The DOI matches its Crossref record; 32 of the 36 references it cites were found in a registry or an index.
Dual Targeting of HSC70 and HSP72 Inhibits HSP90 Function and Induces Tumor-Specific Apoptosis
Open accessAbstract
Heat-shock protein 70 (HSP70) isoforms contribute to tumorigenesis through their well-documented antiapoptotic activity and via their role as cochaperones for the HSP90 molecular chaperone. HSP70 expression is induced following treatment with HSP90 inhibitors, which may attenuate the cell death effects of this class of inhibitor. Here we show that silencing either heat-shock cognate 70 (HSC70) or HSP72 expression in human cancer cell lines has no effect on HSP90 activity or cell proliferation. However, simultaneously reducing the expression of both of these isoforms induces proteasome-dependent degradation of HSP90 client proteins, G1 cell-cycle arrest, and extensive tumor-specific apoptosis. Importantly, simultaneous silencing of HSP70 isoforms in nontumorigenic cell lines does not result in comparable growth arrest or induction of apoptosis, indicating a potential therapeutic window.
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“the latter of which may promote tumor resistance to therapy (23, 25)”
From FKBP51 Promotes Assembly of the Hsp90 Chaperone Complex and Regulates Androgen Receptor Signaling in Prostate Cancer Cells (2010) · cites this paper as [23]
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Items 301–314 of 314
A Novel HSP90 Inhibitor to Disrupt HSP90/p50CDC37 Complex for Pancreatic Cancer Therapy.
Zhang, T. (2011) · Deep Blue (University of Michigan)
Liu, G., Wang, X., Yang, X., Wu, J., Li, Y., Lu, Y., Shang, A., Chen, C., & Sun, R. (2026) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-025-05461-2
Heat Shock Proteins as Targets for Cancer Therapeutics
Trikala, A., Shen, B., & Bhardwaj, S. (2026) · Journal of Clinical Medicine · doi:10.3390/jcm15103605
Hsp90 Inhibition on the Western Blot: N‐Terminal Versus C‐Terminal Inhibitors in Breast Cancer
Dernovšek, J., Cingl, J., Fonović, U. P., & Tomašič, T. (2026) · Medicinal Research Reviews · doi:10.1002/med.70079
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Research progress on the BAG3-HSP70 axis-mediated autophagy in acute myeloid leukemia
Liu, Y., & Wu, T. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1980188
BindingDB (2014) · UC San Diego · doi:10.7270/q2q81fhc
BindingDB Entry 50032408: ATPases as drug targets: insights from heat shock proteins 70 and 90.
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Metadata
- Authors
- Powers, M. V., Clarke, P. A., & Workman, P.
- Affiliations
- Institute of Cancer Research (GB)
- Corresponding author
- Workman, Paul
- Venue
- Cancer Cell
- Publisher
- Elsevier BV
- Published
- 2008-09
- Volume
- 14
- Issue
- 3
- Pages
- 250-262
- ISSN
- 1535-6108 (ISSN-L)
- OpenAlex
- W2170573493
- Cited by
- 307
- References
- 36
- Citations by year
- 2026: 7 · 2025: 4 · 2024: 5 · 2023: 5 · 2022: 9 · 2021: 15 · 2020: 8 · 2019: 17 · 2018: 16 · 2017: 18 · 2016: 24 · 2015: 25 · 2014: 27 · 2013: 29 · 2012: 24
- FWCI
- 10.38
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cancer Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Cancer Research UK (C309/A8274, C309/A2187)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- Hsc70, HSP72, HSP90, Hsp90 inhibitors, proteasomal degradation, Hsp90 client proteins, G1 cell cycle arrest, heat shock proteins, cancer cell lines, therapeutic window, anti-apoptotic effects
- MeSH terms
- Bortezomib, Boronic Acids, Cell Cycle, Cell Line, Humans, Kinetics, Neoplasms, Poly(ADP-ribose) Polymerases, Protease Inhibitors, Pyrazines, Transfection, Benzoquinones, Apoptosis, HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Proto-Oncogene Proteins c-raf, Protein Isoforms, RNA, Small Interfering, HCT116 Cells, Cell Line, Tumor, Proteasome Endopeptidase Complex, Lactams, Macrocyclic, Cell Proliferation, HSC70 Heat-Shock Proteins, HSP72 Heat-Shock Proteins, Cyclin-Dependent Kinase 4, Ubiquitination, Proteasome Inhibitors
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