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...
保存先:
| 出版年: | J Virol |
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| 主要な著者: | , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American Society for Microbiology (ASM)
1992
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| 主題: | |
| オンライン･アクセス: | 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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