О. А. Кост

1.0k total citations
68 papers, 813 citations indexed

About

О. А. Кост is a scholar working on Molecular Biology, Cardiology and Cardiovascular Medicine and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, О. А. Кост has authored 68 papers receiving a total of 813 indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 18 papers in Cardiology and Cardiovascular Medicine and 12 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in О. А. Кост's work include Renin-Angiotensin System Studies (17 papers), Protein Hydrolysis and Bioactive Peptides (12 papers) and Ocular Surface and Contact Lens (9 papers). О. А. Кост is often cited by papers focused on Renin-Angiotensin System Studies (17 papers), Protein Hydrolysis and Bioactive Peptides (12 papers) and Ocular Surface and Contact Lens (9 papers). О. А. Кост collaborates with scholars based in Russia, United States and Tajikistan. О. А. Кост's co-authors include Sergei M. Danilov, Irina V. Balyasnikova, Н. Б. Чеснокова, О. В. Безнос, Ronald F. Albrecht, Natalia L. Klyachko, V. F. Pozdnev, Е. В. Попова, David E. Schwartz and Alexander N. Vaneev and has published in prestigious journals such as SHILAP Revista de lepidopterología, Journal of the American College of Cardiology and PLoS ONE.

In The Last Decade

О. А. Кост

62 papers receiving 788 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
О. А. Кост Russia 18 428 216 156 119 92 68 813
Junxian Lim Australia 21 543 1.3× 65 0.3× 64 0.4× 117 1.0× 7 0.1× 42 1.1k
Charles Day United States 17 664 1.6× 102 0.5× 53 0.3× 23 0.2× 10 0.1× 39 1.2k
Raphaëlle Fanciullino France 18 364 0.9× 19 0.1× 78 0.5× 50 0.4× 43 0.5× 40 1.0k
Ana Negri Spain 18 649 1.5× 72 0.3× 118 0.8× 24 0.2× 6 0.1× 31 1.1k
Carl Crysler United States 19 304 0.7× 31 0.1× 50 0.3× 64 0.5× 53 0.6× 37 782
Butrus Atrash United Kingdom 18 767 1.8× 100 0.5× 30 0.2× 75 0.6× 16 0.2× 39 1.2k
Jun Katada Japan 20 481 1.1× 286 1.3× 39 0.3× 118 1.0× 5 0.1× 36 1.3k
Chris Dockendorff United States 17 458 1.1× 77 0.4× 15 0.1× 56 0.5× 29 0.3× 50 1.5k
Peter Kurtzhals Denmark 20 1.1k 2.7× 23 0.1× 154 1.0× 14 0.1× 86 0.9× 35 2.4k
Marcus Bauser Germany 18 584 1.4× 32 0.1× 109 0.7× 16 0.1× 21 0.2× 35 1.0k

Countries citing papers authored by О. А. Кост

Since Specialization
Citations

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

Fields of papers citing papers by О. А. Кост

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by О. А. Кост. 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 О. А. Кост. The network helps show where О. А. Кост may publish in the future.

Co-authorship network of co-authors of О. А. Кост

This figure shows the co-authorship network connecting the top 25 collaborators of О. А. Кост. A scholar is included among the top collaborators of О. А. Кост 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 О. А. Кост. О. А. Кост 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.
Рогожин, Е. А., Е. В. Попова, О. А. Кост, et al.. (2025). CaP Nanoparticles Improve the Effect of dsRNA on Gene Expression, Growth, and Mycotoxin Production of Toxigenic Fusarium graminearum. International Journal of Molecular Sciences. 26(20). 10021–10021.
2.
Boginskaya, I. A., et al.. (2025). The surface-enhanced Raman scattering method for point-of-care atrial fibrillation diagnostics. Computers in Biology and Medicine. 189. 109923–109923.
3.
Zaklyazminskaya, E. V., Dmitriy Korostin, Pavel A. Petukhov, et al.. (2024). Effects of Angiotensin-I-Converting Enzyme (ACE) Mutations Associated with Alzheimer’s Disease on Blood ACE Phenotype. Biomedicines. 12(10). 2410–2410. 1 indexed citations
4.
Danilov, Sergei M., Pavel A. Petukhov, Valery Ilinsky, et al.. (2023). Blood ACE Phenotyping for Personalized Medicine: Revelation of Patients with Conformationally Altered ACE. Biomedicines. 11(2). 534–534. 4 indexed citations
5.
Попова, Е. В., О. В. Безнос, Н. Б. Чеснокова, et al.. (2023). A Direct Comparison of Peptide Drug Delivery Systems Based on the Use of Hybrid Calcium Phosphate/Chitosan Nanoparticles versus Unmixed Calcium Phosphate or Chitosan Nanoparticles In Vitro and In Vivo. International Journal of Molecular Sciences. 24(21). 15532–15532. 5 indexed citations
6.
Безнос, О. В., et al.. (2023). CHITOSAN NANOPARTICLES - THE DRUG DELIVERY SYSTEM TO THE ANTERIOR SEGMENT OF THE EYE. 64(№2, 2023). 141–151.
7.
Попова, Е. В., О. В. Безнос, Еlena V. Kudryashova, et al.. (2023). Chitosan-Covered Calcium Phosphate Particles Co-Loaded with Superoxide Dismutase 1 and ACE Inhibitor: Development, Characterization and Effect on Intraocular Pressure. Pharmaceutics. 15(2). 550–550. 2 indexed citations
8.
Попова, Е. В., О. В. Безнос, Н. Б. Чеснокова, et al.. (2021). Chitosan-covered calcium phosphate particles as a drug vehicle for delivery to the eye. Nanomedicine Nanotechnology Biology and Medicine. 40. 102493–102493. 14 indexed citations
9.
Кост, О. А., О. В. Безнос, Devika S. Manickam, et al.. (2015). Superoxide Dismutase 1 Nanozyme for Treatment of Eye Inflammation. Oxidative Medicine and Cellular Longevity. 2016(1). 5194239–5194239. 32 indexed citations
10.
Голухова, Е. З., et al.. (2015). PHENOTYPING OF ANGIOTENSIN-CONVERTING ENZYME IN THE HUMAN HEART. Journal of the American College of Cardiology. 65(10). A404–A404. 1 indexed citations
11.
Голухова, Е. З., David E. Schwartz, Randal O. Dull, et al.. (2015). Tissue Specificity of Human Angiotensin I-Converting Enzyme. PLoS ONE. 10(11). e0143455–e0143455. 21 indexed citations
12.
Schwartz, David E., et al.. (2012). Conformational Changes of Blood ACE in Chronic Uremia. PLoS ONE. 7(11). e49290–e49290. 18 indexed citations
13.
Baskin, Igor I., et al.. (2005). Role of Two Chloride-Binding Sites in Functioning of Testicular Angiotensin-Converting Enzyme. Biochemistry (Moscow). 70(10). 1167–1172. 6 indexed citations
14.
Орлова, М. А., et al.. (2002). A Hydrophobic Site on the Surface of the Angiotensin-Converting Enzyme Molecule. Biochemistry (Moscow). 67(5). 553–557. 4 indexed citations
15.
Pozdnev, V. F., et al.. (2001). Characterization of Bovine Atrial Angiotensin-Converting Enzyme. Biochemistry (Moscow). 66(4). 429–434. 3 indexed citations
16.
Eremin, Sergei A., et al.. (2001). Fluorescence Polarization Studies of Different Forms of Angiotensin-Converting Enzyme. Biochemistry (Moscow). 66(7). 788–794. 4 indexed citations
17.
Levashov, Andrey V., et al.. (2001). Unusual Behavior of Membrane Somatic Angiotensin-Converting Enzyme in a Reversed Micelle System. Biochemistry (Moscow). 66(1). 34–41. 2 indexed citations
18.
Кост, О. А., et al.. (2000). New feature of angiotensin-converting enzyme: carbohydrate-recognizing domain. Journal of Molecular Recognition. 13(6). 360–369. 32 indexed citations
19.
Saenger, Wolfram, et al.. (1998). Glycosylation of bovine pulmonary angiotensin‐converting enzyme modulates its catalytic properties. FEBS Letters. 431(2). 255–258. 15 indexed citations
20.
Breydo, Leonid, et al.. (1997). Study of ionization of tyrosine residues in proteins by second-derivative UV spectroscopy. Russian Chemical Bulletin. 46(7). 1339–1343. 3 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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