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 …

Immunosuppressive tumor microenvironment (TME) and ascites-derived spheroids in
ovarian cancer (OC) facilitate tumor growth and progression, and also pose major obstacles …

UBR5 is a nuclear E3 ligase that ubiquitinates a vast range of substrates for proteasomal
degradation. This HECT domain‐containing ubiquitin ligase has recently been identified as …

Histone ubiquitylation is a prominent response to DNA double-strand breaks (DSBs), but
how these modifications are confined to DNA lesions is not understood. Here, we show that …

Background: The up-regulation of PD-L1 is recognized as an adaption of cancer cells to
evade immune surveillance and attack. However, the intrinsic mechanisms of the induction …

A subset of proteins targeted by the N-end rule pathway bear degradation signals called N-
degrons, whose determinants include destabilizing N-terminal residues. Our previous work …

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 …

Patients with triple-negative breast cancers (TNBC) are at high risk for recurrence and
metastasis at an early time despite standard treatment, underscoring the need for novel …

Protein kinases have central functions in various cellular signal transduction pathways
through their substrate phosphorylation. Here we show that a protein kinase, DYRK2, has …