ArticleBioorganic & medicinal chemistry letters2012
Reexamining hydroxamate inhibitors of botulinum neurotoxin serotype A: extending towards the β-exosite.
Article in Bioorganic & medicinal chemistry letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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
8 citing papers in PubMed, 12 citations in OpenAlex.
- Investigations of Thiosemicarbazides as Botulinum Toxin Active-Site Inhibitors: Enzyme, Cellular, and Rodent Intoxication Studies.ACS infectious diseases · 2024Article
- Identification of Slow-Binding Inhibitors of the BoNT/A Protease.ACS medicinal chemistry letters · 2022Article
- Catch and Anchor Approach To Combat Both Toxicity and Longevity of Botulinum Toxin A.Journal of medicinal chemistry · 2020Article
- Strategies to Counteract Botulinum Neurotoxin A: Nature's Deadliest Biomolecule.Accounts of chemical research · 2019Article
- Systematic discovery of molecular probes targeting multiple non-orthosteric and spatially distinct sites in the botulinum neurotoxin subtype A (BoNT/A).Molecular and cellular probes · 2015Article
- Identification of clinically viable quinolinol inhibitors of botulinum neurotoxin A light chain.Journal of medicinal chemistry · 2014Article
- Cargo-delivery platforms for targeted delivery of inhibitor cargos against botulism.Current topics in medicinal chemistry · 2014Review
- A high-throughput-compatible FRET-based platform for identification and characterization of botulinum neurotoxin light chain modulators.Journal of visualized experiments : JoVE · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Botulinum neurotoxins (BoNTs) are the most toxic proteins known to man, exposure to which results in flaccid paralysis. Given their extreme potency, these proteins have become studied as possible weapons of bioterrorism; however, effective treatments that function after intoxication have not progressed to the clinic. Here, we have reexamined one of the most effective inhibitors, 2,4-dichlorocinnamyl hydroxamate, in the context of the known plasticity of the BoNT/A light chain metalloprotease. Our studies have shown that modifications of this compound are tolerated and result in improved inhibitors, with the best compound having an IC(50) of 0.23 μM. Given the inconsistency of structure-activity relationship trends observed across similar compounds, this data argues for caution in extrapolating across structural series.
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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.