How to Inactivate Human Ubiquitin E3 Ligases by Mutation
Frontiers in Cell and Developmental Biology, 2020 E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein.
Cristina Garcia-Barcena +4 more
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Targeted Degradation of 53BP1 Using Ubiquitin Variant Induced Proximity
Biomolecules, 2022 In recent years, researchers have leveraged the ubiquitin-proteasome system (UPS) to induce selective degradation of proteins by E3 ubiquitin ligases, which has great potential as novel therapeutics for human diseases, including cancer and ...
Bayonle Aminu +4 more
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The E3 Ubiquitin Ligase MID1 Catalyzes Ubiquitination and Cleavage of Fu [PDF]
Journal of Biological Chemistry, 2014 SHH (Sonic Hedgehog)-GLI signaling plays an important role during embryogenesis and in tumorigenesis. The survival and growth of several types of cancer depend on autonomously activated SHH-GLI signaling. A protein complex containing the ubiquitin ligase MID1 and protein phosphatase 2A regulates the nuclear localization and transcriptional activity of ...
Schweiger, Susann +8 more
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Regulation of Notch signaling by E3 ubiquitin ligases [PDF]
The FEBS Journal, 2021 Notch signaling is an evolutionarily conserved pathway that is widely used for multiple cellular events during development. Activation of the Notch pathway occurs when the ligand from a neighboring cell binds to the Notch receptor and induces cleavage of the intracellular domain of Notch, which further translocates into the nucleus to activate its ...
Debdeep Dutta +3 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
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Ubiquitination, Biotech Startups, and the Future of TRIM Family Proteins: A TRIM-Endous Opportunity
Cells, 2021 Ubiquitination is a post-translational modification that has pivotal roles in protein degradation and diversified cellular processes, and for more than two decades it has been a subject of interest in the biotech or biopharmaceutical industry. Tripartite
Utsa Bhaduri, Giuseppe Merla
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The involvement of E3 ubiquitin ligases in the development and progression of colorectal cancer
Cell Death Discovery, 2023 To date, colorectal cancer (CRC) still has limited therapeutic efficacy and poor prognosis and there is an urgent need for novel targets to improve the outcome of CRC patients.
Jie Chen +8 more
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A Bacterial Platform for Studying Ubiquitination Cascades Anchored by SCF-Type E3 Ubiquitin Ligases
BiomoleculesUbiquitination is one of the most important post-translational modifications in eukaryotes. The ubiquitination cascade includes ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). The E3 ligases, responsible
Zuo-Xian Pu +9 more
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E3 Ubiquitin Ligases: Potential Therapeutic Targets for Skeletal Pathology and Degeneration
Stem Cells International, 2022 The ubiquitination-proteasome system (UPS) is crucial in regulating a variety of cellular processes including proliferation, differentiation, and survival. Ubiquitin protein ligase E3 is the most critical molecule in the UPS system.
Ruiyin Zeng +6 more
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Decoding the ubiquitin-mediated pathway of arthropod disease vectors. [PDF]
PLoS ONE, 2013 Protein regulation by ubiquitin has been extensively described in model organisms. However, characterization of the ubiquitin machinery in disease vectors remains mostly unknown.
Anthony Choy +5 more
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