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1 tent combined inhibition of human BACE-1 and ChEs, as well as good antioxidant and CNS-permeable prop
2 ignificant in vitro anticholinesterase (anti-ChE) activity, the most potent compound (44) among them
3  Compound 44 showed significant in vivo anti-ChE and antioxidant activities.
4                                         Both ChE transcripts have the characteristics of H-type catal
5 ntact cholinergic cells with cholinesterase (ChE) inhibitors.
6                             Cholinesterases (ChE), use a Glu-His-Ser catalytic triad to enhance the n
7 anophosphate (OP)-inhibited cholinesterases (ChE) was synthesized and tested in vitro and in vivo.
8 es of oxime reactivators of cholinesterases (ChEs) that contain tertiary amine or imidazole protonata
9 e interaction of E2020 with cholinesterases (ChEs) with known sequence differences, was examined in m
10 nd 19 were identified as effective dual FAAH/ChE inhibitors, with well-balanced nanomolar activities.
11 at resembles the acyl pocket of invertebrate ChE, while the acyl-binding site of ChE1 is novel.
12 n this study treatment with the long-lasting ChE inhibitor metrifonate facilitated acquisition and re
13 disparate pH dependences for reactivation of ChE and the general base-catalyzed oximolysis of acetylt
14 n states are involved in the reactivation of ChE conjugates and in conferring nucleophilic reactivity
15        The members of the catalytic triad of ChEs, the three pairs of cysteine residues involved in i
16 e of the severe side effects that can plague ChE inhibitors, supporting metrifonate as a possible tre
17                              We suggest that ChEs achieve their remarkable catalytic power in ester h

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