Kasper Kirschner

4.2k total citations
79 papers, 3.5k citations indexed

About

Kasper Kirschner is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, Kasper Kirschner has authored 79 papers receiving a total of 3.5k indexed citations (citations by other indexed papers that have themselves been cited), including 67 papers in Molecular Biology, 51 papers in Materials Chemistry and 24 papers in Biochemistry. Recurrent topics in Kasper Kirschner's work include Enzyme Structure and Function (51 papers), Biochemical and Molecular Research (29 papers) and Protein Structure and Dynamics (28 papers). Kasper Kirschner is often cited by papers focused on Enzyme Structure and Function (51 papers), Biochemical and Molecular Research (29 papers) and Protein Structure and Dynamics (28 papers). Kasper Kirschner collaborates with scholars based in Switzerland, Germany and United States. Kasper Kirschner's co-authors include Andrew N. Lane, Halina Szadkowski, Hans Bisswanger, Marzell Herold, Michael Hennig, Reinhard Sterner, Ulrich Hommel, Johan N. Jansonius, Thomas Niermann and Karolin Luger and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Kasper Kirschner

79 papers receiving 3.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kasper Kirschner Switzerland 35 3.0k 1.9k 590 460 231 79 3.5k
Edith Wilson Miles United States 39 4.7k 1.6× 3.0k 1.6× 1.5k 2.5× 503 1.1× 232 1.0× 120 6.0k
Johan N. Jansonius Switzerland 39 3.7k 1.2× 2.3k 1.2× 1.4k 2.4× 206 0.4× 149 0.6× 68 4.8k
Marino Martinez‐Carrion United States 32 2.0k 0.7× 1.0k 0.5× 892 1.5× 357 0.8× 229 1.0× 126 3.0k
Kyoko Ogasahara Japan 33 2.4k 0.8× 1.4k 0.8× 154 0.3× 257 0.6× 158 0.7× 91 2.8k
Jorge E. Churchich United States 24 1.2k 0.4× 736 0.4× 567 1.0× 240 0.5× 154 0.7× 126 2.0k
Herman Schreuder Germany 32 1.7k 0.6× 527 0.3× 384 0.7× 198 0.4× 149 0.6× 81 3.1k
Katsuhide Yutani Japan 41 3.8k 1.3× 2.1k 1.1× 86 0.1× 370 0.8× 279 1.2× 154 4.5k
Marvin L. Hackert United States 26 1.8k 0.6× 715 0.4× 971 1.6× 375 0.8× 127 0.5× 74 2.7k
Norman J. Oppenheimer United States 34 2.2k 0.8× 443 0.2× 175 0.3× 203 0.4× 286 1.2× 93 4.4k
Hiroshi Taniuchi United States 33 2.4k 0.8× 722 0.4× 101 0.2× 549 1.2× 276 1.2× 82 3.3k

Countries citing papers authored by Kasper Kirschner

Since Specialization
Citations

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

Fields of papers citing papers by Kasper Kirschner

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kasper Kirschner

This figure shows the co-authorship network connecting the top 25 collaborators of Kasper Kirschner. A scholar is included among the top collaborators of Kasper Kirschner 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 Kasper Kirschner. Kasper Kirschner 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.
Mayans, Olga, et al.. (2002). Stabilization of a (βα)8‐barrel protein by an engineered disulfide bridge. European Journal of Biochemistry. 269(4). 1145–1153. 20 indexed citations
2.
Knöchel, Thorsten, et al.. (2002). The Crystal Structure of Indoleglycerol-phosphate Synthase from Thermotoga maritima. Journal of Biological Chemistry. 277(10). 8626–8634. 20 indexed citations
3.
Sterner, Reinhard, et al.. (2001). [23] Phosphoribosylanthranilate isomerase and indoleglycerol-phosphate synthase: Tryptophan biosynthetic enzymes from Thermotoga maritima. Methods in enzymology on CD-ROM/Methods in enzymology. 331. 270–280. 4 indexed citations
4.
Thoma, Ralf, Michael Hennig, Reinhard Sterner, & Kasper Kirschner. (2000). Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima. Structure. 8(3). 265–276. 83 indexed citations
5.
Thoma, Ralf, Martin Schwander, Wolfgang Liebl, Kasper Kirschner, & Reinhard Sterner. (1998). A histidine gene cluster of the hyperthermophile Thermotoga maritima : sequence analysis and evolutionary significance. Extremophiles. 2(4). 379–389. 18 indexed citations
6.
Sterner, Reinhard, Gerd R. Kleemann, Halina Szadkowski, et al.. (1996). Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer. Protein Science. 5(10). 2000–2008. 69 indexed citations
7.
Niermann, Thomas & Kasper Kirschner. (1995). The predicted secondary structure of the G-type glutamineamidotransferase is compatible with TEM-barrel topology. Protein Engineering Design and Selection. 8(6). 535–542. 3 indexed citations
8.
9.
Tomschy, Andrea, et al.. (1994). Autonomous folding of the excised coenzyme‐binding domain of D‐glyceraldehyde 3‐phosphate dehydrogenase from Thermotoga maritima. Protein Science. 3(3). 411–418. 13 indexed citations
10.
Herold, Marzell, et al.. (1992). Collapsed intermediates in the reconstitution of dimeric aspartate aminotransferase from Escherichia coli. European Journal of Biochemistry. 205(2). 603–611. 25 indexed citations
11.
Szadkowski, Halina, et al.. (1992). A fully active variant of dihydrofolate reductase with a circularly permuted sequence. Biochemistry. 31(6). 1621–1630. 64 indexed citations
12.
Urfer, Roman & Kasper Kirschner. (1992). The importance of surface loops for stabilizing an eightfold βα barrel protein. Protein Science. 1(1). 31–45. 46 indexed citations
13.
Niermann, Thomas & Kasper Kirschner. (1991). Improving the prediction of secondary structure of ‘TIM-barrel’ enzymes. Protein Engineering Design and Selection. 4(3). 359–370. 27 indexed citations
14.
Kirschner, Kasper, Andrew N. Lane, & Alexander W.M. Strasser. (1991). Reciprocal communication between the lyase and synthase active sites of the tryptophan synthase bienzyme complex. Biochemistry. 30(2). 472–478. 63 indexed citations
15.
16.
Luger, Karolin, Halina Szadkowski, & Kasper Kirschner. (1990). An 8-fold βα barrel protein with redundant folding possibilities. Protein Engineering Design and Selection. 3(4). 249–258. 29 indexed citations
17.
Herold, Marzell & Kasper Kirschner. (1990). Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: characterization of a monomeric intermediate. Biochemistry. 29(7). 1907–1913. 91 indexed citations
18.
Eberhard, Marc O. & Kasper Kirschner. (1989). Modification of a catalytically important residue of indoleglycerol‐phosphate synthase from Escherichia coli. FEBS Letters. 245(1-2). 219–222. 8 indexed citations
19.
Jäger, J., E. Köhler, Paul A. Tucker, et al.. (1989). Crystallization and preliminary X-ray studies of an aspartate aminotransferase mutant from Escherichia coli. Journal of Molecular Biology. 209(3). 499–501. 16 indexed citations
20.
Crawford, Irving P., Thomas Niermann, & Kasper Kirschner. (1987). Prediction of secondary structure by evolutionary comparison: Application to the α subunit of tryptophan synthase. Proteins Structure Function and Bioinformatics. 2(2). 118–129. 109 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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