Results 11 to 20 of about 305,105 (318)
The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family
Nature Communications, 2023 RBR E3 ubiquitin ligases utilise a 2-step catalytic mechanism previously defined for only few of the RBR family members. Here, the authors examine the poorly studied RBRs HOIL-1 and RNF216 to define general principles of RBR catalysis and regulation and ...
Xiangyi S. Wang +6 more
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To Be or Not to Be...Ubiquitinated? [PDF]
Cell Cycle, 2004 Levels of p21, a cyclin-dependent kinase (CDK) inhibitor, are controlled in part at the post-translational level by protein degradation. Although the signaling pathways leading to p21 degradation have not yet been fully elucidated, it is evident that p21 ubiquitination is an essential factor in its degradation.
Michele Pagano, Joanna Bloom
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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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Cracking the Ubiquitin Code: The Ubiquitin Toolbox [PDF]
Current Issues in Molecular Biology, 2019 Ubiquitination, a post-translational modification, regulates a vast array of fundamental biological processes with dysregulation of the dedicated enzymes giving rise to pathologies such as cancer and neurodegenerative diseases. Assembly and its ensuing removal of this post-translational modification, determining a large variety of biological functions,
Mulder, M.P.C., Witting, K.F., Ovaa, H.
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The Ubiquitin Ligase SIAH2 Negatively Regulates Glucocorticoid Receptor Activity and Abundance
Biomedicines, 2020 Glucocorticoids are clinically essential drugs used routinely to control inflammation. However, a host of metabolic side effects manifests upon usage beyond a few days.
Susan J. Burke +7 more
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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.
Ivan Dikic +7 more
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To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death [PDF]
Cells, 2021 TRIM17 is a member of the TRIM family, a large class of RING-containing E3 ubiquitin-ligases. It is expressed at low levels in adult tissues, except in testis and in some brain regions. However, it can be highly induced in stress conditions which makes it a putative stress sensor required for the triggering of key cellular responses.
Meenakshi Basu-Shrivastava +3 more
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Cell Research, 2016 Protein ubiquitination is a dynamic multifaceted post-translational modification involved in nearly all aspects of eukaryotic biology. Once attached to a substrate, the 76-amino acid protein ubiquitin is subjected to further modifications, creating a multitude of distinct signals with distinct cellular outcomes, referred to as the 'ubiquitin code ...
Kirby N Swatek, David Komander
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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
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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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