Evidence map›Paper›PMID 38807000›Full record

ArticleMolecular diversity2025

Computational study on the binding mechanism of allosteric drug TNO155 inhibiting SHP2

Longhua Yang, Huijian Zhao, Fanru Yuan, Mengguo Chen, Nannan Ma, Zhili Yin, Hongmin Liu, Yong Guo

Abstract read
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Article in Molecular diversity, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

8 authors.

Longhua YangSchool of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou, 450001, Henan, China. yanglh@zzu.edu.cn.
Huijian ZhaoSchool of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou, 450001, Henan, China.
Fanru YuanSchool of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou, 450001, Henan, China.
Mengguo ChenSchool of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou, 450001, Henan, China.
Nannan MaSchool of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou, 450001, Henan, China.
Zhili YinSchool of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou, 450001, Henan, China.
Hongmin LiuSchool of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou, 450001, Henan, China.
Yong GuoSchool of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou, 450001, Henan, China. guoyong_122@zzu.edu.cn.

Funding

2023 Provincial College Students' Innovation and Entrepreneurship Training Program in Henan Province No. 202310459225The Key Scientific and Technological Projects of Henan Province No. 232102311174The National Natural Science Foundation of China No. 21803058 and No. U21A20416the Science and Technology R&D Programme Joint Fund of Henan Province 232301420097
6 · The paper itself

Abstract

E76A mutations of SHP2 have been reported to associate with genetic developmental diseases and cancers, and TNO155 is one of the effective inhibitors targeted to the allosteric site 1, which has already entered the clinical stage. However, the detailed binding mechanism between them still needs further clarification at micro-atomic level. In this study, the binding mechanism of TNO155 inhibiting SHP2

Indexed as

Enzyme InhibitorsProtein Tyrosine Phosphatase, Non-Receptor Type 11Allosteric RegulationAllosteric SiteDrug DesignHumansHydrogen BondingModels, MolecularMolecular Docking SimulationMolecular Dynamics SimulationMutationProtein BindingStatic ElectricityEnzyme InhibitorsProtein Tyrosine Phosphatase, Non-Receptor Type 11Allosteric inhibitor TNO155Binding mechanismE76A mutationMolecular dynamic simulationSHP2

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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.