Evidence map›Paper›PMID 41079656›Full record

ReviewChemical science2025

Directing the oxidative folding of disulfide-rich peptides for enhanced engineering and applications.

Xueting Cheng, Chuanliu Wu

Abstract readReview
In one paragraph

Review in Chemical science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  3. 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.

Xueting ChengDepartment of Chemistry, College of Chemistry and Chemical Engineering, The MOE Key Laboratory of Spectrochemical Analysis and Instrumentation, Xiamen University Xiamen 361005 P. R. China chlwu@xmu.edu.cn.
Chuanliu WuDepartment of Chemistry, College of Chemistry and Chemical Engineering, The MOE Key Laboratory of Spectrochemical Analysis and Instrumentation, Xiamen University Xiamen 361005 P. R. China chlwu@xmu.edu.cn.ORCID https://orcid.org/0000-0003-2946-7299

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Disulfide-rich peptides (DRPs) leverage dense disulfide networks to form rigid and stable cores, enabling exceptional proteolytic resistance and precise target complementarity. These attributes drive their utility as high-affinity molecular tools in bioanalytics/chemical biology and clinically validated therapeutics (

Identifiers

PMID41079656
PMCPMC12509089

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.