Deubiquitinases (DUBs) are specialized proteases that remove ubiquitin from substrates or
cleave within ubiquitin chains to regulate ubiquitylation and therefore play important roles in …

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

As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal
proteolytic machine responsible for regulated protein degradation in eukaryotic cells. The …

Ubiquitin signaling is a conserved, widespread, and dynamic process in which protein
substrates are rapidly modified by ubiquitin to impact protein activity, localization, or stability …

INTRODUCTION Many cellular proteins are polyubiquitinated but cannot be directly
degraded by the proteasome because they are well folded, associated with binding …

The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is
responsible for selective protein degradation in eukaryotic cells. Here we present cryo …

Proteasomal degradation of ubiquitylated proteins is tightly regulated at multiple levels,–. A
primary regulatory checkpoint is the removal of ubiquitin chains from substrates by the …

INTRODUCTION As the major protease in eukaryotic cells and the final component of the
ubiquitin-proteasome system, the 26 S proteasome is responsible for protein homeostasis …

All eukaryotes rely on selective proteolysis to control the abundance of key regulatory
proteins and maintain a healthy and properly functioning proteome. Most of this turnover is …

The 26S proteasome is involved in degrading and regulating the majority of proteins in
eukaryotic cells, which requires a sophisticated balance of specificity and promiscuity. In this …