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

Investigation of evolved paraoxonase-1 variants for prevention of organophosphorous pesticide compound intoxication.

The Journal of pharmacology and experimental therapeutics - 1 Jun 2014

Mata David G, Rezk Peter E, Sabnekar Praveena, Cerasoli Douglas M, Chilukuri Nageswararao

Abstract excerpt

We investigated the ability of the engineered paraoxonase-1 variants G3C9, VII-D11, I-F11, and VII-D2 to afford protection against paraoxon intoxication. Paraoxon is the toxic metabolite of parathion, a common pesticide still in use in many developing countries. An in vitro investigation showed that VII-D11 is the most efficient variant at hydrolyzing paraoxon with a kcat/Km of 2.1 × 10(6) M(-1) min(-1) and 1.6 ×...

Read the complete abstract on PubMed

Topics

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

Share to Adenoviridae
Share to Aryldialkylphosphatase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Biocatalysis

Share to Gene Transfer Techniques

Share to Genetic Vectors

Share to Lethal Dose 50

Share to Pesticides

Share to Protein Engineering

Source

Identifiers

PMID: 24706983
DOI: 10.1124/jpet.114.213645

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Investigation of evolved paraoxonase-1 variants for prevention of organophosphorous pesticide compound intoxication.PMID 24706983Read ↗

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

Catalytic efficiencies of directly evolved phosphotriesterase variants with structurally different organophosphorus compounds in vitro.Semantic proximity Read ↗

Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides.Semantic proximity Read ↗

Evolved stereoselective hydrolases for broad-spectrum G-type nerve agent detoxification.Semantic proximity Read ↗

Towards Understanding the Catalytic Mechanism of Human Paraoxonase 1: Experimental and In Silico Mutagenesis Studies.Semantic proximity Read ↗

Dramatic differences in organophosphorus hydrolase activity between human and chimeric recombinant mammalian paraoxonase-1 enzymes.Semantic proximity Read ↗

Rational design of organophosphorus hydrolase with high catalytic efficiency for detoxifying a V-type nerve agent.Semantic proximity Read ↗

Paraoxonases-1, -2 and -3: What are their functions?Semantic proximity Read ↗

Paraoxonase 1 status as a risk factor for disease or exposure.Semantic proximity Read ↗

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

A catalytic bioscavenger with improved stability and reduced susceptibility to oxidation for treatment of acute poisoning with neurotoxic organophosphorus compounds.Semantic proximity Read ↗

Variants of Phosphotriesterase for the Enhanced Detoxification of the Chemical Warfare Agent VR.Semantic proximity Read ↗

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