Evidence map›Paper›PMID 35509469›Full record

ArticleChemical science2022

Molecular beacons with oxidized bases report on substrate specificity of DNA oxoguanine glycosylases.

Jingjing Sun, Nicole M Antczak, Hailey L Gahlon, Shana J Sturla

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.3field-weighted citation impact, top 50% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Jingjing SunDepartment of Health Sciences and Technology, ETH Zürich Zürich 8092 Switzerland sturlas@ethz.ch.ORCID https://orcid.org/0000-0002-6892-8177
Nicole M AntczakDepartment of Health Sciences and Technology, ETH Zürich Zürich 8092 Switzerland sturlas@ethz.ch.ORCID https://orcid.org/0000-0001-7970-0779
Hailey L GahlonDepartment of Health Sciences and Technology, ETH Zürich Zürich 8092 Switzerland sturlas@ethz.ch.ORCID https://orcid.org/0000-0003-4388-2798
Shana J SturlaDepartment of Health Sciences and Technology, ETH Zürich Zürich 8092 Switzerland sturlas@ethz.ch.ORCID https://orcid.org/0000-0001-6808-5950
ETH Zurich · CHSkidmore College · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA glycosylase enzymes recognize and remove structurally distinct modified forms of DNA bases, thereby repairing genomic DNA from chemically induced damage or erasing epigenetic marks. However, these enzymes are often promiscuous, and advanced tools are needed to evaluate and engineer their substrate specificity. Thus, in the present study, we developed a new strategy to rapidly profile the substrate specificity of 8-oxoguanine glycosylases, which cleave biologically relevant oxidized forms of guanine. We monitored the enzymatic excision of fluorophore-labeled oligonucleotides containing synthetic modifications 8-oxoG and FapyG, or G. Using this molecular beacon approach, we identified several hOGG1 mutants with higher specificity for FapyG than 8-oxoG. This approach and the newly synthesized probes will be useful for the characterization of glycosylase substrate specificity and damage excision mechanisms, as well as for evaluating engineered enzymes with altered reactivities.

Identifiers

PMID35509469
PMCPMC9007065
OpenAlexW4213102224

What OpenQuestion holds

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Registered trials

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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.