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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Detalles Bibliográficos

Publicado en:	J Virol
Principais autores:	Kemble, G W, Bodian, D L, Rosé, J, Wilson, I A, White, J M
Formato:	Artigo
Idioma:	Inglês
Publicado:	American Society for Microbiology (ASM) 1992
Assuntos:	Research Article
Acceso en liña:	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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