IndraLab

Statements

Vialinin A inhibits USP4. 5 / 5
| 5
reach
"As shown in Figure 4 , treatment with vialinin A reduced the activity of USP4 (IC 50 = 1.5 μM) and UCH-L1 (IC 50 = 22.3 μM), but no significant inhibition was observed in terms of the UCH-L3, USP2, an[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
23791076
reach
"Although USP4 and UCH-L1 were inhibited by vialinin A, the binding affinities to the biotin-DMT probe were different from that of USP5, where USP4 bound the probe more weakly and UCH-L1 did not bind t[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
23791076
reach
"17–20,29 In the present study, we demonstrated that vialinin A, whose structure is different from those of compounds previously reported, strongly inhibited the enzymatic activities of USP5 and USP4."
23791076
reach
"Notably, vialinin A is an inhibitor of ubiquitin-specific peptidase 4 (USP4) that shows anti-inflammatory and antioxidative properties."
38176274
reach
"Mechanistically, vialinin A inhibited the deubiquitinating enzymatic activity of USP4, leading to enhanced ubiquitination of Keap1 and subsequently promoting its degradation."
38176274