Fbxw13 Inhibitors

The class described as Fbxw13 Inhibitors consists of chemical compounds that interfere with the ubiquitin-proteasome system and related cellular functions, potentially affecting the activity of Fbxw13. While these compounds do not directly inhibit Fbxw13, their actions on the ubiquitin-proteasome system can alter the degradation of proteins that are targets of Fbxw13. Compounds like MG132, Bortezomib, Lactacystin, and Epoxomicin inhibit the proteasome's ability to degrade ubiquitinated proteins, potentially resulting in an indirect impact on Fbxw13's function by causing the accumulation of its substrates. PYR-41 and MLN4924 (Pevonedistat) inhibit enzymes that are crucial to the ubiquitination process itself, which can result in reduced ubiquitination of proteins associated with Fbxw13.

In addition, compounds such as Nutlin-3, Celastrol, and Thalidomide act on protein-protein interactions and stress responses that are upstream or parallel to the ubiquitination process. By modulating these interactions and responses, they can indirectly influence the turnover of proteins that Fbxw13 may target for ubiquitination and subsequent degradation. The use of these compounds provides insight into the mechanisms by which Fbxw13 regulates protein ubiquitination and stability, as well as the broader role of Fbxw13 within the cell.