Evidence map›Paper›PMID 38229298›Full record

ArticleApplied microbiology and biotechnology2024

Expression and characterization of the new antimicrobial peptide AP138L-arg26 anti Staphylococcus aureus.

Kun Zhang, Na Yang, Da Teng, Ruoyu Mao, Ya Hao, Jianhua Wang

Open access · goldAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Porcine β-Defensin 2 Expressed inAnimals : an open access journal from MDPI · 2025
    Article
  5. Article
  6. Article
  7. 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

6 authors at 1 institution in 1 country.

Kun ZhangGene Engineering Laboratory, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun Nandajie St., Haidian District, Beijing, 100081, People's Republic of China.
Na YangGene Engineering Laboratory, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun Nandajie St., Haidian District, Beijing, 100081, People's Republic of China. nana_891230@126.com.
Da TengGene Engineering Laboratory, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun Nandajie St., Haidian District, Beijing, 100081, People's Republic of China.
Ruoyu MaoGene Engineering Laboratory, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun Nandajie St., Haidian District, Beijing, 100081, People's Republic of China.
Ya HaoGene Engineering Laboratory, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun Nandajie St., Haidian District, Beijing, 100081, People's Republic of China.
Jianhua WangGene Engineering Laboratory, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun Nandajie St., Haidian District, Beijing, 100081, People's Republic of China. wangjianhua@caas.cn.ORCID http://orcid.org/0000-0002-4048-6055
Chinese Academy of Agricultural Sciences · CN

Funding

National Key Research and Development Plan - High Expression of Thiopeptides and their Analogs 2022-2026National Key Research and Development Plan - High Expression of Thiopeptides and their Analogs 2022YFC2105000-03National Natural Science Foundation of China 31872393The Innovation Program of Agricultural Science and Technology (ASTIP) in CAAS CAAS-ASTIP-2017-FRI-02The key program of Innovation Program of Agricultural Science and Technology (ASTIP) in CAAS CAAS-ZDRW202111The key program of Innovation Program of Agricultural Science and Technology (ASTIP) in CAAS CAAS-ZDXT 201808
6 · The paper itself

Abstract

The low activity and yield of antimicrobial peptides (AMPs) are pressing problems. The improvement of activity and yield through modification and heterologous expression, a potential way to solve the problem, is a research hot-pot. In this work, a new plectasin-derived variant L-type AP138 (AP138L-arg26) was constructed for the study of recombination expression and druggablity. As a result, the total protein concentration of AP138L-arg26 was 3.1 mg/mL in Pichia pastoris X-33 supernatant after 5 days of induction expression in a 5-L fermenter. The recombinant peptide AP138L-arg26 has potential antibacterial activity against selected standard and clinical Gram-positive bacteria (G

Indexed as

Methicillin-Resistant Staphylococcus aureusStaphylococcal InfectionsAnti-Bacterial AgentsAntimicrobial PeptidesMicrobial Sensitivity TestsPichiaRecombinant ProteinsStaphylococcus aureusAnti-Bacterial AgentsAntimicrobial PeptidesRecombinant ProteinsAP138L-arg26Bactericidal mechanismRecombination expressionSafetyStaphylococcus aureus

Identifiers

PMID38229298
PMCPMC10787893
OpenAlexW4390839086

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.