ArticleNucleic acids research2002
Molecular interactions of human Exo1 with DNA.
Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
35 citing papers in PubMed, 1 synthesis or guideline pooled it, 75 citations in OpenAlex.
- The significance of Exo1 K589E polymorphism on cancer susceptibility: evidence based on a meta-analysis.PloS one · 2014Pooled it
- DNA polymerase I: structure, activity, and function in bacterial DNA replication and repair.Critical reviews in biochemistry and molecular biology · 2026Review
- EXO1 as a therapeutic target for Fanconi Anaemia, ZRSR2 and BRCA1-A complex deficient cancers.Nature communications · 2025Article
- Insight into meiotic DNA end resection: Mechanisms and regulation.DNA repair · 2025Review
- Biochemical Mechanisms of Genetic Recombination and DNA Repair.Annual review of biochemistry · 2025Review
- Explore the dominant factor in prime editing via a view of DNA processing.Synthetic and systems biotechnology · 2023Article
- Exo1 protects DNA nicks from ligation to promote crossover formation during meiosis.PLoS biology · 2023Article
- Mechanisms of Genome Maintenance in Plants: Playing It Safe With Breaks and Bumps.Frontiers in genetics · 2021Review
- Intrinsic Strand-Incision Activity of Human UNG: Implications for Nick Generation in Immunoglobulin Gene Diversification.Frontiers in immunology · 2021Article
- Molecular structures and mechanisms of DNA break processing in mouse meiosis.Genes & development · 2020Article
- MutLγ promotes repeat expansion in a Fragile X mouse model while EXO1 is protective.PLoS genetics · 2018Article
- EXO1 suppresses double-strand break induced homologous recombination between diverged sequences in mammalian cells.DNA repair · 2017Article
- Interplay of catalysis, fidelity, threading, and processivity in the exo- and endonucleolytic reactions of human exonuclease I.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Endonuclease EEPD1 Is a Gatekeeper for Repair of Stressed Replication Forks.The Journal of biological chemistry · 2017Article
- Metnase Mediates Loading of Exonuclease 1 onto Single Strand Overhang DNA for End Resection at Stalled Replication Forks.The Journal of biological chemistry · 2017Article
- Proteomic Analysis Reveals a Novel Mutator S (MutS) Partner Involved in Mismatch Repair Pathway.Molecular & cellular proteomics : MCP · 2016Article
- The RecQ DNA helicase Rqh1 constrains Exonuclease 1-dependent recombination at stalled replication forks.Scientific reports · 2016Article
- Human Holliday junction resolvase GEN1 uses a chromodomain for efficient DNA recognition and cleavage.eLife · 2015Article
- EEPD1 Rescues Stressed Replication Forks and Maintains Genome Stability by Promoting End Resection and Homologous Recombination Repair.PLoS genetics · 2015Article
- Exonuclease 1-dependent and independent mismatch repair.DNA repair · 2015Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Human Exo1 is a member of the RAD2 nuclease family with roles in replication, repair and recombination. Despite sharing significant amino acid sequence homology, the RAD2 proteins exhibit disparate nuclease properties and biological functions. In order to identify elements that dictate substrate selectivity within the RAD2 family, we sought to identify residues key to Exo1 nuclease activity and to characterize the molecular details of the human Exo1-DNA interaction. Site-specific mutagenesis studies demonstrate that amino acids D78, D173 and D225 are critical for Exo1 nuclease function. In addition, we show that the chemical nature of the 5'-terminus has a major impact on Exo1 nuclease efficiency, with a 5'-phosphate group stimulating degradation 10-fold and a 5'-biotin inhibiting degradation 10-fold (relative to a 5'-hydroxyl moiety). An abasic lesion located within a substrate DNA strand impedes Exo1 nucleolytic degradation, and a 5'-terminal abasic residue reduces nuclease efficiency 2-fold. Hydroxyl radical footprinting indicates that Exo1 binds predominantly along the minor groove of flap DNA, downstream of the junction. As will be discussed, our results favor the notion that the single-stranded DNA structure is pinched by the helical arch of the protein and not threaded through this key recognition loop. Furthermore, our studies indicate that significant, presumably biologically relevant, differences exist between the active site dynamics of Exo1 and Fen1.
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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.