Evidence map›Paper›PMID 41985411›Full record

ArticleRedox biology2026

Glutaredoxin 1 promotes intestinal epithelial cell copper toxicity in inflammatory bowel disease.

Tiantian Zhang, Xiaofen Zhang, Huimei Cai, Mengli Yu, Qichen Liu, Xin Song, Bingru Lin, Linjie Xu, Lan Li, Zhe Shen and 2 more

Erratum issuedAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Redox biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Tiantian ZhangDepartment of Gastroenterology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, 310003, China.
Xiaofen ZhangDepartment of Gastroenterology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, 310003, China; Department of Gastroenterology and Hepatology, The First Affiliated Hospital of Xiamen University, School of Medicine, Xiamen University, Xiamen, 361003, China.
Huimei CaiDepartment of Gastroenterology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, 310003, China.
Mengli YuDepartment of Gastroenterology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, 310003, China; Department of Gastroenterology, The Fourth Affiliated Hospital, Zhejiang University School of Medicine, Yiwu, 322000, China.
Qichen LiuDepartment of Gastroenterology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, 310003, China.
Xin SongDepartment of Gastroenterology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, 310003, China.
Bingru LinDepartment of Gastroenterology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, 310003, China.
Linjie XuDepartment of Pathology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, 310003, China.
Lan LiDepartment of Gastroenterology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, 310003, China. Electronic address: nalil@zju.edu.cn.
Zhe ShenDepartment of Gastroenterology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, 310003, China. Electronic address: sz8239@zju.edu.cn.
Chaohui YuDepartment of Gastroenterology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, 310003, China. Electronic address: zyyyych@zju.edu.cn.
Jie ZhangDepartment of Gastroenterology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, 310003, China. Electronic address: zhangjiefj@zju.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein S-glutathionylation (PSSG), a redox-sensitive post-translational modification, regulates protein conformation and activity, potentially resulting in cell death. PSSG is dynamically reversed by glutaredoxin 1 (GRX1), a critical oxidoreductase. Here, we observed elevated PSSG levels in colonic tissues of ulcerative colitis (UC) patients and experimental mouse models. Quantitative redox proteomics revealed glutathione disulfide oxidoreductase activity as the most significantly altered pathway in UC patients compared to controls. Interestingly, GRX1 undergoes site-specific S-glutathionylation at its catalytic Cys8 residue in UC patients, resulting in enzymatic inactivation. Grx1 deficiency exacerbated colonic PSSG accumulation and increased susceptibility to dextran sulfate sodium (DSS)- and 2,4,6-trinitrobenzene sulfonic acid (TNBS)-induced colitis, whereas Grx1 overexpression attenuated PSSG and ameliorated disease severity. Transcriptomic profiling identified GRX1 as a regulator of metal ion transmembrane transport, with Grx1 loss inducing copper overload and cuproptosis in vitro. Copper chelation therapy rescued colitis progression in Grx1

Indexed as

CopperEpithelial CellsGlutaredoxinsInflammatory Bowel DiseasesIntestinal MucosaAnimalsColitis, UlcerativeCuproptosisDisease Models, AnimalGlutathioneHumansMiceProtein Processing, Post-TranslationalCopperGlutaredoxinsGlutathioneATPase copper-transporting betaCopper toxicityGlutaredoxin 1Protein S-GlutathionylationUlcerative colitis

Identifiers

PMID41985411
PMCPMC13092873

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.