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Clinical and Experimental Immunology|November 1, 1994
Heat shock proteins as carrier molecules: in vivo helper effect mediated by Escherichia coli GroEL and DnaK proteins requires cross-linking with antigenC Barrios, C Georgopoulos, P H Lambert, et al.
The Journal of Biological Chemistry|August 5, 1991
The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target proteinK Liberek, D Skowyra, M Zylicz, et al.
The Journal of Biological Chemistry|June 25, 1985
Purification and properties of the dnaJ replication protein of Escherichia coliM Zylicz, T Yamamoto, N McKittrick, et al.
The EMBO Journal|December 16, 1996
Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coliD Missiakas, F Schwager, J M Betton, et al.
Molecular Microbiology|April 1, 1997
Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteinsD Missiakas, M P Mayer, M Lemaire, et al.
The Journal of Biological Chemistry|December 7, 2000
DjlA is a third DnaK co-chaperone of Escherichia coli, and DjlA-mediated induction of colanic acid capsule requires DjlA-DnaK interactionP Genevaux, A Wawrzynow, M Zylicz, et al.
The Journal of Biological Chemistry|September 15, 1986
Purification and properties of the groES morphogenetic protein of Escherichia coliG N Chandrasekhar, K Tilly, C Woolford, et al.
The Journal of Biological Chemistry|June 20, 1998
Function of Escherichia coli MsbA, an essential ABC family transporter, in lipid A and phospholipid biosynthesisZ Zhou, K A White, A Polissi, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 15, 1996
Interplay of structure and disorder in cochaperonin mobile loopsS J Landry, A Taher, C Georgopoulos, et al.
The Journal of Biological Chemistry|August 18, 1995
ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substratesA Wawrzynów, B Banecki, D Wall, et al.
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