ArticleChemico-biological interactions2013
Aryl methylcarbamates: potency and selectivity towards wild-type and carbamate-insensitive (G119S) Anopheles gambiae acetylcholinesterase, and toxicity to G3 strain An. gambiae.
Article in Chemico-biological interactions, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Mosquito mutations F290V and F331W expressed in acetylcholinesterase of the sand fly Phlebotomus papatasi (Scopoli): biochemical properties and inhibitor sensitivity.Parasites & vectors · 2025Article
- Structure-Activity Relationships Reveal Beneficial Selectivity Profiles of Inhibitors Targeting Acetylcholinesterase of Disease-Transmitting Mosquitoes.Journal of medicinal chemistry · 2023Article
- Mosquito Acetylcholinesterase as a Target for Novel Phenyl-Substituted Carbamates.International journal of environmental research and public health · 2019Article
- Select β- and γ-branched 1-alkylpyrazol-4-yl methylcarbamates exhibit high selectivity for inhibition ofPesticide biochemistry and physiology · 2018Article
- Discovery of Species-selective and Resistance-breaking Anticholinesterase Insecticides for the Malaria Mosquito.Current medicinal chemistry · 2017Review
- Article
- An insecticide resistance-breaking mosquitocide targeting inward rectifier potassium channels in vectors of Zika virus and malaria.Scientific reports · 2016Article
- Difluoromethyl ketones: Potent inhibitors of wild type and carbamate-insensitive G119S mutant Anopheles gambiae acetylcholinesterase.Bioorganic & medicinal chemistry letters · 2015Article
- Mosquitocidal carbamates with low toxicity to agricultural pests: an advantageous property for insecticide resistance management.Pest management science · 2015Article
- 3-Oxoisoxazole-2(3H)-carboxamides and isoxazol-3-yl carbamates: Resistance-breaking acetylcholinesterase inhibitors targeting the malaria mosquito, Anopheles gambiae.Bioorganic & medicinal chemistry · 2015Article
- Acetylcholinesterase of the sand fly, Phlebotomus papatasi (Scopoli): construction, expression and biochemical properties of the G119S orthologous mutant.Parasites & vectors · 2014Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
New carbamates that are highly selective for inhibition of Anopheles gambiae acetylcholinesterase (AChE) over the human enzyme might be useful in continuing efforts to limit malaria transmission. In this report we assessed 34 synthesized and commercial carbamates for their selectivity to inhibit the AChEs found in carbamate-susceptible (G3) and carbamate-resistant (Akron) An. gambiae, relative to human AChE. Excellent correspondence is seen between inhibition potencies measured with carbamate-susceptible mosquito homogenate and purified recombinant wild-type (WT) An. gambiae AChE (AgAChE). Similarly, excellent correspondence is seen between inhibition potencies measured with carbamate-resistant mosquito homogenate and purified recombinant G119S AgAChE, consistent with our earlier finding that the Akron strain carries the G119S mutation. Although high (100- to 500-fold) WT An. gambiae vs human selectivity is observed for several compounds, none of the carbamates tested potently inhibits the G119S mutant enzyme. Finally, we describe a predictive model for WT An. gambiae tarsal contact toxicity of the carbamates that relies on inhibition potency, molecular volume, and polar surface area.
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