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Membrane Structures of the Hemifusion-Inducing Fusion Peptide Mutant G1S and the Fusion-Blocking Mutant G1V of Influenza Virus Hemagglutinin Suggest a Mechanism for Pore Opening in Membrane Fusion
Influenza virus hemagglutinin (HA)-mediated membrane fusion is initiated by a conformational change that releases a V-shaped hydrophobic fusion domain, the fusion peptide, into the lipid bilayer of the target membrane. The most N-terminal residue of this domain, a glycine, is highly conserved and is...
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| Autori principali: | , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society for Microbiology
2005
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1212637/ https://ncbi.nlm.nih.gov/pubmed/16140782 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JVI.79.18.12065-12076.2005 |
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