Bernd Bukau

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Hsp70 chaperones: Cellular functions and molecular mechanism

Matthias P. Mayer, Bernd Bukau
Cellular and Molecular Life Sciences
2004

Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient… (More)

The Hsp70 and Hsp60 Chaperone Machines

In Hsp70-assisted folding reactions, substrates unAn essential cellular machinery that has been identified dergo repeated cycles of binding/release (Szabo et al., and studied only relatively recently… (More)

Cellular strategies for controlling protein aggregation

Jens Tyedmers, Axel Mogk, Bernd Bukau
Nature Reviews Molecular Cell Biology
2010

The aggregation of misfolded proteins is associated with the perturbation of cellular function, ageing and various human disorders. Mounting evidence suggests that protein aggregation is often part… (More)

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

Stefan Rüdiger, L Germeroth, Jens Schneider-Mergener, Bernd Bukau
The EMBO journal
1997

Hsp70 chaperones assist protein folding by ATP-dependent association with linear peptide segments of a large variety of folding intermediates. The molecular basis for this ability to differentiate… (More)

Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins

Lars Ferbitz, Timm Maier, Holger Patzelt, Bernd Bukau, Elke Deuerling, Nenad Ban
Nature
2004

During protein biosynthesis, nascent polypeptide chains that emerge from the ribosomal exit tunnel encounter ribosome-associated chaperones, which assist their folding to the native state. Here we… (More)

Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation.

Axel Mogk, Elke Deuerling, Sonja Vorderwülbecke, Elizabeth Vierling, Bernd Bukau
Molecular microbiology
2003

Small heat shock proteins (sHsps) can efficiently prevent the aggregation of unfolded proteins in vitro. However, how this in vitro activity translates to function in vivo is poorly understood. We… (More)

Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK.

Axel Mogk, Christian Schlieker, Kenneth L. Friedrich, H. Schönfeld, Elizabeth Vierling, Bernd Bukau
The Journal of biological chemistry
2003

Small heat shock proteins (sHsps) are ubiquitous molecular chaperones that bind denatured proteins in vitro, thereby facilitating their subsequent refolding by ATP-dependent chaperones. The… (More)

Molecular Chaperones and Protein Quality Control

Bernd Bukau, Jonathan S. Weissman, Arthur L Horwich
Cell
2006

In living cells, both newly made and preexisting polypeptide chains are at constant risk for misfolding and aggregation. In accordance with the wide diversity of misfolded forms, elaborate… (More)

The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins

Guenter Kramer, Daniel Boehringer, Nenad Ban, Bernd Bukau
Nature Structural &Molecular Biology
2009

The early events in the life of newly synthesized proteins in the cellular environment are remarkably complex. Concurrently with their synthesis by the ribosome, nascent polypeptides are subjected to… (More)

Trigger factor and DnaK cooperate in folding of newly synthesized proteins

Elke Deuerling, Agnes Schulze-Specking, Toshifumi Tomoyasu, Axel Mogk, Bernd Bukau
Nature
1999

The role of molecular chaperones in assisting the folding of newly synthesized proteins in the cytosol is poorly understood. In Escherichia coli, GroEL assists folding of only a minority of proteins… (More)

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