Fredrik Ekström

1.4k total citations
39 papers, 1.2k citations indexed

About

Fredrik Ekström is a scholar working on Pharmacology, Plant Science and Computational Theory and Mathematics. According to data from OpenAlex, Fredrik Ekström has authored 39 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Pharmacology, 19 papers in Plant Science and 17 papers in Computational Theory and Mathematics. Recurrent topics in Fredrik Ekström's work include Cholinesterase and Neurodegenerative Diseases (30 papers), Computational Drug Discovery Methods (17 papers) and Pesticide Exposure and Toxicity (12 papers). Fredrik Ekström is often cited by papers focused on Cholinesterase and Neurodegenerative Diseases (30 papers), Computational Drug Discovery Methods (17 papers) and Pesticide Exposure and Toxicity (12 papers). Fredrik Ekström collaborates with scholars based in Sweden, United States and Germany. Fredrik Ekström's co-authors include Christine Akfur, Andreas Hörnberg, Yuan‐Ping Pang, Elisabet Artursson, Anna Linusson, Susanne Lundberg, David Andersson, Crister Åstot, Franz Worek and Cecilia Engdahl and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Angewandte Chemie International Edition.

In The Last Decade

Fredrik Ekström

37 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Fredrik Ekström Sweden	20	846	714	369	269	263	39	1.2k
Ondřej Holas Czechia	21	585 0.7×	472 0.7×	211 0.6×	162 0.6×	176 0.7×	47	1.1k
Leo P.A. De Jong Netherlands	25	592 0.7×	1.2k 1.7×	107 0.3×	346 1.3×	266 1.0×	51	1.7k
Veronika Opletalová Czechia	20	429 0.5×	260 0.4×	173 0.5×	117 0.4×	203 0.8×	52	960
Marianne Koller Germany	19	320 0.4×	794 1.1×	57 0.2×	235 0.9×	172 0.7×	44	1.2k
Alexandre A. de Castro Brazil	16	187 0.2×	215 0.3×	132 0.4×	57 0.2×	177 0.7×	57	797
H. P. Benschop Netherlands	19	251 0.3×	740 1.0×	59 0.2×	195 0.7×	219 0.8×	50	1.2k
Tristan Verdelet France	11	330 0.4×	391 0.5×	60 0.2×	108 0.4×	117 0.4×	11	749
Ines Primožič Croatia	18	267 0.3×	177 0.2×	141 0.4×	42 0.2×	208 0.8×	52	836
Frédérique Renault France	16	150 0.2×	247 0.3×	54 0.1×	41 0.2×	224 0.9×	29	640
Daniele Tedesco Italy	15	126 0.1×	83 0.1×	62 0.2×	45 0.2×	278 1.1×	40	804

Countries citing papers authored by Fredrik Ekström

Since Specialization

Citations

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

Fields of papers citing papers by Fredrik Ekström

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Fredrik Ekström

This figure shows the co-authorship network connecting the top 25 collaborators of Fredrik Ekström. A scholar is included among the top collaborators of Fredrik Ekström 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 Fredrik Ekström. Fredrik Ekström 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

Kumari, Rashmi, Rajendra Kumar, Nina Forsgren, et al.. (2024). Enzyme Dynamics Determine the Potency and Selectivity of Inhibitors Targeting Disease-Transmitting Mosquitoes. ACS Infectious Diseases. 10(10). 3664–3680. 2 indexed citations

Ekström, Fredrik, Nina Forsgren, Marco Catto, et al.. (2022). Dual Reversible Coumarin Inhibitors Mutually Bound to Monoamine Oxidase B and Acetylcholinesterase Crystal Structures. ACS Medicinal Chemistry Letters. 13(3). 499–506. 21 indexed citations

Andersson, David, Brijesh Kumar Mishra, Nina Forsgren, Fredrik Ekström, & Anna Linusson. (2020). Physical Mechanisms Governing Substituent Effects on Arene–Arene Interactions in a Protein Milieu. The Journal of Physical Chemistry B. 124(30). 6529–6539. 5 indexed citations

Engdahl, Cecilia, Dariush Nikjoo, Nina Forsgren, et al.. (2017). N-Aryl-N’-ethyleneaminothioureas effectively inhibit acetylcholinesterase 1 from disease-transmitting mosquitoes. European Journal of Medicinal Chemistry. 134. 415–427. 11 indexed citations

Akfur, Christine, et al.. (2016). Structure of a prereaction complex between the nerve agent sarin, its biological target acetylcholinesterase, and the antidote HI-6. Proceedings of the National Academy of Sciences. 113(20). 5514–5519. 46 indexed citations

Engdahl, Cecilia, et al.. (2015). Acetylcholinesterases from the Disease Vectors Aedes aegypti and Anopheles gambiae: Functional Characterization and Comparisons with Vertebrate Orthologues. PLoS ONE. 10(10). e0138598–e0138598. 24 indexed citations

Andersson, David, Cecilia M. Lindgren, Weixing Qian, et al.. (2014). Benefits of statistical molecular design, covariance analysis, and reference models in QSAR: a case study on acetylcholinesterase. Journal of Computer-Aided Molecular Design. 29(3). 199–215. 16 indexed citations

Tong, Fan, et al.. (2013). Effects of anticholinesterases on catalysis and induced conformational change of the peripheral anionic site of murine acetylcholinesterase. Pesticide Biochemistry and Physiology. 106(3). 79–84. 6 indexed citations

Artursson, Elisabet, et al.. (2013). Catalytic-site conformational equilibrium in nerve-agent adducts of acetylcholinesterase: Possible implications for the HI-6 antidote substrate specificity. Biochemical Pharmacology. 85(9). 1389–1397. 34 indexed citations

10.

Qian, Weixing, et al.. (2012). Similar but Different: Thermodynamic and Structural Characterization of a Pair of Enantiomers Binding to Acetylcholinesterase. Angewandte Chemie International Edition. 51(51). 12716–12720. 18 indexed citations

11.

12.

Andersson, David, et al.. (2011). Targeting Acetylcholinesterase: Identification of Chemical Leads by High Throughput Screening, Structure Determination and Molecular Modeling. PLoS ONE. 6(11). e26039–e26039. 63 indexed citations

13.

Artursson, Elisabet, Christine Akfur, Andreas Hörnberg, Franz Worek, & Fredrik Ekström. (2009). Reactivation of tabun-hAChE investigated by structurally analogous oximes and mutagenesis. Toxicology. 265(3). 108–114. 30 indexed citations

14.

Pang, Yuan‐Ping, Fredrik Ekström, Yang Gao, et al.. (2009). Selective and Irreversible Inhibitors of Mosquito Acetylcholinesterases for Controlling Malaria and Other Mosquito-Borne Diseases. PLoS ONE. 4(8). e6851–e6851. 36 indexed citations

15.

Ekström, Fredrik, Crister Åstot, & Yuan‐Ping Pang. (2007). Novel Nerve-Agent Antidote Design Based on Crystallographic and Mass Spectrometric Analyses of Tabun-Conjugated Acetylcholinesterase in Complex with Antidotes. Clinical Pharmacology & Therapeutics. 82(3). 282–293. 69 indexed citations

16.

Svergun, Dmitri I., Fredrik Ekström, Kim D. Vandegriff, et al.. (2007). Solution Structure of Poly(ethylene) Glycol-Conjugated Hemoglobin Revealed by Small-Angle X-Ray Scattering: Implications for a New Oxygen Therapeutic. Biophysical Journal. 94(1). 173–181. 78 indexed citations

17.

Hörnberg, Andreas, et al.. (2007). Crystal Structures of Acetylcholinesterase in Complex with Organophosphorus Compounds Suggest that the Acyl Pocket Modulates the Aging Reaction by Precluding the Formation of the Trigonal Bipyramidal Transition State^,. Biochemistry. 46(16). 4815–4825. 85 indexed citations

18.

Ekström, Fredrik, et al.. (2006). Crystal structures of acetylcholinesterase in complex with HI-6, Ortho-7 and obidoxime: Structural basis for differences in the ability to reactivate tabun conjugates. Biochemical Pharmacology. 72(5). 597–607. 113 indexed citations

19.

Ekström, Fredrik, Günter Stier, & Uwe H. Sauer. (2003). Crystallization of the actin-binding domain of human α-actinin: analysis of microcrystals of SeMet-labelled protein. Acta Crystallographica Section D Biological Crystallography. 59(4). 724–726. 4 indexed citations

20.

Ekström, Fredrik, Günter Stier, Julian T. Eaton, & Uwe H. Sauer. (2003). Crystallization and X-ray analysis of a bacterial non-haem iron-containing phenylalanine hydroxylase from the Gram-negative opportunistic pathogenPseudomonas aeruginosa. Acta Crystallographica Section D Biological Crystallography. 59(7). 1310–1312. 5 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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