Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications [PDF]
, 2012 Conjugation of ubiquitin to proteins (ubiquitylation) has emerged to be one of the most crucial post-translational modifications controlling virtually all cellular processes.
Fulda, Simone +2 more
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RBR E3 ubiquitin ligases: new structures, new insights, new questions [PDF]
, 2014 The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes.
Shaw, Gary S. +2 more
core +1 more source
The roles of E3 ubiquitin ligases in cancer progression and targeted therapy
Clinical and Translational Medicine, 2023 Ubiquitination is one of the most important post‐translational modifications which plays a significant role in conserving the homeostasis of cellular proteins.
Chibuzo Sampson +6 more
doaj +1 more source
E3 ubiquitin ligases in the acute leukemic signaling pathways
Frontiers in Physiology, 2022 Acute leukemia is a common hematologic tumor with highly genetic heterogeneity, and many factors are involved in the pathogenesis and drug-resistance mechanism.
Qianru Zhan +4 more
doaj +1 more source
A general strategy for discovery of inhibitors and activators of RING and U-box E3 ligases with ubiquitin variants [PDF]
, 2017 RING and U-box E3 ubiquitin ligases regulate diverse eukaryotic processes and have been implicated in numerous diseases, but targeting these enzymes remains a major challenge.
Ahmed, Syed Feroj +8 more
core +3 more sources
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
E3 Ubiquitin Ligases as Cancer Targets and Biomarkers
Neoplasia: An International Journal for Oncology Research, 2006 E3 ubiquitin ligases are a large family of proteins that are engaged in the regulation of the turnover and activity of many target proteins. Together with ubiquitinactivating enzyme El and ubiquitin-conjugating enzyme E2, E3 ubiquitin ligases catalyze ...
Yi Sun
doaj +1 more source
Structure of the HHARI catalytic domain shows glimpses of a HECT E3 ligase. [PDF]
PLoS ONE, 2013 The ubiquitin-signaling pathway utilizes E1 activating, E2 conjugating, and E3 ligase enzymes to sequentially transfer the small modifier protein ubiquitin to a substrate protein.
Donald E Spratt +2 more
doaj +1 more source
Targeted Degradation of 53BP1 Using Ubiquitin Variant Induced Proximity
Biomolecules, 2022 In recent years, researchers have leveraged the ubiquitin-proteasome system (UPS) to induce selective degradation of proteins by E3 ubiquitin ligases, which has great potential as novel therapeutics for human diseases, including cancer and ...
Bayonle Aminu +4 more
doaj +1 more source
Viral hijacking of cellular ubiquitination pathways as an anti-innate immunity strategy. [PDF]
, 2006 International audienceViruses are obligate parasites of host cells. Virus-host coevolution has selected virus for growth despite antiviral defenses set up by hosting cells and organisms. Ubiquitin conjugation onto proteins, through a cascade of reactions
Chen, Mingzhou, Gerlier, Denis
core +3 more sources