Ivan Campeotto

826 total citations
16 papers, 576 citations indexed

About

Ivan Campeotto is a scholar working on Molecular Biology, Materials Chemistry and Biotechnology. According to data from OpenAlex, Ivan Campeotto has authored 16 papers receiving a total of 576 indexed citations (citations by other indexed papers that have themselves been cited), including 11 papers in Molecular Biology, 5 papers in Materials Chemistry and 4 papers in Biotechnology. Recurrent topics in Ivan Campeotto's work include Enzyme Structure and Function (5 papers), Malaria Research and Control (3 papers) and Trypanosoma species research and implications (3 papers). Ivan Campeotto is often cited by papers focused on Enzyme Structure and Function (5 papers), Malaria Research and Control (3 papers) and Trypanosoma species research and implications (3 papers). Ivan Campeotto collaborates with scholars based in United Kingdom, United States and Israel. Ivan Campeotto's co-authors include Angelika Gründling, Rebecca M. Corrigan, Vincent T. Lee, Kevin Roelofs, Paul S. Freemont, Christopher F. Schuster, Lauren E. Bellows, T. Tosi, Yong Everett Zhang and Arwen R. Pearson and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Ivan Campeotto

15 papers receiving 573 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ivan Campeotto United Kingdom 10 382 158 97 94 80 16 576
Jan Gundlach Germany 12 489 1.3× 341 2.2× 106 1.1× 118 1.3× 92 1.1× 14 772
Jason J. Paxman Australia 15 337 0.9× 151 1.0× 97 1.0× 62 0.7× 45 0.6× 30 685
Gerd Prehna United States 16 507 1.3× 223 1.4× 46 0.5× 132 1.4× 49 0.6× 31 813
Yu Sang China 14 314 0.8× 97 0.6× 49 0.5× 64 0.7× 90 1.1× 20 565
Martin Stieger Switzerland 14 616 1.6× 203 1.3× 93 1.0× 119 1.3× 61 0.8× 16 914
Thierry Izoré Australia 16 655 1.7× 267 1.7× 47 0.5× 80 0.9× 61 0.8× 23 1.0k
Linda I. Hu United States 9 530 1.4× 123 0.8× 152 1.6× 51 0.5× 123 1.5× 11 766
Sebastian Zoll Czechia 8 346 0.9× 126 0.8× 27 0.3× 201 2.1× 87 1.1× 14 542
Rebecca Conners United Kingdom 14 294 0.8× 61 0.4× 44 0.5× 48 0.5× 68 0.8× 15 516
Holger Kneuper United Kingdom 15 400 1.0× 294 1.9× 58 0.6× 193 2.1× 41 0.5× 18 689

Countries citing papers authored by Ivan Campeotto

Since Specialization
Citations

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

Fields of papers citing papers by Ivan Campeotto

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ivan Campeotto

This figure shows the co-authorship network connecting the top 25 collaborators of Ivan Campeotto. A scholar is included among the top collaborators of Ivan Campeotto 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 Ivan Campeotto. Ivan Campeotto is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

16 of 16 papers shown
1.
Olmo, Francisco, Timothy J. Ragan, Merve Kaplan, et al.. (2025). Cryo-EM led analysis of open and closed conformations of Chagas vaccine candidate TcPOP. Nature Communications. 16(1). 7164–7164.
2.
Alam, Nawsad, Doris Quinkert, Amelia M. Lias, et al.. (2024). Rational structure-guided design of a blood stage malaria vaccine immunogen presenting a single epitope from PfRH5. EMBO Molecular Medicine. 16(10). 2539–2559. 3 indexed citations
3.
Campeotto, Ivan, et al.. (2024). The Potential of Plant-Produced Virus-like Particle Vaccines for African Horse Sickness and Other Equine Orbiviruses. Pathogens. 13(6). 458–458. 2 indexed citations
4.
Mikolajek, Halina, Juan Sánchez-Weatherby, James Sandy, et al.. (2023). Protein-to-structure pipeline for ambient-temperature in situ crystallography at VMXi. IUCrJ. 10(4). 420–429. 11 indexed citations
5.
Campeotto, Ivan, Francis Galaway, Shahid Mehmood, et al.. (2020). The Structure of the Cysteine-Rich Domain of Plasmodium falciparum P113 Identifies the Location of the RH5 Binding Site. mBio. 11(5). 7 indexed citations
6.
Dekel, Elya, Ivan Campeotto, Jennifer M. Marshall, et al.. (2019). Design of a basigin‐mimicking inhibitor targeting the malaria invasion protein RH5. Proteins Structure Function and Bioinformatics. 88(1). 187–195. 7 indexed citations
7.
Campeotto, Ivan, Andrey A. Lebedev, A.M.M. Schreurs, et al.. (2018). Pathological macromolecular crystallographic data affected by twinning, partial-disorder and exhibiting multiple lattices for testing of data processing and refinement tools. Scientific Reports. 8(1). 14876–14876. 12 indexed citations
8.
Campeotto, Ivan, Adi Goldenzweig, Lea Barfod, et al.. (2017). One-step design of a stable variant of the malaria invasion protein RH5 for use as a vaccine immunogen. Proceedings of the National Academy of Sciences. 114(5). 998–1002. 64 indexed citations
9.
Schuster, Christopher F., Lauren E. Bellows, T. Tosi, et al.. (2016). The second messenger c-di-AMP inhibits the osmolyte uptake system OpuC in Staphylococcus aureus. Science Signaling. 9(441). ra81–ra81. 81 indexed citations
10.
11.
Campeotto, Ivan, et al.. (2014). The Chlamydia Effector TarP Mimics the Mammalian Leucine-Aspartic Acid Motif of Paxillin to Subvert the Focal Adhesion Kinase during Invasion. Journal of Biological Chemistry. 289(44). 30426–30442. 30 indexed citations
12.
Campeotto, Ivan, et al.. (2014). Structural and Mechanistic Insight into the Listeria monocytogenes Two-enzyme Lipoteichoic Acid Synthesis System. Journal of Biological Chemistry. 289(41). 28054–28069. 22 indexed citations
13.
Campeotto, Ivan, Marc W. van der Kamp, Chi H. Trinh, et al.. (2014). Reaction Mechanism of N-Acetylneuraminic Acid Lyase Revealed by a Combination of Crystallography, QM/MM Simulation, and Mutagenesis. ACS Chemical Biology. 9(4). 1025–1032. 42 indexed citations
14.
Corrigan, Rebecca M., et al.. (2013). Systematic identification of conserved bacterial c-di-AMP receptor proteins. Proceedings of the National Academy of Sciences. 110(22). 9084–9089. 214 indexed citations
15.
Campeotto, Ivan, C.A. Dennis, Chi H. Trinh, et al.. (2010). Structural Insights into Substrate Specificity in Variants of N-Acetylneuraminic Acid Lyase Produced by Directed Evolution. Journal of Molecular Biology. 404(1). 56–69. 24 indexed citations
16.
Campeotto, Ivan, S.B. Carr, Chi H. Trinh, et al.. (2009). Structure of anEscherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 Å resolution. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(11). 1088–1090. 9 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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