Protein ubiquitination has become one of the most extensively studied post-translational
modifications. Originally discovered as a critical element in highly regulated proteolysis …

Ubiquitination now ranks with phosphorylation as one of the best-studied post-translational
modifications of proteins with broad regulatory roles across all of biology. Ubiquitination …

Protein ubiquitination regulates many cellular processes via attachment of structurally and
functionally distinct ubiquitin (Ub) chains. Several atypical chain types have remained poorly …

Polyubiquitin chains regulate diverse cellular processes through the ability of ubiquitin to
form chains of eight different linkage types. Although detected in yeast and mammals, little is …

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 …

Ubiquitin plays an essential role in modulating protein functions, and deregulation of the
ubiquitin system leads to the development of multiple human diseases. Owing to its …

Ubiquitin (Ub) is a small protein modifier that regulates many biological processes, including
gene transcription, cell‐cycle progression, DNA repair, apoptosis, virus budding and …

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 …

Several ubiquitin chain types have remained unstudied, mainly because tools and
techniques to detect these posttranslational modifications are scarce. Linkage-specific …

Protein ubiquitylation is a recognized signal for protein degradation. However, it is
increasingly realized that ubiquitin conjugation to proteins can be used for many other …