Evidence map›Paper›PMID 37553334›Full record

ArticleNature communications2023

Structure, catalysis, chitin transport, and selective inhibition of chitin synthase.

Dan-Dan Chen, Zhao-Bin Wang, Le-Xuan Wang, Peng Zhao, Cai-Hong Yun, Lin Bai

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
10.5field-weighted citation impact, top 1% 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

34 citing papers in PubMed, 68 citations in OpenAlex.

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  16. bioRxiv : the preprint server for biology · 2025
    Article
  17. Article
  18. Fungal Chitin Synthases: Structure, Function, and Regulation.Journal of fungi (Basel, Switzerland) · 2025
    Review
  19. Review
  20. 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

6 authors at 1 institution in 1 country.

Dan-Dan Chen *Department of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking University, Beijing, China.
Zhao-Bin Wang *Department of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking University, Beijing, China.
Le-Xuan WangDepartment of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking University, Beijing, China.
Peng ZhaoDepartment of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking University, Beijing, China.
Cai-Hong YunDepartment of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking University, Beijing, China. yunch@hsc.pku.edu.cn.ORCID http://orcid.org/0000-0002-5880-8307
Lin BaiDepartment of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking University, Beijing, China. lbai@pku.edu.cn.ORCID http://orcid.org/0000-0002-7535-7819
Peking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chitin is one of the most abundant natural biopolymers and serves as a critical structural component of extracellular matrices, including fungal cell walls and insect exoskeletons. As a linear polymer of β-(1,4)-linked N-acetylglucosamine, chitin is synthesized by chitin synthases, which are recognized as targets for antifungal and anti-insect drugs. In this study, we determine seven different cryo-electron microscopy structures of a Saccharomyces cerevisiae chitin synthase in the absence and presence of glycosyl donor, acceptor, product, or peptidyl nucleoside inhibitors. Combined with functional analyses, these structures show how the donor and acceptor substrates bind in the active site, how substrate hydrolysis drives self-priming, how a chitin-conducting transmembrane channel opens, and how peptidyl nucleoside inhibitors inhibit chitin synthase. Our work provides a structural basis for understanding the function and inhibition of chitin synthase.

Indexed as

ChitinChitin SynthaseCatalysisCryoelectron MicroscopyNucleosidesSaccharomyces cerevisiaeChitinChitin SynthaseNucleosides

Identifiers

PMID37553334
PMCPMC10409773
OpenAlexW4385644820

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.