Joost Snijder

7.2k total citations · 4 hit papers
67 papers, 3.8k citations indexed

About

Joost Snijder is a scholar working on Molecular Biology, Ecology and Infectious Diseases. According to data from OpenAlex, Joost Snijder has authored 67 papers receiving a total of 3.8k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 21 papers in Ecology and 13 papers in Infectious Diseases. Recurrent topics in Joost Snijder's work include Bacteriophages and microbial interactions (21 papers), Monoclonal and Polyclonal Antibodies Research (11 papers) and Glycosylation and Glycoproteins Research (10 papers). Joost Snijder is often cited by papers focused on Bacteriophages and microbial interactions (21 papers), Monoclonal and Polyclonal Antibodies Research (11 papers) and Glycosylation and Glycoproteins Research (10 papers). Joost Snijder collaborates with scholars based in Netherlands, United States and Germany. Joost Snijder's co-authors include Albert J. R. Heck, David Veesler, Alexandra C. Walls, F.A. Rey, M. Alejandra Tortorici, Berend‐Jan Bosch, Xiaoli Xiong, Tobias P. Wörner, Antonette Bennett and Mavis Agbandje‐McKenna and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Joost Snijder

64 papers receiving 3.8k citations

Hit Papers

Tectonic conformational changes of a coronavirus spike gl... 2016 2026 2019 2022 2017 2019 2016 2021 100 200 300

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Joost Snijder Netherlands 34 1.7k 1.4k 684 606 574 67 3.8k
Mark Yeager United States 48 4.2k 2.5× 1.9k 1.4× 280 0.4× 1.2k 2.1× 681 1.2× 115 7.8k
Charlotte Uetrecht Germany 29 1.3k 0.8× 519 0.4× 899 1.3× 730 1.2× 313 0.5× 75 2.8k
Dieter Blaas Austria 49 3.2k 1.9× 1.3k 0.9× 377 0.6× 542 0.9× 648 1.1× 178 7.6k
Kelly K. Lee United States 32 1.8k 1.1× 579 0.4× 338 0.5× 437 0.7× 265 0.5× 82 3.0k
Gerrit Vriend Netherlands 30 3.3k 2.0× 701 0.5× 179 0.3× 494 0.8× 616 1.1× 50 5.2k
Marianne Manchester United States 49 3.0k 1.8× 1.2k 0.9× 299 0.4× 1.9k 3.2× 944 1.6× 97 6.9k
Takanori Nakane Japan 32 6.1k 3.7× 1.1k 0.8× 203 0.3× 611 1.0× 720 1.3× 57 8.7k
Sonia Longhi France 52 4.6k 2.8× 1.2k 0.9× 700 1.0× 744 1.2× 717 1.2× 155 7.9k
Roman Tůma United Kingdom 37 2.3k 1.4× 482 0.3× 163 0.2× 1.2k 2.1× 520 0.9× 107 3.9k
Michael S. Chapman United States 39 3.5k 2.1× 1.1k 0.8× 187 0.3× 457 0.8× 2.5k 4.4× 117 5.6k

Countries citing papers authored by Joost Snijder

Since Specialization
Citations

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

Fields of papers citing papers by Joost Snijder

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Joost Snijder

This figure shows the co-authorship network connecting the top 25 collaborators of Joost Snijder. A scholar is included among the top collaborators of Joost Snijder 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 Joost Snijder. Joost Snijder 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.
Rocha, Rebeca de Paiva Fróes, Ilhan Tomris, Charles A. Bowman, et al.. (2025). Structural and immunological characterization of the H3 influenza hemagglutinin during antigenic drift. Nature Communications. 16(1). 11452–11452.
3.
Granneman, J.C.M., et al.. (2023). Contactin 2 homophilic adhesion structure and conformational plasticity. Structure. 32(1). 60–73.e5. 4 indexed citations
4.
Pronker, Matti F., Ieva Drulyte, Ruben J. G. Hulswit, et al.. (2023). Sialoglycan binding triggers spike opening in a human coronavirus. Nature. 624(7990). 201–206. 37 indexed citations
5.
Wang, Chunyan, Emma L. Hesketh, Wentao Li, et al.. (2022). Antigenic structure of the human coronavirus OC43 spike reveals exposed and occluded neutralizing epitopes. Nature Communications. 13(1). 2921–2921. 20 indexed citations
6.
Hurdiss, Daniel L., Lisa Bauer, Nicolas Papageorgiou, et al.. (2022). Fluoxetine targets an allosteric site in the enterovirus 2C AAA+ ATPase and stabilizes a ring-shaped hexameric complex. Science Advances. 8(1). eabj7615–eabj7615. 18 indexed citations
7.
Kuppeveld, Frank J. M. van, et al.. (2022). Inhibition of H1 and H5 Influenza A Virus Entry by Diverse Macrocyclic Peptides Targeting the Hemagglutinin Stem Region. ACS Chemical Biology. 17(9). 2425–2436. 7 indexed citations
8.
Pronker, Matti F., et al.. (2021). Mass Spectrometry-Based De Novo Sequencing of Monoclonal Antibodies Using Multiple Proteases and a Dual Fragmentation Scheme. Journal of Proteome Research. 20(7). 3559–3566. 39 indexed citations
9.
Bouwman, Kim M., Ilhan Tomris, Hannah L. Turner, et al.. (2021). Multimerization- and glycosylation-dependent receptor binding of SARS-CoV-2 spike proteins. PLoS Pathogens. 17(2). e1009282–e1009282. 23 indexed citations
10.
Wörner, Tobias P., Antonette Bennett, Joost Snijder, et al.. (2021). Adeno-associated virus capsid assembly is divergent and stochastic. Nature Communications. 12(1). 1642–1642. 151 indexed citations breakdown →
11.
Hurdiss, Daniel L., Ieva Drulyte, Yifei Lang, et al.. (2020). Cryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans. Nature Communications. 11(1). 4646–4646. 24 indexed citations
12.
Wörner, Tobias P., et al.. (2020). Mass Spectrometry-Based Structural Virology. Analytical Chemistry. 93(1). 620–640. 38 indexed citations
13.
Walls, Alexandra C., Xiaoli Xiong, Young‐Jun Park, et al.. (2020). Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion. Cell. 183(6). 1732–1732. 21 indexed citations
14.
Dang, Ha V., Yee‐Peng Chan, Young‐Jun Park, et al.. (2019). An antibody against the F glycoprotein inhibits Nipah and Hendra virus infections. Nature Structural & Molecular Biology. 26(10). 980–987. 71 indexed citations
15.
Walls, Alexandra C., Xiaoli Xiong, Young‐Jun Park, et al.. (2019). Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion. Cell. 176(5). 1026–1039.e15. 370 indexed citations breakdown →
16.
Snijder, Joost, Jan M. Schuller, Anika Wiegard, et al.. (2017). Structures of the cyanobacterial circadian oscillator frozen in a fully assembled state. Science. 355(6330). 1181–1184. 76 indexed citations
17.
Waterbeemd, Michiel van de, Aida Llauró, Joost Snijder, et al.. (2017). Structural Analysis of a Temperature-Induced Transition in a Viral Capsid Probed by HDX-MS. Biophysical Journal. 112(6). 1157–1165. 27 indexed citations
18.
Walls, Alexandra C., M. Alejandra Tortorici, Brandon Frenz, et al.. (2016). Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy. Nature Structural & Molecular Biology. 23(10). 899–905. 306 indexed citations breakdown →
19.
Luque, Daniel, Andrés de la Escosura, Joost Snijder, et al.. (2013). Self-assembly and characterization of small and monodisperse dye nanospheres in a protein cage. Chemical Science. 5(2). 575–581. 49 indexed citations
20.
Veesler, David, Reza Khayat, Srinath Krishnamurthy, et al.. (2013). Architecture of a dsDNA Viral Capsid in Complex with Its Maturation Protease. Structure. 22(2). 230–237. 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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