The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Therapeutic and diagnostic implications of Hsp90 activation
Open accessAbstract
The molecular chaperone heat-shock protein 90 (Hsp90) is involved in the stabilization and conformational maturation of many signaling proteins that are deregulated in cancers. Hsp90 inhibition results in the proteasomal degradation of these client proteins and leads to potent antitumor activity. The Hsp90 inhibitor 17-allylaminogeldanamycin (17-AAG) is presently in clinical trials. Recent work has identified the role of Hsp90 in multiple signal transduction pathways and revealed that the molecular mechanism of tumor selectivity by Hsp90 inhibitors is the result of an activated, high-affinity conformation of Hsp90 in tumors. This review discusses these recent advances in the understanding of tumor Hsp90 for the treatment and diagnosis of cancer. In addition, the role of Hsp90 in non-oncological diseases will also be discussed.
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Cites
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Cited by
HSP90 and the chaperoning of cancer
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Hsp90 Potentiates the Rapid Evolution of New Traits: Drug Resistance in Diverse Fungi
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Heat Shock Proteins and Cancer
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Metadata
- Authors
- Kamal, A., Boehm, M. F., & Burrows, F. J.
- Venue
- Trends in Molecular Medicine
- Publisher
- Elsevier BV
- Published
- 2004-06
- Volume
- 10
- Issue
- 6
- Pages
- 283-290
- ISSN
- 1471-4914 (ISSN-L)
- OpenAlex
- W2136966549
- Cited by
- 278
- References
- 8
- FWCI
- 1.17
- Type
- journal article
- Language
- en
- Open access
- bronze
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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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