E.M. Quistgaard

2.3k total citations · 1 hit paper
30 papers, 1.7k citations indexed

About

E.M. Quistgaard is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, E.M. Quistgaard has authored 30 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 10 papers in Materials Chemistry and 7 papers in Biochemistry. Recurrent topics in E.M. Quistgaard's work include Enzyme Structure and Function (10 papers), Amino Acid Enzymes and Metabolism (7 papers) and Protein Structure and Dynamics (7 papers). E.M. Quistgaard is often cited by papers focused on Enzyme Structure and Function (10 papers), Amino Acid Enzymes and Metabolism (7 papers) and Protein Structure and Dynamics (7 papers). E.M. Quistgaard collaborates with scholars based in Sweden, Denmark and Singapore. E.M. Quistgaard's co-authors include Christian Löw, P. Nordlund, Fatma Guettou, Søren Thirup, Per Moberg, Lene H. Madsen, Euan K. James, Simona Radutoiu, Jens Stougaard and L. Tresaugues 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

E.M. Quistgaard

30 papers receiving 1.7k citations

Hit Papers

Understanding transport by the major facilitator superfam... 2016 2026 2019 2022 2016 100 200 300

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
E.M. Quistgaard Sweden 18 789 582 238 181 144 30 1.7k
Alfredo Cravador Portugal 23 581 0.7× 478 0.8× 77 0.3× 106 0.6× 284 2.0× 76 1.5k
Oliver C. Richards United States 31 1.4k 1.8× 417 0.7× 70 0.3× 61 0.3× 103 0.7× 62 2.5k
Ian M. Willis United States 36 3.4k 4.3× 272 0.5× 141 0.6× 83 0.5× 208 1.4× 94 3.9k
Yue Xu China 25 921 1.2× 518 0.9× 107 0.4× 16 0.1× 426 3.0× 51 2.0k
José Antonio Márquez France 27 1.7k 2.2× 1.6k 2.8× 143 0.6× 26 0.1× 119 0.8× 57 3.2k
Christine Kaufmann Germany 19 1.1k 1.4× 158 0.3× 116 0.5× 79 0.4× 107 0.7× 36 1.6k
Trazel Teh Australia 14 1.7k 2.1× 728 1.3× 85 0.4× 28 0.2× 233 1.6× 20 2.4k
Lilin Zhang China 20 904 1.1× 308 0.5× 189 0.8× 39 0.2× 155 1.1× 78 1.6k
Aaron P. van Loon Switzerland 18 1.4k 1.8× 252 0.4× 125 0.5× 15 0.1× 155 1.1× 21 2.0k
Brian S. Imai United States 16 1.6k 2.1× 238 0.4× 151 0.6× 18 0.1× 109 0.8× 20 2.3k

Countries citing papers authored by E.M. Quistgaard

Since Specialization
Citations

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

Fields of papers citing papers by E.M. Quistgaard

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by E.M. Quistgaard. 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 E.M. Quistgaard. The network helps show where E.M. Quistgaard may publish in the future.

Co-authorship network of co-authors of E.M. Quistgaard

This figure shows the co-authorship network connecting the top 25 collaborators of E.M. Quistgaard. A scholar is included among the top collaborators of E.M. Quistgaard 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 E.M. Quistgaard. E.M. Quistgaard 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.
Shahsavar, Azadeh, et al.. (2021). Insights into the mechanism of high lipid–detergent crystallization of membrane proteins. Journal of Applied Crystallography. 54(6). 1775–1783. 2 indexed citations
2.
Quistgaard, E.M.. (2021). BAP31: Physiological functions and roles in disease. Biochimie. 186. 105–129. 40 indexed citations
3.
Dyla, Mateusz, et al.. (2021). The Crystal Structure of the Ca2+-ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation. Journal of Molecular Biology. 433(16). 167015–167015. 8 indexed citations
4.
Quistgaard, E.M., et al.. (2021). Mind the Gap: Molecular Architecture of the Axon Initial Segment – From Fold Prediction to a Mechanistic Model of Function?. Journal of Molecular Biology. 433(20). 167176–167176. 5 indexed citations
5.
Flayhan, Ali, Jan Strauss, Vasileios Rantos, et al.. (2019). Structure of Prototypic Peptide Transporter DtpA fromE. coliin Complex with Valganciclovir Provides Insights into Drug Binding of Human PepT1. Journal of the American Chemical Society. 141(6). 2404–2412. 44 indexed citations
6.
Quistgaard, E.M., et al.. (2018). Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter. Structure. 26(3). 467–476.e4. 52 indexed citations
8.
Januliene, Dovile, Jacob Lauwring Andersen, E.M. Quistgaard, et al.. (2017). Acidic Environment Induces Dimerization and Ligand Binding Site Collapse in the Vps10p Domain of Sortilin. Structure. 25(12). 1809–1819.e3. 18 indexed citations
9.
Quistgaard, E.M., Christian Löw, Fatma Guettou, & P. Nordlund. (2016). Understanding transport by the major facilitator superfamily (MFS): structures pave the way. Nature Reviews Molecular Cell Biology. 17(2). 123–132. 335 indexed citations breakdown →
10.
Quistgaard, E.M., Ulrich Weininger, Kristofer Modig, et al.. (2016). Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD. BMC Biology. 14(1). 82–82. 24 indexed citations
11.
Tsutakawa, Susan E., et al.. (2014). Structural and Biochemical Characterization of Human PR70 in Isolation and in Complex with the Scaffolding Subunit of Protein Phosphatase 2A. PLoS ONE. 9(7). e101846–e101846. 11 indexed citations
12.
Guettou, Fatma, et al.. (2014). Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2. Nature Structural & Molecular Biology. 21(8). 728–731. 68 indexed citations
13.
Löw, Christian, Yin Hoe Yau, Els Pardon, et al.. (2013). Nanobody Mediated Crystallization of an Archeal Mechanosensitive Channel. PLoS ONE. 8(10). e77984–e77984. 21 indexed citations
14.
Quistgaard, E.M., Christian Löw, Per Moberg, et al.. (2013). Structural and Biophysical Characterization of the Cytoplasmic Domains of Human BAP29 and BAP31. PLoS ONE. 8(8). e71111–e71111. 16 indexed citations
15.
Quistgaard, E.M., Christian Löw, Per Moberg, & P. Nordlund. (2013). Metal-mediated crystallization of the xylose transporter XylE from Escherichia coli in three different crystal forms. Journal of Structural Biology. 184(2). 375–378. 6 indexed citations
16.
Guettou, Fatma, E.M. Quistgaard, L. Tresaugues, et al.. (2013). Structural insights into substrate recognition in proton‐dependent oligopeptide transporters. EMBO Reports. 14(9). 804–810. 77 indexed citations
17.
Thirup, Søren, Vikas Gupta, & E.M. Quistgaard. (2012). Up, Down, and Around: Identifying Recurrent Interactions Within and Between Super-secondary Structures in β-Propellers. Methods in molecular biology. 932. 35–50. 2 indexed citations
19.
Radutoiu, Simona, Lene H. Madsen, Esben Bjørn Madsen, et al.. (2007). LysM domains mediate lipochitin–oligosaccharide recognition and Nfr genes extend the symbiotic host range. The EMBO Journal. 26(17). 3923–3935. 260 indexed citations
20.
Kanamori, Norihito, Lene H. Madsen, Simona Radutoiu, et al.. (2006). A nucleoporin is required for induction of Ca 2+ spiking in legume nodule development and essential for rhizobial and fungal symbiosis. Proceedings of the National Academy of Sciences. 103(2). 359–364. 256 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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