Oscar Vadas

2.8k total citations
43 papers, 1.5k citations indexed

About

Oscar Vadas is a scholar working on Molecular Biology, Parasitology and Epidemiology. According to data from OpenAlex, Oscar Vadas has authored 43 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 28 papers in Molecular Biology, 9 papers in Parasitology and 7 papers in Epidemiology. Recurrent topics in Oscar Vadas's work include Protein Kinase Regulation and GTPase Signaling (14 papers), PI3K/AKT/mTOR signaling in cancer (12 papers) and Toxoplasma gondii Research Studies (9 papers). Oscar Vadas is often cited by papers focused on Protein Kinase Regulation and GTPase Signaling (14 papers), PI3K/AKT/mTOR signaling in cancer (12 papers) and Toxoplasma gondii Research Studies (9 papers). Oscar Vadas collaborates with scholars based in Switzerland, United Kingdom and United States. Oscar Vadas's co-authors include John E. Burke, Roger Williams, Olga Perišić, Xuxiao Zhang, Alex Berndt, Glenn R. Masson, Gillian L. Dornan, Meredith L. Jenkins, Karen E. Anderson and Phillip T. Hawkins and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Angewandte Chemie International Edition.

In The Last Decade

Oscar Vadas

40 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Oscar Vadas Switzerland 18 1.1k 273 253 189 189 43 1.5k
Rashna Bhandari India 23 1.0k 0.9× 144 0.5× 539 2.1× 203 1.1× 148 0.8× 40 1.6k
Ingrid Remy Canada 14 1.6k 1.5× 83 0.3× 388 1.5× 300 1.6× 207 1.1× 15 2.2k
Mark R. Parthun United States 33 3.4k 3.0× 123 0.5× 166 0.7× 329 1.7× 149 0.8× 66 3.8k
Séverine Boulon France 17 2.0k 1.8× 80 0.3× 267 1.1× 226 1.2× 111 0.6× 21 2.3k
Till Bartke Germany 22 2.4k 2.1× 191 0.7× 122 0.5× 358 1.9× 219 1.2× 30 2.7k
David R. Loiselle United States 21 927 0.8× 65 0.2× 174 0.7× 111 0.6× 175 0.9× 31 1.3k
Christine Yu United States 15 1.3k 1.2× 101 0.4× 205 0.8× 383 2.0× 303 1.6× 21 1.7k
Sophie Bonnal Spain 20 2.4k 2.1× 102 0.4× 61 0.2× 114 0.6× 154 0.8× 33 2.6k
Alessandro Cuomo Italy 24 1.8k 1.6× 41 0.2× 256 1.0× 350 1.9× 252 1.3× 48 2.3k
Stefan Lampel Germany 13 1.2k 1.1× 132 0.5× 124 0.5× 161 0.9× 72 0.4× 16 1.8k

Countries citing papers authored by Oscar Vadas

Since Specialization
Citations

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

Fields of papers citing papers by Oscar Vadas

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Oscar Vadas

This figure shows the co-authorship network connecting the top 25 collaborators of Oscar Vadas. A scholar is included among the top collaborators of Oscar Vadas 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 Oscar Vadas. Oscar Vadas 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.
Pacheco, Nicolas Dos Santos, et al.. (2026). MyoL-Dependent Coupling of Preconoidal Rings to Conoid Is Required for Motility in Toxoplasma gondii. bioRxiv (Cold Spring Harbor Laboratory).
2.
Marq, Jean‐Baptiste, Nicolas Dos Santos Pacheco, Bohumil Maco, et al.. (2025). RNG2 tethers the conoid to the apical polar ring in Toxoplasma gondii to enable parasite motility and invasion. PLoS Biology. 23(11). e3003506–e3003506. 1 indexed citations
3.
Marq, Jean‐Baptiste, Oscar Vadas, Bohumil Maco, et al.. (2024). Cytokinetic abscission in Toxoplasma gondii is governed by protein phosphatase 2A and the daughter cell scaffold complex. The EMBO Journal. 43(17). 3752–3786.
4.
Höpfler, Markus, Oscar Vadas, Evangelia Vartholomaiou, et al.. (2024). Soluble αβ-tubulins reversibly sequester TTC5 to regulate tubulin mRNA decay. Nature Communications. 15(1). 9963–9963. 7 indexed citations
5.
Wang, Chaoyue, Rafael E. O. Rocha, Joachim Kloehn, et al.. (2024). Apicomplexan mitoribosome from highly fragmented rRNAs to a functional machine. Nature Communications. 15(1). 10689–10689. 2 indexed citations
6.
Kumar, Amit, Oscar Vadas, Nicolas Dos Santos Pacheco, et al.. (2023). Structural and regulatory insights into the glideosome-associated connector from Toxoplasma gondii. eLife. 12. 6 indexed citations
7.
Galdadas, Ioannis, Mark D. Tully, Oscar Vadas, et al.. (2023). Architecture of the MKK6-p38α complex defines the basis of MAPK specificity and activation. Science. 381(6663). 1217–1225. 21 indexed citations
8.
Yang, Lixin, Agnès Zettor, Oscar Vadas, et al.. (2023). Effective Inhibition of TDP‐43 Aggregation by Native State Stabilization. Angewandte Chemie. 136(3). 3 indexed citations
9.
Yang, Lixin, Agnès Zettor, Oscar Vadas, et al.. (2023). Effective Inhibition of TDP‐43 Aggregation by Native State Stabilization. Angewandte Chemie International Edition. 63(3). e202314587–e202314587. 9 indexed citations
10.
Nixon, Gemma L., Neil G. Berry, Suet C. Leung, et al.. (2023). Design, synthesis and modelling of photoreactive chemical probes for investigating target engagement of plasmepsin IX and X in Plasmodium falciparum. RSC Chemical Biology. 5(1). 19–29. 6 indexed citations
11.
Pacheco, Nicolas Dos Santos, Lorenzo Brusini, Nicolò Tosetti, et al.. (2022). Conoid extrusion regulates glideosome assembly to control motility and invasion in Apicomplexa. Nature Microbiology. 7(11). 1777–1790. 32 indexed citations
12.
Lo, Wen‐Ting, Yingyi Zhang, Oscar Vadas, et al.. (2022). Structural basis of phosphatidylinositol 3-kinase C2α function. Nature Structural & Molecular Biology. 29(3). 218–228. 22 indexed citations
13.
Rathinaswamy, Manoj Kumar, Udit Dalwadi, Kaelin D. Fleming, et al.. (2021). Structure of the phosphoinositide 3-kinase (PI3K) p110γ-p101 complex reveals molecular mechanism of GPCR activation. Science Advances. 7(35). 32 indexed citations
14.
Lentini, Gaëlle, Rouaa Ben Chaabene, Oscar Vadas, et al.. (2021). Structural insights into an atypical secretory pathway kinase crucial for Toxoplasma gondii invasion. Nature Communications. 12(1). 3788–3788. 15 indexed citations
15.
Kilic, Sinan, et al.. (2021). SUV39 SET domains mediate crosstalk of heterochromatic histone marks. eLife. 10. 24 indexed citations
16.
Dornan, Gillian L., Braden D. Siempelkamp, Meredith L. Jenkins, et al.. (2017). Conformational disruption of PI3Kδ regulation by immunodeficiency mutations in PIK3CD and PIK3R1. Proceedings of the National Academy of Sciences. 114(8). 1982–1987. 81 indexed citations
17.
Žagar, Andreja Vujičić, Léonardo Scapozza, & Oscar Vadas. (2017). Design and purification of active truncated phosphoinositide 3-kinase gamma protein constructs for structural studies. Protein Expression and Purification. 135. 1–7. 3 indexed citations
18.
Lo, Wen‐Ting, Andreja Vujičić Žagar, Fabian Gerth, et al.. (2017). A Coincidence Detection Mechanism Controls PX-BAR Domain-Mediated Endocytic Membrane Remodeling via an Allosteric Structural Switch. Developmental Cell. 43(4). 522–529.e4. 26 indexed citations
19.
Vadas, Oscar, Meredith L. Jenkins, Gillian L. Dornan, & John E. Burke. (2016). Using Hydrogen–Deuterium Exchange Mass Spectrometry to Examine Protein–Membrane Interactions. Methods in enzymology on CD-ROM/Methods in enzymology. 583. 143–172. 44 indexed citations
20.

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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