ArticleScientific reports2013
Structural basis for a class of nanomolar influenza A neuraminidase inhibitors.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Thirty-Five-Year History of Desialylated Lipoproteins Discovered by Vladimir Tertov.Biomedicines · 2022Review
- Influenza A Virus Neuraminidase Inhibitors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Optimisation of Neuraminidase Expression for Use in Drug Discovery by Using HEK293-6E Cells.Viruses · 2021Article
- Structure-based design of 5'-substituted 1,2,3-triazolylated oseltamivir derivatives as potent influenza neuraminidase inhibitors.RSC advances · 2021Article
- Inhibition of sialidase activity as a therapeutic approach.Drug design, development and therapy · 2018Review
- WD40 repeat domain proteins: a novel target class?Nature reviews. Drug discovery · 2017Review
- Progress of small molecular inhibitors in the development of anti-influenza virus agents.Theranostics · 2017Review
- Resistance to Mutant Group 2 Influenza Virus Neuraminidases of an Oseltamivir-Zanamivir Hybrid Inhibitor.Journal of virology · 2016Article
- Meeting report: 4th ISIRV antiviral group conference: Novel antiviral therapies for influenza and other respiratory viruses.Antiviral research · 2016Article
- Structure-Based Design of Human TLR8-Specific Agonists with Augmented Potency and Adjuvanticity.Journal of medicinal chemistry · 2015Article
- Atypical group 1 neuraminidase pH1N1-N1 bound to a group 1 inhibitor.Protein & cell · 2015Article
- Inhibition of neuraminidase by Ganoderma triterpenoids and implications for neuraminidase inhibitor design.Scientific reports · 2015Article
- Article
- Modulating carnitine levels by targeting its biosynthesis pathway - selective inhibition of γ-butyrobetaine hydroxylase.Chemical science · 2014Article
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Authors and funding
6 authors.
Funding
Abstract
The influenza virus neuraminidase (NA) is essential for the virus life cycle. The rise of resistance mutations against current antiviral therapies has increased the need for the development of novel inhibitors. Recent efforts have targeted a cavity adjacent to the catalytic site (the 150-cavity) in addition to the primary catalytic subsite in order to increase specificity and reduce the likelihood of resistance. This study details structural and in vitro analyses of a class of inhibitors that bind uniquely in both subsites. Crystal structures of three inhibitors show occupation of the 150-cavity in two distinct and novel binding modes. We believe these are the first nanomolar inhibitors of NA to be characterized in this way. Furthermore, we show that one inhibitor, binding within the catalytic site, offers reduced susceptibility to known resistance mutations via increased flexibility of a pendant pentyloxy group and the ability to pivot about a strong hydrogen-bonding network.
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