{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,21]],"date-time":"2026-07-21T00:30:24Z","timestamp":1784593824225,"version":"3.55.0"},"reference-count":230,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31872425"],"award-info":[{"award-number":["31872425"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Colloids and Surfaces B: Biointerfaces"],"published-print":{"date-parts":[[2025,2]]},"DOI":"10.1016\/j.colsurfb.2024.114385","type":"journal-article","created":{"date-parts":[[2024,11,17]],"date-time":"2024-11-17T20:44:31Z","timestamp":1731876271000},"page":"114385","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":8,"special_numbering":"C","title":["Liquid-liquid phase separation in viral infection: From the occurrence and function to treatment potentials"],"prefix":"10.1016","volume":"246","author":[{"given":"Zhaoxiao","family":"Cao","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yanhua","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Simeng","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tiancheng","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peng","family":"L\u00fc","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keping","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.colsurfb.2024.114385_bib1","doi-asserted-by":"crossref","first-page":"1729","DOI":"10.1126\/science.1172046","article-title":"Germline P granules are liquid droplets that localize by controlled dissolution\/condensation","volume":"324","author":"Brangwynne","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.colsurfb.2024.114385_bib2","doi-asserted-by":"crossref","first-page":"4334","DOI":"10.1073\/pnas.1017150108","article-title":"Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes","volume":"108","author":"Brangwynne","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.colsurfb.2024.114385_bib3","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1038\/s41580-020-0272-6","article-title":"The nucleolus as a multiphase liquid condensate","volume":"22","author":"Lafontaine","year":"2021","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib4","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1091\/mbc.e04-08-0742","article-title":"Cajal bodies, nucleoli, and speckles in the Xenopus oocyte nucleus have a low-density, sponge-like structure","volume":"16","author":"Handwerger","year":"2005","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib5","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.molcel.2010.09.024","article-title":"The nucleolus under stress","volume":"40","author":"Boulon","year":"2010","journal-title":"Mol. Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib6","first-page":"a012286","article-title":"P-bodies and stress granules: possible roles in the control of translation and mRNA degradation","volume":"4","author":"Decker","year":"2012","journal-title":"CSH Perspect. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib7","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1083\/jcb.201504117","article-title":"Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles","volume":"210","author":"Hennig","year":"2015","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib8","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.colsurfb.2024.114385_bib9","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1038\/s41421-020-00240-3","article-title":"SARS-CoV-2 nucleocapsid protein undergoes liquid-liquid phase separation into stress granules through its N-terminal intrinsically disordered region","volume":"7","author":"Wang","year":"2021","journal-title":"Cell Discov."},{"key":"10.1016\/j.colsurfb.2024.114385_bib10","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1186\/s12977-023-00619-6","article-title":"Biomolecular condensates: insights into early and late steps of the HIV-1 replication cycle","volume":"20","author":"Di Nunzio","year":"2023","journal-title":"Retrovirology"},{"key":"10.1016\/j.colsurfb.2024.114385_bib11","article-title":"Liquid-liquid phase separation: a new perspective on respiratory diseases","volume":"15","author":"Wang","year":"2024","journal-title":"Front. Immunol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib12","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.colsurfb.2024.114385_bib13","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1523\/JNEUROSCI.1656-20.2020","article-title":"Liquid-liquid phase separation in physiology and pathophysiology of the nervous system","volume":"41","author":"Hayashi","year":"2021","journal-title":"J. Neurosci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib14","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.colsurfb.2024.114385_bib15","doi-asserted-by":"crossref","DOI":"10.1021\/acs.langmuir.3c03272","article-title":"Molecular modeling of the adsorption of an egg yolk protein on a water-oil interface","author":"Lombardo Pontillo","year":"2024","journal-title":"Langmuir 3c03272"},{"key":"10.1016\/j.colsurfb.2024.114385_bib16","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1038\/s41392-021-00678-1","article-title":"Liquid-liquid phase separation in human health and diseases","volume":"6","author":"Wang","year":"2021","journal-title":"Signal Transduct. Tar."},{"key":"10.1016\/j.colsurfb.2024.114385_bib17","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.30294","article-title":"Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins","volume":"6","author":"Harmon","year":"2017","journal-title":"Elife"},{"key":"10.1016\/j.colsurfb.2024.114385_bib18","article-title":"Molecular mechanisms and cellular functions of liquid-liquid phase separation during antiviral immuneresponses","volume":"14","author":"Yang","year":"2023","journal-title":"Front. Immunol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib19","doi-asserted-by":"crossref","first-page":"14823","DOI":"10.1074\/jbc.REV119.007895","article-title":"Formation of biological condensates via phase separation: characteristics, analytical methods, and physiological implications","volume":"294","author":"Feng","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.colsurfb.2024.114385_bib20","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.31486","article-title":"Pi-Pi contacts are an overlooked protein feature relevant to phase separation","volume":"7","author":"Vernon","year":"2018","journal-title":"Elife"},{"key":"10.1016\/j.colsurfb.2024.114385_bib21","doi-asserted-by":"crossref","first-page":"14050","DOI":"10.3390\/ijms232214050","article-title":"Intrinsically disordered proteins: an overview.","volume":"23","author":"Trivedi","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib22","doi-asserted-by":"crossref","first-page":"2499","DOI":"10.1021\/acs.biochem.8b00058","article-title":"Theories for sequence-dependent phase behaviors of biomolecular cndensates","volume":"57","author":"Lin","year":"2018","journal-title":"Biochemistry"},{"key":"10.1016\/j.colsurfb.2024.114385_bib23","doi-asserted-by":"crossref","DOI":"10.1016\/j.jsbmb.2019.105571","article-title":"Ordered structure-forming properties of the intrinsically disordered AB region of hRXR\u03b3 and its ability to promote liquid-liquid phase separation","volume":"198","author":"So\u0142tys","year":"2020","journal-title":"J. Steroid Biochem. Mol. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib24","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.molcel.2016.05.042","article-title":"Sequence determinants of intracellular phase separation by complex coacervation of a disordered protein","volume":"63","author":"Pak","year":"2016","journal-title":"Mol. Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib25","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.tcb.2018.02.004","article-title":"Protein phase separation: a new phase in cell biology","volume":"28","author":"Boeynaems","year":"2018","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib26","doi-asserted-by":"crossref","DOI":"10.1016\/j.bpc.2022.106769","article-title":"Intrinsically disordered proteins\/regions and insight into their biomolecular interactions","volume":"283","author":"Chakrabarti","year":"2022","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.colsurfb.2024.114385_bib27","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1007\/s11427-020-1702-x","article-title":"Liquid-liquid phase separation in biology: mechanisms, physiological functions and human diseases","volume":"63","author":"Zhang","year":"2020","journal-title":"Sci. China Life Sci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib28","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.04123","article-title":"Phase transitions of multivalent proteins can promote clustering of membrane receptors","volume":"3","author":"Banjade","year":"2014","journal-title":"Elife"},{"key":"10.1016\/j.colsurfb.2024.114385_bib29","doi-asserted-by":"crossref","first-page":"18078","DOI":"10.1073\/pnas.1815275116","article-title":"CPEB3 inhibits translation of mRNA targets by localizing them to P bodies","volume":"116","author":"Ford","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.colsurfb.2024.114385_bib30","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1038\/nature10879","article-title":"Phase transitions in the assembly of multivalent signalling proteins","volume":"483","author":"Li","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.colsurfb.2024.114385_bib31","doi-asserted-by":"crossref","DOI":"10.1016\/j.biopha.2021.111520","article-title":"Protein phase separation and its role in chromatin organization and diseases","volume":"138","author":"Li","year":"2021","journal-title":"Biomed. Pharmacother."},{"key":"10.1016\/j.colsurfb.2024.114385_bib32","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/bs.apcsb.2021.12.002","article-title":"Understanding binding affinity and specificity of modular protein domains: a focus in ligand design for the polyproline-binding families","volume":"130","author":"Martinez","year":"2022","journal-title":"Adv. Protein Chem. Struct. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib33","first-page":"3766","article-title":"Liquid-liquid phase separation (LLPS) in cellular physiology and tumor biology","volume":"11","author":"Peng","year":"2021","journal-title":"Am. J. Cancer Res."},{"key":"10.1016\/j.colsurfb.2024.114385_bib34","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/j.molcel.2015.09.017","article-title":"RNA controls polyQ protein phase transitions","volume":"60","author":"Zhang","year":"2015","journal-title":"Mol. Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib35","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1038\/nature22386","article-title":"RNA phase transitions in repeat expansion disorders","volume":"546","author":"Jain","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.colsurfb.2024.114385_bib36","doi-asserted-by":"crossref","first-page":"918","DOI":"10.1126\/science.aar7366","article-title":"RNA buffers the phase separation behavior of prion-like RNA binding proteins","volume":"360","author":"Maharana","year":"2018","journal-title":"Science"},{"key":"10.1016\/j.colsurfb.2024.114385_bib37","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1126\/science.aat1022","article-title":"DNA-induced liquid phase condensation of cGAS activates innate immune signaling","volume":"361","author":"Du","year":"2018","journal-title":"Science"},{"key":"10.1016\/j.colsurfb.2024.114385_bib38","doi-asserted-by":"crossref","first-page":"11946","DOI":"10.1073\/pnas.1905013116","article-title":"Human cGAS catalytic domain has an additional DNA-binding interface that enhances enzymatic activity and liquid-phase condensation","volume":"116","author":"Xie","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.colsurfb.2024.114385_bib39","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1016\/j.cell.2017.02.027","article-title":"Stress-triggered phase separation is an adaptive, evolutionarily tuned response","volume":"168","author":"Riback","year":"2017","journal-title":"Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib40","doi-asserted-by":"crossref","first-page":"691","DOI":"10.3390\/polym11040691","article-title":"Upper critical solution temperature (UCST) behavior of coacervate of cationic protamine and multivalent anions","volume":"11","author":"Kim","year":"2019","journal-title":"Polymers"},{"key":"10.1016\/j.colsurfb.2024.114385_bib41","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1007\/978-1-0716-0524-0_36","article-title":"In vitro transition temperature measurement of phase-separating proteins by microscopy","volume":"2141","author":"Holland","year":"2020","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib42","doi-asserted-by":"crossref","first-page":"1590","DOI":"10.1016\/j.bpj.2020.07.044","article-title":"Liquid phase separation controlled by pH","volume":"119","author":"Adame-Arana","year":"2020","journal-title":"Biophys. J."},{"key":"10.1016\/j.colsurfb.2024.114385_bib43","doi-asserted-by":"crossref","first-page":"27214","DOI":"10.1039\/C8CP05884A","article-title":"Tuning phase transitions of aqueous protein solutions by multivalent cations","volume":"20","author":"Matsarskaia","year":"2018","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.colsurfb.2024.114385_bib44","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1021\/acs.biochem.7b00990","article-title":"Phase separation behavior of supercharged proteins and polyelectrolytes","volume":"57","author":"Cummings","year":"2018","journal-title":"Biochemistry"},{"key":"10.1016\/j.colsurfb.2024.114385_bib45","doi-asserted-by":"crossref","first-page":"13275","DOI":"10.1039\/D1CC05266G","article-title":"Regulation of liquid-liquid phase separation with focus on post-translational modifications","volume":"57","author":"Luo","year":"2021","journal-title":"Chem. Commun."},{"key":"10.1016\/j.colsurfb.2024.114385_bib46","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/j.tibs.2022.12.003","article-title":"Protein SUMOylation and phase separation: partners in stress?","volume":"48","author":"Cheng","year":"2023","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib47","doi-asserted-by":"crossref","first-page":"7137","DOI":"10.1074\/jbc.TM118.001189","article-title":"Friend or foe-post-translational modifications as regulators of phase separation and RNP granule dynamics","volume":"294","author":"Hofweber","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.colsurfb.2024.114385_bib48","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.tcb.2021.08.004","article-title":"Spatiotemporal dynamic regulation of membraneless organelles by chaperone networks","volume":"32","author":"Li","year":"2022","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib49","doi-asserted-by":"crossref","first-page":"9186","DOI":"10.3390\/ijms21239186","article-title":"Mechanistic insights into the role of molecular chaperones in protein misfolding diseases: from molecular recognition to amyloid disassembly","volume":"21","author":"Herv\u00e1s","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib50","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1002\/1873-3468.14682","article-title":"The roles of molecular chaperones in regulating cell metabolism","volume":"597","author":"Binder","year":"2023","journal-title":"FEBS Lett."},{"key":"10.1016\/j.colsurfb.2024.114385_bib51","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/j.cell.2015.07.047","article-title":"A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation","volume":"162","author":"Patel","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib52","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.cell.2016.11.054","article-title":"Spatiotemporal control of intracellular phase transitions using light-activated optoDroplets","volume":"168","author":"Shin","year":"2017","journal-title":"Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib53","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1038\/s41594-019-0193-2","article-title":"A gel phase promotes condensation of liquid P granules in Caenorhabditis elegans embryos","volume":"26","author":"Putnam","year":"2019","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib54","doi-asserted-by":"crossref","DOI":"10.1016\/j.sbi.2022.102346","article-title":"Nucleic acid actions on abnormal protein aggregation, phase transitions and phase separation","volume":"73","author":"Silva","year":"2022","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib55","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2022.167713","article-title":"Liquid-liquid phase separation of \u03b1-synuclein: a new mechanistic insight for \u03b1-synuclein aggregation associated with parkinson's disease pathogenesis","volume":"435","author":"Mukherjee","year":"2023","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib56","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1126\/science.aaf6846","article-title":"ATP as a biological hydrotrope","volume":"356","author":"Patel","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.colsurfb.2024.114385_bib57","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1016\/j.tibs.2020.12.005","article-title":"FUS and TDP-43 phases in health and disease","volume":"46","author":"Portz","year":"2021","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib58","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1038\/s42003-023-04480-3","article-title":"ATP and nucleic acids competitively modulate LLPS of the SARS-CoV2 nucleocapsid protein","volume":"6","author":"Dang","year":"2023","journal-title":"Commun. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib59","doi-asserted-by":"crossref","DOI":"10.15252\/embj.201798049","article-title":"Tau protein liquid-liquid phase separation can initiate tau aggregation","volume":"37","author":"Wegmann","year":"2018","journal-title":"Embo J."},{"key":"10.1016\/j.colsurfb.2024.114385_bib60","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1016\/j.tcb.2022.01.011","article-title":"Tau liquid-liquid phase separation in neurodegenerative diseases","volume":"32","author":"Boyko","year":"2022","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib61","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1038\/s41568-022-00444-7","article-title":"Liquid-liquid phase separation drives cellular function and dysfunction in cancer","volume":"22","author":"Mehta","year":"2022","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.colsurfb.2024.114385_bib62","doi-asserted-by":"crossref","first-page":"5759","DOI":"10.1016\/j.cell.2021.09.032","article-title":"Phase separation drives RNA virus-induced activation of the NLRP6 inflammasome","volume":"184","author":"Shen","year":"2021","journal-title":"Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib63","doi-asserted-by":"crossref","first-page":"4704","DOI":"10.7150\/ijbs.72663","article-title":"Signaling mechanisms of SARS-CoV-2 nucleocapsid protein in viral infection, cell death and inflammation","volume":"18","author":"Wang","year":"2022","journal-title":"Int. J. Biol. Sci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib64","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.42906","article-title":"Nanoscale organization of rotavirus replication machineries","volume":"8","author":"Garc\u00e9s Su\u00e1rez","year":"2019","journal-title":"Elife"},{"key":"10.1016\/j.colsurfb.2024.114385_bib65","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1111\/mmi.15182","article-title":"Molecular mapping of virus-infected cells with immunogold and metal-tagging transmission electron microscopy","volume":"121","author":"Sachse","year":"2024","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib66","doi-asserted-by":"crossref","first-page":"1404","DOI":"10.1128\/JVI.02046-13","article-title":"DNA virus replication compartments","volume":"88","author":"Schmid","year":"2014","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib67","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1146\/annurev-virology-031413-085548","article-title":"Viruses and the DNA damage response: activation and antagonism","volume":"1","author":"Luftig","year":"2014","journal-title":"Annu. Rev. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib68","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1146\/annurev-virology-092917-043534","article-title":"Virus DNA replication and the host DNA damage response","volume":"5","author":"Weitzman","year":"2018","journal-title":"Annu. Rev. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib69","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1128\/CMR.00116-13","article-title":"Adenovirus infections in immunocompetent and immunocompromised patients","volume":"27","author":"Lion","year":"2014","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.colsurfb.2024.114385_bib70","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1186\/s12985-021-01661-6","article-title":"Human adenoviruses in paediatric patients with respiratory tract infections in Beijing, China","volume":"18","author":"Huang","year":"2021","journal-title":"Virol. J."},{"key":"10.1016\/j.colsurfb.2024.114385_bib71","doi-asserted-by":"crossref","first-page":"1778","DOI":"10.3390\/v13091778","article-title":"Evidence that the adenovirus single-stranded DNA binding protein mediates the assembly of biomolecular condensates to form viral replication compartments","volume":"13","author":"Hidalgo","year":"2021","journal-title":"Viruses"},{"key":"10.1016\/j.colsurfb.2024.114385_bib72","doi-asserted-by":"crossref","first-page":"2994","DOI":"10.1002\/j.1460-2075.1994.tb06598.x","article-title":"Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding","volume":"13","author":"Tucker","year":"1994","journal-title":"Embo J."},{"key":"10.1016\/j.colsurfb.2024.114385_bib73","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1128\/JVI.02545-15","article-title":"An adenovirus DNA replication factor, but not incoming genome complexes, targets PML nuclear bodies","volume":"90","author":"Komatsu","year":"2016","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib74","doi-asserted-by":"crossref","first-page":"3518","DOI":"10.1002\/1873-3468.13672","article-title":"Formation of adenovirus DNA replication compartments","volume":"593","author":"Hidalgo","year":"2019","journal-title":"FEBS Lett."},{"key":"10.1016\/j.colsurfb.2024.114385_bib75","doi-asserted-by":"crossref","DOI":"10.3389\/fbinf.2023.1123307","article-title":"Human adenovirus DNA polymerase is evolutionarily and functionally associated with human telomerase reverse transcriptase based on in silico molecular characterization that implicate abacavir and zidovudine","volume":"3","author":"Fatoki","year":"2023","journal-title":"Front. Bioinform."},{"key":"10.1016\/j.colsurfb.2024.114385_bib76","first-page":"a013003","article-title":"Adenovirus DNA replication","volume":"5","author":"Hoeben","year":"2013","journal-title":"Csh. Perspect. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib77","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1016\/j.cell.2018.10.057","article-title":"Liquid nuclear condensates mechanically sense and restructure the genome","volume":"175","author":"Shin","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib78","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1007\/s12250-017-4108-2","article-title":"Herpesviruses: epidemiology, pathogenesis, and interventions","volume":"32","author":"Lan","year":"2017","journal-title":"Virol. Sin."},{"key":"10.1016\/j.colsurfb.2024.114385_bib79","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1055\/s-0039-1687837","article-title":"Herpesvirus infections of the central nervous system","volume":"39","author":"Bharucha","year":"2019","journal-title":"Semin. Neurol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib80","doi-asserted-by":"crossref","DOI":"10.1099\/jgv.0.001673","article-title":"ICTV virus taxonomy profile: Herpesviridae 2021","volume":"102","author":"Gatherer","year":"2021","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib81","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1103411108","article-title":"Herpesviral replication compartments move and coalesce at nuclear speckles to enhance export of viral late mRNA","volume":"108","author":"Chang","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.colsurfb.2024.114385_bib82","doi-asserted-by":"crossref","unstructured":"C.M. Metrick, A.L. Koenigsberg, E.E. Heldwein, 2020. Conserved outer tegument component UL11 from herpes simplex virus 1 is an intrinsically disordered, RNA-binding protein, mBio 11, e00810-20. https:\/\/doi.org\/10.1128\/mBio00810-20.","DOI":"10.1128\/mBio.00810-20"},{"key":"10.1016\/j.colsurfb.2024.114385_bib83","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1186\/s12964-016-0132-3","article-title":"The new (dis)order in RNA regulation","volume":"14","author":"J\u00e4rvelin","year":"2016","journal-title":"Cell Commun. Signal."},{"key":"10.1016\/j.colsurfb.2024.114385_bib84","doi-asserted-by":"crossref","first-page":"5084","DOI":"10.3390\/v7092861","article-title":"Tegument assembly and secondary envelopment of alphaherpesviruses","volume":"7","author":"Owen","year":"2015","journal-title":"Viruses"},{"issue":"9","key":"10.1016\/j.colsurfb.2024.114385_bib85","doi-asserted-by":"crossref","DOI":"10.3390\/ijms22094447","article-title":"The HSV-1 transcription factor ICP4 confers liquid-like properties to viral replication compartments","volume":"22","author":"Seyffert","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib86","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2022.110469","article-title":"Human cytomegalovirus forms phase-separated compartments at viral genomes to facilitate viral replication","volume":"38","author":"Caragliano","year":"2022","journal-title":"Cell Rep."},{"issue":"17","key":"10.1016\/j.colsurfb.2024.114385_bib87","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00254-17","article-title":"Differential requirement of human cytomegalovirus UL112-113 protein isoforms for viral replication","volume":"91","author":"Schommartz","year":"2017","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib88","doi-asserted-by":"crossref","first-page":"1040","DOI":"10.1128\/jvi.68.2.1040-1051.1994","article-title":"Human cytomegalovirus DNA replicates after early circularization by concatemer formation, and inversion occurs within the concatemer","volume":"68","author":"McVoy","year":"1994","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib89","doi-asserted-by":"crossref","first-page":"766","DOI":"10.3390\/v15030766","article-title":"Membraneless compartmentalization of nuclear assembly sites during murine cytomegalovirus infection","volume":"15","author":"Mahmutefendi\u0107 Lu\u010din","year":"2023","journal-title":"Viruses"},{"key":"10.1016\/j.colsurfb.2024.114385_bib90","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01771-19","article-title":"Phase separation of Epstein-Barr virus EBNA2 and its coactivator EBNALP controls gene expression","volume":"94","author":"Peng","year":"2020","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib91","doi-asserted-by":"crossref","first-page":"896","DOI":"10.3390\/microorganisms10050896","article-title":"Replication compartments-the great survival strategy for Epstein-Barr virus lytic replication","volume":"10","author":"Sugimoto","year":"2022","journal-title":"Microorganisms"},{"key":"10.1016\/j.colsurfb.2024.114385_bib92","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1038\/s42003-021-02501-7","article-title":"Phase separation of Epstein-Barr virus EBNA2 protein reorganizes chromatin topology for epigenetic regulation","volume":"4","author":"Yang","year":"2021","journal-title":"Commun. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib93","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1007489","article-title":"LANA oligomeric architecture is essential for KSHV nuclear body formation and viral genome maintenance during latency","volume":"15","author":"De Leo","year":"2019","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.colsurfb.2024.114385_bib94","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1009231","article-title":"Phase separation and DAXX redistribution contribute to LANA nuclear body and KSHV genome dynamics during latency and reactivation","volume":"17","author":"Vladimirova","year":"2021","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.colsurfb.2024.114385_bib95","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1007\/978-981-10-7230-7_14","article-title":"KSHV genome replication and maintenance in latency","volume":"1045","author":"Ueda","year":"2018","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib96","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202201088","article-title":"Liquid-liquid phase separation mediates the formation of herpesvirus assembly compartments","volume":"222","author":"Zhou","year":"2023","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib97","doi-asserted-by":"crossref","first-page":"31534","DOI":"10.1074\/jbc.M705637200","article-title":"Structural and functional studies of the abundant tegument protein ORF52 from murine gammaherpesvirus 68","volume":"282","author":"Benach","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.colsurfb.2024.114385_bib98","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202211015","article-title":"Liquid-liquid phase separation drives herpesvirus assembly in the cytoplasm","volume":"222","author":"Chung","year":"2023","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib99","doi-asserted-by":"crossref","DOI":"10.1111\/boc.202200059","article-title":"Ribonucleoprotein transport in negative strand RNA viruses","volume":"115","author":"Diot","year":"2023","journal-title":"Biol. Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib100","doi-asserted-by":"crossref","first-page":"497","DOI":"10.3390\/v10090497","article-title":"Zoonotic potential of influenza A viruses: a comprehensive overview","volume":"10","author":"Mostafa","year":"2018","journal-title":"Viruses"},{"key":"10.1016\/j.colsurfb.2024.114385_bib101","doi-asserted-by":"crossref","first-page":"1650","DOI":"10.3390\/ijms18081650","article-title":"Evolution of influenza A virus by mutation and re-assortment","volume":"18","author":"Shao","year":"2017","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib102","doi-asserted-by":"crossref","first-page":"1629","DOI":"10.1038\/s41467-019-09549-4","article-title":"Influenza A virus ribonucleoproteins form liquid organelles at endoplasmic reticulum exit sites","volume":"10","author":"Alenquer","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.colsurfb.2024.114385_bib103","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.3002290","article-title":"ATG9A regulates the dissociation of recycling endosomes from microtubules to form liquid influenza A virus inclusions","volume":"21","author":"Vale-Costa","year":"2023","journal-title":"PLoS Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib104","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.3390\/v14051107","article-title":"Type I and type II interferon antagonism strategies used by Paramyxoviridae: previous and new discoveries, in comparison","volume":"14","author":"Pisanelli","year":"2022","journal-title":"Viruses"},{"key":"10.1016\/j.colsurfb.2024.114385_bib105","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00948-19","article-title":"Measles virus forms inclusion bodies with properties of liquid organelles","volume":"93","author":"Zhou","year":"2019","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib106","doi-asserted-by":"crossref","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.colsurfb.2024.114385_bib107","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01726-17","article-title":"Cellular WD repeat-containing protein 5 (WDR5) localizes to cytoplasmic inclusion bodies and enhances measles virus replication","volume":"92","author":"Ma","year":"2018","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib108","doi-asserted-by":"crossref","first-page":"10537","DOI":"10.1021\/acs.jmedchem.1c00037","article-title":"Targeting WD repeat-containing protein 5 (WDR5): a medicinal chemistry perspective","volume":"64","author":"Chen","year":"2021","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.colsurfb.2024.114385_bib109","doi-asserted-by":"crossref","unstructured":"M. Galloux, J. Risso-Ballester, C.A. Richard, J. Fix, M.A. Rameix-Welti, J.F. El\u00e9ou\u00ebt, 2020. Minimal elements required for the formation of respiratory syncytial virus cytoplasmic inclusion bodies in vivo and in vitro, mBio 11, e01202-20. https:\/\/doi.org\/10.1128\/mBio01202-20.","DOI":"10.1128\/mBio.01202-20"},{"key":"10.1016\/j.colsurfb.2024.114385_bib110","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1038\/s41467-017-00655-9","article-title":"Functional organization of cytoplasmic inclusion bodies in cells infected by respiratory syncytial virus","volume":"8","author":"Rincheval","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.colsurfb.2024.114385_bib111","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.00153-24","article-title":"Viral PIC-pocketing: RSV sequestration of translational preinitiation complexes into bi-phasic biomolecular condensates","volume":"98","author":"Jobe","year":"2024","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib112","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01380-20","article-title":"Respiratory syncytial virus sequesters NF-\u03baB subunit p65 to cytoplasmic inclusion bodies to inhibit innate immune signaling","volume":"94","author":"Jobe","year":"2020","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib113","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01282-17","article-title":"Human metapneumovirus induces formation of inclusion bodies for efficient genome replication and transcription","volume":"91","author":"Cifuentes-Mu\u00f1oz","year":"2017","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib114","doi-asserted-by":"crossref","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.colsurfb.2024.114385_bib115","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.00030-23","article-title":"Specific residues in the C-terminal domain of the human metapneumovirus phosphoprotein are indispensable for formation of viral replication centers and regulation of the function of the viral polymerase complex","volume":"97","author":"Thompson","year":"2023","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib116","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00909-21","article-title":"Characterization of the interaction domains between the phosphoprotein and the nucleoprotein of human metapneumovirus","volume":"96","author":"Decool","year":"2022","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib117","doi-asserted-by":"crossref","DOI":"10.1016\/j.vetmic.2023.109800","article-title":"Newcastle disease virus forms inclusion bodies with features of liquid-liquid phase separation","volume":"284","author":"Wang","year":"2023","journal-title":"Vet. Microbiol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib118","doi-asserted-by":"crossref","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."},{"key":"10.1016\/j.colsurfb.2024.114385_bib119","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.virusres.2005.04.011","article-title":"Borna disease virus interference with neuronal plasticity","volume":"111","author":"Gonzalez-Dunia","year":"2005","journal-title":"Virus Res"},{"key":"10.1016\/j.colsurfb.2024.114385_bib120","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1002\/rmv.300","article-title":"Borna disease virus","volume":"11","author":"Jordan","year":"2001","journal-title":"Rev. Med. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib121","doi-asserted-by":"crossref","first-page":"2358","DOI":"10.3390\/v14112358","article-title":"Borna disease virus 1 phosphoprotein forms a tetramer and interacts with host factors involved in DNA double-strand break repair and mRNA processing","volume":"14","author":"Tarbouriech","year":"2022","journal-title":"Viruses"},{"key":"10.1016\/j.colsurfb.2024.114385_bib122","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.ijbiomac.2021.09.153","article-title":"Borna disease virus phosphoprotein triggers the organization of viral inclusion bodies by liquid-liquid phase separation","volume":"192","author":"Hirai","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib123","doi-asserted-by":"crossref","first-page":"2209","DOI":"10.1007\/s00705-013-1674-y","article-title":"Nyamiviridae: proposal for a new family in the order mononegavirales","volume":"158","author":"Kuhn","year":"2013","journal-title":"Arch. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib124","doi-asserted-by":"crossref","first-page":"2914","DOI":"10.1099\/jgv.0.000973","article-title":"ICTV virus taxonomy profile: Byamiviridae","volume":"98","author":"Dietzgen","year":"2017","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib125","doi-asserted-by":"crossref","first-page":"6550","DOI":"10.3390\/ijms24076550","article-title":"Nyamanini virus nucleoprotein and phosphoprotein organize viral inclusion bodies that associate with host biomolecular condensates in the nucleus","volume":"24","author":"Hirai","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib126","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.colsurfb.2024.114385_bib127","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1038\/s41467-017-00102-9","article-title":"Negri bodies are viral factories with properties of liquid organelles","volume":"8","author":"Nikolic","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.colsurfb.2024.114385_bib128","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1011022","article-title":"Properties of rabies virus phosphoprotein and nucleoprotein biocondensates formed in vitro and in cellulo","volume":"18","author":"Nevers","year":"2022","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.colsurfb.2024.114385_bib129","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1053\/tvjl.1998.0303","article-title":"Vesicular stomatitis","volume":"157","author":"Letchworth","year":"1999","journal-title":"Vet. J."},{"key":"10.1016\/j.colsurfb.2024.114385_bib130","doi-asserted-by":"crossref","unstructured":"B.S. Heinrich, Z. Maliga, D.A. Stein, A.A. Hyman, S.P.J. Whelan, 2018. Phase transitions drive the formation of vesicular stomatitis virus replication compartments. mBio 9, e02290-17. https:\/\/doi.org\/10.1128\/mBio02290-17.","DOI":"10.1128\/mBio.02290-17"},{"key":"10.1016\/j.colsurfb.2024.114385_bib131","doi-asserted-by":"crossref","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.colsurfb.2024.114385_bib132","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.74884","article-title":"Host casein kinase 1-mediated phosphorylation modulates phase separation of a rhabdovirus phosphoprotein and virus infection","volume":"11","author":"Fang","year":"2022","journal-title":"Elife"},{"key":"10.1016\/j.colsurfb.2024.114385_bib133","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1016\/j.tcb.2016.05.004","article-title":"Principles and properties of stress granules","volume":"26","author":"Protter","year":"2016","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib134","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.cell.2015.09.015","article-title":"Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization","volume":"163","author":"Molliex","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib135","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.cell.2020.03.046","article-title":"G3BP1 is a tunable switch that triggers phase separation to assemble stress granules","volume":"181","author":"Yang","year":"2020","journal-title":"Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib136","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbamcr.2020.118876","article-title":"Molecular mechanisms of stress granule assembly and disassembly","volume":"1868","author":"Hofmann","year":"2021","journal-title":"Biochim. Biophys. Acta-Mol. Cell Res."},{"key":"10.1016\/j.colsurfb.2024.114385_bib137","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.tim.2012.02.001","article-title":"Regulation of stress granules in virus systems","volume":"20","author":"White","year":"2012","journal-title":"Trends Microbiol"},{"key":"10.1016\/j.colsurfb.2024.114385_bib138","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1007\/s12250-019-00122-3","article-title":"Viral regulation of RNA granules in infected cells","volume":"34","author":"Zhang","year":"2019","journal-title":"Virol. Sin."},{"key":"10.1016\/j.colsurfb.2024.114385_bib139","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/j.virol.2012.11.017","article-title":"Diversion of stress granules and P-bodies during viral infection","volume":"436","author":"Reineke","year":"2013","journal-title":"Virology"},{"key":"10.1016\/j.colsurfb.2024.114385_bib140","doi-asserted-by":"crossref","first-page":"1166","DOI":"10.1007\/s00018-002-8495-6","article-title":"Assembling the human immunodeficiency virus type 1","volume":"59","author":"Cimarelli","year":"2002","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib141","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/S0968-4328(98)00002-X","article-title":"The life-cycle of human immunodeficiency virus type 1","volume":"29","author":"Goto","year":"1998","journal-title":"Micron"},{"key":"10.1016\/j.colsurfb.2024.114385_bib142","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/j.jmb.2011.03.052","article-title":"Jr., A retroviral chimeric capsid protein reveals the role of the N-terminal \u03b2-hairpin in mature core assembly","volume":"410","author":"Cortines","year":"2011","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib143","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1146\/annurev.biochem.67.1.1","article-title":"HIV-1: fifteen proteins and an RNA","volume":"67","author":"Frankel","year":"1998","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.colsurfb.2024.114385_bib144","doi-asserted-by":"crossref","first-page":"14498","DOI":"10.1128\/JVI.79.23.14498-14506.2005","article-title":"Analysis of human immunodeficiency virus type 1 Gag dimerization-induced assembly","volume":"79","author":"Alfadhli","year":"2005","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib145","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1016\/j.colsurfb.2015.10.010","article-title":"Hierarchical multi-step organization during viral capsid assembly","volume":"136","author":"Lampel","year":"2015","journal-title":"Colloids Surf. B"},{"key":"10.1016\/j.colsurfb.2024.114385_bib146","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1261\/rna.064618.117","article-title":"HIV-1 NC-induced stress granule assembly and translation arrest are inhibited by the dsRNA binding protein Staufen1","volume":"24","author":"Rao","year":"2018","journal-title":"RNA"},{"key":"10.1016\/j.colsurfb.2024.114385_bib147","doi-asserted-by":"crossref","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.colsurfb.2024.114385_bib148","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1038\/s41392-023-01623-0","article-title":"CBX4 deletion promotes tumorigenesis under Kras(G12D) background by inducing genomic instability.","volume":"8","author":"Chen","year":"2023","journal-title":"Signal Transduct. Tar."},{"key":"10.1016\/j.colsurfb.2024.114385_bib149","doi-asserted-by":"crossref","DOI":"10.15252\/embr.202153855","article-title":"CBX4 contributes to HIV-1 latency by forming phase-separated nuclear bodies and SUMOylating EZH2","volume":"23","author":"Wu","year":"2022","journal-title":"EMBO Rep."},{"key":"10.1016\/j.colsurfb.2024.114385_bib150","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1159\/000149390","article-title":"Coronaviridae","volume":"20","author":"Siddell","year":"1983","journal-title":"Intervirology"},{"key":"10.1016\/j.colsurfb.2024.114385_bib151","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbadis.2020.165878","article-title":"Insights into SARS-CoV-2 genome, structure, evolution, pathogenesis and therapies: structural genomics approach","volume":"1866","author":"Naqvi","year":"2020","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"issue":"1","key":"10.1016\/j.colsurfb.2024.114385_bib152","doi-asserted-by":"crossref","first-page":"858","DOI":"10.1111\/odi.13447","article-title":"Coronaviridae-old friends, new enemy!","volume":"28","author":"Leao","year":"2022","journal-title":"Oral. Dis."},{"key":"10.1016\/j.colsurfb.2024.114385_bib153","doi-asserted-by":"crossref","first-page":"454","DOI":"10.3390\/biology10060454","article-title":"Viewing SARS-CoV-2 nucleocapsid protein in terms of molecular flexibility","volume":"10","author":"Matsuo","year":"2021","journal-title":"Biology"},{"key":"10.1016\/j.colsurfb.2024.114385_bib154","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.3390\/v13061115","article-title":"The SARS-CoV-2 nucleocapsid protein and its role in viral structure, biological functions, and a potential target for drug or vaccine mitigation","volume":"13","author":"Bai","year":"2021","journal-title":"Viruses"},{"key":"10.1016\/j.colsurfb.2024.114385_bib155","doi-asserted-by":"crossref","first-page":"11273","DOI":"10.1093\/nar\/gkac904","article-title":"Role of NS2 specific RNA binding and phosphorylation in liquid-liquid phase separation and virus assembly","volume":"50","author":"Rahman","year":"2022","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.colsurfb.2024.114385_bib156","doi-asserted-by":"crossref","first-page":"11476","DOI":"10.1128\/JVI.79.17.11476-11486.2005","article-title":"The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation","volume":"79","author":"Surjit","year":"2005","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib157","doi-asserted-by":"crossref","first-page":"1092","DOI":"10.1016\/j.molcel.2020.11.025","article-title":"Phosphoregulation of phase separation by the SARS-CoV-2 N protein suggests a biophysical basis for its dual functions","volume":"80","author":"Carlson","year":"2020","journal-title":"Mol. Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib158","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.colsurfb.2024.114385_bib159","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1016\/j.scib.2021.01.013","article-title":"SARS-CoV-2 nucleocapsid protein phase separates with G3BPs to disassemble stress granules and facilitate viral production","volume":"66","author":"Luo","year":"2021","journal-title":"Sci. Bull."},{"key":"10.1016\/j.colsurfb.2024.114385_bib160","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1016\/j.ijbiomac.2021.09.018","article-title":"Genomics-guided targeting of stress granule proteins G3BP1\/2 to inhibit SARS-CoV-2 propagation","volume":"190","author":"Ali","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib161","doi-asserted-by":"crossref","DOI":"10.1172\/JCI165307","article-title":"Entry receptors - the gateway to alphavirus infection","volume":"133","author":"Zimmerman","year":"2023","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.colsurfb.2024.114385_bib162","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2021719118","article-title":"Stress granule formation, disassembly, and composition are regulated by alphavirus ADP-ribosyl hydrolase activity","volume":"118","author":"Jayabalan","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.colsurfb.2024.114385_bib163","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1042\/BC20040058","article-title":"Virus factories: associations of cell organelles for viral replication and morphogenesis","volume":"97","author":"Novoa","year":"2005","journal-title":"Biol. Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib164","article-title":"Biomolecular condensates with liquid properties formed during viral infections","volume":"8","author":"Glon","year":"2024","journal-title":"Microbes Infect."},{"key":"10.1016\/j.colsurfb.2024.114385_bib165","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/j.vetmic.2009.08.028","article-title":"Zoonotic aspects of rotaviruses","volume":"140","author":"Martella","year":"2010","journal-title":"Vet. Microbiol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib166","doi-asserted-by":"crossref","DOI":"10.1016\/j.virusres.2021.198499","article-title":"Rotavirus research: 2014-2020","volume":"304","author":"Caddy","year":"2021","journal-title":"Virus Res"},{"key":"10.1016\/j.colsurfb.2024.114385_bib167","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2021107711","article-title":"Liquid-liquid phase separation underpins the formation of replication factories in rotaviruses","volume":"40","author":"Geiger","year":"2021","journal-title":"Embo J."},{"key":"10.1016\/j.colsurfb.2024.114385_bib168","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.3390\/v13071349","article-title":"Viroplasms: assembly and functions of rotavirus replication factories","volume":"13","author":"Papa","year":"2021","journal-title":"Viruses"},{"key":"10.1016\/j.colsurfb.2024.114385_bib169","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.00039-23","article-title":"Flexibility of the rotavirus NSP2C-terminal region supports factory formation via liquid-liquid phase separation","volume":"97","author":"Nichols","year":"2023","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib170","doi-asserted-by":"crossref","first-page":"2047","DOI":"10.1007\/s00705-012-1377-9","article-title":"P. Kaiser, An overview of infectious bursal disease","volume":"157","author":"Mahgoub","year":"2012","journal-title":"Arch. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib171","doi-asserted-by":"crossref","first-page":"6973","DOI":"10.1128\/JVI.73.8.6973-6983.1999","article-title":"VP1, the putative RNA-dependent RNA polymerase of infectious bursal disease virus, forms complexes with the capsid protein VP3, leading to efficient encapsidation into virus-like particles","volume":"73","author":"Lombardo","year":"1999","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib172","doi-asserted-by":"crossref","first-page":"5647","DOI":"10.1128\/jvi.71.7.5647-5651.1997","article-title":"VP5 of infectious bursal disease virus is not essential for viral replication in cell culture","volume":"71","author":"Mundt","year":"1997","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib173","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00584-17","article-title":"Voltage-dependent anion channel 1 interacts with ribonucleoprotein complexes to enhance infectious bursal disease virus polymerase activity","volume":"91","author":"Han","year":"2017","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib174","doi-asserted-by":"crossref","DOI":"10.1128\/jvi.02024-21","article-title":"Birnaviridae virus factories show features of liquid-liquid phase separation and are distinct from paracrystalline arrays of virions observed by electron microscopy","volume":"96","author":"Reddy","year":"2022","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib175","doi-asserted-by":"crossref","first-page":"8471","DOI":"10.3390\/ijms24108471","article-title":"The formation and function of Birnaviridae virus factories","volume":"24","author":"Brodrick","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib176","doi-asserted-by":"crossref","first-page":"15208","DOI":"10.1073\/pnas.1413268111","article-title":"Structural studies on the authentic mumps virus nucleocapsid showing uncoiling by the phosphoprotein","volume":"111","author":"Cox","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.colsurfb.2024.114385_bib177","doi-asserted-by":"crossref","first-page":"1877","DOI":"10.1016\/j.cell.2023.03.015","article-title":"Molecular mechanisms of stress-induced reactivation in mumps virus condensates","volume":"186","author":"Zhang","year":"2023","journal-title":"Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib178","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1038\/s41579-018-0003-6","article-title":"Autophagy during viral infection - a double-edged sword","volume":"16","author":"Choi","year":"2018","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib179","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/S0076-6879(08)03612-4","article-title":"Monitoring autophagic degradation of p62\/SQSTM1","volume":"452","author":"Bj\u00f8rk\u00f8y","year":"2009","journal-title":"Methods Enzym."},{"key":"10.1016\/j.colsurfb.2024.114385_bib180","doi-asserted-by":"crossref","first-page":"1200","DOI":"10.1002\/iub.2689","article-title":"p62 bodies: phase separation, NRF2 activation, and selective autophagic degradation","volume":"74","author":"Komatsu","year":"2022","journal-title":"IUBMB Life"},{"key":"10.1016\/j.colsurfb.2024.114385_bib181","doi-asserted-by":"crossref","first-page":"31864","DOI":"10.1074\/jbc.M111.259630","article-title":"Crystal structure of the ubiquitin-associated (UBA) domain of p62 and its interaction with ubiquitin","volume":"286","author":"Isogai","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.colsurfb.2024.114385_bib182","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1038\/s41422-018-0017-7","article-title":"Polyubiquitin chain-induced p62 phase separation drives autophagic cargo segregation","volume":"28","author":"Sun","year":"2018","journal-title":"Cell Res"},{"key":"10.1016\/j.colsurfb.2024.114385_bib183","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1004987","article-title":"Proteotoxic stress induces phosphorylation of p62\/SQSTM1 by ULK1 to regulate selective autophagic clearance of protein aggregates","volume":"11","author":"Lim","year":"2015","journal-title":"PLoS Genet"},{"key":"10.1016\/j.colsurfb.2024.114385_bib184","doi-asserted-by":"crossref","first-page":"7338","DOI":"10.1038\/s41467-023-42829-8","article-title":"Local membrane source gathering by p62 body drives autophagosome formation","volume":"14","author":"Feng","year":"2023","journal-title":"Nat. Commun."},{"key":"10.1016\/j.colsurfb.2024.114385_bib185","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1038\/s41422-022-00662-6","article-title":"Myosin 1D and the branched actin network control the condensation of p62 bodies","volume":"32","author":"Feng","year":"2022","journal-title":"Cell Res"},{"key":"10.1016\/j.colsurfb.2024.114385_bib186","doi-asserted-by":"crossref","first-page":"3029","DOI":"10.1080\/15548627.2023.2210943","article-title":"SQSTM1\/P62 promotes lysophagy via formation of liquid-like condensates maintained by HSP27","volume":"19","author":"Gallagher","year":"2023","journal-title":"Autophagy"},{"key":"10.1016\/j.colsurfb.2024.114385_bib187","doi-asserted-by":"crossref","first-page":"2702","DOI":"10.1080\/15548627.2023.2223468","article-title":"HSPA8 regulates anti-bacterial autophagy through liquid-liquid phase separation","volume":"19","author":"Miao","year":"2023","journal-title":"Autophagy"},{"key":"10.1016\/j.colsurfb.2024.114385_bib188","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1080\/15548627.2015.1009776","article-title":"Heat shock response and autophagy-cooperation and control","volume":"11","author":"Dokladny","year":"2015","journal-title":"Autophagy"},{"key":"10.1016\/j.colsurfb.2024.114385_bib189","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1038\/cr.2017.40","article-title":"Ubiquitylation of p62\/sequestosome1 activates its autophagy receptor function and controls selective autophagy upon ubiquitin stress","volume":"27","author":"Peng","year":"2017","journal-title":"Cell Res"},{"key":"10.1016\/j.colsurfb.2024.114385_bib190","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1038\/s41594-020-0399-3","article-title":"Hsp27 chaperones FUS phase separation under the modulation of stress-induced phosphorylation","volume":"27","author":"Liu","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib191","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.3002529","article-title":"Viral regulation of organelle membrane contact sites","volume":"22","author":"Hofstadter","year":"2024","journal-title":"PLoS Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib192","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1016\/j.tim.2021.12.011","article-title":"Mitochondria-mediated oxidative stress during viral infection","volume":"30","author":"Foo","year":"2022","journal-title":"Trends Microbiol"},{"key":"10.1016\/j.colsurfb.2024.114385_bib193","doi-asserted-by":"crossref","first-page":"2822","DOI":"10.1016\/j.bbamcr.2014.12.040","article-title":"Mitochondrial dynamics and viral infections: a close nexus","volume":"1853","author":"Khan","year":"2015","journal-title":"Biochim Biophys. Acta"},{"key":"10.1016\/j.colsurfb.2024.114385_bib194","doi-asserted-by":"crossref","DOI":"10.1128\/mbio.02096-21","article-title":"Mitochondria and viral infection: advances and emerging battlefronts","volume":"13","author":"Sorouri","year":"2022","journal-title":"mBio"},{"key":"10.1016\/j.colsurfb.2024.114385_bib195","doi-asserted-by":"crossref","first-page":"95","DOI":"10.3389\/fcimb.2019.00095","article-title":"Virus control of cell metabolism for replication and evasion of host immune responses","volume":"9","author":"Moreno-Altamirano","year":"2019","journal-title":"Front. Cell Infect. Microbiol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib196","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.mito.2017.11.007","article-title":"The essential role of mitochondrial dynamics in antiviral immunity","volume":"41","author":"Kim","year":"2018","journal-title":"Mitochondrion"},{"key":"10.1016\/j.colsurfb.2024.114385_bib197","doi-asserted-by":"crossref","first-page":"2359","DOI":"10.3390\/v15122359","article-title":"Regulation of mitochondrial metabolism by hepatitis B virus","volume":"15","author":"Li","year":"2023","journal-title":"Viruses"},{"key":"10.1016\/j.colsurfb.2024.114385_bib198","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2023.167988","article-title":"Condensation goes viral: a polymer physics perspective","volume":"435","author":"Alston","year":"2023","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib199","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.tibs.2022.09.008","article-title":"Let\u2019s phase it: viruses are master architects of biomolecular condensates","volume":"48","author":"Sagan","year":"2023","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib200","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2023.168380","article-title":"Biomolecular condensates as novel antiviral targets","volume":"436","author":"Martin","year":"2024","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib201","doi-asserted-by":"crossref","DOI":"10.1016\/j.colsurfb.2023.113310","article-title":"Construction of nano-drug delivery and antitumor system of stimuli-responsive polypeptides","volume":"226","author":"Hu","year":"2023","journal-title":"Colloids Surf. B"},{"key":"10.1016\/j.colsurfb.2024.114385_bib202","doi-asserted-by":"crossref","DOI":"10.1016\/j.colsurfb.2023.113123","article-title":"Investigation of macromolecular transport through tunable collagen hyaluronic acid matrices","volume":"222","author":"Hakim","year":"2023","journal-title":"Colloids Surf. B"},{"key":"10.1016\/j.colsurfb.2024.114385_bib203","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2022.1007744","article-title":"Principles and functions of condensate modifying drugs","volume":"9","author":"Patel","year":"2022","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib204","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.colsurfb.2024.114385_bib205","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1038\/nbt.1638","article-title":"Identification of influenza A nucleoprotein as an antiviral target","volume":"28","author":"Kao","year":"2010","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib206","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0277073","article-title":"Modifications in the piperazine ring of nucleozin affect anti-influenza activity","volume":"18","author":"Correa-Padilla","year":"2023","journal-title":"PLoS One"},{"key":"10.1016\/j.colsurfb.2024.114385_bib207","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.85182","article-title":"Defining basic rules for hardening influenza A virus liquid condensates","volume":"12","author":"Etibor","year":"2023","journal-title":"Elife"},{"key":"10.1016\/j.colsurfb.2024.114385_bib208","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1128\/JVI.01406-10","article-title":"Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization","volume":"85","author":"Shi","year":"2011","journal-title":"J. Virol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib209","doi-asserted-by":"crossref","first-page":"88","DOI":"10.3390\/biom13010088","article-title":"Efavirenz: history, development and future","volume":"13","author":"Costa","year":"2022","journal-title":"Biomolecules"},{"key":"10.1016\/j.colsurfb.2024.114385_bib210","doi-asserted-by":"crossref","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.colsurfb.2024.114385_bib211","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1186\/s13059-021-02455-3","article-title":"Time-dependent effect of 1,6-hexanediol on biomolecular condensates and 3D chromatin organization","volume":"22","author":"Liu","year":"2021","journal-title":"Genome Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib212","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.100260","article-title":"1,6-hexanediol, commonly used to dissolve liquid-liquid phase separated condensates, directly impairs kinase and phosphatase activities","volume":"296","author":"D\u00fcster","year":"2021","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.colsurfb.2024.114385_bib213","doi-asserted-by":"crossref","DOI":"10.26508\/lsa.202001005","article-title":"1,6-hexanediol rapidly immobilizes and condenses chromatin in living human cells","volume":"4","author":"Itoh","year":"2021","journal-title":"Life Sci. Alliance"},{"key":"10.1016\/j.colsurfb.2024.114385_bib214","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1016\/j.neuron.2019.05.048","article-title":"Small-molecule modulation of TDP-43 recruitment to stress granules prevents persistent TDP-43 accumulation in ALS\/FTD","volume":"103","author":"Fang","year":"2019","journal-title":"Neuron"},{"key":"10.1016\/j.colsurfb.2024.114385_bib215","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1038\/nrm.2017.53","article-title":"The multifaceted roles of PARP1 in DNA repair and chromatin remodelling","volume":"18","author":"Ray Chaudhuri","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib216","doi-asserted-by":"crossref","DOI":"10.1016\/j.dnarep.2019.102651","article-title":"PARP-1 and its associated nucleases in DNA damage response","volume":"81","author":"Wang","year":"2019","journal-title":"DNA Repair"},{"key":"10.1016\/j.colsurfb.2024.114385_bib217","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1038\/s41392-021-00568-6","article-title":"An integrative drug repositioning framework discovered a potential therapeutic agent targeting COVID-19","volume":"6","author":"Ge","year":"2021","journal-title":"Signal Transduct. Tar."},{"key":"10.1016\/j.colsurfb.2024.114385_bib218","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1007\/s13238-021-00832-z","article-title":"Understanding the phase separation characteristics of nucleocapsid protein provides a new therapeutic opportunity against SARS-CoV-2","volume":"12","author":"Zhao","year":"2021","journal-title":"Protein Cell"},{"key":"10.1016\/j.colsurfb.2024.114385_bib219","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.colsurfb.2024.114385_bib220","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1007\/978-3-319-91442-8_15","article-title":"Olaparib","volume":"211","author":"Bochum","year":"2018","journal-title":"Recent Results Cancer Res"},{"key":"10.1016\/j.colsurfb.2024.114385_bib221","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1016\/j.tcb.2020.02.002","article-title":"Poly(ADP-ribose): a dynamic trigger for biomolecular condensate formation","volume":"30","author":"Leung","year":"2020","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib222","doi-asserted-by":"crossref","first-page":"4139","DOI":"10.7150\/ijbs.81521","article-title":"Liquid-liquid phase separation: roles and implications in future cancer treatment","volume":"19","author":"Liu","year":"2023","journal-title":"Int. J. Biol. Sci."},{"key":"10.1016\/j.colsurfb.2024.114385_bib223","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1038\/nm0397-341","article-title":"Azodicarbonamide inhibits HIV-1 replication by targeting the nucleocapsid protein","volume":"3","author":"Rice","year":"1997","journal-title":"Nat. Med."},{"key":"10.1016\/j.colsurfb.2024.114385_bib224","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1039\/C5MB00582E","article-title":"Structure-based virtual screening and experimental validation of the discovery of inhibitors targeted towards the human coronavirus nucleocapsid protein","volume":"12","author":"Chang","year":"2016","journal-title":"Mol. Biosyst."},{"key":"10.1016\/j.colsurfb.2024.114385_bib225","doi-asserted-by":"crossref","first-page":"2114","DOI":"10.1038\/s41467-021-22297-8","article-title":"GCG inhibits SARS-CoV-2 replication by disrupting the liquid phase condensation of its nucleocapsid protein","volume":"12","author":"Zhao","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.colsurfb.2024.114385_bib226","doi-asserted-by":"crossref","DOI":"10.1002\/mef2.29","article-title":"SARS-CoV-2 modulation of RIG-I-MAVS signaling: potential mechanisms of impairment on host antiviral immunity and therapeutic approaches","volume":"1","author":"Wang","year":"2022","journal-title":"MedComm Futur. Med."},{"key":"10.1016\/j.colsurfb.2024.114385_bib227","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1038\/s41556-021-00710-0","article-title":"Targeting liquid-liquid phase separation of SARS-CoV-2 nucleocapsid protein promotes innate antiviral immunity by elevating MAVS activity","volume":"23","author":"Wang","year":"2021","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.colsurfb.2024.114385_bib228","doi-asserted-by":"crossref","first-page":"2327","DOI":"10.1016\/j.scib.2022.10.021","article-title":"Antiviral drug design based on structural insights into the N-terminal domain and C-terminal domain of the SARS-CoV-2 nucleocapsid protein","volume":"67","author":"Luan","year":"2022","journal-title":"Sci. Bull."},{"key":"10.1016\/j.colsurfb.2024.114385_bib229","doi-asserted-by":"crossref","unstructured":"D. Sun, Z. Sang, Y.J. Kim, Y. Xiang, T. Cohen, A.K. Belford, A. Huet, J.F. Conway, J. Sun, D.J. Taylor, D. Schneidman-Duhovny, C. Zhang, W. Huang, Y. Shi, 2021. Potent neutralizing nanobodies resist convergent circulating variants of SARS-CoV-2 by targeting novel and conserved epitopes. bioRxiv. 2021.03.09.434592. https:\/\/doi.org\/10.1101\/2021.03.09.434592.","DOI":"10.1101\/2021.03.09.434592"},{"key":"10.1016\/j.colsurfb.2024.114385_bib230","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2101918118","article-title":"Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice","volume":"118","author":"Pymm","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"}],"container-title":["Colloids and Surfaces B: Biointerfaces"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0927776524006441?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0927776524006441?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,12,13]],"date-time":"2024-12-13T01:14:59Z","timestamp":1734052499000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0927776524006441"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,2]]},"references-count":230,"alternative-id":["S0927776524006441"],"URL":"https:\/\/doi.org\/10.1016\/j.colsurfb.2024.114385","relation":{},"ISSN":["0927-7765"],"issn-type":[{"value":"0927-7765","type":"print"}],"subject":[],"published":{"date-parts":[[2025,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Liquid-liquid phase separation in viral infection: From the occurrence and function to treatment potentials","name":"articletitle","label":"Article Title"},{"value":"Colloids and Surfaces B: Biointerfaces","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.colsurfb.2024.114385","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Elsevier B.V. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"114385"}}