A growing number of cellular functions have been shown to be regulated through protein
degradation. The selective degradation of many short-lived proteins in eukaryotic cells is …

Ubiquitin modification of many cellular proteins targets them for proteasomal degradation,
but in addition can also serve non-proteolytic functions. Over the last years, a significant …

Ubiquitination, the covalent attachment of the small protein modifier ubiquitin to a substrate
protein is involved in virtually all cellular processes by mediating the regulated degradation …

The covalent attachment of the polypeptide ubiquitin to proteins marks them for degradation
by the ubiquitin/26S proteasome‐dependent degradation pathway. This pathway functions …

Owing to the intensive research activity on protein synthesis, little attention was paid in the
1950s and 1960s to protein degradation. However, work by my group and others between …

Intracellular protein degradation is a tightly regulated process that in many cases is
controlled by protein ubiquitylation. The ubiquitin pathway is a major route by which cells not …

Ubiquitination involves the attachment of ubiquitin to lysine residues on substrate proteins or
itself, which can result in protein monoubiquitination or polyubiquitination. Ubiquitin …

The selective degradation of many short-lived proteins in eukaryotic cells is carried out by
the ubiquitin system. In this pathway, proteins are targeted for degradation by covalent …

Ubiquitination is a post-translational modification of proteins involved in a variety of cellular
processes. Ubiquitination requires the sequential action of three enzymes: E1 (ubiquitin …

Covalent attachment of ubiquitin to cellular proteins is essential for cell viability and is
catalysed by a set of distinct ubiquitin-conjugating enzymes. Individual members of this …