The chemical class TRIM80 Inhibitors refers to a diverse group of compounds that indirectly influence the function of TRIM80 by targeting the ubiquitin-proteasome system (UPS) and related cellular processes. These inhibitors typically function by impeding the proteasome's ability to degrade ubiquitinated proteins, leading to an accumulation of these proteins within the cell. This accumulation can have various downstream effects on cellular processes, including those where TRIM80 is presumed to be active.
The compounds in this class include proteasome inhibitors like MG132, Bortezomib, Lactacystin, Withaferin A, Celastrol, Epoxomicin, Velcade, Carfilzomib, Oprozomib, and MLN2238, each of which binds to and inhibits the proteolytic activity of the proteasome. This inhibition can subsequently impact any regulatory roles that TRIM80 has in protein turnover or degradation. Additionally, compounds like Nelfinavir and Disulfiram, although initially developed for other purposes, have been found to have off-target effects on the proteasome, thereby potentially modulating the functional landscape in which TRIM80 operates. By affecting the UPS, these inhibitors can indirectly influence the ubiquitination and subsequent proteasomal degradation of proteins, which is a critical pathway in cellular homeostasis and one in which TRIM80 may have a role.
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