Evidence map›Paper›PMID 38067490›Full record

ArticleMolecules (Basel, Switzerland)2023

A Natural Compound Containing a Disaccharide Structure of Glucose and Rhamnose Identified as Potential N-Glycanase 1 (NGLY1) Inhibitors.

Ruijie Liu, Jingjing Gu, Yilin Ye, Yuxin Zhang, Shaoxing Zhang, Qiange Lin, Shuying Yuan, Yanwen Chen, Xinrong Lu, Yongliang Tong and 3 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecules (Basel, Switzerland), 2023. 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
0.3field-weighted citation impact, top 35% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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

13 authors at 3 institutions in 1 country.

Ruijie LiuSchool of Medical Technology and Information Engineering, Zhejiang Chinese Medical University, Hangzhou 310053, China.
Jingjing GuSchool of Basic Medical Sciences, Zhejiang Chinese Medical University, Hangzhou 310053, China.
Yilin YeSchool of Medical Technology and Information Engineering, Zhejiang Chinese Medical University, Hangzhou 310053, China.
Yuxin ZhangSchool of Medical Technology and Information Engineering, Zhejiang Chinese Medical University, Hangzhou 310053, China.
Shaoxing ZhangSchool of Medical Technology and Information Engineering, Zhejiang Chinese Medical University, Hangzhou 310053, China.
Qiange LinSchool of Medical Technology and Information Engineering, Zhejiang Chinese Medical University, Hangzhou 310053, China.
Shuying YuanDepartment of Clinical Laboratory, Jiaxing Maternity and Child Health Care Hospital, Jiaxing 314001, China.
Yanwen ChenCentral Laboratory, Ningbo Hospital, Renji Hospital, Shanghai Jiao Tong University School of Medicine, Ningbo 315336, China.
Xinrong LuKey Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.
Yongliang TongKey Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.
Shaoxian LvKey Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.
Li ChenKey Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.
Guiqin SunSchool of Medical Technology and Information Engineering, Zhejiang Chinese Medical University, Hangzhou 310053, China.
Zhejiang Chinese Medical University · CNFudan University · CNRenji Hospital · CN

Funding

Natural Science Foundation of Zhejiang Province LY20C050002Research Project of Zhejiang Chinese Medical University 2023GJYY19
6 · The paper itself

Abstract

N-glycanase 1 (NGLY1) is an essential enzyme involved in the deglycosylation of misfolded glycoproteins through the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which could hydrolyze N-glycan from N-glycoprotein or N-glycopeptide in the cytosol. Recent studies indicated that NGLY1 inhibition is a potential novel drug target for antiviral therapy. In this study, structure-based virtual analysis was applied to screen candidate NGLY1 inhibitors from 2960 natural compounds. Three natural compounds, Poliumoside, Soyasaponin Bb, and Saikosaponin B2 showed significantly inhibitory activity of NGLY1, isolated from traditional heat-clearing and detoxifying Chinese herbs. Furthermore, the core structural motif of the three NGLY1 inhibitors was a disaccharide structure with glucose and rhamnose, which might exert its action by binding to important active sites of NGLY1, such as Lys238 and Trp244. In traditional Chinese medicine, many compounds containing this disaccharide structure probably targeted NGLY1. This study unveiled the leading compound of NGLY1 inhibitors with its core structure, which could guide future drug development.

Indexed as

GlucoseRhamnoseCytosolGlycoproteinsPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseGlucoseGlycoproteinsPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseRhamnosenatural compoundNGLY1 inhibitorN-glycanase 1 (NGLY1)structure-based virtual screening

Identifiers

PMID38067490
PMCPMC10707914
OpenAlexW4388969579

What OpenQuestion holds

Textmetadata
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.