Evidence map›Paper›PMID 41087344›Full record

ArticleBiomolecules & therapeutics2025

Involvement of the DNA Demethylase Thymine DNA Glycosylase in Anticancer Drug Resistance.

Kyoung Ah Kang, Mei Jing Piao, Herath Mudiyanselage Maheshika Madhuwanthi Senavirathna, Hye-Jin Boo, Sang Pil Yoon, Joo Mi Yi, Jinny Park, Jin Won Hyun

Abstract read
In one paragraph

Article in Biomolecules & therapeutics, 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
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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

8 authors.

Kyoung Ah KangJeju Natural Medicine Research Center, Jeju National University, Jeju 63243, Republic of Korea.
Mei Jing PiaoJeju Natural Medicine Research Center, Jeju National University, Jeju 63243, Republic of Korea.
Herath Mudiyanselage Maheshika Madhuwanthi SenavirathnaDepartment of Biochemistry, Jeju National University College of Medicine, Jeju 63243, Republic of Korea.
Hye-Jin BooJeju Natural Medicine Research Center, Jeju National University, Jeju 63243, Republic of Korea.
Sang Pil YoonJeju Natural Medicine Research Center, Jeju National University, Jeju 63243, Republic of Korea.
Joo Mi YiDepartment of Microbiology and Immunology, Inje University College of Medicine, Busan 47392, Republic of Korea.
Jinny ParkDepartment of Internal Medicine, Korea University Ansan Hospital, Korea University College of Medicine, Ansan 15355, Republic of Korea.
Jin Won HyunJeju Natural Medicine Research Center, Jeju National University, Jeju 63243, Republic of Korea.ORCID https://orcid.org/0000-0002-3403-3762

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Anticancer drug resistance remains a significant challenge to the efficacy of cancer treatment, with DNA repair enzymes contributing to this resistance. We hypothesized that thymine DNA glycosylases (TDGs) may be involved in anticancer drug resistance given their dual function of DNA repair and demethylation as well as investigated their possible involvement in the induction of β-catenin in SNUC5 cells resistant to 5-fluorouracil (SNUC5/5-FUR) and oxaliplatin (SNUC5/OXTR). The expression of TDG and phospho-β-catenin increased in both resistant cell types when compared to that in SNUC5 cells. Moreover, knockdown of TDG significantly suppressed phospho-β-catenin expression in both resistant cell types, resulting in enhanced sensitivity to anticancer drugs. TDG binding to the β-catenin promoter was stronger in both resistant cell types than in SNUC5 cells, showing a decreased methylation pattern in the CpG islands of the β-catenin promoter. Furthermore, another DNA demethylase, ten-eleven translocation 1 (TET1), showed the same pattern as TDG in both resistant cell types. Additionally, TDG significantly interacted more with TET1 in both resistant cell types than in SNUC5 cells, enhancing binding to the same locus in the β-catenin promoter. These findings suggest that TDG may be a promising target molecule for overcoming drug resistance in colorectal cancer.

Indexed as

Anticancer drug resistanceColorectal cancerDNA demethylaseThymine DNA glycosylaseβ-catenin

Identifiers

PMID41087344
PMCPMC12580638

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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.