ArticleStructure (London, England : 1993)2013
Structural characterization of a mouse ortholog of human NEIL3 with a marked preference for single-stranded DNA.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
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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
41 citing papers in PubMed, 53 citations in OpenAlex.
- A unified catalytic mechanism in bifunctional DNA glycosylases with an evolutionarily conserved aspartate-lysine dyad.Nature communications · 2026Article
- DNA binding and lesion recognition by the bacterial interstrand DNA crosslink glycosylase AlkX.EMBO reports · 2026Article
- DNA binding and lesion recognition by the bacterial interstrand DNA crosslink glycosylase AlkX.bioRxiv : the preprint server for biology · 2025Article
- Review
- Structural and biochemical insights into NEIL2's preference for abasic sites.Nucleic acids research · 2023Article
- DNA polymerase θ-mediated repair of high LET radiation-induced complex DNA double-strand breaks.Nucleic acids research · 2023Article
- Mycobacterial helicase Lhr abets resistance to DNA crosslinking agents mitomycin C and cisplatin.Nucleic acids research · 2023Article
- Pan-Cancer Landscape of NEIL3 in Tumor Microenvironment: A Promising Predictor for Chemotherapy and Immunotherapy.Cancers · 2022Article
- Biological Functions of the DNA Glycosylase NEIL3 and Its Role in Disease Progression Including Cancer.Cancers · 2022Review
- Model of abasic site DNA cross-link repair; from the architecture of NEIL3 DNA binding domains to the X-structure model.Nucleic acids research · 2022Article
- Article
- A Low-Activity Polymorphic Variant of Human NEIL2 DNA Glycosylase.International journal of molecular sciences · 2022Article
- Excision of Oxidatively Generated Guanine Lesions by Competitive DNA Repair Pathways.International journal of molecular sciences · 2021Review
- An autoinhibitory role for the GRF zinc finger domain of DNA glycosylase NEIL3.The Journal of biological chemistry · 2020Article
- A non-canonical role for the DNA glycosylase NEIL3 in suppressing APE1 endonuclease-mediated ssDNA damage.The Journal of biological chemistry · 2020Article
- Escherichia coli YcaQ is a DNA glycosylase that unhooks DNA interstrand crosslinks.Nucleic acids research · 2020Article
- Cooperation of the NEIL3 and Fanconi anemia/BRCA pathways in interstrand crosslink repair.Nucleic acids research · 2020Article
- Unhooking of an interstrand cross-link at DNA fork structures by the DNA glycosylase NEIL3.DNA repair · 2020Article
- Emerging Roles of DNA Glycosylases and the Base Excision Repair Pathway.Trends in biochemical sciences · 2019Review
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Endonuclease VIII-like 3 (Neil3) is a DNA glycosylase of the base excision repair pathway that protects cells from oxidative DNA damage by excising a broad spectrum of cytotoxic and mutagenic base lesions. Interestingly, Neil3 exhibits an unusual preference for DNA with single-stranded regions. Here, we report the 2.0 Å crystal structure of a Neil3 enzyme. Although the glycosylase region of mouse Neil3 (MmuNeil3Δ324) exhibits the same overall fold as that of other Fpg/Nei proteins, it presents distinct structural features. First, MmuNeil3Δ324 lacks the αF-β9/10 loop that caps the flipped-out 8-oxoG in bacterial Fpg, which is consistent with its inability to cleave 8-oxoguanine. Second, Neil3 not only lacks two of the three void-filling residues that stabilize the opposite strand, but it also harbors negatively charged residues that create an unfavorable electrostatic environment for the phosphate backbone of that strand. These structural features provide insight into the substrate specificity and marked preference of Neil3 for ssDNA.
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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.