Crystal structure of an acetylcholinesterase–fasciculin complex: interaction of a three-fingered toxin from snake venom with its target
Open Access
- 1 December 1995
- Vol. 3 (12) , 1355-1366
- https://doi.org/10.1016/s0969-2126(01)00273-8
Abstract
No abstract availableKeywords
This publication has 63 references indexed in Scilit:
- Efficient Rebuilding of Protein StructuresActa Crystallographica Section D-Biological Crystallography, 1996
- Fasciculin 2 Binds to the Peripheral Site on Acetylcholinesterase and Inhibits Substrate Hydrolysis by Slowing a Step Involving Proton Transfer during Enzyme AcylationJournal of Biological Chemistry, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Open "Back Door" in a Molecular Dynamics Simulation of AcetylcholinesteraseScience, 1994
- Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitorsBiochemistry, 1993
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- Slow-cooling protocols for crystallographic refinement by simulated annealingActa Crystallographica Section A Foundations of Crystallography, 1990
- Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition statesChemical Reviews, 1987
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- The inhibitory effect of stilbamidine, curare and related compounds and its relationship to the active groups of acetylcholine esterase. Action of stilbamidine upon nerve impulse conductionBiochimica et Biophysica Acta, 1950