Robert Konrat

7.0k total citations · 1 hit paper
194 papers, 5.3k citations indexed

About

Robert Konrat is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, Robert Konrat has authored 194 papers receiving a total of 5.3k indexed citations (citations by other indexed papers that have themselves been cited), including 146 papers in Molecular Biology, 68 papers in Spectroscopy and 60 papers in Materials Chemistry. Recurrent topics in Robert Konrat's work include Protein Structure and Dynamics (77 papers), Enzyme Structure and Function (49 papers) and Advanced NMR Techniques and Applications (44 papers). Robert Konrat is often cited by papers focused on Protein Structure and Dynamics (77 papers), Enzyme Structure and Function (49 papers) and Advanced NMR Techniques and Applications (44 papers). Robert Konrat collaborates with scholars based in Austria, Poland and United States. Robert Konrat's co-authors include Bernhard Kräutler, Lewis E. Kay, Karin Kloiber, Martin Tollinger, Sébastien J. F. Vincent, Catherine Zwahlen, Pascale Legault, Jack Greenblatt, Georg Kontaxis and Christoph Kreutz and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Robert Konrat

186 papers receiving 5.2k citations

Hit Papers

Methods for Measurement of Intermolecular NOEs by Multinu... 1997 2026 2006 2016 1997 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert Konrat Austria 39 3.9k 1.3k 1.1k 431 395 194 5.3k
Vladimı́r Saudek Czechia 39 6.0k 1.5× 996 0.8× 932 0.8× 224 0.5× 344 0.9× 96 8.4k
Peter Schmieder Germany 42 3.3k 0.9× 1.1k 0.8× 723 0.6× 92 0.2× 350 0.9× 166 5.3k
Richard H. Griffey United States 43 5.1k 1.3× 2.0k 1.6× 611 0.5× 262 0.6× 383 1.0× 139 7.8k
Jonathan P. Waltho United Kingdom 45 4.6k 1.2× 720 0.6× 1.3k 1.2× 141 0.3× 184 0.5× 143 6.0k
Neil A. Farrow United States 30 3.8k 1.0× 849 0.7× 1.1k 1.0× 73 0.2× 277 0.7× 51 5.6k
R. Andrew Byrd United States 36 2.7k 0.7× 1.1k 0.9× 765 0.7× 44 0.1× 440 1.1× 109 4.1k
Christina Redfield United Kingdom 40 4.2k 1.1× 1.0k 0.8× 1.8k 1.6× 48 0.1× 192 0.5× 140 5.5k
Torbjörn Drakenberg Sweden 45 3.1k 0.8× 1.1k 0.9× 948 0.8× 61 0.1× 259 0.7× 182 6.6k
William W. Bachovchin United States 41 2.3k 0.6× 607 0.5× 658 0.6× 109 0.3× 121 0.3× 105 4.4k
Kevin H. Gardner United States 54 7.4k 1.9× 1.1k 0.9× 1.4k 1.2× 39 0.1× 171 0.4× 116 9.8k

Countries citing papers authored by Robert Konrat

Since Specialization
Citations

This map shows the geographic impact of Robert Konrat'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 Robert Konrat with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Robert Konrat more than expected).

Fields of papers citing papers by Robert Konrat

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert Konrat. 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 Robert Konrat. The network helps show where Robert Konrat may publish in the future.

Co-authorship network of co-authors of Robert Konrat

This figure shows the co-authorship network connecting the top 25 collaborators of Robert Konrat. A scholar is included among the top collaborators of Robert Konrat 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 Robert Konrat. Robert Konrat 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.
Sagan, Filip, et al.. (2025). From Weak Interactions to High Stability: Deciphering the Streptavidin–Biotin Interaction through NMR and Computational Analysis. The Journal of Physical Chemistry B. 129(20). 4917–4928.
2.
Barbieri, Letizia, Katharina Maier, Lucia Banci, et al.. (2024). The synthesis of specifically isotope labelled fluorotryptophan and its use in mammalian cell-based protein expression for 19F-NMR applications. Chemical Communications. 60(96). 14188–14191.
3.
Platzer, Gerald, Jark Böttcher, Julian E. Fuchs, et al.. (2023). Ligand 1 H NMR Chemical Shifts as Accurate Reporters for Protein‐Ligand Binding Interfaces in Solution**. ChemPhysChem. 25(1). e202300636–e202300636. 4 indexed citations
4.
Kontaxis, Georg, et al.. (2021). Detecting anisotropic segmental dynamics in disordered proteins by cross-correlated spin relaxation. SHILAP Revista de lepidopterología. 2(2). 557–569. 5 indexed citations
5.
Konrat, Robert, et al.. (2021). Association between Predicted Effects of TP53 Missense Variants on Protein Conformation and Their Phenotypic Presentation as Li-Fraumeni Syndrome or Hereditary Breast Cancer. International Journal of Molecular Sciences. 22(12). 6345–6345. 4 indexed citations
6.
Košťan, Július, Miha Pavšič, Thomas C. Schwarz, et al.. (2021). Molecular basis of F-actin regulation and sarcomere assembly via myotilin. PLoS Biology. 19(4). e3001148–e3001148. 11 indexed citations
7.
Mateos, Borja, Ganeko Bernardo‐Seisdedos, Gabriel Ortega, et al.. (2021). Cosolute modulation of protein oligomerization reactions in the homeostatic timescale. Biophysical Journal. 120(10). 2067–2077. 4 indexed citations
8.
Platzer, Gerald, Moriz Mayer, Sven Brüschweiler, et al.. (2020). Titelbild: PI by NMR: Probing CH–π Interactions in Protein–Ligand Complexes by NMR Spectroscopy (Angew. Chem. 35/2020). Angewandte Chemie. 132(35). 14805–14805. 1 indexed citations
9.
Zawadzka‐Kazimierczuk, Anna, et al.. (2020). Using Cross‐Correlated Spin Relaxation to Characterize Backbone Dihedral Angle Distributions of Flexible Protein Segments. ChemPhysChem. 22(1). 18–28. 9 indexed citations
10.
Olsen, Gregory L., Or Szekely, Borja Mateos, et al.. (2020). Sensitivity-enhanced three-dimensional and carbon-detected two-dimensional NMR of proteins using hyperpolarized water. Journal of Biomolecular NMR. 74(2-3). 161–171. 16 indexed citations
11.
Platzer, Gerald, Moriz Mayer, Sven Brüschweiler, et al.. (2020). PI by NMR: Probing CH–π Interactions in Protein–Ligand Complexes by NMR Spectroscopy. Angewandte Chemie. 132(35). 14971–14978. 13 indexed citations
12.
Platzer, Gerald, Moriz Mayer, Sven Brüschweiler, et al.. (2020). PI by NMR: Probing CH–π Interactions in Protein–Ligand Complexes by NMR Spectroscopy. Angewandte Chemie International Edition. 59(35). 14861–14868. 57 indexed citations
13.
Mateos, Borja, Michał Nowakowski, Mateusz Urbańczyk, et al.. (2020). Temperature as an Extra Dimension in Multidimensional Protein NMR Spectroscopy. Chemistry - A European Journal. 27(5). 1753–1767. 7 indexed citations
14.
Geist, Leonhard, Moriz Mayer, Xiaoling Cockcroft, et al.. (2017). Direct NMR Probing of Hydration Shells of Protein Ligand Interfaces and Its Application to Drug Design. Journal of Medicinal Chemistry. 60(21). 8708–8715. 23 indexed citations
15.
Juen, Michael Andreas, Christoph H. Wunderlich, Felix Nußbaumer, et al.. (2016). Excited States of Nucleic Acids Probed by Proton Relaxation Dispersion NMR Spectroscopy. Angewandte Chemie International Edition. 55(39). 12008–12012. 40 indexed citations
16.
Juen, Michael Andreas, Christoph H. Wunderlich, Felix Nußbaumer, et al.. (2016). Excited States of Nucleic Acids Probed by Proton Relaxation Dispersion NMR Spectroscopy. Angewandte Chemie. 128(39). 12187–12191. 9 indexed citations
17.
Pons, Miquel, et al.. (2011). Meta-structure correlation in protein space unveils different selection rules for folded and intrinsically disordered proteins. Molecular BioSystems. 8(1). 411–416. 12 indexed citations
18.
Schedlbauer, Andreas, Rosaria Gandini, Georg Kontaxis, et al.. (2011). The C-terminus of ICln is Natively Disordered but Displays Local Structural Preformation. Cellular Physiology and Biochemistry. 28(6). 1203–1210. 8 indexed citations
19.
Watschinger, Katrin, Markus A. Keller, Georg Golderer, et al.. (2010). Identification of the gene encoding alkylglycerol monooxygenase defines a third class of tetrahydrobiopterin-dependent enzymes. Proceedings of the National Academy of Sciences. 107(31). 13672–13677. 74 indexed citations
20.
Kreutz, Christoph, Hanspeter Kählig, Robert Konrat, & Ronald Micura. (2005). Ribose 2‘- F Labeling:  A Simple Tool for the Characterization of RNA Secondary Structure Equilibria by 19 F NMR Spectroscopy. Journal of the American Chemical Society. 127(33). 11558–11559. 69 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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