Results 11 to 20 of about 169,475 (267)
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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Using Ubiquitin Binders to Decipher the Ubiquitin Code [PDF]
Trends in Biochemical Sciences, 2019 Post-translational modifications (PTMs) by ubiquitin (Ub) are versatile, highly dynamic, and involved in nearly all aspects of eukaryote biological function. The reversibility and heterogeneity of Ub chains attached to protein substrates have complicated their isolation, quantification, and characterization.
Mattern M +4 more
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Frontiers in Plant Science, 2018 Reversible protein ubiquitination plays essential roles in regulating cellular processes. Although many reports have described the functions of ubiquitination in plant defense responses, few have focused on global changes in the ubiquitome.
Xiao-Lin Chen +10 more
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The Ubiquitination Machinery of the Ubiquitin System [PDF]
The Arabidopsis Book, 2014 The protein ubiquitin is a covalent modifier of proteins, including itself. The ubiquitin system encompasses the enzymes required for catalysing attachment of ubiquitin to substrates as well as proteins that bind to ubiquitinated proteins leading them to their final fate.
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Ubiquitin in Motion: Structural Studies of the Ubiquitin-Conjugating Enzyme∼Ubiquitin Conjugate [PDF]
Biochemistry, 2011 Ubiquitination of proteins provides a powerful and versatile post-translational signal in the eukaryotic cell. The formation of a thioester bond between ubiquitin (Ub) and the active site of a ubiquitin-conjugating enzyme (E2) is critical for the transfer of Ub to substrates. Assembly of a functional ubiquitin ligase (E3) complex poised for Ub transfer
Jonathan N, Pruneda +4 more
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Frontiers in Oncology, 2020 Protein ubiquitination is essential for multiple physiological processes through regulating the stability or function of target proteins and has been found to play critical roles in human cancers.
Yi Zhang +3 more
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Global Screening of LUBAC and OTULIN Interacting Proteins by Human Proteome Microarray
Frontiers in Cell and Developmental Biology, 2021 Linear ubiquitination is a reversible posttranslational modification, which plays key roles in multiple biological processes. Linear ubiquitin chain assembly complex (LUBAC) catalyzes linear ubiquitination, while the deubiquitinase OTULIN (OTU ...
Lijie Zhou +9 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
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PLoS ONE, 2020 LAT molecules defective in ubiquitination have an increased half-life and induce enhanced signaling when expressed in T cells. In this study, we have examined the role of ubiquitination in regulating LAT endocytosis, recycling, and degradation in resting
Lakshmi Balagopalan +6 more
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mUbiSiDa: a comprehensive database for protein ubiquitination sites in mammals. [PDF]
PLoS ONE, 2014 MOTIVATION: Protein ubiquitination is one of the important post-translational modifications by attaching ubiquitin to specific lysine (K) residues in target proteins, and plays important regulatory roles in many cell processes.
Tong Chen +6 more
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