Hemagglutinin Stability Determines Influenza A Virus Susceptibility to a Broad-Spectrum Fusion Inhibitor Arbidol
Author:
Affiliation:
1. Biochemistry Department, Brandeis University, Waltham, Massachusetts 02453, United States
Funder
National Institute of General Medical Sciences
Division of Materials Research
Publisher
American Chemical Society (ACS)
Subject
Infectious Diseases
Link
https://pubs.acs.org/doi/pdf/10.1021/acsinfecdis.2c00178
Reference47 articles.
1. Structure of the Hemagglutinin Precursor Cleavage Site, a Determinant of Influenza Pathogenicity and the Origin of the Labile Conformation
2. Viral membrane fusion
3. Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity
4. Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin
5. A spring-loaded mechanism for the conformational change of influenza hemagglutinin
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