SUMOylation inhibits FOXM1 activity and delays mitotic transition [PDF]
, 2014 The forkhead box transcription factor FOXM1 is an essential effector of G2/M-phase transition, mitosis and the DNA damage response. As such, it is frequently deregulated during tumorigenesis. Here we report that FOXM1 is dynamically modified by SUMO1 but
Brosens, Jan J. +13 more
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E3 Ubiquitin Ligases Neurobiological Mechanisms: Development to Degeneration
Frontiers in Molecular Neuroscience, 2017 Cells regularly synthesize new proteins to replace old or damaged proteins. Deposition of various aberrant proteins in specific brain regions leads to neurodegeneration and aging.
Arun Upadhyay +6 more
doaj +1 more source
Ubiquitination accomplished: E1 and E2 enzymes were not necessary [PDF]
, 2016 Qiu et al. (2016) show that a mono-ADP-ribosyltransferase, SdeA, from Legionella pneumophila catalyzes ADP-ribosylation of ubiquitin, allowing SdeA to modify substrate with ubiquitin in the absence of E1 and E2 ...
Huang, Danny T., Nakasone, Mark
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Role and therapeutic potential of E3s in the tumor microenvironment of hepatocellular carcinoma
Frontiers in ImmunologyHepatocellular carcinoma (HCC) is a high-incidence, poor-prognosis malignancy worldwide, requiring new strategies for treatment. Ubiquitination, especially ubiquitination through E3 ubiquitin ligases, plays an indispensable role in the development and ...
Hailin Wang +10 more
doaj +1 more source
Homo-PROTACs:bivalent small-molecule dimerizers of the VHL E3 ubiquitin ligase to induce self-degradation [PDF]
, 2017 E3 ubiquitin ligases are key enzymes within the ubiquitin proteasome system which catalyze the ubiquitination of proteins, targeting them for proteasomal degradation.
A Grosfeld +73 more
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Expanding the Toolbox of E3 Ligases for Protein Degradation: Targeting the “Undruggable” Fbw7 E3 Ligase [PDF]
The 2nd Molecules Medicinal Chemistry Symposium (MMCS): Facing Novel Challenges in Drug Discovery, 2019 Proteolysis targeting chimera molecules (PROTACS) are heterobifunctional small moleculesdesigned to induce intracellular protein degradation [...]
openaire +2 more sources
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
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F1000Research, 2020 Protein ubiquitylation is essential for the maintenance of cellular homeostasis. E3 ubiquitin ligases are key components of the enzymatic machinery catalyzing the attachment of ubiquitin to substrate proteins. Consequently, enzymatic dysfunction has been
Vishnu Balaji, Thorsten Hoppe
doaj +1 more source
TRIM5α as an E3 ubiquitin ligase
The FASEB Journal, 2009 Human immunodeficiency virus type1 (HIV‐1) efficiently infects susceptible cells and causes acquired immunodeficiency syndrome (AIDS) in humans. Although HIV can also enter the cells of Old World monkeys, it encounters a block before reverse transcription.
Makoto Tanaka +2 more
openaire +1 more source
The proteasome lid triggers COP9 signalosome activity during the transition of Saccharomyces cerevisiae cells into quiescence. [PDF]
, 2019 The class of Cullin–RING E3 ligases (CRLs) selectively ubiquitinate a large portion of proteins targeted for proteolysis by the 26S proteasome. Before degradation, ubiquitin molecules are removed from their conjugated proteins by deubiquitinating enzymes,
Bramasole, Lylan +8 more
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