Dmitri I. Svergun

64.4k total citations · 23 hit papers
569 papers, 50.2k citations indexed

About

Dmitri I. Svergun is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Dmitri I. Svergun has authored 569 papers receiving a total of 50.2k indexed citations (citations by other indexed papers that have themselves been cited), including 396 papers in Molecular Biology, 232 papers in Materials Chemistry and 46 papers in Cell Biology. Recurrent topics in Dmitri I. Svergun's work include Enzyme Structure and Function (212 papers), Protein Structure and Dynamics (137 papers) and RNA and protein synthesis mechanisms (59 papers). Dmitri I. Svergun is often cited by papers focused on Enzyme Structure and Function (212 papers), Protein Structure and Dynamics (137 papers) and RNA and protein synthesis mechanisms (59 papers). Dmitri I. Svergun collaborates with scholars based in Germany, Russia and United Kingdom. Dmitri I. Svergun's co-authors include Maxim V. Petoukhov, Michel H. J. Koch, В. В. Волков, Petr V. Konarev, Daniel Franke, Manuel Koch, L. A. Feĭgin, C. Barberato, Alexey Kikhney and Haydyn D. T. Mertens and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Dmitri I. Svergun

567 papers receiving 49.8k citations

Hit Papers

Determination of the regularization parameter in indirect... 1987 2026 2000 2013 1992 1995 2003 1987 1999 1000 2.0k 3.0k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Dmitri I. Svergun Germany 86 33.2k 15.5k 4.2k 4.1k 3.0k 569 50.2k
Vladimir N. Uversky United States 132 51.9k 1.6× 13.9k 0.9× 3.9k 0.9× 7.2k 1.8× 4.5k 1.5× 1.1k 73.4k
David Eisenberg United States 120 46.7k 1.4× 10.0k 0.6× 4.0k 1.0× 3.9k 1.0× 3.0k 1.0× 409 62.2k
Jeremy C. Smith United States 92 32.0k 1.0× 7.8k 0.5× 4.2k 1.0× 3.3k 0.8× 3.7k 1.3× 848 58.8k
Andrej Săli United States 107 50.4k 1.5× 11.4k 0.7× 5.2k 1.2× 4.8k 1.2× 3.4k 1.1× 381 66.1k
Jane S. Richardson United States 57 43.5k 1.3× 12.8k 0.8× 5.7k 1.4× 4.5k 1.1× 2.2k 0.7× 130 59.8k
Helen M. Berman United States 68 37.5k 1.1× 10.3k 0.7× 3.0k 0.7× 1.6k 0.4× 2.8k 0.9× 247 49.9k
Yang Zhang China 89 37.2k 1.1× 7.2k 0.5× 3.2k 0.8× 2.0k 0.5× 1.9k 0.7× 956 53.4k
Wolfgang Kabsch Germany 47 34.2k 1.0× 12.7k 0.8× 3.7k 0.9× 5.3k 1.3× 2.0k 0.7× 65 47.6k
Erik Lindahl Sweden 54 40.9k 1.2× 12.0k 0.8× 2.7k 0.7× 3.2k 0.8× 4.7k 1.6× 197 71.6k
Barry Honig United States 108 37.5k 1.1× 9.0k 0.6× 2.6k 0.6× 4.2k 1.0× 4.1k 1.4× 347 51.3k

Countries citing papers authored by Dmitri I. Svergun

Since Specialization
Citations

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

Fields of papers citing papers by Dmitri I. Svergun

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Dmitri I. Svergun. 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 Dmitri I. Svergun. The network helps show where Dmitri I. Svergun may publish in the future.

Co-authorship network of co-authors of Dmitri I. Svergun

This figure shows the co-authorship network connecting the top 25 collaborators of Dmitri I. Svergun. A scholar is included among the top collaborators of Dmitri I. Svergun 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 Dmitri I. Svergun. Dmitri I. Svergun 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.
Loers, Gabriele, Cy M. Jeffries, Rob Meijers, et al.. (2023). X‐ray structure and function of fibronectin domains two and three of the neural cell adhesion molecule L1. The FASEB Journal. 37(3). e22823–e22823. 2 indexed citations
2.
Rouillon, Christophe, Stefano Da Vela, Katrin Ackermann, et al.. (2022). Antiviral signalling by a cyclic nucleotide activated CRISPR protease. Nature. 614(7946). 168–174. 30 indexed citations
3.
Mertens, Haydyn D. T., et al.. (2022). N-terminal phosphorylation regulates the activity of glycogen synthase kinase 3 from Plasmodium falciparum. Biochemical Journal. 479(3). 337–356. 3 indexed citations
4.
Svergun, Dmitri I., et al.. (2022). Determinants of receptor tyrosine phosphatase homophilic adhesion: Structural comparison of PTPRK and PTPRM extracellular domains. Journal of Biological Chemistry. 299(1). 102750–102750. 1 indexed citations
5.
Krichel, Boris, Christina Schmidt, Clément Blanchet, et al.. (2021). Hallmarks of Alpha- and Betacoronavirus non-structural protein 7+8 complexes. Science Advances. 7(10). 16 indexed citations
6.
Lyu, Chen, Stefano Da Vela, Youssra K. Al‐Hilaly, et al.. (2021). The Disease Associated Tau35 Fragment has an Increased Propensity to Aggregate Compared to Full-Length Tau. Frontiers in Molecular Biosciences. 8. 779240–779240. 10 indexed citations
7.
Dhamotharan, Karthikeyan, Karol Kaszuba, Haydyn D. T. Mertens, et al.. (2020). Structural role of essential light chains in the apicomplexan glideosome. Communications Biology. 3(1). 568–568. 13 indexed citations
8.
Sadana, Pooja, Cy M. Jeffries, Dmitri I. Svergun, et al.. (2020). RovC - a novel type of hexameric transcriptional activator promoting type VI secretion gene expression. PLoS Pathogens. 16(9). e1008552–e1008552. 7 indexed citations
9.
Różycki, Bartosz, et al.. (2020). Capturing the Conformational Ensemble of the Mixed Folded Polyglutamine Protein Ataxin-3. Structure. 29(1). 70–81.e5. 12 indexed citations
10.
Vela, Stefano Da, et al.. (2018). Structure-specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones. Journal of Biological Chemistry. 293(26). 10071–10083. 9 indexed citations
11.
Filippov, Sergey K., Bart Verbraeken, Petr V. Konarev, et al.. (2017). Block and Gradient Copoly(2-oxazoline) Micelles: Strikingly Different on the Inside. The Journal of Physical Chemistry Letters. 8(16). 3800–3804. 49 indexed citations
12.
Buetow, Lori, Giancarlo Tria, Syed Feroj Ahmed, et al.. (2016). Casitas B-lineage lymphoma linker helix mutations found in myeloproliferative neoplasms affect conformation. BMC Biology. 14(1). 76–76. 15 indexed citations
13.
Blanchet, Clément, C. Hermes, Dmitri I. Svergun, & Stefan Fiedler. (2015). A small and robust active beamstop for scattering experiments on high-brilliance undulator beamlines. Journal of Synchrotron Radiation. 22(2). 461–464. 13 indexed citations
14.
Soykan, Tolga, Giancarlo Tria, Dmitri I. Svergun, et al.. (2014). A conformational switch in collybistin determines the differentiation of inhibitory postsynapses. The EMBO Journal. 33(18). 2113–2133. 80 indexed citations
15.
Otrelo-Cardoso, Ana Rita, M.A.S. Correia, Dmitri I. Svergun, et al.. (2014). Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis. International Journal of Molecular Sciences. 15(2). 2223–2236. 12 indexed citations
16.
Begum, A., Alexey Kikhney, Ingrid Müller, et al.. (2013). Staphylococcus aureusthiaminase II: oligomerization warrants proteolytic protection against serine proteases. Acta Crystallographica Section D Biological Crystallography. 69(12). 2320–2329. 5 indexed citations
17.
Morgan, Hugh P., Haydyn D. T. Mertens, Mara Guariento, et al.. (2012). Structural Analysis of the C-Terminal Region (Modules 18–20) of Complement Regulator Factor H (FH). PLoS ONE. 7(2). e32187–e32187. 44 indexed citations
18.
Clark, Elizabeth A., S.J. Crennell, Abhishek Upadhyay, et al.. (2010). A structural basis for Staphylococcal complement subversion: X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3d. Molecular Immunology. 48(4). 452–462. 18 indexed citations
19.
Fagan, Robert P., D. Albesa-Jové, Omar Qazi, et al.. (2009). Structural insights into the molecular organization of the S‐layer from Clostridium difficile. Molecular Microbiology. 71(5). 1308–1322. 105 indexed citations
20.
Weghofer, Margit, Tea Pavkov‐Keller, Petr V. Konarev, et al.. (2007). Structural characterization of mite allergen Der p 21. Allergy. 62. 300–300. 1 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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