ArticleNature chemical biology2008
Unnatural substrates reveal the importance of 8-oxoguanine for in vivo mismatch repair by MutY.
Article in Nature chemical biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
The trial behind it
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Who cites it
30 citing papers in PubMed.
- Structural Basis for Nucleobase Activation by the Adenine DNA Glycosylase MutY.Chembiochem : a European journal of chemical biology · 2026Article
- Structural Basis for Nucleobase Activation by the Adenine DNA Glycosylase MutY.bioRxiv : the preprint server for biology · 2026Article
- Unlocking the chemistry facilitated by enzymes that process nucleic acids using quantum mechanical and combined quantum mechanics-molecular mechanics techniques.Pure and applied chemistry. Chimie pure et appliquee · 2025Review
- FSHing for DNA Damage: Key Features of MutY Detection of 8-Oxoguanine:Adenine Mismatches.Accounts of chemical research · 2024Review
- Cellular Repair of Synthetic Analogs of Oxidative DNA Damage Reveals a Key Structure-Activity Relationship of the Cancer-Associated MUTYH DNA Repair Glycosylase.ACS central science · 2024Article
- Mass spectrometry-based assays for assessing replicative bypass and repair of DNA alkylation in cells.RSC advances · 2023Review
- Chemical Tools for the Study of DNA Repair.Accounts of chemical research · 2022Article
- Nucleobase-modified nucleosides and nucleotides: Applications in biochemistry, synthetic biology, and drug discovery.Frontiers in chemistry · 2022Review
- Review
- Unique Hydrogen Bonding of Adenine with the Oxidatively Damaged Base 8-Oxoguanine Enables Specific Recognition and Repair by DNA Glycosylase MutY.Journal of the American Chemical Society · 2020Article
- Detection of OG:A Lesion Mispairs by MutY Relies on a Single His Residue and the 2-Amino Group of 8-Oxoguanine.Journal of the American Chemical Society · 2020Article
- 2'-Fluorinated Hydantoins as Chemical Biology Tools for Base Excision Repair Glycosylases.ACS chemical biology · 2020Article
- Structural Basis for Finding OG Lesions and Avoiding Undamaged G by the DNA Glycosylase MutY.ACS chemical biology · 2020Article
- Chemical Analysis of DNA Damage.Analytical chemistry · 2018Review
- Cellular Assays for Studying the Fe-S Cluster Containing Base Excision Repair Glycosylase MUTYH and Homologs.Methods in enzymology · 2018Article
- Structure-Activity Relationships Reveal Key Features of 8-Oxoguanine: A Mismatch Detection by the MutY Glycosylase.ACS chemical biology · 2017Article
- Repair of 8-oxoG:A mismatches by the MUTYH glycosylase: Mechanism, metals and medicine.Free radical biology & medicine · 2017Review
- Mass Spectrometry-Based Quantitative Strategies for Assessing the Biological Consequences and Repair of DNA Adducts.Accounts of chemical research · 2016Review
- Mechanisms for enzymatic cleavage of the N-glycosidic bond in DNA.Organic & biomolecular chemistry · 2014Review
- A zinc linchpin motif in the MUTYH glycosylase interdomain connector is required for efficient repair of DNA damage.Journal of the American Chemical Society · 2014Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Escherichia coli MutY has an important role in preventing mutations associated with the oxidative lesion 7,8-dihydro-8-oxo-2'-deoxyguanosine (OG) in DNA by excising adenines from OG.A mismatches as the first step of base excision repair. To determine the importance of specific steps in the base pair recognition and base removal process of MutY, we have evaluated the effects of modifications of the OG.A substrate on the kinetics of base removal, mismatch affinity and repair to G-C in an E. coli-based assay. Notably, adenine modification was tolerated in the cellular assay, whereas modification of OG resulted in minimal cellular repair. High affinity for the mismatch and efficient base removal required the presence of OG. Taken together, these results suggest that the presence of OG is a critical feature that is necessary for MutY to locate OG.A mismatches and select the appropriate adenines for excision to initiate repair in vivo before replication.
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Registered trials
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