Evidence map›Paper›PMID 40349683›Full record

ArticleCells, tissues, organs2026

Downregulation of Endo-Beta-N-Acetylglucosaminidase in <italic>Caenorhabditis elegans</italic> Improves Stress Adaptivity.

Xinrong Lu, Yongliang Tong, Mengting Wu, Shaoxian Lyu, Jiale Fan, Junyu Zheng, Lin Zou, Danfeng Shen, Lin Rao, Linlin Hou and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cells, tissues, organs, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

15 authors.

Xinrong LuDepartment of Medical Microbiology, Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, School of Basic Medical Sciences, Fudan University, Translational Glycomics Research Center, Fudan Zhangjiang Institute, Shanghai, China.
Yongliang TongDepartment of Medical Microbiology, Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, School of Basic Medical Sciences, Fudan University, Translational Glycomics Research Center, Fudan Zhangjiang Institute, Shanghai, China.
Mengting WuDepartment of Neurosurgery, State Key Laboratory of Medical Neurobiology and MOE Frontiers Center for Brain Science, Institutes of Brain Science, Zhongshan Hospital, Fudan University, Shanghai, China.
Shaoxian LyuDepartment of Medical Microbiology, Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, School of Basic Medical Sciences, Fudan University, Translational Glycomics Research Center, Fudan Zhangjiang Institute, Shanghai, China.
Jiale FanDepartment of Neurosurgery, State Key Laboratory of Medical Neurobiology and MOE Frontiers Center for Brain Science, Institutes of Brain Science, Zhongshan Hospital, Fudan University, Shanghai, China.
Junyu ZhengDepartment of Neurosurgery, State Key Laboratory of Medical Neurobiology and MOE Frontiers Center for Brain Science, Institutes of Brain Science, Zhongshan Hospital, Fudan University, Shanghai, China.
Lin ZouDepartment of Medical Microbiology, Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, School of Basic Medical Sciences, Fudan University, Translational Glycomics Research Center, Fudan Zhangjiang Institute, Shanghai, China.
Danfeng ShenDepartment of Medical Microbiology, Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, School of Basic Medical Sciences, Fudan University, Translational Glycomics Research Center, Fudan Zhangjiang Institute, Shanghai, China.
Lin RaoDepartment of Medical Microbiology, Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, School of Basic Medical Sciences, Fudan University, Translational Glycomics Research Center, Fudan Zhangjiang Institute, Shanghai, China.
Linlin HouCollege of Veterinary Medicine, Qingdao Agricultural University, Qingdao, China.
Cuiying ChenDepartment of Research and Development, SysDiagno (Nanjing) Biotech Co., Ltd., Nanjing, China.
Xunjia ChengDepartment of Medical Microbiology and Parasitology, School of Basic Medical Sciences, Fudan University, Shanghai, China.
Guiqin SunSchool of Medical Technology and Information Engineering, Zhejiang Chinese Medical University, Hangzhou, China, sunguiqin2001@163.com.
Zhiyong ShaoDepartment of Neurosurgery, State Key Laboratory of Medical Neurobiology and MOE Frontiers Center for Brain Science, Institutes of Brain Science, Zhongshan Hospital, Fudan University, Shanghai, China, shaozy@fudan.edu.cn.
Li ChenDepartment of Medical Microbiology, Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, School of Basic Medical Sciences, Fudan University, Translational Glycomics Research Center, Fudan Zhangjiang Institute, Shanghai, China, lichen_bk@fudan.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

<p>Introduction: Endo-beta-N-acetylglucosaminidase (ENGASE) is one of the key enzymes involved in the structural and functional regulations of glycoproteins. Although its enzymatic activities and applications have been well studied in vitro, its biological function in vivo yet remains to be illustrated. In this study, the biological function of ENGASE in Caenorhabditis elegans was explored in detail.

methodsAn Engase gene knockout in C. elegans (CeEng-1 or CeEngase) was constructed and subjected to a panel of phenotypical and glycomics analysis. In addition, in vitro and in vivo ENGASE inhibition assays were performed.

resultsEngase knockout worm's adaptivity to environmental stresses (heat and osmotic) was significantly improved, and its longevity was also increased mildly. A clustered change in basement membrane proteins (e.g., LAM-1, LAM-2, and EPI-1) was illustrated by N-glycopeptide analysis, suggesting that ENGASE is involved in a basement membrane-based stress regulation. Then, the heat stress phenotype was further supported by in vivo CeEngase knockdown assay and in vitro and in vivo small compound inhibitory assay of CeENGASE, indicating that ENGASE is a potential drug target for stress management.

conclusionEngase is actively involved in a basement membrane-mediated stress adaptation and could serve as a potential target for healthcare products. </p>.

Indexed as

Adaptation, PhysiologicalCaenorhabditis elegansCaenorhabditis elegans ProteinsDown-RegulationMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseStress, PhysiologicalAcetylglucosaminidaseAnimalsGene Knockout TechniquesAcetylglucosaminidaseCaenorhabditis elegans ProteinsMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseBasement membraneCaenorhabditis elegansEngaseENGASE inhibitorStress adaptivity

Identifiers

PMID40349683
PMCPMC12187103

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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.