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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
Addiction to Oncogenes--the Achilles Heal of Cancer
Weinstein, I. B. (2002) · Science · doi:10.1126/science.1073096 · Cited by 1,764
A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
Kamal, A., Thao, L., Sensintaffar, J., Zhang, L., Boehm, M. F., Fritz, L. C., & Burrows, F. J. (2003) · Nature · doi:10.1038/nature01913 · Cited by 1,380
The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
Daugaard, M., Rohde, M., & Jäättelä, M. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.05.039 · Cited by 1,177
Pathways of chaperone-mediated protein folding in the cytosol
Young, J. C., Agashe, V. R., Siegers, K., & Hartl, F. U. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1492 · Cited by 1,121
Strategies for silencing human disease using RNA interference
Kim, D. H., & Rossi, J. J. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2006 · Cited by 1,078
Heat Shock Proteins 27 and 70: Anti-Apoptotic Proteins with Tumorigenic Properties
Garrido, C., Brunet, M., Mirjolet, C., Zermati, Y., Schmitt, E., & Kroemer, G. (2006) · Cell Cycle · doi:10.4161/cc.5.22.3448 · Cited by 676
Drugging the Cancer Chaperone HSP90
Workman, P., Burrows, F. J., Neckers, L., & Rosen, N. X. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1391.012 · Cited by 531
Self-citationMolecular chaperones and the stress of oncogenesis
Mosser, D. D., & Morimoto, R. I. (2004) · Oncogene · doi:10.1038/sj.onc.1207529 · Cited by 512
Banerji, U., O’Donnell, A. E., Scurr, M. R., Pacey, S., Stapleton, S., Asad, Y. J., Simmons, L., Maloney, A., Raynaud, F. I., Campbell, M. J., et al. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.00.612 · Cited by 490
Self-citation
Flagged first, then by citations
4 of the 36 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Targeting the dynamic HSP90 complex in cancer
Trepel, J. B., Mollapour, M., Giaccone, G., & Neckers, L. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2887 · Cited by 1,523
Hsp90 Molecular Chaperone Inhibitors: Are We There Yet?
Neckers, L., & Workman, P. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-1000 · Cited by 968
Self-citationMurphy, M. E. (2013) · Carcinogenesis · doi:10.1093/carcin/bgt111 · Cited by 529
Endoplasmic Reticulum Stress in Malignancy
Clarke, H. J., Chambers, J. E., Liniker, E., & Marciniak, S. J. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.03.015 · Cited by 473
Targeting heat shock proteins in cancer
Jégo, G., Hazoumé, A., Seigneuric, R., & Garrido, C. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.10.014 · Cited by 466
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
