Martin Tollinger

3.3k total citations
89 papers, 2.5k citations indexed

About

Martin Tollinger is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Martin Tollinger has authored 89 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 59 papers in Molecular Biology, 20 papers in Materials Chemistry and 19 papers in Spectroscopy. Recurrent topics in Martin Tollinger's work include Protein Structure and Dynamics (29 papers), RNA and protein synthesis mechanisms (20 papers) and Enzyme Structure and Function (18 papers). Martin Tollinger is often cited by papers focused on Protein Structure and Dynamics (29 papers), RNA and protein synthesis mechanisms (20 papers) and Enzyme Structure and Function (18 papers). Martin Tollinger collaborates with scholars based in Austria, Canada and United States. Martin Tollinger's co-authors include Julie D. Forman‐Kay, Lewis E. Kay, Robert Konrat, Sven Brüschweiler, Nikolai R. Skrynnikov, Frans A. A. Mulder, Christoph Kreutz, Kathrin Breuker, Karin A. Crowhurst and Bernhard Kräutler 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

Martin Tollinger

84 papers receiving 2.4k citations

Peers

Martin Tollinger
Mark W.F. Fischer United States
R. Fourme France
Nicholas J. Skelton United States
A. Gilbert United States
Ansgar B. Siemer United States
A. Ducruix France
Andrew L. Lee United States
Suzanne B. Shuker United States
Ananya Majumdar United States
Martin Tollinger
Citations per year, relative to Martin Tollinger Martin Tollinger (= 1×) peers Kazuyuki Akasaka

Countries citing papers authored by Martin Tollinger

Since Specialization
Citations

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

Fields of papers citing papers by Martin Tollinger

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Martin Tollinger

This figure shows the co-authorship network connecting the top 25 collaborators of Martin Tollinger. A scholar is included among the top collaborators of Martin Tollinger 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 Martin Tollinger. Martin Tollinger 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.
Tollinger, Martin, et al.. (2025). Methylation of Cytidine 1407 Increases the Lifetimes of the A-Site Ground and Excited States of E. coli 16S Ribosomal RNA. Journal of the American Chemical Society. 147(30). 26097–26101. 1 indexed citations
2.
Kreutz, Christoph, et al.. (2024). The PR‐10 Protein Pru p 1 is an Endonuclease that Preferentially Cleaves Single–Stranded RNA. ChemBioChem. 25(12). e202400204–e202400204.
3.
Fernández‐Quintero, Monica L., et al.. (2023). Structural Basis of the Immunological Cross-Reactivity between Kiwi and Birch Pollen. Foods. 12(21). 3939–3939.
4.
Cova, Valentina, Anna S. Kamenik, Klaus R. Liedl, et al.. (2022). Ascorbylation of a Reactive Cysteine in the Major Apple Allergen Mal d 1. Foods. 11(19). 2953–2953. 3 indexed citations
5.
Cova, Valentina, Anna S. Kamenik, Klaus R. Liedl, et al.. (2022). Covalent polyphenol modification of a reactive cysteine in the major apple allergen Mal d 1. Food Chemistry. 410. 135374–135374. 15 indexed citations
6.
Kim, Hyeong Jin, M.M. Black, Ross A. Edwards, et al.. (2022). Structural basis for recognition of transcriptional terminator structures by ProQ/FinO domain RNA chaperones. Nature Communications. 13(1). 7076–7076. 8 indexed citations
7.
Tollinger, Martin, et al.. (2021). Microdroplet Mass Spectrometry Enables Extremely Accelerated Pepsin Digestion of Proteins. Journal of the American Society for Mass Spectrometry. 32(7). 1841–1845. 16 indexed citations
8.
Hofer, Florian, et al.. (2021). Structure and Zeatin Binding of the Peach Allergen Pru p 1. Journal of Agricultural and Food Chemistry. 69(29). 8120–8129. 10 indexed citations
9.
Kamenik, Anna S., et al.. (2021). Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens. Scientific Reports. 11(1). 4173–4173. 14 indexed citations
10.
Gallmetzer, Andreas, Yazmid Reyes-Domínguez, Christoph Kreutz, et al.. (2021). (3ξ,4ξ,5ξ,6ξ,7ξ,11ξ)-3,6-Dihydroxy-8-oxo-9-eremophilene-12-oic Acid, a New Phytotoxin of Alternaria alternata ssp. tenuissima Isolates Associated with Fruit Spots on Apple (Malus × domestica Borkh.). Journal of Agricultural and Food Chemistry. 69(48). 14445–14458. 8 indexed citations
11.
Mateos, Borja, Ganeko Bernardo‐Seisdedos, Gabriel Ortega, et al.. (2021). Cosolute modulation of protein oligomerization reactions in the homeostatic timescale. Biophysical Journal. 120(10). 2067–2077. 4 indexed citations
12.
Kim, Hyeong Jin, et al.. (2020). NMR resonance assignments of the FinO-domain of the RNA chaperone RocC. Biomolecular NMR Assignments. 15(1). 61–64. 3 indexed citations
13.
Tollinger, Martin, et al.. (2019). NMR resonance assignments of the four isoforms of the hazelnut allergen Cor a 1.04. Biomolecular NMR Assignments. 14(1). 45–49. 3 indexed citations
14.
Breuker, Kathrin, et al.. (2018). NMR resonance assignments of the pathogenesis-related peach allergen Pru p 1.0101. Biomolecular NMR Assignments. 13(1). 127–130. 7 indexed citations
15.
Wallner, Michael, et al.. (2017). NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1. Biomolecular NMR Assignments. 11(2). 231–234. 3 indexed citations
16.
Fuchs, Julian E., et al.. (2017). Conformational Flexibility Differentiates Naturally Occurring Bet v 1 Isoforms. International Journal of Molecular Sciences. 18(6). 1192–1192. 18 indexed citations
17.
Scheffzek, Klaus, et al.. (2017). NMR resonance assignments of the EVH1 domain of neurofibromin’s recruitment factor Spred1. Biomolecular NMR Assignments. 11(2). 305–308. 2 indexed citations
18.
Juen, Michael Andreas, Christoph H. Wunderlich, Felix Nußbaumer, et al.. (2016). Excited States of Nucleic Acids Probed by Proton Relaxation Dispersion NMR Spectroscopy. Angewandte Chemie International Edition. 55(39). 12008–12012. 40 indexed citations
19.
Tollinger, Martin, Lewis E. Kay, & Julie D. Forman‐Kay. (2005). Measuring p K a Values in Protein Folding Transition State Ensembles by NMR Spectroscopy. Journal of the American Chemical Society. 127(25). 8904–8905. 13 indexed citations
20.
Tollinger, Martin, Karin A. Crowhurst, Lewis E. Kay, & Julie D. Forman‐Kay. (2003). Site-specific contributions to the pH dependence of protein stability. Proceedings of the National Academy of Sciences. 100(8). 4545–4550. 76 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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