Ubiquitination regulates many essential cellular processes in eukaryotes. This post-
translational modification (PTM) is typically achieved by E1, E2, and E3 enzymes that …

Ubiquitination plays a pivotal role in several cellular processes and is critical for protein
degradation and signaling. E3 ubiquitin ligases are the matchmakers in the ubiquitination …

Ubiquitination, the covalent attachment of ubiquitin to proteins, by E3 ligases of the HECT
(homologous to E6AP C terminus) family is critical in controlling diverse physiological …

Ubiquitin ligases (E3 enzymes) transfer ubiquitin from ubiquitin-conjugating (E2) enzymes to
target proteins. By determining the selection of target proteins, modification sites on those …

Protein quality control (PQC) machineries play a critical role in selective identification and
removal of mistargeted, misfolded, and aberrant proteins. This task is extremely complicated …

The HECT (homologous to E6AP C-terminus) ubiquitin ligases (E3s) are a small family of
highly conserved enzymes involved in diverse cellular functions and pathological …

The HECT E3 ligase family regulates key cellular signaling pathways, with its 28 members
divided into three subfamilies: NEDD4 subfamily (9 members), HERC subfamily (6 …

Employing 125 I-polyubiquitin chain formation as a functional readout of ligase activity,
biochemical and biophysical evidence demonstrates that catalytically active E6-associated …

Protein ubiquitylation is essential for the maintenance of cellular homeostasis. E3 ubiquitin
ligases are key components of the enzymatic machinery catalyzing the attachment of …

Abstract Mortalin (mot-2) induces inactivation of the tumor suppressor p53's transcriptional
and apoptotic functions by cytoplasmic sequestration of p53 in select cancers. The mot-2 …