The posttranslational modification with ubiquitin, a process referred to as ubiquitylation,
controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a …

Between the 1960s and 1980s, most life scientists focused their attention on studies of
nucleic acids and the translation of the coded information. Protein degradation was a …

The ubiquitin–proteasome system (UPS) is the primary selective degradation system in the
nuclei and cytoplasm of eukaryotic cells, required for the turnover of myriad soluble proteins …

The proteasome is an intricate molecular machine, which serves to degrade proteins
following their conjugation to ubiquitin. Substrates dock onto the proteasome at its 19 …

Most cellular processes are carried out by multiprotein complexes. The identification and
analysis of their components provides insight into how the ensemble of expressed proteins …

The proteasome is the major ATP-dependent protease in eukaryotic cells, but limited
structural information restricts a mechanistic understanding of its activities. The proteasome …

Proteasomes, the primary mediators of ubiquitin–protein conjugate degradation, are
regulated through complex and poorly understood mechanisms. Here we show that USP14 …

The proteasome is a highly sophisticated protease complex designed to carry out selective,
efficient and processive hydrolysis of client proteins. It is known to collaborate with ubiquitin …

The eukaryotic endoplasmic reticulum (ER) maintains protein homeostasis by eliminating
unwanted proteins through the evolutionarily conserved ER-associated degradation (ERAD) …

Protein folding in the endoplasmic reticulum (ER) is monitored by ER quality control (ERQC)
mechanisms. Proteins that pass ERQC criteria traffic to their final destinations through the …