Sort   by:  
 Page size 
ProteomicsStructural insights into a HECT-type E3 ligase AREL1
Structural insights into a HECT-type E3 ligase AREL1 and its ubiquitination activities in vitro
ORGANISM(S): Homo sapiens (Human) 
2019-11-25 | PXD016016 | Pride
Second mitochondria-derived activator of caspase (smac) Cancer Hect domain Apoptosis-resistant e3 ligase 1 (arel1) Structural biology Autopolyubiquitination Ubiquitination Protein degradation Apoptosis Posttranslational modification 
UnknownRedefining the catalytic HECT domain boundaries for the HECT E3 ubiquitin ligase family.
Not available
S-EPMC9547173 | biostudies-literature
ProteomicsTherapeutic potential of allosteric HECT E3 ligase inhibition
Supplemental proteomics data Abstract: Inhibition of ubiquitin E3-ligases is therapeutically attractive; however, the absence of an active-site pocket impedes computational approaches to inhibitor identification. In a large unbiased physical screen, we discovered inhibitors that bind a cryptic cavi...
ORGANISM(S): Homo sapiens (Human) 
2025-05-26 | PXD051134 | Pride
Drug discovery E6ap Pulmonary arterial hypertension Small molecule Ubiquitin e3-ligase Vascular remodeling Hect Allosteric inhibition Smurf1 Glycine hinge 
ProteomicsHECTD3 is a small HECT E3 ligase with unique features
HECT E3 ligases regulate many cellular processes, yet how they recognise their substrates and synthesise specific types of poly-ubiquitin chains is still incompletely understood. HECTD3, a member of the “other HECT” family, is implicated in the regulation of inflammation, apoptosis, and infection an...
ORGANISM(S): Homo sapiens (Human) 
2026-01-15 | PXD066996 | Pride
E3 ligase Cross-linking 
UnknownRegulating the human HECT E3 ligases.
Not available
S-EPMC6063350 | biostudies-literature
UnknownEvolution of plant HECT ubiquitin ligases.
Not available
S-EPMC3712016 | biostudies-literature
UnknownA Tunable Brake for HECT Ubiquitin Ligases.
Not available
S-EPMC5489419 | biostudies-literature
UnknownStructure of the HECT domain of human WWP2.
Not available
S-EPMC4601588 | biostudies-literature
UnknownAnimal HECT ubiquitin ligases: evolution and functional implications.
Not available
S-EPMC2837046 | biostudies-literature
ProteomicsStructural ubiquitin contributes to K48 linkage-specificity of the HECT ligase Tom1
Homologous to E6AP C-Terminus (HECT) ubiquitin ligases play key roles in essential pathways such as DNA repair, cell cycle control or protein quality control. Tom1 is one of five HECT ubiquitin E3 ligases in budding yeast S. cerevisiae and prototypical for a ligase with pleiotropic functions such as...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2025-08-07 | PXD062321 | Pride
Hect  ubiquitin  orphan quality control  huwe1  tom1  protein ubiquitylation  cryo-em 
Sort   by:  
 Page size