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

Designing inhibitors of M2 proton channel against H1N1 swine influenza virus.

PloS one - 23 Feb 2010

Du Qi-Shi, Huang Ri-Bo, Wang Shu-Qing, Chou Kuo-Chen

Abstract excerpt

BACKGROUND: M2 proton channel of H1N1 influenza A virus is the target protein of anti-flu drugs amantadine and rimantadine. However, the two once powerful adamantane-based drugs lost their 90% bioactivity because of mutations of virus in recent twenty years. The NMR structure of the M2 channel pr...

Read the complete abstract on PubMed

Topics

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

Share to Drug Design
Share to Influenza A Virus, H1N1 Subtype
Share to Ion Channels

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to Molecular Structure

Share to Orthomyxoviridae Infections

Share to Swine Diseases

Share to Viral Matrix Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 20186344
DOI: 10.1371/journal.pone.0009388
PMCID: PMC2826421

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20186344-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Designing inhibitors of M2 proton channel against H1N1 swine influenza virus.PMID 20186344Read ↗

Recent progress in designing inhibitors that target the drug‐resistant M2 proton channels from the influenza A virusesSemantic proximity Read ↗

Computational investigation of drug-resistant mutant of M2 proton channel (S31N) against rimantadine.Semantic proximity Read ↗

Influenza virus proton channels.Semantic proximity Read ↗

Structural comparison of the wild-type and drug-resistant mutants of the influenza A M2 proton channel by molecular dynamics simulations.Semantic proximity Read ↗

An in-depth analysis of the biological functional studies based on the NMR M2 channel structure of influenza A virus.Semantic proximity Read ↗

Flu channel drug resistance: a tale of two sites.Semantic proximity Read ↗

Insights from studying the mutation-induced allostery in the M2 proton channel by molecular dynamics.Semantic proximity Read ↗

Research/review: Structure and linkage disequilibrium analysis of adamantane resistant mutations in influenza virus m2 proton channel.Semantic proximity Read ↗

A Study of the Activity of Adamantyl Amines against Mutant Influenza A M2 Channels Identified a Polycyclic Cage Amine Triple Blocker, Explored by Molecular Dynamics Simulations and Solid-State NMR.Semantic proximity Read ↗

Functional studies and modeling of pore-lining residue mutants of the influenza a virus M2 ion channel.Semantic proximity Read ↗

Easily accessible polycyclic amines that inhibit the wild-type and amantadine-resistant mutants of the M2 channel of influenza A virus.Semantic proximity Read ↗

Structure and inhibition of the drug-resistant S31N mutant of the M2 ion channel of influenza A virus.Semantic proximity Read ↗

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