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http://dx.doi.org/10.5012/bkcs.2013.34.5.1425

Salinosporamides A and B Inhibit Proteasome Activity and Delay the Degradation of N-end Rule Model Substrates  

Shin, Seung Kyun (Department of Applied Chemistry, College of Applied Sciences, Kyung Hee University)
Bang, Dae In (Department of Applied Chemistry, College of Applied Sciences, Kyung Hee University)
Choi, Won Hoon (Department of Applied Chemistry, College of Applied Sciences, Kyung Hee University)
Kim, Seong-Hwan (Natural Products Research Institute, College of Pharmacy, Seoul National University)
Oh, Dong-Chan (Natural Products Research Institute, College of Pharmacy, Seoul National University)
Lee, Min Jae (Department of Applied Chemistry, College of Applied Sciences, Kyung Hee University)
Publication Information
Bulletin of the Korean Chemical Society / v.34, no.5, 2013 , pp. 1425-1428 More about this Journal
Abstract
The proteasome, which is highly evolutionarily conserved, is responsible for the degradation of most short-lived proteins in cells. Small-molecule inhibitors targeting the proteasome's degradative activity have been extensively developed as lead compounds for various human diseases. An exemplified molecule is bortezomib, which was approved by FDA in 2003 for the treatment of multiple myeloma. Here, using transiently and stably expressed N-end rule model substrates in mammalian cells, we evaluated and identified that salinosporamide A and salinosporamide B effectively inhibited the proteasomal degradation. Considering that a variety of proteasome substrates are implicated in the pathogenesis of many diseases, they have the potential to be clinically applicable as therapeutic agents.
Keywords
Degradation; Ubiquitin; Proteasome; Inhibitor; N-end rule;
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