Results 31 to 40 of about 143,768 (336)
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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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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Role of RING-Type E3 Ubiquitin Ligases in Inflammatory Signalling and Inflammatory Bowel Disease
Mediators of Inflammation, 2020 Ubiquitination is a three-step enzymatic cascade for posttranslational protein modification. It includes the ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3).
Liguo Zhu +7 more
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Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA
Frontiers in Plant Science, 2021 Protein modification by the small ubiquitin-like modifier (SUMO) plays an important role in multiple plant processes, including growth, development, and the response to abiotic stresses.
Souleimen Jmii, Laurent Cappadocia
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HECT E3 ubiquitin ligases – emerging insights into their biological roles and disease relevance
Journal of Cell Science, 2020 Homologous to E6AP C-terminus (HECT) E3 ubiquitin ligases play a critical role in various cellular pathways, including but not limited to protein trafficking, subcellular localization, innate immune response, viral infections, DNA damage responses and ...
Yaya Wang +4 more
semanticscholar +1 more source
Annual Review of Biochemistry, 1992 DNA LIGASE I .... ... ....... ...... . . . . . .. . . . .. ........ . 255 Structure. . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 255 Gene Structure and Chromosome Mapping . . . . ......... . . . . . .. . . . . .
T, Lindahl, D E, Barnes
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Molecular Medicine, 2023 The homologous to the E6-AP carboxyl terminus (HECT)-type E3 ubiquitin ligases are the selective executers in the protein ubiquitination, playing a vital role in modulation of the protein function and stability. Evidence shows the regulatory role of HECT-
Rui Zhang, Shaoqing Shi
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Cullin 3 ubiquitin ligases in cancer biology: functions and therapeutic implications
Frontiers in Oncology, 2016 Cullin-RING ubiquitin ligases are the largest E3 ligase family in eukaryotes and are multi-protein complexes. In these complexes, the Cullin protein serves as a scaffold to connect two functional modules of the ligases, the catalytic subunit and ...
Hsin-Yi eChen +2 more
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Frontiers in Oncology, 2021 Female breast cancer has become the most commonly occurring cancer worldwide. Although it has a good prognosis under early diagnosis and appropriate treatment, breast cancer metastasis drastically causes mortality.
Yingshuang Wang +8 more
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Ubiquitin ligases and beyond [PDF]
BMC Biology, 2012 In a review published in 2004 [1] and that still repays reading today, Cecile Pickart traced the evolution of research on ubiquitination from its origins in the proteasomal degradation of proteins through the revelation that it has a central role in cell cycle regulation and the recognition of regulatory roles for ubiquitin in intracellular membrane ...
Đikić, Ivan, Robertson, Miranda
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