Role of ionic interactions in cholinesterase catalysis. (Q41249133)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8948485 AND SRC:MED&resulttype=core&format=json

21 October 2019

review article

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title

Role of ionic interactions in cholinesterase catalysis (English)

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21 October 2019

author name string

V Tõugu

series ordinal

1

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21 October 2019

T Kesvatera

series ordinal

2

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21 October 2019

publication date

1 November 1996

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Biochimica et Biophysica Acta

21 October 2019

published in

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8948485 AND SRC:MED&resulttype=core&format=json

21 October 2019

volume

1298

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21 October 2019

issue

1

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21 October 2019

page(s)

12-30

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Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states

21 October 2019

cites work

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

The cholinesterases: from genes to proteins

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands.

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Acetylcholinesterase: electrostatic steering increases the rate of ligand binding.

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Acetylcholinesterase as polyelectrolyte in reaction with cationic substrates.

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Open "back door" in a molecular dynamics simulation of acetylcholinesterase.

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Molecular and cellular biology of cholinesterases

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Differentiation of 3 types of competitive cholinesterase inhibitors

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

The structure of the active surface of serum cholinesterase

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Ligand binding properties of acetylcholinesterase determined with fluorescent probes.

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Kinetic, equilibrium and spectroscopic studies on cation association at the active center of acetylcholinesterase: topographic distinction between trimethyl and trimethylammonium sites

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

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 conduction

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Site-directed mutagenesis of active-site-related residues in Torpedo acetylcholinesterase Presence of a glutamic acid in the catalytic triad

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Excavations into the active-site gorge of cholinesterases

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Asp7O in the peripheral anionic site of human butyrylcholinesterase

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Expression of recombinant acetylcholinesterase in a baculovirus system: kinetic properties of glutamate 199 mutants

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Residues important for folding and dimerisation of recombinant Torpedo californica acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Simulation of charge-mutant acetylcholinesterases

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Acetylcholinesterase as polyelectrolyte: interaction with multivalent cationic inhibitors.

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Inorganic ion effects on the kinetic parameters of acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Acetylcholinesterase: evidence that sodium ion binding at the anionic site causes inhibition of the second-order hydrolysis of acetylcholine and a decrease of its pKa as well as of deacetylation

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Tailoring the pH dependence of enzyme catalysis using protein engineering

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Energetics of charge-charge interactions in proteins.

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

The role of arginine 143 in the electrostatics and mechanism of Cu,Zn superoxide dismutase: computational and experimental evaluation by mutational analysis

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Binding of Ca2 to calbindin D9k: structural stability and function at high salt concentration

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

SOME EFFECTS OF SALTS ON TRUE CHOLINESTERASE

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

The ionic strength dependence of the rate of a reaction between a small ion and a large ion with a dipole moment

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Limiting Laws and Counterion Condensation in Polyelectrolyte Solutions I. Colligative Properties

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Ion effects on ligand-nucleic acid interactions

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

pH-dependent salting-out effect in enzyme-catalyzed reaction kinetics.

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Ligand exclusion on acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Structure-activity relationships in acetylcholinesterase reactions. Hydrolysis of non-ionic acetic esters

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Effects of volume and surface property in hydrolysis by acetylcholinesterase. The trimethyl site

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Molecular recognition in acetylcholinesterase catalysis: free-energy correlations for substrate turnover and inhibition by trifluoro ketone transition-state analogs

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

On the relationship between structure and reactivity of alpha-chymotrypsin substrates

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Catalytic properties of serine proteases. 2. Comparison between human urinary kallikrein and human urokinase, bovine beta-trypsin, bovine thrombin, and bovine alpha-chymotrypsin

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Thermolysin: Kinetic Study with Oligopeptides

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Hydrophobic interaction in thermolysin specificity

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

On the specificity of tryptic catalysis

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Structural basis of the activation and action of trypsin

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

The structure of bovine trypsin : Electron density maps of the inhibited enzyme at 5 Å and at 2·7 Å resolution

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6 Å resolution

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Relocating a negative charge in the binding pocket of trypsin

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Structural and functional integrity of specificity and catalytic sites of trypsin.

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Acetylcholine binding by a synthetic receptor: implications for biological recognition

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Hydrophobic Effects. Opinions and Facts

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Atom/fragment contribution method for estimating octanol-water partition coefficients.

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

A comparative molecular field analysis study of N-benzylpiperidines as acetylcholinesterase inhibitors

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Kinetics of acetylthiocholine binding to electric eel acetylcholinesterase in glycerol/water solvents of increased viscosity. Evidence for a diffusion-controlled reaction

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Interaction of ligands with acetylcholinesterase. Use of temperature-jump relaxation kinetics in the binding of specific fluorescent ligands

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Catalysis by acetylcholinesterase in two-hydronic-reactive states. Integrity of deuterium oxide effects and hydron inventories

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Acetylcholinesterase: diffusional encounter rate constants for dumbbell models of ligand

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Trp279 is involved in the binding of quaternary ammonium at the peripheral site of Torpedo marmorata acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Docking analysis of a series of benzylamino acetylcholinesterase inhibitors with a phthalimide, benzoyl, or indanone moiety

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Acetylcholinesterase: theory of noncompetitive inhibition.

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Efficient product clearance through exit channels in substrate hydrolysis by acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function.

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016/S0167-4838(96)00128-8

7 January 2021

10.1016/S0167-4838(96)00128-8

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21 October 2019

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