Ubiquitin-ligases or E3s are components of the ubiquitin proteasome system (UPS) that
coordinate the transfer of ubiquitin to the target protein. A major class of ubiquitin-ligases …

Protein ubiquitination is a major post-translational modification that regulates development,
apoptosis, responses to environmental cues, and other processes in eukaryotes. Although …

Selective modification of proteins by ubiquitination is directed by diverse families of ubiquitin-
protein ligases (or E3s). A large collection of E3s use Cullins (CULs) as scaffolds to form …

Ubiquitin (Ub) is a small peptide that is covalently attached to proteins in a posttranslational
reaction. Ubiquitination is a precise regulatory system that is present in all eukaryotic …

Posttranslational modifications add complexity and diversity to cellular proteomes. One of
the most prevalent modifications across eukaryotes is ubiquitination, which is orchestrated …

The protein ubiquitin is a covalent modifier of proteins, including itself. The ubiquitin system
encompasses the enzymes required for catalysing attachment of ubiquitin to substrates as …

Selective ubiquitination of proteins is directed by diverse families of ubiquitin-protein ligases
(or E3s) in plants. One important type uses Cullin-3 as a scaffold to assemble multisubunit …

The majority of proteins in eukaryotic cells are modified according to highly regulated
mechanisms to fulfill specific functions and to achieve localization, stability, and transport …

Background Ubiquitination is a post-translation modification where ubiquitin is attached to a
substrate. Ubiquitin-conjugating enzymes (E2s) play a major role in the ubiquitin transfer …

Ubiquitin ligases play an important regulatory role in the control of protein degradation
processes via the ubiquitin/26S proteasome pathway in eukaryotes. These enzymes …