Andrey Rogachev

1.6k total citations
56 papers, 890 citations indexed

About

Andrey Rogachev is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Andrey Rogachev has authored 56 papers receiving a total of 890 indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 15 papers in Materials Chemistry and 10 papers in Spectroscopy. Recurrent topics in Andrey Rogachev's work include Mass Spectrometry Techniques and Applications (9 papers), Protein Structure and Dynamics (8 papers) and RNA and protein synthesis mechanisms (8 papers). Andrey Rogachev is often cited by papers focused on Mass Spectrometry Techniques and Applications (9 papers), Protein Structure and Dynamics (8 papers) and RNA and protein synthesis mechanisms (8 papers). Andrey Rogachev collaborates with scholars based in Russia, France and Germany. Andrey Rogachev's co-authors include A. I. Kuklin, Dmytro Soloviov, Valentin Gordeliy, Oleksandr I. Ivankov, Yu. S. Kovalev, A.V. Vlasov, Valentin Borshchevskiy, T. N. Murugova, Ivan Gushchin and Olga E. Philippova and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Langmuir and Scientific Reports.

In The Last Decade

Andrey Rogachev

52 papers receiving 884 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Andrey Rogachev Russia 18 346 246 149 111 96 56 890
Dmytro Soloviov Russia 14 293 0.8× 232 0.9× 97 0.7× 54 0.5× 151 1.6× 60 687
David V. Tulumello Canada 11 467 1.3× 124 0.5× 142 1.0× 40 0.4× 110 1.1× 16 815
Barbara Sartori Austria 18 440 1.3× 372 1.5× 196 1.3× 30 0.3× 306 3.2× 51 1.0k
Stefania Perticaroli United States 18 430 1.2× 298 1.2× 83 0.6× 60 0.5× 116 1.2× 36 1.0k
Gemma Newby France 15 353 1.0× 162 0.7× 218 1.5× 106 1.0× 88 0.9× 26 733
Joshua Jasensky United States 20 448 1.3× 170 0.7× 74 0.5× 71 0.6× 184 1.9× 33 1.0k
Hong Qiu China 8 526 1.5× 153 0.6× 309 2.1× 72 0.6× 52 0.5× 16 833
Hanna Wacklin France 19 789 2.3× 108 0.4× 191 1.3× 24 0.2× 201 2.1× 25 1.1k
Viviana Cristiglio France 18 175 0.5× 501 2.0× 73 0.5× 13 0.1× 131 1.4× 66 1.1k
R. Michael Everly United States 16 379 1.1× 232 0.9× 98 0.7× 62 0.6× 53 0.6× 23 887

Countries citing papers authored by Andrey Rogachev

Since Specialization
Citations

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

Fields of papers citing papers by Andrey Rogachev

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Andrey Rogachev

This figure shows the co-authorship network connecting the top 25 collaborators of Andrey Rogachev. A scholar is included among the top collaborators of Andrey Rogachev 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 Andrey Rogachev. Andrey Rogachev 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.
Ryzhykau, Yury L., T. S. Kurkin, Andrey Rogachev, et al.. (2025). Chain-like supramolecular assemblies of inactivated actin oligomers reveal a multistage assembly pathway. Biochemical and Biophysical Research Communications. 796. 153122–153122.
2.
Andronache, C., et al.. (2023). Influence of the Structure on Magnetic Properties of Calcium-Phosphate Systems Doped with Iron and Vanadium Ions. International Journal of Molecular Sciences. 24(8). 7366–7366. 2 indexed citations
3.
Guskov, Albert, et al.. (2023). Structural Study of the Candida auris Ribosome. Moscow University Biological Sciences Bulletin. 78(S1). S56–S58. 1 indexed citations
4.
Vlasov, A.V., Yury L. Ryzhykau, И. В. Манухов, et al.. (2023). The Possibilities of Studying Biological Objects on a Pulsed Reactor. BIOPHYSICS. 68(2). 207–222. 1 indexed citations
5.
Guskov, Albert, et al.. (2023). Structural study of the Candida auris ribosome. 78(№3s, 2023). 47–50.
6.
Islamov, Daut R., Andrey Rogachev, Shamil Validov, et al.. (2023). Extraction, Purification, and Crystallization of GTPase Era from Staphylococcus aureus. Crystallography Reports. 68(2). 288–292.
7.
Murugova, T. N., Oleksandr I. Ivankov, Yury L. Ryzhykau, et al.. (2022). Mechanisms of membrane protein crystallization in ‘bicelles’. Scientific Reports. 12(1). 11109–11109. 18 indexed citations
8.
Wu, Cheng, Konstantin S. Usachev, Shamil Validov, et al.. (2022). E-site drug specificity of the human pathogen Candida albicans ribosome. Science Advances. 8(21). eabn1062–eabn1062. 13 indexed citations
9.
Orekhov, Philipp S., Irina Grabovec, Egor Marin, et al.. (2022). Structural insights into the effects of glycerol on ligand binding to cytochrome P450. Acta Crystallographica Section D Structural Biology. 79(1). 66–77. 1 indexed citations
10.
Borshchevskiy, Valentin, Kirill Kovalev, Ekaterina Round, et al.. (2022). True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins. Nature Structural & Molecular Biology. 29(5). 440–450. 31 indexed citations
11.
Bazhenov, Sergey V., Yury L. Ryzhykau, Vladimir N. Uversky, et al.. (2022). Ferritin self-assembly, structure, function, and biotechnological applications. International Journal of Biological Macromolecules. 224. 319–343. 63 indexed citations
12.
Bezrodnykh, Evgeniya A., et al.. (2022). A feasible approach to tune the interaction of chitosan with sodium dodecyl sulfate. Carbohydrate Polymers. 292. 119642–119642. 6 indexed citations
13.
Vlasov, A.V., Vladimir N. Uversky, Valentin Borshchevskiy, et al.. (2022). ATP synthase FOF1 structure, function, and structure-based drug design. Cellular and Molecular Life Sciences. 79(3). 179–179. 19 indexed citations
14.
Ryzhykau, Yury L., A.V. Vlasov, Philipp S. Orekhov, et al.. (2021). Ambiguities in and completeness of SAS data analysis of membrane proteins: the case of the sensory rhodopsin II–transducer complex. Acta Crystallographica Section D Structural Biology. 77(11). 1386–1400. 9 indexed citations
15.
Kovalev, Kirill, Roman Astashkin, Alexey Alekseev, et al.. (2020). High-resolution structural insights into the heliorhodopsin family. Proceedings of the National Academy of Sciences. 117(8). 4131–4141. 58 indexed citations
16.
Marin, Egor, Aleksandra Luginina, Anastasiia Gusach, et al.. (2020). Small-wedge synchrotron and serial XFEL datasets for Cysteinyl leukotriene GPCRs. Scientific Data. 7(1). 388–388. 6 indexed citations
17.
Łudzik, Katarzyna, Wojciech Zając, Monika Jażdżewska, et al.. (2020). Can the Isothermal Calorimetric Curve Shapes Suggest the Structural Changes in Micellar Aggregates?. International Journal of Molecular Sciences. 21(16). 5828–5828. 3 indexed citations
18.
Bălăşoiu, M., et al.. (2020). Ferrihydrite nanoparticles insights: Structural characterization, lactate dehydrogenase binding and virtual screening assay. International Journal of Biological Macromolecules. 164. 3559–3567. 10 indexed citations
19.
Rogachev, Andrey, et al.. (2019). β-Lactoglobulin associative interactions: a small-angle scattering study. European Biophysics Journal. 48(3). 285–295. 17 indexed citations
20.
Vlasov, A.V., Kirill Kovalev, Ivan Gushchin, et al.. (2019). Unusual features of the c-ring of F1FO ATP synthases. Scientific Reports. 9(1). 18547–18547. 18 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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