N.S. Laursen

3.1k total citations
33 papers, 1.0k citations indexed

About

N.S. Laursen is a scholar working on Immunology, Radiology, Nuclear Medicine and Imaging and Molecular Biology. According to data from OpenAlex, N.S. Laursen has authored 33 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Immunology, 16 papers in Radiology, Nuclear Medicine and Imaging and 9 papers in Molecular Biology. Recurrent topics in N.S. Laursen's work include Complement system in diseases (19 papers), Monoclonal and Polyclonal Antibodies Research (16 papers) and Blood groups and transfusion (6 papers). N.S. Laursen is often cited by papers focused on Complement system in diseases (19 papers), Monoclonal and Polyclonal Antibodies Research (16 papers) and Blood groups and transfusion (6 papers). N.S. Laursen collaborates with scholars based in Denmark, United States and Germany. N.S. Laursen's co-authors include G.R. Andersen, Ian A. Wilson, Lars Sottrup‐Jensen, Steffen Thiel, Rasmus K. Jensen, Kasper R. Andersen, Edzard Spillner, Folmer Fredslund, R.T. Kidmose and Péter Gál and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

N.S. Laursen

32 papers receiving 1.0k citations

Peers

N.S. Laursen
Bo Zheng United States
Joseph J. E. Caesar United Kingdom
Gabriela Canziani United States
Bo Zheng United States
N.S. Laursen
Citations per year, relative to N.S. Laursen N.S. Laursen (= 1×) peers Bo Zheng

Countries citing papers authored by N.S. Laursen

Since Specialization
Citations

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

Fields of papers citing papers by N.S. Laursen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of N.S. Laursen

This figure shows the co-authorship network connecting the top 25 collaborators of N.S. Laursen. A scholar is included among the top collaborators of N.S. Laursen 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 N.S. Laursen. N.S. Laursen 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.
Bennike, Tue Bjerg, Gunna Christiansen, Jeppe Emmersen, et al.. (2025). Differences in complement activation of serum-resistant and serum-sensitive Klebsiella pneumoniae isolates. Molecular Immunology. 183. 274–285. 1 indexed citations
2.
Sitsel, Oleg, Christina Grønberg, Kasper R. Andersen, et al.. (2024). Transition metal transporting P‐type ATPases : terminal metal‐binding domains serve as sensors for autoinhibitory tails. FEBS Journal. 292(7). 1654–1674. 1 indexed citations
3.
Pedersen, Dennis, et al.. (2023). Nanobody‐mediated complement activation to kill HIV ‐infected cells. EMBO Molecular Medicine. 15(4). e16422–e16422. 10 indexed citations
4.
Pedersen, Dennis, Annette G. Hansen, Steffen Thiel, et al.. (2023). Bispecific Complement Engagers for Targeted Complement Activation. The Journal of Immunology. 211(3). 403–413. 7 indexed citations
5.
Pedersen, Henrik, Rasmus K. Jensen, Annette G. Hansen, et al.. (2022). Structure-Guided Engineering of a Complement Component C3-Binding Nanobody Improves Specificity and Adds Cofactor Activity. Frontiers in Immunology. 13. 872536–872536. 6 indexed citations
6.
Jensen, Rasmus K., et al.. (2022). Structural insights into the function-modulating effects of nanobody binding to the integrin receptor αMβ2. Journal of Biological Chemistry. 298(8). 102168–102168. 7 indexed citations
7.
Pedersen, Henrik, et al.. (2021). Nanobodies Provide Insight into the Molecular Mechanisms of the Complement Cascade and Offer New Therapeutic Strategies. Biomolecules. 11(2). 298–298. 10 indexed citations
8.
Laursen, N.S., et al.. (2021). Purification of Human Complement Component C4 and Sample Preparation for Structural Biology Applications. Methods in molecular biology. 2227. 249–264. 2 indexed citations
9.
Présumey, Jessy, Esra Yalçın, Rachel Fox, et al.. (2020). An Ultrahigh-Affinity Complement C4b-Specific Nanobody Inhibits In Vivo Assembly of the Classical Pathway Proconvertase. The Journal of Immunology. 205(6). 1678–1694. 15 indexed citations
10.
Pedersen, Henrik, Rasmus K. Jensen, Jens Magnus Bernth Jensen, et al.. (2020). A Complement C3–Specific Nanobody for Modulation of the Alternative Cascade Identifies the C-Terminal Domain of C3b as Functional in C5 Convertase Activity. The Journal of Immunology. 205(8). 2287–2300. 12 indexed citations
11.
Pedersen, Henrik, Rasmus K. Jensen, Annette G. Hansen, et al.. (2020). A C3-specific nanobody that blocks all three activation pathways in the human and murine complement system. Journal of Biological Chemistry. 295(26). 8746–8758. 20 indexed citations
12.
Gysel, Kira, Maria Vinther, Artur Muszyński, et al.. (2020). Structural signatures in EPR3 define a unique class of plant carbohydrate receptors. Nature Communications. 11(1). 3797–3797. 31 indexed citations
13.
Pedersen, Dennis, Thies Rösner, Annette G. Hansen, et al.. (2020). Recruitment of properdin by bi-specific nanobodies activates the alternative pathway of complement. Molecular Immunology. 124. 200–210. 10 indexed citations
14.
Pedersen, Dennis, Caroline Thomas, Yong Wang, et al.. (2019). Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System. Frontiers in Immunology. 10. 2007–2007. 50 indexed citations
15.
Grønberg, Christina, et al.. (2018). Isolation and Characterization of Nanobodies against a Zinc-Transporting P-Type ATPase. Antibodies. 7(4). 39–39. 3 indexed citations
16.
Laursen, N.S., et al.. (2017). Introducing site-specific cysteines into nanobodies for mercury labelling allows de novo phasing of their crystal structures. Acta Crystallographica Section D Structural Biology. 73(10). 804–813. 12 indexed citations
17.
Laursen, N.S., Rasmus K. Jensen, Michaela Miehe, et al.. (2017). Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction. Nature Communications. 9(1). 7–7. 107 indexed citations
18.
Laursen, N.S., et al.. (2012). Structure, Function and Control of Complement C5 and its Proteolytic Fragments. Current Molecular Medicine. 12(8). 1083–1097. 29 indexed citations
19.
Laursen, N.S., Kasper R. Andersen, Ingke Braren, et al.. (2011). Substrate recognition by complement convertases revealed in the C5–cobra venom factor complex. The EMBO Journal. 30(3). 606–616. 65 indexed citations
20.
Fredslund, Folmer, N.S. Laursen, Pietro Roversi, et al.. (2008). Structure of and influence of a tick complement inhibitor on human complement component 5. Nature Immunology. 9(7). 753–760. 108 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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