S
Stefan G.D. Rüdiger
Researcher at Utrecht University
Publications - 74
Citations - 7663
Stefan G.D. Rüdiger is an academic researcher from Utrecht University. The author has contributed to research in topics: Chaperone (protein) & Protein folding. The author has an hindex of 41, co-authored 72 publications receiving 6812 citations. Previous affiliations of Stefan G.D. Rüdiger include Heidelberg University & Medical Research Council.
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Journal ArticleDOI
Substrate specificity of the DnaK chaperone determined by screening cellulose‐bound peptide libraries
TL;DR: An algorithm was established that predicts DnaK binding sites in protein sequences with high accuracy and is based on data identified by screening 4360 cellulose‐bound peptides scanning the sequences of 37 biologically relevant proteins.
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Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB
Axel Mogk,Toshifumi Tomoyasu,Pierre Goloubinoff,Stefan G.D. Rüdiger,Daniel Röder,Hanno Langen,Bernd Bukau +6 more
TL;DR: The data indicate that large‐sized proteins are most vulnerable to thermal unfolding and aggregation, and that the DnaK system has central, dual protective roles for these proteins by preventing their aggregation and, cooperatively with ClpB, mediating their disaggregation.
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Interaction of Hsp70 chaperones with substrates
TL;DR: Determination of the structure of the substrate binding domain of the Escherichia coli Hsp70 chaperone, DnaK, and the biochemical characterisation of the motif it recognizes within substrates provide insights into the principles governing H Sp70 interaction with polypeptide chains.
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Multistep mechanism of substrate binding determines chaperone activity of Hsp70
TL;DR: In this article, the authors analyzed mutants of DnaK, an Hsp70 homolog, altered in key residues of its substrate binding domain and found that the conformational changes in the alpha-helical lid and the beta-domain caused the opening of the substrate binding cavity.
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A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.
J. Gamer,Gerd Multhaup,Toshifumi Tomoyasu,John S. McCarty,Stefan G.D. Rüdiger,H. J. Schönfeld,C. Schirra,Hermann Bujard,Bernd Bukau +8 more
TL;DR: Data indicate that reversible inhibition of sigma32 activity through transient association of DnaK and DnaJ is a central regulatory element of the heat shock response and it is proposed that the principles of this cycle also operate in other chaperone activities of the DNAK system.