USP9Y (Ubiquitin-specific peptidase 9, Y-linked) is part of the ubiquitin-specific proteases family, playing a role in the process of deubiquitination, which is critical for maintaining protein stability and function. Given the lack of direct chemical activators, attention is directed to compounds that influence the ubiquitin-proteasome system and related cellular processes, potentially modulating USP9Y activity indirectly.
Proteasome inhibitors like MG132, Bortezomib, and Epoxomicin may affect the cellular environment of protein degradation, potentially impacting USP9Y's role in this process. Broad-spectrum DUB inhibitors (e.g., PR-619) and specific inhibitors like LDN-57444 (UCH-L1 inhibitor) offer insights into the regulation of deubiquitination processes relevant to USP9Y. Compounds affecting the ubiquitination process itself, such as PYR-41 (an E1 inhibitor), and agents modulating protein degradation pathways, including Thalidomide and its analogs (Lenalidomide, Pomalidomide), provide alternative routes to influence USP9Y activity. Tyrosine kinase inhibitors like Nilotinib and Dasatinib may impact USP9Y indirectly through alterations in cell signaling pathways. Additionally, Rapamycin, as an mTOR inhibitor, represents another avenue for indirect modulation, given mTOR's central role in cellular metabolism and growth.
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