ArticleJournal of medicinal chemistry2025
Bifunctional Inhibition of Botulinum Neurotoxin A Protease: Unexpected Active Site Inhibition Enhances Covalent Targeting of an Allosteric Site.
Article in Journal of medicinal chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Botulinum neurotoxin: from molecular pathogenesis to emerging countermeasures.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Botulinum neurotoxin (BoNT) is the most toxic protein known to man and a Tier 1 bioterrorism agent. Among its serotypes, BoNT/A possesses the greatest potency and persistence, as such strategies to counteract it are highly coveted. Bifunctional molecules incorporating both metal chelation and a covalent warhead have shown great potential for blunting BoNT/A LC's toxicity/longevity. To further explore this idea, new warheads as well as zinc metal-chelating scaffolds were prepared and examined. The structure-activity relationship and kinetic analyses of these inhibitors challenged the standard protease assay leading to a new screening platform implemented and validated. Reconnaissance studies from this new screening platform delineated an unprecedented structural flexibility associated with BoNT/A's enzyme pocket, which can be induced by a small molecule for enhanced allosteric target inhibition of the protease. The culmination of these findings offers previously unrealized opportunities for neutralizing the BoNT/A protease and thus 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.