Results 11 to 20 of about 77,898 (323)
DNA ligases as therapeutic targets. [PDF]
Transl Cancer Res, 2013 During DNA replication, DNA joining events link Okazaki fragments on the lagging strand. In addition, they are required to repair DNA single- and double-strand breaks and to complete repair events initiated by the excision of mismatched and damaged bases. In human cells, there are three genes encoding DNA ligases.
Tomkinson AE, Howes TR, Wiest NE.
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SUMO chain formation is required for response to replication arrest in S. pombe [PDF]
, 2009 SUMO is a ubiquitin-like protein that is post-translationally attached to one or more lysine residues on target proteins. Despite having only 18% sequence identity with ubiquitin, SUMO contains the conserved betabetaalphabetabetaalphabeta fold present in
A Gorg +41 more
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Identification of Novel Inhibitors of Escherichia coli DNA Ligase (LigA)
Molecules, 2021 Present in all organisms, DNA ligases catalyse the formation of a phosphodiester bond between a 3′ hydroxyl and a 5′ phosphate, a reaction that is essential for maintaining genome integrity during replication and repair.
Arqam Alomari +10 more
doaj +1 more source
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
doaj +1 more source
Annual Review of Biochemistry, 1992 DNA LIGASE I .... ... ....... ...... . . . . . .. . . . .. ........ . 255 Structure. . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 255 Gene Structure and Chromosome Mapping . . . . ......... . . . . . .. . . . . .
Deborah E. Barnes, Tomas Lindahl
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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
openaire +3 more sources
Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications [PDF]
, 2012 Conjugation of ubiquitin to proteins (ubiquitylation) has emerged to be one of the most crucial post-translational modifications controlling virtually all cellular processes.
Fulda, Simone +2 more
core +2 more sources
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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