The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Heat Shock Protein 90 as a Drug Target: Some Like It Hot
Abstract
Heat shock protein 90 (HSP90) is a ubiquitously expressed chaperone that is involved in the posttranslational folding and stability of proteins. Inhibition at the NH2-terminal ATP-binding site leads to the degradation of client proteins by the ubiquitin proteasome pathway. Inhibition of HSP90 leads to the degradation of known oncogenes, such as ERB-B2, BRAF, and BCR-ABL, leading to the combinatorial blockade of multiple signal transduction pathways, such as the RAS-RAF-mitogen-activated protein/extracellular signal-regulated kinase kinase-extracellular signal-regulated kinase and phosphatidylinositol 3-kinase pathways. Multiple structurally diverse HSP90 inhibitors are undergoing early clinical evaluation. The clinical focus of these drugs should be solid tumors, such as breast, prostate, and lung cancers, along with malignant melanoma, in addition to hematologic malignancies, such as chronic myeloid leukemia and multiple myeloma. HSP90 inhibitors can be used as single agents or in combination with other targeted treatments or conventional forms of treatment such as chemotherapy and radiotherapy. Clinical trials evaluating efficacy of these agents should include innovative designs to capture cytostasis evidenced by clinical nonprogression and enrichment of patient populations by molecular characterization. The results of clinical trials evaluating the efficacy of drugs targeting this exciting target are awaited.
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Cites
Mutations of the BRAF gene in human cancer
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Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1α-degradative pathway
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Haigis, K. M., Kendall, K. R., Wang, Y., Cheung, A., Haigis, M. C., Glickman, J. N., Niwa-Kawakita, M., Sweet-Cordero, A., Sebolt-Leopold, J., Shannon, K. M., et al. (2008) · Nature Genetics · doi:10.1038/ng.115 · Cited by 610
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The Hsp90 molecular chaperone: an open and shut case for treatment
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Cited by
Combinatorial drug therapy for cancer in the post-genomic era
Al-Lazikani, B., Banerji, U., & Workman, P. (2012) · Nature Biotechnology · doi:10.1038/nbt.2284 · Cited by 1,070
Self-citationUpdate on Hsp90 Inhibitors in Clinical Trial
Kim, Y., Alarcon, S., Lee, S., Lee, M.-J., Giaccone, G., Neckers, L., & Trepel, J. (2009) · Current Topics in Medicinal Chemistry · doi:10.2174/156802609789895728 · Cited by 311
Woodhead, A. J., Angove, H., Carr, M. G., Chessari, G., Congreve, M., Coyle, J. E., Cosme, J., Graham, B., Day, P. J., Downham, R., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100060b · Cited by 264
Piotrowska, Z., Costa, D. B., Oxnard, G. R., Huberman, M., Gainor, J. F., Lennes, I. T., Muzikansky, A., Shaw, A. T., Azzoli, C. G., Heist, R. S., et al. (2018) · Annals of Oncology · doi:10.1093/annonc/mdy336 · Cited by 79
Wu (2011) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2011.600 · Cited by 59
Metadata
- Authors
- Banerji, U.
- Venue
- Clinical Cancer Research
- Published
- 2008-12-31
- Volume
- 15
- Issue
- 1
- Pages
- 9-14
- ISSN
- 1078-0432 (ISSN-L)
- 1557-3265
- OpenAlex
- W2131384028
- Cited by
- 244
- References
- 8
- FWCI
- 9.68
- Type
- journal article
- Language
- en
- Open access
- closed
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