Frank Sobott

10.8k total citations · 1 hit paper
169 papers, 7.2k citations indexed

About

Frank Sobott is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, Frank Sobott has authored 169 papers receiving a total of 7.2k indexed citations (citations by other indexed papers that have themselves been cited), including 102 papers in Molecular Biology, 71 papers in Spectroscopy and 23 papers in Materials Chemistry. Recurrent topics in Frank Sobott's work include Mass Spectrometry Techniques and Applications (68 papers), Protein Structure and Dynamics (27 papers) and Analytical Chemistry and Chromatography (23 papers). Frank Sobott is often cited by papers focused on Mass Spectrometry Techniques and Applications (68 papers), Protein Structure and Dynamics (27 papers) and Analytical Chemistry and Chromatography (23 papers). Frank Sobott collaborates with scholars based in United Kingdom, Belgium and United States. Frank Sobott's co-authors include Carol V. Robinson, Albert Konijnenberg, Justin L. P. Benesch, Margaret G. McCammon, Helena Hernández, Frederik Lermyte, Annika Butterer, Bernhard Brutschy, J. Günter Grossmann and Brandon T. Ruotolo and has published in prestigious journals such as Nature, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

Frank Sobott

168 papers receiving 7.2k citations

Hit Papers

A homologue of the Parkinson’s disease-associated protein... 2017 2026 2020 2023 2017 100 200 300 400

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Frank Sobott United Kingdom 49 4.5k 2.5k 970 597 474 169 7.2k
Andrew J. Baldwin United Kingdom 38 5.7k 1.3× 1.4k 0.6× 1.2k 1.2× 281 0.5× 567 1.2× 87 7.5k
Gavin E. Reid Australia 52 7.0k 1.6× 3.9k 1.5× 489 0.5× 375 0.6× 481 1.0× 204 11.0k
Perdita E. Barran United Kingdom 47 3.3k 0.7× 2.9k 1.2× 825 0.9× 123 0.2× 238 0.5× 194 6.7k
Justin L. P. Benesch United Kingdom 51 6.1k 1.4× 3.6k 1.4× 1.6k 1.6× 437 0.7× 849 1.8× 130 8.7k
Arthur Laganowsky United States 35 4.1k 0.9× 1.8k 0.7× 678 0.7× 212 0.4× 406 0.9× 105 5.7k
Michael A. Baldwin United States 39 4.3k 1.0× 1.9k 0.8× 344 0.4× 317 0.5× 269 0.6× 99 6.1k
Cait E. MacPhee United Kingdom 44 4.6k 1.0× 1.1k 0.4× 1.3k 1.3× 446 0.7× 374 0.8× 97 7.0k
Masahiro Shirakawa Japan 56 6.8k 1.5× 813 0.3× 2.2k 2.3× 1.0k 1.7× 674 1.4× 205 9.7k
Wenzhu Zhang China 40 3.9k 0.9× 1.8k 0.7× 1.4k 1.4× 228 0.4× 340 0.7× 109 6.4k
J. Martin Scholtz United States 45 8.5k 1.9× 1.2k 0.5× 3.0k 3.1× 619 1.0× 748 1.6× 91 10.9k

Countries citing papers authored by Frank Sobott

Since Specialization
Citations

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

Fields of papers citing papers by Frank Sobott

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Frank Sobott

This figure shows the co-authorship network connecting the top 25 collaborators of Frank Sobott. A scholar is included among the top collaborators of Frank Sobott 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 Frank Sobott. Frank Sobott 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.
Brockwell, David J., et al.. (2025). Zn2+ Binding Shifts the Conformational Ensemble of α-Synuclein Monomers toward Accelerated Amyloid Formation. Journal of the American Chemical Society. 147(40). 36464–36477. 1 indexed citations
2.
Singh, Ranjan K., et al.. (2024). Toxin:antitoxin ratio sensing autoregulation of the Vibrio cholerae parDE2 module. Science Advances. 10(1). eadj2403–eadj2403. 2 indexed citations
3.
Uddin, Muhammad Ramiz, Mohammad Moniruzzaman, Katie M. Kuo, et al.. (2023). Conformational restriction shapes the inhibition of a multidrug efflux adaptor protein. Nature Communications. 14(1). 3900–3900. 15 indexed citations
4.
Yusupov, Maksudbek, et al.. (2022). Molecular understanding of the possible mechanisms of oligosaccharide oxidation by cold plasma. Plasma Processes and Polymers. 20(2). 10 indexed citations
5.
Ulamec, Sabine M., Roberto Maya‐Martinez, Yong Xu, et al.. (2022). Single residue modulators of amyloid formation in the N-terminal P1-region of α-synuclein. Nature Communications. 13(1). 4986–4986. 34 indexed citations
7.
Germani, Francesca, David Hoogewijs, Marcelo A. Martí, et al.. (2021). Structural modeling of a novel membrane-bound globin-coupled sensor in Geobacter sulfurreducens. Computational and Structural Biotechnology Journal. 19. 1874–1888. 1 indexed citations
8.
Klebl, David P., Stephan Niebling, Martin A. Schroer, et al.. (2021). Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis. Nature Communications. 12(1). 2889–2889. 13 indexed citations
9.
Bruyn, Pieter De, Milan Malfait, Yann G.‐J. Sterckx, et al.. (2021). Nanobody-aided crystallization of the transcription regulator PaaR2 from Escherichia coli O157:H7. Acta Crystallographica Section F Structural Biology Communications. 77(10). 374–384. 1 indexed citations
10.
Cánovas, Rocío, Elise Daems, Rui Campos, et al.. (2021). Novel electrochemiluminescent assay for the aptamer-based detection of testosterone. Talanta. 239. 123121–123121. 20 indexed citations
11.
Maso, Lorenzo, Giulia Moro, Elise Daems, et al.. (2021). Unveiling the binding mode of perfluorooctanoic acid to human serum albumin. Protein Science. 30(4). 830–841. 46 indexed citations
12.
Cecco, Elena De, Erika Ponzini, Pierluigi Mauri, et al.. (2021). Profiling Dopamine-Induced Oxidized Proteoforms of β-synuclein by Top-Down Mass Spectrometry. Antioxidants. 10(6). 893–893. 2 indexed citations
13.
Moons, Rani, et al.. (2020). Effects of Detergent on α-Synuclein Structure: A Native MS-Ion Mobility Study. International Journal of Molecular Sciences. 21(21). 7884–7884. 13 indexed citations
14.
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
15.
Leemans, Margaux, Egon Deyaert, Elise Daems, et al.. (2020). Allosteric modulation of the GTPase activity of a bacterial LRRK2 homolog by conformation-specific Nanobodies. Biochemical Journal. 477(7). 1203–1218. 11 indexed citations
16.
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
17.
Ponzini, Erika, Antonella De Palma, Antonino Natalello, et al.. (2019). Methionine oxidation in α-synuclein inhibits its propensity for ordered secondary structure. Journal of Biological Chemistry. 294(14). 5657–5665. 31 indexed citations
18.
Li, Jinyu, Giulia Rossetti, Albert Konijnenberg, et al.. (2017). Proton Dynamics in Protein Mass Spectrometry. The Journal of Physical Chemistry Letters. 8(6). 1105–1112. 39 indexed citations
19.
Chatzi, Katerina E., Marios Frantzeskos Sardis, Alexandra Tsirigotaki, et al.. (2017). Preprotein mature domains contain translocase targeting signals that are essential for secretion. The Journal of Cell Biology. 216(5). 1357–1369. 57 indexed citations
20.
Burger, Virginia, Jelle Hendrix, Albert Konijnenberg, et al.. (2017). Hidden States within Disordered Regions of the CcdA Antitoxin Protein. Journal of the American Chemical Society. 139(7). 2693–2701. 6 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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