The ubiquitylation of proteins is carried out by E1, E2 and E3 (ubiquitin ligase) enzymes, and
targets them for degradation or for other cellular fates. The HECT enzymes, including Nedd4 …

Members of the HECT family of E3 ubiquitin-protein ligases are characterized by a C-
terminal HECT domain that catalyzes the covalent attachment of ubiquitin to substrate …

The N-end rule pathway is a proteolytic system in which N-terminal residues of short-lived
proteins are recognized by recognition components (N-recognins) as essential components …

Protein ubiquitylation is a widespread post-translational modification, regulating cellular
signalling with many outcomes, such as protein degradation, endocytosis, cell cycle …

Tight control of translation is fundamental for eukaryotic cells, and deregulation of proteins
implicated contributes to numerous human diseases. The neurodegenerative disorder …

Abstract Receptor-interacting protein 1 (RIP1) is a Ser/Thr kinase with both kinase-
dependent and kinase-independent roles in death receptor signaling. The kinase activity of …

Translational control of gene expression plays a key role in many biological processes.
Consequently, the activity of the translation apparatus is under tight homeostatic control …

The inhibition of the ubiquitin-dependent proteasome system (UPS) via specific drugs is one
type of approach used to combat cancer. Although it has been suggested that UPS inhibition …

The human UBR5 is a single polypeptide chain homology to E6AP C terminus (HECT)-type
E3 ubiquitin ligase essential for embryonic development in mammals. Dysregulated UBR5 …

Abstract The Ubiquitin-Proteasome System (UPS) is an important regulator of cell signaling
and proteostasis, which are essential to a variety of cellular processes. The UPS is disrupted …