J.S. Kastrup

5.2k total citations
140 papers, 3.9k citations indexed

About

J.S. Kastrup is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Spectroscopy. According to data from OpenAlex, J.S. Kastrup has authored 140 papers receiving a total of 3.9k indexed citations (citations by other indexed papers that have themselves been cited), including 107 papers in Molecular Biology, 61 papers in Cellular and Molecular Neuroscience and 21 papers in Spectroscopy. Recurrent topics in J.S. Kastrup's work include Neuroscience and Neuropharmacology Research (58 papers), Receptor Mechanisms and Signaling (28 papers) and Molecular Sensors and Ion Detection (20 papers). J.S. Kastrup is often cited by papers focused on Neuroscience and Neuropharmacology Research (58 papers), Receptor Mechanisms and Signaling (28 papers) and Molecular Sensors and Ion Detection (20 papers). J.S. Kastrup collaborates with scholars based in Denmark, United States and Belgium. J.S. Kastrup's co-authors include Michael Gajhede, Karla Frydenvang, Darryl S. Pickering, Jan Egebjerg, Bente Vestergaard, Ingrid Kjøller Larsen, Tommy Liljefors, Lars K. Skov, Peter Naur and Thomas Balle 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

J.S. Kastrup

139 papers receiving 3.9k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
J.S. Kastrup Denmark	38	2.8k	1.4k	510	429	328	140	3.9k
Moriz Mayer Austria	19	3.1k 1.1×	1.2k 0.8×	604 1.2×	503 1.2×	389 1.2×	42	4.3k
Dale F. Mierke United States	40	3.8k 1.3×	1.3k 0.9×	859 1.7×	557 1.3×	224 0.7×	180	5.1k
Juan Llopis Spain	29	5.3k 1.9×	1.5k 1.0×	559 1.1×	436 1.0×	427 1.3×	69	7.9k
Henning Thøgersen Denmark	25	2.3k 0.8×	1.3k 0.9×	455 0.9×	255 0.6×	207 0.6×	49	3.7k
Craig A. Behnke United States	19	5.8k 2.1×	3.4k 2.3×	347 0.7×	284 0.7×	180 0.5×	26	6.8k
Andrei L. Lomize United States	28	4.0k 1.4×	1.1k 0.8×	201 0.4×	429 1.0×	238 0.7×	63	4.9k
Keitaro Yamashita Japan	34	2.8k 1.0×	821 0.6×	239 0.5×	192 0.4×	989 3.0×	102	4.5k
Seok‐Yong Lee United States	38	2.8k 1.0×	862 0.6×	215 0.4×	156 0.4×	187 0.6×	65	4.2k
Delia Picone Italy	31	2.4k 0.8×	825 0.6×	218 0.4×	249 0.6×	294 0.9×	115	3.6k
Piero Andrea Temussi Italy	41	4.3k 1.5×	1.5k 1.0×	438 0.9×	647 1.5×	861 2.6×	214	6.5k

Countries citing papers authored by J.S. Kastrup

Since Specialization

Citations

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

Fields of papers citing papers by J.S. Kastrup

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of J.S. Kastrup

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

All Works

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20 of 20 papers shown

Thorsen, Thor S., Yashraj Kulkarni, David A. Sykes, et al.. (2025). Structural basis of THC analog activity at the Cannabinoid 1 receptor. Nature Communications. 16(1). 486–486. 5 indexed citations

Pickering, Darryl S., Karla Frydenvang, Pierre Francotte, et al.. (2024). Crystal structure of the GluK1 ligand-binding domain with kainate and the full-spanning positive allosteric modulator BPAM538. Journal of Structural Biology. 216(3). 108113–108113. 3 indexed citations

Venskutonytė, Raminta, Thor S. Thorsen, Maria Musgaard, et al.. (2023). Small‐molecule positive allosteric modulation of homomeric kainate receptors GluK1 ‐3: development of screening assays and insight into GluK3 structure. FEBS Journal. 291(7). 1506–1529. 5 indexed citations

Laulumaa, Saara, et al.. (2022). Differences between the GluD1 and GluD2 receptors revealed by GluD1 X‐ray crystallography, binding studies and molecular dynamics. FEBS Journal. 290(15). 3781–3801. 10 indexed citations

Hansen, R, Birgitte Nielsen, Ana V. Paternain, et al.. (2019). N-(7-(1H-Imidazol-1-yl)-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl)benzamide, a New Kainate Receptor Selective Antagonist and Analgesic: Synthesis, X-ray Crystallography, Structure–Affinity Relationships, and in Vitro and in Vivo Pharmacology. ACS Chemical Neuroscience. 10(11). 4685–4695. 6 indexed citations

Brogi, Simone, Margherita Brindisi, Stefania Butini, et al.. (2018). (S)-2-Amino-3-(5-methyl-3-hydroxyisoxazol-4-yl)propanoic Acid (AMPA) and Kainate Receptor Ligands: Further Exploration of Bioisosteric Replacements and Structural and Biological Investigation. Journal of Medicinal Chemistry. 61(5). 2124–2130. 17 indexed citations

Kristensen, O., et al.. (2016). The Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate. Structure. 24(9). 1582–1589. 9 indexed citations

Frydenvang, Karla, et al.. (2016). Lessons from crystal structures of kainate receptors. Neuropharmacology. 112(Pt A). 16–28. 42 indexed citations

Kastrup, J.S., et al.. (2016). A pharmacological profile of the high-affinity GluK5 kainate receptor. European Journal of Pharmacology. 788. 315–320. 6 indexed citations

10.

Shahsavar, Azadeh, Philip K. Ahring, Christian Krintel, et al.. (2015). Acetylcholine-binding protein engineered to mimic the alpha4- alpha 4 binding pocket in alpha 4beta2 nicotinic acetylcholine receptors reveals interface specific interactions important for binding and activity. Molecular Pharmacology. 88(4). 697–707. 1 indexed citations

11.

Demmer, Charles S., Charlotte Møller, Patricia M.G.E. Brown, et al.. (2015). Binding Mode of an α-Amino Acid-Linked Quinoxaline-2,3-dione Analogue at Glutamate Receptor Subtype GluK1. ACS Chemical Neuroscience. 6(6). 845–854. 16 indexed citations

12.

Venskutonytė, Raminta, Karla Frydenvang, Michael Gajhede, et al.. (2014). Molecular Recognition of Two 2,4‐syn‐Functionalized (S)‐Glutamate Analogues by the Kainate Receptor GluK3 Ligand Binding Domain. ChemMedChem. 9(10). 2254–2259. 9 indexed citations

13.

Venskutonytė, Raminta, Karla Frydenvang, Ewa Szymańska, et al.. (2012). Structural and Pharmacological Characterization of Phenylalanine‐Based AMPA Receptor Antagonists at Kainate Receptors. ChemMedChem. 7(10). 1793–1798. 12 indexed citations

14.

Venskutonytė, Raminta, Sophie Faure, Thierry Gefflaut, et al.. (2012). Pharmacological and structural characterization of conformationally restricted (S)-glutamate analogues at ionotropic glutamate receptors. Journal of Structural Biology. 180(1). 39–46. 12 indexed citations

15.

Venskutonytė, Raminta, Karla Frydenvang, Michael Gajhede, et al.. (2011). Binding site and interlobe interactions of the ionotropic glutamate receptor GluK3 ligand binding domain revealed by high resolution crystal structure in complex with (S)-glutamate. Journal of Structural Biology. 176(3). 307–314. 20 indexed citations

16.

Venskutonytė, Raminta, Stefania Butini, Salvatore Sanna Coccone, et al.. (2011). Selective Kainate Receptor (GluK1) Ligands Structurally Based upon 1H-Cyclopentapyrimidin-2,4(1H,3H)-dione: Synthesis, Molecular Modeling, and Pharmacological and Biostructural Characterization. Journal of Medicinal Chemistry. 54(13). 4793–4805. 18 indexed citations

17.

Frydenvang, Karla, L. Leanne Lash, Peter Naur, et al.. (2009). Full Domain Closure of the Ligand-binding Core of the Ionotropic Glutamate Receptor iGluR5 Induced by the High Affinity Agonist Dysiherbaine and the Functional Antagonist 8,9-Dideoxyneodysiherbaine. Journal of Biological Chemistry. 284(21). 14219–14229. 48 indexed citations

18.

Clausen, Rasmus P., Peter Naur, Anders S. Kristensen, et al.. (2009). The Glutamate Receptor GluR5 Agonist (S)-2-Amino-3-(3-hydroxy-7,8-dihydro-6H-cyclohepta[d]isoxazol-4-yl)propionic Acid and the 8-Methyl Analogue: Synthesis, Molecular Pharmacology, and Biostructural Characterization†PDB ID: 2WKY.. Journal of Medicinal Chemistry. 52(15). 4911–4922. 20 indexed citations

19.

Harpsøe, Kasper, J.S. Kastrup, Darryl S. Pickering, et al.. (2007). Structural Proof of a Dimeric Positive Modulator Bridging Two Identical AMPA Receptor-Binding Sites. Chemistry & Biology. 14(11). 1294–1303. 52 indexed citations

20.

Naur, Peter, Bente Vestergaard, Lars K. Skov, et al.. (2005). Crystal structure of the kainate receptor GluR5 ligand‐binding core in complex with (S)‐glutamate. FEBS Letters. 579(5). 1154–1160. 77 indexed citations

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