(Q74615783)

English

Electron paramagnetic resonance reveals altered topography of the active center gorge of acetylcholinesterase after binding of fasciculin to the peripheral site

scientific article published on 01 March 1999

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scholarly article

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12 November 2019

Electron paramagnetic resonance reveals altered topography of the active center gorge of acetylcholinesterase after binding of fasciculin to the peripheral site (English)

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12 November 2019

Pascale Marchot

4

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12 November 2019

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M Sentjurc

1

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12 November 2019

S Pecar

2

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12 November 2019

J Stojan

3

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12 November 2019

Z Radić

5

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12 November 2019

Z Grubic

6

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12 November 2019

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1 March 1999

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12 November 2019

Biochimica et Biophysica Acta

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12 November 2019

1430

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12 November 2019

2

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12 November 2019

349-358

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12 November 2019

Molecular and cellular biology of cholinesterases

1 reference

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The cholinesterases: from genes to proteins

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Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence

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

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From molecular structure to Alzheimer therapy

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Interaction of fluorescence probes with acetylcholinesterase. Site and specificity of propidium binding

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Excavations into the active-site gorge of cholinesterases

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

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Studies on the Topography of the Catalytic Site of Acetylcholinesterase Using Polyclonal and Monoclonal Antibodies

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Differences in conformational stability between native and phosphorylated acetylcholinesterase as evidenced by a monoclonal antibody

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7 January 2021

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Different effects of two peripheral anionic site-binding ligands on acetylcholinesterase active-site gorge topography revealed by electron paramagnetic resonance

1 reference

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7 January 2021

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Cloning and expression of acetylcholinesterase from Bungarus fasciatus venom. A new type of cooh-terminal domain; involvement of a positively charged residue in the peripheral site

1 reference

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7 January 2021

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Binding of the neurotoxin fasciculin 2 to the acetylcholinesterase peripheral site drastically reduces the association and dissociation rate constants for N-methylacridinium binding to the active site

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7 January 2021

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Nonequilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands

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7 January 2021

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

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7 January 2021

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Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin

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7 January 2021

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Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite.

1 reference

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7 January 2021

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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

1 reference

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7 January 2021

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Allosteric control of acetylcholinesterase catalysis by fasciculin

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7 January 2021

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Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex

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An ESR study of the influence of some physico-chemical factors on the conformation of a postsynaptic acetylcholinesterase

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On the location of active serines of membrane acetylcholinesterase studied by the ESR method

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Amino acid residues controlling reactivation of organophosphonyl conjugates of acetylcholinesterase by mono- and bisquaternary oximes

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Soluble monomeric acetylcholinesterase from mouse: expression, purification, and crystallization in complex with fasciculin.

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A new and rapid colorimetric determination of acetylcholinesterase activity

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Simultaneous analysis for testing of models and parameter estimation

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Regression analysis of nonlinear Arrhenius plots: an empirical model and a computer program

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Secondary structure and temperature behaviour of acetylcholinesterase. Studies by Fourier-transform infrared spectroscopy.

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Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates

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Identifiers

10.1016/S0167-4838(99)00018-7

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10082962%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10082962%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

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