ArticleThe Journal of biological chemistry2013
Gedunin inactivates the co-chaperone p23 protein causing cancer cell death by apoptosis.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed, 145 citations in OpenAlex.
- Heat Shock Protein 90: From Molecular Chaperone Function to Therapeutic Targeting in Malignancies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Evolution of Hsp90 targeting: From stress biology to clinical translation.Cell stress & chaperones · 2026Review
- Chemical and Antiplasmodial Investigations onACS omega · 2025Article
- p23 protects against ferroptosis of brain microvascular endothelial cells in ischemic stroke.International journal of molecular medicine · 2025Article
- Geldanamycins: Potent Hsp90 Inhibitors with Significant Potential in Cancer Therapy.International journal of molecular sciences · 2024Review
- Gedunin modulates cellular growth and apoptosis in glioblastoma cell lines.Cancer reports (Hoboken, N.J.) · 2024Article
- FRET Assays for the Identification ofPharmaceuticals (Basel, Switzerland) · 2024Article
- Review
- The Interplay between Heat Shock Proteins and Cancer Pathogenesis: A Novel Strategy for Cancer Therapeutics.Cancers · 2024Review
- The integration of multidisciplinary approaches revealed PTGES3 as a novel drug target for breast cancer treatment.Journal of translational medicine · 2024Article
- Enniatin A inhibits the chaperone Hsp90 and unleashes the immune system against triple-negative breast cancer.iScience · 2023Article
- Uncovering the Role of Natural and Synthetic Small Molecules in Counteracting the Burden of α-Synuclein Aggregates and Related Toxicity in Different Models of Parkinson's Disease.International journal of molecular sciences · 2023Review
- Capsaicin binds the N-terminus of Hsp90, induces lysosomal degradation of Hsp70, and enhances the anti-tumor effects of 17-AAG (Tanespimycin).Scientific reports · 2023Article
- Natural Compounds: Co-Delivery Strategies with Chemotherapeutic Agents or Nucleic Acids Using Lipid-Based Nanocarriers.Pharmaceutics · 2023Review
- Impact of Co-chaperones and Posttranslational Modifications Toward Hsp90 Drug Sensitivity.Sub-cellular biochemistry · 2023Article
- Comprehensive pan-cancer analysis of PTGES3 and its prognostic role in hepatocellular carcinoma.Frontiers in oncology · 2023Article
- HSP90 mediates the connection of multiple programmed cell death in diseases.Cell death & disease · 2022Review
- Identification of Gedunin from a Phytochemical Depository as a Novel Multidrug Resistance-Bypassing Tubulin Inhibitor of Cancer Cells.Molecules (Basel, Switzerland) · 2022Article
- Targeting HSP90 as a Novel Therapy for Cancer: Mechanistic Insights and Translational Relevance.Cells · 2022Review
- Hsp90 and Associated Co-Chaperones of the Malaria Parasite.Biomolecules · 2022Review
11 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 5 institutions in 1 country.
Funding
Abstract
Pharmacological inhibition of Hsp90 is an exciting option for cancer therapy. The clinical efficacy of Hsp90 inhibitors is, however, less than expected. Binding of the co-chaperone p23 to Hsp90 and induced overexpression of anti-apoptotic proteins Hsp70 and Hsp27 are thought to contribute to this outcome. Herein, we report that the natural product gedunin may provide a new alternative to inactivate the Hsp90 machine. We show that gedunin directly binds to p23 and inactivates it, without overexpression of Hsp27 and relatively modest induction of Hsp70. Using molecular docking and mutational analysis, we mapped the gedunin-binding site on p23. Functional analysis shows that gedunin inhibits the p23 chaperoning activity, blocks its cellular interaction with Hsp90, and interferes with p23-mediated gene regulation. Cell treatment with gedunin leads to cancer cell death by apoptosis through inactivation of p23 and activation of caspase 7, which cleaves p23 at the C terminus. These results provide important insight into the molecular mechanism of action of this promising lead compound.
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Registered trials
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.