Ubiquitin specific protease 7 (USP7) is a member of the deubiquitinating enzyme class that contains 106 representatives in human cells. USP7 removes the post-translational tag ubiquitin from several protein targets 1.
USP7 best characterised role is the removal of ubiquitin from the oncogene MDM2 and thus regulating the tumour suppressor protein p53 2.
It has also been shown to deubiquitinate other substrates including N-MYC 3 and Histone H2B 4 as well several tumour promoters and immune modulators , highlighting strong disease linkages in oncology. It’s main attraction as a therapeutic target has been linked to the modulation of the p53-MDM2 axis but also in modulating the immune response 5.
Recently, breakthroughs have been made by Almac Discovery 6 7 and others 8 9 10 in the discovery of highly potent and selective USP7 inhibitors, providing powerful pharmacological tools for further USP7 biology exploration. The USP7 programme at Almac Discovery is progressing towards pre-clinical candidate nomination.
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