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

Identification of the pore-lining residues of the BM2 ion channel protein of influenza B virus.

The Journal of biological chemistry - 6 Jun 2008

Ma Chunlong, Soto Cinque S, Ohigashi Yuki, Taylor Albert, Bournas Vasilios, Glawe Brett, Udo Maria K, Degrado William F, Lamb Robert A, Pinto Lawrence H

Abstract excerpt

The influenza B virus BM2 proton-selective ion channel is essential for virus uncoating, a process that occurs in the acidic environment of the endosome. The BM2 channel causes acidification of the interior of the virus particle, which results in dissociation of the viral membrane protein from the ribonucleo-protein core. The BM2 protein is similar to the A/M2 protein ion channel of influenza A virus (A/M2) in...

Read the complete abstract on PubMed

Topics

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

Share to Amantadine
Share to Amino Acid Motifs

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Resistance, Viral

Share to Endosomes

Share to Influenza B virus

Share to Ion Channels

Share to Oocytes

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 18408016
DOI: 10.1074/jbc.M710302200
PMCID: PMC2414288

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

Identification of the pore-lining residues of the BM2 ion channel protein of influenza B virus.PMID 18408016Read ↗

Influenza B virus BM2 protein has ion channel activity that conducts protons across membranes.Semantic proximity Read ↗

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

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

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

Analysis of the pore structure of the influenza A virus M(2) ion channel by the substituted-cysteine accessibility method.Semantic proximity Read ↗

Functional studies reveal the similarities and differences between AM2 and BM2 proton channels from influenza viruses.Semantic proximity Read ↗

Comparison of the activities of BM2 protein and its H19 and W23 mutants of influenza B virus with activities of M2 protein and its H37 and W41 mutants of influenza A virus.Semantic proximity Read ↗

The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue.Semantic proximity Read ↗

Mutations in the membrane-proximal region of the influenza A virus M2 protein cytoplasmic tail have modest effects on virus replication.Semantic proximity Read ↗

Direct measurement of the influenza A virus M2 protein ion channel activity in mammalian cells.Semantic proximity Read ↗

Influenza virus proton channels.Semantic proximity Read ↗

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

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