dc.contributor.author | Harrison, Stephen | |
dc.date.accessioned | 2010-03-03T14:53:43Z | |
dc.date.issued | 2008 | |
dc.identifier.citation | Harrison, Stephen C. 2008. Viral membrane fusion. Nature Structural and Molecular Biology 15, no. 7: 690-698. | en |
dc.identifier.issn | 1545-9993 | en |
dc.identifier.uri | http://nrs.harvard.edu/urn-3:HUL.InstRepos:3710801 | |
dc.description.abstract | Infection 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.sponsorship | Chemistry and Chemical Biology | en |
dc.description.sponsorship | Molecular and Cellular Biology | en |
dc.language.iso | en_US | en |
dc.publisher | Nature Publishing Group | en |
dc.relation.isversionof | http://dx.doi.org/10.1038/nsmb.1456 | en |
dash.license | LAA | |
dc.title | Viral Membrane Fusion | en |
dc.relation.journal | Nature Structural and Molecular Biology | en |
dash.depositing.author | Harrison, Stephen | |
dc.date.available | 2010-03-03T14:53:43Z | |
dc.identifier.doi | 10.1038/nsmb.1456 | * |
dash.contributor.affiliated | Harrison, Stephen | |