Evidence map›Paper›PMID 42634536›Full record

ArticleJournal of cellular biochemistry2026

Impacts of N-glycanase1 (NGLY1) Down Regulation on the Function of Mitochondria.

Yanwen Chen, Ruijie Liu, Shaoxing Zhang, Yuxin Zhang, Qiange Lin, Yilin Ye, Shuying Yuan, Xinrong Lu, Linfei Wang, Li Chen and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of cellular biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Yanwen ChenSchool of Medical Technology, Zhejiang Chinese Medical University, Hangzhou, China.ORCID https://orcid.org/0009-0008-9784-6147
Ruijie LiuSchool of Medical Technology, Zhejiang Chinese Medical University, Hangzhou, China.
Shaoxing ZhangSchool of Medical Technology, Zhejiang Chinese Medical University, Hangzhou, China.
Yuxin ZhangSchool of Medical Technology, Zhejiang Chinese Medical University, Hangzhou, China.
Qiange LinSchool of Medical Technology, Zhejiang Chinese Medical University, Hangzhou, China.
Yilin YeSchool of Medical Technology, Zhejiang Chinese Medical University, Hangzhou, China.
Shuying YuanDepartment of Clinical Laboratory, Jiaxing Maternity and Child Health Care Hospital, Jiaxing, China.
Xinrong LuKey Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai, China.
Linfei WangLinhai Second People's Hospital, Taizhou, China.
Li ChenKey Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai, China.
Guiqin SunSchool of Medical Technology, Zhejiang Chinese Medical University, Hangzhou, China.ORCID https://orcid.org/0000-0002-2819-6063

Funding

Open Research Fund of State Key Laboratory of Genetic Engineering, Fudan University SKLGE-2314Zhejiang Chinese Medical University - Linhai Second People's Hospital Cooperation Program 2023-HT-1266Zhejiang Provincial Medical and Health Science and Technology Plan 2025KY308
6 · The paper itself

Abstract

N-glycanase 1 (NGLY1) is involved in intracellular misfolded protein degradation, releasing a de-N-glycosylated protein and a complete N-oligosaccharide. Enzymatic defects in NGLY1 may cause NGLY1-related congenital disorder of deglycosylation (NGLY1-CDDG). NGLY1 patients exhibit cognition and coordination defects, and the regulatory impact of NGLY1 in the organism deserves in-depth investigation. In this study, we established NGLY1-knockdown human foreskin fibroblasts-1 (HFF-1) cells and observed mitochondrial function impairments. We conservatively suggest that NGLY1 has global regulatory roles within cells. The Calnexin/IP3R/VDAC1 axis acts as a communication bridge and represents one mechanism underlying NGLY1-mediated modulation of mitochondrial function. This has significant implications for addressing the clinical disease problems presented by NGLY1-CDDG.

Indexed as

MitochondriaPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseCell LineDown-RegulationFibroblastsGlycosylationHumansNGLY1 protein, humanPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidasedeglycosylationmitochondriamolecular mechanismNGLY1N‐glycanase 1

Identifiers

PMID42634536
PMCPMC13501143

What OpenQuestion holds

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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.