Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-018-24140-5.pdf
Reference65 articles.
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3. Zolkiewski, M. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. The Journal of biological chemistry 274, 28083–28086 (1999).
4. Acebron, S. P., Martin, I., del Castillo, U., Moro, F. & Muga, A. DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface. FEBS letters 583, 2991–2996, https://doi.org/10.1016/j.febslet.2009.08.020 (2009).
5. Winkler, J., Tyedmers, J., Bukau, B. & Mogk, A. Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. The Journal of cell biology 198, 387–404, https://doi.org/10.1083/jcb.201201074 (2012).
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