ArticleJournal of enzyme inhibition and medicinal chemistry2010
Inactivation of acetylcholinesterase by various fluorophores.
Article in Journal of enzyme inhibition and medicinal chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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Who cites it
1 citing paper in PubMed, 1 citations in OpenAlex.
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The inhibition of recombinant mouse acetylcholinesterase (rMAChE) and electric eel acetylcholinesterase (EEAChE) by seven, structurally different chromophore-based (dansyl, pyrene, dabsyl, diethylamino- and methoxycoumarin, Lissamine rhodamine B, and Texas Red) propargyl carboxamides or sulfonamides was studied. Diethylaminocoumarin, Lissamine, and Texas Red amides inhibited rMAChE with IC50 values of 1.00 microM, 0.05 microM, and 0.70 microM, respectively. Lissamine and Texas Red amides inhibited EEAChE with IC50 values of 3.57 and 10.4 microM, respectively. The other chromophore amides did not inhibit either AChE. The surprising inhibitory potency of Lissamine was examined in further detail against EEAChE and revealed a mixed-type inhibition with Ki = 11.7 microM (competitive) and Ki' = 24.9 microM (noncompetitive), suggesting that Lissamine binds to free enzyme and enzyme-substrate complex.
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Registered trials
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