The scientist’s investigation covers issues in GTPase, Biochemistry, GTPase-activating protein, Stereochemistry and Protein structure. Klaus Scheffzek has included themes like GTP' and Catalysis, Active site in his GTPase study. In his study, Guanosine is strongly linked to G protein, which falls under the umbrella field of Active site.
His research investigates the connection with Biochemistry and areas like Cell biology which intersect with concerns in Actinin. Within one scientific family, he focuses on topics pertaining to Neurofibromin 1 under GTPase-activating protein, and may sometimes address concerns connected to Missense mutation, Cancer research, Neurofibroma, Mutation and Phenotype. His work carried out in the field of Protein structure brings together such families of science as Guanosine triphosphate and Binding site.
Klaus Scheffzek focuses on Biochemistry, Cell biology, GTPase, GTPase-activating protein and Protein structure. In his research, DNA damage and Macro domain is intimately related to Histone, which falls under the overarching field of Cell biology. The study incorporates disciplines such as Mutant, Catalysis, Guanosine, GTP' and HRAS in addition to GTPase.
His studies in GTP' integrate themes in fields like Crystallography, GTP-binding protein regulators and Stereochemistry. His research in GTPase-activating protein intersects with topics in Neurofibromin 1, Cell growth and Function. His research integrates issues of Cdc42 GTP-Binding Protein, Biophysics, Peptide sequence, Autophosphorylation and Binding site in his study of Protein structure.
His primary scientific interests are in Cell biology, Biochemistry, Neurofibromin 1, Enzyme and Signal transduction. His work on Intracellular and GTPase as part of general Cell biology study is frequently linked to Expression and Structure function, bridging the gap between disciplines. His GTPase research is multidisciplinary, relying on both Subcellular localization, Mutant, Cell growth and Function.
His Neurofibromin 1 research includes elements of EVH1 domain, GTPase-activating protein and Phosphorylation. His study on Metalloproteinase, Protease inhibitor and Protease is often connected to Contamination as part of broader study in Enzyme. His Signal transduction study which covers Protein domain that intersects with Lysosome, mTORC1, PI3K/AKT/mTOR pathway and Ragulator complex.
His scientific interests lie mostly in Cell biology, Signal transduction, Mechanistic target of rapamycin, Protein domain and Gene isoform. Cell biology is closely attributed to Neurofibromin 1 in his work. His Neurofibromin 1 research is multidisciplinary, incorporating elements of HEK 293 cells, EVH1 domain and GTPase-activating protein.
His Gene isoform study integrates concerns from other disciplines, such as Chromatin, Heterochromatin, Histone and Epigenetics. His Endosome research incorporates elements of Activator, Epidermal growth factor and Organelle. His Ragulator complex study combines topics in areas such as GTPase and Lysosome.
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The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras Mutants
Klaus Scheffzek;Mohammad Reza Ahmadian;Wolfgang Kabsch;Lisa Wiesmüller.
Structural basis for the autoinhibition of c-Abl tyrosine kinase
Bhushan Nagar;Oliver Hantschel;Matthew A. Young;Klaus Scheffzek.
GTPase-activating proteins: helping hands to complement an active site
Klaus Scheffzek;Mohammad Reza Ahmadian;Alfred Wittinghofer.
Trends in Biochemical Sciences (1998)
Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras
Mohammad Reza Ahmadian;Patricia Stege;Klaus Scheffzek;Alfred Wittinghofer.
Nature Structural & Molecular Biology (1997)
A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation.
Gyula Timinszky;Susanne Till;Paul O Hassa;Michael Hothorn.
Nature Structural & Molecular Biology (2009)
Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteins.
Thomas Schweins;Matthias Geyer;Klaus Scheffzek;Arieh Warshel.
Nature Structural & Molecular Biology (1995)
Splicing regulates NAD metabolite binding to histone macroH2A.
Georg Kustatscher;Michael Hothorn;Céline Pugieux;Klaus Scheffzek.
Nature Structural & Molecular Biology (2005)
The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI.
Klaus Scheffzek;Ilona Stephan;Ole N. Jensen;Daria Illenberger.
Nature Structural & Molecular Biology (2000)
Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form.
Klaus Scheffzek;Christian Klebe;Karin Fritz-Wolf;Wolfgang Kabsch.
Crystal structure of the alpha-actinin rod reveals an extensive torsional twist
Jari Ylänne;Klaus Scheffzek;Paul Young;Matti Saraste.
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