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

New polycyclic dual inhibitors of the wild type and the V27A mutant M2 channel of the influenza A virus with unexpected binding mode.

European journal of medicinal chemistry - 1 Jan 2015

Rey-Carrizo Matias, Gazzarrini Sabrina, Llabrés Salomé, Frigolé-Vivas Marta, Juárez-Jiménez Jordi, Font-Bardia Mercè, Naesens Lieve, Moroni Anna, Luque F Javier, Vázquez Santiago

Abstract excerpt

Two new polycyclic scaffolds were synthesized and evaluated as anti-influenza A compounds. The 5-azapentacyclo[6.4.0.0(2,10).0(3,7).0(9,11)]dodecane derivatives were only active against the wild-type M2 channel in the low-micromolar range. However, some of the 14-azaheptacyclo[8.6.1.0(2,5).0(3,11...

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 Cell Survival

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Influenza A virus

Share to Molecular Structure

Share to Polycyclic Compounds

Share to Structure-Activity Relationship

Share to Viral Matrix Proteins

Source

Identifiers

PMID: 25899336
DOI: 10.1016/j.ejmech.2015.04.030

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25899336-2026-09-04.2. 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

New polycyclic dual inhibitors of the wild type and the V27A mutant M2 channel of the influenza A virus with unexpected binding mode.PMID 25899336Read ↗

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

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 ↗

3-Azatetracyclo[5.2.1.1(5,8).0(1,5)]undecane derivatives: from wild-type inhibitors of the M2 ion channel of influenza A virus to derivatives with potent activity against the V27A mutant.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 ↗

Potent Anti-Influenza Synergistic Activity of Theobromine and ArainosineSemantic 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 ↗

Imidazole-based pinanamine derivatives: Discovery of dual inhibitors of the wild-type and drug-resistant mutant of the influenza A virus.Semantic proximity Read ↗

Exploring organosilane amines as potent inhibitors and structural probes of influenza a virus M2 proton channel.Semantic proximity Read ↗

Chemical Probes for Blocking of Influenza A M2 Wild-type and S31N Channels.Semantic proximity Read ↗

[Molecular Ion Channel Blockers of Influenza A and SARS-CoV-2 Viruses].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 ↗

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