Ubiquitination is an essential regulator of most, if not all, signalling pathways, and defects in
cellular signalling are central to cancer initiation, progression and, eventually, metastasis …

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 …

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

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 …

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 …

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 …

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 …

Posttranslational modification of cell-cycle regulators with ubiquitin chains is essential for
eukaryotic cell division. Such chains can be connected through seven lysine residues or the …

The proteasome has emerged as an intricate machine that has dynamic mechanisms to
regulate the timing of its activity, its selection of substrates, and its processivity. The 19 …