Sonja A. Dames

1.4k total citations
35 papers, 1.2k citations indexed

About

Sonja A. Dames is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, Sonja A. Dames has authored 35 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Biology, 9 papers in Cell Biology and 7 papers in Materials Chemistry. Recurrent topics in Sonja A. Dames's work include Protein Structure and Dynamics (9 papers), Enzyme Structure and Function (7 papers) and Protein Kinase Regulation and GTPase Signaling (6 papers). Sonja A. Dames is often cited by papers focused on Protein Structure and Dynamics (9 papers), Enzyme Structure and Function (7 papers) and Protein Kinase Regulation and GTPase Signaling (6 papers). Sonja A. Dames collaborates with scholars based in Germany, Switzerland and Canada. Sonja A. Dames's co-authors include Maria A. Martinez‐Yamout, Roberto N. De Guzman, Peter E. Wright, H. Jane Dyson, Stephan Grzesiek, Konrad Beyreuther, Heinrich Sticht, Rainer Frank, Dieter Willbold and C. Hilbich 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

Sonja A. Dames

35 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Sonja A. Dames Germany 16 967 260 220 137 130 35 1.2k
Till Maurer Germany 17 1.2k 1.2× 100 0.4× 62 0.3× 148 1.1× 121 0.9× 32 1.5k
Jane L. Wagstaff United Kingdom 14 956 1.0× 108 0.4× 99 0.5× 52 0.4× 120 0.9× 23 1.2k
Séverine Boulon France 17 2.0k 2.1× 84 0.3× 152 0.7× 90 0.7× 267 2.1× 21 2.3k
Sandra L. Harper United States 20 823 0.9× 319 1.2× 70 0.3× 68 0.5× 194 1.5× 43 1.3k
Aron W. Fenton United States 22 1.1k 1.1× 134 0.5× 106 0.5× 339 2.5× 90 0.7× 64 1.3k
Eduard V. Bocharov Russia 30 1.8k 1.9× 231 0.9× 61 0.3× 120 0.9× 238 1.8× 114 2.3k
Aaron H. Phillips United States 16 1.1k 1.2× 260 1.0× 34 0.2× 171 1.2× 102 0.8× 30 1.3k
Guilherme A. P. de Oliveira Brazil 21 1.2k 1.2× 228 0.9× 89 0.4× 153 1.1× 182 1.4× 61 1.7k
Eeson Rajendra United Kingdom 17 1.4k 1.4× 104 0.4× 99 0.5× 96 0.7× 249 1.9× 23 1.6k
Bruce A. Posner United States 12 1.5k 1.6× 57 0.2× 160 0.7× 103 0.8× 327 2.5× 19 1.9k

Countries citing papers authored by Sonja A. Dames

Since Specialization
Citations

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

Fields of papers citing papers by Sonja A. Dames

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Sonja A. Dames. 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 Sonja A. Dames. The network helps show where Sonja A. Dames may publish in the future.

Co-authorship network of co-authors of Sonja A. Dames

This figure shows the co-authorship network connecting the top 25 collaborators of Sonja A. Dames. A scholar is included among the top collaborators of Sonja A. Dames 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 Sonja A. Dames. Sonja A. Dames 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.
Oliva, Rosario, Marco Stellato, Pompea Del Vecchio, et al.. (2024). Structural characterization of the antimicrobial peptides myxinidin and WMR in bacterial membrane mimetic micelles and bicelles. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1866(3). 184272–184272. 1 indexed citations
2.
Tieleman, D. Peter, et al.. (2019). NMR– and MD simulation–based structural characterization of the membrane-associating FATC domain of ataxia telangiectasia mutated. Journal of Biological Chemistry. 294(17). 7098–7112. 5 indexed citations
5.
Wittwer, Matthias, Qi Luo, Ville R. I. Kaila, & Sonja A. Dames. (2016). Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G. Journal of Biological Chemistry. 291(53). 27062–27072. 14 indexed citations
6.
Wittwer, Matthias & Sonja A. Dames. (2015). Expression and purification of the natively disordered and redox sensitive metal binding regions of Mycobacterium tuberculosis protein kinase G. Protein Expression and Purification. 111. 68–74. 5 indexed citations
8.
Bigalke, Janna M., Sonja A. Dames, Wulf Blankenfeldt, Stephan Grzesiek, & Matthias Geyer. (2011). Structure and Dynamics of a Stabilized Coiled-Coil Domain in the P-TEFb Regulator Hexim1. Journal of Molecular Biology. 414(5). 639–653. 12 indexed citations
9.
Dames, Sonja A., et al.. (2011). Positional screening and NMR structure determination of side-chain-to-side-chain cyclized β3-peptides. Organic & Biomolecular Chemistry. 10(7). 1365–1373. 3 indexed citations
10.
Dames, Sonja A., André Schönichen, & Matthias Geyer. (2010). 1H, 15N, and 13C assignments of the N-terminal activation domain of Dictyostelium discoideum Formin C. Biomolecular NMR Assignments. 5(1). 47–49. 2 indexed citations
11.
Dames, Sonja A.. (2009). Structural Basis for the Association of the Redox-sensitive Target of Rapamycin FATC Domain with Membrane-mimetic Micelles. Journal of Biological Chemistry. 285(10). 7766–7775. 21 indexed citations
12.
Dames, Sonja A.. (2008). A fast and simple method to prepare the FKBP-rapamycin binding domain of human target of rapamycin for NMR binding assays. Protein Expression and Purification. 59(1). 31–37. 3 indexed citations
13.
Dames, Sonja A., Eunjung Bang, Daniel Häußinger, et al.. (2008). Insights into the Low Adhesive Capacity of Human T-cadherin from the NMR Structure of Its N-terminal Extracellular Domain. Journal of Biological Chemistry. 283(34). 23485–23495. 28 indexed citations
14.
Dames, Sonja A., et al.. (2005). The Solution Structure of the FATC Domain of the Protein Kinase Target of Rapamycin Suggests a Role for Redox-dependent Structural and Cellular Stability. Journal of Biological Chemistry. 280(21). 20558–20564. 106 indexed citations
15.
Alexandrescu, Andrei T., et al.. (1999). NMR Hydrogen Exchange of the OB-fold Protein LysN as a Function of Denaturant: The Most Conserved Elements of Structure are the Most Stable to Unfolding. Journal of Molecular Biology. 289(4). 1041–1054. 27 indexed citations
16.
Dames, Sonja A., Richard A. Kammerer, Detlef Moskau, Jürgen Engel, & Andrei T. Alexandrescu. (1999). Contributions of the ionization states of acidic residues to the stability of the coiled coil domain of matrilin‐1. FEBS Letters. 446(1). 75–80. 17 indexed citations
17.
Dames, Sonja A., et al.. (1998). NMR structure of a parallel homotrimeric coiled coil. Nature Structural & Molecular Biology. 5(8). 687–691. 44 indexed citations
19.
Alexandrescu, Andrei T., Sonja A. Dames, & Ronald Wiltscheck. (1996). A fragment of staphylococcal nuclease with an OB‐fold structure shows hydrogen‐exchange protection factors in the range reported for “molten globules”. Protein Science. 5(9). 1942–1946. 11 indexed citations
20.
Sticht, Heinrich, Peter Bayer, Dieter Willbold, et al.. (1995). Structure of Amyloid A4‐(1–40)‐Peptide of Alzheimer's Disease. European Journal of Biochemistry. 233(1). 293–298. 255 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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