{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,4]],"date-time":"2026-11-04T21:20:03Z","timestamp":1793827203508,"version":"4.6.1"},"reference-count":45,"publisher":"Elsevier BV","issue":"20","license":[{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["P01AI120943"],"award-info":[{"award-number":["P01AI120943"]}],"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":["P41GM103422"],"award-info":[{"award-number":["P41GM103422"]}],"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":["R01AI107056"],"award-info":[{"award-number":["R01AI107056"]}],"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":["R01AI123926"],"award-info":[{"award-number":["R01AI123926"]}],"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":["R01AI143292"],"award-info":[{"award-number":["R01AI143292"]}],"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":["R01AI148663 C.F.B"],"award-info":[{"award-number":["R01AI148663 C.F.B"]}],"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":["R24GM136766"],"award-info":[{"award-number":["R24GM136766"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2023,10]]},"DOI":"10.1016\/j.jmb.2023.168241","type":"journal-article","created":{"date-parts":[[2023,8,19]],"date-time":"2023-08-19T02:43:20Z","timestamp":1692413000000},"page":"168241","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":11,"title":["Disruption of Ebola NP0VP35 Inclusion Body-like Structures reduce Viral Infection"],"prefix":"10.1016","volume":"435","author":[{"given":"Chao","family":"Wu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicole D.","family":"Wagner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Austin B.","family":"Moyle","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Annie","family":"Feng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nitin","family":"Sharma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah H.","family":"Stubbs","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Callie","family":"Donahue","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert A.","family":"Davey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael L.","family":"Gross","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daisy W.","family":"Leung","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0418-9707","authenticated-orcid":false,"given":"Gaya K.","family":"Amarasinghe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2023.168241_b0005","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1038\/s41579-019-0233-2","article-title":"Therapeutic strategies to target the Ebola virus life cycle","volume":"17","author":"Hoenen","year":"2019","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.jmb.2023.168241_b0010","doi-asserted-by":"crossref","first-page":"e231","DOI":"10.1016\/S1473-3099(20)30282-6","article-title":"Recent successes in therapeutics for Ebola virus disease: no time for complacency","volume":"20","author":"Iversen","year":"2020","journal-title":"Lancet Infect. Dis."},{"key":"10.1016\/j.jmb.2023.168241_b0015","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1038\/nrmicro3524","article-title":"Filovirus pathogenesis and immune evasion: insights from Ebola virus and Marburg virus","volume":"13","author":"Messaoudi","year":"2015","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.jmb.2023.168241_b0020","doi-asserted-by":"crossref","first-page":"11779","DOI":"10.1128\/JVI.01525-12","article-title":"Inclusion bodies are a site of ebolavirus replication","volume":"86","author":"Hoenen","year":"2012","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2023.168241_b0025","doi-asserted-by":"crossref","first-page":"4914","DOI":"10.1128\/JVI.03257-15","article-title":"Dynamic phosphorylation of VP30 Is essential for Ebola virus life cycle","volume":"90","author":"Biedenkopf","year":"2016","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2023.168241_b0030","doi-asserted-by":"crossref","first-page":"e0005996","DOI":"10.1371\/journal.pntd.0005996","article-title":"Characterization of the catalytic center of the Ebola virus L polymerase","volume":"11","author":"Schmidt","year":"2017","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.jmb.2023.168241_b0035","doi-asserted-by":"crossref","first-page":"e02100","DOI":"10.1128\/JVI.02100-19","article-title":"Ebola virus inclusion body formation and RNA synthesis are controlled by a novel domain of nucleoprotein interacting with VP35","volume":"94","author":"Miyake","year":"2020","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2023.168241_b0040","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/nrm.2017.7","article-title":"Biomolecular condensates: organizers of cellular biochemistry","volume":"18","author":"Banani","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2023.168241_b0045","first-page":"null","article-title":"Liquid phase partitioning in virus replication: observations and opportunities","volume":"9","author":"Wu","year":"2022","journal-title":"Ann. Rev. Virol."},{"key":"10.1016\/j.jmb.2023.168241_b0050","doi-asserted-by":"crossref","first-page":"e01099","DOI":"10.1128\/mbio.01099-22","article-title":"Human metapneumovirus phosphoprotein independently drives phase separation and recruits nucleoprotein to liquid-like bodies","volume":"13","author":"Boggs","year":"2022","journal-title":"MBio"},{"key":"10.1016\/j.jmb.2023.168241_b0055","doi-asserted-by":"crossref","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":"10.1016\/j.jmb.2023.168241_b0060","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1038\/s41586-021-03703-z","article-title":"A condensate-hardening drug blocks RSV replication in vivo","volume":"595","author":"Risso-Ballester","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2023.168241_b0065","doi-asserted-by":"crossref","first-page":"2698","DOI":"10.1099\/vir.0.2008\/004051-0","article-title":"Human metapneumovirus nucleoprotein and phosphoprotein interact and provide the minimal requirements for inclusion body formation","volume":"89","author":"Derdowski","year":"2008","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.jmb.2023.168241_b0070","doi-asserted-by":"crossref","first-page":"7948","DOI":"10.1128\/JVI.00554-09","article-title":"Functional characterization of Negri Bodies (NBs) in rabies virus-infected cells: evidence that NBs are sites of viral transcription and replication","volume":"83","author":"Lahaye","year":"2009","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2023.168241_b0075","doi-asserted-by":"crossref","first-page":"e1000958","DOI":"10.1371\/journal.ppat.1000958","article-title":"Protein expression redirects vesicular stomatitis virus RNA synthesis to cytoplasmic inclusions","volume":"6","author":"Heinrich","year":"2010","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2023.168241_b0080","doi-asserted-by":"crossref","first-page":"2229","DOI":"10.1016\/j.celrep.2019.10.052","article-title":"PI4KB on inclusion bodies formed by ER membrane remodeling facilitates replication of human Parainfluenza virus type 3","volume":"29","author":"Li","year":"2019","journal-title":"Cell Reports"},{"key":"10.1016\/j.jmb.2023.168241_b0085","doi-asserted-by":"crossref","first-page":"e1007733","DOI":"10.1371\/journal.ppat.1007733","article-title":"Nipah virus induces two inclusion body populations: Identification of novel inclusions at the plasma membrane","volume":"15","author":"Ringel","year":"2019","journal-title":"PLoS Pathog."},{"issue":"Pt 12","key":"10.1016\/j.jmb.2023.168241_b0090","doi-asserted-by":"crossref","first-page":"3525","DOI":"10.1099\/0022-1317-75-12-3525","article-title":"Evidence that the paramyxovirus simian virus 5 can establish quiescent infections by remaining inactive in cytoplasmic inclusion bodies","volume":"75","author":"Fearns","year":"1994","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.jmb.2023.168241_b0105","doi-asserted-by":"crossref","first-page":"7268","DOI":"10.1128\/JVI.00459-16","article-title":"Ebola virus does not induce stress granule formation during infection and sequesters stress granule proteins within viral inclusions","volume":"90","author":"Nelson","year":"2016","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2023.168241_b0135","doi-asserted-by":"crossref","first-page":"366","DOI":"10.3390\/v13030366","article-title":"Liquid biomolecular condensates and viral lifecycles: review and perspectives","volume":"13","author":"Etibor","year":"2021","journal-title":"Viruses"},{"key":"10.1016\/j.jmb.2023.168241_b0140","doi-asserted-by":"crossref","first-page":"S878","DOI":"10.1093\/infdis\/jir310","article-title":"The importance of the NP: VP35 ratio in Ebola virus nucleocapsid formation","volume":"204","author":"Noda","year":"2011","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.jmb.2023.168241_b0145","doi-asserted-by":"crossref","first-page":"2223727","DOI":"10.1080\/22221751.2023.2223727","article-title":"Ebola virus inclusion bodies are liquid organelles whose formation is facilitated by nucleoprotein oligomerization","author":"Bodmer","year":"2023","journal-title":"Emerg. Microbes Infect."},{"key":"10.1016\/j.jmb.2023.168241_b0150","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.virol.2017.09.006","article-title":"Dynamic phosphorylation of Ebola virus VP30 in NP-induced inclusion bodies","volume":"512","author":"Lier","year":"2017","journal-title":"Virology"},{"key":"10.1016\/j.jmb.2023.168241_b0155","doi-asserted-by":"crossref","first-page":"15576","DOI":"10.1038\/ncomms15576","article-title":"Ebola virus VP30 and nucleoprotein interactions modulate viral RNA synthesis","volume":"8","author":"Xu","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jmb.2023.168241_b0160","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1021\/acs.biochem.8b01154","article-title":"The Ebola viral protein 35 N-terminus is a parallel tetramer","volume":"58","author":"Chanthamontri","year":"2019","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2023.168241_b0165","doi-asserted-by":"crossref","first-page":"966","DOI":"10.1016\/j.cell.2018.02.009","article-title":"Electron cryo-microscopy structure of Ebola virus nucleoprotein reveals a mechanism for nucleocapsid-like assembly","volume":"172","author":"Su","year":"2018","journal-title":"Cell."},{"key":"10.1016\/j.jmb.2023.168241_b0170","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1016\/j.celrep.2015.03.034","article-title":"An intrinsically disordered peptide from Ebola virus VP35 controls viral RNA synthesis by modulating nucleoprotein-RNA interactions","volume":"11","author":"Leung","year":"2015","journal-title":"Cell Rep"},{"key":"10.1016\/j.jmb.2023.168241_b0175","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.cell.2018.12.035","article-title":"Considerations and challenges in studying liquid-liquid phase separation and biomolecular condensates","volume":"176","author":"Alberti","year":"2019","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2023.168241_b0180","doi-asserted-by":"crossref","first-page":"10581","DOI":"10.1128\/JVI.00925-10","article-title":"Basic residues within the Ebolavirus VP35 protein are required for its viral polymerase cofactor function","volume":"84","author":"Prins","year":"2010","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2023.168241_b0185","doi-asserted-by":"crossref","first-page":"7500","DOI":"10.1021\/acs.chemrev.1c00786","article-title":"Cross-linking mass spectrometry for investigating protein conformations and protein-protein interactions\u2500A method for all seasons","volume":"122","author":"Piersimoni","year":"2022","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jmb.2023.168241_b0195","doi-asserted-by":"crossref","first-page":"6642","DOI":"10.1128\/JVI.00602-16","article-title":"HSP90 chaperoning in addition to phosphoprotein required for folding but not for supporting enzymatic activities of measles and Nipah virus L polymerases","volume":"90","author":"Bloyet","year":"2016","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2023.168241_b0200","doi-asserted-by":"crossref","first-page":"e02220","DOI":"10.1128\/JVI.02220-16","article-title":"Heat shock protein 90 ensures efficient mumps virus replication by assisting with viral polymerase complex formation","volume":"91","author":"Katoh","year":"2017","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2023.168241_b0205","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/j.str.2022.02.002","article-title":"Chemical probing provides insight into the native assembly state of a bacterial microcompartment","volume":"30","author":"Trettel","year":"2022","journal-title":"Structure."},{"key":"10.1016\/j.jmb.2023.168241_b0210","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1007\/s13361-015-1331-7","article-title":"Conformational analysis of proteins in highly concentrated solutions by dialysis-coupled hydrogen\/deuterium exchange mass spectrometry","volume":"27","author":"Houde","year":"2016","journal-title":"J. Am. Soc. Mass Spectrom."},{"key":"10.1016\/j.jmb.2023.168241_b0215","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1080\/19420862.2019.1589850","article-title":"Hydrogen\/deuterium exchange-mass spectrometry analysis of high concentration biotherapeutics: application to phase-separated antibody formulations","volume":"11","author":"Tian","year":"2019","journal-title":"MAbs"},{"key":"10.1016\/j.jmb.2023.168241_b0220","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1074\/mcp.M200025-MCP200","article-title":"Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics","volume":"1","author":"Ong","year":"2002","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.jmb.2023.168241_b0225","doi-asserted-by":"crossref","first-page":"eabb4309","DOI":"10.1126\/science.abb4309","article-title":"HSP70 chaperones RNA-free TDP-43 into anisotropic intranuclear liquid spherical shells","volume":"371","author":"Yu","year":"2021","journal-title":"Science"},{"key":"10.1016\/j.jmb.2023.168241_b0230","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1038\/nsmb.3368","article-title":"The evolutionary capacitor HSP90 buffers the regulatory effects of mammalian endogenous retroviruses","volume":"24","author":"Hummel","year":"2017","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jmb.2023.168241_b0235","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1038\/24550","article-title":"Hsp90 as a capacitor for morphological evolution","volume":"396","author":"Rutherford","year":"1998","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2023.168241_b0245","doi-asserted-by":"crossref","first-page":"2690","DOI":"10.1074\/mcp.M110.003418","article-title":"Identification of essential filovirion-associated host factors by serial proteomic analysis and RNAi screen","volume":"9","author":"Spurgers","year":"2010","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.jmb.2023.168241_b0250","doi-asserted-by":"crossref","first-page":"4290","DOI":"10.1021\/acs.jproteome.6b00337","article-title":"Elucidation of the cellular interactome of ebola virus nucleoprotein and identification of therapeutic targets","volume":"15","author":"Garc\u00eda-Dorival","year":"2016","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.jmb.2023.168241_b0255","doi-asserted-by":"crossref","first-page":"3970","DOI":"10.1038\/s41598-018-22328-3","article-title":"Recombinant RNA-dependent RNA polymerase complex of Ebola virus","volume":"8","author":"Tchesnokov","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jmb.2023.168241_b0260","doi-asserted-by":"crossref","first-page":"10511","DOI":"10.1128\/JVI.01272-14","article-title":"A novel life cycle modeling system for Ebola virus shows a genome length-dependent role of VP24 in virus infectivity","volume":"88","author":"Watt","year":"2014","journal-title":"J. Virol."},{"key":"10.1016\/j.jmb.2023.168241_bib261","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1073\/pnas.0807854106","article-title":"Structure of the Ebola VP35 interferon inhibitory domain","volume":"106","author":"Leung","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"10.1016\/j.jmb.2023.168241_bib262","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1038\/nsmb.1765","article-title":"Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35","volume":"17","author":"Leung","year":"2010","journal-title":"Nat. Struct. Mol. Biol."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283623003522?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283623003522?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T21:56:10Z","timestamp":1758318970000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283623003522"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,10]]},"references-count":45,"journal-issue":{"issue":"20","published-print":{"date-parts":[[2023,10]]}},"alternative-id":["S0022283623003522"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2023.168241","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2023,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Disruption of Ebola NP0VP35 Inclusion Body-like Structures reduce Viral Infection","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2023.168241","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}],"article-number":"168241"}}