Hartwig Schröder

Nucleotide-induced Conformational Changes in the ATPase and Substrate Binding Domains of the DnaK Chaperone Provide Evidence for Interdomain Communication (*)

J. Reinstein, B. Bukau, A. Buchberger, 1995, The Journal of Biological Chemistry.

Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.

A Valencia, A. Valencia, M. Mayer, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Multistep mechanism of substrate binding determines chaperone activity of Hsp70

Bernd Bukau, Matthias P. Mayer, M. Mayer, 2000, Nature Structural Biology.

The DnaK Chaperone System of Escherichia coli: Quaternary Structures and Interactions of the DnaK and GrpE Components (*)

B. Bukau, D. Schmidt, H. Schönfeld, 1995, The Journal of Biological Chemistry.

A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE

A. Valencia, B. Bukau, A. Buchberger, 1994, Nature Structural Biology.

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.

F. Hartl, T. Langer, B. Bukau, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

B. Bukau, A. Buchberger, T. Hesterkamp, 1996, Journal of molecular biology.