Results 11 to 20 of about 191,822 (309)
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
core +7 more sources
PKC-Dependent GlyT1 Ubiquitination Occurs Independent of Phosphorylation: Inespecificity in Lysine Selection for Ubiquitination. [PDF]
PLoS ONE, 2015 Neurotransmitter transporter ubiquitination is emerging as the main mechanism for endocytosis and sorting of cargo into lysosomes. In this study, we demonstrate PKC-dependent ubiquitination of three different isoforms of the glycine transporter 1 (GlyT1).
Susana P Barrera +6 more
doaj +3 more sources
Non-degradative Ubiquitination of Protein Kinases. [PDF]
PLoS Computational Biology, 2016 Growing evidence supports other regulatory roles for protein ubiquitination in addition to serving as a tag for proteasomal degradation. In contrast to other common post-translational modifications, such as phosphorylation, little is known about how non ...
K Aurelia Ball +6 more
doaj +4 more sources
SCUD:
BMC Genomics, 2008 Background Ubiquitination is an important post-translational modification involved in diverse biological processes. Therefore, genomewide representation of the ubiquitination system for a species is important. Description SCUD is a web-based database for
Jung Jin Woo +4 more
doaj +2 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.
Joanna, Bloom, Michele, Pagano
openaire +2 more sources
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
Computational prediction of protein ubiquitination sites mapping on Arabidopsis thaliana [PDF]
, 2020 Among the protein post-translational modifications (PTMs), ubiquitination is considered as one of the most significant processes which can regulate the cellular functions and various diseases.
Ahmed, Fee Faysal +5 more
core +1 more source
Analysis of Flagellar Protein Ubiquitination [PDF]
, 2013 Flagella/cilia are conserved organelles existing in unicellular protists and multicellular animals, where they perform essential motile and sensory functions.
Huan Long +3 more
core +3 more sources
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
openaire +2 more sources
On the possibility that bond strain is the mechanism of RING E3 activation in the E2-catalyzed ubiquitination reaction [PDF]
, 2022 Ubiquitination is a type of post translational modification wherein the small protein ubiquitin (Ub) is covalently bound to a lysine on a target protein.
Isaiah, Sumner, Jay-Anne K., Johnson
core +1 more source