Erik G. Marklund

4.5k total citations · 1 hit paper
54 papers, 2.6k citations indexed

About

Erik G. Marklund is a scholar working on Molecular Biology, Spectroscopy and Computational Mechanics. According to data from OpenAlex, Erik G. Marklund has authored 54 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 28 papers in Spectroscopy and 11 papers in Computational Mechanics. Recurrent topics in Erik G. Marklund's work include Mass Spectrometry Techniques and Applications (27 papers), Protein Structure and Dynamics (18 papers) and Enzyme Structure and Function (11 papers). Erik G. Marklund is often cited by papers focused on Mass Spectrometry Techniques and Applications (27 papers), Protein Structure and Dynamics (18 papers) and Enzyme Structure and Function (11 papers). Erik G. Marklund collaborates with scholars based in Sweden, United Kingdom and Germany. Erik G. Marklund's co-authors include Justin L. P. Benesch, Carol V. Robinson, Andrew J. Baldwin, Georg Hochberg, Michael T. Marty, David van der Spoel, Anel Mahmutovic, Johan Elf, Petter Hammar and Otto G. Berg and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Erik G. Marklund

53 papers receiving 2.5k citations

Hit Papers

align trajectories

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.

Bayesian Deconvolution of Mass and Ion Mobility Spectra: From Binary Interactions to Polydisperse Ensembles

2015 686 citations Michael T. Marty, Andrew J. Baldwin et al. Analytical Chemistry profile →

Peers

Erik G. Marklund

SPECT

GENET

RADIA

Arash Zarrine‐Afsar Canada

Xiongwu Wu United States

Armin Wagner United Kingdom

Lois Pollack United States

Johan Hattne United States

Robin L. Owen United Kingdom

Richard E. Gillilan United States

Thomas Earnest United States

Zhong Ren United States

Vladislav Orekhov Sweden

Arash Zarrine‐Afsar Canada

Erik G. Marklund

1.6k ×1.0

635 ×0.7

SPECT

773 ×2.5

68 ×0.3

GENET

41 ×0.2

RADIA

Citations per year, relative to Erik G. Marklund Erik G. Marklund (= 1×) peers Arash Zarrine‐Afsar

Countries citing papers authored by Erik G. Marklund

Since Specialization

Citations

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

Fields of papers citing papers by Erik G. Marklund

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Erik G. Marklund. 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 Erik G. Marklund. The network helps show where Erik G. Marklund may publish in the future.

Co-authorship network of co-authors of Erik G. Marklund

This figure shows the co-authorship network connecting the top 25 collaborators of Erik G. Marklund. A scholar is included among the top collaborators of Erik G. Marklund 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 Erik G. Marklund. Erik G. Marklund 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

Jakobsson, Eric, et al.. (2025). Dipole orientation of hydrated gas phase proteins. Physical Chemistry Chemical Physics. 27(21). 10939–10948. 1 indexed citations

Corey, Robin A., Louise Persson, Abraham O. Oluwole, et al.. (2025). Engineering cardiolipin binding to an artificial membrane protein reveals determinants for lipid-mediated stabilization. eLife. 14.

Heimerl, Thomas, Stefan Bohn, Louise Persson, et al.. (2024). Emergence of fractal geometries in the evolution of a metabolic enzyme. Nature. 628(8009). 894–900. 26 indexed citations

Ekeberg, Tomas, et al.. (2024). Enhanced EMC—Advantages of partially known orientations in x-ray single particle imaging. The Journal of Chemical Physics. 160(11). 4 indexed citations

Persson, Louise, Cagla Sahin, Michael Landreh, & Erik G. Marklund. (2024). High-Performance Molecular Dynamics Simulations for Native Mass Spectrometry of Large Protein Complexes with the Fast Multipole Method. Analytical Chemistry. 96(37). 15023–15030. 4 indexed citations

Caleman, Carl, et al.. (2023). Rehydration Post-orientation: Investigating Field-Induced Structural Changes via Computational Rehydration. The Protein Journal. 42(3). 205–218. 5 indexed citations

Persson, Louise, et al.. (2023). Engineered aldolases catalyzing stereoselective aldol reactions between aryl-substituted ketones and aldehydes. Catalysis Science & Technology. 13(17). 4978–4987. 5 indexed citations

Yen, Hsin‐Yung, Mark T. Agasid, Dilraj Lama, et al.. (2022). Electrospray ionization of native membrane proteins proceeds via a charge equilibration step. RSC Advances. 12(16). 9671–9680. 6 indexed citations

Sahin, Cagla, Nicklas Österlund, Jannik Nedergaard Pedersen, et al.. (2022). Structural Basis for Dityrosine-Mediated Inhibition of α-Synuclein Fibrillization. Journal of the American Chemical Society. 144(27). 11949–11954. 11 indexed citations

10.

Mandl, Thomas, et al.. (2021). Protein orientation in time-dependent electric fields: orientation before destruction. Biophysical Journal. 120(17). 3709–3717. 19 indexed citations

11.

Landreh, Michael, Cagla Sahin, Joseph Gault, et al.. (2020). Predicting the Shapes of Protein Complexes through Collision Cross Section Measurements and Database Searches. Analytical Chemistry. 92(18). 12297–12303. 22 indexed citations

12.

Allison, Timothy M., Perdita E. Barran, Sarah Cianférani, et al.. (2020). Computational Strategies and Challenges for Using Native Ion Mobility Mass Spectrometry in Biophysics and Structural Biology. Analytical Chemistry. 92(16). 10872–10880. 29 indexed citations

13.

Allison, Timothy M., Perdita E. Barran, Justin L. P. Benesch, et al.. (2020). Software Requirements for the Analysis and Interpretation of Native Ion Mobility Mass Spectrometry Data. Analytical Chemistry. 92(16). 10881–10890. 17 indexed citations

14.

Marklund, Erik G. & Justin L. P. Benesch. (2019). Weighing-up protein dynamics: the combination of native mass spectrometry and molecular dynamics simulations. Current Opinion in Structural Biology. 54. 50–58. 33 indexed citations

15.

Hochberg, Georg, Dale A. Shepherd, Erik G. Marklund, et al.. (2018). Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions. Science. 359(6378). 930–935. 47 indexed citations

16.

Gault, Joseph, Marcus J.G.W. Ladds, Ingeborg M.M. van Leeuwen, et al.. (2018). Lipids Shape the Electron Acceptor-Binding Site of the Peripheral Membrane Protein Dihydroorotate Dehydrogenase. Cell chemical biology. 25(3). 309–317.e4. 23 indexed citations

17.

Marklund, Erik G., Yichen Zhang, Eman Basha, Justin L. P. Benesch, & Elizabeth Vierling. (2018). Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis. Cell Stress and Chaperones. 23(4). 723–732. 6 indexed citations

18.

Landreh, Michael, Erik G. Marklund, Povilas Uzdavinys, et al.. (2017). Integrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters. Nature Communications. 8(1). 13993–13993. 63 indexed citations

19.

Hammar, Petter, Prune Leroy, Anel Mahmutovic, et al.. (2012). The lac Repressor Displays Facilitated Diffusion in Living Cells. Science. 336(6088). 1595–1598. 309 indexed citations

20.

Spoel, David van der, Erik G. Marklund, Daniel S. D. Larsson, & Carl Caleman. (2010). Proteins, Lipids, and Water in the Gas Phase. Macromolecular Bioscience. 11(1). 50–59. 71 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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