Cathleen Zeymer

1.3k total citations · 1 hit paper
29 papers, 936 citations indexed

About

Cathleen Zeymer is a scholar working on Molecular Biology, Materials Chemistry and Renewable Energy, Sustainability and the Environment. According to data from OpenAlex, Cathleen Zeymer has authored 29 papers receiving a total of 936 indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 9 papers in Materials Chemistry and 8 papers in Renewable Energy, Sustainability and the Environment. Recurrent topics in Cathleen Zeymer's work include Protein Structure and Dynamics (9 papers), Enzyme Structure and Function (7 papers) and Enzyme Catalysis and Immobilization (6 papers). Cathleen Zeymer is often cited by papers focused on Protein Structure and Dynamics (9 papers), Enzyme Structure and Function (7 papers) and Enzyme Catalysis and Immobilization (6 papers). Cathleen Zeymer collaborates with scholars based in Germany, Switzerland and United States. Cathleen Zeymer's co-authors include Donald Hilvert, Jochen Reinstein, Andreas Klein, Nicolas D. Werbeck, Reinhard Zschoche, Moritz Pott, Andrew D. Griffiths, Jeffrey W. Bode, Richard Obexer and Thomas Wucherpfennig and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Cathleen Zeymer

25 papers receiving 929 citations

Hit Papers

Directed Evolution of Protein Catalysts 2018 2026 2020 2023 2018 100 200 300

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Cathleen Zeymer Germany 17 647 192 163 127 100 29 936
Adrian Romero‐Rivera Spain 15 482 0.7× 211 1.1× 121 0.7× 174 1.4× 48 0.5× 19 801
Daniel F. Sauer Germany 18 457 0.7× 89 0.5× 413 2.5× 82 0.6× 78 0.8× 36 772
Carolin Mügge Germany 15 457 0.7× 82 0.4× 238 1.5× 112 0.9× 117 1.2× 36 735
Vincent Lebrun France 11 481 0.7× 220 1.1× 412 2.5× 79 0.6× 133 1.3× 26 1.0k
Fahui Li China 17 648 1.0× 166 0.9× 152 0.9× 172 1.4× 33 0.3× 45 1.1k
Boyan Zhang China 25 965 1.5× 221 1.2× 106 0.7× 110 0.9× 213 2.1× 54 1.7k
Alexandre Barrozo France 15 335 0.5× 152 0.8× 93 0.6× 47 0.4× 122 1.2× 23 721
Anca Pordea United Kingdom 14 388 0.6× 116 0.6× 466 2.9× 81 0.6× 105 1.1× 27 805
Yakov Kipnis United States 12 582 0.9× 135 0.7× 86 0.5× 91 0.7× 31 0.3× 15 733
Ivana Drienovská Netherlands 13 601 0.9× 88 0.5× 349 2.1× 54 0.4× 69 0.7× 23 818

Countries citing papers authored by Cathleen Zeymer

Since Specialization
Citations

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

Fields of papers citing papers by Cathleen Zeymer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Cathleen Zeymer

This figure shows the co-authorship network connecting the top 25 collaborators of Cathleen Zeymer. A scholar is included among the top collaborators of Cathleen Zeymer 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 Cathleen Zeymer. Cathleen Zeymer 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.
Klassen, R. Bryan, et al.. (2025). A Luminescence-Based Screening Platform for Lanthanide-Binding Peptides and Proteins. ACS Chemical Biology. 20(12). 2897–2906.
3.
Klein, Andreas, Ghulam Mustafa, Erling Thyrhaug, et al.. (2025). The Natural Redox Cofactor Pyrroloquinoline Quinone (PQQ) Enables Photocatalytic Radical Cyclizations. Angewandte Chemie International Edition. 64(40). e202505431–e202505431.
4.
Vornholt, Tobias, et al.. (2024). Artificial metalloenzymes. Nature Reviews Methods Primers. 4(1). 28 indexed citations
5.
Klein, Andreas, et al.. (2024). A De Novo Metalloenzyme for Cerium Photoredox Catalysis. Journal of the American Chemical Society. 146(38). 25976–25985. 33 indexed citations
6.
Beil, Sebastian B., Sylvestre Bonnet, Carla Casadevall, et al.. (2024). Challenges and Future Perspectives in Photocatalysis: Conclusions from an Interdisciplinary Workshop. JACS Au. 4(8). 2746–2766. 51 indexed citations
7.
Steudtner, Robin, Andreas Klein, Cathleen Zeymer, et al.. (2023). Innentitelbild: Minor Actinides Can Replace Essential Lanthanides in Bacterial Life (Angew. Chem. 31/2023). Angewandte Chemie. 135(31).
8.
Steudtner, Robin, Andreas Klein, Cathleen Zeymer, et al.. (2023). Minor Actinides Can Replace Essential Lanthanides in Bacterial Life**. Angewandte Chemie International Edition. 62(31). e202303669–e202303669. 14 indexed citations
9.
Steudtner, Robin, Andreas Klein, Cathleen Zeymer, et al.. (2023). Minor Actinides Can Replace Essential Lanthanides in Bacterial Life**. Angewandte Chemie. 135(31). 1 indexed citations
10.
Klein, Andreas & Cathleen Zeymer. (2021). Design and engineering of artificial metalloproteins: from de novo metal coordination to catalysis. Protein Engineering Design and Selection. 34. 20 indexed citations
11.
Drobot, Björn, et al.. (2021). Americium preferred: lanmodulin, a natural lanthanide-binding protein favors an actinide over lanthanides. Chemical Science. 12(47). 15581–15587. 31 indexed citations
12.
Hofmann, Raphael, et al.. (2020). Lysine acylation using conjugating enzymes for site-specific modification and ubiquitination of recombinant proteins. Nature Chemistry. 12(11). 1008–1015. 57 indexed citations
13.
Huang, Po‐Ssu, et al.. (2020). Tight and specific lanthanide binding in a de novo TIM barrel with a large internal cavity designed by symmetric domain fusion. Proceedings of the National Academy of Sciences. 117(48). 30362–30369. 46 indexed citations
14.
Bunzel, H. Adrian, Hajo Kries, Cathleen Zeymer, et al.. (2019). Emergence of a Negative Activation Heat Capacity during Evolution of a Designed Enzyme. Journal of the American Chemical Society. 141(30). 11745–11748. 45 indexed citations
15.
Zeymer, Cathleen, Reinhard Zschoche, & Donald Hilvert. (2017). Optimization of Enzyme Mechanism along the Evolutionary Trajectory of a Computationally Designed (Retro-)Aldolase. Journal of the American Chemical Society. 139(36). 12541–12549. 43 indexed citations
16.
Zeymer, Cathleen, Nicolas D. Werbeck, Sabine Zimmermann, Jochen Reinstein, & D. Flemming Hansen. (2016). Characterizing Active Site Conformational Heterogeneity along the Trajectory of an Enzymatic Phosphoryl Transfer Reaction. Angewandte Chemie. 128(38). 11705–11709. 1 indexed citations
17.
Zeymer, Cathleen, Nicolas D. Werbeck, Sabine Zimmermann, Jochen Reinstein, & D. Flemming Hansen. (2016). Characterizing Active Site Conformational Heterogeneity along the Trajectory of an Enzymatic Phosphoryl Transfer Reaction. Angewandte Chemie International Edition. 55(38). 11533–11537. 18 indexed citations
18.
Loll, Bernhard, et al.. (2014). RNA Specificity and Regulation of Catalysis in the Eukaryotic Polynucleotide Kinase Clp1. Molecular Cell. 54(6). 975–986. 18 indexed citations
19.
Zeymer, Cathleen, Nicolas D. Werbeck, Ilme Schlichting, & Jochen Reinstein. (2013). The Molecular Mechanism of Hsp100 Chaperone Inhibition by the Prion Curing Agent Guanidinium Chloride. Journal of Biological Chemistry. 288(10). 7065–7076. 18 indexed citations
20.
Phillips, Aaron H., Dehua Zhao, Marie Demuez, et al.. (2010). A Sterile α-Motif Domain in NafY Targets Apo-NifDK for Iron-Molybdenum Cofactor Delivery via a Tethered Domain. Journal of Biological Chemistry. 286(8). 6321–6328. 15 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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