Evidence map›Paper›PMID 39387674›Full record

ArticleChembiochem : a European journal of chemical biology2025

Human 8-Oxoguanine Glycosylase OGG1 Cleaves Abasic Sites and Covalently Conjugates to 3'-DNA Termini via Cysteine and Histidine Addition.

Cameron Bryan, Kun Yang

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
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

2 authors.

Cameron BryanDivision of Chemical Biology and Medicinal Chemistry, College of Pharmacy, The University of Texas at Austin, Austin, Texas, 78712, United States.
Kun YangDivision of Chemical Biology and Medicinal Chemistry, College of Pharmacy, The University of Texas at Austin, Austin, Texas, 78712, United States.ORCID https://orcid.org/0000-0001-5532-8810

Funding

Formation and Repair Mechanisms of DNA-Protein Cross-Links, and Functions and Regulatory Mechanisms of TREX1 in DNA RepairR35GM155148 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Kun Yang · 2024 to 2026
$1.2M
NIGMS NIH HHS R35 GM155148University of Texas at Austin and National Institute of General Medical Sciences of the National Institutes of Health R35GM155148
6 · The paper itself

Abstract

8-Oxoguanine glycosylase 1 (OGG1) repairs the major oxidative DNA damage, 8-oxo-2'-deoxyguanosine. It has been reported that OGG1 incises the most frequently formed DNA lesion, apurinic/apyrimidinic (AP) site, and in the process a stable DNA-OGG1 cross-link is formed. However, the chemical structure of the adduct is not characterized. Here, we report that DNA-OGG1 cross-links result from cysteine and histidine addition to incised AP sites at 3'-DNA termini.

Indexed as

CysteineDNADNA GlycosylasesHistidineDNA DamageHumansCysteineDNADNA GlycosylasesHistidineoxoguanine glycosylase 1, humanAbasic siteDNA-protein cross-linkOGG1

Identifiers

PMID39387674
PMCPMC11779587

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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.