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Development of LC/MS/MS, high-throughput enzymatic and cellular assays for the characterization of compounds that inhibit kynurenine monooxygenase (KMO).

Authors: Winkler, Dirk  Beconi, Maria  Toledo-Sherman, Leticia M  Prime, Michael  Ebneth, Andreas  Dominguez, Celia  Muñoz-Sanjuan, Ignacio 
Citation: Winkler D, etal., J Biomol Screen. 2013 Sep;18(8):879-89. doi: 10.1177/1087057113489731. Epub 2013 May 20.
Pubmed: (View Article at PubMed) PMID:23690293
DOI: Full-text: DOI:10.1177/1087057113489731

Kynurenine monooxygenase (KMO) catalyzes the conversion of kynurenine to 3-hydroxykynurenine. Modulation of KMO activity has been implicated in several neurodegenerative diseases, including Huntington disease. Our goal is to develop potent and selective small-molecule KMO inhibitors with suitable pharmacokinetic characteristics for in vivo proof-of-concept studies and subsequent clinical development. We developed a comprehensive panel of biochemical and cell-based assays that use liquid chromatography/tandem mass spectrometry to quantify unlabeled kynurenine and 3-hydroxykynurenine. We describe assays to measure KMO inhibition in cell and tissue extracts, as well as cellular assays including heterologous cell lines and primary rat microglia and human peripheral blood mononuclear cells.


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CRRD Object Information
CRRD ID: 13513904
Created: 2018-03-08
Species: All species
Last Modified: 2018-03-08
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.