Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism-Reference-Cited by-同舟云学术

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Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism

Published:2017-01-27 Issue:1 Volume:7 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Anglès Fréderic,Castanié-Cornet Marie-Pierre,Slama Nawel,Dinclaux Mickael,Cirinesi Anne-Marie,Portais Jean-Charles,Létisse Fabien,Genevaux Pierre

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep41341.pdf

Reference51 articles.

1. Hartl, F. U. Chaperone-assisted protein folding: the path to discovery from a personal perspective. Nat Med 17, 1206–1210, doi: 10.1038/nm.2467 (2011).

2. Bukau, B., Weissman, J. & Horwich, A. Molecular chaperones and protein quality control. Cell 125, 443–451 (2006).

3. Genevaux, P., Georgopoulos, C. & Kelley, W. L. The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions. Mol. Microbiol. 66, 840–857 (2007).

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 Lett 583, 2991–2996, doi: 10.1016/j.febslet.2009.08.020 (2009).

5. Kramer, G., Boehringer, D., Ban, N. & Bukau, B. The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Nature Structural & Molecular Biology 16, 589–597 (2009).

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