A common mechanism for influenza virus fusion activity and inactivation
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00062a006
Reference38 articles.
1. pH-dependent fusion of vesicular stomatitis virus with Vero cells. Measurement by dequenching of octadecyl rhodamine fluorescence.
2. Fusion activity of influenza virus PR8/34 correlates with a temperature-induced conformational change within the hemagglutinin ectodomain detected by photochemical labeling
3. Quaternary structure of influenza virus hemagglutinin after acid treatment
4. Membrane fusion activity of the influenza virus hemagglutinin. The low pH-induced conformational change.
5. Membrane action of synthetic N-terminal peptides of influenza virus hemagglutinin and its mutants
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3. Inhibition of Viral Membrane Fusion by Peptides and Approaches to Peptide Design;Pathogens;2021-12-09
4. Mildly Acidic pH Triggers an Irreversible Conformational Change in the Fusion Domain of Herpes Simplex Virus 1 Glycoprotein B and Inactivation of Viral Entry;Journal of Virology;2017-03
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