Nucleotide exchange factors Fes1 and HspBP1 mimic substrate to release misfolded proteins from Hsp70
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/s41594-017-0008-2.pdf
Reference46 articles.
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2. Kim, Y. E., Hipp, M. S., Bracher, A., Hayer-Hartl, M. & Hartl, F. U. Molecular chaperone functions in protein folding and proteostasis. Annu. Rev. Biochem. 82, 323–355 (2013).
3. Bracher, A. & Verghese, J. The nucleotide exchange factors of Hsp70 molecular chaperones. Front. Mol. Biosci. 2, 10 (2015).
4. Cyr, D. M. Swapping nucleotides, tuning Hsp70. Cell 133, 945–947 (2008).
5. Bracher, A. & Verghese, J. GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: nucleotide exchange factors for Hsp70 molecular chaperones. Subcell. Biochem. 78, 1–33 (2015).
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