USP Inhibitors

Ubiquitin-specific peptidase (USP) family inhibitors are compounds or molecules designed to block or reduce the activity of specific deubiquitinase enzymes within the numerous members of the USP family. Deubiquitinases are enzymes that remove ubiquitin molecules from proteins, thus regulating the ubiquitin-proteasome system, which is critical for protein degradation and various cellular processes. USPs play important roles in controlling protein stability, cell signaling, DNA repair, and immune responses. By inhibiting the activity of USP enzymes, these inhibitors interfere with the removal of ubiquitin from targeted proteins, leading to altered protein turnover and affecting cellular processes regulated by ubiquitination. USP inhibitors have potential implications in cancer therapy, as many USPs are overexpressed or dysregulated in cancer cells, leading to abnormal protein degradation and cell signaling. Moreover, USP inhibitors have shown promise in modulating immune responses, neurodegenerative diseases, and other conditions where protein homeostasis is disrupted.