Evidence map›Paper›PMID 40324009›Full record

ArticlePloS one2025

Virtual screening and molecular dynamics simulation study of ATP-competitive inhibitors targeting mTOR protein.

Mei-Yu Jin, Hao Yu, Qiong Deng, Zhu Wang, Jie-Yan Wang, Hao-Long Li, Hui Liang

Abstract read
In one paragraph

Article in PloS one, 2025. 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. 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

7 authors.

Mei-Yu JinShenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen, China.
Hao YuState Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, Institute of Zoonosis, and College of Veterinary Medicine, Jilin University, Changchun, China.
Qiong DengDepartment of Urology, People's Hospital of Longhua, Shenzhen, China.
Zhu WangDepartment of Urology, People's Hospital of Longhua, Shenzhen, China.
Jie-Yan WangDepartment of Urology, People's Hospital of Longhua, Shenzhen, China.
Hao-Long LiShenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen, China.
Hui LiangDepartment of Urology, People's Hospital of Longhua, Shenzhen, China.ORCID https://orcid.org/0000-0003-1460-8335

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In order to explore efficient ATP-competitive mTOR inhibitors and aid the development of targeted anticancer drugs, this study focuses on virtual screening and molecular dynamics simulations. The compounds were sourced from the ChemDiv commercial compound library, and through virtual screening, 50 ligands with favorable binding modes and excellent docking scores were selected from 902,998 compounds. Molecular dynamics simulations, including RMSD (Root Mean Square Deviation) and RMSF (Root Mean Square Fluctuation), were used to further evaluate these 50 ligands. Structural stability, key residue interactions, hydrogen bonding, binding free energy, and other factors were quantitatively and qualitatively analyzed. Top1, top2, and top6, which exhibited outstanding performance, were identified. Simulations revealed that they bind stably in the active region of the mTOR protein, forming hydrogen bonds, π-π interactions, and hydrophobic interactions with key amino acid residues such as VAL-2240 and TRP-2239. This study provides a solid theoretical foundation for the development of mTOR inhibitors. Subsequent efforts will focus on optimizing these compounds, targeting structural adjustments to enhance their biological activity and specificity towards mTOR, thereby achieving more precise targeting and treatment of tumors.

Indexed as

Adenosine TriphosphateMolecular Dynamics SimulationMTOR InhibitorsTOR Serine-Threonine KinasesHumansHydrogen BondingLigandsMolecular Docking SimulationProtein BindingAdenosine TriphosphateLigandsMTOR InhibitorsMTOR protein, humanTOR Serine-Threonine Kinases

Identifiers

PMID40324009
PMCPMC12052163

What Socratic 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 Socratic graph.