Evidence map›Paper›PMID 42254499›Full record

ArticleFrontiers in microbiology2026

Quantifying arsenic-binding affinities of ArsR proteins via biomimetic self-assembly.

Liang Cui, Xiaobo Zhang, Xiaohui Sun, Yi Yang, Bitong Zhu, Shasha Wang, RuoXin Lin, Chungui Zhao, Guangya Zhang, Jian Chen and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in microbiology, 2026. 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
–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

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

11 authors.

Liang Cui *Department of Bioengineering and Biotechnology, College of Chemical Engineering, Huaqiao University, Xiamen, Fujian, China.
Xiaobo Zhang *Department of Bioengineering and Biotechnology, College of Chemical Engineering, Huaqiao University, Xiamen, Fujian, China.
Xiaohui SunDepartment of Bioengineering and Biotechnology, College of Chemical Engineering, Huaqiao University, Xiamen, Fujian, China.
Yi YangDepartment of Bioengineering and Biotechnology, College of Chemical Engineering, Huaqiao University, Xiamen, Fujian, China.
Bitong ZhuDepartment of Bioengineering and Biotechnology, College of Chemical Engineering, Huaqiao University, Xiamen, Fujian, China.
Shasha WangDepartment of Bioengineering and Biotechnology, College of Chemical Engineering, Huaqiao University, Xiamen, Fujian, China.
RuoXin LinDepartment of Bioengineering and Biotechnology, College of Chemical Engineering, Huaqiao University, Xiamen, Fujian, China.
Chungui ZhaoDepartment of Bioengineering and Biotechnology, College of Chemical Engineering, Huaqiao University, Xiamen, Fujian, China.
Guangya ZhangDepartment of Bioengineering and Biotechnology, College of Chemical Engineering, Huaqiao University, Xiamen, Fujian, China.
Jian ChenDepartment of Cellular Biology and Pharmacology, Herbert Wertheim College of Medicine, Florida International University, Miami, FL, United States.
Suping YangDepartment of Bioengineering and Biotechnology, College of Chemical Engineering, Huaqiao University, Xiamen, Fujian, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ArsR, an As(III)-binding transcriptional repressor protein, plays a critical role in arsenic (As) detoxification by selectively binding As(III) and regulating cellular responses. Recent studies have revealed that ArsRs exhibit broad diversity in their arsenic recognition and binding sites. Multiple ArsRs are often found in highly As-resistant microbes, allowing for coping with complicated arsenical stresses. However, quantitative assessments of ArsR binding affinities and their contributions to arsenic resistance remain limited due to methodological challenges. In this study, we developed a novel biomimetic self-assembly approach, applied in a protein purification-free manner after initial validation, to quantify the arsenic binding affinity of ArsR-As interaction. ArsR was immobilized on the surface of biosilica spheres (S) via the covalently cross-link self-assembly of ArsR-SpyTag and ELP-SpyCatcher@SiO

Indexed as

arsenicArsR (As(III)-binding transcriptional repressor protein)Rhodopseudomonas palustris CGA009solid-phase arsenic adsorbentSpyCatcher/SpyTag

Identifiers

PMID42254499
PMCPMC13236881

What Socratic 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 Socratic graph.