期刊
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 26, 期 18, 页码 4492-4496出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2016.07.070
关键词
Histone lysine demethylases; KDM5 inhibitors; Epigenetics
资金
- U.S. Department of Energy, Office of Science, and Office of Basic Energy Sciences [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research
- National Institutes of Health, National Institute of General Medical Sciences [P41GM103393]
- Discovery Chemistry Small Molecule analytical group
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). (c) 2016 Elsevier Ltd. All rights reserved.
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