Klaus Scheffzek

9.8k total citations · 2 hit papers
78 papers, 7.1k citations indexed

About

Klaus Scheffzek is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Klaus Scheffzek has authored 78 papers receiving a total of 7.1k indexed citations (citations by other indexed papers that have themselves been cited), including 58 papers in Molecular Biology, 23 papers in Materials Chemistry and 20 papers in Cell Biology. Recurrent topics in Klaus Scheffzek's work include Enzyme Structure and Function (22 papers), Protein Kinase Regulation and GTPase Signaling (16 papers) and Cellular transport and secretion (10 papers). Klaus Scheffzek is often cited by papers focused on Enzyme Structure and Function (22 papers), Protein Kinase Regulation and GTPase Signaling (16 papers) and Cellular transport and secretion (10 papers). Klaus Scheffzek collaborates with scholars based in Germany, Austria and United States. Klaus Scheffzek's co-authors include Alfred Wittinghofer, Mohammad Reza Ahmadian, Wolfgang Kabsch, Michael Hothorn, Alfred Lautwein, Lisa Wiesmüller, Frank Schmitz, Stefan Welti, Andreas G. Ladurner and Georg Kustatscher and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Klaus Scheffzek

77 papers receiving 7.0k citations

Hit Papers

The Ras-RasGAP Complex: Structural Basis for GTPase Activ... 1997 2026 2006 2016 1997 2003 400 800 1.2k

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Klaus Scheffzek Germany 43 5.2k 1.5k 991 797 582 78 7.1k
Claude Cochet France 50 5.8k 1.1× 1.0k 0.7× 1.9k 1.9× 438 0.5× 404 0.7× 191 8.1k
Mathew E. Sowa United States 40 9.7k 1.9× 2.4k 1.6× 1.7k 1.8× 433 0.5× 405 0.7× 50 12.0k
Sean A. Beausoleil United States 25 7.3k 1.4× 1.5k 1.0× 1.0k 1.0× 251 0.3× 247 0.4× 30 9.0k
Blagoy Blagoev Denmark 42 10.6k 2.0× 1.8k 1.2× 1.6k 1.6× 356 0.4× 340 0.6× 108 14.1k
Tony Hunter United States 33 6.5k 1.2× 1.6k 1.1× 2.0k 2.1× 261 0.3× 639 1.1× 52 8.6k
Florian Gnad Germany 37 11.3k 2.2× 1.7k 1.1× 1.9k 2.0× 530 0.7× 504 0.9× 54 13.6k
Anne Marie Quinn United States 17 5.0k 1.0× 1.1k 0.7× 791 0.8× 329 0.4× 825 1.4× 32 6.7k
Mark Skehel United Kingdom 54 8.0k 1.5× 1.5k 1.0× 1.1k 1.2× 279 0.4× 561 1.0× 151 9.9k
Olga Perišić United Kingdom 43 6.5k 1.2× 2.5k 1.7× 645 0.7× 297 0.4× 404 0.7× 66 8.3k
Scott B. Ficarro United States 56 7.8k 1.5× 888 0.6× 1.7k 1.7× 307 0.4× 182 0.3× 117 10.3k

Countries citing papers authored by Klaus Scheffzek

Since Specialization
Citations

This map shows the geographic impact of Klaus Scheffzek's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Klaus Scheffzek with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Klaus Scheffzek more than expected).

Fields of papers citing papers by Klaus Scheffzek

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Klaus Scheffzek. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Klaus Scheffzek. The network helps show where Klaus Scheffzek may publish in the future.

Co-authorship network of co-authors of Klaus Scheffzek

This figure shows the co-authorship network connecting the top 25 collaborators of Klaus Scheffzek. A scholar is included among the top collaborators of Klaus Scheffzek based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Klaus Scheffzek. Klaus Scheffzek is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Chaker-Margot, Malik, Sebastiaan Werten, Theresia Dunzendorfer-Matt, et al.. (2022). Structural basis of activation of the tumor suppressor protein neurofibromin. Molecular Cell. 82(7). 1288–1296.e5. 17 indexed citations
2.
Dharmaiah, Srisathiyanarayanan, Anatoly Urisman, Matthew Drew, et al.. (2020). Structural Insights into the SPRED1-Neurofibromin-KRAS Complex and Disruption of SPRED1-Neurofibromin Interaction by Oncogenic EGFR. Cell Reports. 32(3). 107909–107909. 43 indexed citations
3.
Kozłowski, Marek, David Corujo, Michael Hothorn, et al.. (2018). MacroH2A histone variants limit chromatin plasticity through two distinct mechanisms. EMBO Reports. 19(10). 62 indexed citations
4.
Scheffzek, Klaus, et al.. (2017). NMR resonance assignments of the EVH1 domain of neurofibromin’s recruitment factor Spred1. Biomolecular NMR Assignments. 11(2). 305–308. 2 indexed citations
5.
Naschberger, Andreas, Barbara G. Fürnrohr, Theresia Dunzendorfer-Matt, et al.. (2014). Cleaning protocols for crystallization robots: preventing protease contamination. Acta Crystallographica Section F Structural Biology Communications. 71(1). 100–102. 1 indexed citations
6.
Hothorn, Michael, Wim Van den Ende, Willem Lammens, Vladimir Rybin, & Klaus Scheffzek. (2010). Structural insights into the pH-controlled targeting of plant cell-wall invertase by a specific inhibitor protein. Proceedings of the National Academy of Sciences. 107(40). 17427–17432. 83 indexed citations
7.
Welti, Stefan, Sonja Kühn, I. D’Angelo, et al.. (2010). Structural and biochemical consequences of NF1 associated nontruncating mutations in the Sec14-PH module of neurofibromin. Human Mutation. 32(2). 191–197. 23 indexed citations
8.
Herrmann, Christian, et al.. (2009). Activity of the Enterococcus faecalis EIIAgnt PTS component and its strong interaction with EIIBgnt. Biochemical and Biophysical Research Communications. 388(4). 630–636. 6 indexed citations
9.
Reinelt, Stefan, et al.. (2009). Structure of the Enterococcus faecalis EIIAgnt PTS component. Biochemical and Biophysical Research Communications. 388(4). 626–629. 6 indexed citations
10.
Hothorn, Michael, Heinz Neumann, Esther D. Lenherr, et al.. (2009). Catalytic Core of a Membrane-Associated Eukaryotic Polyphosphate Polymerase. Science. 324(5926). 513–516. 242 indexed citations
11.
Gromes, Roland, Michael Hothorn, Esther D. Lenherr, et al.. (2008). The redox switch of γ‐glutamylcysteine ligase via a reversible monomer–dimer transition is a mechanism unique to plants. The Plant Journal. 54(6). 1063–1075. 56 indexed citations
12.
Denayer, Ellen, Annabel Parret, Magdalena Chmara, et al.. (2007). Mutation analysis in Costello syndrome: functional and structural characterization of theHRASp.Lys117Arg mutation. Human Mutation. 29(2). 232–239. 38 indexed citations
13.
Reinelt, Stefan, et al.. (2006). Structure of the Full-length Enzyme I of the Phosphoenolpyruvate-dependent Sugar Phosphotransferase System. Journal of Biological Chemistry. 281(43). 32508–32515. 26 indexed citations
14.
Reynaud, Emmanuel G., Miguel A. Andrade‐Navarro, Fabien Bonneau, et al.. (2005). Human Lsg1 defines a family of essential GTPases that correlates with the evolution of compartmentalization. BMC Biology. 3(1). 21–21. 46 indexed citations
15.
Hothorn, Michael, I. D’Angelo, José Antonio Márquez, Steffen Greiner, & Klaus Scheffzek. (2003). The Invertase Inhibitor Nt-CIF from Tobacco: A Highly Thermostable Four-helix Bundle with an Unusual N-terminal Extension. Journal of Molecular Biology. 335(4). 987–995. 41 indexed citations
16.
Mijakovic̀, Ivan, Sandrine Poncet, Anne Galinier, et al.. (2002). Pyrophosphate-producing protein dephosphorylation by HPr kinase/phosphorylase: A relic of early life?. Proceedings of the National Academy of Sciences. 99(21). 13442–13447. 100 indexed citations
17.
Russell, Robert B., José Antonio Márquez, Wolfgang Hengstenberg, & Klaus Scheffzek. (2002). Evolutionary relationship between the bacterial HPr kinase and the ubiquitous PEP‐carboxykinase: expanding the P‐loop nucleotidyl transferase superfamily. FEBS Letters. 517(1-3). 1–6. 16 indexed citations
18.
Ylänne, Jari, Klaus Scheffzek, Paul Young, & Matti Saraste. (2001). Crystal Structure of the α-Actinin Rod Reveals an Extensive Torsional Twist. Structure. 9(7). 597–604. 152 indexed citations
19.
Scheffzek, Klaus, Christian Klebe, Karin Fritz‐Wolf, Wolfgang Kabsch, & Alfred Wittinghofer. (1995). Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form. Nature. 374(6520). 378–381. 164 indexed citations
20.
Franken, Sybille, Axel J. Scheidig, Ute Krengel, et al.. (1993). Three-dimensional structures and properties of a transforming and a nontransforming glycine-12 mutant of p21H-ras. Biochemistry. 32(33). 8411–8420. 76 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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