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1 nd peripheral site inhibitors (gallamine and fasciculin).
2 d with a K(S) of 0.4+/- 0.2 mM measured with fasciculin.
3 with its peptidic inhibitor, the neurotoxin fasciculin.
4 n of the AChE was resistant to inhibition by fasciculin.
5 anionic site ligands, such as propidium and fasciculin.
6 hat the dissociation of fluorescently-tagged fasciculin 2 (a specific and selective peptide inhibitor
9 The availability of a crystal structure of a fasciculin 2 (Fas2)-acetylcholinesterase complex affords
10 lation of the protein-protein complex, where fasciculin 2 appears to sterically block access of ligan
15 is of the relaxation times in the absence of fasciculin 2 gave estimates of the N-methylacridinium as
17 ased by more than 3 orders of magnitude when fasciculin 2 was bound, consistent with a pronounced ste
18 ium with AChE in the presence and absence of fasciculin 2 were measured by fluorescence temperature j
19 n, we synthesized a fluorescent conjugate of fasciculin 2, a snake alpha-neurotoxin that tightly bind
20 ral site where inhibitors like propidium and fasciculin 2, a snake neurotoxin, bind and interfere wit
21 one-time blockade of AChEs with fluorescent fasciculin 2, AChEs are removed from synapses initially
22 er, when AChEs are continuously blocked with fasciculin 2, the removal rate increases substantially (
26 formed by one of the apo forms of neurotoxin fasciculin-2 (FAS2) and its high-affinity binding protei
30 tors, measurements of phosphorylation of the fasciculin-AChE complex by AChE inactivation gave mislea
33 ns of the conformationally flexible proteins fasciculin and calmodulin, as well as the less flexible
34 sample transitions between the substates of fasciculin and calmodulin, GNEIMO simulations show the t
38 ]-4-methylcoumarin (EMPC) that resulted from fasciculin binding, decreased from 0.002 in wild-type hu
44 demonstrate that a fluorescently conjugated fasciculin can be used to monitor total, active, and OP-
46 GNEIMO with replica exchange to the study of fasciculin conformational dynamics produced sampling of
47 ecular dynamics trajectories of apo forms of fasciculin, corresponding to different conformational su
49 , and the peripheral site peptide inhibitor, fasciculin, had no effect on the anisotropy decay of flu
53 c obstruction seen in the crystal structure, fasciculin may inhibit acetylcholinesterase by combined
54 he 287 position, in a manner consistent with fasciculin reducing the segmental motion of the peptide
55 6H9, and 5E8 interfered with the binding of fasciculin to the complexed enzyme, suggesting that part
56 t, the binding of the polypeptide neurotoxin fasciculin to the peripheral site of AChE dramatically d
61 acity to influence the binding of a peptide, fasciculin, which inhibits catalysis peripherally by sea
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