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Ubiquitin carboxyl-terminal hydrolase isozyme L3 (UCH-L3) is a deubiquitinating enzyme and thiol-dependent hydrolase.1,2,3,4 TCID is a tetrachloro indandione that acts as a potent inhibitor of UCH-L3 and demonstrates 125-fold selectivity over UCH-L1 (IC50s = 0.6 and 75 µM, respectively).5
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1. Substrate profiling of deubiquitin hydrolases with a positional scanning library and mass spectrometry. Biochemistry 43(21), 6535-6544 (2004).
2. Ubiquitin dimers control the hydrolase activity of UCH-
3. Cleavage of the C-
4. Profiling ubiquitin linkage specificities of deubiquitinating enzymes with branched ubiquitin isopeptide probes. Chembiochem 13(10), 1416-1420 (2012).
5. Discovery of inhibitors that elucidate the role of UCH-