Evidence map›Paper›PMID 37190766›Full record

ReviewMolecules and cells2023

Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin.

Danbi Yoon, Ju Heun Moon, Anna Cho, Hyejoon Boo, Jeong Seok Cha, Yoonji Lee, Jiho Yoo

Open access · diamondAbstract readReview
In one paragraph

Review in Molecules and cells, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

27 citing papers in PubMed, 34 citations in OpenAlex.

  1. Over-expression, purification, and kinetic analysis ofJournal of enzyme inhibition and medicinal chemistry · 2026
    Article
  2. Article
  3. Article
  4. Oxidative protein folding and CaCellular and molecular life sciences : CMLS · 2026
    Review
  5. Article
  6. Cell surface (Amsterdam, Netherlands) · 2026
    Article
  7. Article
  8. The E3 Ligase RNF8 Promotes Ubiquitination and Degradation of ChREBPα During Liver Stress Response.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
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  10. Article
  11. Article
  12. Review
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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

7 authors at 1 institution in 1 country.

Danbi YoonCollege of Pharmacy, Chung-Ang University, Seoul 06974, Korea.ORCID https://orcid.org/0009-0004-1718-5707
Ju Heun MoonCollege of Pharmacy, Chung-Ang University, Seoul 06974, Korea.ORCID https://orcid.org/0009-0009-1501-3457
Anna ChoCollege of Pharmacy, Chung-Ang University, Seoul 06974, Korea.ORCID https://orcid.org/0009-0000-2496-9850
Hyejoon BooCollege of Pharmacy, Chung-Ang University, Seoul 06974, Korea.ORCID https://orcid.org/0009-0001-8928-7954
Jeong Seok ChaCollege of Pharmacy, Chung-Ang University, Seoul 06974, Korea.ORCID https://orcid.org/0000-0001-7856-1236
Yoonji LeeCollege of Pharmacy, Chung-Ang University, Seoul 06974, Korea.ORCID https://orcid.org/0000-0002-2494-5792
Jiho YooCollege of Pharmacy, Chung-Ang University, Seoul 06974, Korea.ORCID https://orcid.org/0000-0002-0864-2142
Chung-Ang University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-glycosylation, a common post-translational modification, is widely acknowledged to have a significant effect on protein stability and folding. N-glycosylation is a complex process that occurs in the endoplasmic reticulum (ER) and requires the participation of multiple enzymes. GlcNAc-1-P-transferase (GPT) is essential for initiating N-glycosylation in the ER. Tunicamycin is a natural product that inhibits N-glycosylation and produces ER stress, and thus it is utilized in research. The molecular mechanism by which GPT triggers N-glycosylation is discussed in this review based on the GPT structure. Based on the structure of the GPT-tunicamycin complex, we also discuss how tunicamycin reduces GPT activity, which prevents N-glycosylation. This review will be highly useful for understanding the role of GPT in the N-glycosylation of proteins, as well as presents a potential for considering tunicamycin as an antibiotic treatment.

Indexed as

Endoplasmic Reticulum StressProtein Processing, Post-TranslationalEndoplasmic ReticulumGlycosylationTunicamycinTunicamycinDPAGT1GlcNAc-1-P transferaseGPTN-glyco­sylationtunicamycin

Identifiers

PMID37190766
PMCPMC10258461
OpenAlexW4376642661

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.