S. Leysen

1.1k total citations
25 papers, 636 citations indexed

About

S. Leysen is a scholar working on Molecular Biology, Pharmacology and Genetics. According to data from OpenAlex, S. Leysen has authored 25 papers receiving a total of 636 indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 8 papers in Pharmacology and 7 papers in Genetics. Recurrent topics in S. Leysen's work include Ubiquitin and proteasome pathways (12 papers), 14-3-3 protein interactions (12 papers) and Microbial Natural Products and Biosynthesis (7 papers). S. Leysen is often cited by papers focused on Ubiquitin and proteasome pathways (12 papers), 14-3-3 protein interactions (12 papers) and Microbial Natural Products and Biosynthesis (7 papers). S. Leysen collaborates with scholars based in Netherlands, United Kingdom and Belgium. S. Leysen's co-authors include Christian Ottmann, Luc Brunsveld, Chris W. Michiels, Lise Vanderkelen, Joris M. Van Herreweghe, L. Callewaert, L.‐G. Milroy, Eline Sijbesma, Sergei V. Strelkov and Femke A. Meijer and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

S. Leysen

24 papers receiving 626 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
S. Leysen Netherlands 13 474 135 79 64 61 25 636
Christine E. Hajdin United States 10 1.1k 2.3× 50 0.4× 67 0.8× 50 0.8× 47 0.8× 10 1.3k
Ellene H. Mashalidis United States 10 380 0.8× 62 0.5× 94 1.2× 49 0.8× 32 0.5× 13 531
Simon A. Weston United Kingdom 7 601 1.3× 65 0.5× 87 1.1× 84 1.3× 60 1.0× 8 761
Jing Hou China 13 412 0.9× 135 1.0× 92 1.2× 72 1.1× 53 0.9× 23 637
Jerry M. Troutman United States 14 482 1.0× 34 0.3× 146 1.8× 79 1.2× 43 0.7× 31 647
Antonietta M. Lillo United States 11 454 1.0× 114 0.8× 35 0.4× 61 1.0× 52 0.9× 24 616
Sandra Lightle United States 10 279 0.6× 37 0.3× 96 1.2× 75 1.2× 41 0.7× 10 469
Jacob Lesniak United States 7 353 0.7× 75 0.6× 102 1.3× 60 0.9× 37 0.6× 8 555
M. Blaesse Germany 9 443 0.9× 54 0.4× 45 0.6× 75 1.2× 74 1.2× 12 546
G. Malojcic Switzerland 15 393 0.8× 27 0.2× 84 1.1× 55 0.9× 73 1.2× 18 673

Countries citing papers authored by S. Leysen

Since Specialization
Citations

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

Fields of papers citing papers by S. Leysen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of S. Leysen

This figure shows the co-authorship network connecting the top 25 collaborators of S. Leysen. A scholar is included among the top collaborators of S. Leysen 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 S. Leysen. S. Leysen 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.
2.
Sijbesma, Eline, S. Leysen, Peter J. Cossar, et al.. (2023). Molecular basis and dual ligand regulation of tetrameric estrogen receptor α/14-3-3ζ protein complex. Journal of Biological Chemistry. 299(7). 104855–104855. 11 indexed citations
3.
Leysen, S., et al.. (2022). Molecular glues to stabilise protein–protein interactions. Current Opinion in Chemical Biology. 69. 102169–102169. 28 indexed citations
4.
Leysen, S., Rebecca J. Burnley, Elizabeth Rodríguez, et al.. (2021). A Structural Study of the Cytoplasmic Chaperone Effect of 14-3-3 Proteins on Ataxin-1. Journal of Molecular Biology. 433(19). 167174–167174. 8 indexed citations
5.
Leysen, S., et al.. (2021). The identification and structural analysis of potential 14-3-3 interaction sites on the bone regulator protein Schnurri-3. Acta Crystallographica Section F Structural Biology Communications. 77(8). 254–261. 1 indexed citations
6.
7.
Leysen, S., et al.. (2020). A biophysical and structural analysis of the interaction of BLNK with 14-3-3 proteins. Journal of Structural Biology. 212(3). 107662–107662. 10 indexed citations
8.
Sijbesma, Eline, Kenneth K. Hallenbeck, S. Leysen, et al.. (2019). Site-Directed Fragment-Based Screening for the Discovery of Protein–Protein Interaction Stabilizers. Journal of the American Chemical Society. 141(8). 3524–3531. 79 indexed citations
9.
Meijer, Femke A., Richard G. Doveston, S. Leysen, et al.. (2019). Ligand-Based Design of Allosteric Retinoic Acid Receptor-Related Orphan Receptor γt (RORγt) Inverse Agonists. Journal of Medicinal Chemistry. 63(1). 241–259. 30 indexed citations
10.
Sijbesma, Eline, Lukasz Skóra, S. Leysen, et al.. (2017). Identification of Two Secondary Ligand Binding Sites in 14-3-3 Proteins Using Fragment Screening. Biochemistry. 56(30). 3972–3982. 37 indexed citations
11.
Scheepstra, Marcel, Sebastian A. Andrei, Anna K. H. Hirsch, et al.. (2017). Designed Spiroketal Protein Modulation. Angewandte Chemie International Edition. 56(20). 5480–5484. 12 indexed citations
12.
Stevers, Loes M., S. Leysen, Femke A. Meijer, et al.. (2016). Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. Proceedings of the National Academy of Sciences. 113(9). E1152–61. 117 indexed citations
13.
Leysen, S., Joris M. Van Herreweghe, Kazunari Yoneda, et al.. (2015). The structure of the proteinaceous inhibitor PliI fromAeromonas hydrophilain complex with its target lysozyme. Acta Crystallographica Section D Biological Crystallography. 71(2). 344–351. 7 indexed citations
14.
Milroy, L.‐G., Maria Bartel, Morkos A. Henen, et al.. (2015). Stabilizer‐Guided Inhibition of Protein–Protein Interactions. Angewandte Chemie International Edition. 54(52). 15720–15724. 55 indexed citations
15.
Milroy, L.‐G., Maria Bartel, Morkos A. Henen, et al.. (2015). Stabilizer‐Guided Inhibition of Protein–Protein Interactions. Angewandte Chemie. 127(52). 15946–15950. 10 indexed citations
16.
Scheepstra, Marcel, Lidia Nieto, Anna K. H. Hirsch, et al.. (2014). A Natural‐Product Switch for a Dynamic Protein Interface. Angewandte Chemie International Edition. 53(25). 6443–6448. 29 indexed citations
17.
Leysen, S., et al.. (2012). Structural characterization of the PliG lysozyme inhibitor family. Journal of Structural Biology. 180(1). 235–242. 12 indexed citations
18.
Leysen, S., Lise Vanderkelen, S.D. Weeks, Chris W. Michiels, & Sergei V. Strelkov. (2012). Structural basis of bacterial defense against g-type lysozyme-based innate immunity. Cellular and Molecular Life Sciences. 70(6). 1113–1122. 24 indexed citations
19.
Callewaert, L., Joris M. Van Herreweghe, Lise Vanderkelen, et al.. (2012). Guards of the great wall: bacterial lysozyme inhibitors. Trends in Microbiology. 20(10). 501–510. 75 indexed citations
20.
Leysen, S., et al.. (2010). Molecular Basis of Bacterial Defense against Host Lysozymes: X-ray Structures of Periplasmic Lysozyme Inhibitors PliI and PliC. Journal of Molecular Biology. 405(5). 1233–1245. 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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