The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Structural basis of influenza virus fusion inhibition by the antiviral drug Arbidol
Open accessAbstract
Significance: Influenza virus is an important human pathogen. The circulating strains of influenza virus are constantly mutating and are acquiring resistance to all approved drugs. Therefore, development of influenza therapeutics against novel targets is urgently required. The hemagglutinin envelope glycoprotein (HA) is a promising target for small-molecule design. However, Arbidol is the only available antiviral drug that targets the HA. The absence of structural information on drug–HA complexes has hindered further therapeutic development efforts against this viral pathogen. Here, we report crystal structures of Arbidol in complex with influenza HAs. This structural information advances our understanding of how small molecules, such as Arbidol, can function as influenza fusion inhibitors and can be used for development of broad-spectrum, small-molecule therapeutics.
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Metadata
- Authors
- Kadam, R. U., & Wilson, I. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2016-12-21
- Volume
- 114
- Issue
- 2
- Pages
- 206-214
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2563411735
- Cited by
- 435
- References
- 40
- FWCI
- 14.45
- Type
- journal article
- Language
- en
- Open access
- bronze
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