Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
https://www.nature.com/articles/s41586-021-04252-1.pdf
Reference75 articles.
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2. Genest, O., Wickner, S. & Doyle, S. M. Hsp90 and Hsp70 chaperones: collaborators in protein remodeling. J. Biol. Chem. 294, 2109–2120 (2019).
3. Lorenz, O. R. et al. Modulation of the Hsp90 chaperone cycle by a stringent client protein. Mol. Cell 53, 941–953 (2014).
4. Picard, D. et al. Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature 348, 166–168 (1990).
5. Nathan, D. F., Vos, M. H. & Lindquist, S. In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc Natl Acad. Sci. USA 94, 12949–12956 (1997).
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