T. A. Chubar

407 total citations
26 papers, 345 citations indexed

About

T. A. Chubar is a scholar working on Molecular Biology, Plant Science and Electrical and Electronic Engineering. According to data from OpenAlex, T. A. Chubar has authored 26 papers receiving a total of 345 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 9 papers in Plant Science and 5 papers in Electrical and Electronic Engineering. Recurrent topics in T. A. Chubar's work include Enzyme-mediated dye degradation (7 papers), Electrochemical sensors and biosensors (5 papers) and Enzyme Structure and Function (5 papers). T. A. Chubar is often cited by papers focused on Enzyme-mediated dye degradation (7 papers), Electrochemical sensors and biosensors (5 papers) and Enzyme Structure and Function (5 papers). T. A. Chubar collaborates with scholars based in Russia, United States and Tajikistan. T. A. Chubar's co-authors include Irina G. Gazaryan, В. И. Тишков, Dmitry M. Hushpulian, Ivan Yu. Sakharov, Igor Yu. Galaev, Jaime Castillo, Elisabeth Csöregi, Lo Gorton, Elena E. Ferapontova and John J. Castillo and has published in prestigious journals such as Biochemical and Biophysical Research Communications, Electrochemistry Communications and Plant Science.

In The Last Decade

T. A. Chubar

24 papers receiving 337 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
T. A. Chubar Russia 11 169 123 107 64 46 26 345
George W. Robinson United States 9 206 1.2× 33 0.3× 31 0.3× 41 0.6× 32 0.7× 12 387
Parveen Kumar India 11 224 1.3× 39 0.3× 315 2.9× 96 1.5× 175 3.8× 13 565
Rohit Sharma India 8 175 1.0× 30 0.2× 51 0.5× 10 0.2× 48 1.0× 42 301
Haruyo Hatanaka Japan 11 250 1.5× 113 0.9× 38 0.4× 18 0.3× 80 1.7× 16 386
Ingo Krest Germany 11 151 0.9× 236 1.9× 56 0.5× 20 0.3× 32 0.7× 12 373
Jidong Wang China 12 199 1.2× 69 0.6× 20 0.2× 9 0.1× 21 0.5× 30 342
G Marcozzi Italy 11 152 0.9× 68 0.6× 27 0.3× 11 0.2× 28 0.6× 33 368
Sivakumar Allur Subramaniyan South Korea 12 188 1.1× 18 0.1× 43 0.4× 37 0.6× 69 1.5× 20 517
Joannès Nari France 13 353 2.1× 388 3.2× 35 0.3× 21 0.3× 32 0.7× 21 625
Shiying Zou China 12 248 1.5× 132 1.1× 65 0.6× 11 0.2× 39 0.8× 24 528

Countries citing papers authored by T. A. Chubar

Since Specialization
Citations

This map shows the geographic impact of T. A. Chubar'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 T. A. Chubar with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites T. A. Chubar more than expected).

Fields of papers citing papers by T. A. Chubar

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of T. A. Chubar

This figure shows the co-authorship network connecting the top 25 collaborators of T. A. Chubar. A scholar is included among the top collaborators of T. A. Chubar 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 T. A. Chubar. T. A. Chubar 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.
Тишков, В. И., et al.. (2025). Effect of the C-terminal sequence on the catalytic properties and thermal stability of bacterial formate dehydrogenase. Russian Chemical Bulletin. 74(8). 2485–2493.
2.
Hushpulian, Dmitry M., Irina N. Gaisina, С. В. Никулин, et al.. (2024). High Throughput Screening in Drug Discovery: Problems and Solutions. Moscow University Chemistry Bulletin. 79(2). 93–104. 3 indexed citations
3.
Савин, С. С., et al.. (2023). Engineering the N-Terminal Sequence of Glycine max Soybean Formate Dehydrogenase. Moscow University Chemistry Bulletin. 78(4). 220–229. 1 indexed citations
4.
Hushpulian, Dmitry M., et al.. (2021). Fast Responding Genes to HIF Prolyl Hydroxylase Inhibitors. Moscow University Chemistry Bulletin. 76(2). 114–121. 1 indexed citations
5.
Hushpulian, Dmitry M., N. A. Smirnova, T. A. Chubar, et al.. (2020). Optimization of Neh2-Luc Reporter for Screening of Activators of Antioxidant Program. Moscow University Chemistry Bulletin. 75(3). 172–178. 1 indexed citations
6.
Filatova, Lyubov Y., et al.. (2019). Kinetics of inactivation of staphylolytic enzymes: Qualitative and quantitative description. Biochimie. 162. 77–87. 2 indexed citations
7.
Smirnova, N. A., Dmitry M. Hushpulian, С. В. Никулин, et al.. (2018). HIF2 ODD-luciferase reporter: the most sensitive assay for HIF prolyl hydroxylase inhibitors. Russian Chemical Bulletin. 67(1). 150–156. 4 indexed citations
8.
Smirnova, N. A., Dmitry M. Hushpulian, С. В. Никулин, et al.. (2017). Enzyme–substrate reporters for evaluation of substrate specificity of HIF prolyl hydroxylase isoforms. Biochemistry (Moscow). 82(10). 1207–1214. 10 indexed citations
9.
Полозников, А. А., N. A. Smirnova, Dmitry M. Hushpulian, et al.. (2017). L-ascorbic acid: A true substrate for HIF prolyl hydroxylase?. Biochimie. 147. 46–54. 23 indexed citations
10.
Filatova, Lyubov Y., David M. Donovan, Juli Foster‐Frey, et al.. (2015). Bacteriophage phi11 lysin: Physicochemical characterization and comparison with phage phi80α lysin. Enzyme and Microbial Technology. 73-74. 51–58. 15 indexed citations
11.
Захарова, Г. С., А. А. Полозников, T. A. Chubar, Irina G. Gazaryan, & В. И. Тишков. (2015). High-yield reactivation of anionic tobacco peroxidase overexpressed in Escherichia coli. Protein Expression and Purification. 113. 85–93. 3 indexed citations
12.
Полозников, А. А., Г. С. Захарова, T. A. Chubar, et al.. (2015). Site-directed mutagenesis of tobacco anionic peroxidase: Effect of additional aromatic amino acids on stability and activity. Biochimie. 115. 71–77. 3 indexed citations
13.
Комарова, Н. В., et al.. (2012). Engineering of substrate specificity of D-amino acid oxidase from the yeast Trigonopsis variabilis: Directed mutagenesis of Phe258 residue. Biochemistry (Moscow). 77(10). 1181–1189. 12 indexed citations
14.
Castillo, John J., Elena E. Ferapontova, Dmitry M. Hushpulian, et al.. (2006). Direct electrochemistry and bioelectrocatalysis of H2O2 reduction of recombinant tobacco peroxidase on graphite. Effect of peroxidase single-point mutation on Ca2+-modulated catalytic activity. Journal of Electroanalytical Chemistry. 588(1). 112–121. 32 indexed citations
15.
Орлова, М. А., T. A. Chubar, О. В. Игнатенко, et al.. (2003). Conformational Differences between Native and Recombinant Horseradish Peroxidase Revealed by Tritium Planigraphy. Biochemistry (Moscow). 68(11). 1225–1230. 6 indexed citations
16.
Hushpulian, Dmitry M., A. Rojkova, T. A. Chubar, et al.. (2003). Expression and Refolding of Tobacco Anionic Peroxidase from E. coli Inclusion Bodies. Biochemistry (Moscow). 68(11). 1189–1194. 22 indexed citations
17.
Castillo, Jaime, et al.. (2002). Purification and substrate specificity of peroxidase from sweet potato tubers. Plant Science. 163(5). 1011–1019. 75 indexed citations
18.
Игнатенко, О. В., et al.. (2000). Catalytic properties of tryptophanless recombinant horseradish peroxidase.. PubMed. 65(5). 583–7. 6 indexed citations
19.
Gazaryan, Irina G., T. A. Chubar, О. В. Игнатенко, et al.. (1999). Tryptophanless Recombinant Horseradish Peroxidase: Stability and Catalytic Properties. Biochemical and Biophysical Research Communications. 262(1). 297–301. 18 indexed citations
20.
Орлова, М. А., et al.. (1998). Effect of calcium and magnesium ions on radiation-induced inactivation of plant peroxidases. Russian Chemical Bulletin. 47(3). 505–509. 2 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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