Design and evaluation of 1,7-naphthyridones as novel KDM5 inhibitors
Copyright policy )Design and evaluation of 1,7-naphthyridones as novel KDM5 inhibitors
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).
- University of California, San Diego United States
- GENENTECH INC United States
Jumonji Domain-Containing Histone Demethylases, Nuclear Proteins, Crystallography, X-Ray, Madin Darby Canine Kidney Cells, Repressor Proteins, Structure-Activity Relationship, Dogs, Drug Design, Animals, Humans, Naphthyridines, Retinoblastoma-Binding Protein 2
Jumonji Domain-Containing Histone Demethylases, Nuclear Proteins, Crystallography, X-Ray, Madin Darby Canine Kidney Cells, Repressor Proteins, Structure-Activity Relationship, Dogs, Drug Design, Animals, Humans, Naphthyridines, Retinoblastoma-Binding Protein 2
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