Evidence map›Paper›PMID 40664262›Full record

ArticleJournal of advanced research2026

Identification of Bruceine A as a novel HSP90AB1 inhibitor for suppressing hepatocellular carcinoma growth.

Weijun Peng, Dazun Shi, Die Xu, Xiaowei Wang, Yisi Cai, Yejun Tan, Yuqing Liu, Yajuan Cui, Lemei Zhu, Ke Ye and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of advanced research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

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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

12 authors.

Weijun PengDepartment of Integrated Traditional Chinese & Western Medicine, National Clinical Research Center for Metabolic Diseases, The Second Xiangya Hospital, Central South University, Changsha 410011, China; Academician Workstation, Changsha Medical University, Changsha 410219, China. Electronic address: pengweijun87@csu.edu.cn.
Dazun ShiDepartment of Gynecology, Xiangya Hospital, Central South University, Changsha 410008, China; The Hunan Engineering Research Center of Skin Health and Disease, Department of Dermatology, Xiangya Hospital, Central South University, Changsha 410008, China.
Die XuDepartment of Integrated Traditional Chinese & Western Medicine, National Clinical Research Center for Metabolic Diseases, The Second Xiangya Hospital, Central South University, Changsha 410011, China.
Xiaowei WangDepartment of Pathology, The Second Xiangya Hospital, Central South University, Changsha, Hunan Province 410011, China.
Yisi CaiDepartment of Integrated Traditional Chinese & Western Medicine, National Clinical Research Center for Metabolic Diseases, The Second Xiangya Hospital, Central South University, Changsha 410011, China.
Yejun TanSchool of Mathematics, University of Minnesota Twin Cities, Minneapolis 55455 MN, USA.
Yuqing LiuDepartment of Cardiology, The Third Xiangya Hospital of Central South University, Central South University, Changsha 410013, China.
Yajuan CuiDepartment of Hematology, Institute of Molecular Hematology, The Second Xiangya Hospital, Central South University, Changsha 410011, China.
Lemei ZhuDepartment of Integrated Traditional Chinese & Western Medicine, National Clinical Research Center for Metabolic Diseases, The Second Xiangya Hospital, Central South University, Changsha 410011, China; Academician Workstation, Changsha Medical University, Changsha 410219, China.
Ke YeDepartment of Liver Surgery, Xiangya Hospital, Central South University, Changsha 410008, China.
Kuan HuDepartment of Liver Surgery, Xiangya Hospital, Central South University, Changsha 410008, China.
Jun FuClinical Research Center (CRC), Medical Pathology Center (MPC), Cancer Early Detection and Treatment Center (CEDTC), and Translational Medicine Research Center (TMRC), Chongqing University Three Gorges Hospital, Chongqing University, Wanzhou, Chongqing, China; Chongqing University, Three Gorges Hospital, and Academy for Advanced Interdisciplinary Technology, CQU-Ferenc Krausz Nobel Laureate Scientific Workstation, Chongqing, China; Institute of Advanced Interdisciplinary Studies, Chongqing University, China; Chongqing Technical Innovation Center for Quality Evaluation and Identification of Authentic Medicinal Herbs, Wanzhou, Chongqing, China; School of Medicine, Chongqing University, Chongqing, China. Electronic address: jf1977@cqu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

introductionHepatocellular carcinoma (HCC) remains a leading cause of cancer-related mortality worldwide, with limited therapeutic options available. Natural compounds, such as Bruceine A (BRA), derived from Brucea javanica, have emerged as promising anticancer agents. However, the underlying mechanisms of action in HCC remain largely unexplored.

objectivesThis study aims to identify the molecular target of BRA and elucidate its anticancer effects.

methodsPatient-derived organoids (PDOs) and xenograft (PDX) models were employed to assess the anticancer activity of BRA. Chemical proteomics and binding assays, including MST, SPR, and CETSA, facilitated the identification of heat shock protein 90α family class B member 1 (HSP90AB1) as the primary target of BRA, with SER-108 identified as the critical binding site. HSP90AB1 knockdown further confirmed its pivotal role in BRA-mediated anti-HCC effects. Additionally, TMT-based proteomics was applied to investigate the downstream chaperones of HSP90AB1.

resultsBRA significantly suppressed HCC proliferation and induced apoptosis. Molecular analyses revealed HSP90AB1 as the key target, with SER-108 as the critical binding site. Proteomic analysis identified downstream HSP90AB1 partner proteins, including PIK3CG, EGFR, and KDM5C, as contributors to BRA's inhibitory effects on HCC progression.

conclusionThis study establishes HSP90AB1 as the primary target of BRA, which exerts its anti-HCC effects through modulation of downstream chaperones PIK3CG, EGFR, and KDM5C. These findings highlight the therapeutic potential of BRA in HCC and suggest that HSP90AB1 represents a promising target for future drug development.

Indexed as

Antineoplastic AgentsCarcinoma, HepatocellularHSP90 Heat-Shock ProteinsLiver NeoplasmsAnimalsApoptosisCell Line, TumorCell ProliferationHumansMiceMice, NudeXenograft Model Antitumor AssaysAntineoplastic AgentsHSP90AB1 protein, humanHSP90 Heat-Shock ProteinsBruceine AChemical proteomicsEGFRHepatocellular carcinomaHSP90AB1KDM5CPIK3CGTarget identification

Identifiers

PMID40664262
PMCPMC13001032

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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.