Results 21 to 30 of about 117,949 (359)

Role of the deubiquitylating enzyme DmUsp5 in coupling ubiquitin equilibrium to development and apoptosis in Drosophila melanogaster. [PDF]

PLoS ONE, 2015
Protein ubiquitylation is a dynamic process that affects the function and stability of proteins and controls essential cellular processes ranging from cell proliferation to cell death. This process is regulated through the balanced action of E3 ubiquitin
Levente Kovács, Olga Nagy, Margit Pál, Andor Udvardy, Octavian Popescu, Péter Deák   +5 more
doaj   +1 more source

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, Ivan Dikic, Sissy Kalayil, Sagar Bhogaraju, Ivan Matic, Florian Bonn, Yaobin Liu, Thomas Colby   +7 more
openaire   +4 more sources

Translocation of polyubiquitinated protein substrates by the hexameric Cdc48 ATPase

bioRxiv, 2021
The hexameric Cdc48 ATPase (p97 or VCP in mammals) cooperates with its cofactor Ufd1/Npl4 to extract polyubiquitinated proteins from membranes or macromolecular complexes for degradation by the proteasome.
Zhejian Ji, Hao Li, D. Peterle, J. Paulo, S. Ficarro, T. Wales, J. Marto, S. Gygi, J. Engen, T. Rapoport   +9 more
semanticscholar   +1 more source

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, Alina Kozoriz, Solange Desagher, Iréna Lassot   +3 more
openaire   +5 more sources

Mechanism of selective recognition of Lys48-linked polyubiquitin by macrocyclic peptide inhibitors of proteasomal degradation

Nature Communications, 2023
Post-translational modification of proteins with polyubiquitin chains is a critical cellular signaling mechanism in eukaryotes with implications in various cellular states and processes.
Betsegaw Lemma, Di Zhang, Ganga B. Vamisetti, Bryan G. Wentz, Hiroaki Suga, Ashraf Brik, Jacek Lubkowski, David Fushman   +7 more
doaj   +1 more source

Regulation of the linear ubiquitination of STAT1 controls antiviral interferon signaling

Nature Communications, 2020
LUBAC is involved in adding linear ubiquitin chains to important immune signaling proteins. Here the authors show that this mechanism is effective in inhibiting STAT1-mediated interferon signaling, and that the deubiquitinase OTULIN can remove these ...
Yibo Zuo, Qian Feng, Lincong Jin, Fan Huang, Ying Miao, Jin Liu, Ying Xu, Xiangjie Chen, Hongguang Zhang, Tingting Guo, Yukang Yuan, Liting Zhang, Jun Wang, Hui Zheng   +13 more
doaj   +1 more source

Ubiquitin-related modifiers of Arabidopsis thaliana influence root development. [PDF]

PLoS ONE, 2014
Ubiquitins are small peptides that allow for posttranslational modification of proteins. Ubiquitin-related modifier (URM) proteins belong to the class of ubiquitin-like proteins. A primary function of URM proteins has been shown to be the sulfur transfer
Florian John, Matthias Philipp, Ruth-Maria Leiber, Sanae Errafi, Christoph Ringli   +4 more
doaj   +1 more source

Ubiquitin modifications [PDF]

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
openaire   +2 more sources

Regulation of Wnt Signaling through Ubiquitination and Deubiquitination in Cancers

International Journal of Molecular Sciences, 2020
The Wnt signaling pathway plays important roles in embryonic development, homeostatic processes, cell differentiation, cell polarity, cell proliferation, and cell migration via the β-catenin binding of Wnt target genes.
Hong-Beom Park, Ju-Won Kim, K. Baek
semanticscholar   +1 more source