D-Index & Metrics Best Publications

D-Index & Metrics D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines.

Discipline name D-index D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines. Citations Publications World Ranking National Ranking
Biology and Biochemistry D-index 42 Citations 8,728 68 World Ranking 17070 National Ranking 403

Overview

What is he best known for?

The fields of study he is best known for:

  • Amino acid
  • Biochemistry
  • Genetics

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 most cited work include:

  • Substrate specificity of the DnaK chaperone determined by screening cellulose‐bound peptide libraries (671 citations)
  • Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB (519 citations)
  • Multistep mechanism of substrate binding determines chaperone activity of Hsp70 (319 citations)

What are the main themes of his work throughout his whole career to date?

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.

He most often published in these fields:

  • Biochemistry (51.47%)
  • Chaperone (41.18%)
  • Protein folding (38.24%)

What were the highlights of his more recent work (between 2017-2021)?

  • Chaperone (41.18%)
  • Tau protein (16.18%)
  • Hsp90 (27.94%)

In recent papers he was focusing on the following fields of study:

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.

Between 2017 and 2021, his most popular works were:

  • Hsp90 Breaks the Deadlock of the Hsp70 Chaperone System. (62 citations)
  • The Hsp70-Hsp90 Chaperone Cascade in Protein Folding. (56 citations)
  • Dancing with the Diva: Hsp90–Client Interactions (44 citations)

In his most recent research, the most cited papers focused on:

  • Amino acid
  • Biochemistry
  • Genetics

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.

This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.

Best Publications

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)

946 Citations

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)

702 Citations

Interaction of Hsp70 chaperones with substrates

Stefan Rüdiger;Alexander Buchberger;Bernd Bukau;Bernd Bukau.
Nature Structural & Molecular Biology (1997)

476 Citations

Multistep mechanism of substrate binding determines chaperone activity of Hsp70

Matthias P. Mayer;Hartwig Schröder;Stefan Rüdiger;Klaus Paal.
Nature Structural & Molecular Biology (2000)

439 Citations

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)

349 Citations

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)

340 Citations

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)

335 Citations

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.
Cell (2014)

272 Citations

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)

270 Citations

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)

265 Citations

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