ReviewOrganic & biomolecular chemistry2014
Mechanisms for enzymatic cleavage of the N-glycosidic bond in DNA.
Review in Organic & biomolecular chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
38 citing papers in PubMed, 76 citations in OpenAlex.
- Robust excision of different purine lesions by homologs thymine DNA glycosylase and mismatch-specific uracil DNA-glycosylase.The Journal of biological chemistry · 2026Article
- Structural basis for uracil removal from DNA by human SMUG1.Nature communications · 2026Article
- Postmortem Stability Analysis of Lipids and Polar Metabolites in Human, Rat, and Mouse Brains.Biomolecules · 2025Article
- A Method for Constructing Nucleosome Arrays with Spatially Defined Histone PTMs and DNA Damage.Angewandte Chemie (International ed. in English) · 2025Article
- Structural and functional coupling in cross-linking uracil-DNA glycosylase UDGX.Bioscience reports · 2024Article
- Mechanism of substrate hydrolysis by the human nucleotide pool sanitiser DNPH1.Nature communications · 2023Article
- Structural and functional characterization of the cytotoxic protein ledodin, an atypical ribosome-inactivating protein from shiitake mushroom (Lentinula edodes).Protein science : a publication of the Protein Society · 2023Article
- Experimental and computational snapshots of C-C bond formation in a C-nucleoside synthase.Open biology · 2023Article
- Computational investigations on target-site searching and recognition mechanisms by thymine DNA glycosylase during DNA repair process.Acta biochimica et biophysica Sinica · 2022Review
- Kinetic Analysis of the Effect ofBiochemistry · 2022Article
- Base excision repair system targeting DNA adducts of trioxacarcin/LL-D49194 antibiotics for self-resistance.Nucleic acids research · 2022Article
- Article
- Interaction of Thymine DNA Glycosylase with Oxidised 5-Methyl-cytosines in Their Amino- and Imino-Forms.Molecules (Basel, Switzerland) · 2021Article
- Structural Insights into the Mechanism of Base Excision by MBD4.Journal of molecular biology · 2021Article
- Atomic resolution of short-range sliding dynamics of thymine DNA glycosylase along DNA minor-groove for lesion recognition.Nucleic acids research · 2021Article
- Nucleosomal embedding reshapes the dynamics of abasic sites.Scientific reports · 2020Article
- Excision of 5-Carboxylcytosine by Thymine DNA Glycosylase.Journal of the American Chemical Society · 2019Article
- Acetylation of the histone H3 tail domain regulates base excision repair on higher-order chromatin structures.Scientific reports · 2019Article
- Synthesis of 5-Dihydroxyboryluridine Phosphoramidite and Its Site-Specific Incorporation into Oligonucleotides for Probing Thymine DNA Glycosylase.Organic letters · 2019Article
- Emerging Roles of DNA Glycosylases and the Base Excision Repair Pathway.Trends in biochemical sciences · 2019Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
DNA glycosylases remove damaged or enzymatically modified nucleobases from DNA, thereby initiating the base excision repair (BER) pathway, which is found in all forms of life. These ubiquitous enzymes promote genomic integrity by initiating repair of mutagenic and/or cytotoxic lesions that arise continuously due to alkylation, deamination, or oxidation of the normal bases in DNA. Glycosylases also perform essential roles in epigenetic regulation of gene expression, by targeting enzymatically-modified forms of the canonical DNA bases. Monofunctional DNA glycosylases hydrolyze the N-glycosidic bond to liberate the target base, while bifunctional glycosylases mediate glycosyl transfer using an amine group of the enzyme, generating a Schiff base intermediate that facilitates their second activity, cleavage of the DNA backbone. Here we review recent advances in understanding the chemical mechanism of monofunctional DNA glycosylases, with an emphasis on how the reactions are influenced by the properties of the nucleobase leaving-group, the moiety that varies across the vast range of substrates targeted by these enzymes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.