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- W1001181796 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." @default.
- W1001181796 created "2016-06-24" @default.
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- W1001181796 date "2015-11-01" @default.
- W1001181796 modified "2023-09-24" @default.
- W1001181796 title "A computational view on the significance of E-ring in binding of (+)-arisugacin A to acetylcholinesterase" @default.
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- W1001181796 doi "https://doi.org/10.1016/j.bmcl.2015.06.047" @default.
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