Attachment of ubiquitin or ubiquitin-like proteins (known as UBLs) to their targets through
multienzyme cascades is a central mechanism to modulate protein functions. This process is …

Ubiquitin (Ub) and ubiquitin-like proteins (Ubls) are conjugated to their targets by specific
cascades involving three classes of enzymes, E1, E2, and E3. Each E1 adenylates the C …

Since its discovery as a post-translational signal for protein degradation, our understanding
of ubiquitin (Ub) has vastly evolved. Today, we recognize that the role of Ub signaling is …

Summary Ubiquitin (Ub)-binding domains (UBDs) are key elements in conveying Ub-based
cellular signals. UBD-containing proteins interact with ubiquitinated targets and control …

The family of ubiquitin‐conjugating (E2) enzymes is characterized by the presence of a
highly conserved ubiquitin‐conjugating (UBC) domain. These domains accommodate the …

Ubiquitination is a post-translational modification pathway involved in myriad cellular
regulation and disease pathways. The Ub (ubiquitin) transfer cascade requires three …

Attachment of ubiquitin (Ub) and ubiquitin-like proteins (Ubls) to cellular proteins regulates
numerous cellular processes including transcription, the cell cycle, stress responses, DNA …

Post-translational modifications of proteins with ubiquitin (Ub) and ubiquitin-like modifiers
(Ubls), orchestrated by a cascade of specialized E1, E2 and E3 enzymes, control a wide …

Ubiquitin signalling is a fundamental eukaryotic regulatory system, controlling diverse
cellular functions. A cascade of E1, E2, and E3 enzymes is required for assembly of distinct …

Ubiquitin (Ub) and ubiquitin-like (Ubl) proteins regulate a diverse array of cellular pathways
through post-translational attachment to protein substrates. Ub/Ubl-mediated signaling is …