| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1369428 | Bioorganic & Medicinal Chemistry Letters | 2016 | 5 Pages |
Abstract
Features from a high throughput screening (HTS) hit and a previously reported scaffold were combined to generate 1,7-naphthyridones as novel KDM5 enzyme inhibitors with nanomolar potencies. These molecules exhibited high selectivity over the related KDM4C and KDM2B isoforms. An X-ray co-crystal structure of a representative molecule bound to KDM5A showed that these inhibitors are competitive with the co-substrate (2-oxoglutarate or 2-OG).
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Sharada S. Labadie, Peter S. Dragovich, Richard T. Cummings, Gauri Deshmukh, Amy Gustafson, Ning Han, Jean-Christophe Harmange, James R. Kiefer, Yue Li, Jun Liang, Bianca M. Liederer, Yichin Liu, Wanda Manieri, Wiefeng Mao, Lesley Murray,