The DOI matches its Crossref record; 90 of the 90 references it cites were found in a registry or an index.
Influenza Hemagglutinin and Neuraminidase Membrane Glycoproteins
Open accessAbstract
Considerable progress has been made toward understanding the structural basis of the interaction of the two major surface glycoproteins of influenza A virus with their common ligand/substrate: carbohydrate chains terminating in sialic acid. The specificity of virus attachment to target cells is mediated by hemagglutinin, which acquires characteristic changes in its receptor-binding site to switch its host from avian species to humans. Anti-influenza drugs mimic the natural sialic acid substrate of the virus neuraminidase enzyme but utilize the much tighter binding of the drugs for efficacy. Resistance to one of the two main antiviral drugs is differentially acquired by the two distinct subsets of neuraminidase as a consequence of structural differences in the enzyme active site between the two phylogenetic groups.
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Cites
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Cited by
New World Bats Harbor Diverse Influenza A Viruses
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Molecular basis of the structure and function of H1 hemagglutinin of influenza virus
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Metadata
- Authors
- Gamblin, S. J., & Skehel, J. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-09
- Volume
- 285
- Issue
- 37
- Pages
- 28403-28409
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2083419156
- Cited by
- 638
- References
- 90
- FWCI
- 24.95
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Gamblin, S. J., & Skehel, J. J. (2010). Influenza Hemagglutinin and Neuraminidase Membrane Glycoproteins. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.r110.129809
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
