Mette Laursen

1.0k total citations
10 papers, 743 citations indexed

About

Mette Laursen is a scholar working on Molecular Biology, Oncology and Endocrinology, Diabetes and Metabolism. According to data from OpenAlex, Mette Laursen has authored 10 papers receiving a total of 743 indexed citations (citations by other indexed papers that have themselves been cited), including 8 papers in Molecular Biology, 2 papers in Oncology and 2 papers in Endocrinology, Diabetes and Metabolism. Recurrent topics in Mette Laursen's work include Ion Transport and Channel Regulation (6 papers), Ion channel regulation and function (3 papers) and ATP Synthase and ATPases Research (3 papers). Mette Laursen is often cited by papers focused on Ion Transport and Channel Regulation (6 papers), Ion channel regulation and function (3 papers) and ATP Synthase and ATPases Research (3 papers). Mette Laursen collaborates with scholars based in Denmark, United States and South Africa. Mette Laursen's co-authors include Poul Nissen, Natalya U. Fedosova, Laure Yatime, J.L. Gregersen, Jens Preben Morth, Mikael Esmann, Maike Bublitz, Jesper V. Møller, Howard S. Young and Claus Olesen 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

Mette Laursen

9 papers receiving 738 citations

Peers

Mette Laursen
J O Höög Sweden
Adam B. Weinglass United States
William J. Driscoll United States
Patria Danielson United States
Brigitte Simons United States
Tracy I. Stevenson United States
J O Höög Sweden
Mette Laursen
Citations per year, relative to Mette Laursen Mette Laursen (= 1×) peers J O Höög

Countries citing papers authored by Mette Laursen

Since Specialization
Citations

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

Fields of papers citing papers by Mette Laursen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mette Laursen

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

All Works

10 of 10 papers shown
1.
Gysel, Kira, Mette Laursen, Feng Feng, et al.. (2025). The Medicago truncatulaLYR4 intracellular domain serves as a scaffold in immunity signaling independent of its phosphorylation activity. New Phytologist. 246(4). 1423–1431. 1 indexed citations
2.
Malinge, Pauline, Xavier Chauchet, Sébastien Calloud, et al.. (2024). Structural analysis of light chain-driven bispecific antibodies targeting CD47 and PD-L1. mAbs. 16(1). 2362432–2362432.
3.
Wu, Fan, Linlin Yang, Mette Laursen, et al.. (2020). Full-length human GLP-1 receptor structure without orthosteric ligands. Nature Communications. 11(1). 1272–1272. 93 indexed citations
4.
Laursen, Mette, J.L. Gregersen, Laure Yatime, Poul Nissen, & Natalya U. Fedosova. (2015). Structures and characterization of digoxin- and bufalin-bound Na + ,K + -ATPase compared with the ouabain-bound complex. Proceedings of the National Academy of Sciences. 112(6). 1755–1760. 169 indexed citations
5.
Reinhard, Linda, et al.. (2014). Crystals of Na+/K+-ATPase with bound cisplatin. Biochemical Pharmacology. 92(3). 494–498. 18 indexed citations
6.
Laursen, Mette, Herman G.P. Swarts, Anthonius H. J. Engwerda, et al.. (2014). Na+,K+-ATPase Isoform Selectivity for Digitalis-Like Compounds Is Determined by Two Amino Acids in the First Extracellular Loop. Chemical Research in Toxicology. 27(12). 2082–2092. 18 indexed citations
7.
Laursen, Mette, Laure Yatime, Poul Nissen, & Natalya U. Fedosova. (2013). Crystal structure of the high-affinity Na + ,K + -ATPase–ouabain complex with Mg 2+ bound in the cation binding site. Proceedings of the National Academy of Sciences. 110(27). 10958–10963. 208 indexed citations
8.
Yatime, Laure, Mette Laursen, Jens Preben Morth, et al.. (2010). Structural insights into the high affinity binding of cardiotonic steroids to the Na+,K+-ATPase. Journal of Structural Biology. 174(2). 296–306. 135 indexed citations
9.
Laursen, Mette, Maike Bublitz, Karine Moncoq, et al.. (2009). Cyclopiazonic Acid Is Complexed to a Divalent Metal Ion When Bound to the Sarcoplasmic Reticulum Ca2+-ATPase. Journal of Biological Chemistry. 284(20). 13513–13518. 82 indexed citations
10.
Liu, Fengli, et al.. (2008). A tomato ER-type Ca2+-ATPase, LCA1, has a low thapsigargin-sensitivity and can transport manganese. Archives of Biochemistry and Biophysics. 481(2). 157–168. 19 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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