نتایج جستجو برای: hsp90α

تعداد نتایج: 193  

Journal: :Epigenomics 2015
Carole Seidel Michael Schnekenburger Mario Dicato Marc Diederich

Histone deacetylase (HDAC)6 is a member of the class IIb HDAC family. This enzyme is zinc-dependent and mainly localized in the cytoplasm. HDAC6 is a unique isoenzyme with two functional catalytic domains and specific physiological roles. Indeed, HDAC6 deacetylates various substrates including α-tubulin and HSP90α, and is involved in protein trafficking and degradation, cell shape and migration...

2012
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

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 redox-active iron. As a result of the cleavage, we observed a disruption of the chaperoning functi...

Journal: :The Journal of biological chemistry 2016
Suman Ghosh Heather E Shinogle Nadezhda A Galeva Rick T Dobrowsky Brian S J Blagg

Heat shock protein 90 (HSP90) is a molecular chaperone that is up-regulated in cancer and is required for the folding of numerous signaling proteins. Consequently, HSP90 represents an ideal target for the development of new anti-cancer agents. The human HSP90 isoform, glucose-regulated protein 94 (GRP94), resides in the endoplasmic reticulum and regulates secretory pathways, integrins, and Toll...

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