Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complex
- 3 November 1995
- journal article
- research article
- Published by Elsevier BV in Cell
- Vol. 83 (3), 503-512
- https://doi.org/10.1016/0092-8674(95)90128-0
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Fasciculin 2 Binds to the Peripheral Site on Acetylcholinesterase and Inhibits Substrate Hydrolysis by Slowing a Step Involving Proton Transfer during Enzyme AcylationPublished by Elsevier BV ,1995
- 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
- Three-dimensional structures of neurotoxins and cardiotoxinsChemical Research in Toxicology, 1993
- Nuclear magnetic resonance solution structure of the α-neurotoxin from the black mamba (Dendroaspis polylepis polylepis)Journal of Molecular Biology, 1992
- A visual protein crystallographic software system for X11/XviewJournal of Molecular Graphics, 1992
- Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptorNeuron, 1989
- Surface, subunit interfaces and interior of oligomeric proteinsJournal of Molecular Biology, 1988
- Toxins from the venom of the green mamba Dendroaspis angusticeps that inhibit the binding of quinuclidinyl benzilate to muscarinic acetylcholine receptorsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1988
- Solvent content of protein crystalsJournal of Molecular Biology, 1968