Results 1 to 10 of about 278,733 (404)
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
openaire +6 more sources
KLHL12 promotes non-lysine ubiquitination of the dopamine receptors D-4.2 and D-4.4, but not of the ADHD-associated D-4.7 variant [PDF]
, 2015 Dopamine D-4 Receptor Polymorphism : The dopamine D-4 receptor has an important polymorphism in its third intracellular loop that is intensively studied and has been associated with several abnormal conditions, among others, attention deficit ...
Lintermans, Béatrice +3 more
core +11 more sources
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.
openaire +3 more sources
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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In the family with ubiquitin [PDF]
EMBO reports, 2011 The Cold Spring Harbor meeting on ‘The Ubiquitin family’, held in May 2011, brought together scientists from a wide range of fields, all under the common umbrella of ubiquitin and ubiquitin‐like protein structure, function and regulation.
Alexandru, Gabriela +2 more
openaire +5 more sources
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
openaire +3 more sources
OTUB1 triggers lung cancer development by inhibiting RAS monoubiquitination [PDF]
, 2016 Activation of the RAS oncogenic pathway, frequently ensuing from mutations in RAS genes, is a common event in human cancer. Recent reports demonstrate that reversible ubiquitination of RAS GTPases dramatically affects their activity, suggesting that ...
Asbagh, Layka Abbasi +10 more
core +1 more source
A Novel Peptide-Based SILAC Method to Identify the Posttranslational Modifications Provides Evidence for Unconventional Ubiquitination in the ER-Associated Degradation Pathway. [PDF]
, 2013 The endoplasmic reticulum-associated degradation (ERAD) pathway is responsible for disposing misfolded proteins from the endoplasmic reticulum by inducing their ubiquitination and degradation.
Anania, Veronica +4 more
core +3 more sources