His main research concerns Biochemistry, Chaperone, Cell biology, CLPB and Protein aggregation. His study in Binding site and Signal transducing adaptor protein is carried out as part of his Biochemistry studies. The study incorporates disciplines such as Escherichia coli, Protein structure, Threading, AAA proteins and Vibrio cholerae in addition to Chaperone.
His Cell biology research includes themes of Nucleotide exchange factor, Hsp70, Cell survival and Gene cluster. His CLPB research is multidisciplinary, relying on both In vitro, Small Heat-Shock Proteins, Chromosomal translocation, Biophysics and GroEL. Within one scientific family, Axel Mogk focuses on topics pertaining to Protein folding under Protein aggregation, and may sometimes address concerns connected to Heat shock protein and JUNQ and IPOD.
His scientific interests lie mostly in Biochemistry, Cell biology, Chaperone, Protein aggregation and CLPB. His work in the fields of Biochemistry, such as Signal transducing adaptor protein, Escherichia coli, Protease and N-end rule, overlaps with other areas such as Endopeptidase Clp. He works mostly in the field of Cell biology, limiting it down to topics relating to Protein structure and, in certain cases, Gene cluster, as a part of the same area of interest.
His Chaperone research incorporates themes from Protein degradation, Mutant, Cytosol, Threading and AAA proteins. The concepts of his Protein aggregation study are interwoven with issues in Heat shock protein, Fibril, Proteasome, JUNQ and IPOD and Intracellular. The various areas that he examines in his CLPB study include ATPase, Plasma protein binding, Biophysics, Protein family and GroEL.
Axel Mogk focuses on Cell biology, Chaperone, Protein aggregation, Proteostasis and Protein folding. His Cell biology research is multidisciplinary, incorporating elements of Hsp70 and Threading. His Chaperone study incorporates themes from Coiled coil, Mutant, Protein degradation and Cytosol.
Axel Mogk has researched Protein aggregation in several fields, including Heat shock protein and Huntingtin. His work carried out in the field of Protein folding brings together such families of science as Small Heat-Shock Proteins, Biophysics, Protein refolding and Solubilization. His Proteases study introduces a deeper knowledge of Biochemistry.
Protein folding, Cell biology, Chaperone, Hsp70 and Protein aggregation are his primary areas of study. His study brings together the fields of Saccharomyces cerevisiae and Cell biology. His study in Chaperone is interdisciplinary in nature, drawing from both Heat shock protein, Heat shock, Cytosol, Signal transduction and Intracellular.
His Hsp70 study combines topics from a wide range of disciplines, such as Solubilization, Biophysics, Folding, Substrate and Protein refolding. His research on Protein aggregation concerns the broader Biochemistry. His research in the fields of Huntingtin, Proteome, In vitro and Amyloid beta overlaps with other disciplines such as In vivo.
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Cellular strategies for controlling protein aggregation
Jens Tyedmers;Axel Mogk;Bernd Bukau.
Nature Reviews Molecular Cell Biology (2010)
Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation through the Central Pore of ClpB
Jimena Weibezahn;Peter Tessarz;Christian Schlieker;Regina Zahn.
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.
Molecular Microbiology (2003)
Remodelling of VipA/VipB tubules by ClpV-mediated threading is crucial for type VI protein secretion.
Gabriele Bönemann;Aleksandra Pietrosiuk;Alexander Diemand;Hanswalter Zentgraf.
The EMBO Journal (2009)
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;Hans-Joachim Schönfeld.
Journal of Biological Chemistry (2003)
The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies.
Axel Mogk;Ronny Schmidt;Bernd Bukau.
Trends in Cell Biology (2007)
Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli.
Ario de Marco;Elke Deuerling;Axel Mogk;Toshifumi Tomoyasu.
BMC Biotechnology (2007)
Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
Sebastian Specht;Stephanie B.M. Miller;Axel Mogk;Bernd Bukau.
Journal of Cell Biology (2011)
Quantitative and spatio‐temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing
Juliane Winkler;Anja Seybert;Lars König;Sabine Pruggnaller.
The EMBO Journal (2010)
Substrate recognition by the AAA+ chaperone ClpB.
Christian Schlieker;Christian Schlieker;Jimena Weibezahn;Holger Patzelt;Peter Tessarz.
Nature Structural & Molecular Biology (2004)
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