Evidence map›Paper›PMID 39912732›Full record

ArticleChembiochem : a European journal of chemical biology2025

Cyclization of Short Peptides Designed from Late Embryogenesis Abundant Protein to Improve Stability and Functionality.

Yinghan Wu, Shinya Ikeno

Abstract read
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In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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.

Yinghan WuDepartment of Biological Functions Engineering, Kyushu Institute of Technology, Kitakyushu Science and Research Park, Kitakyushu, Fukuoka, Japan.
Shinya IkenoDepartment of Biological Functions Engineering, Kyushu Institute of Technology, Kitakyushu Science and Research Park, Kitakyushu, Fukuoka, Japan.ORCID https://orcid.org/0000-0003-2937-4025

Funding

JSPS KAKENHI JP22K04844
6 · The paper itself

Abstract

LEA peptides, which are designed based on late embryogenic abundant (LEA) protein sequences, have demonstrated chaperone-like functions, such as improving drought stress tolerance of Escherichia coli (E. coli). Previous studies have focused on the biological functions of linear LEA peptides. However, the function of cyclic LEA peptide still unknown. This study aimed to explore the cyclic LEA peptides' bio function like enhance the drought stress tolerance of E. coli by cyclizing the LEA peptide using SICLOPPS (Split Intein Circular Ligation of Peptides and Proteins). The results indicated that cyclization significantly improved the function and extended the potential applications. At the same time, we found that peptides containing numerous lysine residues exhibited reduced performance, which may be due to the exteins' residues affecting the SICLOPPS efficiency.

Indexed as

PeptidesPeptides, CyclicPlant ProteinsAmino Acid SequenceCyclizationEscherichia coliProtein Stabilitylate embryogenesis abundant protein, plantPeptidesPeptides, CyclicPlant Proteinscyclizationdrought stressLEA peptideSICLOPPS

Identifiers

PMID39912732
PMCPMC12007072

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Registered trials

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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.