Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin.

At a low pH, the influenza virus hemagglutinin (HA) undergoes conformational changes that promote membrane fusion. While the critical role of fusion peptide release from the trimer interface has been demonstrated previously, the role of globular head dissociation in the overall fusion mechanism rema...

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Bibliografiske detaljer

Udgivet i:	J Virol
Principais autores:	Kemble, G W, Bodian, D L, Rosé, J, Wilson, I A, White, J M
Format:	Artigo
Sprog:	Inglês
Udgivet:	American Society for Microbiology (ASM) 1992
Fag:	Research Article
Online adgang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC241339/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1629960/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.66.8.4940-4950.1992
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