Results 21 to 30 of about 211,577 (291)
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
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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
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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
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Pto kinase binds two domains of AvrPtoB and its proximity to the effector E3 ligase determines if it evades degradation and activates plant immunity. [PDF]
PLoS Pathogens, 2014 The tomato--Pseudomonas syringae pv. tomato (Pst)--pathosystem is one of the best understood models for plant-pathogen interactions. Certain wild relatives of tomato express two closely related members of the same kinase family, Pto and Fen, which ...
Johannes Mathieu +2 more
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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.
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Biochemistry and Biophysics Reports, 2020 TRIM family of E3 ubiquitin ligases have an amino-terminal conserved tripartite motif consisting of RING, B-Box, coiled-coil domain and different C-terminal domain leading it to classification into 11 subclasses.
Ishita Gupta +3 more
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An ORFeome of rice E3 ubiquitin ligases for global analysis of the ubiquitination interactome
Genome Biology, 2022 Background Ubiquitination is essential for many cellular processes in eukaryotes, including 26S proteasome-dependent protein degradation, cell cycle progression, transcriptional regulation, and signal transduction.
Ruyi Wang +26 more
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Inhibitors of ubiquitin E3 ligase as potential new antimalarial drug leads
BMC Pharmacology and Toxicology, 2017 Background Protein ubiquitylation is an important post-translational regulation, which has been shown to be necessary for life cycle progression and survival of Plasmodium falciparum.
Jagrati Jain +3 more
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Frontiers in Cellular Neuroscience, 2021 The Ubiquitin Proteasome System (UPS) is responsible for the degradation of misfolded or aggregated proteins via a multistep ATP-dependent proteolytic mechanism. This process involves a cascade of ubiquitin (Ub) transfer steps from E1 to E2 to E3 ligase.
Frances M. Potjewyd, Alison D. Axtman
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E3 Ligase Ligands for PROTACs: How They Were Found and How to Discover New Ones
SLAS discovery : advancing life sciences R & D, 2020 Bifunctional degrader molecules, also called proteolysis-targeting chimeras (PROTACs), are a new modality of chemical tools and potential therapeutics to understand and treat human disease.
T. Ishida, A. Ciulli
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