Birgit Strodel

6.4k total citations
119 papers, 3.9k citations indexed

About

Birgit Strodel is a scholar working on Molecular Biology, Physiology and Materials Chemistry. According to data from OpenAlex, Birgit Strodel has authored 119 papers receiving a total of 3.9k indexed citations (citations by other indexed papers that have themselves been cited), including 91 papers in Molecular Biology, 47 papers in Physiology and 21 papers in Materials Chemistry. Recurrent topics in Birgit Strodel's work include Protein Structure and Dynamics (67 papers), Alzheimer's disease research and treatments (43 papers) and Enzyme Structure and Function (19 papers). Birgit Strodel is often cited by papers focused on Protein Structure and Dynamics (67 papers), Alzheimer's disease research and treatments (43 papers) and Enzyme Structure and Function (19 papers). Birgit Strodel collaborates with scholars based in Germany, Sweden and Nigeria. Birgit Strodel's co-authors include David J. Wales, Martín Carballo‐Pacheco, Bogdan Barz, Olujide O. Olubiyi, Michael C. Owen, Qinghua Liao, Chetan Poojari, Dieter Willbold, Jennifer Loschwitz and Dušan Petrović and has published in prestigious journals such as Chemical Reviews, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Birgit Strodel

114 papers receiving 3.9k citations

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Birgit Strodel 2.7k 1.7k 699 676 473 119 3.9k
Jacques‐Philippe Colletier 2.5k 0.9× 630 0.4× 368 0.5× 737 1.1× 933 2.0× 65 4.4k
Colin Blake 3.3k 1.2× 1.8k 1.1× 642 0.9× 721 1.1× 173 0.4× 29 4.4k
Jeffrey Brender 4.1k 1.5× 3.8k 2.3× 1.0k 1.4× 671 1.0× 667 1.4× 93 6.7k
Danilo Milardi 2.1k 0.8× 1.5k 0.9× 298 0.4× 372 0.6× 196 0.4× 126 3.4k
Arthur Laganowsky 4.1k 1.5× 960 0.6× 401 0.6× 678 1.0× 206 0.4× 105 5.7k
Orlando Crescenzi 1.5k 0.6× 514 0.3× 230 0.3× 553 0.8× 225 0.5× 113 3.8k
Jüri Jarvet 1.7k 0.6× 1.3k 0.8× 357 0.5× 247 0.4× 283 0.6× 69 2.7k
Melinda Balbirnie 3.5k 1.3× 2.4k 1.4× 1.2k 1.8× 787 1.2× 211 0.4× 11 4.6k
Govardhan Reddy 1.2k 0.5× 431 0.3× 244 0.3× 590 0.9× 98 0.2× 63 1.9k
Gianluigi Veglia 4.9k 1.8× 705 0.4× 211 0.3× 1.4k 2.1× 277 0.6× 216 7.6k

Countries citing papers authored by Birgit Strodel

Since Specialization
Citations

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

Fields of papers citing papers by Birgit Strodel

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Birgit Strodel

This figure shows the co-authorship network connecting the top 25 collaborators of Birgit Strodel. A scholar is included among the top collaborators of Birgit Strodel 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 Birgit Strodel. Birgit Strodel 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.
Olubiyi, Olujide O., Birgit Strodel, Raphael J. Eberle, et al.. (2025). Novel dietary herbal preparations with inhibitory activities against multiple SARS-CoV-2 targets: A multidisciplinary investigation into antiviral activities. Food Chemistry Advances. 7. 100969–100969.
2.
Wales, David J., et al.. (2024). The energy landscape of Aβ42: a funnel to disorder for the monomer becomes a folding funnel for self-assembly. Chemical Communications. 60(92). 13574–13577. 2 indexed citations
3.
Kamp, Marc W. van der, et al.. (2024). Influence of Wobbling Tryptophan and Mutations on PET Degradation Explored by QM/MM Free Energy Calculations. Journal of Chemical Information and Modeling. 64(19). 7544–7554. 8 indexed citations
4.
Doerr, Mark, et al.. (2024). From Bulk to Binding: Decoding the Entry of PET into Hydrolase Binding Pockets. SHILAP Revista de lepidopterología. 4(10). 4000–4012. 16 indexed citations
5.
Kav, Batuhan, et al.. (2024). A brief history of amyloid aggregation simulations. Wiley Interdisciplinary Reviews Computational Molecular Science. 14(1). 11 indexed citations
6.
Weert, Marco van de, et al.. (2024). Insulin amyloid morphology is encoded in H-bonds and electrostatics interactions ruling protein phase separation. Journal of Colloid and Interface Science. 683(Pt 1). 1175–1187.
7.
Strodel, Birgit, et al.. (2023). Transition Networks Unveil Disorder-to-Order Transformations in Aβ Caused by Glycosaminoglycans or Lipids. International Journal of Molecular Sciences. 24(14). 11238–11238. 6 indexed citations
8.
Strodel, Birgit, et al.. (2023). Comparative molecular dynamics simulations of pathogenic and non-pathogenic huntingtin protein monomers and dimers. Frontiers in Molecular Biosciences. 10. 1143353–1143353. 6 indexed citations
9.
Kav, Batuhan & Birgit Strodel. (2022). Does the inclusion of electronic polarisability lead to a better modelling of peptide aggregation?. RSC Advances. 12(32). 20829–20837. 4 indexed citations
10.
Pfaff, Lara, Jian Gao, Zhishuai Li, et al.. (2022). Multiple Substrate Binding Mode-Guided Engineering of a Thermophilic PET Hydrolase. ACS Catalysis. 12(15). 9790–9800. 126 indexed citations
11.
Owen, Michael C., et al.. (2021). Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane. Proceedings of the National Academy of Sciences. 118(39). 79 indexed citations
12.
Kav, Batuhan, et al.. (2021). Disorder-to-order transition of the amyloid-β peptide upon lipid binding. Biophysical Chemistry. 280. 106700–106700. 64 indexed citations
13.
Loschwitz, Jennifer, et al.. (2021). Novel inhibitors of the main protease enzyme of SARS-CoV-2 identified via molecular dynamics simulation-guided in vitro assay. Bioorganic Chemistry. 111. 104862–104862. 33 indexed citations
14.
Huesgen, Pitter F., Heinrich Sticht, Birgit Strodel, et al.. (2019). Solution structure of the autophagy-related protein LC3C reveals a polyproline II motif on a mobile tether with phosphorylation site. Scientific Reports. 9(1). 14167–14167. 10 indexed citations
15.
Sengupta, Ushnish, Martín Carballo‐Pacheco, & Birgit Strodel. (2019). Automated Markov state models for molecular dynamics simulations of aggregation and self-assembly. The Journal of Chemical Physics. 150(11). 115101–115101. 52 indexed citations
16.
Owen, Michael C., David Gnutt, Mimi Gao, et al.. (2019). Effects ofin vivoconditions on amyloid aggregation. Chemical Society Reviews. 48(14). 3946–3996. 141 indexed citations
17.
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
18.
Viennet, Thibault, Michael M. Wördehoff, Chetan Poojari, et al.. (2018). Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation. Communications Biology. 1(1). 44–44. 86 indexed citations
19.
Petrović, Dušan, Xue Wang, & Birgit Strodel. (2018). How accurately do force fields represent protein side chain ensembles?. Proteins Structure Function and Bioinformatics. 86(9). 935–944. 15 indexed citations
20.
Poojari, Chetan & Birgit Strodel. (2013). Stability of Transmembrane Amyloid β-Peptide and Membrane Integrity Tested by Molecular Modeling of Site-Specific Aβ42 Mutations. PLoS ONE. 8(11). e78399–e78399. 26 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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