Stefan G.D. Rüdiger mainly investigates Biochemistry, Chaperone, Protein folding, Binding site and Biophysics. Stefan G.D. Rüdiger combines subjects such as Hsp70 and Heat shock with his study of Biochemistry. His work deals with themes such as Oligopeptide, Chaperone activity and Mutational analysis, which intersect with Hsp70.
His research in Biophysics focuses on subjects like Adenosine triphosphate, which are connected to RNA polymerase, Allosteric regulation and Enzyme activator. His Plasma protein binding study combines topics in areas such as Binding domain and Protein aggregation. Stefan G.D. Rüdiger has included themes like Amino acid and Substrate binding domain in his Peptide study.
His primary areas of investigation include Biochemistry, Chaperone, Protein folding, Biophysics and Hsp90. His study in Biochemistry focuses on Binding site, Protein structure, Peptide, Plasma protein binding and In vitro. His biological study spans a wide range of topics, including Amino acid, Molecular biology and Oligopeptide.
His Chaperone research includes themes of Heat shock factor, RNA polymerase and Heat shock. His study in Protein folding is interdisciplinary in nature, drawing from both Hsp70, Co-chaperone and Protein aggregation. His work on Fibril as part of general Biophysics study is frequently connected to Tau protein, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them.
Stefan G.D. Rüdiger focuses on Chaperone, Tau protein, Hsp90, Cell biology and Fibril. His work carried out in the field of Chaperone brings together such families of science as Proteostasis, Hsp70 and Protein folding. His studies deal with areas such as HEK 293 cells and Phosphorylation as well as Hsp90.
His Fibril study introduces a deeper knowledge of Biophysics. His Biophysics research is multidisciplinary, incorporating elements of Plasma protein binding, Arginine and Protein Homeostasis. His In vitro study is associated with Biochemistry.
Hsp90, Chaperone, Proteostasis, Protein folding and Cell biology are his primary areas of study. His Hsp90 research incorporates themes from Fibril, Biophysics, Kinase and Mitochondrion. Stefan G.D. Rüdiger performs multidisciplinary study in the fields of Chaperone and Neurodegeneration via his papers.
His Proteostasis research includes elements of Hsp70 and Computational biology. He undertakes multidisciplinary investigations into Hsp70 and General function in his work. His work on Microtubule is typically connected to Linker as part of general Cell biology study, connecting several disciplines of science.
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Substrate specificity of the DnaK chaperone determined by screening cellulose‐bound peptide libraries
Stefan Rüdiger;Lothar Germeroth;Jens Schneider‐Mergener;Bernd Bukau.
The EMBO Journal (1997)
Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB
Axel Mogk;Toshifumi Tomoyasu;Pierre Goloubinoff;Stefan Rüdiger.
The EMBO Journal (1999)
Interaction of Hsp70 chaperones with substrates
Stefan Rüdiger;Alexander Buchberger;Bernd Bukau;Bernd Bukau.
Nature Structural & Molecular Biology (1997)
Multistep mechanism of substrate binding determines chaperone activity of Hsp70
Matthias P. Mayer;Hartwig Schröder;Stefan Rüdiger;Klaus Paal.
Nature Structural & Molecular Biology (2000)
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;G. Multhaup;T. Tomoyasu;J. S. McCarty.
The EMBO Journal (1996)
Its substrate specificity characterizes the DnaJ co‐chaperone as a scanning factor for the DnaK chaperone
Stefan Rüdiger;Jens Schneider‐Mergener;Bernd Bukau.
The EMBO Journal (2001)
A peptide that binds and stabilizes p53 core domain: Chaperone strategy for rescue of oncogenic mutants
Assaf Friedler;Lars O. Hansson;Dmitry B. Veprintsev;Stefan M. V. Freund.
Proceedings of the National Academy of Sciences of the United States of America (2002)
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
G. Elif Karagöz;G. Elif Karagöz;Afonso M.S. Duarte;Afonso M.S. Duarte;Elias Akoury;Hans Ippel;Hans Ippel.
Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein.
Jan Brix;Stefan Rüdiger;Bernd Bukau;Jens Schneider-Mergener.
Journal of Biological Chemistry (1999)
Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange.
Dirk Brehmer;Stefan Rüdiger;Claudia S. Gässler;Dagmar Klostermeier;Dagmar Klostermeier.
Nature Structural & Molecular Biology (2001)
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