Jan Dohnálek

1.5k total citations
73 papers, 1.1k citations indexed

About

Jan Dohnálek is a scholar working on Molecular Biology, Materials Chemistry and Biotechnology. According to data from OpenAlex, Jan Dohnálek has authored 73 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 52 papers in Molecular Biology, 20 papers in Materials Chemistry and 18 papers in Biotechnology. Recurrent topics in Jan Dohnálek's work include Enzyme Structure and Function (20 papers), Enzyme Production and Characterization (13 papers) and Protein Structure and Dynamics (11 papers). Jan Dohnálek is often cited by papers focused on Enzyme Structure and Function (20 papers), Enzyme Production and Characterization (13 papers) and Protein Structure and Dynamics (11 papers). Jan Dohnálek collaborates with scholars based in Czechia, Denmark and United Kingdom. Jan Dohnálek's co-authors include Tereza Skálová, Jindřich Hašek, Jarmila Dušková, Petr Kolenko, T. Kovaĺ, Petra Lipovová, Lars Østergaard, Vojtěch Spiwok, Blanka Králová and Peter R. Østergaard and has published in prestigious journals such as Journal of the American Chemical Society, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Jan Dohnálek

70 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jan Dohnálek Czechia 20 663 197 188 179 129 73 1.1k
Tereza Skálová Czechia 16 424 0.6× 116 0.6× 145 0.8× 155 0.9× 100 0.8× 43 787
Yeon Gyu Yu South Korea 20 790 1.2× 203 1.0× 90 0.5× 109 0.6× 67 0.5× 73 1.2k
Da‐Cheng Wang China 20 544 0.8× 117 0.6× 66 0.4× 133 0.7× 154 1.2× 55 1.1k
L. Chantalat France 16 805 1.2× 172 0.9× 188 1.0× 87 0.5× 64 0.5× 27 1.2k
Saul Treviño United States 10 1.2k 1.8× 364 1.8× 127 0.7× 87 0.5× 62 0.5× 11 1.7k
Harumi Fukada Japan 22 1.3k 2.0× 246 1.2× 285 1.5× 181 1.0× 65 0.5× 65 1.8k
Georg Zocher Germany 25 1.3k 2.0× 263 1.3× 129 0.7× 149 0.8× 140 1.1× 44 2.0k
Ingar Leiros Norway 21 1.3k 2.0× 241 1.2× 115 0.6× 104 0.6× 109 0.8× 49 1.7k
Jozef Ševčı́k Slovakia 16 891 1.3× 284 1.4× 185 1.0× 118 0.7× 39 0.3× 34 1.3k
Gerrit G. Langer Germany 5 1.1k 1.6× 451 2.3× 138 0.7× 107 0.6× 80 0.6× 8 1.5k

Countries citing papers authored by Jan Dohnálek

Since Specialization
Citations

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

Fields of papers citing papers by Jan Dohnálek

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jan Dohnálek

This figure shows the co-authorship network connecting the top 25 collaborators of Jan Dohnálek. A scholar is included among the top collaborators of Jan Dohnálek 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 Jan Dohnálek. Jan Dohnálek 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.
Dohnálek, Jan, Jana Škerlová, Stancho Stanchev, et al.. (2024). Extensive targeting of chemical space at the prime side of ketoamide inhibitors of rhomboid proteases by branched substituents empowers their selectivity and potency. European Journal of Medicinal Chemistry. 275. 116606–116606. 2 indexed citations
2.
Kovaĺ, T., et al.. (2023). A highly active S1‐P1 nuclease from the opportunistic pathogen Stenotrophomonas maltophilia cleaves c‐di‐GMP. FEBS Letters. 597(16). 2103–2118. 2 indexed citations
3.
Kovaĺ, T., Lars Østergaard, Jarmila Dušková, et al.. (2022). Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects. Acta Crystallographica Section D Structural Biology. 78(10). 1194–1209. 2 indexed citations
4.
Dohnálek, Jan, Jarmila Dušková, Galina Tishchenko, et al.. (2021). Chitinase Chit62J4 Essential for Chitin Processing by Human Microbiome Bacterium Clostridium paraputrificum J4. Molecules. 26(19). 5978–5978. 6 indexed citations
5.
Østergaard, Lars, Tereza Skálová, Kirk Schnorr, et al.. (2021). Crystallographic fragment screening-based study of a novel FAD-dependent oxidoreductase from Chaetomium thermophilum. Acta Crystallographica Section D Structural Biology. 77(6). 755–775. 6 indexed citations
6.
Malý, Martin, Kay Diederichs, Jan Dohnálek, & Petr Kolenko. (2021). PAIREF : paired refinement also for Phenix users. KOPS (University of Konstanz). 3 indexed citations
7.
Malý, Martin, Kay Diederichs, Jan Dohnálek, & Petr Kolenko. (2020). Paired refinement under the control ofPAIREF. IUCrJ. 7(4). 681–692. 24 indexed citations
8.
Kouba, Tomáš, T. Kovaĺ, Jarmila Hnilicová, et al.. (2020). Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase. Nature Communications. 11(1). 6419–6419. 22 indexed citations
9.
Srb, Pavel, Hana Šanderová, Libor Krásný, et al.. (2019). Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase. Journal of the American Chemical Society. 141(42). 16817–16828. 10 indexed citations
10.
Kovaĺ, T., Lars Østergaard, Tereza Skálová, et al.. (2019). Trp–His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer. Scientific Reports. 9(1). 13700–13700. 11 indexed citations
11.
Agirre, Jon, A. Ariza, Wendy A. Offen, et al.. (2016). Three-dimensional structures of two heavily N-glycosylatedAspergillussp. family GH3 β-D-glucosidases. Acta Crystallographica Section D Structural Biology. 72(2). 254–265. 40 indexed citations
12.
Kádek, Alan, et al.. (2015). Crystallization of nepenthesin I using a low-pH crystallization screen. Acta Crystallographica Section F Structural Biology Communications. 72(1). 24–28. 6 indexed citations
13.
Stsiapanava, Alena, Jan Dohnálek, Michal Kutý, et al.. (2010). Atomic resolution studies of haloalkane dehalogenases DhaA04, DhaA14 and DhaA15 with engineered access tunnels. Acta Crystallographica Section D Biological Crystallography. 66(9). 962–969. 13 indexed citations
14.
Dohnálek, Jan, et al.. (2010). Structure analysis of group I plant nucleases. Journal of Synchrotron Radiation. 18(1). 29–30. 4 indexed citations
15.
Skálová, Tereza, Jan Dohnálek, Lars Østergaard, et al.. (2008). Structure of laccase fromStreptomyces coelicolor. Acta Crystallographica Section A Foundations of Crystallography. 64(a1). C351–C351. 1 indexed citations
16.
Skálová, Tereza, Jan Dohnálek, Lars Østergaard, et al.. (2008). The Structure of the Small Laccase from Streptomyces coelicolor Reveals a Link between Laccases and Nitrite Reductases. Journal of Molecular Biology. 385(4). 1165–1178. 123 indexed citations
17.
Skálová, Tereza, Jan Dohnálek, Lars Østergaard, et al.. (2007). Crystallization and preliminary X-ray diffraction analysis of the small laccase fromStreptomyces coelicolor. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63(12). 1077–1079. 15 indexed citations
18.
Skálová, Tereza, Jindřich Hašek, Jan Dohnálek, et al.. (2003). An Ethylenamine Inhibitor Binds Tightly to Both Wild Type and Mutant HIV-1 Proteases. Structure and Energy Study. Journal of Medicinal Chemistry. 46(9). 1636–1644. 8 indexed citations
19.
Dohnálek, Jan, Jindřich Hašek, Jarmila Dušková, et al.. (2002). Hydroxyethylamine Isostere of an HIV-1 Protease Inhibitor Prefers Its Amine to the Hydroxy Group in Binding to Catalytic Aspartates. A Synchrotron Study of HIV-1 Protease in Complex with a Peptidomimetic Inhibitor. Journal of Medicinal Chemistry. 45(7). 1432–1438. 15 indexed citations
20.
Phillips, Christopher, Jan Dohnálek, S. Gover, Michael P. Barrett, & Margaret Adams. (1998). A 2.8 Å resolution structure of 6-phosphogluconate dehydrogenase from the protozoan parasite Trypanosoma brucei : comparison with the sheep enzyme accounts for differences in activity with coenzyme and substrate analogues 1 1Edited by R. Huber. Journal of Molecular Biology. 282(3). 667–681. 48 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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