Evidence map›Paper›PMID 37829030›Full record

ArticleChemical science2023

Engineering of antimicrobial peptide fibrils with feedback degradation of bacterial-secreted enzymes.

Fenghua Wang, Wencheng Xia, Mingming Zhang, Rongrong Wu, Xiaolu Song, Yun Hao, Yonghai Feng, Liwei Zhang, Dan Li, Wenyan Kang and 2 more

Erratum issuedOpen access · diamondAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemical science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
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

4 citing papers in PubMed, 14 citations in OpenAlex.

  1. Therapeutic Bioactivity Exerted by theMolecules (Basel, Switzerland) · 2025
    Article
  2. Review
  3. Review
  4. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 1 country.

Fenghua WangInstitute for Advanced Materials, School of Materials Science and Engineering, Jiangsu University Zhenjiang Jiangsu 212013 China liul@ujs.edu.cn.
Wencheng XiaInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences Shanghai 201210 China liulab@sioc.ac.cn.
Mingming ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences Shanghai 201210 China liulab@sioc.ac.cn.
Rongrong WuInstitute for Advanced Materials, School of Materials Science and Engineering, Jiangsu University Zhenjiang Jiangsu 212013 China liul@ujs.edu.cn.
Xiaolu SongInstitute for Advanced Materials, School of Materials Science and Engineering, Jiangsu University Zhenjiang Jiangsu 212013 China liul@ujs.edu.cn.
Yun HaoInstitute for Advanced Materials, School of Materials Science and Engineering, Jiangsu University Zhenjiang Jiangsu 212013 China liul@ujs.edu.cn.
Yonghai FengInstitute for Advanced Materials, School of Materials Science and Engineering, Jiangsu University Zhenjiang Jiangsu 212013 China liul@ujs.edu.cn.
Liwei ZhangInstitute for Advanced Materials, School of Materials Science and Engineering, Jiangsu University Zhenjiang Jiangsu 212013 China liul@ujs.edu.cn.
Dan LiBio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders (Ministry of Education), Shanghai Jiao Tong University Shanghai 200030 China.
Wenyan KangDepartment of Neurology and Institute of Neurology, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine Shanghai 200025 China.
Cong LiuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences Shanghai 201210 China liulab@sioc.ac.cn.ORCID https://orcid.org/0000-0003-3425-6672
Lei LiuInstitute for Advanced Materials, School of Materials Science and Engineering, Jiangsu University Zhenjiang Jiangsu 212013 China liul@ujs.edu.cn.ORCID https://orcid.org/0000-0002-6265-9412
Jiangsu University · CNShanghai Jiao Tong University · CNChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins and peptides can assemble into functional amyloid fibrils with distinct architectures. These amyloid fibrils can fulfil various biological functions in living organisms, and then be degraded. By incorporating an amyloidogenic segment and enzyme-cleavage segment together, we designed a peptide (enzyme-cleavage amyloid peptides (EAP))-based functional fibril which could be degraded specifically by gelatinase. To gain molecular insights into the assembly and degradation of EAP fibrils, we determined the atomic structure of the EAP fibril using cryo-electron microscopy. The amyloidogenic segment of EAP adopted a β-strand conformation and mediated EAP-fibril formation mainly

Identifiers

PMID37829030
PMCPMC10566480
OpenAlexW4386506744

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.