Results 21 to 30 of about 197,780 (305)
Hepatology Communications, 2021 We aimed to identify a microRNA (miRNA)‐E3 ubiquitin ligase regulatory network for protein substrates enriched in cell death pathways and investigate the underlying molecular mechanisms in alcohol‐associated hepatitis (AH).
Xiude Fan +8 more
doaj +1 more source
MDM2 E3 ligase activity is essential for p53 regulation and cell cycle integrity.
PLoS Genetics, 2022 MDM2 and MDM4 are key regulators of p53 and function as oncogenes when aberrantly expressed. MDM2 and MDM4 partner to suppress p53 transcriptional transactivation and polyubiquitinate p53 for degradation.
Meenalakshmi Chinnam +8 more
doaj +1 more source
EMBO reports, 2014 The RING-in-between-RING (RBR) E3s are a curious family of ubiquitin E3-ligases, whose mechanism of action is unusual in several ways. Their activities are auto-inhibited, causing a requirement for activation by protein-protein interactions or posttranslational modifications.
Judith J, Smit, Titia K, Sixma
openaire +2 more sources
Discovery of E3 Ligase Ligands for Target Protein Degradation
Molecules, 2022 Target protein degradation has emerged as a promising strategy for the discovery of novel therapeutics during the last decade. Proteolysis-targeting chimera (PROTAC) harnesses a cellular ubiquitin-dependent proteolysis system for the efficient ...
Jaeseok Lee +5 more
doaj +1 more source
Activity-based E3 ligase profiling uncovers an E3 ligase with esterification activity [PDF]
Nature, 2018 Ubiquitination is initiated by transfer of ubiquitin (Ub) from a ubiquitin-activating enzyme (E1) to a ubiquitin-conjugating enzyme (E2), producing a covalently linked intermediate (E2-Ub) 1 . Ubiquitin ligases (E3s) of the 'really interesting new gene' (RING) class recruit E2-Ub via their RING domain and then mediate direct transfer of ubiquitin to ...
Pao, Kuan-Chuan +9 more
openaire +3 more sources
A Comprehensive Atlas of E3 Ubiquitin Ligase Mutations in Neurological Disorders
Frontiers in Genetics, 2018 Protein ubiquitination is a posttranslational modification that plays an integral part in mediating diverse cellular functions. The process of protein ubiquitination requires an enzymatic cascade that consists of a ubiquitin activating enzyme (E1 ...
Arlene J. George +4 more
doaj +1 more source
Ubiquitin E3 ligase FIEL1 regulates fibrotic lung injury through SUMO-E3 ligase PIAS4 [PDF]
The Journal of Cell Biology, 2016 The E3 small ubiquitin-like modifier (SUMO) protein ligase protein inhibitor of activated STAT 4 (PIAS4) is a pivotal protein in regulating the TGFβ pathway. In this study, we discovered a new protein isoform encoded by KIAA0317, termed fibrosis-inducing E3 ligase 1 (FIEL1), which potently stimulates the TGFβ signaling pathway through the site-specific
Lear, Travis +10 more
openaire +2 more sources
SUMO chain-induced dimerization activates RNF4 [PDF]
, 2014 Dimeric RING E3 ligases interact with protein substrates and conformationally restrain the ubiquitin-E2-conjugating enzyme thioester complex such that it is primed for catalysis.
Alejandro Rojas-Fernandez +64 more
core +3 more sources
Science-Business eXchange, 2010 Two groups of researchers have identified inhibitors of E3 ubiquitin ligase, which has been considered difficult, if not impossible, to target with small molecules. The findings could lead to compounds that are more specific disrupters of tumor cell proliferation than the proteasome inhibitor Velcade bortezomib.
openaire +1 more source
Structure-guided design and optimization of small molecules targeting the protein-protein interaction between the von hippel-lindau (VHL) E3 ubiquitin ligase and the hypoxia inducible factor (HIF) alpha subunit with in vitro nanomolar affinities [PDF]
, 2014 E3 ubiquitin ligases are attractive targets in the ubiquitin-proteasome system, however, the development of small-molecule ligands has been rewarded with limited success.
Adams J. +31 more
core +5 more sources