Evidence map›Paper›PMID 41507603›Full record

ArticleNature structural & molecular biology2026

Redox-driven ADAR1 activation promotes Okazaki fragment maturation and DNA replication integrity.

Bin Chen, Guangchao Sun, Jake A Kloeber, Huaping Xiao, Yaobin Ouyang, Fei Zhao, Ya Li, Shilin Xu, Sonja Dragojevic, Zheming Wu and 14 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. ADAR1 is an editor of DNA replication forks.Nature structural & molecular biology · 2026
    Article
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

24 authors.

Bin Chen *Department of Oncology, Mayo Clinic, Rochester, MN, USA.
Guangchao Sun *Maize Research Institute, Sichuan Agricultural University, Chengdu, China.ORCID http://orcid.org/0000-0003-3942-6175
Jake A Kloeber *Department of Oncology, Mayo Clinic, Rochester, MN, USA.ORCID http://orcid.org/0000-0002-6646-564X
Huaping Xiao *Department of Radiation Oncology, Mayo Clinic, Rochester, MN, USA.
Yaobin Ouyang *Department of Oncology, Mayo Clinic, Rochester, MN, USA.
Fei ZhaoDepartment of Oncology, Mayo Clinic, Rochester, MN, USA.
Ya LiDepartment of Oncology, Mayo Clinic, Rochester, MN, USA.
Shilin XuDepartment of Medicinal Chemistry, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Sonja DragojevicDepartment of Radiation Oncology, Mayo Clinic, Rochester, MN, USA.
Zheming WuDepartment of Radiation Oncology, Mayo Clinic, Rochester, MN, USA.ORCID http://orcid.org/0009-0008-2248-0654
Shouhai ZhuDepartment of Oncology, Mayo Clinic, Rochester, MN, USA.
Yiqun HanDepartment of Radiation Oncology, Mayo Clinic, Rochester, MN, USA.
Ping YinDepartment of Oncology, Mayo Clinic, Rochester, MN, USA.
Xinyi TuDepartment of Radiation Oncology, Mayo Clinic, Rochester, MN, USA.ORCID http://orcid.org/0000-0001-5845-7968
Hongran QinDepartment of Oncology, Mayo Clinic, Rochester, MN, USA.
Xiang ZhouDepartment of Oncology, Mayo Clinic, Rochester, MN, USA.
Kuntian LuoDepartment of Oncology, Mayo Clinic, Rochester, MN, USA.
Kevin L PetersonDepartment of Oncology, Mayo Clinic, Rochester, MN, USA.
Jinzhou HuangDepartment of Oncology, Mayo Clinic, Rochester, MN, USA.ORCID http://orcid.org/0000-0002-5956-0905
Taro HitosugiDepartment of Oncology, Mayo Clinic, Rochester, MN, USA.
Haiming DaiDepartment of Oncology, Mayo Clinic, Rochester, MN, USA.
Min DengState Key Laboratory of Molecular Oncology and Department of Radiation Oncology, National Cancer Center, National Clinical Research Center for Cancer and Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China. dengmin@cicams.ac.cn.ORCID http://orcid.org/0000-0003-1987-9775
Robert W MutterDepartment of Radiation Oncology, Mayo Clinic, Rochester, MN, USA. Mutter.Robert@mayo.edu.ORCID http://orcid.org/0000-0002-9430-7323
Zhenkun LouDepartment of Oncology, Mayo Clinic, Rochester, MN, USA. Lou.Zhenkun@mayo.edu.ORCID http://orcid.org/0000-0003-1938-3091

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Okazaki fragment maturation requires efficient removal of RNA primers to form a continuous lagging strand, yet how mismatched primers introduced by error-prone primase are corrected remains unresolved. Here, we show that physiological levels of reactive oxygen species (ROS) initiate a redox-dependent mechanism that drives ADAR1-mediated adenosine-to-inosine (A-to-I) editing. Oxidation triggers ADAR1 dimerization at replication forks, enhancing RNA editing of mismatched primers-particularly those caused by ATP misincorporation on d(T+C)-rich centromeric DNA. This A-to-I editing step facilitates more efficient RNA primer degradation by RNase H2, thereby ensuring proper Okazaki fragment maturation. Disruption of ADAR1 oxidation results in increased unligated Okazaki fragments, single-stranded gaps and double-strand breaks, most prominently at centromeres. These findings reveal a role for ROS in safeguarding lagging-strand synthesis by coupling ADAR1 oxidation-induced A-to-I RNA editing to replication fork stability.

Indexed as

Adenosine DeaminaseDNADNA ReplicationRNA-Binding ProteinsAdenosineHumansInosineOxidation-ReductionReactive Oxygen SpeciesRibonuclease HRNARNA EditingADAR protein, humanAdenosineAdenosine DeaminaseDNAInosineOkazaki fragmentsReactive Oxygen SpeciesRibonuclease HRNARNA-Binding Proteins

Identifiers

PMID41507603

What OpenQuestion holds

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Registered trials

None linked

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.