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

Quantitative analysis of influenza M2 channel blockers.

Biochimica et biophysica acta - 1 Jan 2011

Astrahan Peleg, Flitman-Tene Ravenna, Bennett Estelle R, Krugliak Miriam, Gilon Chaim, Arkin Isaiah T

Abstract excerpt

The influenza M2 H(+) channel enables the concomitant acidification of the viral lumen upon endosomic internalization. This process is critical to the viral infectivity cycle, demonstrated by the fact that M2 is one of only two targets for anti-flu agents. However, aminoadamantyls that block the M2 channel are of limited therapeutic use due to the emergence of resistance mutations in the protein. Herein, using an...

Read the complete abstract on PubMed

Topics

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

Share to Amantadine
Share to Antiviral Agents
Share to Blotting, Western

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chemistry, Pharmaceutical

Share to Crystallography, X-Ray

Share to Influenza A Virus, H1N1 Subtype

Share to Plasmids

Share to Viral Matrix Proteins

Source

Identifiers

PMID: 20831860
DOI: 10.1016/j.bbamem.2010.08.021

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Quantitative analysis of influenza M2 channel blockers.PMID 20831860Read ↗

How do aminoadamantanes block the influenza M2 channel, and how does resistance develop?Semantic proximity Read ↗

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

Influenza Viruses: Harnessing the Crucial Role of the M2 Ion-Channel and Neuraminidase toward Inhibitor DesignSemantic proximity Read ↗

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

An amantadine-sensitive chimeric BM2 ion channel of influenza B virus has implications for the mechanism of drug inhibition.Semantic proximity Read ↗

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

Potent Anti-Influenza Synergistic Activity of Theobromine and ArainosineSemantic proximity Read ↗

Influenza virus proton channels.Semantic proximity Read ↗

Discovery of M2 channel blockers targeting the drug-resistant double mutants M2-S31N/L26I and M2-S31N/V27A from the influenza A viruses.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 ↗

An M2-V27A channel blocker demonstrates potent in vitro and in vivo antiviral activities against amantadine-sensitive and -resistant influenza A viruses.Semantic proximity Read ↗

Slow but Steady Wins the Race: Dissimilarities among New Dual Inhibitors of the Wild-Type and the V27A Mutant M2 Channels of Influenza A Virus.Semantic proximity Read ↗

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