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Nature Structural Biology|May 1, 1997
Interaction of Hsp70 chaperones with substratesS Rüdiger, A Buchberger, B BukauCurrent Biology : CB|January 16, 2002
Protein turnover: a CHIP programmed for proteolysisT Wiederkehr, B Bukau, A BuchbergerJournal of Molecular Biology|May 26, 1995
The role of ATP in the functional cycle of the DnaK chaperone systemJ S McCarty, A Buchberger, J Reinstein, et al.Biological Chemistry|November 15, 2000
Molecular basis for interactions of the DnaK chaperone with substratesM P Mayer, S Rüdiger, B BukauThe EMBO Journal|March 7, 2001
Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperoneS Rüdiger, J Schneider-Mergener, B BukauNature 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.The EMBO Journal|April 1, 1994
The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171A Buchberger, A Valencia, R McMacken, et al.Biological Chemistry|October 11, 2001
Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and thermally denatured proteinsE Schaffitzel, S Rüdiger, B Bukau, et al.The Journal of Biological Chemistry|December 23, 1999
Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communicationA Buchberger, C S Gässler, M Büttner, et al.Journal of Molecular Biology|August 23, 1996
Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein foldingA Buchberger, H Schröder, T Hesterkamp, et al.Pageof 15