Protein turnover, a highly regulated process governed by the ubiquitin–proteasome system
(UPS), is essential for maintaining cellular homeostasis. Dysregulation of the UPS has been …

Deubiquitinases (DUBs) have been the subject of intense scrutiny in recent years. Many of
their diverse enzymatic mechanisms are well characterized in vitro; however, our …

Ubiquitin-conjugating E2 enzymes are central to the ubiquitination cascade and have been
implicated in cancer and other diseases. Despite strong interest in developing specific E2 …

Ubiquitin modifications of target proteins act to localise, direct and specify a diverse range of
cellular processes, many of which are biomedically relevant. To allow this diversity, ubiquitin …

Ubiquitination is a crucial posttranslational protein modification involved in a myriad of
biological pathways. This modification is reversed by deubiquitinases (DUBs) that …

Ubiquitin (Ub)-binding domains embedded in intracellular proteins act as readers of the
complex Ub code and contribute to regulation of numerous eukaryotic processes. Ub …

Abstract Domains found in ubiquitin specific proteases (DUSPs) occur in seven members of
the ubiquitin specific protease (USP) family. DUSPs are defined by a distinct structural fold …

Targeted inhibition of misregulated protein–protein interactions (PPIs) has been a promising
area of investigation in drug discovery and development for human diseases. However …

Ubiquitination is an important protein post-translational modification that is essential for
almost all cellular processes in human cells. The reverse process, deubiquitination is …