The chemical class of ASB17 activators includes a range of compounds that indirectly influence the activity of ASB17, primarily through modulation of protein ubiquitination, degradation pathways, and cellular signaling. This group comprises various proteasome inhibitors like MG132, Bortezomib, Lactacystin, Velcade, and Epoxomicin. By impacting the ubiquitin-proteasome system, these inhibitors could alter the protein degradation pathways where ASB17 may be involved, thereby potentially influencing its function in ubiquitination processes.
Additionally, this class may encompass compounds that affect specific aspects of ubiquitination and protein stability, such as MLN4924, PYR-41, and IU1. These compounds, by targeting ubiquitin activation, neddylation processes, and deubiquitination mechanisms, respectively, offer indirect routes to modulate ASB17 activity. Furthermore, compounds like Nutlin-3 and Thalidomide, which influence ubiquitin ligase activity, and 17-AAG, an Hsp90 inhibitor, also contribute to this class by affecting protein stability and degradation pathways. Moreover, Chloroquine, an autophagy inhibitor, highlights the interconnected nature of cellular degradation pathways, including both the ubiquitin-proteasome system and autophagic processes.
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