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 …

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 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 …

Post-translational modification with ubiquitin is required for cell division, differentiation, and
survival in all eukaryotes. As part of an intricate signaling code, ubiquitin is attached to its …

DNA double strand breaks need to be repaired in an organized fashion to preserve genomic
integrity. In the organization of faithful repair, histone ubiquitination plays a crucial role …

The polycomb group (PcG) proteins are a large and diverse family that epigenetically
repress the transcription of key developmental genes. They form three broad groups of …

The 26S proteasome is a 2.5-MDa complex responsible for the selective, ATP-dependent
degradation of ubiquitylated proteins in eukaryotic cells. Substrates in hundreds cellular …