Sine Larsen

8.2k total citations · 1 hit paper
266 papers, 6.5k citations indexed

About

Sine Larsen is a scholar working on Molecular Biology, Organic Chemistry and Materials Chemistry. According to data from OpenAlex, Sine Larsen has authored 266 papers receiving a total of 6.5k indexed citations (citations by other indexed papers that have themselves been cited), including 88 papers in Molecular Biology, 76 papers in Organic Chemistry and 76 papers in Materials Chemistry. Recurrent topics in Sine Larsen's work include Enzyme Structure and Function (44 papers), Biochemical and Molecular Research (35 papers) and Metal complexes synthesis and properties (34 papers). Sine Larsen is often cited by papers focused on Enzyme Structure and Function (44 papers), Biochemical and Molecular Research (35 papers) and Metal complexes synthesis and properties (34 papers). Sine Larsen collaborates with scholars based in Denmark, France and United States. Sine Larsen's co-authors include Leila Lo Leggio, Kaj Frank Jensen, Heidi A. Ernst, Sakari Kauppinen, Anne Mølgaard, Anders Kadziola, Paul Rowland, Jens-Christian N. Poulsen, Anders Ø. Madsen and Karen Skriver and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Advanced Materials.

In The Last Decade

Sine Larsen

264 papers receiving 6.3k citations

Hit Papers

Stimulation of Lignocellulosic Biomass Hydrolysis by Prot... 2010 2026 2015 2020 2010 100 200 300 400 500

Peers

Sine Larsen
Sine Larsen
Citations per year, relative to Sine Larsen Sine Larsen (= 1×) peers Felix Frolow

Countries citing papers authored by Sine Larsen

Since Specialization
Citations

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

Fields of papers citing papers by Sine Larsen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Sine Larsen

This figure shows the co-authorship network connecting the top 25 collaborators of Sine Larsen. A scholar is included among the top collaborators of Sine Larsen 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 Sine Larsen. Sine Larsen 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.
Laux, Valérie, Michael Haertlein, Elisabetta Boeri Erba, et al.. (2021). Structural insights into protein folding, stability and activity using in vivo perdeuteration of hen egg-white lysozyme. IUCrJ. 8(3). 372–386. 8 indexed citations
2.
Christiansen, Thomas L., Marine Cotte, Wout De Nolf, et al.. (2020). Insights into the composition of ancient Egyptian red and black inks on papyri achieved by synchrotron-based microanalyses. Proceedings of the National Academy of Sciences. 117(45). 27825–27835. 25 indexed citations
3.
Ernst, Heidi A., Klaus Piontek, Dietmar A. Plattner, et al.. (2018). A comparative structural analysis of the surface properties of asco-laccases. PLoS ONE. 13(11). e0206589–e0206589. 21 indexed citations
4.
Skubák, Pavol, Demet Araç, Matthew W. Bowler, et al.. (2018). A new MR-SAD algorithm for the automatic building of protein models from low-resolution X-ray data and a poor starting model. IUCrJ. 5(2). 166–171. 33 indexed citations
5.
Jacobsen, J. Steven, Marcia L. Moss, Fred Rasmussen, et al.. (2015). The function of the milk-clotting enzymes bovine and camel chymosin studied by a fluorescence resonance energy transfer assay. Journal of Dairy Science. 98(5). 2853–2860. 11 indexed citations
6.
Johansson, Eva, et al.. (2009). Concerted bifunctionality of the dCTP deaminase-dUTPase from Methanocaldococcus jannaschii: A structural and pre-steady state kinetic analysis. Archives of Biochemistry and Biophysics. 490(1). 42–49. 5 indexed citations
7.
Nours, Jérôme Le, Leonardo De Maria, Ditte Hededam Welner, et al.. (2008). Investigating the binding of β‐1,4‐galactan to Bacillus licheniformis β‐1,4‐galactanase by crystallography and computational modeling. Proteins Structure Function and Bioinformatics. 75(4). 977–989. 14 indexed citations
8.
Larsen, Sine. (2008). Structure, mechanism, and evolution of organophosphorus hydrolase from Deinococcus radiodurans.. Figshare. 2 indexed citations
9.
Ernst, Heidi A., Leila Lo Leggio, Martin Willemoës, et al.. (2006). Structure of the Sulfolobus solfataricus α-Glucosidase: Implications for Domain Conservation and Substrate Recognition in GH31. Journal of Molecular Biology. 358(4). 1106–1124. 124 indexed citations
10.
Cipriani, F., Franck Felisaz, L. Launer, et al.. (2006). Automation of sample mounting for macromolecular crystallography. Acta Crystallographica Section D Biological Crystallography. 62(10). 1251–1259. 81 indexed citations
11.
Sommer, Morten Otto Alexander & Sine Larsen. (2005). Crystallizing proteins on the basis of their precipitation diagram determined using a microfluidic formulator. Journal of Synchrotron Radiation. 12(6). 779–785. 11 indexed citations
12.
Olsen, Addie N., Heidi A. Ernst, Leila Lo Leggio, et al.. (2003). Preliminary crystallographic analysis of the NAC domain of ANAC, a member of the plant-specific NAC transcription factor family. Acta Crystallographica Section D Biological Crystallography. 60(1). 112–115. 24 indexed citations
13.
Nours, Jérôme Le, Leila Lo Leggio, Peter R. Østergaard, et al.. (2003). Structure of two fungal β‐1,4‐galactanases: Searching for the basis for temperature and pH optimum. Protein Science. 12(6). 1195–1204. 37 indexed citations
14.
McDonough, M.A., et al.. (2002). Crystallization and preliminary X-ray characterization of a thermostable pectate lyase fromThermotoga maritima. Acta Crystallographica Section D Biological Crystallography. 58(4). 709–711. 4 indexed citations
15.
Kadziola, Anders, et al.. (2002). Binding of cations in Bacillus subtilis phosphoribosyldiphosphate synthetase and their role in catalysis. Protein Science. 11(2). 271–279. 19 indexed citations
16.
Leggio, Leila Lo, Florence Dal Degan, Peter Poulsen, et al.. (2001). Crystallization and preliminary X-ray analysis of maltose O-acetyltransferase. Acta Crystallographica Section D Biological Crystallography. 57(12). 1915–1918. 4 indexed citations
17.
Hilden, Ida, Leila Lo Leggio, Sine Larsen, & Peter Poulsen. (2000). Characterization and crystallization of an active N‐terminally truncated form of the Escherichia coli glycogen branching enzyme. European Journal of Biochemistry. 267(8). 2150–2155. 22 indexed citations
18.
Mølgaard, Anne, Sakari Kauppinen, & Sine Larsen. (2000). Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases. Structure. 8(4). 373–383. 176 indexed citations
19.
Krotz, Achim H., Sine Larsen, Ole Buchardt, Magdalena Eriksson, & Peter E. Nielsen. (1998). A ‘Retro–Inverso’ PNA: structural implications for DNA and RNA binding. Bioorganic & Medicinal Chemistry. 6(11). 1983–1992. 10 indexed citations
20.
Petersen, Jens, Anders Kadziola, & Sine Larsen. (1994). Three‐dimensional structure of a recombinant peroxidase from Coprinus cinereus at 2.6 Å resolution. FEBS Letters. 339(3). 291–296. 67 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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