期刊
JOURNAL OF MEDICINAL CHEMISTRY
卷 56, 期 2, 页码 547-555出版社
AMER CHEMICAL SOC
DOI: 10.1021/jm301583m
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资金
- British Heart Foundation
- Engineering and Physical Sciences Research Council (EPSRC)
- Wellcome Trust
- European Research Council (ERC)
- Open Horizons program of the Dinu Patriciu Foundation
- British Heart Foundation [PG/12/33/29546] Funding Source: researchfish
- EPSRC [EP/L003376/1] Funding Source: UKRI
The human 2-oxoglutarate (2OG) dependent oxygenases belong to a family of structurally related enzymes that play important roles in many biological processes. We report that competition-based NMR methods, using 2OG as a reporter ligand, can be used for quantitative and site-specific screening of ligand binding to 2OG oxygenases. The method was demonstrated using hypoxia inducible factor hydroxylases and histone demethylases, and K-D values were determined for inhibitors that compete with 2OG at the metal center. This technique is also useful as a screening or validation tool for inhibitor discovery, as exemplified by work with protein-directed dynamic combinatorial chemistry.
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