ArticleNature communications2011
Mechanism of 150-cavity formation in influenza neuraminidase.
Article in Nature communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 145 citations in OpenAlex.
- Curtisians W and X, two new p-terphenyls from the fruiting bodies of Pseudomerulius curtisii, and their neuraminidase inhibitory activity.The Journal of antibiotics · 2026Article
- Discovery of Influenza Neuraminidase Inhibitors: Structure-Based Virtual Screening and Biological Evaluation of Novel Chemotypes.Molecules (Basel, Switzerland) · 2025Article
- Identification of Novel Neuraminidase Inhibitors as Potential Anti-Influenza Agents: Virtual Screening, Molecular Docking, in vitro Validation and Molecular Dynamic Simulation Studies.Cell biochemistry and biophysics · 2025Article
- Broad neuraminidase antibodies confer protection against seasonal and avian influenza viruses.Nature communications · 2025Article
- Formulation development of a stable influenza recombinant neuraminidase vaccine candidate.Human vaccines & immunotherapeutics · 2024Article
- Molecular dynamics study on the effect of the N1 neuraminidase double mutant G147R/H274Y on oseltamivir sensitivity.RSC advances · 2024Article
- Indole-core inhibitors of influenza a neuraminidase: iterative medicinal chemistry and molecular modeling.European journal of medicinal chemistry · 2024Article
- Antiviral Susceptibility of Highly Pathogenic Avian Influenza A(H5N1) Viruses Circulating Globally in 2022-2023.The Journal of infectious diseases · 2024Article
- Worth the Weight: Sub-Pocket EXplorer (SubPEx), a Weighted Ensemble Method to Enhance Binding-Pocket Conformational Sampling.Journal of chemical theory and computation · 2023Article
- Worth the weight: Sub-Pocket EXplorer (SubPEx), a weighted-ensemble method to enhance binding-pocket conformational sampling.bioRxiv : the preprint server for biology · 2023Article
- FPocketWeb: protein pocket hunting in a web browser.Journal of cheminformatics · 2022Article
- Binding mechanism of oseltamivir and influenza neuraminidase suggests perspectives for the design of new anti-influenza drugs.PLoS computational biology · 2022Article
- Structure-based design of stabilized recombinant influenza neuraminidase tetramers.Nature communications · 2022Article
- Effect of SerialJournal of veterinary research · 2022Article
- Influenza A Virus Neuraminidase Inhibitors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Drug Design Strategies to Avoid Resistance in Direct-Acting Antivirals and Beyond.Chemical reviews · 2021Review
- Structure-based design of 5'-substituted 1,2,3-triazolylated oseltamivir derivatives as potent influenza neuraminidase inhibitors.RSC advances · 2021Article
- Bioinformatic analysis of subfamily-specific regions in 3D-structures of homologs to study functional diversity and conformational plasticity in protein superfamilies.Computational and structural biotechnology journal · 2021Article
- Influenza Neuraminidase Characteristics and Potential as a Vaccine Target.Frontiers in immunology · 2021Review
- Characterization of Natural and Synthetic Sialoglycans Targeting the Hemagglutinin-Neuraminidase of Mumps Virus.Frontiers in chemistry · 2021Article
5 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The recently discovered 150-cavity in the active site of group-1 influenza A neuraminidase (NA) proteins provides a target for rational structure-based drug development to counter the increasing frequency of antiviral resistance in influenza. Surprisingly, the 2009 H1N1 pandemic virus (09N1) neuraminidase was crystalized without the 150-cavity characteristic of group-1 NAs. Here we demonstrate, through a total sum of 1.6 μs of biophysical simulations, that 09N1 NA exists in solution preferentially with an open 150-cavity. Comparison with simulations using avian N1, human N2 and 09N1 with a I149V mutation and an extensive bioinformatics analysis suggests that the conservation of a key salt bridge is crucial in the stabilization of the 150-cavity across both subtypes. This result provides an atomic-level structural understanding of the recent finding that antiviral compounds designed to take advantage of contacts in the 150-cavity can inactivate both 2009 H1N1 pandemic and avian H5N1 viruses.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.