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 …

Ubiquitination regulates nearly all cellular processes by coordinated activity of ubiquitin
writers (E1, E2, and E3 enzymes), erasers (deubiquitinating enzymes) and readers (proteins …

Ubiquitin-binding proteins play an important role in eukaryotes by translating differently
linked polyubiquitin chains into proper cellular responses. Current knowledge about …

The ubiquitin-proteasome system (UPS) is critical for protein quality control and regulating
protein lifespans. Following ubiquitination, UPS substrates bind multidomain receptors that …

Ubiquitination is the major criteria for the recognition of a substrate-protein by the 26S
proteasome. Additionally, a disordered segment on the substrate—either intrinsic or induced …

The life of every organism is dependent on the fine-tuned mechanisms of protein synthesis
and breakdown. The degradation of most intracellular proteins is performed by the ubiquitin …

Spatial management of stress-induced protein aggregation is an integral part of the
proteostasis network. Protein modification by the ubiquitin-like molecule NEDD8 increases …

Protein ubiquitination regulates almost every process in eukaryotic cells. The study of the
many enzymes involved in the ubiquitination system and the development of ubiquitination …

Post-translational substrate modification with ubiquitin is essential for eukaryotic cellular
signaling. Polymeric ubiquitin chains are assembled with specific architectures, which …

Post-translational modification of proteins by ubiquitin is required for nearly all aspects of
eukaryotic cell function. The numerous targets of ubiquitylation, and variety of ubiquitin …