{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T02:41:51Z","timestamp":1792636911626,"version":"4.5.0"},"reference-count":57,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,2,28]],"date-time":"2025-02-28T00:00:00Z","timestamp":1740700800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/100015691","name":"National Institute of Allergy and Infectious Diseases Division of Microbiology and Infectious Diseases","doi-asserted-by":"publisher","award":["75N93022C00035"],"award-info":[{"award-number":["75N93022C00035"]}],"id":[{"id":"10.13039\/100015691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100015691","name":"National Institute of Allergy and Infectious Diseases Division of Microbiology and Infectious Diseases","doi-asserted-by":"publisher","award":["R01-AI141436"],"award-info":[{"award-number":["R01-AI141436"]}],"id":[{"id":"10.13039\/100015691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100015691","name":"National Institute of Allergy and Infectious Diseases Division of Microbiology and Infectious Diseases","doi-asserted-by":"publisher","award":["R01-AI153209"],"award-info":[{"award-number":["R01-AI153209"]}],"id":[{"id":"10.13039\/100015691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100015691","name":"National Institute of Allergy and Infectious Diseases Division of Microbiology and Infectious Diseases","doi-asserted-by":"publisher","award":["U19-AI142790"],"award-info":[{"award-number":["U19-AI142790"]}],"id":[{"id":"10.13039\/100015691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100015691","name":"National Institute of Allergy and Infectious Diseases Division of Microbiology and Infectious Diseases","doi-asserted-by":"publisher","award":["T32-AI007172"],"award-info":[{"award-number":["T32-AI007172"]}],"id":[{"id":"10.13039\/100015691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014451","name":"Center for Cellular Imaging, Washington University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100014451","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000774","name":"Defense Threat Reduction Agency","doi-asserted-by":"publisher","award":["MCDC2103-01"],"award-info":[{"award-number":["MCDC2103-01"]}],"id":[{"id":"10.13039\/100000774","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["T32-CA009547"],"award-info":[{"award-number":["T32-CA009547"]}],"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":["AI201800001"],"award-info":[{"award-number":["AI201800001"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell"],"published-print":{"date-parts":[[2025,5]]},"DOI":"10.1016\/j.cell.2025.02.036","type":"journal-article","created":{"date-parts":[[2025,4,6]],"date-time":"2025-04-06T16:13:38Z","timestamp":1743956018000},"page":"2943-2956.e24","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":10,"title":["Structural basis for plasticity in receptor engagement by an encephalitic alphavirus"],"prefix":"10.1016","volume":"188","author":[{"given":"Saravanan","family":"Raju","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sathvik","family":"Palakurty","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alan","family":"Sariol","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ngan","family":"Wagoner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lucas J.","family":"Adams","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sean","family":"Hui","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William B.","family":"Klimstra","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daved H.","family":"Fremont","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael S.","family":"Diamond","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.cell.2025.02.036_bib1","series-title":"Fields Virology: Emerging Viruses","author":"Howley","year":"2020"},{"key":"10.1016\/j.cell.2025.02.036_bib2","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/j.vetmic.2009.08.023","article-title":"Encephalitic alphaviruses","volume":"140","author":"Zacks","year":"2010","journal-title":"Vet. Microbiol."},{"key":"10.1016\/j.cell.2025.02.036_bib3","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1038\/nrmicro1006","article-title":"Transmission cycles, host range, evolution and emergence of arboviral disease","volume":"2","author":"Weaver","year":"2004","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.cell.2025.02.036_bib4","doi-asserted-by":"crossref","first-page":"9095","DOI":"10.1073\/pnas.90.19.9095","article-title":"Three-dimensional structure of a membrane-containing virus","volume":"90","author":"Paredes","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cell.2025.02.036_bib5","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1016\/0092-8674(95)90516-2","article-title":"Nucleocapsid and glycoprotein organization in an enveloped virus","volume":"80","author":"Cheng","year":"1995","journal-title":"Cell"},{"key":"10.1016\/j.cell.2025.02.036_bib6","doi-asserted-by":"crossref","first-page":"4818","DOI":"10.1016\/j.cell.2023.09.007","article-title":"Vertebrate-class-specific binding modes of the alphavirus receptor MXRA8","volume":"186","author":"Zimmerman","year":"2023","journal-title":"Cell"},{"key":"10.1016\/j.cell.2025.02.036_bib7","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1038\/s41586-024-07740-2","article-title":"Shifts in receptors during submergence of an encephalitic arbovirus","volume":"632","author":"Li","year":"2024","journal-title":"Nature"},{"key":"10.1016\/j.cell.2025.02.036_bib8","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2024.114809","article-title":"The VLDLR entry receptor is required for the pathogenesis of multiple encephalitic alphaviruses","volume":"43","author":"Palakurty","year":"2024","journal-title":"Cell Rep."},{"key":"10.1016\/j.cell.2025.02.036_bib9","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1038\/s41422-024-01031-1","article-title":"PCDH10 is a neuronal receptor for western equine encephalitis virus","volume":"34","author":"Yang","year":"2024","journal-title":"Cell Res."},{"key":"10.1016\/j.cell.2025.02.036_bib10","article-title":"The low-density lipoprotein receptor promotes infection of multiple encephalitic alphaviruses","volume":"15","author":"Ma","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.cell.2025.02.036_bib11","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1008102","article-title":"\u201cSubmergence\u201d of Western equine encephalitis virus: Evidence of positive selection argues against genetic drift and fitness reductions","volume":"16","author":"Bergren","year":"2020","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.cell.2025.02.036_bib12","doi-asserted-by":"crossref","first-page":"1725","DOI":"10.1016\/j.cell.2019.04.006","article-title":"Cryo-EM Structure of Chikungunya Virus in Complex with the Mxra8 Receptor","volume":"177","author":"Basore","year":"2019","journal-title":"Cell"},{"key":"10.1016\/j.cell.2025.02.036_bib13","first-page":"1714","article-title":"Molecular Basis of Arthritogenic Alphavirus Receptor MXRA8 Binding to Chikungunya Virus Envelope","volume":"177","author":"Song","year":"2019","journal-title":"Protein Cell"},{"key":"10.1016\/j.cell.2025.02.036_bib14","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1038\/s41586-021-03909-1","article-title":"Structure of Venezuelan equine encephalitis virus with its receptor LDLRAD3","volume":"598","author":"Ma","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.cell.2025.02.036_bib15","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1038\/s41586-021-03963-9","article-title":"Structure of Venezuelan equine encephalitis virus in complex with the LDLRAD3 receptor","volume":"598","author":"Basore","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.cell.2025.02.036_bib16","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.cell.2023.11.031","article-title":"Structural and functional basis of VLDLR usage by Eastern equine encephalitis virus","volume":"187","author":"Adams","year":"2024","journal-title":"Cell"},{"key":"10.1016\/j.cell.2025.02.036_bib17","article-title":"Structural basis for VLDLR recognition by eastern equine encephalitis virus","volume":"15","author":"Yang","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.cell.2025.02.036_bib18","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-024-51293-x","article-title":"The receptor VLDLR binds Eastern Equine Encephalitis virus through multiple distinct modes","volume":"15","author":"Cao","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.cell.2025.02.036_bib19","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.it.2023.11.006","article-title":"The many ways in which alphaviruses bind to cells","volume":"45","author":"Raju","year":"2023","journal-title":"Trends Immunol."},{"key":"10.1016\/j.cell.2025.02.036_bib20","doi-asserted-by":"crossref","first-page":"2208","DOI":"10.1016\/j.cell.2023.03.032","article-title":"Structure of Semliki Forest virus in complex with its receptor VLDLR","volume":"186","author":"Cao","year":"2023","journal-title":"Cell"},{"key":"10.1016\/j.cell.2025.02.036_bib21","article-title":"Structural basis for VLDLR recognition by eastern equine encephalitis virus","author":"Yang","year":"2023","journal-title":"bioRxiv"},{"key":"10.1016\/j.cell.2025.02.036_bib22","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.hlife.2023.11.001","article-title":"Structural basis of Semliki Forest virus entry using the very-low-density lipoprotein receptor","volume":"1","author":"Li","year":"2023","journal-title":"hLife"},{"key":"10.1016\/j.cell.2025.02.036_bib23","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1012770","article-title":"Structural insights into Semiliki forest virus receptor binding modes indicate novel mechanism of virus endocytosis","volume":"20","author":"Yang","year":"2024","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.cell.2025.02.036_bib24","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1038\/s41586-021-04326-0","article-title":"VLDLR and ApoER2 are receptors for multiple alphaviruses","volume":"602","author":"Clark","year":"2022","journal-title":"Nature"},{"key":"10.1016\/j.cell.2025.02.036_bib25","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1038\/s41586-018-0121-3","article-title":"Mxra8 is a receptor for multiple arthritogenic alphaviruses","volume":"557","author":"Zhang","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.cell.2025.02.036_bib26","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1128\/JVI.80.2.737-749.2006","article-title":"Characterization of Ross River virus tropism and virus-induced inflammation in a mouse model of viral arthritis and myositis","volume":"80","author":"Morrison","year":"2006","journal-title":"J. Virol."},{"key":"10.1016\/j.cell.2025.02.036_bib27","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","article-title":"Accurate structure prediction of biomolecular interactions with AlphaFold 3","volume":"630","author":"Abramson","year":"2024","journal-title":"Nature"},{"key":"10.1016\/j.cell.2025.02.036_bib28","doi-asserted-by":"crossref","first-page":"2655","DOI":"10.1016\/j.celrep.2020.02.003","article-title":"Family-wide structural and biophysical analysis of binding interactions among non-clustered \u03b4-protocadherins","volume":"30","author":"Harrison","year":"2020","journal-title":"Cell Rep."},{"key":"10.1016\/j.cell.2025.02.036_bib29","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-024-55493-3","article-title":"VLDLR mediates Semliki Forest virus neuroinvasion through the blood-cerebrospinal fluid barrier","volume":"15","author":"Martikainen","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.cell.2025.02.036_bib30","doi-asserted-by":"crossref","first-page":"1151","DOI":"10.1038\/nn1960","article-title":"OL-Protocadherin is essential for growth of striatal axons and thalamocortical projections","volume":"10","author":"Uemura","year":"2007","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.cell.2025.02.036_bib31","doi-asserted-by":"crossref","first-page":"4250","DOI":"10.1523\/JNEUROSCI.1843-21.2022","article-title":"ASD\/OCD-linked protocadherin-10 regulates synapse, but not axon, development in the amygdala and contributes to fear- and anxiety-related behaviors","volume":"42","author":"Hoshina","year":"2022","journal-title":"J. Neurosci."},{"key":"10.1016\/j.cell.2025.02.036_bib32","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1016\/S0092-8674(00)80782-5","article-title":"Reeler\/Disabled-like disruption of neuronal migration in knockout mice lacking the VLDL receptor and ApoE receptor 2","volume":"97","author":"Trommsdorff","year":"1999","journal-title":"Cell"},{"key":"10.1016\/j.cell.2025.02.036_bib33","doi-asserted-by":"crossref","DOI":"10.3390\/v8090250","article-title":"The Host Cell Receptors for Measles Virus and Their Interaction with the Viral Hemagglutinin (H) Protein","volume":"8","author":"Lin","year":"2016","journal-title":"Viruses"},{"key":"10.1016\/j.cell.2025.02.036_bib34","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1038\/nsmb.1726","article-title":"Structure of the measles virus hemagglutinin bound to the CD46 receptor","volume":"17","author":"Santiago","year":"2010","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.cell.2025.02.036_bib35","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1038\/nsmb.2432","article-title":"Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4","volume":"20","author":"Zhang","year":"2013","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.cell.2025.02.036_bib36","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1038\/nsmb.1969","article-title":"Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM","volume":"18","author":"Hashiguchi","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.cell.2025.02.036_bib37","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1038\/s41564-024-01672-3","article-title":"Crimean-Congo haemorrhagic fever virus uses LDLR to bind and enter host cells","volume":"9","author":"Monteil","year":"2024","journal-title":"Nat. Microbiol."},{"key":"10.1016\/j.cell.2025.02.036_bib38","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1038\/s41422-023-00917-w","article-title":"LDLR is an entry receptor for Crimean-Congo hemorrhagic fever virus","volume":"34","author":"Xu","year":"2024","journal-title":"Cell Res."},{"key":"10.1016\/j.cell.2025.02.036_bib39","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2204706119","article-title":"Oropouche orthobunyavirus infection is mediated by the cellular host factor Lrp1","volume":"119","author":"Schwarz","year":"2022","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cell.2025.02.036_bib40","doi-asserted-by":"crossref","first-page":"7306","DOI":"10.1073\/pnas.1214441110","article-title":"LDL receptor and its family members serve as the cellular receptors for vesicular stomatitis virus","volume":"110","author":"Finkelshtein","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cell.2025.02.036_bib41","doi-asserted-by":"crossref","first-page":"5163","DOI":"10.1016\/j.cell.2021.09.001","article-title":"Lrp1 is a host entry factor for Rift Valley fever virus","volume":"184","author":"Ganaie","year":"2021","journal-title":"Cell"},{"key":"10.1016\/j.cell.2025.02.036_bib42","doi-asserted-by":"crossref","DOI":"10.3390\/v15010005","article-title":"In vitro and in vivo phenotypes of Venezuelan, eastern and western equine encephalitis viruses derived from cDNA clones of human isolates","volume":"15","author":"Gardner","year":"2022","journal-title":"Viruses"},{"key":"10.1016\/j.cell.2025.02.036_bib43","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1008061","article-title":"Human monoclonal antibodies against chikungunya virus target multiple distinct epitopes in the E1 and E2 glycoproteins","volume":"15","author":"Quiroz","year":"2019","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.cell.2025.02.036_bib44","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1038\/s41586-020-2915-3","article-title":"LDLRAD3 is a receptor for Venezuelan equine encephalitis virus","volume":"588","author":"Ma","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.cell.2025.02.036_bib45","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.ade8273","article-title":"A chikungunya virus-like particle vaccine induces broadly neutralizing and protective antibodies against alphaviruses in humans","volume":"15","author":"Raju","year":"2023","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.cell.2025.02.036_bib46","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1038\/nmeth.4169","article-title":"cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination","volume":"14","author":"Punjani","year":"2017","journal-title":"Nat. Methods"},{"key":"10.1016\/j.cell.2025.02.036_bib47","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.cell.2025.02.036_bib48","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1038\/s41592-022-01488-1","article-title":"ColabFold - Making protein folding accessible to all","volume":"19","author":"Mirdita","year":"2021","journal-title":"Nat. Methods"},{"key":"10.1016\/j.cell.2025.02.036_bib49","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/j.cell.2025.02.036_bib50","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1107\/S2059798318002425","article-title":"ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps","volume":"74","author":"Croll","year":"2018","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/j.cell.2025.02.036_bib51","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/j.cell.2025.02.036_bib52","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"Krissinel","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.cell.2025.02.036_bib53","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1002\/pro.3235","article-title":"UCSF ChimeraX: Meeting modern challenges in visualization and analysis","volume":"27","author":"Goddard","year":"2018","journal-title":"Protein Sci."},{"key":"10.1016\/j.cell.2025.02.036_bib54","doi-asserted-by":"crossref","first-page":"9278","DOI":"10.1128\/JVI.77.17.9278-9286.2003","article-title":"Recombinant sindbis\/Venezuelan equine encephalitis virus is highly attenuated and immunogenic","volume":"77","author":"Paessler","year":"2003","journal-title":"J. Virol."},{"key":"10.1016\/j.cell.2025.02.036_bib55","doi-asserted-by":"crossref","first-page":"7573","DOI":"10.1016\/j.vaccine.2007.07.061","article-title":"Chimeric Sindbis\/eastern equine encephalitis vaccine candidates are highly attenuated and immunogenic in mice","volume":"25","author":"Wang","year":"2007","journal-title":"Vaccine"},{"key":"10.1016\/j.cell.2025.02.036_bib56","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1006\/viro.1995.1516","article-title":"Double-subgenomic Sindbis virus recombinants expressing immunogenic proteins of Japanese encephalitis virus induce significant protection in mice against lethal JEV infection","volume":"212","author":"Pugachev","year":"1995","journal-title":"Virology"},{"key":"10.1016\/j.cell.2025.02.036_bib57","doi-asserted-by":"crossref","first-page":"2035","DOI":"10.1128\/JVI.02990-13","article-title":"Stable, high-level expression of reporter proteins from improved alphavirus expression vectors to track replication and dissemination during encephalitic and arthritogenic disease","volume":"88","author":"Sun","year":"2014","journal-title":"J. Virol."}],"container-title":["Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867425002727?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867425002727?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,5,29]],"date-time":"2025-05-29T14:41:27Z","timestamp":1748529687000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0092867425002727"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,5]]},"references-count":57,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2025,5]]}},"alternative-id":["S0092867425002727"],"URL":"https:\/\/doi.org\/10.1016\/j.cell.2025.02.036","relation":{},"ISSN":["0092-8674"],"issn-type":[{"value":"0092-8674","type":"print"}],"subject":[],"published":{"date-parts":[[2025,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural basis for plasticity in receptor engagement by an encephalitic alphavirus","name":"articletitle","label":"Article Title"},{"value":"Cell","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cell.2025.02.036","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"https:\/\/doi.org\/10.1016\/j.cell.2025.03.029","name":"associatedlink","label":"CrossRef DOI link to the associated document"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Author(s). Published by Elsevier Inc.","name":"copyright","label":"Copyright"}]}}