Results 11 to 20 of about 86,842 (296)
Ubiquitin-protein ligases [PDF]
Journal of Cell Science, 2004 Post-translational covalent tagging of proteins with the 76-residue protein ubiquitin (Ub) serves many functions. Polyubiquitylated proteins are directed to the large multi-component, multi-catalytic protease the 26S proteasome.
P A, Robinson, H C, Ardley
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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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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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Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins
Frontiers in Immunology, 2021 Poxviruses have evolved a variety of innate immunity evasion mechanisms, some of which involve poxvirus-encoded E3 ubiquitin ligases and adaptor proteins.
Haoran Cui +7 more
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Scientific Reports, 2021 The sarcomere protein titin is a major determinant of cardiomyocyte stiffness and ventricular distensibility. The constant mechanical stress on titin requires well-controlled protein quality control, the exact mechanisms of which have not yet been fully ...
Erik Müller +5 more
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Expanding PROTACtable genome universe of E3 ligases
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 +9 more
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Cold Spring Harbor Protocols, 2019 DNA ligases are used chiefly to create novel combinations of nucleic acid molecules and to attach them to vectors before molecular cloning. They are either of bacterial origin or bacteriophage encoded and have different properties, as discussed here.
Michael R, Green, Joseph, Sambrook
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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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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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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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