ArticleBiochemistry2014
Probing BoNT/A protease exosites: implications for inhibitor design and light chain longevity.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
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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.
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Who cites it
7 citing papers in PubMed.
- Regulation of Peptidase Activity beyond the Active Site in Human Health and Disease.International journal of molecular sciences · 2023Review
- Strategies to Counteract Botulinum Neurotoxin A: Nature's Deadliest Biomolecule.Accounts of chemical research · 2019Article
- Natural Compounds and Their Analogues as Potent Antidotes against the Most Poisonous Bacterial Toxin.Applied and environmental microbiology · 2018Article
- A novel role of C-terminus in introducing a functionally flexible structure critical for the biological activity of botulinum neurotoxin.Scientific reports · 2018Article
- Examination of α-exosite inhibitors against Botulinum neurotoxin A protease through structure-activity relationship studies of chicoric acid.Bioorganic & medicinal chemistry letters · 2017Article
- Small molecule metalloprotease inhibitor with in vitro, ex vivo and in vivo efficacy against botulinum neurotoxin serotype A.Toxicon : official journal of the International Society on Toxinology · 2017Article
- Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Botulinum neurotoxin serotype A (BoNT/A) is one of the most lethal toxins known. Its extreme toxicity is due to its light chain (LC), a zinc protease that cleaves SNAP-25, a synaptosome-associated protein, leading to the inhibition of neuronal activity. Studies on BoNT/A LC have revealed that two regions, termed exosites, can play an important role in BoNT catalytic activity. A clear understanding of how these exosites influence neurotoxin catalytic activity would provide a critical framework for deciphering the mechanism of SNAP-25 cleavage and the design of inhibitors. Herein, based on the crystallographic structure of BoNT/A LC complexed with its substrate, we designed an α-exosite binding probe. Experiments with this unique probe demonstrated that α-exosite binding enhanced both catalytic activity and stability of the LC. These data help delineate why α-exosite binding is needed for SNAP-25 cleavage and also provide new insights into the extended lifetime observed for BoNT/A LC in vivo.
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Registered trials
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