Evidence map›Paper›PMID 41417189›Full record

ArticleMolecular diversity2026

Discovery of a small-molecule inhibitor targeting human GMP synthetase.

Zhiyan Wang, Rajamanikandan Sundarraj, Boao Mao, Jun-An Ma, Kunrong Mei, Zhiguang Yuchi

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular diversity, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Piperazine derivatives as anticancer agents: a medicinal chemistry review of structure, mechanism, and clinical translation.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
    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

6 authors.

Zhiyan Wang *Department of Molecular Pharmacology, National Clinical Research Center for Cancer, Key Laboratory of Cancer Prevention and Therapy, Tianjin, Tianjin's Clinical Research Center for Cancer, Tianjin Medical University Cancer Institute & Hospital, Tianjin, 300060, China.
Rajamanikandan Sundarraj *State Key Laboratory of Synthetic Biology and Frontiers Science Center for Synthetic Biology; Tianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, School of Pharmaceutical Science and Technology, Faculty of Medicine, Tianjin University, Tianjin, 300072, China.
Boao MaoState Key Laboratory of Synthetic Biology and Frontiers Science Center for Synthetic Biology; Tianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, School of Pharmaceutical Science and Technology, Faculty of Medicine, Tianjin University, Tianjin, 300072, China.
Jun-An MaDepartment of Chemistry, State Key Laboratory Synthetic Biology, Tianjin University, Tianjin, 300072, China.
Kunrong MeiState Key Laboratory of Synthetic Biology and Frontiers Science Center for Synthetic Biology; Tianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, School of Pharmaceutical Science and Technology, Faculty of Medicine, Tianjin University, Tianjin, 300072, China. kmei@tju.edu.cn.
Zhiguang YuchiDepartment of Molecular Pharmacology, National Clinical Research Center for Cancer, Key Laboratory of Cancer Prevention and Therapy, Tianjin, Tianjin's Clinical Research Center for Cancer, Tianjin Medical University Cancer Institute & Hospital, Tianjin, 300060, China. yuchi@tju.edu.cn.

Funding

Fundamental and Interdisciplinary Disciplines Breakthrough Plan of the Ministry of Education of China JYB2025XDXM503Haihe Laboratory of Sustainable Chemical Transformations 24HHWCSS00005National Key Research and Development Program of China 2025YFC3409400National Natural Science Foundation of China 32372580National Natural Science Foundation of China 92156025
6 · The paper itself

Abstract

Guanosine monophosphate synthetase (GMPS) catalyzes the ATP-dependent conversion of xanthosine monophosphate (XMP) to guanosine monophosphate (GMP), a key step in de novo purine biosynthesis. Dysregulation of GMPS expression has been implicated in multiple cancers, underscoring its potential as a therapeutic target. Here, we identified a novel small molecule GMPS inhibitor, G18, through large-scale virtual screening of 1.27 million compounds. Biochemical validation using an inorganic phosphatase (IPP1)-coupled colorimetric assay demonstrated that G18 inhibits GMPS with an IC

Indexed as

Carbon-Nitrogen LigasesDrug DiscoveryEnzyme InhibitorsSmall Molecule LibrariesAntineoplastic AgentsCell ProliferationHeLa CellsHumansMolecular Docking SimulationMolecular Dynamics SimulationProtein BindingAntineoplastic AgentsCarbon-Nitrogen LigasesEnzyme InhibitorsGMP synthase (glutamine-hydrolyzing)Small Molecule LibrariesAnticancerG18Guanosine monophosphate synthetase (GMPS)Molecular targetStructure-based virtual screening

Identifiers

What OpenQuestion holds

Textmetadata
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.