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HECT-Type E3 Ubiquitin Ligases in Cancer
Trends in Biochemical Sciences, 2019Ubiquitination, a post-translational modification that involves a covalent attachment of ubiquitin to a protein substrate, is essential for cellular homeostatic maintenance. At the end of a three-enzyme cascade, E3 ubiquitin ligases (E3s) recruit substrates and promote or directly catalyze ubiquitin transfer to targets.
Francesca Bernassola +2 more
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The HECT family of E3 ubiquitin ligases and PTEN
Seminars in Cancer Biology, 2022Members of the HECT family of E3 ubiquitin ligases have emerged as prominent regulators of PTEN function, subcellular localization and levels. In turn this unfolding regulatory network is allowing for the identification of genes directly involved in both tumorigenesis at large and cancer susceptibility syndromes. While the complexity of this regulatory
Song, Min Sup, Pandolfi, Pier Paolo
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Pseudophosphatase as E3 ubiquitin ligase inhibitor
Science Signaling, 2017The pseudophosphatase STYX prevents the substrate recognition subunit FBXW7 from binding the catalytic E3 ubiquitin ligase complex.
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E3 ubiquitin ligases in cancer and implications for therapies
Cancer and Metastasis Reviews, 2017E3 ligases are a class of enzymes that can transfer ubiquitin to substrates for their degradation, which are of importance in cellular homeostasis. Since many oncogenic or tumor-suppressive proteins are reported to be regulated by the ubiquitin-proteasome system (UPS), E3 ligases, which function as substrate interacting modules, have been attracting ...
Dong, Wang +4 more
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Role of E3 ubiquitin ligases in insulin resistance
Diabetes, Obesity and Metabolism, 2016E3 ubiquitin ligases are a large family of proteins that catalyse the ubiquitination of many proteins for degradation by the 26S proteasome. E3 ubiquitin ligases play pivotal roles in the process of insulin resistance and diabetes.
X-D, Yang, D-X, Xiang, Y-Y, Yang
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Trim45: An emerging E3 ubiquitin ligases in cancer
Cellular SignallingThe ubiquitin proteasome system is the major pathway for intracellular protein degradation and relies on ATP supply to specifically degrade misfolded or damaged proteins. The system consists of E1, E2, and E3 enzymes that mediate the ubiquitination modification of substrate proteins, followed by proteasomal recognition and degradation of the substrate ...
Huhu, Zhang +9 more
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C-Degron Mimicry Confers E3 Ligase Selectivity
Nature Reviews Molecular Cell Biology, 2023Lisa Heinke
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Ubiquitin Ligases: Guardians of Mammalian Development
Nature Reviews Molecular Cell Biology, 2022Alex N Bullock +2 more
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