Entamoeba histolytica: identification of thioredoxin-targeted proteins and analysis of serine acetyltransferase-1 as a prototype example.

doi:10.1042/BJ20121798

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Entamoeba histolytica: identification of thioredoxin-targeted proteins and analysis of serine acetyltransferase-1 as a prototype example.

The Biochemical journal - 15 Apr 2013

Schlosser Sarah, Leitsch David, Duchêne Michael

Abstract excerpt

Entamoeba histolytica, the causative agent of amoebiasis, possesses the dithiol-containing redox proteins Trx (thioredoxin) and TrxR (Trx reductase). Both proteins were found to be covalently modified and inactivated by metronidazole, a 5-nitroimidazole drug that is commonly used to treat infections with microaerophilic protozoan parasites in humans. Currently, very little is known about enzymes and other...

Topics

Antiprotozoal Agents
Blotting, Western
Catalytic Domain
Chromatography, Affinity
Disulfides
Electrophoresis, Gel, Two-Dimensional
Entamoeba histolytica
Mass Spectrometry
Metronidazole
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Oxidation-Reduction

Oxidative Stress

Peroxiredoxins

Protozoan Proteins

Serine O-Acetyltransferase

Thioredoxin-Disulfide Reductase

Thioredoxins

Source

Open in PubMed

Identifiers

PMID: 23398389
DOI: 10.1042/BJ20121798

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