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

Magic-angle-spinning NMR of the drug resistant S31N M2 proton transporter from influenza A.

Journal of the American Chemical Society - 2 May 2012

Andreas Loren B, Eddy Matthew T, Chou James J, Griffin Robert G

Abstract excerpt

We report chemical shift assignments of the drug-resistant S31N mutant of M2(18-60) determined using 3D magic-angle-spinning (MAS) NMR spectra acquired with a (15)N-(13)C ZF-TEDOR transfer followed by (13)C-(13)C mixing by RFDR. The MAS spectra reveal two sets of resonances, indicating that the tetramer assembles as a dimer of dimers, similar to the wild-type channel. Helicies from the two sets of chemical shifts...

Read the complete abstract on PubMed

Topics

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

Share to Antiviral Agents
Share to Carrier Proteins
Share to Drug Resistance, Viral

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Influenza A virus

Share to Influenza, Human

Share to Magnetic Resonance Spectroscopy

Share to Protons

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 22480220
DOI: 10.1021/ja3003606
PMCID: PMC3342473

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Magic-angle-spinning NMR of the drug resistant S31N M2 proton transporter from influenza A.PMID 22480220Read ↗

Drug-induced conformational and dynamical changes of the S31N mutant of the influenza M2 proton channel investigated by solid-state NMR.Semantic proximity Read ↗

Dynamic nuclear polarization study of inhibitor binding to the M2(18-60) proton transporter from influenza A.Semantic proximity Read ↗

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

Flipping in the pore: discovery of dual inhibitors that bind in different orientations to the wild-type versus the amantadine-resistant S31N mutant of the influenza A 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 ↗

Discovery of novel dual inhibitors of the wild-type and the most prevalent drug-resistant mutant, S31N, of the M2 proton channel from influenza A virus.Semantic proximity Read ↗

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

Crystal structure of the drug-resistant S31N influenza M2 proton channel.Semantic proximity Read ↗

X-ray Crystal Structures of the Influenza M2 Proton Channel Drug-Resistant V27A Mutant Bound to a Spiro-Adamantyl Amine Inhibitor Reveal the Mechanism of Adamantane Resistance.Semantic proximity Read ↗

Antiviral mechanisms and preclinical evaluation of amantadine analogs that continue to inhibit influenza A viruses with M2S31N-based drug resistance.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 ↗

Hydrogen-bonded water molecules in the M2 channel of the influenza A virus guide the binding preferences of ammonium-based inhibitors.Semantic proximity Read ↗

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