Results 1 to 10 of about 77,505 (293)
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
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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.
Jinyao Zhao, Yang Wang
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Molecular Microbiology, 2001 DNA ligases join breaks in the phosphodiester backbone of DNA molecules and are used in many essential reactions within the cell. All DNA ligases follow the same reaction mechanism, but they may use either ATP or NAD+ as a cofactor. All Bacteria (eubacteria) contain NAD+‐dependent DNA ligases, and the uniqueness of these enzymes to Bacteria makes them ...
Wilkinson, A, Day, J, Bowater, R
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Thermostable DNA ligases from hyperthermophiles in biotechnology [PDF]
Frontiers in Microbiology, 2023 DNA ligase is an important enzyme ubiquitous in all three kingdoms of life that can ligate DNA strands, thus playing essential roles in DNA replication, repair and recombination in vivo.
Jingru Shi +3 more
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E3 ubiquitin ligases in bone homeostasis: from regulatory mechanisms to skeletal diseases and therapeutic targeting [PDF]
Frontiers in Cell and Developmental BiologyE3 ubiquitin ligases are key determinants of substrate specificity within the ubiquitin–proteasome system and have emerged as important regulators of skeletal biology.
Yutong Zhao +4 more
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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.
Wuxiyar Otkur, Haifeng Zhao, Yun Lu
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Ubiquitination mediated by RING-type E3 ligases in the progression of digestive system tumors: mechanistic insights and potential therapeutic strategies [PDF]
Frontiers in Cell and Developmental BiologyUbiquitination is a core mechanism for the precise regulation of protein fate, closely related to the occurrence and development of many diseases. As the most critical enzymes in the ubiquitination process, really interesting new gene (RING)-type E3 ...
Yuwei Wu +3 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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E3 ubiquitin ligases: structural diversity, dysregulation in disease, and their emerging role in targeted therapeutic strategies [PDF]
Frontiers in Molecular BiosciencesThe Ubiquitin-Proteasome System (UPS) is a key mechanism of cellular homeostasis. A central part of this mechanism is E3 ubiquitin ligases, which selectively direct proteins to be ubiquitinated for degradation via the UPS.
Srineevas Sriram +2 more
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HERC Ubiquitin Ligases in Cancer [PDF]
Cancers, 2020 HERC proteins are ubiquitin E3 ligases of the HECT family. The HERC subfamily is composed of six members classified by size into large (HERC1 and HERC2) and small (HERC3–HERC6). HERC family ubiquitin ligases regulate important cellular processes, such as neurodevelopment, DNA damage response, cell proliferation, cell migration, and immune responses ...
Joan Sala-Gaston +7 more
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