Results 11 to 20 of about 51,453 (260)
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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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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Detection of ligation products of DNA linkers with 5'-OH ends by denaturing PAGE silver stain. [PDF]
PLoS ONE, 2012 To explore if DNA linkers with 5'-hydroxyl (OH) ends could be joined by commercial T4 and E. coli DNA ligase, these linkers were synthesized by using the solid-phase phosphoramidite method and joined by using commercial T4 and E. coli DNA ligases.
Feng Gao +3 more
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DNA Ligase I, the Replicative DNA Ligase [PDF]
, 2012 Multiple DNA ligation events are required to join the Okazaki fragments generated during lagging strand DNA synthesis. In eukaryotes, this is primarily carried out by members of the DNA ligase I family. The C-terminal catalytic region of these enzymes is composed of three domains: a DNA binding domain, an adenylation domain and an OB-fold domain.
Timothy R L, Howes, Alan E, Tomkinson
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Inactivating UBE2M impacts the DNA damage response and genome integrity involving multiple cullin ligases. [PDF]
PLoS ONE, 2014 Protein neddylation is involved in a wide variety of cellular processes. Here we show that the DNA damage response is perturbed in cells inactivated with an E2 Nedd8 conjugating enzyme UBE2M, measured by RAD51 foci formation kinetics and cell based DNA ...
Scott Cukras +3 more
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Biomedicines, 2023 Ubiquitination is a post-translational modification (PTM) that is involved in proteolysis, protein–protein interaction, and signal transduction. Accumulation of mutations and genomic instability are characteristic of cancer cells, and dysfunction of the ...
Hae Ryung Chang
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Novel E3 ubiquitin ligases that regulate histone protein levels in the budding yeast Saccharomyces cerevisiae. [PDF]
PLoS ONE, 2012 Core histone proteins are essential for packaging the genomic DNA into chromatin in all eukaryotes. Since multiple genes encode these histone proteins, there is potential for generating more histones than what is required for chromatin assembly.
Rakesh Kumar Singh +3 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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Thoracic Cancer, 2022 Background Lung adenocarcinoma (LUAD) is the most common subtype of non‐small cell lung cancer and has a poor prognosis. RBR E3 ubiquitin ligases are a special class of E3 ubiquitin ligases which contain three zinc‐bing domains that catalyze ubiquitin to
Hao Ding +12 more
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The regulatory roles of the E3 ubiquitin ligase NEDD4 family in DNA damage response
Frontiers in Physiology, 2022 E3 ubiquitin ligases, an important part of ubiquitin proteasome system, catalyze the covalent binding of ubiquitin to target substrates, which plays a role in protein ubiquitination and regulates different biological process. DNA damage response (DDR) is
Xinxin Lu +7 more
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