Hsp90 is cleaved by reactive oxygen species at a highly conserved N-terminal amino acid motif.

Hsp90 is cleaved by reactive oxygen species at a highly conserved N-terminal amino acid motif.

Hsp90 is an essential chaperone that is necessary for the folding, stability and activity of numerous proteins. In this study, we demonstrate that free radicals formed during oxidative stress conditions can cleave Hsp90. This cleavage occurs through a Fenton reaction which requires the presence of r...

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Bibliographic Details
Main Authors: Raphaël Beck, Nicolas Dejeans, Christophe Glorieux, Mélanie Creton, Edouard Delaive, Marc Dieu, Martine Raes, Philippe Levêque, Bernard Gallez, Matthieu Depuydt, Jean-François Collet, Pedro Buc Calderon, Julien Verrax
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2012-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3407180?pdf=render

Internet

http://europepmc.org/articles/PMC3407180?pdf=render

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