ArticleMembranes2025
Conformation and Membrane Topology of the N-Terminal Ectodomain of Influenza A M2 Protein.
Article in Membranes, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
3 citing papers in PubMed.
- Pentameric M2e influenza vaccine candidate generates strong immunity with limited survival benefit.Human vaccines & immunotherapeutics · 2026Article
- A New Model for the Transmembrane Heterocomplex of Hemagglutinin HA and Ionic Channel M2 Proteins in Influenza A Virus.Doklady. Biochemistry and biophysics · 2026Article
- Preparing for the Next Influenza Pandemic: Vaccine Progress, Challenges, and Prospects.China CDC weekly · 2025Article
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Authors and funding
2 authors.
Funding
Abstract
The N-terminal ectodomain of the influenza A M2 protein is a target for universal influenza vaccine development and novel antiviral strategies. Despite the significance of this domain, it is poorly understood and most structural studies of the M2 protein have disregarded the N-terminal ectodomain in their analyses. Here, we report conformational properties and describe insights into the membrane topology of sites along the N-terminal ectodomain. Full-length M2 protein is embedded in lipid bilayer nanodiscs and studied using site-directed spin labeling electron paramagnetic resonance spectroscopy. Results are consistent with a turn in the middle of the ectodomain that changes in proximity to the membrane surface upon the addition of cholesterol or the antiviral drug rimantadine. Similarly to other domains of M2 protein, lineshape analysis suggests that the N-terminal ectodomain can adopt multiple conformations.
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Registered trials
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