Evidence mapPaperPMID 40707464Full record

ReviewNature communications2025

Nanozymes expanding the boundaries of biocatalysis.

Ruofei Zhang, Xiyun Yan, Lizeng Gao, Kelong Fan

Abstract readReview
In one paragraph

Review in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Sulfur-modified VRSC advances · 2026
    Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. 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

4 authors.

Ruofei ZhangState Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-4186-4951
Xiyun YanState Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-7290-352X
Lizeng GaoState Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China. gaolizeng@ibp.ac.cn.ORCID http://orcid.org/0000-0003-0265-4027
Kelong FanState Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China. fankelong@ibp.ac.cn.ORCID http://orcid.org/0000-0001-6285-1933

Funding

National Natural Science Foundation of China (National Science Foundation of China) 22121003National Natural Science Foundation of China (National Science Foundation of China) 81930050
6 · The paper itself

Abstract

Biocatalysis is fundamental to biological processes and sustainable applications. Over time, the understanding of biocatalysis has evolved considerably. Initially, protein enzymes were recognized as the primary biocatalysts due to their high catalytic efficiency under mild conditions. The discovery of ribozymes expanded the scope of biocatalysts to include nucleic acids and the development of synthetic or semisynthetic artificial enzymes sought to overcome the limitations of natural enzymes. The emergence of nanozymes, nanomaterials with intrinsic biocatalytic activity, has further broadened this field. Nanozymes possess abundant active sites, multiple active phases, and nanostructures that maintain stability even under extreme conditions, along with unique physicochemical properties. These attributes enable nanozymes to perform efficient biocatalysis in diverse forms and under a wide range of conditions. The discovery of natural biogenic nanozymes, such as magnetosomes, ferritin iron cores, and amyloid protein assemblies, underscores their potential physiological functions and roles in disease pathogenesis. This review explores the distinct properties and catalytic mechanisms of nanozymes, elucidates their structure-activity relationships, and discusses their transformative impact on biocatalysis, highlighting their potential to reshape fundamental concepts and practical applications in the field.

Indexed as

BiocatalysisEnzymesNanostructuresHumansStructure-Activity RelationshipEnzymes

Identifiers

PMID40707464
PMCPMC12290111

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.