Evidence map›Paper›PMID 42155112›Full record

ArticlePest management science2026

Discovery of novel uridine-based chitin synthase inhibitors: Design, synthesis and structure-activity relationships.

Xiangyang Lv, Bin Liu, Hanghang Fu, Dongyu Lei, Sichang Yan, Quanjia Chen, Lu Jin, Le Pan

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Pest management science, 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
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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

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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

8 authors.

Xiangyang Lv *College of Chemistry and Chemical Engineering, Xinjiang Agricultural University, Urumqi, P. R. China.
Bin Liu *College of Chemistry and Chemical Engineering, Xinjiang Agricultural University, Urumqi, P. R. China.
Hanghang FuCollege of Chemistry and Chemical Engineering, Xinjiang Agricultural University, Urumqi, P. R. China.
Dongyu LeiDepartment of Physiology, Preclinical School, Xinjiang Medical University, Urumqi, P. R. China.
Sichang YanCollege of Chemistry and Chemical Engineering, Xinjiang Agricultural University, Urumqi, P. R. China.
Quanjia ChenCollege of Agriculture, Xinjiang Agricultural University, Urumqi, P. R. China.
Lu JinCollege of Chemistry and Chemical Engineering, Xinjiang Agricultural University, Urumqi, P. R. China.
Le PanCollege of Chemistry and Chemical Engineering, Xinjiang Agricultural University, Urumqi, P. R. China.ORCID https://orcid.org/0009-0006-9214-9639

Funding

National Natural Science Foundation of China 31960547The Fund of the Key Laboratory of Xinjiang Uygur Autonomous Region on High-value Utilization of Agricultural and Animal Husbandry By-products.Tianshan Innovation Team Foundation of Xinjiang, China 2024D14008
6 · The paper itself

Abstract

backgroundChitin synthase (CHS) enables the construction of fungi cell wall and insect skeleton by catalyzing the formation of chitin. CHS inhibitor (CHSI) disrupts the integrity of these structural barriers, leading to fungal cell lysis. Notably, CHSIs are considered non-toxic to vertebrates, making CHS a promising target for the development of novel antifungal agents.

resultsThirty-three novel uridine-based derivatives (UDs) were designed and synthesized through fragment-based drug design (FBDD) to discover potential CHSIs. Bioassays demonstrated that most of the synthesized compounds exhibited excellent fungicidal activity against Alternaria alternata and Botrytis cinerea, with inhibition rates exceeding 80% at 100 μg mL

conclusionCompound 5a is a promising antifungal agent with a unique mechanism of action by targeting fungal CHS. This study discovered a series of novel CHSIs with excellent fungicidal activities, offering valuable candidates for fungicide development. © 2026 Society of Chemical Industry.

Indexed as

AlternariaAntifungal AgentsBotrytisChitin SynthaseEnzyme InhibitorsFungicides, IndustrialUridineDrug DesignStructure-Activity RelationshipAntifungal AgentsChitin SynthaseEnzyme InhibitorsFungicides, IndustrialUridineantifungal activitychitin synthase inhibitorsmolecular dockingstructure–activity relationshipsuridine derivatives

Identifiers

PMID42155112
PMCPMC13453165

What OpenQuestion holds

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Read underepoch 390

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.