Results 21 to 30 of about 596,162 (342)
Frontiers in Molecular Neuroscience, 2023 The tripartite motif (TRIM) protein family members have been implicated in a multitude of physiologies and pathologies in different tissues. With diverse functions in cellular processes including regulation of signaling pathways, protein degradation, and
Jane Dudley-Fraser, Katrin Rittinger
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E3 ubiquitin ligases: styles, structures and functions
Molecular Biomedicine, 2021 E3 ubiquitin ligases are a large family of enzymes that join in a three-enzyme ubiquitination cascade together with ubiquitin activating enzyme E1 and ubiquitin conjugating enzyme E2.
Quan Yang +3 more
semanticscholar +1 more source
Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination [PDF]
Cell, 2016 Conventional ubiquitination involves the ATP-dependent formation of amide bonds between the ubiquitin C terminus and primary amines in substrate proteins. Recently, SdeA, an effector protein of pathogenic Legionella pneumophila, was shown to mediate NAD-dependent and ATP-independent ubiquitin transfer to host proteins.
Bhogaraju, S. +6 more
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Ubiquitin signalling in neurodegeneration: mechanisms and therapeutic opportunities
Cell Death and Differentiation, 2021 Neurodegenerative diseases are characterised by progressive damage to the nervous system including the selective loss of vulnerable populations of neurons leading to motor symptoms and cognitive decline.
Marlene Schmidt +3 more
semanticscholar +1 more source
A Ubiquitin-like Protein Unleashes Ubiquitin Ligases [PDF]
Cell, 2008 Modification of cullin-RING ubiquitin ligases by the ubiquitin-like molecule Nedd8 promotes substrate ubiquitination. A crystal structure of a cullin modified by Nedd8 recently reported in Cell (Duda et al., 2008) and a biochemical study in Molecular Cell (Saha and Deshaies, 2008) reveal the dramatic impact on the ligase machinery by conjugation of ...
Saifee, Nabiha Huq, Zheng, Ning
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Strategies to Investigate Ubiquitination in Huntington's Disease
Frontiers in Chemistry, 2020 Many neurodegenerative disorders including Huntington's Disease are hallmarked by intracellular protein aggregates that are decorated by ubiquitin and different ubiquitin ligases and deubiquitinating enzymes. The protein aggregates observed in Huntington'
Karen A. Sap, Eric A. Reits
doaj +1 more source
Dss1 is a 26S proteasome ubiquitin receptor [PDF]
, 2014 The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Arrigoni +35 more
core +5 more sources
SUV39 SET domains mediate crosstalk of heterochromatic histone marks
eLife, 2021 The SUV39 class of methyltransferase enzymes deposits histone H3 lysine 9 di- and trimethylation (H3K9me2/3), the hallmark of constitutive heterochromatin.
Alessandro Stirpe +7 more
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A Conditional Yeast E1 Mutant Blocks the Ubiquitin–Proteasome Pathway and Reveals a Role for Ubiquitin Conjugates in Targeting Rad23 to the Proteasome [PDF]
, 2007 E1 ubiquitin activating enzyme catalyzes the initial step in all ubiquitin-dependent processes. We report the isolation of uba1-204, a temperature-sensitive allele of the essential Saccharomyces cerevisiae E1 gene, UBA1.
Amerik A. Y. +59 more
core +2 more sources
Terminating protein ubiquitination [PDF]
Cell Cycle, 2011 Ubiquitination is a post-translational modification that generally directs proteins for degradation by the proteasome or by lysosomes. However, ubiquitination has been implicated in many other cellular processes, including transcriptional regulation, DNA repair, regulation of protein-protein interactions and association with ubiquitin-binding scaffolds.
Daniel K, Stringer, Robert C, Piper
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