2014
DOI: 10.1586/14760584.2015.961431
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Dengue virus envelope protein domain I/II hinge: a key target for dengue virus vaccine design?

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Cited by 9 publications
(1 citation statement)
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“…The characterization of large panels of potently neutralizing MAbs has greatly improved our understanding of the molecular basis of antibody neutralization and has the potential to inform vaccine design (7,(268)(269)(270). Because of the complex and dense arrangement of flavivirus E proteins on the virion surface, not all epitopes are equally accessible to antibodies (173).…”
Section: Epitope Specificities Of Neutralizing Antibodies Inform Vaccmentioning
confidence: 99%
“…The characterization of large panels of potently neutralizing MAbs has greatly improved our understanding of the molecular basis of antibody neutralization and has the potential to inform vaccine design (7,(268)(269)(270). Because of the complex and dense arrangement of flavivirus E proteins on the virion surface, not all epitopes are equally accessible to antibodies (173).…”
Section: Epitope Specificities Of Neutralizing Antibodies Inform Vaccmentioning
confidence: 99%