Results 51 to 60 of about 349,913 (393)
RMND5 from Xenopus laevis is an E3 ubiquitin-ligase and functions in early embryonic forebrain development. [PDF]
PLoS ONE, 2015 In Saccharomyces cerevisiae the Gid-complex functions as an ubiquitin-ligase complex that regulates the metabolic switch between glycolysis and gluconeogenesis.
Thorsten Pfirrmann +5 more
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Nature Communications, 2016 The NLRP3 inflammasome has a fundamental role in host defence against microbial pathogens and its deregulation may cause diverse inflammatory diseases. NLRP3 protein expression is a rate-limiting step for inflammasome activation, thus its expression must
Hui Song +10 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
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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G Protein Mono-ubiquitination by the Rsp5 Ubiquitin Ligase [PDF]
Journal of Biological Chemistry, 2009 Emerging evidence suggests that ubiquitination serves as a protein trafficking signal in addition to its well characterized role in promoting protein degradation. The yeast G protein α subunit Gpa1 represents a rare example of a protein that undergoes both mono- and poly-ubiquitination.
Matthew P, Torres +6 more
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A Generic Platform for Cellular Screening Against Ubiquitin Ligases [PDF]
, 2016 Ubiquitin signalling regulates most aspects of cellular life, thus deregulation of ubiquitylation has been linked with a number of diseases. E3 ubiquitin ligases provide substrate selectivity in ubiquitylation cascades and are therefore considered to be ...
AD Capili +31 more
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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.
Wei Jiang, Bao-Liang Song
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TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions
Computational and Structural Biotechnology Journal, 2023 Protein ubiquitination is a post-translation modification mediated by E3 ubiquitin ligases. The RING domain E3 ligases are the largest family of E3 ubiquitin ligases, they act as a scaffold, bringing the E2-ubiquitin complex and its substrate together to
Xiaohua Lou +7 more
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The E3 ubiquitin ligase RNF185 facilitates the cGAS-mediated innate immune response
PLoS Pathogens, 2017 The cyclic GMP-AMP synthase (cGAS), upon cytosolic DNA stimulation, catalyzes the formation of the second messenger 2′3′-cGAMP, which then binds to stimulator of interferon genes (STING) and activates downstream signaling. It remains to be elucidated how
Qiang Wang +14 more
semanticscholar +1 more source
BiomedicinesUbiquitylation is a post-translational modification originally identified as the first step in protein degradation by the ubiquitin–proteasome system. Ubiquitylation is also known to regulate many cellular processes without degrading the ubiquitylated ...
Koji Matsuhisa +2 more
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