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Ubiquitin carboxyl-terminal hydrolase 11 (USP11) is an enzyme encoded by the USP11 gene in humans and is a member of the largest subfamily of deubiquitinating enzymes (DUBs), specifically the ubiquitin-specific proteases (USPs). USP11 mediates the removal of ubiquitin from protein targets, reversing ubiquitin-mediated protein degradation and modulating diverse cellular processes such as DNA repair, cell cycle regulation, apoptosis, transcription, and signal transduction. It consists of distinct structural domains, including a DUSP domain and multiple ubiquitin-like (UBL) domains, conferring substrate recognition and regulatory capacity. USP11 plays a dual role in tumor biology, participating both in DNA repair and cellular stress responses, which makes it a potential—but complex—therapeutic target in oncology and other diseases linked to genomic instability or dysregulated proteostasis.
Drugs or molecular agents targeting USP11 would act as enzyme inhibitors or activators, affecting the deubiquitination of substrate proteins, altering cellular protein stability and signaling
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