J.R. Mesters

4.9k total citations · 1 hit paper
58 papers, 3.6k citations indexed

About

J.R. Mesters is a scholar working on Molecular Biology, Materials Chemistry and Infectious Diseases. According to data from OpenAlex, J.R. Mesters has authored 58 papers receiving a total of 3.6k indexed citations (citations by other indexed papers that have themselves been cited), including 39 papers in Molecular Biology, 16 papers in Materials Chemistry and 11 papers in Infectious Diseases. Recurrent topics in J.R. Mesters's work include RNA and protein synthesis mechanisms (16 papers), Enzyme Structure and Function (16 papers) and Protein Structure and Dynamics (9 papers). J.R. Mesters is often cited by papers focused on RNA and protein synthesis mechanisms (16 papers), Enzyme Structure and Function (16 papers) and Protein Structure and Dynamics (9 papers). J.R. Mesters collaborates with scholars based in Germany, Netherlands and Czechia. J.R. Mesters's co-authors include R. Hilgenfeld, K. Anand, John Ziebuhr, Parvesh Wadhwani, Bart P. H. J. Thomma, Andrea Sánchez‐Vallet, Guido Hansen, Rolf Hilgenfeld, Jinzhi Tan and Barend Kraal and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

J.R. Mesters

57 papers receiving 3.6k citations

Hit Papers

Coronavirus Main Proteinase (3CL pro ) Structure: Basis f... 2003 2026 2010 2018 2003 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
J.R. Mesters Germany 26 1.6k 1.3k 815 670 332 58 3.6k
Pieter Leyssen Belgium 46 2.1k 1.4× 2.6k 2.0× 580 0.7× 560 0.8× 1.1k 3.3× 170 6.7k
M.M. Cherney Canada 31 1.9k 1.2× 783 0.6× 225 0.3× 174 0.3× 365 1.1× 75 3.4k
Xuejun C. Zhang China 38 2.5k 1.6× 921 0.7× 290 0.4× 236 0.4× 131 0.4× 108 4.4k
K.P. Battaile United States 34 2.1k 1.3× 739 0.6× 467 0.6× 121 0.2× 232 0.7× 131 3.6k
Shilong Fan China 18 2.5k 1.6× 3.4k 2.6× 676 0.8× 310 0.5× 134 0.4× 63 5.8k
Markus Wiederstein Austria 15 3.6k 2.3× 614 0.5× 499 0.6× 464 0.7× 234 0.7× 22 5.1k
Ute Curth Germany 23 2.0k 1.3× 1.3k 1.0× 1.4k 1.7× 142 0.2× 511 1.5× 45 3.9k
Yu Guo China 31 1.2k 0.7× 862 0.7× 247 0.3× 238 0.4× 144 0.4× 95 2.6k
R. Hilgenfeld Germany 18 1.5k 0.9× 2.0k 1.5× 1.4k 1.7× 100 0.1× 471 1.4× 29 3.8k
K. Anand Germany 18 1.7k 1.1× 1.8k 1.4× 1.4k 1.7× 79 0.1× 474 1.4× 29 3.8k

Countries citing papers authored by J.R. Mesters

Since Specialization
Citations

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

Fields of papers citing papers by J.R. Mesters

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by J.R. Mesters. 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 J.R. Mesters. The network helps show where J.R. Mesters may publish in the future.

Co-authorship network of co-authors of J.R. Mesters

This figure shows the co-authorship network connecting the top 25 collaborators of J.R. Mesters. A scholar is included among the top collaborators of J.R. Mesters 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 J.R. Mesters. J.R. Mesters 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.
Galchenkova, M., Oleksandr Yefanov, Johanna Hakanpää, et al.. (2023). JINXED: just in time crystallization for easy structure determination of biological macromolecules. IUCrJ. 10(3). 253–260. 12 indexed citations
2.
Tian, Hui, Gabriel L. Fiorin, Anja Kombrink, J.R. Mesters, & Bart P. H. J. Thomma. (2022). Fungal dual-domain LysM effectors undergo chitin-induced intermolecular, and not intramolecular, dimerization. PLANT PHYSIOLOGY. 190(3). 2033–2044. 10 indexed citations
3.
Tian, Hui, Luis Rodríguez‐Moreno, Grardy C. M. van den Berg, et al.. (2021). Three LysM effectors of Zymoseptoria tritici collectively disarm chitin‐triggered plant immunity. Molecular Plant Pathology. 22(6). 683–693. 37 indexed citations
4.
Sánchez‐Vallet, Andrea, Hui Tian, Luis Rodríguez‐Moreno, et al.. (2020). A secreted LysM effector protects fungal hyphae through chitin-dependent homodimer polymerization. PLoS Pathogens. 16(6). e1008652–e1008652. 53 indexed citations
5.
Snelders, Nick C., Hanna Rövenich, Gabriella C. Petti, et al.. (2020). Microbiome manipulation by a soil-borne fungal plant pathogen using effector proteins. Nature Plants. 6(11). 1365–1374. 151 indexed citations
6.
Brynda, J., Petr Pachl, J.R. Mesters, et al.. (2019). A novel structurally characterized haloacid dehalogenase superfamily phosphatase fromThermococcus thioreducenswith diverse substrate specificity. Acta Crystallographica Section D Structural Biology. 75(8). 743–752. 2 indexed citations
7.
Sánchez‐Vallet, Andrea, J.R. Mesters, & Bart P. H. J. Thomma. (2015). The battle for chitin recognition in plant-microbe interactions. FEMS Microbiology Reviews. 39(2). 171–183. 205 indexed citations
9.
Mesters, J.R., Alena Stsiapanava, Radka Chaloupková, et al.. (2014). Crystallographic analysis of 1,2,3-trichloropropane biodegradation by the haloalkane dehalogenase DhaA31. Acta Crystallographica Section D Biological Crystallography. 70(2). 209–217. 11 indexed citations
10.
Brix, Britta, J.R. Mesters, Luc Pellerin, & Olaf Jöhren. (2012). Endothelial Cell-Derived Nitric Oxide Enhances Aerobic Glycolysis in Astrocytes via HIF-1 -Mediated Target Gene Activation. Journal of Neuroscience. 32(28). 9727–9735. 84 indexed citations
11.
Mesters, J.R., et al.. (2011). Crystal structure of the middle domain of human poly(A)-binding protein-interacting protein 1. Biochemical and Biophysical Research Communications. 408(4). 680–685. 4 indexed citations
12.
Tan, Jinzhi, Clemens Vonrhein, Oliver S. Smart, et al.. (2009). The SARS-unique domain of SARS-CoV contains two macrodomains that bind G-quadruplexes. Acta Crystallographica Section A Foundations of Crystallography. 65(a1). s143–s143. 1 indexed citations
13.
Verschueren, Koen H. G., Ksenia Pumpor, Stefan Anemüller, et al.. (2008). A Structural View of the Inactivation of the SARS Coronavirus Main Proteinase by Benzotriazole Esters. Chemistry & Biology. 15(6). 597–606. 65 indexed citations
14.
Mesters, J.R., J. Brynda, Rita Grandori, et al.. (2007). Crystallization and preliminary diffraction analysis ofEscherichia coliWrbA in complex with its cofactor flavin mononucleotide. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63(7). 571–575. 5 indexed citations
15.
Weber, Jan, J.R. Mesters, Martin Lepšı́k, et al.. (2002). Unusual Binding Mode of an HIV-1 Protease Inhibitor Explains its Potency against Multi-drug-resistant Virus Strains. Journal of Molecular Biology. 324(4). 739–754. 43 indexed citations
16.
Vogeley, Lutz, Gottfried J. Palm, J.R. Mesters, & R. Hilgenfeld. (2001). Conformational Change of Elongation Factor Tu (EF-Tu) Induced by Antibiotic Binding. Journal of Biological Chemistry. 276(20). 17149–17155. 100 indexed citations
17.
Zeef, Leo, J.R. Mesters, Kathy Boon, et al.. (1995). Antibiotic resistance mechanisms of mutant EF-Tu species in Escherichia coli. Biochemistry and Cell Biology. 73(11-12). 1167–1177. 22 indexed citations
18.
Bilgin, N., Carsten Lindschau, J.R. Mesters, et al.. (1995). Phosphorylation of Elongation Factor Tu Prevents Ternary Complex Formation. Journal of Biological Chemistry. 270(24). 14541–14547. 66 indexed citations
19.
Zeef, Leo, J.R. Mesters, Barend Kraal, & Leendert Bosch. (1995). A growth-defective kirromycin-resistant EF-Tu Escherichia coli mutant and a spontaneously evolved suppression of the defect. Gene. 165(1). 39–43. 5 indexed citations
20.
Sweere, A. P. J., et al.. (1988). Experimental simulation of oxygen profiles and their influence on baker's yeast production: I. One‐fermentor system. Biotechnology and Bioengineering. 31(6). 567–578. 61 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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