Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Exploring the mechanism of zanamivir resistance in a neuraminidase mutant: a molecular dynamics study.

PloS one - 1 Jan 2012

Han Nanyu, Liu Xuewei, Mu Yuguang

Abstract excerpt

It is critical to understand the molecular basis of the drug resistance of influenza viruses to efficiently treat this infectious disease. Recently, H1N1 strains of influenza A carrying a mutation of Q136K in neuraminidase were found. The new strain showed a strong Zanamivir neutralization effect...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Apoproteins
Share to Hydrogen Bonding
Share to Influenza A Virus, H1N1 Subtype

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Mutant Proteins

Share to Neuraminidase

Share to Structural Homology, Protein

Share to Zanamivir

Source

Open in PubMed Open full text

Identifiers

PMID: 22970161
DOI: 10.1371/journal.pone.0044057
PMCID: PMC3435372

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22970161-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Exploring the mechanism of zanamivir resistance in a neuraminidase mutant: a molecular dynamics study.PMID 22970161Read ↗

Prediction of zanamivir efficiency over the possible 2009 influenza A (H1N1) mutants by multiple molecular dynamics simulations and free energy calculations.Semantic proximity Read ↗

<i>In Silico</i> Identification of the Potential Drug Resistance Sites over 2009 Influenza A (H1N1) Virus NeuraminidaseSemantic proximity Read ↗

Structural insight into the mechanism of neuraminidase inhibitor-resistant mutations in human-infecting H10N8 Influenza A virusSemantic proximity Read ↗

In silico study on multidrug resistance conferred by I223R/H275Y double mutant neuraminidase.Semantic proximity Read ↗

Study of drug resistance of chicken influenza A virus (H5N1) from homology-modeled 3D structures of neuraminidases.Semantic proximity Read ↗

Computational studies of H5N1 influenza virus resistance to oseltamivir.Semantic proximity Read ↗

Structural analysis of the novel influenza A (H7N9) viral Neuraminidase interactions with current approved neuraminidase inhibitors Oseltamivir, Zanamivir, and Peramivir in the presence of mutation R289K.Semantic proximity Read ↗

In silico prediction of drug resistance due to S247R mutation of Influenza H1N1 neuraminidase protein.Semantic proximity Read ↗

Molecular basis of drug resistance in A/H1N1 virus.Semantic proximity Read ↗

In Silico Studies Reveal Peramivir and Zanamivir as an Optimal Drug Treatment Even If H7N9 Avian Type Influenza Virus Acquires Further Resistance.Semantic proximity Read ↗

Theoretical studies on the susceptibility of oseltamivir against variants of 2009 A/H1N1 influenza neuraminidase.Semantic proximity Read ↗

Mechanism of 150-cavity formation in influenza neuraminidaseSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.