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Backdoor opening mechanism in acetylcholinesterase based on X-ray crystallography and molecular dynamics simulations. Protein Science, 20, 1114–1118
DOI: 10.1002/pro.661
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Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase. Acta Crystallographica, Section D, Biological crystallography, 58(10/2), 1765–1771
DOI: 10.1107/S0907444902011642
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X-ray structures of Torpedo californica acetylcholinesterase complexed with (+)-huperzine A and (-)-huperzine B: structural evidence for an active site rearrangement. Biochemistry, 41(35), 10810–10818
DOI: 10.1021/bi020151+
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3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates. Biochemistry, 41(9), 2970–2981
DOI: 10.1021/bi011652i
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A neutral molecule in a cation-binding site: specific binding of a PEG-SH to acetylcholinesterase from Torpedo californica. Journal of Molecular Biology, 320(4), 721–725
DOI: 10.1016/S0022-2836(02)00475-8
Histochemical method for characterization of enzyme crystals: application to crystals of Torpedo californica acetylcholinesterase. Acta Crystallographica, Section D, Biological crystallography, 57(9), 1348–1350
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Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo californica. Journal of Molecular Biology, 296(2), 713–735
DOI: 10.1006/jmbi.1999.3468