Results 11 to 20 of about 39,029 (256)

Ubiquitination and De-Ubiquitination in the Synthesis of Cow Milk Fat: Reality and Prospects

open access: yesMolecules
Ubiquitination modifications permit the degradation of labelled target proteins with the assistance of proteasomes and lysosomes, which is the main protein degradation pathway in eukaryotic cells.
Rui Gao   +7 more
doaj   +2 more sources

PKC-Dependent GlyT1 Ubiquitination Occurs Independent of Phosphorylation: Inespecificity in Lysine Selection for Ubiquitination. [PDF]

open access: yesPLoS 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   +2 more sources

SCUD: Saccharomyces Cerevisiae Ubiquitination Database [PDF]

open access: yesBMC 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]

open access: yesCell 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]

open access: yesCurrent 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]

open access: yesCell, 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, Sagar   +6 more
openaire   +3 more sources

A versatile plasmid system for reconstitution and analysis of mammalian ubiquitination cascades in yeast [PDF]

open access: yes, 2017
Ubiquitination is a posttranslational protein modification that regulates most aspects of cellular life. The sheer number of ubiquitination enzymes that are present in a mammalian cell, over 700 in total, has thus far hampered the analysis of distinct ...
Rossella Avagliano Trezza   +3 more
core   +2 more sources

Using Ubiquitin Binders to Decipher the Ubiquitin Code [PDF]

open access: yesTrends 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   +3 more sources

Generation and physiological roles of linear ubiquitin chains [PDF]

open access: yes, 2012
Ubiquitination now ranks with phosphorylation as one of the best-studied post-translational modifications of proteins with broad regulatory roles across all of biology.
Iwai Kazuhiro   +11 more
core   +1 more source

The Ubiquitination Machinery of the Ubiquitin System [PDF]

open access: yesThe 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.
openaire   +4 more sources

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