Results 41 to 50 of about 248,165 (360)
The E3 ubiquitin ligase Pellino2 mediates priming of the NLRP3 inflammasome
Nature Communications, 2018 The NLRP3 inflammasome has an important function in inflammation by promoting the processing of pro-IL-1β and pro-IL-18 to their mature bioactive forms, and by inducing cell death via pyroptosis.
Fiachra Humphries +8 more
semanticscholar +1 more source
Dysregulation of ubiquitin ligases in cancer [PDF]
Drug Resistance Updates, 2015 Ubiquitin ligases (UBLs) are critical components of the ubiquitin proteasome system (UPS), which governs fundamental processes regulating normal cellular homeostasis, metabolism, and cell cycle in response to external stress signals and DNA damage. Among multiple steps of the UPS system required to regulate protein ubiquitination and stability, UBLs ...
Ze'ev Ronai, Jianfei Qi
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E3 Ubiquitin Ligase TRIM Proteins, Cell Cycle and Mitosis
Cells, 2019 The cell cycle is a series of events by which cellular components are accurately segregated into daughter cells, principally controlled by the oscillating activities of cyclin-dependent kinases (CDKs) and their co-activators.
S. Venuto, G. Merla
semanticscholar +1 more source
Tag Team Ubiquitin Ligases [PDF]
Cell, 2016 Cullin-RING (CRL) and RING1-IBR-RING2 (RBR) are two distinct types of ubiquitin ligases. In this issue, Scott et al. show that CRLs activate the RBR enzyme ARIH1 to initiate ubiquitin chains on CRL substrates, thereby marking an unexpected and important advance in our understanding of both enzymes.
Gary Kleiger +2 more
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Novel Functions of Ubiquitin Ligase HRD1 With Transmembrane and Proline-Rich Domains
Journal of Pharmacological Sciences, 2008 Human ubiquitin ligase HRD1 is involved in endoplasmic reticulum-associated degradation (ERAD). We recently reported that HRD1 interacts with Parkin-associated endothelin receptor-like receptor (Pael-R), a substrate of Parkin, and promotes Pael-R ...
Tomohiro Omura +7 more
doaj +1 more source
Ubiquitin Ligation without a Ligase [PDF]
Developmental Cell, 2007 Classically, ubiquitination requires three enzymes acting in sequence: E1, E2, and E3. E3 ubiquitin ligases typically provide substrate specificity. An article in Molecular Cell (Hoeller et al., 2007) now describes the E3-independent monoubiquitination of certain proteins. The mechanism has interesting parallels to SUMO ligation.
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New Phytologist, 2017 Summary N6‐adenosine methylation (m6A) of mRNA is an essential process in most eukaryotes, but its role and the status of factors accompanying this modification are still poorly understood.
Kamil Růžička +14 more
semanticscholar +1 more source
Ubiquitin Ligases in Cholesterol Metabolism
Diabetes & Metabolism Journal, 2014 To maintain cholesterol homeostasis, the processes of cholesterol metabolism are regulated at multiple levels including transcription, translation, and enzymatic activity. Recently, the regulation of protein stability of some key players in cholesterol metabolism has been characterized.
Bao-Liang Song, Wei Jiang
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FBXL17/spastin axis as a novel therapeutic target of hereditary spastic paraplegia
Cell & Bioscience, 2022 Background Spastin significantly influences microtubule regulation in neurons and is implicated in the pathogenesis of hereditary spastic paraplegia (HSP). However, post-translational regulation of the spastin protein remains nebulous.
Hyun Mi Kang +10 more
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SUMO-targeted ubiquitin ligases
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014 Covalent posttranslational modification with SUMO (small ubiquitin-related modifier) modulates functions of a wide range of proteins in eukaryotic cells. Sumoylation affects the activity, interaction properties, subcellular localization and the stability of its substrate proteins.
R. Jürgen Dohmen +1 more
openaire +3 more sources