Evidence map›Paper›PMID 38977710›Full record

ArticleNature communications2024

Metal-ligand dual-site single-atom nanozyme mimicking urate oxidase with high substrates specificity.

Kaiyuan Wang, Qing Hong, Caixia Zhu, Yuan Xu, Wang Li, Ying Wang, Wenhao Chen, Xiang Gu, Xinghua Chen, Yanfeng Fang and 3 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Can nanozymes achieve more than enzymes?Nature reviews. Materials · 2026
    Article
  8. Review
  9. Review
  10. Nanozymes for Energy and Environmental Sustainability.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  11. Atomically Precise Clusterzymes: A Programmable Optoelectronic Platform for Neuroscience.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  12. Review
  13. Review
  14. Review
  15. Biomedical Applications of Nanozymes: An Enzymology Perspective.Angewandte Chemie (International ed. in English) · 2025
    Review
  16. Review
  17. Bimetallic Cu/Zn Single-Atom Nanozyme with Superoxide Dismutase-Like Activity.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  18. Article
  19. Article
  20. 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

13 authors.

Kaiyuan WangJiangsu Engineering Research Center for Carbon-Rich Materials and Devices, Jiangsu Province Hi-Tech Key Laboratory for Bio-Medical Research, School of Chemistry and Chemical Engineering, Nanjing, 211189, China.
Qing HongJiangsu Engineering Research Center for Carbon-Rich Materials and Devices, Jiangsu Province Hi-Tech Key Laboratory for Bio-Medical Research, School of Chemistry and Chemical Engineering, Nanjing, 211189, China.
Caixia ZhuJiangsu Engineering Research Center for Carbon-Rich Materials and Devices, Jiangsu Province Hi-Tech Key Laboratory for Bio-Medical Research, School of Chemistry and Chemical Engineering, Nanjing, 211189, China.
Yuan XuJiangsu Engineering Research Center for Carbon-Rich Materials and Devices, Jiangsu Province Hi-Tech Key Laboratory for Bio-Medical Research, School of Chemistry and Chemical Engineering, Nanjing, 211189, China.
Wang LiJiangsu Engineering Research Center for Carbon-Rich Materials and Devices, Jiangsu Province Hi-Tech Key Laboratory for Bio-Medical Research, School of Chemistry and Chemical Engineering, Nanjing, 211189, China.
Ying WangJiangsu Engineering Research Center for Carbon-Rich Materials and Devices, Jiangsu Province Hi-Tech Key Laboratory for Bio-Medical Research, School of Chemistry and Chemical Engineering, Nanjing, 211189, China.
Wenhao ChenJiangsu Engineering Research Center for Carbon-Rich Materials and Devices, Jiangsu Province Hi-Tech Key Laboratory for Bio-Medical Research, School of Chemistry and Chemical Engineering, Nanjing, 211189, China.
Xiang GuJiangsu Engineering Research Center for Carbon-Rich Materials and Devices, Jiangsu Province Hi-Tech Key Laboratory for Bio-Medical Research, School of Chemistry and Chemical Engineering, Nanjing, 211189, China.
Xinghua ChenJiangsu Engineering Research Center for Carbon-Rich Materials and Devices, Jiangsu Province Hi-Tech Key Laboratory for Bio-Medical Research, School of Chemistry and Chemical Engineering, Nanjing, 211189, China.
Yanfeng FangJiangsu Engineering Research Center for Carbon-Rich Materials and Devices, Jiangsu Province Hi-Tech Key Laboratory for Bio-Medical Research, School of Chemistry and Chemical Engineering, Nanjing, 211189, China.
Yanfei ShenMedical School, Southeast University, Nanjing, 210009, China. Yanfei.Shen@seu.edu.cn.ORCID 0000-0003-0369-5920
Songqin LiuJiangsu Engineering Research Center for Carbon-Rich Materials and Devices, Jiangsu Province Hi-Tech Key Laboratory for Bio-Medical Research, School of Chemistry and Chemical Engineering, Nanjing, 211189, China.
Yuanjian ZhangJiangsu Engineering Research Center for Carbon-Rich Materials and Devices, Jiangsu Province Hi-Tech Key Laboratory for Bio-Medical Research, School of Chemistry and Chemical Engineering, Nanjing, 211189, China. Yuanjian.Zhang@seu.edu.cn.ORCID 0000-0003-2932-4159

Funding

National Natural Science Foundation of China (National Science Foundation of China) 22074015National Natural Science Foundation of China (National Science Foundation of China) 22174014
6 · The paper itself

Abstract

In nature, coenzyme-independent oxidases have evolved in selective catalysis using isolated substrate-binding pockets. Single-atom nanozymes (SAzymes), an emerging type of non-protein artificial enzymes, are promising to simulate enzyme active centers, but owing to the lack of recognition sites, realizing substrate specificity is a formidable task. Here we report a metal-ligand dual-site SAzyme (Ni-DAB) that exhibited selectivity in uric acid (UA) oxidation. Ni-DAB mimics the dual-site catalytic mechanism of urate oxidase, in which the Ni metal center and the C atom in the ligand serve as the specific UA and O

Indexed as

Oxidation-ReductionUrate OxidaseUric AcidBinding SitesCatalysisCatalytic DomainHumansLigandsModels, MolecularNickelSubstrate SpecificityX-Ray Absorption SpectroscopyLigandsNickelUrate OxidaseUric Acid

Identifiers

PMID38977710
PMCPMC11231224

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.