As an important post-translational modification, ubiquitination mediates∼ 80% of protein
degradation in eukaryotes. The degree of protein ubiquitination is tightly determined by the …

The ubiquitination mediated by ubiquitin activating enzyme (E1), ubiquitin conjugating
enzyme (E2), and ubiquitin ligase (E3) cascade is crucial to protein degradation …

Motivation Protein ubiquitination plays a central role in important cellular machineries such
as protein degradation or chromatin-mediated signaling. With the recent discovery of the first …

Ubiquitination is an important post-translational modification, which controls protein turnover
by labeling malfunctional and redundant proteins for proteasomal degradation, and also …

Intracellular signaling via the covalent attachment of different ubiquitin linkages to protein
substrates is fundamental to many cellular processes. Although linkage-selective ubiquitin …

Ubiquitination plays an important role in many cellular processes and is implicated in many
diseases. Experimental identification of ubiquitination sites is challenging due to rapid …

Protein ubiquitination is one of the most important reversible post-translational modifications
(PTMs). In many biochemical, pathological and pharmaceutical studies on understanding …

It has been more than 30 years since the initial report of the discovery of ubiquitin as an 8.5
kDa protein of unknown function expressed universally in living cells. And still, protein …

Background The conjugation of ubiquitin to a substrate protein (protein ubiquitylation), which
involves a sequential process–E1 activation, E2 conjugation and E3 ligation, is crucial to the …

The ubiquitin-proteasome system plays a critical role in biology by regulating protein
degradation. Despite their importance, precise recognition specificity is known for a few of …