Gunnar F. Schröder

10.5k total citations · 4 hit papers
87 papers, 7.4k citations indexed

About

Gunnar F. Schröder is a scholar working on Molecular Biology, Materials Chemistry and Physiology. According to data from OpenAlex, Gunnar F. Schröder has authored 87 papers receiving a total of 7.4k indexed citations (citations by other indexed papers that have themselves been cited), including 55 papers in Molecular Biology, 24 papers in Materials Chemistry and 18 papers in Physiology. Recurrent topics in Gunnar F. Schröder's work include Enzyme Structure and Function (24 papers), Protein Structure and Dynamics (22 papers) and Alzheimer's disease research and treatments (18 papers). Gunnar F. Schröder is often cited by papers focused on Enzyme Structure and Function (24 papers), Protein Structure and Dynamics (22 papers) and Alzheimer's disease research and treatments (18 papers). Gunnar F. Schröder collaborates with scholars based in Germany, United States and Switzerland. Gunnar F. Schröder's co-authors include Helmut Grubmüller, Edward H. Egelman, Michael Levitt, Axel T. Brünger, Erich Lanka, Matthijn Vos, Wolfgang Hoyer, Dieter Willbold, Qian Yin and Jianbin Ruan and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Gunnar F. Schröder

83 papers receiving 7.3k citations

Hit Papers

Unified Polymerization Mechanism for the Assembly of ASC-... 2008 2026 2014 2020 2014 2008 2017 2010 250 500 750 1000

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Gunnar F. Schröder Germany 41 5.0k 1.2k 1.2k 796 731 87 7.4k
Henning Stahlberg Switzerland 56 7.5k 1.5× 963 0.8× 1.1k 1.0× 789 1.0× 920 1.3× 220 12.3k
Duilio Cascio United States 55 8.0k 1.6× 2.0k 1.6× 1.4k 1.2× 316 0.4× 705 1.0× 156 10.8k
Elena V. Orlova United Kingdom 48 6.3k 1.2× 1.2k 1.0× 889 0.8× 570 0.7× 692 0.9× 151 9.3k
José Valpuesta Spain 54 6.1k 1.2× 1.5k 1.3× 869 0.8× 998 1.3× 1.1k 1.5× 176 8.6k
Raimond B. G. Ravelli Netherlands 47 5.2k 1.0× 2.1k 1.7× 958 0.8× 223 0.3× 1.3k 1.8× 118 9.2k
Martin Zacharias Germany 53 8.2k 1.6× 1.7k 1.4× 598 0.5× 1.1k 1.4× 554 0.8× 346 10.4k
Andreas Herrmann Germany 63 8.1k 1.6× 569 0.5× 1.2k 1.0× 947 1.2× 1.4k 1.8× 330 12.2k
Yves Engelborghs Belgium 51 5.0k 1.0× 1.0k 0.8× 482 0.4× 285 0.4× 928 1.3× 202 8.3k
Tamir Gonen United States 52 7.2k 1.4× 2.8k 2.3× 661 0.6× 260 0.3× 1.2k 1.6× 148 10.8k
David Sept United States 41 6.7k 1.3× 1.1k 0.9× 443 0.4× 551 0.7× 2.5k 3.4× 110 11.2k

Countries citing papers authored by Gunnar F. Schröder

Since Specialization
Citations

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

Fields of papers citing papers by Gunnar F. Schröder

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Gunnar F. Schröder. 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 Gunnar F. Schröder. The network helps show where Gunnar F. Schröder may publish in the future.

Co-authorship network of co-authors of Gunnar F. Schröder

This figure shows the co-authorship network connecting the top 25 collaborators of Gunnar F. Schröder. A scholar is included among the top collaborators of Gunnar F. Schröder 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 Gunnar F. Schröder. Gunnar F. Schröder 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.
Willbold, Dieter, et al.. (2025). Lecanemab Binds to Transgenic Mouse Model‐Derived Amyloid‐β Fibril Structures Resembling Alzheimer's Disease Type I, Type II and Arctic Folds. Neuropathology and Applied Neurobiology. 51(3). e70022–e70022. 2 indexed citations
2.
Frieg, Benedikt, Dirk Matthes, Andrei Leonov, et al.. (2025). Anle138b binds predominantly to the central cavity in lipidic Aβ₄₀ fibrils and modulates fibril formation. Nature Communications. 16(1). 8850–8850.
3.
Gremer, Lothar, Benedikt Frieg, Luisa U. Schäfer, et al.. (2023). Cryo-EM of Aβ fibrils from mouse models find tg-APPArcSwe fibrils resemble those found in patients with sporadic Alzheimer’s disease. Nature Neuroscience. 26(12). 2073–2080. 30 indexed citations
4.
Matthes, Dirk, Rıza Dervişoğlu, Benedikt Frieg, et al.. (2022). The clinical drug candidate anle138b binds in a cavity of lipidic α-synuclein fibrils. Nature Communications. 13(1). 5385–5385. 34 indexed citations
5.
Frieg, Benedikt, Timo Strohäker, Christian Dienemann, et al.. (2022). Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein. Communications Biology. 5(1). 1040–1040. 16 indexed citations
6.
Cukkemane, Abhishek, Nina I. Becker, Benedikt Frieg, et al.. (2021). Conformational heterogeneity coupled with β-fibril formation of a scaffold protein involved in chronic mental illnesses. Translational Psychiatry. 11(1). 639–639. 9 indexed citations
7.
Hänsch, Sebastian, et al.. (2021). Endo-lysosomal Aβ concentration and pH trigger formation of Aβ oligomers that potently induce Tau missorting. Nature Communications. 12(1). 84 indexed citations
8.
Schröder, Gunnar F., et al.. (2021). Challenges in sample preparation and structure determination of amyloids by cryo-EM. Journal of Biological Chemistry. 297(2). 100938–100938. 27 indexed citations
9.
Corte, Dennis Della, Hugo L. van Beek, Marcus Schallmey, et al.. (2020). Engineering and application of a biosensor with focused ligand specificity. Nature Communications. 11(1). 4851–4851. 79 indexed citations
10.
Gremer, Lothar, Raimond B. G. Ravelli, Dieter Willbold, et al.. (2019). Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy. Nature Communications. 10(1). 3754–3754. 31 indexed citations
11.
Kühnemuth, Ralf, Dennis Della Corte, Gunnar F. Schröder, et al.. (2018). Integrated NMR, Fluorescence, and Molecular Dynamics Benchmark Study of Protein Mechanics and Hydrodynamics. The Journal of Physical Chemistry B. 123(7). 1453–1480. 25 indexed citations
12.
Gremer, Lothar, C. Schenk, Elke Reinartz, et al.. (2017). Fibril structure of amyloid-β(1–42) by cryo–electron microscopy. Science. 358(6359). 116–119. 802 indexed citations breakdown →
13.
Schröder, Gunnar F., Michael Levitt, & Axel T. Brünger. (2014). Deformable elastic network refinement for low-resolution macromolecular crystallography. Acta Crystallographica Section D Biological Crystallography. 70(9). 2241–2255. 25 indexed citations
14.
Lu, Alvin, Venkat Giri Magupalli, Jianbin Ruan, et al.. (2014). Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes. Cell. 156(6). 1193–1206. 1069 indexed citations breakdown →
15.
Kalisman, Nir, Gunnar F. Schröder, & Michael Levitt. (2013). The Crystal Structures of the Eukaryotic Chaperonin CCT Reveal Its Functional Partitioning. Structure. 21(4). 540–549. 49 indexed citations
16.
O’Donovan, Daniel J., Ian Stokes-Rees, Yunsun Nam, et al.. (2012). A grid-enabled web service for low-resolution crystal structure refinement. Acta Crystallographica Section D Biological Crystallography. 68(3). 261–267. 16 indexed citations
17.
Schröder, Gunnar F., Ralf Schuelein, Maxime Québatte, & Christoph Dehio. (2011). Conjugative DNA transfer into human cells by the VirB/VirD4 type IV secretion system of the bacterial pathogen Bartonella henselae. Proceedings of the National Academy of Sciences. 108(35). 14643–14648. 72 indexed citations
18.
Galkin, Vitold E., Albina Orlova, Dmitri S. Kudryashov, et al.. (2011). Remodeling of actin filaments by ADF/cofilin proteins. Proceedings of the National Academy of Sciences. 108(51). 20568–20572. 177 indexed citations
19.
Schülein, Ralf, Patrick Guye, Michael C. Schmid, et al.. (2005). A bipartite signal mediates the transfer of type IV secretion substrates of Bartonella henselae into human cells. Proceedings of the National Academy of Sciences. 102(3). 856–861. 193 indexed citations
20.
Schröder, Gunnar F., Ulrike Alexiev, & Helmut Grubmüller. (2005). Simulation of Fluorescence Anisotropy Experiments: Probing Protein Dynamics. Biophysical Journal. 89(6). 3757–3770. 125 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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