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A global view of the proteome perturbations by Hsp90 inhibitors

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Published in W. A Houry. The Molecular Chaperones Interaction Networks in Protein Folding and Degradation: Springer. 2014, p. 133-150
Abstract Heat shock protein 90 (Hsp90) is a highly efficient molecular chaperone and a major hub in the protein network that maintains cellular homeostasis and function. The qualitative and quantitative changes and rewiring of this protein network in tumor cells make them vastly dependent on Hsp90, which therefore becomes a key target to fight cancer. The inhibition of Hsp90 creates a profound transformation in the cell proteome. In this chapter, we review and analyze the most recent efforts that take advantage of the druggability of Hsp90 in order to understand the global changes at the proteome level that this inhibition produces. The considerable impact that the targeting of Hsp90 has on the structure of these protein networks is also discussed.
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ISBN: 978-1-4939-1129-5
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Book chapter (Published version) (3.6 MB) - document accessible for UNIGE members only Limited access to UNIGE
Structures
Research group Groupe Picard
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ECHEVERRIA, Pablo Christian, PICARD, Didier. A global view of the proteome perturbations by Hsp90 inhibitors. In: W. A Houry (Ed.). The Molecular Chaperones Interaction Networks in Protein Folding and Degradation. [s.l.] : Springer, 2014. p. 133-150. https://archive-ouverte.unige.ch/unige:74466

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Deposited on : 2015-08-04

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