ArticleBiochemistry2026
Structural Bases for the Unconventional Activity of a Viroporin Channel.
Article in Biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Viroporins alter the permeability of cell membranes and regulate the initiation/progression of the viral infection cycle. However, the "unconventional" membrane channel behavior displayed by many members of the family challenges their general validation as therapeutic targets. The reported capacity of the Classical Swine Fever Virus p7 viroporin for establishing ion-conducting channels of different sizes exemplifies that behavior. Using all-atom molecular dynamics (MD) simulations, we attempted to elucidate the structural basis and mechanisms underlying the atypical activity of p7. Based on AlphaFold-predicted CSFV p7 hexamer structures with folded-back helical hairpins, we first generated monomers that spanned the entire thickness of the lipid bilayer. Next, we assembled oligomers of varying stoichiometry (pentamers, hexamers, and heptamers) based on those extended transmembrane hairpin (TMH) protomers. We focused on two hexameric models: TMH1, preserving the helix-helix packing interactions observed in the initial model, and TMH2
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.