2005 - German National Academy of Sciences Leopoldina - Deutsche Akademie der Naturforscher Leopoldina – Nationale Akademie der Wissenschaften Biochemistry and Biophysics
Member of the European Molecular Biology Organization (EMBO)
His primary scientific interests are in Biochemistry, Chaperone, Protein folding, Cell biology and Escherichia coli. His is doing research in CLPB, Protein aggregation, Binding site, Hsp70 and Plasma protein binding, both of which are found in Biochemistry. His Chaperone research is multidisciplinary, incorporating perspectives in Heat shock protein, Biophysics, Protein structure and Protein biosynthesis.
In general Heat shock protein study, his work on Heat shock often relates to the realm of Luciferase, thereby connecting several areas of interest. His Protein folding research integrates issues from ATP hydrolysis, ATPase, Adenosine triphosphate, 'de novo' protein folding and Cytosol. His Cell biology research is multidisciplinary, incorporating perspectives in JUNQ and IPOD, Protein subunit, Protein quality and Co-chaperone.
Bernd Bukau mainly investigates Biochemistry, Chaperone, Cell biology, Protein folding and Hsp70. As part of the same scientific family, Bernd Bukau usually focuses on Biochemistry, concentrating on Biophysics and intersecting with Helix. His biological study spans a wide range of topics, including Heat shock protein, Protein aggregation, ATP hydrolysis, Mutant and Binding site.
His Cell biology research is multidisciplinary, relying on both Translation, Ribosome, Saccharomyces cerevisiae and Cytosol. His studies in Protein folding integrate themes in fields like Plasma protein binding, Co-chaperone, Peptide sequence, GroEL and Computational biology. His study in Hsp70 is interdisciplinary in nature, drawing from both Caenorhabditis elegans and Yeast.
His primary areas of investigation include Cell biology, Chaperone, Protein aggregation, Protein folding and Hsp70. Bernd Bukau interconnects Translation, Ribosome, Saccharomyces cerevisiae and Heat shock protein in the investigation of issues within Cell biology. Chaperone connects with themes related to Ribosomal protein in his study.
His Protein aggregation research includes themes of Amyloid fibril, Protein degradation, Biophysics, Protein domain and Cytosol. His Protein folding research incorporates themes from Protein quality, HSPA1A and SOD1. The Hsp70 study combines topics in areas such as Fibril, Caenorhabditis elegans and Function.
Bernd Bukau mainly focuses on Cell biology, Chaperone, Protein aggregation, Protein folding and Hsp70. His Cell biology research is multidisciplinary, incorporating elements of Proteome, Ribosome profiling, Saccharomyces cerevisiae and Ribosomal RNA. His Chaperone research incorporates elements of ATP hydrolysis, Protein subunit, CLPB, Protein biosynthesis and Unfolded protein response.
His Protein aggregation research focuses on Biophysics and how it relates to Motor activity, Folding, ATPase and Cooperativity. His work carried out in the field of Protein folding brings together such families of science as Heat shock protein, Sequence, Translation, Proteostasis and Ribosome. His Heat shock protein research integrates issues from Chaperonin, Protein domain and Cytosol.
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The Hsp70 and Hsp60 chaperone machines.
Bernd Bukau;Arthur L Horwich.
Cell (1998)
Hsp70 chaperones: Cellular functions and molecular mechanism
Matthias P. Mayer;Bernd Bukau.
Cellular and Molecular Life Sciences (2005)
Molecular Chaperones and Protein Quality Control
Bernd Bukau;Jonathan Weissman;Arthur Horwich;Arthur Horwich.
Cell (2006)
Cellular strategies for controlling protein aggregation
Jens Tyedmers;Axel Mogk;Bernd Bukau.
Nature Reviews Molecular Cell Biology (2010)
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)
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.
H. Schröder;T. Langer;F.U. Hartl;B. Bukau.
The EMBO Journal (1993)
The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE
A Szabo;T Langer;T Langer;H Schröder;J Flanagan.
Proceedings of the National Academy of Sciences of the United States of America (1994)
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
Pierre Goloubinoff;Axel Mogk;Anat Peres Ben Zvi;Toshifumi Tomoyasu.
Proceedings of the National Academy of Sciences of the United States of America (1999)
Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones
Thomas Laufen;Matthias P. Mayer;Christian Beisel;Dagmar Klostermeier.
Proceedings of the National Academy of Sciences of the United States of America (1999)
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