Yakov E. Dunaevsky

1.4k total citations
47 papers, 1.1k citations indexed

About

Yakov E. Dunaevsky is a scholar working on Molecular Biology, Food Science and Plant Science. According to data from OpenAlex, Yakov E. Dunaevsky has authored 47 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 15 papers in Food Science and 13 papers in Plant Science. Recurrent topics in Yakov E. Dunaevsky's work include Insect Resistance and Genetics (16 papers), Seed and Plant Biochemistry (13 papers) and Peptidase Inhibition and Analysis (11 papers). Yakov E. Dunaevsky is often cited by papers focused on Insect Resistance and Genetics (16 papers), Seed and Plant Biochemistry (13 papers) and Peptidase Inhibition and Analysis (11 papers). Yakov E. Dunaevsky collaborates with scholars based in Russia, United States and Tajikistan. Yakov E. Dunaevsky's co-authors include Mikhail A. Belozersky, Elena N. Elpidina, Klaus Müntz, Jens Tiedemann, Armin Schlereth, D. P. Zhuzhikov, Brenda Oppert, Konstantin S. Vinokurov, Natalia Voskoboynikova and I. Yu. Filippova and has published in prestigious journals such as SHILAP Revista de lepidopterología, Analytical Biochemistry and Biochemical Journal.

In The Last Decade

Yakov E. Dunaevsky

45 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
Yakov E. Dunaevsky Russia 20 623 555 247 231 169 47 1.1k
Mikhail A. Belozersky Russia 23 831 1.3× 647 1.2× 287 1.2× 354 1.5× 215 1.3× 64 1.4k
Elena N. Elpidina Russia 20 786 1.3× 382 0.7× 553 2.2× 147 0.6× 55 0.3× 51 1.1k
Paula Verı́ssimo Portugal 19 661 1.1× 579 1.0× 82 0.3× 238 1.0× 137 0.8× 34 1.2k
Rafaél I. Monsalve Spain 25 445 0.7× 225 0.4× 163 0.7× 171 0.7× 150 0.9× 47 1.8k
Pilar Carbonero Spain 36 2.3k 3.7× 2.9k 5.2× 179 0.7× 504 2.2× 92 0.5× 64 3.6k
Richard F. Barker United Kingdom 23 1.8k 2.9× 1.5k 2.8× 427 1.7× 528 2.3× 69 0.4× 25 2.5k
Khalil Elmorjani France 18 525 0.8× 544 1.0× 39 0.2× 96 0.4× 161 1.0× 25 1.0k
Andrei D. Shutov Moldova 17 528 0.8× 816 1.5× 22 0.1× 267 1.2× 237 1.4× 35 1.2k
Gloria García‐Casado Spain 26 1.8k 2.9× 3.6k 6.5× 1.5k 6.2× 256 1.1× 97 0.6× 39 4.9k
Aldo Ceriotti Italy 26 1.3k 2.0× 864 1.6× 23 0.1× 800 3.5× 79 0.5× 62 2.1k

Countries citing papers authored by Yakov E. Dunaevsky

Since Specialization
Citations

This map shows the geographic impact of Yakov 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 Yakov 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 Yakov E. Dunaevsky more than expected).

Fields of papers citing papers by Yakov E. Dunaevsky

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

This figure shows the co-authorship network connecting the top 25 collaborators of Yakov E. Dunaevsky. A scholar is included among the top collaborators of Yakov 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 Yakov E. Dunaevsky. Yakov 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.
Vinokurov, Konstantin S., et al.. (2024). The Set of Serine Peptidases of the Tenebrio molitor Beetle: Transcriptomic Analysis on Different Developmental Stages. International Journal of Molecular Sciences. 25(11). 5743–5743.
2.
Gerasimov, Evgeny S., et al.. (2023). Dynamics of Podospora anserina Genome Evolution in a Long-Term Experiment. International Journal of Molecular Sciences. 24(15). 12009–12009.
3.
Serebryakova, Marina V., et al.. (2022). Recombinant Cathepsin L of Tribolium castaneum and Its Potential in the Hydrolysis of Immunogenic Gliadin Peptides. International Journal of Molecular Sciences. 23(13). 7001–7001. 4 indexed citations
4.
Oppert, Brenda, et al.. (2021). The dataset of predicted trypsin serine peptidases and their inactive homologs in Tenebrio molitor transcriptomes. SHILAP Revista de lepidopterología. 38. 107301–107301. 3 indexed citations
5.
Dunaevsky, Yakov E., et al.. (2020). Human proline specific peptidases: A comprehensive analysis. Biochimica et Biophysica Acta (BBA) - General Subjects. 1864(9). 129636–129636. 28 indexed citations
6.
Elpidina, Elena N., Tatiana A. Semashko, Yakov E. Dunaevsky, et al.. (2018). Direct detection of cysteine peptidases for MALDI-TOF MS analysis using fluorogenic substrates. Analytical Biochemistry. 567. 45–50. 4 indexed citations
7.
Goptar, Irina, D. P. Zhuzhikov, Marina V. Serebryakova, et al.. (2016). Dipeptidyl peptidase 4 – An important digestive peptidase in Tenebrio molitor larvae. Insect Biochemistry and Molecular Biology. 76. 38–48. 16 indexed citations
8.
Semashko, Tatiana A., Konstantin S. Vinokurov, Yakov E. Dunaevsky, et al.. (2014). Selective chromogenic and fluorogenic peptide substrates for the assay of cysteine peptidases in complex mixtures. Analytical Biochemistry. 449. 179–187. 12 indexed citations
9.
10.
Goptar, Irina, Dmitry A. Shagin, Irina A. Shagina, et al.. (2013). A digestive prolyl carboxypeptidase in Tenebrio molitor larvae. Insect Biochemistry and Molecular Biology. 43(6). 501–509. 19 indexed citations
11.
Dunaevsky, Yakov E., et al.. (2010). Novel cathepsin L-like protease from dermestid beetle Dermestes frischii maggot. Biochimie. 93(2). 141–148. 4 indexed citations
12.
Dunaevsky, Yakov E., et al.. (2009). Trypsin-like proteins of the fungi as possible markers of pathogenicity. Fungal Biology. 114(2-3). 151–159. 36 indexed citations
13.
Goptar, Irina, I. Yu. Filippova, E. N. Lysogorskaya, et al.. (2007). Localization of post-proline cleaving peptidases in Tenebrio molitor larval midgut. Biochimie. 90(3). 508–514. 10 indexed citations
14.
Vinokurov, Konstantin S., Elena N. Elpidina, Brenda Oppert, et al.. (2006). Fractionation of digestive proteinases from Tenebrio molitor (Coleoptera: Tenebrionidae) larvae and role in protein digestion. Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology. 145(2). 138–146. 38 indexed citations
15.
Vinokurov, Konstantin S., et al.. (2005). Participation of different digestive proteinases of the yellow mealworm, Tenebrio molitor, in initial stages of hydrolysis of the main dietary protein. FEBS Journal. 272. 153–153. 1 indexed citations
16.
Dunaevsky, Yakov E., et al.. (2005). Digestive proteinases of yellow mealworm (Tenebrio molitor) larvae: Purification and characterization of a trypsin-like proteinase. Biochemistry (Moscow). 70(3). 300–305. 52 indexed citations
17.
Dunaevsky, Yakov E., et al.. (2004). Cationic Inhibitors of Serine Proteinases from Buckwheat Seeds: Study of Their Interaction with Exogenous Proteinases. Biochemistry (Moscow). 69(4). 441–444. 2 indexed citations
18.
Elpidina, Elena N., et al.. (2001). Proteinase inhibitors in Nauphoeta cinerea midgut. Archives of Insect Biochemistry and Physiology. 48(4). 217–222. 10 indexed citations
19.
Müntz, Klaus, Mikhail A. Belozersky, Yakov E. Dunaevsky, Armin Schlereth, & Jens Tiedemann. (2001). Stored proteinases and the initiation of storage protein mobilization in seeds during germination and seedling growth. Journal of Experimental Botany. 52(362). 1741–1752. 222 indexed citations
20.
Dunaevsky, Yakov E., et al.. (1996). Isolation and properties of anionic protease inhibitors from buckwheat seeds. IUBMB Life. 40(1). 199–208. 10 indexed citations

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