ArticleOpen biology2021
Anchored linear oligonucleotides: the effective tool for the real-time measurement of uracil DNA glycosylase activity.
Article in Open biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- A hybrid RNA-based reporter assay for robust quantification of cytidine deaminase activity.Nucleic acids research · 2026Article
- A Rapid Approach for Identifying Cell Lines Lacking Functional Cytidine Deaminase.International journal of molecular sciences · 2025Article
- The kinetics of uracil-N-glycosylase distribution inside replication foci.Scientific reports · 2025Article
- A new technique for the analysis of metabolic pathways of cytidine analogues and cytidine deaminase activities in cells.Scientific reports · 2023Article
- Anchored linear oligonucleotides: the effective tool for the real-time measurement of uracil DNA glycosylase activity.Open biology · 2021Article
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5 authors.
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Abstract
Base excision repair is one of the important DNA repair mechanisms in cells. The fundamental role in this complex process is played by DNA glycosylases. Here, we present a novel approach for the real-time measurement of uracil DNA glycosylase activity, which employs selected oligonucleotides immobilized on the surface of magnetic nanoparticles and Förster resonance energy transfer. We also show that the approach can be performed by surface plasmon resonance sensor technology. We demonstrate that the immobilization of oligonucleotides provides much more reliable data than the free oligonucleotides including molecular beacons. Moreover, our results show that the method provides the possibility to address the relationship between the efficiency of uracil DNA glycosylase activity and the arrangement of the used oligonucleotide probes. For instance, the introduction of the nick into oligonucleotide containing the target base (uracil) resulted in the substantial decrease of uracil DNA glycosylase activity of both the bacterial glycosylase and glycosylases naturally present in nuclear lysates.
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