Kurt D. Berndt

4.4k total citations · 1 hit paper
50 papers, 3.6k citations indexed

About

Kurt D. Berndt is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Kurt D. Berndt has authored 50 papers receiving a total of 3.6k indexed citations (citations by other indexed papers that have themselves been cited), including 38 papers in Molecular Biology, 10 papers in Materials Chemistry and 6 papers in Genetics. Recurrent topics in Kurt D. Berndt's work include Protein Structure and Dynamics (13 papers), Redox biology and oxidative stress (10 papers) and Enzyme Structure and Function (10 papers). Kurt D. Berndt is often cited by papers focused on Protein Structure and Dynamics (13 papers), Redox biology and oxidative stress (10 papers) and Enzyme Structure and Function (10 papers). Kurt D. Berndt collaborates with scholars based in Sweden, United States and Switzerland. Kurt D. Berndt's co-authors include Fredrik Åslund, Arne Holmgren, Rudolf Ladenstein, Birgitta Agerberth, Guðmundur H. Guðmundsson, Martı́n E. Rottenberg, Jan Johansson, Udo Oppermann, Kerstin Nordstrand and Kurt Wüthrich and has published in prestigious journals such as Cell, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Kurt D. Berndt

48 papers receiving 3.5k citations

Hit Papers

Conformation-dependent An... 1998 2026 2007 2016 1998 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
Kurt D. Berndt Sweden 30 2.6k 731 494 330 325 50 3.6k
Boguslaw Stec United States 38 3.1k 1.2× 903 1.2× 265 0.5× 712 2.2× 407 1.3× 106 5.3k
Thierry Meinnel France 48 4.8k 1.8× 423 0.6× 466 0.9× 155 0.5× 332 1.0× 127 6.4k
Chitrananda Abeygunawardana United States 34 2.2k 0.8× 577 0.8× 231 0.5× 325 1.0× 143 0.4× 55 3.4k
Jimmy B. Feix United States 29 1.8k 0.7× 296 0.4× 559 1.1× 226 0.7× 204 0.6× 80 2.9k
Se Won Suh South Korea 40 4.2k 1.6× 906 1.2× 111 0.2× 317 1.0× 287 0.9× 196 5.7k
Octavian Bârzu France 31 2.5k 0.9× 815 1.1× 167 0.3× 144 0.4× 251 0.8× 124 3.6k
Lanette Fee United States 10 2.9k 1.1× 717 1.0× 103 0.2× 252 0.8× 358 1.1× 12 4.0k
Chuen‐Shang C. Wu United States 14 2.4k 0.9× 414 0.6× 195 0.4× 178 0.5× 278 0.9× 26 3.2k
Alexander Shekhtman United States 37 3.1k 1.2× 301 0.4× 210 0.4× 507 1.5× 227 0.7× 133 4.6k
Pierre Lavigne Canada 33 2.1k 0.8× 273 0.4× 266 0.5× 175 0.5× 294 0.9× 118 4.1k

Countries citing papers authored by Kurt D. Berndt

Since Specialization
Citations

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

Fields of papers citing papers by Kurt D. Berndt

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Kurt D. Berndt. 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 Kurt D. Berndt. The network helps show where Kurt D. Berndt may publish in the future.

Co-authorship network of co-authors of Kurt D. Berndt

This figure shows the co-authorship network connecting the top 25 collaborators of Kurt D. Berndt. A scholar is included among the top collaborators of Kurt D. Berndt 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 Kurt D. Berndt. Kurt D. Berndt 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
2.
Nilsson, Ola B., Justus Adédoyin, Claudio Rhyner, et al.. (2011). In Vitro Evolution of Allergy Vaccine Candidates, with Maintained Structure, but Reduced B Cell and T Cell Activation Capacity. PLoS ONE. 6(9). e24558–e24558. 22 indexed citations
3.
Glaser, Andreas, Margit Schmidt, Catharina Johansson, et al.. (2008). Mutational analysis of amino acid residues involved in IgE-binding to the Malassezia sympodialis allergen Mala s 11. Molecular Immunology. 46(2). 294–303. 18 indexed citations
4.
Kaiser, Liselotte, Tanja Ćirković Veličković, Justus Adédoyin, et al.. (2007). Structural Characterization of the Tetrameric form of the Major Cat Allergen Fel d 1. Journal of Molecular Biology. 370(4). 714–727. 47 indexed citations
5.
Elgán, Tobias H., et al.. (2007). Redox properties and evolution of human glutaredoxins. Proteins Structure Function and Bioinformatics. 68(4). 879–892. 46 indexed citations
6.
Wagner, Claudia, Alexander Rölle, David Cosman, et al.. (2007). Structural Elements Underlying the High Binding Affinity of Human Cytomegalovirus UL18 to Leukocyte Immunoglobulin-like Receptor-1. Journal of Molecular Biology. 373(3). 695–705. 15 indexed citations
7.
Wu, Xiaoqiu, Hans Jörnvall, Kurt D. Berndt, & Udo Oppermann. (2003). Codon optimization reveals critical factors for high level expression of two rare codon genes in Escherichia coli: RNA stability and secondary structure but not tRNA abundance. Biochemical and Biophysical Research Communications. 313(1). 89–96. 93 indexed citations
8.
Filling, Charlotta, Kurt D. Berndt, Jordi Benach, et al.. (2002). Critical Residues for Structure and Catalysis in Short-chain Dehydrogenases/Reductases. Journal of Biological Chemistry. 277(28). 25677–25684. 496 indexed citations
9.
Foloppe, Nicolas, et al.. (2001). Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: comparison with functionally related proteins. Journal of Molecular Biology. 310(2). 449–470. 81 indexed citations
10.
Nordstrand, Kerstin, Anna Sandström, Fredrik Åslund, et al.. (2000). NMR structure of oxidized glutaredoxin 3 from Escherichia coli. Journal of Molecular Biology. 303(3). 423–432. 44 indexed citations
11.
Tjernberg, Lars O., Aladdin Pramanik, Sofie C. Björling, et al.. (1999). Amyloid β-peptide polymerization studied using fluorescence correlation spectroscopy. Chemistry & Biology. 6(1). 53–62. 130 indexed citations
12.
Nordstrand, Kerstin, et al.. (1999). NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism 1 1Edited by P. E. Wright. Journal of Molecular Biology. 286(2). 541–552. 116 indexed citations
13.
Johansson, Jan, Guðmundur H. Guðmundsson, Martı́n E. Rottenberg, Kurt D. Berndt, & Birgitta Agerberth. (1998). Conformation-dependent Antibacterial Activity of the Naturally Occurring Human Peptide LL-37. Journal of Biological Chemistry. 273(6). 3718–3724. 541 indexed citations breakdown →
14.
Hurme, Reini, Kurt D. Berndt, Ellen Namork, & Mikael Rhen. (1996). DNA binding exerted by a bacterial gene regulator with an extensive coiled-coil domain.. Journal of Biological Chemistry. 271(29). 17592–17592. 1 indexed citations
15.
Knapp, Stefan, Andrej Karshikoff, Kurt D. Berndt, et al.. (1996). Thermal Unfolding of the DNA-binding Protein Sso7d from the HyperthermophileSulfolobus solfataricus. Journal of Molecular Biology. 264(5). 1132–1144. 86 indexed citations
16.
Åslund, Fredrik, Kerstin Nordstrand, Kurt D. Berndt, et al.. (1996). Glutaredoxin-3 from Escherichia coli. Journal of Biological Chemistry. 271(12). 6736–6745. 61 indexed citations
17.
Brunne, Roger M., Kurt D. Berndt, Peter Güntert, Kurt Wüthrich, & Wilfred F. van Gunsteren. (1995). Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long‐time molecular dynamics simulations. Proteins Structure Function and Bioinformatics. 23(1). 49–62. 41 indexed citations
18.
Berndt, Kurt D., et al.. (1993). Designed replacement of an internal hydration water molecule in BPTI: structural and functional implications of a Gly-to-Ser mutation. Biochemistry. 32(17). 4564–4570. 48 indexed citations
19.
Berndt, Kurt D., Peter Güntert, Leonard P. M. Orbons, & Kurt Wüthrich. (1992). Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures. Journal of Molecular Biology. 227(3). 757–775. 173 indexed citations
20.
Lerner, Stephen A., et al.. (1984). Effect of Highly Potent Antipseudomonal β-Lactam Agents Alone and in Combination with Aminoglycosides Against Pseudomonas aeruginosa. Clinical Infectious Diseases. 6(Supplement_3). S678–S688. 16 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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