Ulf J. Nilsson

11.5k total citations
236 papers, 8.3k citations indexed

About

Ulf J. Nilsson is a scholar working on Molecular Biology, Immunology and Organic Chemistry. According to data from OpenAlex, Ulf J. Nilsson has authored 236 papers receiving a total of 8.3k indexed citations (citations by other indexed papers that have themselves been cited), including 153 papers in Molecular Biology, 122 papers in Immunology and 52 papers in Organic Chemistry. Recurrent topics in Ulf J. Nilsson's work include Galectins and Cancer Biology (118 papers), Glycosylation and Glycoproteins Research (100 papers) and Carbohydrate Chemistry and Synthesis (48 papers). Ulf J. Nilsson is often cited by papers focused on Galectins and Cancer Biology (118 papers), Glycosylation and Glycoproteins Research (100 papers) and Carbohydrate Chemistry and Synthesis (48 papers). Ulf J. Nilsson collaborates with scholars based in Sweden, United States and United Kingdom. Ulf J. Nilsson's co-authors include Hakon Leffler, Anders Sundin, Ola Karnland, Ian Cumpstey, Pernilla Sörme, Siv Olsson, Christopher T. Öberg, Barbro Kahl‐Knutsson, Emma Salomonsson and Johan Billing and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Ulf J. Nilsson

233 papers receiving 8.1k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Ulf J. Nilsson Sweden	52	4.9k	4.0k	1.4k	1.2k	493	236	8.3k
Yasuo Tanaka Japan	48	2.8k 0.6×	1.2k 0.3×	2.5k 1.8×	1.2k 0.9×	200 0.4×	295	9.5k
Yongjun Liu China	51	2.2k 0.4×	1.5k 0.4×	835 0.6×	484 0.4×	99 0.2×	503	9.8k
Mei Zhang China	54	2.6k 0.5×	868 0.2×	804 0.6×	1.8k 1.4×	444 0.9×	343	10.8k
Jinfeng Liu China	48	7.5k 1.5×	1.8k 0.5×	211 0.1×	1.1k 0.9×	157 0.3×	202	10.4k
Yan Liu China	55	4.3k 0.9×	621 0.2×	443 0.3×	954 0.8×	273 0.6×	400	11.4k
Hiroyuki Saito Japan	45	4.2k 0.9×	725 0.2×	429 0.3×	699 0.6×	246 0.5×	384	8.1k
Juanjuan Liu China	39	2.8k 0.6×	652 0.2×	328 0.2×	539 0.4×	413 0.8×	375	6.3k
Junru Wang China	38	2.5k 0.5×	375 0.1×	538 0.4×	485 0.4×	233 0.5×	236	6.1k
Tae Sung Kim South Korea	50	3.2k 0.6×	1.8k 0.4×	372 0.3×	1.3k 1.0×	123 0.2×	309	8.3k
S. Ramaswamy United States	46	4.6k 0.9×	432 0.1×	684 0.5×	701 0.6×	163 0.3×	264	8.7k

Countries citing papers authored by Ulf J. Nilsson

Since Specialization

Citations

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

Fields of papers citing papers by Ulf J. Nilsson

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ulf J. Nilsson

This figure shows the co-authorship network connecting the top 25 collaborators of Ulf J. Nilsson. A scholar is included among the top collaborators of Ulf J. Nilsson 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 Ulf J. Nilsson. Ulf J. Nilsson 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

Tomašič, Tihomir, Jurij Lah, Anders Sundin, et al.. (2025). Nanomolar inhibitor of the galectin-8 N-terminal domain binds via a non-canonical cation-π interaction. Communications Chemistry. 8(1). 59–59. 1 indexed citations

MacKinnon, Alison C., Duncan C. Humphries, James A. Roper, et al.. (2024). Effect of GB1107, a novel galectin-3 inhibitor on pro-fibrotic signalling in the liver. European Journal of Pharmacology. 985. 177077–177077. 4 indexed citations

Yoshida, Akari, Masaki Magari, Naoya Hatano, et al.. (2024). Development of a novel AAK1 inhibitor via Kinobeads-based screening. Scientific Reports. 14(1). 6723–6723. 1 indexed citations

Håkansson, M., Richard Johnsson, Žiga Jakopin, et al.. (2024). Galectin-8N-Selective 4-Halophenylphthalazinone-Galactals Double π-Stack in a Unique Pocket. ACS Medicinal Chemistry Letters. 15(8). 1319–1324. 2 indexed citations

Cao, Zhiyi, Fredrik R. Zetterberg, Ulf J. Nilsson, et al.. (2023). Galectin-8 Downmodulates TLR4 Activation and Impairs Bacterial Clearance in a Mouse Model of Pseudomonas aeruginosa Keratitis. The Journal of Immunology. 210(4). 398–407. 1 indexed citations

Jakopin, Žiga, et al.. (2022). Design and synthesis of novel 3-triazolyl-1-thiogalactosides as galectin-1, -3 and -8 inhibitors. RSC Advances. 12(29). 18973–18984. 6 indexed citations

Sundin, Anders, Žiga Jakopin, Marko Anderluh, et al.. (2021). Selective Galectin‐8N Ligands: The Design and Synthesis of Phthalazinone‐d‐Galactals. ChemMedChem. 17(6). e202100575–e202100575. 6 indexed citations

Ignjatović, Majda Misini, Octav Caldararu, Kristoffer Peterson, et al.. (2021). Entropy–Entropy Compensation between the Protein, Ligand, and Solvent Degrees of Freedom Fine-Tunes Affinity in Ligand Binding to Galectin-3C. SHILAP Revista de lepidopterología. 1(4). 484–500. 28 indexed citations

Tomašič, Tihomir, Žiga Jakopin, Hakon Leffler, et al.. (2021). Selective Monovalent Galectin‐8 Ligands Based on 3‐Lactoylgalactoside. ChemMedChem. 17(3). e202100514–e202100514. 7 indexed citations

10.

Sundin, Anders, M. Håkansson, Hakon Leffler, et al.. (2021). Structure-Guided Design of d-Galactal Derivatives with High Affinity and Selectivity for the Galectin-8 N-Terminal Domain. ACS Medicinal Chemistry Letters. 12(11). 1745–1752. 10 indexed citations

11.

Stenström, Olof, Carl Diehl, Kristofer Modig, Ulf J. Nilsson, & Mikael Akke. (2020). Mapping the energy landscape of protein–ligand binding via linear free energy relationships determined by protein NMR relaxation dispersion. RSC Chemical Biology. 2(1). 259–265. 8 indexed citations

12.

Kulcsár, A, et al.. (2020). Coupling of N-tosylhydrazones with tetrazoles: synthesis of 2-β-d-glycopyranosylmethyl-5-substituted-2H-tetrazole type glycomimetics. Organic & Biomolecular Chemistry. 19(3). 605–618. 3 indexed citations

13.

Vuong, Lynda, Claire Rooney, Brian J. McHugh, et al.. (2019). An Orally Active Galectin-3 Antagonist Inhibits Lung Adenocarcinoma Growth and Augments Response to PD-L1 Blockade. Cancer Research. 79(7). 1480–1492. 104 indexed citations

14.

Bratteby, Klas, Kristoffer Peterson, Vladimir Shalgunov, et al.. (2019). In Vivo Veritas: ¹⁸F-Radiolabeled Glycomimetics Allow Insights into the Pharmacological Fate of Galectin-3 Inhibitors. Journal of Medicinal Chemistry. 63(2). 747–755. 20 indexed citations

15.

Bojić‐Trbojević, Žanka, Milica Jovanović Krivokuća, Aleksandra Vilotić, et al.. (2019). Human trophoblast requires galectin-3 for cell migration and invasion. Scientific Reports. 9(1). 2136–2136. 29 indexed citations

16.

Stenström, Olof, Majda Misini Ignjatović, Octav Caldararu, et al.. (2019). Interplay between Conformational Entropy and Solvation Entropy in Protein–Ligand Binding. Journal of the American Chemical Society. 141(5). 2012–2026. 102 indexed citations

17.

Peterson, Kristoffer, Olof Stenström, Priya Ranjan Prasad Verma, et al.. (2017). Systematic Tuning of Fluoro-galectin-3 Interactions Provides Thiodigalactoside Derivatives with Single-Digit nM Affinity and High Selectivity. Journal of Medicinal Chemistry. 61(3). 1164–1175. 84 indexed citations

18.

Saraboji, K., Janina Sprenger, Ulf J. Nilsson, et al.. (2016). Perdeuteration, crystallization, data collection and comparison of five neutron diffraction data sets of complexes of human galectin-3C. Acta Crystallographica Section D Structural Biology. 72(11). 1194–1202. 15 indexed citations

19.

Delaine, Tamara, P.M. Collins, Alison C. MacKinnon, et al.. (2016). Galectin‐3‐Binding Glycomimetics that Strongly Reduce Bleomycin‐Induced Lung Fibrosis and Modulate Intracellular Glycan Recognition. ChemBioChem. 17(18). 1759–1770. 151 indexed citations

20.

Lin, Chi‐Iou, Edward E. Whang, David B. Donner, et al.. (2009). Galectin-3 Targeted Therapy with a Small Molecule Inhibitor Activates Apoptosis and Enhances Both Chemosensitivity and Radiosensitivity in Papillary Thyroid Cancer. Molecular Cancer Research. 7(10). 1655–1662. 55 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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