TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions
Computational and Structural Biotechnology Journal, 2023 Protein ubiquitination is a post-translation modification mediated by E3 ubiquitin ligases. The RING domain E3 ligases are the largest family of E3 ubiquitin ligases, they act as a scaffold, bringing the E2-ubiquitin complex and its substrate together to
Xiaohua Lou +7 more
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E3 Ubiquitin Ligases as Cancer Targets and Biomarkers
Neoplasia: An International Journal for Oncology Research, 2006 E3 ubiquitin ligases are a large family of proteins that are engaged in the regulation of the turnover and activity of many target proteins. Together with ubiquitinactivating enzyme El and ubiquitin-conjugating enzyme E2, E3 ubiquitin ligases catalyze ...
Yi Sun
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Genome-wide analysis of HECT E3 ubiquitin ligase gene family in Solanum lycopersicum
Scientific Reports, 2021 The E3 ubiquitin ligases have been known to intrigue many researchers to date, due to their heterogenicity and substrate mediation for ubiquitin transfer to the protein.
Bhaskar Sharma +2 more
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The Biological Function and Roles in Phytohormone Signaling of the F-Box Protein in Plants
Agronomy, 2021 The ubiquitin–proteasome pathway (UPP) is an important protein degradation pathway that can participate in the regulation of the physiological process of organisms by specifically removing abnormal peptides and degrading cell regulators.
Keheng Xu +5 more
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RBR E3 ubiquitin ligases: new structures, new insights, new questions [PDF]
, 2014 The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes.
Shaw, Gary S. +2 more
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Genome-Wide Identification and Expression of Xenopus F-Box Family of Proteins. [PDF]
PLoS ONE, 2015 Protein degradation via the multistep ubiquitin/26S proteasome pathway is a rapid way to alter the protein profile and drive cell processes and developmental changes.
Banu Saritas-Yildirim +3 more
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Computational and Structural Biotechnology Journal, 2022 Protein ubiquitination plays a vital role in controlling the degradation of intracellular proteins and in regulating cell signaling pathways. Functionally, E3 ubiquitin ligases control the transfer of ubiquitin to the target substrates. As a major family
Xiaohua Lou +7 more
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Research Progress on the Role of E3 Ubiquitin Ligases in Regulating the Growth, Development and Stress Response of Fruits and Vegetables [PDF]
Shipin KexueProtein ubiquitination, an important post-translational modification, plays a wide role in the life activities of eukaryotic cells. E3 ubiquitin ligases specifically recognize target proteins in the ubiquitin-proteasome degradation system and play a ...
DING Jun, LI Fujun, LI Xiao’an, ZHANG Xinhua
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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
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The role of Schizosaccharomyces pombe SUMO ligases in genome stability [PDF]
, 2007 SUMOylation is a post-translational modification that affects a large number of proteins, many of which are nuclear. While the role of SUMOylation is beginning to be elucidated, it is clear that understanding the mechanisms that regulate the process is ...
A. Skilton +44 more
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