Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target (Q27733273)

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18 October 2019

title

Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target (English)

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18 October 2019

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2

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18 October 2019

Raimond Ravelli

3

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18 October 2019

author name string

M Harel

1

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18 October 2019

I Silman

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18 October 2019

J L Sussman

5

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18 October 2019

publication date

1 December 1995

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18 October 2019

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18 October 2019

volume

3

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18 October 2019

issue

12

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18 October 2019

page(s)

1355-1366

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Further studies on the binding properties of cobra neurotoxin to cholinergic receptors in mouse skeletal muscle

18 October 2019

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NMR and restrained molecular dynamics study of the three-dimensional solution structure of toxin FS2, a specific blocker of the L-type calcium channel, isolated from black mamba venom

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Atomic Structure of Acetylcholinesterase from Torpedo californica : A Prototypic Acetylcholine-Binding Protein

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An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase

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Study of structure-activity relationship of fasciculin by acetylation of amino groups.

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Fasciculin 2 Binds to the Peripheral Site on Acetylcholinesterase and Inhibits Substrate Hydrolysis by Slowing a Step Involving Proton Transfer during Enzyme Acylation

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Allosteric Control of Acetylcholinesterase Catalysis by Fasciculin

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Role of arginine residues for the activity of fasciculin

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Fasciculin inhibition of acetylcholinesterase is prevented by chemical modification of the enzyme at a peripheral site

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Theoretical analysis of the structure of the peptide fasciculin and its docking to acetylcholinesterase

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Structure and dynamics of the active site gorge of acetylcholinesterase: synergistic use of molecular dynamics simulation and X-ray crystallography

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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors

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The Ace locus of Drosophila melanogaster: structural gene for acetylcholinesterase with an unusual 5' leader.

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Acetylcholinesterase: electrostatic steering increases the rate of ligand binding.

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Identifiers

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Consolidated OpenCitations Corpus – April 2017

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18 October 2019

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017