Luitgard Nagel‐Steger

2.7k total citations
58 papers, 2.0k citations indexed

About

Luitgard Nagel‐Steger is a scholar working on Molecular Biology, Physiology and Computational Theory and Mathematics. According to data from OpenAlex, Luitgard Nagel‐Steger has authored 58 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 39 papers in Molecular Biology, 26 papers in Physiology and 11 papers in Computational Theory and Mathematics. Recurrent topics in Luitgard Nagel‐Steger's work include Alzheimer's disease research and treatments (25 papers), Computational Drug Discovery Methods (11 papers) and Protein Structure and Dynamics (9 papers). Luitgard Nagel‐Steger is often cited by papers focused on Alzheimer's disease research and treatments (25 papers), Computational Drug Discovery Methods (11 papers) and Protein Structure and Dynamics (9 papers). Luitgard Nagel‐Steger collaborates with scholars based in Germany, United States and France. Luitgard Nagel‐Steger's co-authors include Dieter Willbold, Detlev Riesner, Thomas van Groen, Birgit Strodel, Inga Kadish, Katja Wiesehan, Michael C. Owen, Susanne Aileen Funke, Jan Stöhr and Lothar Gremer and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Luitgard Nagel‐Steger

56 papers receiving 2.0k citations

Peers

Luitgard Nagel‐Steger
Ivo C. Martins Portugal
Rui Zhou China
Johnny Habchi United Kingdom
Yuri Sokolov United States
Peter Friedhoff Germany
Jennifer Reed Germany
Marina Kirkitadze Canada
Satish Kumar India
Ricardo Capone United States
Chi L.L. Pham Australia
Ivo C. Martins Portugal
Luitgard Nagel‐Steger
Citations per year, relative to Luitgard Nagel‐Steger Luitgard Nagel‐Steger (= 1×) peers Ivo C. Martins

Countries citing papers authored by Luitgard Nagel‐Steger

Since Specialization
Citations

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

Fields of papers citing papers by Luitgard Nagel‐Steger

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Luitgard Nagel‐Steger. 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 Luitgard Nagel‐Steger. The network helps show where Luitgard Nagel‐Steger may publish in the future.

Co-authorship network of co-authors of Luitgard Nagel‐Steger

This figure shows the co-authorship network connecting the top 25 collaborators of Luitgard Nagel‐Steger. A scholar is included among the top collaborators of Luitgard Nagel‐Steger 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 Luitgard Nagel‐Steger. Luitgard Nagel‐Steger 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.
Pauly, Thomas, Roland Fenk, Luitgard Nagel‐Steger, et al.. (2025). Tracking reduction-induced molecular changes in pathological free light chains by SV-AUC. European Biophysics Journal. 54(6). 365–383.
2.
Pauly, Thomas, Jan Ove Hansen, Magnus Haraldson Høie, et al.. (2023). Widespread amyloidogenicity potential of multiple myeloma patient-derived immunoglobulin light chains. BMC Biology. 21(1). 21–21. 5 indexed citations
3.
Pauly, Thomas, et al.. (2022). Differentiation of subnucleus-sized oligomers and nucleation-competent assemblies of the Aβ peptide. Biophysical Journal. 122(2). 269–278. 1 indexed citations
4.
Pauly, Thomas, et al.. (2022). Met/Val129 polymorphism of the full-length human prion protein dictates distinct pathways of amyloid formation. Journal of Biological Chemistry. 298(10). 102430–102430. 2 indexed citations
5.
Dingley, Andrew J., Joachim Granzin, Luitgard Nagel‐Steger, et al.. (2019). Structure of the SLy1 SAM homodimer reveals a new interface for SAM domain self-association. Scientific Reports. 9(1). 12 indexed citations
6.
Höppner, Astrid, Clarisa E. Álvarez, Holger Gohlke, et al.. (2019). Posttranslational Modification of the NADP-Malic Enzyme Involved in C 4 Photosynthesis Modulates the Enzymatic Activity during the Day. The Plant Cell. 31(10). 2525–2539. 17 indexed citations
7.
Groen, Thomas van, Oleksandr Brener, Lothar Gremer, et al.. (2017). The Aβ oligomer eliminating D-enantiomeric peptide RD2 improves cognition without changing plaque pathology. Scientific Reports. 7(1). 16275–16275. 47 indexed citations
8.
Frieg, Benedikt, Finn K. Hansen, Andreas Marmann, et al.. (2017). EDTA aggregates induce SYPRO orange-based fluorescence in thermal shift assay. PLoS ONE. 12(5). e0177024–e0177024. 25 indexed citations
9.
Biehl, Ralf, et al.. (2016). Monomeric Amyloid Beta Peptide in Hexafluoroisopropanol Detected by Small Angle Neutron Scattering. PLoS ONE. 11(2). e0150267–e0150267. 32 indexed citations
10.
Smits, Sander H. J., et al.. (2016). The Chlamydia pneumoniae Adhesin Pmp21 Forms Oligomers with Adhesive Properties. Journal of Biological Chemistry. 291(43). 22806–22818. 12 indexed citations
11.
Olubiyi, Olujide O., Dirk Bartnik, Oleksandr Brener, et al.. (2014). Amyloid Aggregation Inhibitory Mechanism of Arginine-rich D-peptides. Current Medicinal Chemistry. 21(12). 1448–1457. 29 indexed citations
12.
Wurm, Reinhild, Oleksandr Brener, Philipp Ellinger, et al.. (2013). Double-strand DNA end-binding and sliding of the toroidal CRISPR-associated protein Csn2. Nucleic Acids Research. 41(12). 6347–6359. 40 indexed citations
13.
Bannach, Oliver, Jan Stöhr, Michael M. Wördehoff, et al.. (2013). Seeded Fibrillation as Molecular Basis of the Species Barrier in Human Prion Diseases. PLoS ONE. 8(8). e72623–e72623. 14 indexed citations
14.
Wolff, Martin, et al.. (2013). The Off-rate of Monomers Dissociating from Amyloid-β Protofibrils. Journal of Biological Chemistry. 288(52). 37104–37111. 24 indexed citations
15.
Kroth, Heiko, Annalisa Ansaloni, Yvan Varisco, et al.. (2012). Discovery and Structure Activity Relationship of Small Molecule Inhibitors of Toxic β-Amyloid-42 Fibril Formation. Journal of Biological Chemistry. 287(41). 34786–34800. 46 indexed citations
16.
Hickman, David T., María Pilar López-Deber, Deepak Nand, et al.. (2011). Sequence-independent Control of Peptide Conformation in Liposomal Vaccines for Targeting Protein Misfolding Diseases. Journal of Biological Chemistry. 286(16). 13966–13976. 66 indexed citations
17.
18.
Demeler, Borries, Emre Brookes, & Luitgard Nagel‐Steger. (2009). Chapter 4 Analysis of Heterogeneity in Molecular Weight and Shape by Analytical Ultracentrifugation Using Parallel Distributed Computing. Methods in enzymology on CD-ROM/Methods in enzymology. 454. 87–113. 32 indexed citations
19.
Groen, Thomas van, Katja Wiesehan, Susanne Aileen Funke, et al.. (2008). Reduction of Alzheimer’s Disease Amyloid Plaque Load in Transgenic Mice by D3, a D ‐Enantiomeric Peptide Identified by Mirror Image Phage Display. ChemMedChem. 3(12). 1848–1852. 110 indexed citations
20.
Schell, Jeff, Katja Jansen, Ralf Lucassen, et al.. (2004). The Structural Transition of the Prion Protein into its Pathogenic Conformation is Induced by Unmasking Hydrophobic Sites. Journal of Molecular Biology. 344(3). 839–853. 36 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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