His scientific interests lie mostly in Biochemistry, GTPase, Effector, Nucleotide and GTP'. His research in the fields of GTP-binding protein regulators, Guanine nucleotide exchange factor, Kinase and Peptide sequence overlaps with other disciplines such as Proto-Oncogene Proteins c-raf. His work carried out in the field of GTPase brings together such families of science as Guanylate-binding protein, Signal transduction and Binding site.
His Binding site research incorporates themes from Protein structure, Plasma protein binding, PI3K/AKT/mTOR pathway and Mutant. His Effector study combines topics in areas such as Binding domain, Rap GTP-binding protein and Ral Guanine Nucleotide Exchange Factor. The concepts of his Nucleotide study are interwoven with issues in Adenosine triphosphate, Chaperone, Transmembrane domain and Enzyme.
His primary areas of study are Biochemistry, GTPase, Biophysics, Cell biology and GTP'. His is doing research in GTP-binding protein regulators, Binding domain, Mutant, Guanine nucleotide exchange factor and Binding site, both of which are found in Biochemistry. The study incorporates disciplines such as Guanylate-binding protein, Dimer, Nucleotide and Vesicle in addition to GTPase.
In his study, Crystallography and Isothermal titration calorimetry is inextricably linked to Protein structure, which falls within the broad field of Biophysics. His biological study spans a wide range of topics, including Cleavage and Stereochemistry. His research integrates issues of Plasma protein binding, Signal transduction, Rap GTP-binding protein and Ral Guanine Nucleotide Exchange Factor in his study of Effector.
Christian Herrmann spends much of his time researching Biophysics, GTPase, Förster resonance energy transfer, Biochemistry and Protein–protein interaction. His studies in Biophysics integrate themes in fields like Osmolyte, Protein domain, Oligomer, Dimer and Solvent effects. While working on this project, Christian Herrmann studies both GTPase and Proto-Oncogene Proteins p21.
With his scientific publications, his incorporates both Biochemistry and Streptomyces hygroscopicus. His Protein–protein interaction study integrates concerns from other disciplines, such as Melting point, Stereochemistry, Protein Data Bank and Homologous series. In Guanylate-binding protein, Christian Herrmann works on issues like Cell adhesion, which are connected to Cell biology.
His primary areas of investigation include GTPase, Cell biology, Biochemistry, Stereochemistry and Protein–protein interaction. His GTPase study incorporates themes from Guanylate-binding protein and Vesicle. His studies deal with areas such as Colorectal cancer, Actin cytoskeleton and Protein polymerization as well as Cell biology.
His work in the fields of Small GTPase and Ras superfamily overlaps with other areas such as Bisphenol S, Proto-Oncogene Proteins p21 and Oncogene. Christian Herrmann has included themes like Size-exclusion chromatography, Monomer, Heat shock protein and Förster resonance energy transfer in his Stereochemistry study. His Protein–protein interaction research is multidisciplinary, relying on both Ion, Protein folding, Thermodynamics and Homologous series.
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The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue.
Nicolas Nassar;Gudrun Horn;Christian A. Herrmann;Anna Scherer.
Quantitative Analysis of the Complex between p21ras and the Ras-binding Domain of the Human Raf-1 Protein Kinase (∗)
Christian Herrmann;George A. Martin;Alfred Wittinghofer.
Journal of Biological Chemistry (1995)
Differential Interaction of the Ras Family GTP-binding Proteins H-Ras, Rap1A, and R-Ras with the Putative Effector Molecules Raf Kinase and Ral-Guanine Nucleotide Exchange Factor*
Christian Herrmann;Gudrun Horn;Marcel Spaargaren;Alfred Wittinghofer.
Journal of Biological Chemistry (1996)
Dynamic properties of the Ras switch I region and its importance for binding to effectors.
Michael Spoerner;Christian Herrmann;Ingrid R. Vetter;Hans Robert Kalbitzer.
Proceedings of the National Academy of Sciences of the United States of America (2001)
Protein denaturation by ionic liquids and the Hofmeister series: a case study of aqueous solutions of ribonuclease A.
Diana Constantinescu;Hermann Weingärtner;Christian Herrmann.
Angewandte Chemie (2007)
Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins.
Balaji Prakash;Gerrit J. K. Praefcke;Louis Renault;Alfred Wittinghofer.
Ligand Discrimination by TPR Domains RELEVANCE AND SELECTIVITY OF EEVD-RECOGNITION IN Hsp70·Hop·Hsp90 COMPLEXES
Achim Brinker;Clemens Scheufler;Florian von der Mülbe;Burkhard Fleckenstein.
Journal of Biological Chemistry (2002)
Conformational transitions in p21ras and in its complexes with the effector protein Raf-RBD and the GTPase activating protein GAP.
Matthias Geyer;Thomas Schweins;Christian Herrmann;Thomas Prisner.
Protein Stabilization by Macromolecular Crowding through Enthalpy Rather Than Entropy
Michael Senske;Lisa Törk;Benjamin Born;Martina Havenith.
Journal of the American Chemical Society (2014)
Ras/Rap effector specificity determined by charge reversal
Nicolas Nassar;Gudrun Horn;Christian Herrmann;Christoph Block.
Nature Structural & Molecular Biology (1996)
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