A. A. Leontievsky

2.0k total citations
58 papers, 1.5k citations indexed

About

A. A. Leontievsky is a scholar working on Plant Science, Biotechnology and Pollution. According to data from OpenAlex, A. A. Leontievsky has authored 58 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 44 papers in Plant Science, 29 papers in Biotechnology and 17 papers in Pollution. Recurrent topics in A. A. Leontievsky's work include Enzyme-mediated dye degradation (36 papers), Microbial Metabolism and Applications (19 papers) and Pesticide and Herbicide Environmental Studies (14 papers). A. A. Leontievsky is often cited by papers focused on Enzyme-mediated dye degradation (36 papers), Microbial Metabolism and Applications (19 papers) and Pesticide and Herbicide Environmental Studies (14 papers). A. A. Leontievsky collaborates with scholars based in Russia, United Kingdom and Czechia. A. A. Leontievsky's co-authors include L. A. Golovleva, I. T. Ermakova, T. V. Shushkova, Nina M. Myasoedova, A. V. Lisov, А. В. Свиридов, A. G. Zavarzına, N. N. Pozdnyakova, D. O. Epiktetov and Ivanova Ev and has published in prestigious journals such as PLoS ONE, FEBS Letters and International Journal of Molecular Sciences.

In The Last Decade

A. A. Leontievsky

58 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
A. A. Leontievsky Russia 20 1.1k 622 502 180 176 58 1.5k
N. N. Pozdnyakova Russia 18 750 0.7× 371 0.6× 383 0.8× 111 0.6× 175 1.0× 45 1.0k
Rui Zhuo China 18 827 0.8× 334 0.5× 398 0.8× 168 0.9× 253 1.4× 26 1.3k
Pavla Erbanová Czechia 16 744 0.7× 535 0.9× 325 0.6× 96 0.5× 293 1.7× 18 1.1k
Ladislav Homolka Czechia 20 884 0.8× 186 0.3× 371 0.7× 161 0.9× 214 1.2× 46 1.2k
Ivana Eichlerová Czechia 19 892 0.8× 154 0.2× 374 0.7× 141 0.8× 191 1.1× 29 1.3k
Christiane Liers Germany 20 1.2k 1.1× 145 0.2× 525 1.0× 376 2.1× 155 0.9× 47 1.6k
Tushar Kanti Maiti India 26 1.3k 1.2× 461 0.7× 194 0.4× 431 2.4× 280 1.6× 63 2.2k
H. P. Molitoris Germany 17 560 0.5× 194 0.3× 299 0.6× 246 1.4× 90 0.5× 37 995
Jolanta Luterek Poland 11 773 0.7× 108 0.2× 445 0.9× 126 0.7× 62 0.4× 21 986
Étienne Odier France 17 884 0.8× 165 0.3× 521 1.0× 125 0.7× 122 0.7× 30 1.2k

Countries citing papers authored by A. A. Leontievsky

Since Specialization
Citations

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

Fields of papers citing papers by A. A. Leontievsky

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of A. A. Leontievsky

This figure shows the co-authorship network connecting the top 25 collaborators of A. A. Leontievsky. A scholar is included among the top collaborators of A. A. Leontievsky 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 A. A. Leontievsky. A. A. Leontievsky 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.
Gabdulkhakov, Azat, K. Egorov, Svetlana Tishchenko, et al.. (2024). Site-Directed Mutagenesis of Two-Domain Laccase ScaSL for Obtaining a Biocatalyst with Improved Characteristics. Catalysts. 14(10). 694–694. 2 indexed citations
2.
Lisov, A. V., et al.. (2023). Two β-glucanases from bacterium Cellulomonas flavigena : expression in Pichia pastoris , properties, biotechnological potential. Preparative Biochemistry & Biotechnology. 53(10). 1313–1321. 1 indexed citations
3.
Epiktetov, D. O., et al.. (2023). Phosphonatase Operons of Organophosphonate-Degrading Soil Bacteria of the Genus Achromobacter. Microbiology. 92(S1). S45–S49. 1 indexed citations
4.
Lisov, A. V., et al.. (2023). A Novel Two-Domain Laccase with Middle Redox Potential: Physicochemical and Structural Properties. Biochemistry (Moscow). 88(10). 1658–1667. 3 indexed citations
5.
Zavarzına, A. G., et al.. (2022). Heterophase Synthesis of Humic Substances at Low Substrate Concentrations and Flow-Through Conditions. Eurasian Soil Science. 55(7). 911–925. 1 indexed citations
6.
7.
Tishchenko, Svetlana, et al.. (2015). Crystallization and X-ray diffraction studies of a two-domain laccase fromStreptomyces griseoflavus. Acta Crystallographica Section F Structural Biology Communications. 71(9). 1200–1204. 6 indexed citations
8.
Shushkova, T. V., Б. П. Баскунов, N. F. Zelenkova, et al.. (2015). Glyphosate acetylation as a specific trait of Achromobacter sp. Kg 16 physiology. Applied Microbiology and Biotechnology. 100(2). 847–855. 17 indexed citations
9.
Tishchenko, Svetlana, et al.. (2015). Structural and functional characterization of two-domain laccase from Streptomyces viridochromogenes. Biochimie. 112. 151–159. 49 indexed citations
10.
Lisov, A. V., et al.. (2014). Xylanase and cellulase of fungus Cerrena unicolor VKM F-3196: Production, properties, and applications for the saccharification of plant material. Applied Biochemistry and Microbiology. 50(2). 148–153. 18 indexed citations
11.
Свиридов, А. В., N. F. Zelenkova, N. G. Vinokurova, I. T. Ermakova, & A. A. Leontievsky. (2011). New approaches to identification and activity estimation of glyphosate degradation enzymes. Biochemistry (Moscow). 76(6). 720–725. 11 indexed citations
12.
Gabdulkhakov, Azat, et al.. (2011). Purification, crystallization and preliminary X-ray structure analysis of the laccase fromGanoderma lucidum. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(8). 926–929. 8 indexed citations
13.
Lisov, A. V., et al.. (2010). Two laccase isoforms of the basidiomycete Cerrena unicolor VKMF‐3196. Induction, isolation and properties. Journal of Basic Microbiology. 50(1). 72–82. 38 indexed citations
14.
Lisov, A. V., A. A. Leontievsky, & L. A. Golovleva. (2007). Hybrid Mn-peroxidases from basidiomycetes. Applied Biochemistry and Microbiology. 43(5). 536–543. 6 indexed citations
15.
Keshavarz, Tajalli, et al.. (2003). Transformation of high concentrations of chlorophenols by the white-rot basidiomycete Trametes versicolor immobilized on nylon mesh. Electronic Journal of Biotechnology. 6(2). 104–114. 37 indexed citations
16.
Lisov, A. V., A. A. Leontievsky, & L. A. Golovleva. (2003). Hybrid Mn-Peroxidase from the Ligninolytic Fungus Panus tigrinus 8/18. Isolation, Substrate Specificity, and Catalytic Cycle. Biochemistry (Moscow). 68(9). 1027–1035. 20 indexed citations
17.
Leontievsky, A. A., et al.. (2002). Adaptation of the white-rot basidiomycete Panus tigrinus for transformation of high concentrations of chlorophenols. Applied Microbiology and Biotechnology. 59(4-5). 599–604. 29 indexed citations
18.
Leontievsky, A. A., Nina M. Myasoedova, Б. П. Баскунов, et al.. (2001). Transformation of 2,4,6-trichlorophenol by free and immobilized fungal laccase. Applied Microbiology and Biotechnology. 57(1-2). 85–91. 58 indexed citations
19.
Leontievsky, A. A., Nina M. Myasoedova, & L. A. Golovleva. (1994). Production of ligninolytic enzymes of the white rot fungus Panus tigrinus. Journal of Biotechnology. 32(3). 299–307. 21 indexed citations
20.
Mal’tseva, O. V., Marja‐Leena Niku‐Paavola, A. A. Leontievsky, Nina M. Myasoedova, & L. A. Golovleva. (1991). Ligninolytic enzymes of the white rot fungus Panus tigrinus. Biotechnology and Applied Biochemistry. 13(3). 291–302. 66 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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