The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Hsp90 inhibitors: Small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation
Abstract
The 90 kDa heat shock proteins (Hsp90) are responsible for the conformational maturation of nascent polypeptides and the renaturation of denatured proteins. In transformed cells, numerous mutated and overexpressed proteins rely on the Hsp90 protein folding machinery for tumor progression. The Hsp90‐mediated protein folding process is dependent upon ATP, and when inhibitors of ATP are present, the Hsp90 machinery is unable to fold client proteins into their biologically active form, which results in the degradation of protein substrates via the ubiquitin‐proteasome pathway. Consequently, Hsp90 has evolved into a promising anti‐cancer target because multiple oncogenic proteins can be simultaneously degraded as a consequence of Hsp90 inhibition. This review serves to explain the Hsp90 protein folding process, the impact of Hsp90 inhibition, the identification of natural product inhibitors, and the development of rationally designed inhibitors of the Hsp90 protein folding machinery. © 2005 Wiley Periodicals, Inc.
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Cites
Hsp90 as a capacitor for morphological evolution
Rutherford, S. L., & Lindquist, S. (1998) · Nature · doi:10.1038/24550 · Cited by 2,270
Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8324 · Cited by 1,444
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Structure and in vivo function of Hsp90
Pearl, L. H., & Prodromou, C. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00047-0 · Cited by 317
Binding of p23 and hsp90 during assembly with the progesterone receptor.
Johnson, J. L., & Toft, D. O. (1995) · Molecular Endocrinology · doi:10.1210/mend.9.6.8592513 · Cited by 233
Signal-transduction cascades as targets for therapeutic intervention by natural products
Cardenas, M. E., Sanfridson, A., Cutler, N. S., & Heitman, J. (1998) · Trends in Biotechnology · doi:10.1016/s0167-7799(98)01239-6 · Cited by 101
Cited by
The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
Hoter, A., El-Sabban, M. E., & Naim, H. Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092560 · Cited by 693
An Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone Function
Scroggins, B. T., Robzyk, K., Wang, D., Marcu, M. G., Tsutsumi, S., Beebe, K., Cotter, R. J., Felts, S., Toft, D., Karnitz, L., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.008 · Cited by 413
Regulation and function of the human HSP90AA1 gene
Zuehlke, A. D., Beebe, K., Neckers, L., & Prince, T. (2015) · Gene · doi:10.1016/j.gene.2015.06.018 · Cited by 347
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
Can DyeCycling break the photobleaching limit in single-molecule FRET?
Vermeer, B., & Schmid, S. (2022) · Nano Research · doi:10.1007/s12274-022-4420-5 · Cited by 25
Metadata
- Authors
- Blagg, B. S. J., & Kerr, T. D.
- Venue
- Medicinal Research Reviews
- Publisher
- Wiley
- Published
- 2005-12-29
- Volume
- 26
- Issue
- 3
- Pages
- 310-338
- ISSN
- 0198-6325 (ISSN-L)
- 1098-1128
- OpenAlex
- W2951057995
- Cited by
- 189
- References
- 7
- FWCI
- 3.34
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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