Péter Tompa

33.7k total citations · 12 hit papers
240 papers, 23.8k citations indexed

About

Péter Tompa is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Péter Tompa has authored 240 papers receiving a total of 23.8k indexed citations (citations by other indexed papers that have themselves been cited), including 209 papers in Molecular Biology, 66 papers in Materials Chemistry and 65 papers in Cell Biology. Recurrent topics in Péter Tompa's work include Protein Structure and Dynamics (104 papers), Enzyme Structure and Function (66 papers) and RNA and protein synthesis mechanisms (52 papers). Péter Tompa is often cited by papers focused on Protein Structure and Dynamics (104 papers), Enzyme Structure and Function (66 papers) and RNA and protein synthesis mechanisms (52 papers). Péter Tompa collaborates with scholars based in Hungary, Belgium and United States. Péter Tompa's co-authors include István Simon, Mónika Fuxreiter, Zsuzsanna Dosztányi, Veronika Csizmók, Rohit V. Pappu, Vladimir N. Uversky, Clifford P. Brangwynne, Péter Friedrich, Dénes Kovács and Rita Pancsa and has published in prestigious journals such as Cell, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

Péter Tompa

239 papers receiving 23.6k citations

Hit Papers

Intrinsically unstructured proteins 2002 2026 2010 2018 2002 2005 2014 2018 2015 500 1000 1.5k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Péter Tompa Hungary 64 19.9k 4.9k 3.4k 1.8k 1.6k 240 23.8k
A. Keith Dunker United States 75 22.6k 1.1× 6.2k 1.3× 2.8k 0.8× 2.0k 1.1× 1.6k 1.0× 163 26.8k
Michaël Nilges France 64 23.8k 1.2× 7.0k 1.4× 3.1k 0.9× 2.7k 1.5× 1.2k 0.8× 219 30.5k
Geerten W. Vuister Netherlands 46 15.8k 0.8× 3.8k 0.8× 2.0k 0.6× 3.0k 1.7× 883 0.6× 120 20.2k
Luís Serrano Spain 76 19.6k 1.0× 5.5k 1.1× 2.5k 0.7× 1.4k 0.8× 788 0.5× 314 23.5k
John Kuriyan United States 99 28.8k 1.4× 4.5k 0.9× 4.9k 1.5× 1.1k 0.6× 941 0.6× 235 38.8k
Christopher J. Oldfield United States 52 14.3k 0.7× 4.0k 0.8× 1.7k 0.5× 1.4k 0.8× 913 0.6× 89 17.1k
Guang Zhu Hong Kong 32 13.7k 0.7× 3.1k 0.6× 1.9k 0.6× 2.3k 1.3× 685 0.4× 125 18.4k
Julie D. Forman‐Kay Canada 77 18.7k 0.9× 4.9k 1.0× 2.2k 0.6× 2.8k 1.6× 653 0.4× 218 21.8k
T. Alwyn Jones Sweden 66 21.1k 1.1× 6.0k 1.2× 2.5k 0.7× 762 0.4× 2.1k 1.3× 181 29.7k
Wayne A. Hendrickson United States 89 20.0k 1.0× 5.5k 1.1× 3.9k 1.1× 1.1k 0.6× 831 0.5× 300 32.6k

Countries citing papers authored by Péter Tompa

Since Specialization
Citations

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

Fields of papers citing papers by Péter Tompa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Péter Tompa

This figure shows the co-authorship network connecting the top 25 collaborators of Péter Tompa. A scholar is included among the top collaborators of Péter Tompa 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 Péter Tompa. Péter Tompa 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.
Lázár, Tamás, et al.. (2025). Phase-separating fusion proteins drive cancer by upsetting transcription regulation. Genome biology. 26(1). 330–330. 1 indexed citations
2.
Lengerer, Birgit, Joris Van Lindt, Sébastien Carpentier, et al.. (2024). Recurrent evolution of adhesive defence systems in amphibians by parallel shifts in gene expression. Nature Communications. 15(1). 5612–5612. 1 indexed citations
3.
Lázár, Tamás, Attila Mészáros, Quentin Galand, et al.. (2024). C9orf72-linked arginine-rich dipeptide repeats aggravate pathological phase separation of G3BP1. Proceedings of the National Academy of Sciences. 121(50). e2402847121–e2402847121. 1 indexed citations
4.
Rocha, Fernando, et al.. (2023). Quantification of Surface Tension Effects and Nucleation‐and‐Growth Rates during Self‐Assembly of Biological Condensates. Advanced Science. 10(23). e2301501–e2301501. 3 indexed citations
5.
Groot, Anke de, Stefan Magez, Didier Vertommen, et al.. (2023). Biophysical characterization of the Plasmodium falciparum circumsporozoite protein's N‐terminal domain. Protein Science. 33(1). e4852–e4852. 4 indexed citations
6.
Michiels, Emiel, Anna Bratek‐Skicki, Mathias De Decker, et al.. (2021). Liquid–Liquid Phase Separation Enhances TDP-43 LCD Aggregation but Delays Seeded Aggregation. Biomolecules. 11(4). 548–548. 33 indexed citations
7.
Boeynaems, Steven, Alex S. Holehouse, Venera Weinhardt, et al.. (2019). Spontaneous driving forces give rise to protein−RNA condensates with coexisting phases and complex material properties. Proceedings of the National Academy of Sciences. 116(16). 7889–7898. 341 indexed citations breakdown →
8.
Mészáros, Bálint, Gábor Erdős, Beáta Szabó, et al.. (2019). PhaSePro: the database of proteins driving liquid–liquid phase separation. Nucleic Acids Research. 48(D1). D360–D367. 138 indexed citations
9.
Contreras-Martos, Sara, Alessandro Piai, Simone Kosol, et al.. (2017). Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. Scientific Reports. 7(1). 32 indexed citations
10.
Fischer, Baptiste, Beatriz M. Bonini, Héctor Quezada, et al.. (2017). Fructose-1,6-bisphosphate couples glycolytic flux to activation of Ras. Nature Communications. 8(1). 922–922. 144 indexed citations
11.
Boeynaems, Steven, Mathias De Decker, Péter Tompa, & Ludo Van Den Bosch. (2017). Arginine-rich Peptides Can Actively Mediate Liquid-liquid Phase Separation. BIO-PROTOCOL. 7(17). e2525–e2525. 27 indexed citations
12.
Guharoy, Mainak, Pallab Bhowmick, & Péter Tompa. (2016). Design Principles Involving Protein Disorder Facilitate Specific Substrate Selection and Degradation by the Ubiquitin-Proteasome System. Journal of Biological Chemistry. 291(13). 6723–6731. 40 indexed citations
13.
Aouacheria, Abdel, Christophe Combet, Péter Tompa, & J. Marie Hardwick. (2015). Redefining the BH3 Death Domain as a ‘Short Linear Motif’. Trends in Biochemical Sciences. 40(12). 736–748. 44 indexed citations
14.
Lee, Robin van der, Marija Buljan, Benjamin Lang, et al.. (2014). Classification of Intrinsically Disordered Regions and Proteins. Repository of the Academy's Library (Library of the Hungarian Academy of Sciences). 1 indexed citations
15.
Tantos, Ágnes, Beáta Szabó, András Láng, et al.. (2013). Multiple fuzzy interactions in the moonlighting function of thymosin-β4. PubMed. 1(1). e26204–e26204. 10 indexed citations
16.
Fuxreiter, Mónika & Péter Tompa. (2012). Fuzziness : structural disorder in protein complexes. DIAL (Catholic University of Leuven). 23 indexed citations
17.
Hegyi, Hédi & Péter Tompa. (2011). Increased structural disorder of proteins encoded on human sex chromosomes. Molecular BioSystems. 8(1). 229–236. 19 indexed citations
18.
Tompa, Péter, et al.. (2009). Limitations of Induced Folding in Molecular Recognition by Intrinsically Disordered Proteins. ChemPhysChem. 10(9-10). 1415–1419. 84 indexed citations
19.
Kovács, Dénes, Éva Kalmár, Zsolt Török, & Péter Tompa. (2008). Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins. PLANT PHYSIOLOGY. 147(1). 381–390. 325 indexed citations
20.
Tompa, Péter, Éva Schád, & Péter Friedrich. (2003). A Sensitive and Continuous Fluorometric Activity Assay Using a Natural Substrate: Microtubule-Associated Protein 2. Humana Press eBooks. 144. 137–141. 3 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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