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UCHL1 inhibits Proteasome. 6 / 7
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"Reichelt et al. [29] found that non-functional UCH-L1 impairs the proteasome and drives podocyte injury in mice with membranous nephropathy."
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"On the other hand, UCH-L1 could be a part of the feedback mechanism to decrease in poly-ubiquitinated proteins and impaired the proteasome activity."
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"Only non-functional UCH-L1 inhibits proteasome activity, especially of the 20S proteasome and its β1c and β5c subunits, potentially by binding to α subunits and thus preventing unhindered access of substrates to the α-ring pore."
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"These results suggest that the promotion of UCHL1 on decidualization and modulation of dNKs by DSCs is dependent on the activation of JAK2/STAT3 signaling.UCHL1 is a deubiquitinating enzyme, and as its name implies, the function of UCHL1 relies on its C-terminal hydrolase to remove ubiquitin from proteins and thus inhibit protein degradation via the proteasome [35]."
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"Although the overexpression of UCH-L1 inhibits proteasome activity in cultured cells, its biological significance in living organisms has not been clarified in detail."
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"Utilizing gracile axonal dystrophy (gad) mice and derived cell lines, that fail to express UCHL1 [92] could facilitate characterization of off-target effects of UCHL1 inhibitors.Inhibitors of two prot[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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