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 …

The ubiquitin proteasome pathway is responsible for most of the protein degradation in
mammalian cells. Rates of degradation by this pathway have generally been assumed to be …

The proteasome degrades most cellular proteins in a controlled and tightly regulated
manner and thereby controls many processes, including cell cycle, transcription, signalling …

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

Cryo-electron microscopy (cryo-EM) of non-crystalline single particles is a biophysical
technique that can be used to determine the structure of biological macromolecules and …

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 …

Abstract Knowledge of the three-dimensional structures of proteins and other biological
macromolecules often aids understanding of how they perform complicated tasks in the cell …

The eukaryotic 26S proteasome is a large multisubunit complex that degrades the majority
of proteins in the cell under normal conditions. The 26S proteasome can be divided into two …

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 …