ArticleVirology journal2025
Discovery of a novel broad-spectrum inhibitor against influenza virus A.
Article in Virology journal, 2025. 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
4 authors.
Funding
Abstract
The pandemic of influenza A virus (IAV) is on the rise worldwide, however, drug resistance to anti-influenza drugs has been widely found. The viral mutation of IAV highlights the necessitate for discovery of new antiviral agents with broad-spectrum efficacy. Arbidol, an effective pharmaceutical against IAV and other viruses, inhibits viral fusion by targeting a conserved binding region across multiple virus types. The binding area of Arbidol is conserved towards many types of viruses, however, the structural characteristics of Arbidol make it possible human ether-α-go-go related gene (hERG) potassium channel inhibitory. The risk of arrhythmias by Arbidol will limit its further application. Therefore, developing new broad-spectrum antiviral drugs with reduced side effects based on Arbidol's scaffold is imperative. In this study, 50 natural products were screened for effective universal antiviral drug based on the structure-activity relationship between Arbidol and hemagglutinin (HA). Due to the structural characters of Arbidol related to hERG inhibition, the inhibitory activity of Arbidol on hERG channels were also analyzed by patch clamp technology and molecular docking for toxicity and safety evaluation of drug screening and development. The IC50 of Arbidol to hERG was 0.3030 µM. The results showed that Glycyrrhetinic acid has lower binding energy than Arbidol in the binding site. The molecular structure of Glycyrrhetinic acid is more flexible, which avoids significant interactions with hERG. These findings highlight glycyrrhetinic acid as a promising broad-spectrum anti-IAV candidate drug.
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.