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Heat shock protein 90 targeting therapy: state of the art and future perspective
Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that plays a role in stabilizing and activating more than 200 client proteins. It is required for the stability and function of numerous oncogenic signaling proteins that determine the hallmarks of cancer. Since the initial discov...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Leibniz Research Centre for Working Environment and Human Factors
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4652636/ https://www.ncbi.nlm.nih.gov/pubmed/26600741 http://dx.doi.org/10.17179/excli2014-586 |
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author | Tatokoro, Manabu Koga, Fumitaka Yoshida, Soichiro Kihara, Kazunori |
author_facet | Tatokoro, Manabu Koga, Fumitaka Yoshida, Soichiro Kihara, Kazunori |
author_sort | Tatokoro, Manabu |
collection | PubMed |
description | Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that plays a role in stabilizing and activating more than 200 client proteins. It is required for the stability and function of numerous oncogenic signaling proteins that determine the hallmarks of cancer. Since the initial discovery of the first Hsp90 inhibitor in the 1970s, multiple phase II and III clinical trials of several Hsp90 inhibitors have been undertaken. This review provides an overview of the current status on clinical trials of Hsp90 inhibitors and future perspectives on novel anticancer strategies using Hsp90 inhibitors. |
format | Online Article Text |
id | pubmed-4652636 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Leibniz Research Centre for Working Environment and Human Factors |
record_format | MEDLINE/PubMed |
spelling | pubmed-46526362015-11-23 Heat shock protein 90 targeting therapy: state of the art and future perspective Tatokoro, Manabu Koga, Fumitaka Yoshida, Soichiro Kihara, Kazunori EXCLI J Review Article Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that plays a role in stabilizing and activating more than 200 client proteins. It is required for the stability and function of numerous oncogenic signaling proteins that determine the hallmarks of cancer. Since the initial discovery of the first Hsp90 inhibitor in the 1970s, multiple phase II and III clinical trials of several Hsp90 inhibitors have been undertaken. This review provides an overview of the current status on clinical trials of Hsp90 inhibitors and future perspectives on novel anticancer strategies using Hsp90 inhibitors. Leibniz Research Centre for Working Environment and Human Factors 2015-01-06 /pmc/articles/PMC4652636/ /pubmed/26600741 http://dx.doi.org/10.17179/excli2014-586 Text en Copyright © 2015 Tatokoro et al. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Licence (http://creativecommons.org/licenses/by/4.0/) You are free to copy, distribute and transmit the work, provided the original author and source are credited. |
spellingShingle | Review Article Tatokoro, Manabu Koga, Fumitaka Yoshida, Soichiro Kihara, Kazunori Heat shock protein 90 targeting therapy: state of the art and future perspective |
title | Heat shock protein 90 targeting therapy: state of the art and future perspective |
title_full | Heat shock protein 90 targeting therapy: state of the art and future perspective |
title_fullStr | Heat shock protein 90 targeting therapy: state of the art and future perspective |
title_full_unstemmed | Heat shock protein 90 targeting therapy: state of the art and future perspective |
title_short | Heat shock protein 90 targeting therapy: state of the art and future perspective |
title_sort | heat shock protein 90 targeting therapy: state of the art and future perspective |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4652636/ https://www.ncbi.nlm.nih.gov/pubmed/26600741 http://dx.doi.org/10.17179/excli2014-586 |
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