Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli.

Por Hesterkamp, T, Bukau, B
Publicado em 1998

Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism.

Por Bukau, B, Walker, G C
Publicado em 1989

Delta dnaK52 mutants of Escherichia coli have defects in chromosome segregation and plasmid maintenance at normal growth temperatures.

Por Bukau, B, Walker, G C
Publicado em 1989

Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone.

Por Bukau, B, Walker, G C
Publicado em 1990

Hsp70 chaperones: Cellular functions and molecular mechanism

Por Mayer, M. P., Bukau, B.
Publicado em 2005

Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

Por Hesterkamp, T, Hauser, S, Lütcke, H, Bukau, B
Publicado em 1996

Osmoregulation of the maltose regulon in Escherichia coli.

Por Bukau, B, Ehrmann, M, Boos, W
Publicado em 1986

Reconstitution of maltose transport in Escherichia coli: conditions affecting import of maltose-binding protein into the periplasm of calcium-treated cells.

Por Brass, J M, Ehmann, U, Bukau, B
Publicado em 1983

Ca2+-induced permeabilization of the Escherichia coli outer membrane: comparison of transformation and reconstitution of binding-protein-dependent transport.

Por Bukau, B, Brass, J M, Boos, W
Publicado em 1985

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

Por Schröder, H, Langer, T, Hartl, F U, Bukau, B
Publicado em 1993

Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries.

Por Rüdiger, S, Germeroth, L, Schneider-Mergener, J, Bukau, B
Publicado em 1997

Contrasting mechanisms of envZ control of mal and pho regulon genes in Escherichia coli.

Por Case, C C, Bukau, B, Granett, S, Villarejo, M R, Boos, W
Publicado em 1986

The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171.

Por Buchberger, A, Valencia, A, McMacken, R, Sander, C, Bukau, B
Publicado em 1994

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

Por Szabo, A, Langer, T, Schröder, H, Flanagan, J, Bukau, B, Hartl, F U
Publicado em 1994

Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

Por Mogk, A, Tomoyasu, T, Goloubinoff, P, Rüdiger, S, Röder, D, Langen, H, Bukau, B
Publicado em 1999

A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.

Por Gamer, J, Multhaup, G, Tomoyasu, T, McCarty, J S, Rüdiger, S, Schönfeld, H J, Schirra, C, Bujard, H, Bukau, B
Publicado em 1996

Functional Dissection of Escherichia coli Trigger Factor: Unraveling the Function of Individual Domains

Por Kramer, G., Rutkowska, A., Wegrzyn, R. D., Patzelt, H., Kurz, T. A., Merz, F., Rauch, T., Vorderwülbecke, S., Deuerling, E., Bukau, B.
Publicado em 2004

Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32.

Por Tomoyasu, T, Gamer, J, Bukau, B, Kanemori, M, Mori, H, Rutman, A J, Oppenheim, A B, Yura, T, Yamanaka, K, Niki, H
Publicado em 1995