ArticleDNA repair2020
Recognition of DNA adducts by edited and unedited forms of DNA glycosylase NEIL1.
Article in DNA repair, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.
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Who cites it
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.
- Destabilizing the genome as a therapeutic strategy to enhance response to immune checkpoint blockade: a systematic review of clinical trials evidence from solid and hematological tumors.Frontiers in pharmacology · 2023Pooled it
- OGG1 and MUTYH DNA Glycosylases, the Dynamic Duo Against 8-Oxoguanine DNA Lesion: Structure, Regulation, and Novel Emerging Roles.Biomolecules · 2026Review
- Development and characterization of a novel NEIL1 nanobody.DNA repair · 2025Article
- Role of NEIL1 in genome maintenance.DNA repair · 2025Review
- Aflatoxin BEnvironmental and molecular mutagenesis · 2025Article
- DNA repair and disease: insights from the human DNA glycosylase NEIL family.Experimental & molecular medicine · 2025Review
- Research progress on the role of the NEIL family in cancer.Frontiers in cell and developmental biology · 2025Review
- Functional characterization of single nucleotide polymorphic variants of DNA repair enzyme NEIL1 in South Asian populations.DNA repair · 2024Article
- Frequencies and spectra of aflatoxin BNAR molecular medicine · 2024Article
- Exploring DNA Damage and Repair Mechanisms: A Review with Computational Insights.Biotech (Basel (Switzerland)) · 2024Review
- Functional analyses of single nucleotide polymorphic variants of the DNA glycosylase NEIL1 in sub-Saharan African populations.DNA repair · 2023Article
- Spatial mapping of the DNA adducts in cancer.DNA repair · 2023Review
- Base excision repair of the N-(2-deoxy-d-erythro-pentofuranosyl)-urea lesion by the hNEIL1 glycosylase.Nucleic acids research · 2023Article
- Synthesis and Characterization ofACS omega · 2023Article
- Characterization of a Novel Thermostable DNA Lyase Used To Prepare DNA for Next-Generation Sequencing.Chemical research in toxicology · 2023Article
- Article
- NEIL1 Recoding due to RNA Editing Impacts Lesion-Specific Recognition and Excision.Journal of the American Chemical Society · 2022Article
- Uracil-DNA Glycosylase Assay by Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry Analysis.Journal of visualized experiments : JoVE · 2022Article
- Measurement of deaminated cytosine adducts in DNA using a novel hybrid thymine DNA glycosylase.The Journal of biological chemistry · 2022Article
- Dynamics of 5R-Tg Base Flipping in DNA Duplexes Based on Simulations─Agreement with Experiments and Beyond.Journal of chemical information and modeling · 2022Article
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Authors and funding
13 authors at 5 institutions in 1 country.
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Abstract
Pre-mRNA encoding human NEIL1 undergoes editing by adenosine deaminase ADAR1 that converts a single adenosine to inosine, and this conversion results in an amino acid change of lysine 242 to arginine. Previous investigations of the catalytic efficiencies of the two forms of the enzyme revealed differential release of thymine glycol (ThyGly) from synthetic oligodeoxynucleotides, with the unedited form, NEIL1 K242 being ≈30-fold more efficient than the edited NEIL1 K242R. In contrast, when these enzymes were reacted with oligodeoxynucleotides containing guanidinohydantoin or spiroiminohydantoin, the edited K242R form was ≈3-fold more efficient than the unedited NEIL1. However, no prior studies have investigated the efficiencies of these two forms of NEIL1 on either high-molecular weight DNA containing multiple oxidatively-induced base damages, or oligodeoxynucleotides containing a bulky alkylated formamidopyrimidine. To understand the extent of changes in substrate recognition, γ-irradiated calf thymus DNA was treated with either edited or unedited NEIL1 and the released DNA base lesions analyzed by gas chromatography-tandem mass spectrometry. Of all the measured DNA lesions, imidazole ring-opened 4,6-diamino-5-formamidopyrimidine (FapyAde) and 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua) were preferentially released by both NEIL1 enzymes with K242R being ≈1.3 and 1.2-fold more efficient than K242 on excision of FapyAde and FapyGua, respectively. Consistent with the prior literature, large differences (≈7.5 to 12-fold) were measured in the excision of ThyGly from genomic DNA by the unedited versus edited NEIL1. In contrast, the edited NEIL1 was more efficient (≈3 to 5-fold) on release of 5-hydroxycytosine. Excision kinetics on DNA containing a site-specific aflatoxin B
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