Yaroslav Tsybovsky

8.2k total citations
62 papers, 1.7k citations indexed

About

Yaroslav Tsybovsky is a scholar working on Molecular Biology, Epidemiology and Infectious Diseases. According to data from OpenAlex, Yaroslav Tsybovsky has authored 62 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 20 papers in Epidemiology and 16 papers in Infectious Diseases. Recurrent topics in Yaroslav Tsybovsky's work include Monoclonal and Polyclonal Antibodies Research (13 papers), HIV Research and Treatment (10 papers) and Glycosylation and Glycoproteins Research (7 papers). Yaroslav Tsybovsky is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (13 papers), HIV Research and Treatment (10 papers) and Glycosylation and Glycoproteins Research (7 papers). Yaroslav Tsybovsky collaborates with scholars based in United States, Belarus and Russia. Yaroslav Tsybovsky's co-authors include Krzysztof Palczewski, Robert S. Molday, Sergey A. Krupenko, Natalia I. Krupenko, Henry Donato, Masaru Kanekiyo, Peter D. Kwong, Małgorzata Świder, Sharon Schwartz and Samuel G. Jacobson and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Yaroslav Tsybovsky

60 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Yaroslav Tsybovsky United States 24 965 474 295 259 256 62 1.7k
Russell J. Diefenbach Australia 29 887 0.9× 1.2k 2.6× 106 0.4× 150 0.6× 849 3.3× 62 2.7k
Karen Meerovitch Canada 20 1.7k 1.7× 173 0.4× 61 0.2× 351 1.4× 239 0.9× 26 2.5k
Wenwei Li China 21 411 0.4× 334 0.7× 37 0.1× 215 0.8× 311 1.2× 55 1.3k
Leo Kei Iwai Brazil 21 488 0.5× 347 0.7× 79 0.3× 104 0.4× 201 0.8× 61 1.2k
Silke Hoffmann Germany 23 830 0.9× 131 0.3× 45 0.2× 134 0.5× 110 0.4× 63 1.6k
Nicholas S. Duesbery United States 22 1.9k 1.9× 103 0.2× 70 0.2× 228 0.9× 232 0.9× 48 2.2k
Andrew W. Tai United States 29 1.2k 1.2× 613 1.3× 25 0.1× 351 1.4× 326 1.3× 55 2.6k
Bärbel S. Blaum Germany 22 563 0.6× 166 0.4× 159 0.5× 206 0.8× 927 3.6× 36 1.9k
Alik Honigman Israel 25 918 1.0× 428 0.9× 30 0.1× 142 0.5× 384 1.5× 59 1.8k
B A Nichols United States 19 355 0.4× 328 0.7× 78 0.3× 57 0.2× 240 0.9× 26 1.4k

Countries citing papers authored by Yaroslav Tsybovsky

Since Specialization
Citations

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

Fields of papers citing papers by Yaroslav Tsybovsky

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yaroslav Tsybovsky

This figure shows the co-authorship network connecting the top 25 collaborators of Yaroslav Tsybovsky. A scholar is included among the top collaborators of Yaroslav Tsybovsky 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 Yaroslav Tsybovsky. Yaroslav Tsybovsky 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.
Gardner, Christina L., S. Pletnev, Jinny L. Liu, et al.. (2025). Demonstration of in vivo efficacy, cryo-EM-epitope identification, and breadth of two anti-alphavirus bispecific single domain antibodies. Journal of Virology. 100(1). e0187525–e0187525.
2.
Bu, Wei, Wei‐Hung Chen, Rebecca A. Gillespie, et al.. (2025). Structural basis for complement receptor engagement and virus neutralization through Epstein-Barr virus gp350. Immunity. 58(2). 295–308.e5. 3 indexed citations
3.
Shimberg, Geoffrey D., Grace Mantus, Yaroslav Tsybovsky, et al.. (2025). Early influenza virus exposure shapes the B cell response to influenza vaccination in individuals 50 years later. Immunity. 58(3). 728–744.e9. 5 indexed citations
4.
Zhang, Peng, Jason Gorman, Yaroslav Tsybovsky, et al.. (2024). Design of soluble HIV-1 envelope trimers free of covalent gp120-gp41 bonds with prevalent native-like conformation. Cell Reports. 43(8). 114518–114518. 3 indexed citations
5.
Loomis, Rebecca J., Yen‐Ting Lai, Sun B. Sowers, et al.. (2024). Structure-based design of glycoprotein subunit vaccines for mumps. Proceedings of the National Academy of Sciences. 121(47). e2404053121–e2404053121. 1 indexed citations
6.
Ataca, Sila, Maya Sangesland, Rebeca de Paiva Fróes Rocha, et al.. (2024). Modulating the immunodominance hierarchy of immunoglobulin germline-encoded structural motifs targeting the influenza hemagglutinin stem. Cell Reports. 43(12). 114990–114990. 1 indexed citations
8.
Ou, Li, I‐Ting Teng, Lijuan Yang, et al.. (2023). Structure-based design of a single-chain triple-disulfide-stabilized fusion-glycoprotein trimer that elicits high-titer neutralizing responses against human metapneumovirus. PLoS Pathogens. 19(9). e1011584–e1011584. 5 indexed citations
9.
Byrne, Patrick O., Brian E. Fisher, David R. Ambrozak, et al.. (2023). Structural basis for antibody recognition of vulnerable epitopes on Nipah virus F protein. Nature Communications. 14(1). 1494–1494. 20 indexed citations
10.
Gorman, Jason, Chunyan Wang, Rosemarie D. Mason, et al.. (2022). Cryo-EM structures of prefusion SIV envelope trimer. Nature Structural & Molecular Biology. 29(11). 1080–1091. 7 indexed citations
11.
Xu, Kai, Yiran Wang, Chen‐Hsiang Shen, et al.. (2021). Structural basis of LAIR1 targeting by polymorphic Plasmodium RIFINs. Nature Communications. 12(1). 4226–4226. 6 indexed citations
12.
Crooks, Emma T., E. Duggan, Jinsong Zhang, et al.. (2021). Engineering well-expressed, V2-immunofocusing HIV-1 envelope glycoprotein membrane trimers for use in heterologous prime-boost vaccine regimens. PLoS Pathogens. 17(10). e1009807–e1009807. 8 indexed citations
13.
Chen, Yiwei, Kai Xu, Luca Piccoli, et al.. (2021). Structural basis of malaria RIFIN binding by LILRB1-containing antibodies. Nature. 592(7855). 639–643. 14 indexed citations
14.
Creanga, Adrian, Rebecca A. Gillespie, Brian E. Fisher, et al.. (2021). A comprehensive influenza reporter virus panel for high-throughput deep profiling of neutralizing antibodies. Nature Communications. 12(1). 1722–1722. 37 indexed citations
15.
Verardi, Raffaello, Lisa C. Lindesmith, Yaroslav Tsybovsky, et al.. (2020). Disulfide stabilization of human norovirus GI.1 virus-like particles focuses immune response toward blockade epitopes. npj Vaccines. 5(1). 110–110. 10 indexed citations
16.
Bu, Wei, Michael Joyce, Hanh Nguyen, et al.. (2019). Immunization with Components of the Viral Fusion Apparatus Elicits Antibodies That Neutralize Epstein-Barr Virus in B Cells and Epithelial Cells. Immunity. 50(5). 1305–1316.e6. 129 indexed citations
17.
Zhang, Baoshan, Chen Lei, Chiara Silacci, et al.. (2017). Protection of calves by a prefusion-stabilized bovine RSV F vaccine. npj Vaccines. 2(1). 7–7. 37 indexed citations
18.
Kabanova, Anna, Jessica Marcandalli, Tongqing Zhou, et al.. (2016). Platelet-derived growth factor-α receptor is the cellular receptor for human cytomegalovirus gHgLgO trimer. Nature Microbiology. 1(8). 16082–16082. 140 indexed citations
19.
Tsybovsky, Yaroslav, Tivadar Orban, Robert S. Molday, Derek J. Taylor, & Krzysztof Palczewski. (2013). Molecular Organization and ATP-Induced Conformational Changes of ABCA4, the Photoreceptor-Specific ABC Transporter. Structure. 21(5). 854–860. 46 indexed citations
20.
Tsybovsky, Yaroslav & Sergey A. Krupenko. (2011). Conserved Catalytic Residues of the ALDH1L1 Aldehyde Dehydrogenase Domain Control Binding and Discharging of the Coenzyme. Journal of Biological Chemistry. 286(26). 23357–23367. 30 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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