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Ubiquitin carboxyl-terminal hydrolase 24 is an enzymatic member of the deubiquitinase family involved in the removal of ubiquitin moieties from substrate proteins, thus regulating their stability, turnover, and fate. This enzyme is understood to play critical roles in cell survival and protein homeostasis, acting within the ubiquitin-proteasome system to maintain proper cellular function[7]. Like other UCH family members, its enzymatic activity may influence key biological processes such as cell proliferation, apoptosis, and response to cellular stress or damage[1][7]. Although direct pharmacological targeting is not well developed, modulation of this enzyme is of interest in cancer biology and potentially in neurodegenerative and other diseases linked to disturbed protein degradation.
Drugs targeting deubiquitinases usually act via: - Inhibition of catalytic activity affecting removal of ubiquitin from substrate proteins - Modulation of cell survival by altering ubiquitin-dependent protein degradation and signaling[7]
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