ArticleScientific reports2026
Lethal effects of ivermectin structures on malaria vectors and in silico analysis of interactions with their glutamate-gated chloride ion channels.
Article in Scientific reports, 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
10 authors.
Funding
Abstract
Ivermectin is lethal to Anopheles mosquitoes making it a possible malaria control intervention. The primary mode of action of ivermectin occurs when it binds to the glutamate-gated chloride channel (GluCl), allowing for continuous flow of chloride leading to flaccid paralysis and death of the mosquito. In Caenorhabditis elegans, ivermectin is thought to open the GluCl channel when the M2-M3 loop forms Van der Waals bonds with the first sugar ring and aglycone structure of ivermectin. Here we investigate in Anopheles dirus and Anopheles minimus the mosquito-lethal effect of ivermectin (both sugar rings), monosaccharide (one sugar ring), and aglycone (no sugar rings) demonstrating full, partial, and no effect, respectively. The Anopheles GluCl protein sequences were determined and used to a create 3-D structural docking models. The docking models identified new binding interactions with a hydrogen bond forming between the second sugar ring hydroxyl group (4″-OH) and THR304 of the Anopheles GluCl M2-M3 loop. This hydrogen bond is possible due to a single substitution in the M2-M3 loop from C. elegans ILE273 to Anopheles THR304. The work presented here improves our understanding of Anopheles GluCl-ivermectin interactions as well as how ivermectin resistance could arise in the future.
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.