Kathleen Aertgeerts

3.2k total citations · 1 hit paper
31 papers, 2.3k citations indexed

About

Kathleen Aertgeerts is a scholar working on Molecular Biology, Oncology and Cancer Research. According to data from OpenAlex, Kathleen Aertgeerts has authored 31 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 10 papers in Oncology and 10 papers in Cancer Research. Recurrent topics in Kathleen Aertgeerts's work include Protease and Inhibitor Mechanisms (10 papers), Neuropeptides and Animal Physiology (9 papers) and Blood Coagulation and Thrombosis Mechanisms (8 papers). Kathleen Aertgeerts is often cited by papers focused on Protease and Inhibitor Mechanisms (10 papers), Neuropeptides and Animal Physiology (9 papers) and Blood Coagulation and Thrombosis Mechanisms (8 papers). Kathleen Aertgeerts collaborates with scholars based in United States, Japan and Belgium. Kathleen Aertgeerts's co-authors include David J. Loskutoff, Ralf‐Peter Czekay, Andy Jennings, Jason K. Yano, Scott A. Curriden, R.J. Skene, G. Snell, Bi‐Ching Sang, Paul Declerck and Mike Tennant and has published in prestigious journals such as Nature, Journal of Biological Chemistry and The Journal of Cell Biology.

In The Last Decade

Kathleen Aertgeerts

31 papers receiving 2.3k citations

Hit Papers

Pharmacology and Mechanism of Action of Suzetrigine, a Po... 2025 2026 2025 10 20 30 40

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kathleen Aertgeerts United States 19 1.1k 833 583 410 375 31 2.3k
Athanasios Yiotakis Greece 34 1.7k 1.5× 1.3k 1.5× 857 1.5× 217 0.5× 105 0.3× 74 3.1k
Liguang Lou China 36 1.9k 1.7× 1.5k 1.8× 307 0.5× 206 0.5× 90 0.2× 135 4.0k
Harshani R. Lawrence United States 35 2.1k 1.9× 1.3k 1.5× 283 0.5× 54 0.1× 272 0.7× 75 3.5k
Juan C. Jaén United States 32 1.2k 1.1× 809 1.0× 100 0.2× 256 0.6× 120 0.3× 102 3.4k
Michelle A. Blaskovich United States 27 1.9k 1.7× 1.4k 1.7× 360 0.6× 67 0.2× 89 0.2× 44 3.3k
Haiching Ma United States 23 1.7k 1.5× 406 0.5× 140 0.2× 73 0.2× 552 1.5× 37 3.0k
Yoshihiro Sowa Japan 30 2.9k 2.6× 968 1.2× 440 0.8× 150 0.4× 62 0.2× 88 3.7k
Anthony Tumber United Kingdom 32 2.9k 2.5× 584 0.7× 676 1.2× 64 0.2× 80 0.2× 95 3.6k
Markus D. Siegelin United States 39 2.7k 2.4× 786 0.9× 1.0k 1.7× 107 0.3× 132 0.4× 109 4.1k
Masami Kusaka Japan 25 1.1k 1.0× 426 0.5× 488 0.8× 105 0.3× 431 1.1× 47 2.2k

Countries citing papers authored by Kathleen Aertgeerts

Since Specialization
Citations

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

Fields of papers citing papers by Kathleen Aertgeerts

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kathleen Aertgeerts

This figure shows the co-authorship network connecting the top 25 collaborators of Kathleen Aertgeerts. A scholar is included among the top collaborators of Kathleen Aertgeerts 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 Kathleen Aertgeerts. Kathleen Aertgeerts 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.
Osteen, Jeremiah D., et al.. (2025). Pharmacology and Mechanism of Action of Suzetrigine, a Potent and Selective NaV1.8 Pain Signal Inhibitor for the Treatment of Moderate to Severe Pain. Pain and Therapy. 14(2). 655–674. 44 indexed citations breakdown →
2.
Aertgeerts, Kathleen, et al.. (2022). Optimization of Recombinant GPCR Proteins for Biophysical and Structural Studies Using Virus-like Particles. Methods in molecular biology. 2507. 327–336. 2 indexed citations
3.
Scott, Trevor P., Yingzhuo Yan, Ali Tabatabaei, et al.. (2019). Target Engagement of a Phosphodiesterase 2A Inhibitor Affecting Long-Term Memory in the Rat. Journal of Pharmacology and Experimental Therapeutics. 370(3). 399–407. 8 indexed citations
4.
Nguyen, Jasmine, Juping Liu, Paweł Stańczak, et al.. (2017). Method for rapid optimization of recombinant GPCR protein expression and stability using virus-like particles. Protein Expression and Purification. 133. 41–49. 10 indexed citations
5.
Nguyen, Jasmine, Juping Liu, Paweł Stańczak, et al.. (2017). Dataset on Galanin Receptor 3 mutants that improve recombinant receptor expression and stability in an agonist and antagonist bound form. Data in Brief. 12. 603–607. 2 indexed citations
6.
Srivastava, Ankita, Jason K. Yano, Yoshihiko Hirozane, et al.. (2014). High-resolution structure of the human GPR40 receptor bound to allosteric agonist TAK-875. Nature. 513(7516). 124–127. 288 indexed citations
7.
Okaniwa, Masanori, Masaaki Hirose, Takeo Arita, et al.. (2013). Discovery of a Selective Kinase Inhibitor (TAK-632) Targeting Pan-RAF Inhibition: Design, Synthesis, and Biological Evaluation of C-7-Substituted 1,3-Benzothiazole Derivatives. Journal of Medicinal Chemistry. 56(16). 6478–6494. 90 indexed citations
8.
Ishikawa, Tomoyasu, Masaki Seto, Hiroshi Banno, et al.. (2011). Design and Synthesis of Novel Human Epidermal Growth Factor Receptor 2 (HER2)/Epidermal Growth Factor Receptor (EGFR) Dual Inhibitors Bearing a Pyrrolo[3,2-d]pyrimidine Scaffold. Journal of Medicinal Chemistry. 54(23). 8030–8050. 180 indexed citations
9.
Maezaki, Hironobu, Yasufumi Miyamoto, Tomoko Asakawa, et al.. (2011). Discovery of potent, selective, and orally bioavailable quinoline-based dipeptidyl peptidase IV inhibitors targeting Lys554. Bioorganic & Medicinal Chemistry. 19(15). 4482–4498. 28 indexed citations
10.
Aertgeerts, Kathleen, R.J. Skene, Jason K. Yano, et al.. (2011). Structural Analysis of the Mechanism of Inhibition and Allosteric Activation of the Kinase Domain of HER2 Protein. Journal of Biological Chemistry. 286(21). 18756–18765. 310 indexed citations
11.
Miyamoto, Yasufumi, Takashi Yamashita, Tatsuhiko Fujimoto, et al.. (2010). Design and synthesis of 3-pyridylacetamide derivatives as dipeptidyl peptidase IV (DPP-4) inhibitors targeting a bidentate interaction with Arg125. Bioorganic & Medicinal Chemistry. 19(1). 172–185. 23 indexed citations
12.
Aertgeerts, Kathleen, Irena Levin, Lihong Shi, et al.. (2005). Structural and Kinetic Analysis of the Substrate Specificity of Human Fibroblast Activation Protein α. Journal of Biological Chemistry. 280(20). 19441–19444. 229 indexed citations
13.
Aertgeerts, Kathleen, Sheng Ye, Mike Tennant, et al.. (2004). Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation. Protein Science. 13(2). 412–421. 162 indexed citations
14.
Degryse, Bernard, Jaap G. Neels, Ralf‐Peter Czekay, et al.. (2004). The Low Density Lipoprotein Receptor-related Protein Is a Motogenic Receptor for Plasminogen Activator Inhibitor-1. Journal of Biological Chemistry. 279(21). 22595–22604. 168 indexed citations
15.
Hosfield, David J., Yiqin Wu, R.J. Skene, et al.. (2004). Conformational Flexibility in Crystal Structures of Human 11β-Hydroxysteroid Dehydrogenase Type I Provide Insights into Glucocorticoid Interconversion and Enzyme Regulation. Journal of Biological Chemistry. 280(6). 4639–4648. 93 indexed citations
16.
Rabijns, Anja, Kathleen Aertgeerts, Isabelle Knockaert, et al.. (1999). Plasminogen activator inhibitor 1 (PAI-1) in its active conformation: crystallization and preliminary X-ray diffraction data. Acta Crystallographica Section D Biological Crystallography. 55(2). 574–576. 4 indexed citations
17.
Gils, Ann, Jie Lu, Kathleen Aertgeerts, Isabelle Knockaert, & Paul Declerck. (1997). Identification of positively charged residues contributing to the stability of plasminogen activator inhibitor 1. FEBS Letters. 415(2). 192–195. 19 indexed citations
18.
Aertgeerts, Kathleen, et al.. (1995). Crystal-structure of a cleaved variant of human plasminogen-activator inhibitor-1. Thrombosis and Haemostasis. 73(6). 1006–1006. 3 indexed citations
19.
Aertgeerts, Kathleen, et al.. (1995). Crystallization and X‐ray diffraction data of the cleaved form of plasminogen activator inhibitor‐1. Proteins Structure Function and Bioinformatics. 23(1). 118–121. 16 indexed citations
20.
Aertgeerts, Kathleen, Hendrik L. De Bondt, C. J. De Ranter, & Paul Declerck. (1995). Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1. Nature Structural Biology. 2(10). 891–897. 96 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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