ReviewProgress in molecular biology and translational science2012
The Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damage.
Review in Progress in molecular biology and translational science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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
65 citing papers in PubMed.
- Mechanisms of search for specific sites in DNA by DNA-binding proteins.Biochemistry and biophysics reports · 2026Review
- The Link Between Human Alkyladenine DNA Glycosylase and Cancer Development.International journal of molecular sciences · 2025Review
- Development and characterization of a novel NEIL1 nanobody.DNA repair · 2025Article
- Impact of Ultra-High-Dose-Rate Irradiation on DNA: Single-Strand Breaks and Base Damage.International journal of molecular sciences · 2025Article
- Artificial targeting of the NEIL1 DNA glycosylase to the mitochondria.Environmental and molecular mutagenesis · 2024Article
- An Insight into the Mechanism of DNA Cleavage by DNA Endonuclease from the Hyperthermophilic ArchaeonInternational journal of molecular sciences · 2024Article
- Deciphering the crystal structure of a novel nanobody against the NEIL1 DNA glycosylase.Acta crystallographica. Section D, Structural biology · 2024Article
- ELISL: early-late integrated synthetic lethality prediction in cancer.Bioinformatics (Oxford, England) · 2024Article
- Metagenome mining and functional analysis reveal oxidized guanine DNA repair at the Lost City Hydrothermal Field.PloS one · 2024Article
- Structural and biochemical insights into NEIL2's preference for abasic sites.Nucleic acids research · 2023Article
- The H2TH-like motif of the Escherichia coli multifunctional protein KsgA is required for DNA binding involved in DNA repair and the suppression of mutation frequencies.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2023Article
- The 2Ih andMolecules (Basel, Switzerland) · 2023Article
- The SMC-like RecN protein is at the crossroads of several genotoxic stress responses inFrontiers in microbiology · 2023Article
- Article
- Biological Functions of the DNA Glycosylase NEIL3 and Its Role in Disease Progression Including Cancer.Cancers · 2022Review
- Noncatalytic Domains in DNA Glycosylases.International journal of molecular sciences · 2022Review
- Colon fibroblasts from Pirc rats (F344/NTac-ApcInternational journal of cancer · 2022Article
- Novel interaction interfaces mediate the interaction between the NEIL1 DNA glycosylase and mitochondrial transcription factor A.Frontiers in cell and developmental biology · 2022Article
- Structural and Evolutionary Adaptations of Nei-Like DNA Glycosylases Proteins Involved in Base Excision Repair of Oxidative DNA Damage in Vertebrates.Oxidative medicine and cellular longevity · 2022Article
- Review
5 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
During the initial stages of the base excision DNA repair pathway, DNA glycosylases are responsible for locating and removing the majority of endogenous oxidative base lesions. The bifunctional formamidopyrimidine DNA glycosylase (Fpg) and endonuclease VIII (Nei) are members of the Fpg/Nei family, one of the two families of glycosylases that recognize oxidized DNA bases, the other being the HhH/GPD (or Nth) superfamily. Structural and biochemical developments over the past decades have led to novel insights into the mechanism of damage recognition by the Fpg/Nei family of enzymes. Despite the overall structural similarity among members of this family, these enzymes exhibit distinct features that make them unique. This review summarizes the current structural knowledge of the Fpg/Nei family members, emphasizes their substrate specificities, and describes how these enzymes search for lesions.
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