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dc.contributor.authorHarrison, Stephen
dc.date.accessioned2010-03-03T14:53:43Z
dc.date.issued2008
dc.identifier.citationHarrison, Stephen C. 2008. Viral membrane fusion. Nature Structural and Molecular Biology 15, no. 7: 690-698.en
dc.identifier.issn1545-9993en
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:3710801
dc.description.abstractInfection by viruses having lipid-bilayer envelopes proceeds through fusion of the viral membrane with a membrane of the target cell. Viral ‘fusion proteins’ facilitate this process. They vary greatly in structure, but all seem to have a common mechanism of action, in which a ligand-triggered, largescale conformational change in the fusion protein is coupled to apposition and merger of the two bilayers. We describe three examples—the influenza virus hemagglutinin, the flavivirus E protein and the vesicular stomatitis virus G protein—in some detail, to illustrate the ways in which different structures have evolved to implement this common mechanism. Fusion inhibitors can be effective antiviral agents.en
dc.description.sponsorshipChemistry and Chemical Biologyen
dc.description.sponsorshipMolecular and Cellular Biologyen
dc.language.isoen_USen
dc.publisherNature Publishing Groupen
dc.relation.isversionofhttp://dx.doi.org/10.1038/nsmb.1456en
dash.licenseLAA
dc.titleViral Membrane Fusionen
dc.relation.journalNature Structural and Molecular Biologyen
dash.depositing.authorHarrison, Stephen
dc.date.available2010-03-03T14:53:43Z
dc.identifier.doi10.1038/nsmb.1456*
dash.contributor.affiliatedHarrison, Stephen


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