Ubiquitylation is a reversible protein modification that is implicated in many cellular
functions. Recently, much progress has been made in the characterization of a superfamily …

The deubiquitylating enzymes (DUBs, also known as deubiquitylases or deubiquitinases)
maintain the dynamic state of the cellular ubiquitome by releasing conjugated ubiquitin from …

Protein ubiquitination is one of the most powerful posttranslational modifications of proteins,
as it regulates a plethora of cellular processes in distinct manners. Simple …

Deubiquitylating (or deubiquitinating) enzymes (DUBs) are proteases that reverse protein
ubiquitylation and therefore modulate the outcome of this post-translational modification …

In eukaryotes, deubiquitinases (DUBs) remove ubiquitin conjugates from diverse substrates,
altering their stabilities, localizations or activities. Here we show that many DUBs of the USP …

A common strategy for exploring the biological roles of deubiquitinating enzymes (DUB s) in
different pathways is to study the effects of replacing the wild‐type DUB with a catalytically …

Removal of ubiquitin from modified proteins is an important process to regulate the ubiquitin
system. Roughly 100 dedicated enzymes for this purpose, the deubiquitinases, exist in …

Addition and removal of ubiquitin or ubiquitin chains to and from proteins is a tightly
regulated process that contributes to cellular signaling and protein stability. Here we show …

An astounding number of important regulatory and structural proteins are subject to
modification by the attachment of ubiquitin or ubiquitin‐like proteins. This modification acts …

Since its discovery forty years ago, protein ubiquitination has been an ever-expanding field.
Virtually all biological processes are controlled by the post-translational conjugation of …