Ya. E. Dunaevsky

741 total citations
31 papers, 582 citations indexed

About

Ya. E. Dunaevsky is a scholar working on Molecular Biology, Biotechnology and Plant Science. According to data from OpenAlex, Ya. E. Dunaevsky has authored 31 papers receiving a total of 582 indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 18 papers in Biotechnology and 10 papers in Plant Science. Recurrent topics in Ya. E. Dunaevsky's work include Enzyme Production and Characterization (13 papers), Insect Resistance and Genetics (8 papers) and Protein Hydrolysis and Bioactive Peptides (7 papers). Ya. E. Dunaevsky is often cited by papers focused on Enzyme Production and Characterization (13 papers), Insect Resistance and Genetics (8 papers) and Protein Hydrolysis and Bioactive Peptides (7 papers). Ya. E. Dunaevsky collaborates with scholars based in Russia, Tajikistan and United States. Ya. E. Dunaevsky's co-authors include Mikhail A. Belozersky, Elena N. Elpidina, D. P. Zhuzhikov, Brenda Oppert, Konstantin S. Vinokurov, Ts. A. Egorov, G. N. Rudenskaya, V. M. Stepanov, А. В. Кузнецова and Andrea Preusser and has published in prestigious journals such as Biochemical Journal, FEBS Letters and Planta.

In The Last Decade

Ya. E. Dunaevsky

30 papers receiving 555 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ya. E. Dunaevsky Russia 13 401 222 196 153 54 31 582
Milan Osusky Canada 11 345 0.9× 172 0.8× 178 0.9× 29 0.2× 37 0.7× 17 500
Knud Vad Denmark 9 791 2.0× 708 3.2× 159 0.8× 65 0.4× 18 0.3× 13 1.2k
Isabelle Rahioui France 15 287 0.7× 191 0.9× 65 0.3× 229 1.5× 32 0.6× 27 540
Arthur K. Weissinger United States 16 795 2.0× 567 2.6× 316 1.6× 22 0.1× 41 0.8× 26 1.0k
Xiaomin Si China 9 752 1.9× 631 2.8× 70 0.4× 98 0.6× 24 0.4× 13 983
Sylvia de Pater Netherlands 19 937 2.3× 847 3.8× 131 0.7× 54 0.4× 38 0.7× 32 1.3k
Bernd Mechler Germany 12 743 1.9× 107 0.5× 118 0.6× 26 0.2× 53 1.0× 17 870
D. P. Zhuzhikov Russia 11 406 1.0× 198 0.9× 52 0.3× 374 2.4× 13 0.2× 22 604
Xiao‐Ren Chen China 18 233 0.6× 574 2.6× 58 0.3× 29 0.2× 25 0.5× 33 744
Uri Hanania Israel 13 554 1.4× 456 2.1× 238 1.2× 15 0.1× 41 0.8× 19 774

Countries citing papers authored by Ya. E. Dunaevsky

Since Specialization
Citations

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

Fields of papers citing papers by Ya. E. Dunaevsky

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ya. E. Dunaevsky. 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 Ya. E. Dunaevsky. The network helps show where Ya. E. Dunaevsky may publish in the future.

Co-authorship network of co-authors of Ya. E. Dunaevsky

This figure shows the co-authorship network connecting the top 25 collaborators of Ya. E. Dunaevsky. A scholar is included among the top collaborators of Ya. E. Dunaevsky 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 Ya. E. Dunaevsky. Ya. E. Dunaevsky 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.
2.
Korostyleva, Tatyana V., Е. А. Истомина, Ya. E. Dunaevsky, et al.. (2017). Molecular genetic analysis of collection of transgenic tobacco plants with buckwheat serine proteases inhibitor gene during long-term subculture. Russian Journal of Genetics. 53(11). 1200–1210. 1 indexed citations
3.
Кураков, А. В., et al.. (2016). An activity and spectrum of extracellular peptidases in phytopathogenic micromycetes Fusarium anguioides and Fusarium sambucinum. 50(4). 250–256. 3 indexed citations
4.
Dunaevsky, Ya. E., et al.. (2016). Organotrophic bacteria of the Baikal Rift Zone hot springs. Microbiology. 85(3). 367–378. 9 indexed citations
5.
Dunaevsky, Ya. E., et al.. (2015). Some properties and possible biological role of peptidase inhibitors from the entomopathogenic fungus Tolypocladium cylindrosporum. Archives of Microbiology. 197(8). 1001–1010. 1 indexed citations
6.
Dunaevsky, Ya. E., et al.. (2012). Comparative analysis of tobacco and Arabidopsis insertional mutants, transformed with equal vector constructions. Russian Journal of Genetics. 48(2). 170–178. 2 indexed citations
7.
Минеев, Константин С., et al.. (2012). Buckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptides. Biochemical Journal. 446(2). 331–331. 2 indexed citations
8.
Goptar, Irina, Tatiana A. Semashko, E. N. Lysogorskaya, et al.. (2011). Cysteine digestive peptidases function as post-glutamine cleaving enzymes in tenebrionid stored-product pests. Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology. 161(2). 148–154. 30 indexed citations
9.
Намсараев, З. Б., et al.. (2010). Anoxybacillus mongoliensis sp. nov., a novel thermophilic proteinase producing bacterium isolated from alkaline hot spring, Central Mongolia. Microbiology. 79(4). 491–499. 26 indexed citations
10.
Семенова, Т. А., et al.. (2010). Secreted proteinase of entomopathogenic fungus Cordyceps militaris. I. Development of cultivation medium and of purification protocol.. 44(6). 535–541. 1 indexed citations
11.
Dunaevsky, Ya. E., et al.. (2009). The study of two alkaliphilic thermophile bacteria of the Anoxybacillus genus as producers of extracellular proteinase. Applied Biochemistry and Microbiology. 45(5). 484–488. 10 indexed citations
12.
Burmistrova, Olga, et al.. (2008). Isolation and properties of Serratia proteamaculans 94 cysteine protease. Russian Journal of Bioorganic Chemistry. 34(3). 274–279. 7 indexed citations
13.
Dunaevsky, Ya. E., et al.. (2007). Extracellular alkaline proteinase of Colletotrichum gloeosporioides. Biochemistry (Moscow). 72(3). 345–350. 12 indexed citations
14.
Vinokurov, Konstantin S., Elena N. Elpidina, Brenda Oppert, et al.. (2006). Diversity of digestive proteinases in Tenebrio molitor (Coleoptera: Tenebrionidae) larvae. Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology. 145(2). 126–137. 94 indexed citations
15.
Elpidina, Elena N., et al.. (2005). A chymotrypsin-like proteinase from the midgut of larvae. Biochimie. 87(8). 771–779. 62 indexed citations
16.
Dunaevsky, Ya. E., et al.. (2004). New protease inhibitors from buckwheat seeds: properties, partial amino acid sequences and possible biological role. Biological Chemistry. 385(5). 429–34. 15 indexed citations
17.
Rudenskaya, G. N., et al.. (1998). Taraxalisin – a serine proteinase from dandelion Taraxacum officinale Webb s.l. FEBS Letters. 437(3). 237–240. 50 indexed citations
18.
Belozersky, Mikhail A., et al.. (1995). Complete amino acid sequence of the protease inhibitor from buckwheat seeds. FEBS Letters. 371(3). 264–266. 39 indexed citations
19.
Dunaevsky, Ya. E., Mikhail A. Belozersky, & Natalia Voskoboynikova. (1993). In vitro reconstitution of the proteolytic system responsible for hydrolysis of the 13S globulin in buckwheat seeds. FEBS Letters. 324(2). 216–218. 6 indexed citations
20.
Belozersky, Mikhail A., et al.. (1989). Aspartic proteinase from wheat seeds: isolation, properties and action on gliadin. Planta. 177(3). 321–326. 82 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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