IndraLab

Statements


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"For elderly patients with dysregulated protein homeostasis, high levels of UCHL5 inhibited proteasome activity, and were determined to promote the apoptosis of cancer cells (28)."

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"UCH-L5 can suppress proteasome mediated degradation via the disassembly of distal polyubiquitin moieties."

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"Uch37/UCHL5 appears to be reversibly associates with the proteasome ( Hamazaki et al., 2006; Jorgensen et al., 2006; Qiu et al., 2006; Yao et al., 2006 )."

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"Possibly, Uch37 functions to orchestrate such ordering of degradation rates.The third deubiquitinating enzyme, Ubp6, also appears to inhibit proteasome-mediated degradation [53] ."

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"In particular, deubiquitinating enzymes Uch37 and Usp14, being physically associated with the proteasome, may suppress proteasome activity through deubiquitinating a subset of ubiquitinated substrates, once the substrate is docked at the proteasome."

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"It is possible that excess UCHL5 expression substantially impairs proteasome activity, causing abnormal accumulation of proteasomal substrates, and harming tumor cells."

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"For elderly patients with reduced proteostasis capacity, high UCHL5 levels may further inhibit proteasome activity, thereby promoting apoptosis in cancer cells."