Expanding PROTACtable genome universe of E3 ligases [PDF]
Nature Communications, 2023 Proteolysis-targeting chimera (PROTAC) and other targeted protein degradation (TPD) molecules that induce degradation by the ubiquitin-proteasome system (UPS) offer new opportunities to engage targets that remain challenging to be inhibited by ...
Yuan Liu, Mei Luo, Yamei Chen
exaly +3 more sources
E3 ubiquitin ligases: styles, structures and functions
Molecular Biomedicine, 2021 E3 ubiquitin ligases are a large family of enzymes that join in a three-enzyme ubiquitination cascade together with ubiquitin activating enzyme E1 and ubiquitin conjugating enzyme E2.
Yang Wang
exaly +2 more sources
The roles of E3 ubiquitin ligases in cancer progression and targeted therapy
Clinical and Translational Medicine, 2023 Ubiquitination is one of the most important post‐translational modifications which plays a significant role in conserving the homeostasis of cellular proteins.
Qiuping Wang, Haifeng Zhao, Yun Lu
exaly +2 more sources
The enigma of the RING-UIM E3 ligases: its transformative impact on cancer research [PDF]
Journal of Translational MedicineRING-UIM E3 ligases, a subfamily within the RING-type E3 ligases, comprise four members: RNF114, RNF125, RNF138, and RNF166. These ligases are crucial in various biological processes, including immunity, inflammation, epigenetics, and homologous ...
Ye Wang, Yue Zhao, Qi Xin, Jihong Zhang
doaj +2 more sources
E3 Ubiquitin Ligases as Cancer Targets and Biomarkers
Neoplasia, 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
exaly +3 more sources
Genetically engineered mouse models for functional studies of SKP1-CUL1-F-box-protein (SCF) E3 ubiquitin ligases [PDF]
Cell Research, 2013 The SCF (SKP1 (S-phase-kinase-associated protein 1), Cullin-1, F-box protein) E3 ubiquitin ligases, the founding member of Cullin-RING ligases (CRLs), are the largest family of E3 ubiquitin ligases in mammals.
Weihua Zhou, Wenyi Wei, Yi Sun
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BioE3 identifies specific substrates of ubiquitin E3 ligases [PDF]
Nature Communications, 2023 Hundreds of E3 ligases play a critical role in recognizing specific substrates for modification by ubiquitin (Ub). Separating genuine targets of E3s from E3-interactors remains a challenge. We present BioE3, a powerful approach for matching substrates to
Orhi Barroso-Gomila +14 more
doaj +2 more sources
Advances of E3 ligases in lung cancer [PDF]
Biochemistry and Biophysics ReportsLung cancer is a leading cause of cancer-related death, and the most common type of lung cancer is non-small cell lung cancer, which accounts for approximately 85 % of lung cancer diagnoses.
Jingwen Yu, Yiqi Zhao, Yue Xie
doaj +2 more sources
Discovering Uncharted Binding Pockets on E3 Ligases Leads to the Identification of FBW7 Allosteric Modulators [PDF]
Advanced ScienceE3 ligases are key regulators of the ubiquitin‐proteasome system (UPS) and have emerged as attractive drug target candidates for precise therapeutic intervention.
Míriam Martínez‐Cartró +13 more
doaj +2 more sources
Erioflorin stabilizes the tumor suppressor Pdcd4 by inhibiting its interaction with the E3-ligase β-TrCP1 [PDF]
, 2012 Loss of the tumor suppressor Pdcd4 was reported for various tumor entities and proposed as a prognostic marker in tumorigenesis. We previously characterized decreased Pdcd4 protein stability in response to mitogenic stimuli, which resulted from p70S6K1 ...
Bajer, Magdalena M. +11 more
core +19 more sources