Michael Kotik

1.5k total citations
42 papers, 1.1k citations indexed

About

Michael Kotik is a scholar working on Molecular Biology, Nutrition and Dietetics and Biotechnology. According to data from OpenAlex, Michael Kotik has authored 42 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 10 papers in Nutrition and Dietetics and 10 papers in Biotechnology. Recurrent topics in Michael Kotik's work include Microbial Metabolic Engineering and Bioproduction (14 papers), Enzyme Catalysis and Immobilization (12 papers) and Microbial Metabolites in Food Biotechnology (9 papers). Michael Kotik is often cited by papers focused on Microbial Metabolic Engineering and Bioproduction (14 papers), Enzyme Catalysis and Immobilization (12 papers) and Microbial Metabolites in Food Biotechnology (9 papers). Michael Kotik collaborates with scholars based in Czechia, Belarus and France. Michael Kotik's co-authors include Pavel Kyslı́k, Alain Archelas, Ludmila Martı́nková, Vladimı́r Křen, Ladislav Homolka, Sheena E. Radford, H. Zuber, Roland Wohlgemuth, Helena Marešová and Helena Pelantová and has published in prestigious journals such as Journal of Molecular Biology, The Science of The Total Environment and Biochemistry.

In The Last Decade

Michael Kotik

42 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
Michael Kotik Czechia 20 763 164 160 133 129 42 1.1k
Nicole G. H. Leferink United Kingdom 22 991 1.3× 144 0.9× 155 1.0× 129 1.0× 256 2.0× 32 1.4k
Martha S. Smit South Africa 20 1.1k 1.5× 73 0.4× 162 1.0× 450 3.4× 152 1.2× 56 1.6k
Noriyuki Doukyu Japan 19 1.1k 1.4× 87 0.5× 359 2.2× 191 1.4× 133 1.0× 42 1.3k
Baixue Lin China 16 748 1.0× 97 0.6× 119 0.7× 284 2.1× 58 0.4× 38 1.1k
Marie Dominique Legoy France 23 870 1.1× 58 0.4× 213 1.3× 241 1.8× 78 0.6× 59 1.2k
W. J. J. van den Tweel Netherlands 19 579 0.8× 84 0.5× 85 0.5× 114 0.9× 47 0.4× 45 814
Ee Lui Ang Singapore 26 1.4k 1.9× 93 0.6× 275 1.7× 323 2.4× 144 1.1× 62 2.0k
Marianne Graber France 22 699 0.9× 42 0.3× 117 0.7× 192 1.4× 100 0.8× 50 1.1k
Stephanie Bringer‐Meyer Germany 25 1.6k 2.1× 164 1.0× 102 0.6× 309 2.3× 98 0.8× 35 1.9k
Sabine Lutz‐Wahl Germany 17 655 0.9× 38 0.2× 157 1.0× 112 0.8× 57 0.4× 31 937

Countries citing papers authored by Michael Kotik

Since Specialization
Citations

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

Fields of papers citing papers by Michael Kotik

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Michael Kotik

This figure shows the co-authorship network connecting the top 25 collaborators of Michael Kotik. A scholar is included among the top collaborators of Michael Kotik 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 Michael Kotik. Michael Kotik 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.
Martı́nková, Ludmila, Natalia Kulik, Lenka Rucká, et al.. (2024). Biotransformation of free cyanide to formic acid by a cyanide hydratase−formamidase cascade reaction. Process Biochemistry. 142. 62–67. 2 indexed citations
2.
Martı́nková, Ludmila, et al.. (2024). Aldoxime dehydratases: production, immobilization, and use in multistep processes. Applied Microbiology and Biotechnology. 108(1). 518–518. 1 indexed citations
3.
Kotik, Michael, Natalia Kulik, & Kateřina Valentová. (2023). Flavonoids as Aglycones in Retaining Glycosidase-Catalyzed Reactions: Prospects for Green Chemistry. Journal of Agricultural and Food Chemistry. 71(41). 14890–14910. 19 indexed citations
4.
Bojarová, Pavla, Natalia Kulik, Kristýna Slámová, et al.. (2019). Selective β-N-acetylhexosaminidase from Aspergillus versicolor—a tool for producing bioactive carbohydrates. Applied Microbiology and Biotechnology. 103(4). 1737–1753. 16 indexed citations
5.
Mazzaferro, Laura S., et al.. (2019). The flavonoid degrading fungus Acremonium sp. DSM 24697 produces two diglycosidases with different specificities. Applied Microbiology and Biotechnology. 103(23-24). 9493–9504. 13 indexed citations
6.
Rucká, Lenka, Petr Novotný, Lucie Petrásková, et al.. (2018). Overproduction and characterization of the first enzyme of a new aldoxime dehydratase family in Bradyrhizobium sp.. International Journal of Biological Macromolecules. 115. 746–753. 21 indexed citations
7.
Pachl, Petr, Jana Škerlová, Daniela Šimčíková, et al.. (2018). Crystal structure of native α-L-rhamnosidase from Aspergillus terreus. Acta Crystallographica Section D Structural Biology. 74(11). 1078–1084. 19 indexed citations
8.
Kotik, Michael, et al.. (2017). Metagenome-derived haloalkane dehalogenases with novel catalytic properties. Applied Microbiology and Biotechnology. 101(16). 6385–6397. 8 indexed citations
9.
Martı́nková, Ludmila, et al.. (2016). Biodegradation of phenolic compounds by Basidiomycota and its phenol oxidases: A review. Chemosphere. 149. 373–382. 123 indexed citations
10.
Archelas, Alain, Wei Zhao, Bruno Faure, Gilles Iacazio, & Michael Kotik. (2015). Epoxide hydrolase-catalyzed enantioselective conversion of trans -stilbene oxide: Insights into the reaction mechanism from steady-state and pre-steady-state enzyme kinetics. Archives of Biochemistry and Biophysics. 591. 66–75. 6 indexed citations
11.
Kotik, Michael, Anna Davidová, Jana Voříšková, & Petr Baldrián. (2013). Bacterial communities in tetrachloroethene-polluted groundwaters: A case study. The Science of The Total Environment. 454-455. 517–527. 55 indexed citations
12.
Kotik, Michael, et al.. (2011). Laboratory evolution of an epoxide hydrolase – Towards an enantioconvergent biocatalyst. Journal of Biotechnology. 156(1). 1–10. 28 indexed citations
14.
Kotik, Michael, et al.. (2005). Novel microbial epoxide hydrolases for biohydrolysis of glycidyl derivatives. Journal of Biotechnology. 120(4). 364–375. 35 indexed citations
15.
Kotik, Michael & Pavel Kyslı́k. (2005). Purification and characterisation of a novel enantioselective epoxide hydrolase from Aspergillus niger M200. Biochimica et Biophysica Acta (BBA) - General Subjects. 1760(2). 245–252. 28 indexed citations
16.
Kotik, Michael, et al.. (2004). High-level expression of a fungal pyranose oxidase in high cell-density fed-batch cultivations of Escherichia coli using lactose as inducer. Protein Expression and Purification. 36(1). 61–69. 25 indexed citations
17.
Parrado, Juan, Francisco Conejero‐Lara, Michael Kotik, et al.. (1996). Molecular characterisation of a thermoactive β-1,3-glucanase from Oerskovia xanthineolytica. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1296(2). 145–151. 12 indexed citations
18.
Kotik, Michael, Sheena E. Radford, & Christopher M. Dobson. (1995). Comparison of the Refolding Hen Lysozyme from Dimethyl Sulfoxide and Guanidinium Chloride. Biochemistry. 34(5). 1714–1724. 41 indexed citations
19.
Yang, Jenny J., Matthias Buck, Maureen Pitkeathly, et al.. (1995). Conformational Properties of Four Peptides Spanning the Sequence of Hen Lysozyme. Journal of Molecular Biology. 252(4). 483–491. 104 indexed citations
20.
Kotik, Michael & H. Zuber. (1992). Evidence for temperature-dependent conformational changes in the L-lactate dehydrogenase from Bacillus stearothermophilus. Biochemistry. 31(34). 7787–7795. 21 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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