Results 31 to 40 of about 254,188 (362)
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
Cell, 2016 Ubiquitination is a post-translational modification of proteins involved in a variety of cellular processes. Ubiquitination requires the sequential action of three enzymes: E1 (ubiquitin-activating enzymes), E2 (ubiquitin-conjugating enzymes), and E3 (ubiquitin ligases).
Morreale, Francesca Ester, Walden, Helen
openaire +2 more sources
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
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
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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
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.
Sriramachandran, Annie M. +1 more
openaire +2 more sources
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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Proceedings of the National Academy of Sciences of the United States of America, 2019 Significance The formation of isopeptide bonds between the C-terminal carboxylate of ubiquitin and ε-amino groups of lysine residues on another protein is a major mechanism for regulating protein function. Ubiquitin can also form peptide bonds with the N-
Ian R. Kelsall +4 more
semanticscholar +1 more source
Nature Communications, 2017 The ubiquitination mediated by ubiquitin activating enzyme (E1), ubiquitin conjugating enzyme (E2), and ubiquitin ligase (E3) cascade is crucial to protein degradation, transcription regulation, and cell signaling in eukaryotic cells.
Yang Li +12 more
semanticscholar +1 more source
Linear ubiquitin chains: enzymes, mechanisms and biology [PDF]
Open Biology, 2017 Ubiquitination is a versatile post-translational modification that regulates a multitude of cellular processes. Its versatility is based on the ability of ubiquitin to form multiple types of polyubiquitin chains, which are recognized by specific ...
Katrin Rittinger, Fumiyo Ikeda
doaj +1 more source