ArticleBioorganic & medicinal chemistry letters2015
A computational view on the significance of E-ring in binding of (+)-arisugacin A to acetylcholinesterase.
Article in Bioorganic & medicinal chemistry letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Design, Synthesis, andACS omega · 2022Article
- Synthesis of novel benzothiazole derivatives and investigation of their enzyme inhibitory effects against Alzheimer's disease.RSC advances · 2022Article
- A Comprehensive Review of Cholinesterase Modeling and Simulation.Biomolecules · 2021Review
- Design, Synthesis, and Structure-Activity Relationships of Thiazole Analogs as Anticholinesterase Agents for Alzheimer's Disease.Molecules (Basel, Switzerland) · 2020Article
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Abstract
A computational docking study of a series of de novo structural analogs of the highly potent, non-nitrogen containing, acetylcholinesterase inhibitor (+)-arisugacin A is presented. In direct comparison to the recently reported X-ray single-crystal structure of (+)-territrem B bound hAChE, the modeling suggests that there is a unique conformational preference for the E-ring that is responsible for the superior inhibitory activity of (+)-arisugacin A against hAChE relative to (+)-territrem B, and that substitutions on the E-ring also play an important role in the protein-ligand interaction.
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