Posttranslational modification with ubiquitin chains controls cell fate in all eukaryotes.
Depending on the connectivity between subunits, different ubiquitin chain types trigger …

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 …

Protein ubiquitination shows remarkable topological and functional diversity through the
polymerization of ubiquitin via different linkages. Deciphering the cellular ubiquitin code is of …

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

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 …

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 …

Polyubiquitination is a posttranslational modification where ubiquitin chains containing
isopeptide bonds linking one of seven ubiquitin lysines with the C terminus of an adjoining …

Ubiquitination of proteins is a sophisticated post-translational modification implicated in the
regulation of an ever-growing abundance of cellular processes. Recent insights into different …

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

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 …