Ivan Gushchin

2.5k total citations
65 papers, 1.4k citations indexed

About

Ivan Gushchin is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Genetics. According to data from OpenAlex, Ivan Gushchin has authored 65 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 50 papers in Molecular Biology, 33 papers in Cellular and Molecular Neuroscience and 7 papers in Genetics. Recurrent topics in Ivan Gushchin's work include Photoreceptor and optogenetics research (33 papers), Photosynthetic Processes and Mechanisms (18 papers) and Neuroscience and Neuropharmacology Research (14 papers). Ivan Gushchin is often cited by papers focused on Photoreceptor and optogenetics research (33 papers), Photosynthetic Processes and Mechanisms (18 papers) and Neuroscience and Neuropharmacology Research (14 papers). Ivan Gushchin collaborates with scholars based in Russia, Germany and France. Ivan Gushchin's co-authors include Valentin Gordeliy, Valentin Borshchevskiy, Ekaterina Round, Vitaly Polovinkin, А. Н. Попов, Taras Balandin, Pavel Buslaev, Sergei Grudinin, Kirill Kovalev and Andrii Ishchenko and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Ivan Gushchin

60 papers receiving 1.4k citations

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Ivan Gushchin 984 615 164 129 129 65 1.4k
Valentin Borshchevskiy 1.0k 1.0× 753 1.2× 111 0.7× 152 1.2× 184 1.4× 87 1.6k
Hüseyin Besir 1.1k 1.1× 361 0.6× 173 1.1× 111 0.9× 101 0.8× 24 1.5k
Keiichi Kawano 1.2k 1.3× 271 0.4× 150 0.9× 96 0.7× 241 1.9× 111 2.1k
Taras Balandin 632 0.6× 473 0.8× 85 0.5× 113 0.9× 116 0.9× 37 985
Захар О. Шенкарев 1.9k 2.0× 301 0.5× 229 1.4× 53 0.4× 63 0.5× 102 2.5k
Joachim Granzin 1.5k 1.6× 684 1.1× 207 1.3× 44 0.3× 235 1.8× 55 1.9k
Rich Olson 1.5k 1.5× 790 1.3× 155 0.9× 134 1.0× 86 0.7× 31 2.1k
Randal B. Bass 1.2k 1.2× 195 0.3× 390 2.4× 110 0.9× 98 0.8× 14 1.4k
Hugo Fraga 946 1.0× 294 0.5× 71 0.4× 187 1.4× 103 0.8× 34 1.1k
Katarzyna P. Adamala 1.3k 1.3× 423 0.7× 131 0.8× 286 2.2× 111 0.9× 58 1.7k

Countries citing papers authored by Ivan Gushchin

Since Specialization
Citations

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

Fields of papers citing papers by Ivan Gushchin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ivan Gushchin

This figure shows the co-authorship network connecting the top 25 collaborators of Ivan Gushchin. A scholar is included among the top collaborators of Ivan Gushchin 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 Ivan Gushchin. Ivan Gushchin 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., et al.. (2025). High‐Throughput Evaluation of Natural Diversity of F‐Type ATP Synthase Rotor Ring Stoichiometries. Proteins Structure Function and Bioinformatics. 93(6). 1128–1140.
2.
Bazhenov, Sergey V., Alina Remeeva, Nikolai N. Sluchanko, et al.. (2024). luxA Gene From Enhygromyxa salina Encodes a Functional Homodimeric Luciferase. Proteins Structure Function and Bioinformatics. 92(12). 1449–1458.
3.
Remeeva, Alina, et al.. (2024). Re‐engineering of a carotenoid‐binding protein based on NMR structure. Protein Science. 33(12). e5216–e5216. 2 indexed citations
4.
Marin, Egor, Valentin A. Manuvera, Kirill Kovalev, et al.. (2023). Structural insights into thrombolytic activity of destabilase from medicinal leech. Scientific Reports. 13(1). 6641–6641. 5 indexed citations
5.
Gushchin, Ivan, et al.. (2023). Why Na+ has higher propensity than K+ to condense DNA in a crowded environment. The Journal of Chemical Physics. 159(14). 3 indexed citations
6.
Болдырев, К. Н., Eugene G. Maksimov, Valentin Borshchevskiy, et al.. (2023). Two distinct mechanisms of flavoprotein spectral tuning revealed by low‐temperature and time‐dependent spectroscopy. Protein Science. 33(1). e4851–e4851. 1 indexed citations
7.
Bogorodskiy, Andrey, et al.. (2023). Fine spectral tuning of a flavin-binding fluorescent protein for multicolor imaging. Journal of Biological Chemistry. 299(3). 102977–102977. 13 indexed citations
8.
Astashkin, Roman, Kirill Kovalev, Alexey Alekseev, et al.. (2022). Structural insights into light-driven anion pumping in cyanobacteria. Nature Communications. 13(1). 6460–6460. 12 indexed citations
9.
Orekhov, Philipp S., Marine E. Bozdaganyan, Natalia Voskoboynikova, et al.. (2022). Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review. Nanomaterials. 12(3). 361–361. 18 indexed citations
10.
Orekhov, Philipp S., et al.. (2022). Structure and dynamics of the SARS‐CoV ‐2 envelope protein monomer. Proteins Structure Function and Bioinformatics. 90(5). 1102–1114. 26 indexed citations
11.
Remeeva, Alina, et al.. (2021). Insights into the mechanisms of light‐oxygen‐voltage domain color tuning from a set of high‐resolution X‐ray structures. Proteins Structure Function and Bioinformatics. 89(8). 1005–1016. 9 indexed citations
12.
Bâcle, Amélie, Pavel Buslaev, Rebeca García‐Fandiño, et al.. (2021). Inverse Conformational Selection in Lipid–Protein Binding. Journal of the American Chemical Society. 143(34). 13701–13709. 22 indexed citations
13.
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
14.
Maslov, Ivan, et al.. (2020). Rational Design of a Split Flavin-Based Fluorescent Reporter. ACS Synthetic Biology. 10(1). 72–83. 13 indexed citations
15.
Kovalev, Kirill, Vitaly Polovinkin, Ivan Gushchin, et al.. (2019). Structure and mechanisms of sodium-pumping KR2 rhodopsin. Science Advances. 5(4). eaav2671–eaav2671. 63 indexed citations
16.
Antila, Hanne, Pavel Buslaev, Tiago Mendes Ferreira, et al.. (2019). Headgroup Structure and Cation Binding in Phosphatidylserine Lipid Bilayers. The Journal of Physical Chemistry B. 123(43). 9066–9079. 44 indexed citations
17.
Melnikov, Igor, Vitaly Polovinkin, Kirill Kovalev, et al.. (2017). Fast iodide-SAD phasing for high-throughput membrane protein structure determination. Science Advances. 3(5). e1602952–e1602952. 33 indexed citations
18.
Gushchin, Ivan, Igor Melnikov, Vitaly Polovinkin, et al.. (2017). Mechanism of transmembrane signaling by sensor histidine kinases. Science. 356(6342). 131 indexed citations
19.
Nikolaev, Mikhail, Ekaterina Round, Ivan Gushchin, et al.. (2017). Integral Membrane Proteins Can Be Crystallized Directly from Nanodiscs. Crystal Growth & Design. 17(3). 945–948. 26 indexed citations
20.
Petrovskaya, L. E., Sergei P. Balashov, Е. П. Лукашев, et al.. (2015). ESR — A retinal protein with unusual properties from Exiguobacterium sibiricum. Biochemistry (Moscow). 80(6). 688–700. 12 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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