| Literature DB >> 23791076 |
Kiyoshi Okada1, Yue Qi Ye, Kayoko Taniguchi, Ayaka Yoshida, Tomonori Akiyama, Yasukiyo Yoshioka, Jun-ichi Onose, Hiroyuki Koshino, Shunya Takahashi, Arata Yajima, Naoki Abe, Shunsuke Yajima.
Abstract
Vialinin A, a small compound isolated from the Chinese mushroom Thelephora vialis, exhibits more effective anti-inflammatory activity than the widely used immunosuppressive drug tacrolimus (FK506). Here, we show that ubiquitin-specific peptidase 5/isopeptidase T (USP5/IsoT) is a target molecule of vialinin A, identified by using a beads-probe method. Vialinin A inhibited the peptidase activity of USP5/IsoT and also inhibited the enzymatic activities of USP4 among deubiquitinating enzymes tested. Although USPs are a member of thiol protease family, vialinin A exhibited no inhibitions for other thiol proteases, such as calpain and cathepsin.Entities:
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Year: 2013 PMID: 23791076 DOI: 10.1016/j.bmcl.2013.05.093
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN: 0960-894X Impact factor: 2.823