Oliver Einsle

14.1k total citations · 3 hit papers
186 papers, 9.7k citations indexed

About

Oliver Einsle is a scholar working on Molecular Biology, Renewable Energy, Sustainability and the Environment and Inorganic Chemistry. According to data from OpenAlex, Oliver Einsle has authored 186 papers receiving a total of 9.7k indexed citations (citations by other indexed papers that have themselves been cited), including 84 papers in Molecular Biology, 83 papers in Renewable Energy, Sustainability and the Environment and 43 papers in Inorganic Chemistry. Recurrent topics in Oliver Einsle's work include Metalloenzymes and iron-sulfur proteins (81 papers), Metal-Catalyzed Oxygenation Mechanisms (37 papers) and Photosynthetic Processes and Mechanisms (32 papers). Oliver Einsle is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (81 papers), Metal-Catalyzed Oxygenation Mechanisms (37 papers) and Photosynthetic Processes and Mechanisms (32 papers). Oliver Einsle collaborates with scholars based in Germany, United States and France. Oliver Einsle's co-authors include Douglas C. Rees, Susana L. A. Andrade, Peter M. H. Kroneck, James B. Howard, F. Akif Tezcan, Thomas Spatzal, Daniel Sippel, Albrecht Messerschmidt, Benedikt Schmid and Mika Yoshida and has published in prestigious journals such as Nature, Science and Chemical Reviews.

In The Last Decade

Oliver Einsle

182 papers receiving 9.6k citations

Hit Papers

align trajectories sort by overperformance

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Nitrogenase MoFe-Protein at 1.16 Å Resolution: A Central Ligand in the FeMo-Cofactor

2002 875 citations Oliver Einsle, F. Akif Tezcan et al. Science profile →
Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor

2011 728 citations Thomas Spatzal, Susana L. A. Andrade et al. Science profile →
Structural basis of biological nitrogen fixation

2005 673 citations Douglas C. Rees, F. Akif Tezcan et al. Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences profile →

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author						Papers	Cites
Oliver Einsle	4.5k	2.9k	2.4k	2.1k	2.0k	186	9.7k
John W. Peters	8.7k 1.9×	3.4k 1.2×	1.9k 0.8×	2.1k 1.0×	2.6k 1.3×	226	14.0k
Robert R. Eady	3.3k 0.7×	2.4k 0.8×	1.2k 0.5×	1.8k 0.9×	1.4k 0.7×	162	6.6k
Isabel Moura	5.7k 1.3×	4.5k 1.6×	568 0.2×	3.5k 1.6×	2.5k 1.2×	375	12.8k
José J. G. Moura	6.5k 1.5×	5.9k 2.0×	673 0.3×	4.2k 2.0×	3.2k 1.6×	491	16.0k
Dennis R. Dean	13.1k 2.9×	5.1k 1.8×	5.6k 2.3×	3.5k 1.6×	3.5k 1.8×	228	17.9k
James B. Howard	4.3k 1.0×	2.8k 1.0×	1.8k 0.8×	1.9k 0.9×	1.6k 0.8×	89	8.5k
Holger Dobbek	3.7k 0.8×	2.3k 0.8×	814 0.3×	1.7k 0.8×	1.3k 0.7×	117	6.6k
Markus W. Ribbe	5.1k 1.1×	1.0k 0.4×	2.4k 1.0×	1.8k 0.8×	1.6k 0.8×	147	6.7k
Lance C. Seefeldt	12.9k 2.9×	2.2k 0.8×	8.3k 3.5×	3.2k 1.5×	4.7k 2.3×	213	17.1k
Juan C. Fontecilla‐Camps	7.7k 1.7×	3.9k 1.4×	725 0.3×	1.8k 0.8×	2.9k 1.5×	153	14.1k

Countries citing papers authored by Oliver Einsle

Since Specialization

Citations

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

Fields of papers citing papers by Oliver Einsle

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Oliver Einsle

This figure shows the co-authorship network connecting the top 25 collaborators of Oliver Einsle. A scholar is included among the top collaborators of Oliver Einsle 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 Oliver Einsle. Oliver Einsle is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Saleem-Batcha, R., Josef Winter, S. Gerhardt, et al.. (2025). Structural Insights into Broad‐Range Polyphosphate Kinase 2‐II Enzymes Applicable for Pyrimidine Nucleoside Diphosphate Synthesis. ChemBioChem. 26(5). e202400970–e202400970. 3 indexed citations

Breit, Bernhard, et al.. (2025). A Novel Inhibitor against the Bromodomain Protein 1 of the Malaria Pathogen Plasmodium Falciparum. ChemMedChem. 20(11). e202500024–e202500024. 1 indexed citations

Zhang, Lin, et al.. (2024). How sensor Amt-like proteins integrate ammonium signals. Science Advances. 10(23). eadm9441–eadm9441. 6 indexed citations

Melesina, Jelena, Dina Robaa, Lin Zhang, et al.. (2024). Structure–Activity Studies of 1,2,4-Oxadiazoles for the Inhibition of the NAD⁺-Dependent Lysine Deacylase Sirtuin 2. Journal of Medicinal Chemistry. 67(12). 10076–10095. 7 indexed citations

Einsle, Oliver. (2023). On the Shoulders of Giants—Reaching for Nitrogenase. Molecules. 28(24). 7959–7959. 6 indexed citations

Einsle, Oliver. (2023). Catalysis and structure of nitrogenases. Current Opinion in Structural Biology. 83. 102719–102719. 17 indexed citations

Lycus, Pawel, Oliver Einsle, & Lin Zhang. (2023). Structural biology of proteins involved in nitrogen cycling. Current Opinion in Chemical Biology. 74. 102278–102278. 4 indexed citations

Wohlwend, Daniel, et al.. (2022). Respiratory complex I with charge symmetry in the membrane arm pumps protons. Proceedings of the National Academy of Sciences. 119(27). e2123090119–e2123090119. 12 indexed citations

Campo, Julia S. Martín del, Marcelo Bueno Batista, Florence Mus, et al.. (2022). Overview of physiological, biochemical, and regulatory aspects of nitrogen fixation in Azotobacter vinelandii. Critical Reviews in Biochemistry and Molecular Biology. 57(5-6). 492–538. 25 indexed citations

10.

Zhang, Lin, et al.. (2021). Architecture of the membrane-bound cytochrome c heme lyase CcmF. Nature Chemical Biology. 17(7). 800–805. 19 indexed citations

11.

Costa, Nazua L., B. A. Hermann, Vincent Fourmond, et al.. (2019). How Thermophilic Gram-Positive Organisms Perform Extracellular Electron Transfer: Characterization of the Cell Surface Terminal Reductase OcwA. mBio. 10(4). 34 indexed citations

12.

Sippel, Daniel, Michael F. Rohde, H. Netzer, et al.. (2018). A bound reaction intermediate sheds light on the mechanism of nitrogenase. Science. 359(6383). 1484–1489. 247 indexed citations

13.

Birke, Jakob, et al.. (2017). Structural and Functional Analysis of Latex Clearing Protein (Lcp) Provides Insight into the Enzymatic Cleavage of Rubber. Scientific Reports. 7(1). 6179–6179. 35 indexed citations

14.

Dantas, Joana M., et al.. (2017). NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens. FEBS Letters. 591(12). 1657–1666. 18 indexed citations

15.

Gerhardt, S., et al.. (2016). Crystal structure of Cdc11, a septin subunit from Saccharomyces cerevisiae. Journal of Structural Biology. 193(3). 157–161. 24 indexed citations

16.

Spatzal, Thomas, Kathryn Perez, Oliver Einsle, James B. Howard, & Douglas C. Rees. (2014). Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase. Science. 345(6204). 1620–1623. 343 indexed citations

17.

Schmitt, Georg, et al.. (2013). Structure of the processive rubber oxygenase RoxA from Xanthomonas sp. Proceedings of the National Academy of Sciences. 110(34). 13833–13838. 39 indexed citations

18.

Ullmann, G. Matthias, et al.. (2007). Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase. Proceedings of the National Academy of Sciences. 104(9). 3073–3077. 111 indexed citations

19.

Rees, Douglas C., F. Akif Tezcan, Chad Haynes, et al.. (2005). Structural basis of biological nitrogen fixation. Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences. 363(1829). 971–984. 673 indexed citations breakdown →

20.

Messerschmidt, Albrecht, et al.. (2004). Crystal structure of pyrogallol–phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols. Proceedings of the National Academy of Sciences. 101(32). 11571–11576. 39 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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