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Structural and functional characterization of ubiquitin variant inhibitors for the JAMM-family deubiquitinases STAMBP and STAMBPL1

Yusong Guo, Qi Liu, Evan Mallette, Cody Caba, Feng Hou, Julia Fux, Gabriel LaPlante, Aiping Dong, Qi Zhang, Hui Zheng, Yufeng Tong, Wei Zhang

2021Journal of Biological Chemistry21 citationsDOIOpen Access PDF

Abstract

are potent inhibitors of STAMBP isopeptidase activity, far exceeding the reported small-molecule inhibitor BC-1471. This work demonstrates that UbV technology is suitable to develop molecules as tools to target metalloproteases, which can be used to further understand the cellular function of JAMM family DUBs.

Topics & Concepts

Deubiquitinating enzymeUbiquitinProteasesDrug discoveryCysteine proteaseComputational biologyProteaseSmall moleculeBiologyBiochemistryEnzymeChemistryGeneUbiquitin and proteasome pathwaysPeptidase Inhibition and AnalysisGlycosylation and Glycoproteins Research
Structural and functional characterization of ubiquitin variant inhibitors for the JAMM-family deubiquitinases STAMBP and STAMBPL1 | Litcius