Detoxication of Anticholinesterase Pesticides - Wikidata - awgldk - TriplyDB

Detoxication of Anticholinesterase Pesticides

Detoxication of Anticholinesterase Pesticides

http://www.wikidata.org/entity/Q57201890

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Contribution of carboxylesterase and cytochrome P450 to the bioactivation and detoxification of isocarbophos and its enantiomers in human liver microsomes.

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Detoxication of Anticholinesterase Pesticides

http://www.wikidata.org/entity/Q57201890

description

wetenschappelijk artikel

@nl

наукова стаття, опублікована в березні 2011

@uk

name

Detoxication of Anticholinesterase Pesticides

@en

Detoxication of Anticholinesterase Pesticides

@nl

type

label

Detoxication of Anticholinesterase Pesticides

@en

Detoxication of Anticholinesterase Pesticides

@nl

prefLabel

Detoxication of Anticholinesterase Pesticides

@en

Detoxication of Anticholinesterase Pesticides

@nl

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Q57201890-E9C78AAA-6B32-4CCD-AA2D-E9533BCAD788

P356

9780470640500.CH10

P1476

Detoxication of Anticholinesterase Pesticides

@en

P2093

Eugenio Vilanova

http://www.w3.org/2001/XMLSchema#string

Miguel A. Sogorb

http://www.w3.org/2001/XMLSchema#string

P2860

In vitro metabolism of carbofuran by human, mouse, and rat cytochrome P450 and interactions with chlorpyrifos, testosterone, and estradiol

In vitro sulfoxidation of thioether compounds by human cytochrome P450 and flavin-containing monooxygenase isoforms with particular reference to the CYP2C subfamily

In vitro rat hepatic and intestinal metabolism of the organophosphate pesticides chlorpyrifos and diazinon

Toxicity of chlorpyrifos and chlorpyrifos oxon in a transgenic mouse model of the human paraoxonase (PON1) Q192R polymorphism

Structural basis for natural lactonase and promiscuous phosphotriesterase activities

Biodegradation of carbaryl by a Micrococcus species

Role of paraoxonase (PON1) status in pesticide sensitivity: genetic and temporal determinants

Mice lacking serum paraoxonase are susceptible to organophosphate toxicity and atherosclerosis

Structural determinants of the substrate and stereochemical specificity of phosphotriesterase.

Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues.

P304

121-132

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P31

scholarly article

P356

10.1002/9780470640500.CH10

http://www.w3.org/2001/XMLSchema#string

P577

2011-03-28T00:00:00Z

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