Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Acetylcholinesterase: converting a vulnerable target to a template for antidotes and detection of inhibitor exposure.

Toxicology - 20 Apr 2007

Taylor Palmer, Kovarik Zrinka, Reiner Elsa, Radić Zoran

Abstract excerpt

Applications of recombinant DNA technology, chemical synthesis on biological templates and fluorescence detection of organophosphorylation provide unexplored avenues for development of antidotes and approaches for remote detection of organophosphate nerve agents and pesticides. We discuss here how acetylcholinesterase (AChE), through appropriate mutations, becomes more susceptible to oxime reactivation. Since the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acetylcholinesterase
Share to Binding, Competitive
Share to Cholinesterase Inhibitors

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Drug Design

Share to Hydrolysis

Share to Organophosphorus Compounds

Share to Oximes

Share to Spectrometry, Fluorescence

Source

Open in PubMed Open full text

Identifiers

PMID: 17196318
DOI: 10.1016/j.tox.2006.11.061
PMCID: PMC3279330

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Acetylcholinesterase: converting a vulnerable target to a template for antidotes and detection of inhibitor exposure.PMID 17196318Read ↗

Mutant acetylcholinesterases as potential detoxification agents for organophosphate poisoning.Semantic proximity Read ↗

Direct detection of the hydrolysis of nerve agent model compounds using a fluorescent probe.Semantic proximity Read ↗

Successive organophosphate inhibition and oxime reactivation reveals distinct responses of recombinant human cholinesterase variants.Semantic proximity Read ↗

Organophosphate hydrolases as catalytic bioscavengers of organophosphorus nerve agents.Semantic proximity Read ↗

Mutation of acetylcholinesterase to enhance oxime-assisted catalytic turnover of methylphosphonates.Semantic proximity Read ↗

Acetylcholinesterase mutants: oxime-assisted catalytic scavengers of organophosphonates.Semantic proximity Read ↗

Investigating the structural influence of surface mutations on acetylcholinesterase inhibition by organophosphorus compounds and oxime reactivation.Semantic proximity Read ↗

Identification of human butyrylcholinesterase organophosphate-resistant variants through a novel mammalian enzyme functional screen.Semantic proximity Read ↗

A rationally designed mutant of plasma platelet-activating factor acetylhydrolase hydrolyzes the organophosphorus nerve agent soman.Semantic proximity Read ↗

Inhibitors tethered near the acetylcholinesterase active site serve as molecular rulers of the peripheral and acylation sites.Semantic proximity Read ↗

Drosophila melanogaster as a model organism for screening acetylcholinesterase reactivatorsSemantic proximity Read ↗

Nerve agent hydrolysis activity designed into a human drug metabolism enzyme.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.