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Updated: Mar 16, 2026

Direct Measurement of KDM1A Target Engagement Using Chemoprobe-based Immunoassays
Published on: June 13, 2019
Design and evaluation of 1,7-naphthyridones as novel KDM5 inhibitors
Sharada S Labadie1, Peter S Dragovich1, Richard T Cummings2
1Genentech Inc., 1 DNA Way, South San Francisco, CA 94080, USA.
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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