TRIM61 Inhibitors

Lactacystin is a specific inhibitor of the proteasomal beta subunits. By inhibiting these subunits, lactacystin prevents the degradation of polyubiquitinated proteins, which would otherwise be mediated by E3 ubiquitin ligases like TRIM61. This leads to a functional inhibition of TRIM61 by blocking the downstream effects of its E3 ligase activity.

MG-132 is a potent, reversible proteasome inhibitor that can prevent the degradation of ubiquitin-conjugated proteins. As TRIM61 is involved in tagging proteins with ubiquitin for proteasomal degradation, MG-132's inhibition of the proteasome indirectly inhibits the functional role of TRIM61 by disrupting the proteolytic pathway it utilizes.

Epoxomicin is a selective proteasome inhibitor that covalently binds to and inhibits the chymotrypsin-like activity of the proteasome. By doing so, epoxomicin prevents the degradation of proteins that TRIM61 marks for destruction, indirectly inhibiting TRIM61's function in the protein degradation process.

Bortezomib is a dipeptide boronic acid analog that inhibits the 26S proteasome. By inhibiting the proteasome, bortezomib impairs the degradation of proteins ubiquitinated by E3 ubiquitin ligases like TRIM61, thus indirectly inhibiting the functional role of TRIM61 by disrupting its role in targeting proteins for degradation.

Carfilzomib is a proteasome inhibitor that irreversibly binds to and inhibits the proteasome's chymotrypsin-like site. Inhibition of the proteasome by carfilzomib results in the accumulation of proteins that TRIM61 would target for ubiquitination and subsequent degradation, thereby functionally inhibiting TRIM61's role in protein homeostasis.

Oprozomib is an orally bioavailable proteasome inhibitor that targets and inhibits the enzymatic activity of the proteasome. Through its action, oprozomib causes an accumulation of proteins targeted for degradation by TRIM61, thus functionally inhibiting TRIM61 by blocking the proteolytic pathway essential for its activity.

Nelfinavir is a drug known for its protease inhibitory action, but it also displays off-target effects including the inhibition of the proteasome. By inhibiting the proteasome, nelfinavir can lead to the accumulation of ubiquitinated proteins, which are substrates of E3 ligases like TRIM61. This results in the functional inhibition of TRIM61 by impeding the degradation pathway it depends on.

Withaferin A has been shown to inhibit the proteasomal activity, thereby leading to the accumulation of ubiquitinated proteins. Since TRIM61's function involves ubiquitin-mediated protein degradation, the action of withaferin A can functionally inhibit TRIM61 by preventing the degradation of its substrates, thus interrupting TRIM61's role in the ubiquitin-proteasome pathway.

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