Eberhard Warkentin

3.2k total citations
61 papers, 2.6k citations indexed

About

Eberhard Warkentin is a scholar working on Molecular Biology, Materials Chemistry and Renewable Energy, Sustainability and the Environment. According to data from OpenAlex, Eberhard Warkentin has authored 61 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 29 papers in Materials Chemistry and 19 papers in Renewable Energy, Sustainability and the Environment. Recurrent topics in Eberhard Warkentin's work include Metalloenzymes and iron-sulfur proteins (19 papers), Enzyme Structure and Function (17 papers) and Metabolism and Genetic Disorders (11 papers). Eberhard Warkentin is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (19 papers), Enzyme Structure and Function (17 papers) and Metabolism and Genetic Disorders (11 papers). Eberhard Warkentin collaborates with scholars based in Germany, Japan and France. Eberhard Warkentin's co-authors include Ulrich Ermler, Seigo Shima, Ulrich Ermler, Rudolf K. Thauer, Ulrike Demmer, Sonja Vogt, Oliver Pilak, Wolfram Meyer‐Klaucke, Michael Schick and Christoph H. Hagemeier and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Eberhard Warkentin

61 papers receiving 2.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Eberhard Warkentin Germany 27 1.1k 1.0k 744 693 195 61 2.6k
Evert C. Duin United States 32 1.5k 1.3× 1.1k 1.1× 797 1.1× 679 1.0× 168 0.9× 74 3.0k
Eric M. Shepard United States 28 2.1k 1.9× 1.2k 1.2× 460 0.6× 933 1.3× 261 1.3× 70 3.3k
Ulrich Ermler Germany 30 1.6k 1.5× 2.2k 2.1× 946 1.3× 859 1.2× 228 1.2× 85 4.2k
Jacques Meyer France 29 1.8k 1.7× 1.3k 1.3× 525 0.7× 771 1.1× 82 0.4× 62 3.1k
Peter‐Leon Hagedoorn Netherlands 33 646 0.6× 1.5k 1.4× 494 0.7× 570 0.8× 245 1.3× 127 3.2k
Christopher Dennison United Kingdom 35 513 0.5× 1.8k 1.7× 574 0.8× 775 1.1× 133 0.7× 130 3.4k
Jacques Gaillard France 31 1.0k 1.0× 1.2k 1.2× 550 0.7× 794 1.1× 131 0.7× 109 2.9k
Francis E. Jenney United States 34 808 0.8× 1.9k 1.9× 688 0.9× 780 1.1× 52 0.3× 70 3.4k
Susana L. A. Andrade Germany 25 2.3k 2.1× 936 0.9× 933 1.3× 1.0k 1.5× 449 2.3× 52 4.0k
Margarida Archer Portugal 24 623 0.6× 1.1k 1.0× 263 0.4× 416 0.6× 166 0.9× 66 2.1k

Countries citing papers authored by Eberhard Warkentin

Since Specialization
Citations

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

Fields of papers citing papers by Eberhard Warkentin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Eberhard Warkentin

This figure shows the co-authorship network connecting the top 25 collaborators of Eberhard Warkentin. A scholar is included among the top collaborators of Eberhard Warkentin 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 Eberhard Warkentin. Eberhard Warkentin 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.
Huang, Gangfeng, Tristan Wagner, Ulrike Demmer, et al.. (2020). The Hydride Transfer Process in NADP-dependent Methylene-tetrahydromethanopterin Dehydrogenase. Journal of Molecular Biology. 432(7). 2042–2054. 5 indexed citations
2.
Liu, Wenxia, Aijun Liu, Hailong Gao, et al.. (2018). Structural properties of the peroxiredoxin AhpC2 from the hyperthermophilic eubacterium Aquifex aeolicus. Biochimica et Biophysica Acta (BBA) - General Subjects. 1862(12). 2797–2805. 4 indexed citations
3.
Jiang, Shuai, Lingling Wang, Mengmeng Huang, et al.. (2017). DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum. Frontiers in Immunology. 8. 1607–1607. 37 indexed citations
4.
Schühle, Karola, et al.. (2017). Structure of the acetophenone carboxylase core complex: prototype of a new class of ATP-dependent carboxylases/hydrolases. Scientific Reports. 7(1). 39674–39674. 23 indexed citations
5.
Warkentin, Eberhard, et al.. (2014). Structural diversity of polyoxomolybdate clusters along the three-fold axis of the molybdenum storage protein. Journal of Inorganic Biochemistry. 138. 122–128. 17 indexed citations
6.
Olkhova, Elena, Jochen Wiesner, Ulrike Demmer, et al.. (2013). Structure of the (E)‐4‐hydroxy‐3‐methyl‐but‐2‐enyl‐diphosphate reductase from Plasmodium falciparum. FEBS Letters. 587(24). 3968–3972. 23 indexed citations
7.
Demmer, Ulrike, Eberhard Warkentin, Daniel Kockelkorn, et al.. (2013). Structural Basis for a Bispecific NADP+ and CoA Binding Site in an Archaeal Malonyl-Coenzyme A Reductase. Journal of Biological Chemistry. 288(9). 6363–6370. 19 indexed citations
8.
Harder, Jens, et al.. (2012). Crystal structure of a ring‐cleaving cyclohexane‐1,2‐dione hydrolase, a novel member of the thiamine diphosphate enzyme family. FEBS Journal. 279(7). 1209–1219. 14 indexed citations
9.
Buschmann, Sabine, Eberhard Warkentin, Hao Xie, et al.. (2010). The Structure of cbb 3 Cytochrome Oxidase Provides Insights into Proton Pumping. Science. 329(5989). 327–330. 202 indexed citations
10.
Shima, Seigo, Oliver Pilak, Sonja Vogt, et al.. (2008). The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site. Science. 321(5888). 572–575. 484 indexed citations
11.
Parey, Kristian, Eberhard Warkentin, Kay Diederichs, et al.. (2008). Structure of the Dissimilatory Sulfite Reductase from the Hyperthermophilic Archaeon Archaeoglobus fulgidus. Journal of Molecular Biology. 379(5). 1063–1074. 59 indexed citations
12.
Seedorf, Henning, Christoph H. Hagemeier, Seigo Shima, et al.. (2007). Structure of coenzyme F420H2 oxidase (FprA), a di‐iron flavoprotein from methanogenic Archaea catalyzing the reduction of O2 to H2O. FEBS Journal. 274(6). 1588–1599. 62 indexed citations
13.
Schemberg, Jörg, Klaus Schneider, Ulrike Demmer, et al.. (2007). Towards Biological Supramolecular Chemistry: A Variety of Pocket‐Templated, Individual Metal Oxide Cluster Nucleations in the Cavity of a Mo/W‐Storage Protein. Angewandte Chemie International Edition. 46(14). 2408–2413. 84 indexed citations
14.
Hagemeier, Christoph H., et al.. (2006). Insight into the mechanism of biological methanol activation based on the crystal structure of the methanol-cobalamin methyltransferase complex. Proceedings of the National Academy of Sciences. 103(50). 18917–18922. 72 indexed citations
15.
Acharya, Priyamvada, Eberhard Warkentin, Ulrich Ermler, Rudolf K. Thauer, & Seigo Shima. (2006). The Structure of Formylmethanofuran: Tetrahydromethanopterin Formyltransferase in Complex with its Coenzymes. Journal of Molecular Biology. 357(3). 870–879. 12 indexed citations
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Warkentin, Eberhard, et al.. (2004). Coenzyme Binding in F420-Dependent Secondary Alcohol Dehydrogenase, a Member of the Bacterial Luciferase Family. Structure. 12(3). 361–370. 55 indexed citations
19.
Hagemeier, Christoph H., Seigo Shima, Eberhard Warkentin, Rudolf K. Thauer, & Ulrich Ermler. (2003). Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase fromMethanopyrus kandleri: the selenomethionine-labelled and non-labelled enzyme crystallized in two different forms. Acta Crystallographica Section D Biological Crystallography. 59(9). 1653–1655. 8 indexed citations
20.
Shima, Seigo, Eberhard Warkentin, Rudolf K. Thauer, & Ulrich Ermler. (2002). Structure and function of enzymes involved in the methanogenic pathway utilizing carbon dioxide and molecular hydrogen. Journal of Bioscience and Bioengineering. 93(6). 519–530. 66 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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