Evidence map›Paper›PMID 38180646›Full record

ReviewApplied biochemistry and biotechnology2024

Recent Progress on Peroxidase Modification and Application.

Chen Shen, Yongfa Wang

Abstract readReview
PubMed Publisher
In one paragraph

Review in Applied biochemistry and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Thiolated Polymers in 3D Bioprinting: Control of Gelation.Advanced materials (Deerfield Beach, Fla.) · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Catalase-peroxidase StKatG2 fromFrontiers in microbiology · 2024
    Article
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

2 authors.

Chen ShenCollege of Chemical & Pharmaceutical Engineering, Hebei University of Science & Technology, Shijiazhuang, 050018, China. pharma_sc@163.com.
Yongfa WangCollege of Chemical & Pharmaceutical Engineering, Hebei University of Science & Technology, Shijiazhuang, 050018, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxdiase is one of the member of oxireductase super family, which has a broad substrate range and a variety of reaction types, including hydroxylation, epoxidation or halogenation of unactivated C-H bonds, and aromatic group or biophenol compounds. Here, we summarized the recently discovered enzymes with peroxidation activity, and focused on the special structures, sites, and corresponding strategies that can change the peroxidase catalytic activity, stability, and substrate range. The comparison of the structural differences between these natural enzymes and the mimic enzymes of binding nanomaterials and polymer materials is helpful to expand the application of peroxidase in industry. In addition, we also reviewed the catalytic application of peroxidase in the synthesis of important organic molecules and the degradation of pollutants.

Indexed as

BiochemistryBiotechnologyPeroxidasesBacteriaEnvironmental Restoration and RemediationPlantsPeroxidasesBiological oxidationChemical synthesisFungal enzymeLigninPeroxidase

Identifiers

What OpenQuestion holds

Textmetadata
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.