Evidence map›Paper›PMID 40778759›Full record

ArticlemBio2025

Structural insights into manganese-dependent arylsulfatase from

Lulu Guo, Xuanjia Dong, Zetao Hu, Ling Zeng, Zhaohui Jin, Lin Jiang, Wenting Dai, Jinbiao Ma, Shili Chen, Ying Huang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in mBio, 2025. 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

10 authors.

Lulu GuoShanghai Key Laboratory of Biliary Tract Disease Research, Department of General Surgery, Xinhua Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.ORCID 0009-0006-8330-0958
Xuanjia DongShanghai Key Laboratory of Biliary Tract Disease Research, Department of General Surgery, Xinhua Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Zetao HuState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Biochemistry and Biophysics, Institute of Plant Biology, School of Life Sciences, Fudan University, Shanghai, China.
Ling ZengShanghai Key Laboratory of Biliary Tract Disease Research, Department of General Surgery, Xinhua Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Zhaohui JinShanghai Key Laboratory of Biliary Tract Disease Research, Department of General Surgery, Xinhua Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Lin JiangShanghai Key Laboratory of Biliary Tract Disease Research, Department of General Surgery, Xinhua Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Wenting DaiShanghai Key Laboratory of Biliary Tract Disease Research, Department of General Surgery, Xinhua Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Jinbiao MaState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Biochemistry and Biophysics, Institute of Plant Biology, School of Life Sciences, Fudan University, Shanghai, China.
Shili ChenShanghai Key Laboratory of Biliary Tract Disease Research, Department of General Surgery, Xinhua Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.ORCID 0009-0007-6886-2204
Ying HuangShanghai Key Laboratory of Biliary Tract Disease Research, Department of General Surgery, Xinhua Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.ORCID 0000-0002-2806-2874

Funding

National Natural Science Foundation of China 32171186
6 · The paper itself

Abstract

Catalytic promiscuity, wherein enzymes catalyze multiple distinct reactions by stabilizing various transition states, is well documented in the alkaline phosphatase superfamily. In this study, we determined the crystal structure of an arylsulfatase from

Indexed as

ArylsulfatasesEnterococcus faeciumManganeseCatalytic DomainCrystallography, X-RayModels, MolecularMutagenesis, Site-DirectedProtein ConformationProtein MultimerizationSubstrate SpecificitySulfatesArylsulfatasesManganeseSulfatesarylsulfatasebiomoleculecatalytic promiscuitycrystal structureEnterococcus faeciumgut microbiome

Identifiers

PMID40778759
PMCPMC12421950

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.