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Hsp90 isoforms: functions, expression and clinical importance
Open accessAbstract
The 90 kDa heat shock protein, Hsp90, is a main functional component of an important cytoplasmic chaperone complex, and it is involved in various cellular processes, such as cell proliferation, differentiation and apoptosis. Identification of Hsp90 as a molecular target of various anticancer drugs highlighted its importance from the clinical point of view. Here we summarize the current knowledge on various Hsp90 isoforms regarding their genomic location, molecular evolution, functional differences, differential induction after various environmental stresses and in pathological conditions as well as the growing importance of discriminating between Hsp90 isoforms in clinical practice.
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Citations
Cited by
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
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
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
Li, J., Soroka, J., & Buchner, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.003 · Cited by 498
The Hsp90 molecular chaperone: an open and shut case for treatment
Pearl, L. H., Prodromou, C., & Workman, P. (2008) · Biochemical Journal · doi:10.1042/bj20071640 · Cited by 447
Heat shock proteins: Cellular and molecular mechanisms in the central nervous system
Stetler, R. A., Gan, Y., Zhang, W., Liou, A. K., Gao, Y., Cao, G., & Chen, J. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.05.002 · Cited by 305
Metadata
- Authors
- Subbarao Sreedhar, A., Kalmár, É., Csermely, P., & Shen, Y.-F.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2004-03-05
- Volume
- 562
- Issue
- 1-3
- Pages
- 11-15
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2103327164
- Cited by
- 620
- References
- 0
- FWCI
- 5.58
- Type
- journal article
- Language
- en
- Open access
- bronze
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