Results 11 to 20 of about 33,989 (317)
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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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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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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Regulation of ubiquitin and ubiquitin‐like modifiers by phosphorylation [PDF]
The FEBS Journal, 2021 The regulatory influence of ubiquitin is vast, encompassing all cellular processes, by virtue of its central roles in protein degradation, membrane trafficking, and cell signaling. But how does ubiquitin, a 76 amino acid peptide, carry out such diverse, complex functions in eukaryotic cells? Part of the answer is rooted in the high degree of complexity
Nathaniel L. Hepowit +4 more
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Ubiquitin carboxyl-terminal hydrolases are required for period maintenance of the circadian clock at high temperature in Arabidopsis [PDF]
, 2019 Protein ubiquitylation participates in a number of essential cellular processes including signal transduction and transcription, often by initiating the degradation of specific substrates through the 26S proteasome. Within the ubiquitin-proteasome system,
Coupland, George +6 more
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A comparative analysis of the ubiquitination kinetics of multiple degrons to identify an ideal targeting sequence for a proteasome reporter. [PDF]
PLoS ONE, 2013 The ubiquitin proteasome system (UPS) is the primary pathway responsible for the recognition and degradation of misfolded, damaged, or tightly regulated proteins.
Adam T Melvin +5 more
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Frontiers in Microbiology, 2022 Phytophthora sp. are invasive groups of pathogens belonging to class Oomycetes. In order to contain and control them, a deep knowledge of their biology and infection strategy is imperative.
Kajal Mandal +7 more
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The ubiquitin-proteasome pathway in Huntington's disease. [PDF]
, 2008 The accumulation of mutant protein is a common feature of neurodegenerative disease. In Huntington's disease, a polyglutamine expansion in the huntingtin protein triggers neuronal toxicity.
Finkbeiner, Steven, Mitra, Siddhartha
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