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The Journal of Biological Chemistry|February 3, 1995
The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE componentsH J Schönfeld, D Schmidt, H Schröder, et al.
Reviews of Physiology, Biochemistry and Pharmacology|July 10, 2004
Recruitment of Hsp70 chaperones: a crucial part of viral survival strategiesM P Mayer
The Journal of Biological Chemistry|May 10, 2000
Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machineryS Diamant, A P Ben-Zvi, B Bukau, et al.
Nature Structural Biology|February 1, 1994
A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpEA Buchberger, H Schröder, M Büttner, et al.
Journal of Molecular Biology|November 15, 1996
The second step of ATP binding to DnaK induces peptide releaseH Theyssen, H P Schuster, L Packschies, et al.
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