journal-title":"The Journal of Biological Chemistry"},{"key":"bib37","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-020-19619-7","type":"journal-article","article-title":"SARS-CoV-2 structure and replication characterized by in situ cryo-electron tomography","volume":"11","author":"Klein","year":"2020","journal-title":"Nature Communications"},{"key":"bib38","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-38882-y","type":"journal-article","article-title":"The preference signature of the SARS-CoV-2 Nucleocapsid NTD for its 5\u2019-genomic RNA elements","volume":"14","author":"Korn","year":"2023","journal-title":"Nature Communications"},{"key":"bib39","doi-asserted-by":"publisher","DOI":"10.1101\/2024.03.08.584120","type":"preprint","article-title":"Variant mutation in SARS-CoV-2 nucleocapsid enhances viral infection via altered genomic encapsidation","volume-title":"bioRxiv","author":"Kubinski","year":"2024"},{"key":"bib40","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-025-61861-4","type":"journal-article","article-title":"Structural stabilization of the intrinsically disordered SARS-CoV-2 N by binding to RNA sequences engineered from the viral genome fragment","volume":"16","author":"Landeras-Bueno","year":"2025","journal-title":"Nature Communications"},{"key":"bib41","doi-asserted-by":"publisher","DOI":"10.1101\/2023.12.12.571262","type":"preprint","article-title":"Syncytia Formation Promotes Virus Resistance to Interferon and Neutralizing Antibodies","volume-title":"bioRxiv","author":"Li","year":"2023"},{"key":"bib42","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2305674120","type":"journal-article","article-title":"Nsp3-N interactions are critical for SARS-CoV-2 fitness and virulence","volume":"120","author":"Li","year":"2023","journal-title":"PNAS"},{"key":"bib43","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1012886","type":"journal-article","article-title":"The R203M and D377Y mutations of the nucleocapsid protein promote SARS-CoV-2 infectivity by impairing RIG-I-mediated antiviral signaling","volume":"21","author":"Li","year":"2025","journal-title":"PLOS Pathogens"},{"key":"bib44","doi-asserted-by":"publisher","first-page":"3091","DOI":"10.1007\/s00018-017-2556-3","type":"journal-article","article-title":"How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication","volume":"74","author":"Longhi","year":"2017","journal-title":"Cellular and Molecular Life Sciences"},{"key":"bib45","volume-title":"Evidence for the Dependence of the SARS-Cov-2 Delta High Diffusivity on the Associated N:G215C Nucleocapsid Mutation","author":"Marchitelli","year":"2021","type":"book"},{"key":"bib46","doi-asserted-by":"publisher","first-page":"361","DOI":"10.1038\/s41579-023-00878-2","type":"journal-article","article-title":"The evolution of SARS-CoV-2","volume":"21","author":"Markov","year":"2023","journal-title":"Nature Reviews. Microbiology"},{"key":"bib47","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.3002982","type":"journal-article","article-title":"Emergence of SARS-CoV-2 subgenomic RNAs that enhance viral fitness and immune evasion","volume":"23","author":"Mears","year":"2025","journal-title":"PLOS Biology"},{"key":"bib48","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1038\/s41592-022-01488-1","type":"journal-article","article-title":"ColabFold: making protein folding accessible to all","volume":"19","author":"Mirdita","year":"2022","journal-title":"Nature Methods"},{"key":"bib49","doi-asserted-by":"publisher","DOI":"10.1101\/2025.02.15.638421","type":"preprint","article-title":"A Truncated SARS-CoV-2 Nucleocapsid Protein Enhances Virus Fitness by Evading Antiviral Responses","volume-title":"bioRxiv","author":"Mulloy","year":"2025"},{"key":"bib50","doi-asserted-by":"publisher","first-page":"85","DOI":"10.1016\/bs.pmbts.2019.05.004","type":"journal-article","article-title":"Translational diffusion of unfolded and intrinsically disordered proteins","volume":"166","author":"Nesmelova","year":"2019","journal-title":"Progress in Molecular Biology and Translational Science"},{"key":"bib51","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.94836","type":"journal-article","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":"bib52","doi-asserted-by":"publisher","DOI":"10.1038\/s42003-023-04570-2","type":"journal-article","article-title":"Structural insights into ribonucleoprotein dissociation by nucleocapsid protein interacting with non-structural protein 3 in SARS-CoV-2","volume":"6","author":"Ni","year":"2023","journal-title":"Communications Biology"},{"key":"bib53","doi-asserted-by":"publisher","first-page":"1327","DOI":"10.1126\/science.abm1208","type":"journal-article","article-title":"Analysis of 6.4 million SARS-CoV-2 genomes identifies mutations associated with fitness","volume":"376","author":"Obermeyer","year":"2022","journal-title":"Science"},{"key":"bib54","doi-asserted-by":"publisher","first-page":"3175","DOI":"10.1007\/s00018-017-2560-7","type":"journal-article","article-title":"Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness","volume":"74","author":"Olsen","year":"2017","journal-title":"Cellular and Molecular Life Sciences"},{"key":"bib55","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0238665","type":"journal-article","article-title":"Generalized linear models provide a measure of virulence for specific mutations in SARS-CoV-2 strains","volume":"16","author":"Oulas","year":"2021","journal-title":"PLOS ONE"},{"key":"bib56","doi-asserted-by":"publisher","first-page":"18349","DOI":"10.1073\/pnas.0806270105","type":"journal-article","article-title":"Molecular structural basis for polymorphism in Alzheimer\u2019s \u03b2-amyloid fibrils","volume":"105","author":"Paravastu","year":"2008","journal-title":"PNAS"},{"key":"bib57","doi-asserted-by":"publisher","DOI":"10.21769\/BioProtoc.4195","type":"journal-article","article-title":"Measurement of the translational diffusion coefficient and hydrodynamic radius of proteins by dynamic light scattering","volume":"11","author":"Parker","year":"2021","journal-title":"Bio-Protocol"},{"key":"bib58","doi-asserted-by":"publisher","first-page":"1","DOI":"10.15252\/embj.2020106478","type":"journal-article","article-title":"SARS\u2010CoV\u20102 nucleocapsid protein phase\u2010separates with RNA and with human hnRNPs","volume":"39","author":"Perdikari","year":"2020","journal-title":"The EMBO Journal"},{"key":"bib59","doi-asserted-by":"publisher","first-page":"70","DOI":"10.1002\/pro.3943","type":"journal-article","article-title":"UCSF ChimeraX: Structure visualization for researchers, educators, and developers","volume":"30","author":"Pettersen","year":"2021","journal-title":"Protein Science"},{"key":"bib60","doi-asserted-by":"publisher","DOI":"10.1002\/pro.4447","type":"journal-article","article-title":"Evolutionary trajectory of receptor binding specificity and promiscuity of the spike protein of SARS-CoV-2","volume":"31","author":"Planchais","year":"2022","journal-title":"Protein Science"},{"key":"bib61","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1016\/j.virusres.2003.11.008","type":"journal-article","article-title":"Transient disulfide bonds formation in conformational maturation of influenza virus nucleocapsid protein (NP)","volume":"99","author":"Prokudina","year":"2004","journal-title":"Virus Research"},{"key":"bib62","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.56159","type":"journal-article","article-title":"Dynamic metastable long-living droplets formed by sticker-spacer proteins","volume":"9","author":"Ranganathan","year":"2020","journal-title":"eLife"},{"key":"bib63","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2215828120","type":"journal-article","article-title":"Phosphorylation sites are evolutionary checkpoints against liquid\u2013solid transition in protein condensates","volume":"120","author":"Ranganathan","year":"2023","journal-title":"PNAS"},{"key":"bib64","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-44502-6","type":"journal-article","article-title":"TRIM28-mediated nucleocapsid protein SUMOylation enhances SARS-CoV-2 virulence","volume":"15","author":"Ren","year":"2024","journal-title":"Nature Communications"},{"key":"bib65","doi-asserted-by":"publisher","first-page":"1","DOI":"10.15252\/embr.202255393","type":"journal-article","article-title":"Molecular adaptations during viral epidemics","volume":"23","author":"Rochman","year":"2022","journal-title":"EMBO Reports"},{"key":"bib66","doi-asserted-by":"publisher","first-page":"8168","DOI":"10.1093\/nar\/gkac596","type":"journal-article","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 Research"},{"key":"bib67","doi-asserted-by":"publisher","DOI":"10.1016\/j.bpc.2022.106843","type":"journal-article","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":"Biophysical Chemistry"},{"key":"bib68","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-020-19843-1","type":"journal-article","article-title":"Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates","volume":"11","author":"Savastano","year":"2020","journal-title":"Nature Communications"},{"key":"bib69","doi-asserted-by":"publisher","DOI":"10.3390\/microorganisms13020253","type":"journal-article","article-title":"SARS-CoV-2 XEC: a genome-based survey","volume":"13","author":"Scarpa","year":"2025","journal-title":"Microorganisms"},{"key":"bib70","doi-asserted-by":"publisher","DOI":"10.3390\/biom12091302","type":"journal-article","article-title":"The Role of disordered regions in orchestrating the properties of multidomain proteins: the SARS-CoV-2 nucleocapsid protein and its interaction with enoxaparin","volume":"12","author":"Schiavina","year":"2022","journal-title":"Biomolecules"},{"key":"bib71","doi-asserted-by":"publisher","first-page":"2005","DOI":"10.1016\/j.bpj.2009.12.4336","type":"journal-article","article-title":"Sedimentation patterns of rapidly reversible protein interactions","volume":"98","author":"Schuck","year":"2010","journal-title":"Biophysical Journal"},{"key":"bib72","doi-asserted-by":"publisher","DOI":"10.1201\/b19028","type":"book","volume-title":"Basic Principles of Analytical Ultracentrifugation","author":"Schuck","year":"2015"},{"key":"bib73","doi-asserted-by":"publisher","DOI":"10.1201\/9781315367231","type":"book","volume-title":"Sedimentation Velocity Analytical Ultracentrifugation: Discrete Species and Size-Distributions of Macromolecules and Particles","author":"Schuck","year":"2016"},{"key":"bib74","doi-asserted-by":"publisher","DOI":"10.1201\/b21988","type":"book","volume-title":"Sedimentation Velocity Analytical Ultracentrifugation: Interacting Systems","author":"Schuck","year":"2017"},{"key":"bib75","doi-asserted-by":"publisher","DOI":"10.1128\/mbio.02388-23","type":"journal-article","article-title":"Diversity of short linear interaction motifs in SARS-CoV-2 nucleocapsid protein","volume":"14","author":"Schuck","year":"2023","journal-title":"mBio"},{"key":"bib76","doi-asserted-by":"publisher","DOI":"10.15252\/embj.2020106501","type":"journal-article","article-title":"Opposing activities of IFITM proteins in SARS\u2010CoV\u20102 infection","volume":"40","author":"Shi","year":"2021","journal-title":"The EMBO Journal"},{"key":"bib77","doi-asserted-by":"publisher","DOI":"10.1172\/JCI160766","type":"journal-article","article-title":"Rapalogs downmodulate intrinsic immunity and promote cell entry of SARS-CoV-2","volume":"132","author":"Shi","year":"2022","journal-title":"The Journal of Clinical Investigation"},{"key":"bib78","doi-asserted-by":"publisher","DOI":"10.1101\/2021.08.05.21261642","type":"preprint","article-title":"The Unique Evolutionary Dynamics of the SARS-CoV-2 Delta Variant Israel Consortium of SARS-CoV-2 Sequencing","volume-title":"medRxiv","author":"Stern","year":"2021"},{"key":"bib79","doi-asserted-by":"publisher","first-page":"1626","DOI":"10.1126\/science.abl6184","type":"journal-article","article-title":"Rapid assessment of SARS-CoV-2-evolved variants using virus-like particles","volume":"374","author":"Syed","year":"2021","journal-title":"Science"},{"key":"bib80","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1012741","type":"journal-article","article-title":"SARS-CoV-2 evolution balances conflicting roles of N protein phosphorylation","volume":"20","author":"Syed","year":"2024","journal-title":"PLOS Pathogens"},{"key":"bib81","doi-asserted-by":"publisher","first-page":"391","DOI":"10.1016\/j.ijbiomac.2021.08.026","type":"journal-article","article-title":"The method utilized to purify the SARS-CoV-2 N protein can affect its molecular properties","volume":"188","author":"Tarczewska","year":"2021","journal-title":"International Journal of Biological Macromolecules"},{"key":"bib82","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1016\/j.tibs.2008.10.009","type":"journal-article","article-title":"Do viral proteins possess unique biophysical features?","volume":"34","author":"Tokuriki","year":"2009","journal-title":"Trends in Biochemical Sciences"},{"key":"bib83","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1126\/science.1169375","type":"journal-article","article-title":"Protein dynamism and evolvability","volume":"324","author":"Tokuriki","year":"2009","journal-title":"Science"},{"key":"bib84","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1016\/j.tibs.2007.10.003","type":"journal-article","article-title":"Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions","volume":"33","author":"Tompa","year":"2008","journal-title":"Trends in Biochemical Sciences"},{"key":"bib85","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2022.167891","type":"journal-article","article-title":"Human 14-3-3 proteins site-selectively bind the mutational hotspot region of SARS-CoV-2 nucleoprotein modulating its phosphoregulation","volume":"435","author":"Tugaeva","year":"2023","journal-title":"Journal of Molecular Biology"},{"key":"bib86","doi-asserted-by":"publisher","first-page":"262","DOI":"10.1080\/22221751.2019.1575700","type":"journal-article","article-title":"Genetic diversity and host adaptation of avian H5N1 influenza viruses during human infection","volume":"8","author":"Welkers","year":"2019","journal-title":"Emerging Microbes & Infections"},{"key":"bib87","doi-asserted-by":"publisher","first-page":"1996","DOI":"10.1017\/ice.2021.390","type":"journal-article","article-title":"First identification of SARS-CoV-2 lambda (C.37) variant in Southern Brazil","volume":"43","author":"Wink","year":"2022","journal-title":"Infection Control and Hospital Epidemiology"},{"key":"bib88","doi-asserted-by":"publisher","first-page":"4546","DOI":"10.1128\/jvi.77.8.4546-4557.2003","type":"journal-article","article-title":"Homo-oligomerization of the porcine reproductive and respiratory syndrome virus nucleocapsid protein and the role of disulfide linkages","volume":"77","author":"Wootton","year":"2003","journal-title":"Journal of Virology"},{"key":"bib89","doi-asserted-by":"publisher","first-page":"1055","DOI":"10.1016\/j.cell.2016.05.004","type":"journal-article","article-title":"The structure and dynamics of higher-order assemblies: amyloids, signalosomes, and granules","volume":"165","author":"Wu","year":"2016","journal-title":"Cell"},{"key":"bib90","doi-asserted-by":"publisher","first-page":"403","DOI":"10.1007\/s00249-021-01513-9","type":"journal-article","article-title":"Standard protocol for mass photometry experiments","volume":"50","author":"Wu","year":"2021","journal-title":"European Biophysics Journal"},{"key":"bib91","doi-asserted-by":"publisher","first-page":"1788","DOI":"10.1016\/j.chom.2021.11.005","type":"journal-article","article-title":"Nucleocapsid mutations R203K\/G204R increase the infectivity, fitness, and virulence of SARS-CoV-2","volume":"29","author":"Wu","year":"2021","journal-title":"Cell Host & Microbe"},{"key":"bib92","doi-asserted-by":"publisher","DOI":"10.1186\/s12985-023-01968-6","type":"journal-article","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":"Virology Journal"},{"key":"bib93","doi-asserted-by":"publisher","first-page":"6880","DOI":"10.1021\/cr4005692","type":"journal-article","article-title":"Structural disorder in viral proteins","volume":"114","author":"Xue","year":"2014","journal-title":"Chemical Reviews"},{"key":"bib94","doi-asserted-by":"publisher","first-page":"730","DOI":"10.1016\/j.cell.2020.09.018","type":"journal-article","article-title":"Molecular architecture of the SARS-CoV-2 virus","volume":"183","author":"Yao","year":"2020","journal-title":"Cell"},{"key":"bib95","doi-asserted-by":"publisher","DOI":"10.1128\/mBio.02168-20","type":"journal-article","article-title":"Rescue of SARS-CoV-2 from a single bacterial artificial chromosome","volume":"11","author":"Ye","year":"2020","journal-title":"mBio"},{"key":"bib96","doi-asserted-by":"publisher","first-page":"1890","DOI":"10.1002\/pro.3909","type":"journal-article","article-title":"Architecture and self-assembly of the SARS-CoV-2 nucleocapsid protein","volume":"29","author":"Ye","year":"2020","journal-title":"Protein Science"},{"key":"bib97","doi-asserted-by":"publisher","first-page":"23280","DOI":"10.1074\/jbc.M501015200","type":"journal-article","article-title":"Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain","volume":"280","author":"Yu","year":"2005","journal-title":"The Journal of Biological Chemistry"},{"key":"bib98","doi-asserted-by":"publisher","first-page":"911","DOI":"10.14348\/molcells.2022.0130","type":"journal-article","article-title":"Glycogen synthase kinase-3 interaction domain enhances phosphorylation of SARS-CoV-2 nucleocapsid protein","volume":"45","author":"Yun","year":"2022","journal-title":"Molecules and Cells"},{"key":"bib99","doi-asserted-by":"publisher","DOI":"10.1002\/pro.4409","type":"journal-article","article-title":"Contributions of the N-terminal intrinsically disordered region of the severe acute respiratory syndrome coronavirus 2 nucleocapsid protein to RNA-induced phase separation","volume":"31","author":"Zachrdla","year":"2022","journal-title":"Protein Science"},{"key":"bib100","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.60220","type":"journal-article","article-title":"Identifying molecular features that are associated with biological function of intrinsically disordered protein regions","volume":"10","author":"Zarin","year":"2021","journal-title":"eLife"},{"key":"bib101","doi-asserted-by":"publisher","first-page":"3181","DOI":"10.1021\/ac500093m","type":"journal-article","article-title":"Analysis of protein interactions with picomolar binding affinity by fluorescence-detected sedimentation velocity","volume":"86","author":"Zhao","year":"2014","journal-title":"Analytical Chemistry"},{"key":"bib102","doi-asserted-by":"publisher","DOI":"10.1016\/j.isci.2021.102523","type":"journal-article","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":"bib103","doi-asserted-by":"publisher","DOI":"10.1093\/pnasnexus\/pgac049","type":"journal-article","article-title":"Plasticity in structure and assembly of SARS-CoV-2 nucleocapsid protein","volume":"1","author":"Zhao","year":"2022","journal-title":"PNAS Nexus"},{"key":"bib104","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.adg6473","type":"journal-article","article-title":"A conserved oligomerization domain in the disordered linker of coronavirus nucleocapsid proteins","volume":"9","author":"Zhao","year":"2023","journal-title":"Science Advances"},{"key":"bib105","doi-asserted-by":"publisher","first-page":"6647","DOI":"10.1093\/nar\/gkae256","type":"journal-article","article-title":"Assembly of SARS-CoV-2 nucleocapsid protein with nucleic acid","volume":"52","author":"Zhao","year":"2024","journal-title":"Nucleic Acids Research"},{"key":"bib106","doi-asserted-by":"publisher","first-page":"54","DOI":"10.1016\/j.bbrc.2020.09.131","type":"journal-article","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":"Biochemical and Biophysical Research Communications"},{"key":"dataset1","doi-asserted-by":"publisher","DOI":"10.7910\/DVN\/4JPARC","type":"dataset","article-title":"Replication Data for: Evolution of a fuzzy ribonucleoprotein complex in viral assembly","volume-title":"Harvard Dataverse","author":"Zhao","year":"2025","unstructured":"Zhao H, Li T, Hassan SA, Nguyen A, Datta SAK, Zhang G, Trent C, Czaja AM, Wu D, Aronova MA, Lai KK, Piszczek G, Leapman RD, Yewdell JW, Schuck P. 2025. Replication Data for: Evolution of a fuzzy ribonucleoprotein complex in viral assembly. Harvard Dataverse."}],"container-title":["eLife"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/cdn.elifesciences.org\/articles\/108922\/elife-108922-v1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/cdn.elifesciences.org\/articles\/108922\/elife-108922-v1.xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/elifesciences.org\/articles\/108922","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T09:13:31Z","timestamp":1787562811000},"score":1,"resource":{"primary":{"URL":"https:\/\/elifesciences.org\/articles\/108922"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12,30]]},"references-count":107,"alternative-id":["10.7554\/eLife.108922"],"URL":"https:\/\/doi.org\/10.7554\/elife.108922","archive":["CLOCKSS"],"relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2025.04.26.650775","asserted-by":"subject"}],"is-same-as":[{"id-type":"doi","id":"10.7554\/eLife.108922.3","asserted-by":"subject"}],"is-version-of":[{"id-type":"doi","id":"10.7554\/eLife.108922.1","asserted-by":"subject"},{"id-type":"doi","id":"10.7554\/eLife.108922.2","asserted-by":"subject"}],"is-supplemented-by":[{"id-type":"doi","id":"10.7910\/DVN\/4JPARC","asserted-by":"subject"}]},"ISSN":["2050-084X"],"issn-type":[{"value":"2050-084X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,12,30]]},"assertion":[{"value":"single anonymised","name":"peer_review_transparency","label":"Peer review transparency","group":{"name":"peer_review_taxonomy"}},{"value":"other reviewer(s), editor","name":"peer_review_interaction","label":"Peer review interaction","group":{"name":"peer_review_taxonomy"}},{"value":"review summaries, review reports, author\/editor communication, reviewer identities reviewer opt in, editor identities","name":"peer_review_published","label":"Peer review published","group":{"name":"peer_review_taxonomy"}},{"value":"open (sign in with ORCID iD required)","name":"post_publication_commenting","label":"Post publication commenting","group":{"name":"post_publication_commenting"}}],"article-number":"RP108922"}}