Evidence map›Paper›PMID 39841140›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

A periplasmic protein modulates the proteolysis of peptidoglycan hydrolases to maintain cell wall homeostasis in

Sohee Park, Wook-Jong Jeon, Yeseul Lee, Chae Lim Lim, Eunyeong Lee, Han Byeol Oh, Gyu Sung Lee, Oh Hyun Kwon, Bumhan Ryu, Yong-Joon Cho and 4 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Control of theJournal of bacteriology · 2025
    Article
  4. 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

14 authors.

Sohee ParkDepartment of Biological Sciences, College of Natural Sciences, Sungkyunkwan University, Suwon 16419, Republic of Korea.ORCID 0009-0007-6153-8073
Wook-Jong JeonDepartment of Biological Sciences, College of Natural Sciences, Sungkyunkwan University, Suwon 16419, Republic of Korea.ORCID 0009-0007-7021-6666
Yeseul LeeDepartment of Biotechnology, The Catholic University of Korea, Bucheon 14662, Republic of Korea.
Chae Lim LimDepartment of Biological Sciences, College of Natural Sciences, Sungkyunkwan University, Suwon 16419, Republic of Korea.ORCID 0009-0005-5288-9301
Eunyeong LeeDepartment of Biological Sciences, College of Natural Sciences, Sungkyunkwan University, Suwon 16419, Republic of Korea.ORCID 0009-0000-7232-6737
Han Byeol OhDivision of Biomedical Convergence, College of Biomedical Science, Kangwon National University, Chuncheon 24341, Republic of Korea.
Gyu Sung LeeDepartment of Biopharmaceutical Convergence, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Oh Hyun KwonDepartment of Biological Sciences, College of Natural Sciences, Sungkyunkwan University, Suwon 16419, Republic of Korea.ORCID 0000-0002-8609-0654
Bumhan RyuResearch Solution Center, Institute for Basic Science, Daejeon 34126, Republic of Korea.
Yong-Joon ChoDepartment of Molecular Bioscience, Kangwon National University, Chuncheon 24341, Republic of Korea.
Chung Sub KimDepartment of Biopharmaceutical Convergence, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Sung-Il YoonDivision of Biomedical Convergence, College of Biomedical Science, Kangwon National University, Chuncheon 24341, Republic of Korea.
Jeong Min ChungDepartment of Biotechnology, The Catholic University of Korea, Bucheon 14662, Republic of Korea.
Hongbaek ChoDepartment of Biological Sciences, College of Natural Sciences, Sungkyunkwan University, Suwon 16419, Republic of Korea.ORCID 0000-0001-9360-6981

Funding

National Research Foundation of Korea (NRF) NRF-2022M3A9F3082329National Research Foundation of Korea (NRF) NRF-2022R1C1C1003352National Research Foundation of Korea (NRF) NRF-RS-2023-00228746
6 · The paper itself

Abstract

Bacterial cell wall assembly and remodeling require activities of peptidoglycan (PG) hydrolases as well as PG synthases. In particular, the activity of DD-endopeptidases, which cleave the 4-3 peptide crosslinks in PG, is essential for PG expansion in gram-negative bacteria. Maintaining optimal levels of DD-endopeptidases is critical for expanding PG without compromising its integrity. In

Indexed as

Cell WallEscherichia coliEscherichia coli ProteinsN-Acetylmuramoyl-L-alanine AmidasePeriplasmic ProteinsEndopeptidasesHomeostasisPeptidoglycanPeriplasmProteolysisEndopeptidasesEscherichia coli ProteinsN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanPeriplasmic Proteinscell wallhomeostatic controlpeptidoglycan hydrolasesperiplasmic proteolysis

Identifiers

PMID39841140
PMCPMC11789061

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.