(Q73409107)

English

Molecular recognition by acetylcholinesterase at the peripheral anionic site: structure-activity relationships for inhibitions by aryl carbamates

scientific article published on 01 December 1999

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scholarly article

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3 November 2019

Molecular recognition by acetylcholinesterase at the peripheral anionic site: structure-activity relationships for inhibitions by aryl carbamates (English)

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3 November 2019

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G Lin

1

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3 November 2019

C Y Lai

2

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3 November 2019

W C Liao

3

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3 November 2019

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1 December 1999

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3 November 2019

Bioorganic & Medicinal Chemistry

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3 November 2019

7

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3 November 2019

12

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3 November 2019

2683-2689

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3 November 2019

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

1 reference

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

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The X-ray Structure of a Transition State Analog Complex Reveals the Molecular Origins of the Catalytic Power and Substrate Specificity of Acetylcholinesterase

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

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Biochemistry of Alzheimer's dementia

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Recording spectrophotometric method for determination of dissociation and phosphorylation constants for the inhibition of acetylcholinesterase by organophosphates in the presence of substrate

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Inhibition kinetics of acetylcholinesterase with fluoromethyl ketones

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Physostigmine: Improvement of Long-Term Memory Processes in Normal Humans

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Anticholinesterase activity of a new carbamate, heptylphysostigmine, in view of its use in patients with Alzheimer-type dementia.

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Total syntheses and anticholinesterase activities of (3aS)-N(8)-norphysostigmine, (3aS)-N(8)-norphenserine, their antipodal isomers, and other N(8)-substituted analogues

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Enantiomeric inhibitors of cholesterol esterase and acetylcholinesterase

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Differences in active site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase

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Oral tetrahydroaminoacridine in long-term treatment of senile dementia, Alzheimer type.

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Study of the substituent effect on alpha-chymotrypsin-catalyzed hydrolysis of phenyl acetates by using a stopped-flow titration method.

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Substituent Effects on Substrate Activation and Michaelis-Menten Kinetic Parameters in the α-Chymotrypsin-catalyzed Hydrolysis of Phenyl Acetates1

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

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Molecular Recognition by Cholesterol Esterase of Active Site Ligands: Structure−Reactivity Effects for Inhibition by Aryl Carbamates and Subsequent Carbamylenzyme Turnover†

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A new and rapid colorimetric determination of acetylcholinesterase activity

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Structure-reactivity probes for active site shapes of cholesterol esterase by carbamate inhibitors

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Structure-reactivity relationships for the inhibition mechanism at the second alkyl-chain-binding site of cholesterol esterase and lipase

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Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase

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Identifiers

10.1016/S0968-0896(99)00213-8

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10658572%20AND%20SRC:MED&resulttype=core&format=json

3 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:10658572%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

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