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What makes a good drug target? Technology Networks has recently featured an article highlighting some of the challenges that the Huber Lab aims to tackle.

Dr Kilian V. M. Huber states,"A good drug target needs to be relevant to the disease phenotype and should be amenable to therapeutic modulation. At the same time, you need to have a good therapeutic window to assure that any therapeutic modality aimed at the target will not cause side effects by disrupting the physiological function of the target in healthy tissue."

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Sun Jung has joined the Huber Lab as a research assistant.

Our latest research published in Angewandte Chemie

Histone lysine demethylases (KDMs) are involved in the dynamic regulation of gene expression and they play a critical role in several biological processes. Achieving selectivity over the different KDMs has been a major challenge for KDM inhibitor development. Here we report potent and selective KDM5 covalent inhibitors designed to target cysteine residues only present in the KDM5 sub‐family. The covalent binding to the targeted proteins was confirmed by MS and time‐dependent inhibition. Additional competition assays show that compounds were non 2‐OG competitive. Target engagement and ChIP‐seq analysis showed that the compounds inhibited the KDM5 members in cells at nano‐ to micromolar levels and induce a global increase of the H3K4me3 mark at transcriptional start sites.

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