Ubiquitin Variant Inhibitors Meet the Deubiquitinase USP15

Adam J Middleton; Catherine L Day

doi:10.1016/j.str.2019.03.011

Ubiquitin Variant Inhibitors Meet the Deubiquitinase USP15

Structure. 2019 Apr 2;27(4):564-565. doi: 10.1016/j.str.2019.03.011.

Authors

Adam J Middleton¹, Catherine L Day²

Affiliations

¹ Department of Biochemistry, School of Biomedical Sciences, University of Otago, Dunedin 9054, New Zealand.
² Department of Biochemistry, School of Biomedical Sciences, University of Otago, Dunedin 9054, New Zealand. Electronic address: catherine.day@otago.ac.nz.

PMID: 30943387
DOI: 10.1016/j.str.2019.03.011

Abstract

Deubiquitinases (DUBs) are important regulators of cellular function and selective inhibitors are required to reveal their biological role and therapeutic potential. In this issue of Structure, Teyra et al. (2019) report the development of DUB USP15 inhibitors that provide a starting point for the analysis of USP15 function.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Deubiquitinating Enzymes*
Protein Processing, Post-Translational
Ubiquitin*
Ubiquitin-Specific Proteases

Substances

Ubiquitin
Deubiquitinating Enzymes
Ubiquitin-Specific Proteases