ArticleBiomolecules2012
Human DNA Glycosylase NEIL1's Interactions with Downstream Repair Proteins Is Critical for Efficient Repair of Oxidized DNA Base Damage and Enhanced Cell Survival.
Article in Biomolecules, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 40 citations in OpenAlex.
- Molecular Duality of OGG1: From Genomic Guardian to Redox-Sensitive Modulator in Diseases.Antioxidants (Basel, Switzerland) · 2025Review
- Protein-Protein Interactions in Base Excision Repair.Biomolecules · 2025Review
- Development and characterization of a novel NEIL1 nanobody.DNA repair · 2025Article
- Research progress on the role of the NEIL family in cancer.Frontiers in cell and developmental biology · 2025Review
- Deciphering the crystal structure of a novel nanobody against the NEIL1 DNA glycosylase.Acta crystallographica. Section D, Structural biology · 2024Article
- The Impact of Human DNA Glycosylases on the Activity of DNA Polymerase β toward Various Base Excision Repair Intermediates.International journal of molecular sciences · 2023Article
- New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts.NAR genomics and bioinformatics · 2023Article
- Noncatalytic Domains in DNA Glycosylases.International journal of molecular sciences · 2022Review
- OGG1 in Lung-More than Base Excision Repair.Antioxidants (Basel, Switzerland) · 2022Review
- Novel interaction interfaces mediate the interaction between the NEIL1 DNA glycosylase and mitochondrial transcription factor A.Frontiers in cell and developmental biology · 2022Article
- Sirt3 Regulates Response to Oxidative Stress by Interacting with BER Proteins in Colorectal Cancer.Genetics research · 2022Article
- Genetic variations in DNA repair gene NEIL1 associated with radiation pneumonitis risk in lung cancer patients.Molecular genetics & genomic medicine · 2021Article
- Ligand-induced gene activation is associated with oxidative genome damage whose repair is required for transcription.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- NEIL1 stimulates neurogenesis and suppresses neuroinflammation after stress.Free radical biology & medicine · 2019Article
- The C-terminal tail of the NEIL1 DNA glycosylase interacts with the human mitochondrial single-stranded DNA binding protein.DNA repair · 2018Article
- Article
- Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase.Nucleic acids research · 2017Article
- Regulation of oxidized base damage repair by chromatin assembly factor 1 subunit A.Nucleic acids research · 2017Article
- Mitochondrial (Dys) Function in Inflammaging: Do MitomiRs Influence the Energetic, Oxidative, and Inflammatory Status of Senescent Cells?Mediators of inflammation · 2017Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
NEIL1 is unique among the oxidatively damaged base repair-initiating DNA glycosylases in the human genome due to its S phase-specific activation and ability to excise substrate base lesions from single-stranded DNA. We recently characterized NEIL1's specific binding to downstream canonical repair and non-canonical accessory proteins, all of which involve NEIL1's disordered C-terminal segment as the common interaction domain (CID). This domain is dispensable for NEIL1's base excision and abasic (AP) lyase activities, but is required for its interactions with other repair proteins. Here, we show that truncated NEIL1 lacking the CID is markedly deficient in initiating in vitro repair of 5-hydroxyuracil (an oxidative deamination product of C) in a plasmid substrate compared to the wild-type NEIL1, thus suggesting a critical role of CID in the coordination of overall repair. Furthermore, while NEIL1 downregulation significantly sensitized human embryonic kidney (HEK) 293 cells to reactive oxygen species (ROS), ectopic wild-type NEIL1, but not the truncated mutant, restored resistance to ROS. These results demonstrate that cell survival and NEIL1-dependent repair of oxidative DNA base damage require interactions among repair proteins, which could be explored as a cancer therapeutic target in order to increase the efficiency of chemo/radiation treatment.
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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.