В. А. Костевич

1.2k total citations
66 papers, 956 citations indexed

About

В. А. Костевич is a scholar working on Immunology, Physiology and Nutrition and Dietetics. According to data from OpenAlex, В. А. Костевич has authored 66 papers receiving a total of 956 indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Immunology, 26 papers in Physiology and 17 papers in Nutrition and Dietetics. Recurrent topics in В. А. Костевич's work include Neutrophil, Myeloperoxidase and Oxidative Mechanisms (40 papers), Nitric Oxide and Endothelin Effects (23 papers) and Trace Elements in Health (10 papers). В. А. Костевич is often cited by papers focused on Neutrophil, Myeloperoxidase and Oxidative Mechanisms (40 papers), Nitric Oxide and Endothelin Effects (23 papers) and Trace Elements in Health (10 papers). В. А. Костевич collaborates with scholars based in Russia, Belarus and Czechia. В. А. Костевич's co-authors include Sokolov Av, V. B. Vasilyev, О. М. Панасенко, Е. Т. Захарова, И. В. Горудко, Irina I. Vlasova, D. V. Grigorieva, Elena V. Mikhalchik, В. Р. Самыгина and С. Н. Черенкевич and has published in prestigious journals such as Biochemical and Biophysical Research Communications, Free Radical Biology and Medicine and Archives of Biochemistry and Biophysics.

In The Last Decade

В. А. Костевич

64 papers receiving 946 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
В. А. Костевич Russia 19 377 265 220 184 146 66 956
V. B. Vasilyev Russia 27 637 1.7× 558 2.1× 505 2.3× 283 1.5× 143 1.0× 101 1.7k
И. В. Горудко Belarus 17 435 1.2× 102 0.4× 257 1.2× 228 1.2× 34 0.2× 73 858
Е. Т. Захарова Russia 20 345 0.9× 405 1.5× 220 1.0× 149 0.8× 62 0.4× 38 839
Juan Cheng China 19 366 1.0× 37 0.1× 342 1.6× 160 0.9× 98 0.7× 48 1.3k
Oriana Bórquez-Ojeda United States 9 183 0.5× 272 1.0× 310 1.4× 48 0.3× 37 0.3× 16 873
Jean-Christophe Simard Canada 12 372 1.0× 42 0.2× 423 1.9× 66 0.4× 218 1.5× 17 932
Mohammed Nader Shalaby Egypt 16 180 0.5× 46 0.2× 333 1.5× 89 0.5× 43 0.3× 41 1.0k
C.E. Hulstaert Netherlands 17 164 0.4× 95 0.4× 350 1.6× 132 0.7× 47 0.3× 38 1.2k
Jianfeng Shi China 23 258 0.7× 28 0.1× 477 2.2× 120 0.7× 38 0.3× 52 1.2k
Hermann‐Josef Thierse Germany 19 268 0.7× 55 0.2× 307 1.4× 132 0.7× 27 0.2× 39 1.2k

Countries citing papers authored by В. А. Костевич

Since Specialization
Citations

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

Fields of papers citing papers by В. А. Костевич

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of В. А. Костевич

This figure shows the co-authorship network connecting the top 25 collaborators of В. А. Костевич. A scholar is included among the top collaborators of В. А. Костевич 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 В. А. Костевич. В. А. Костевич 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.
Grigorieva, D. V., N. Gorbunov, В. А. Костевич, et al.. (2025). Human serum albumin modified in myeloperoxidase-dependent reactions is a mediator of neutrophil extracellular trap formation. Journal of Biomedical Research. 40(2). 147–147.
2.
Grigorieva, D. V., et al.. (2024). Detection of the Brominating Activity of Myeloperoxidase Using Fluorescein. Journal of Applied Spectroscopy. 91(2). 313–322. 1 indexed citations
3.
Shmeleva, Evgeniya V., И. В. Горудко, D. V. Grigorieva, et al.. (2024). Hypochlorous Acid-Modified Serum Albumin Causes NETosis in the Whole Blood Ex Vivo and in Isolated Neutrophils. Bulletin of Experimental Biology and Medicine. 177(2). 197–202. 2 indexed citations
4.
5.
Горудко, И. В., D. V. Grigorieva, N. Gorbunov, et al.. (2022). Structure-biological activity relationships of myeloperoxidase to effect on platelet activation. Archives of Biochemistry and Biophysics. 728. 109353–109353. 2 indexed citations
6.
Panteleev, Pavel V., N. Gorbunov, В. А. Костевич, et al.. (2022). In Vitro Modulation of Complement Activation by Therapeutically Prospective Analogues of the Marine Polychaeta Arenicin Peptides. Marine Drugs. 20(10). 612–612. 6 indexed citations
7.
Av, Sokolov, et al.. (2021). Myeloperoxidase/high-density lipoprotein cholesterol ratio in patients with arterial hypertension and chronic coronary heart disease. Medical academic journal. 21(2). 75–86. 4 indexed citations
8.
Костевич, В. А., et al.. (2019). The specific activity of proteins involved in iron metabolism depends on compensation of type 2 diabetes mellitus. Medical academic journal. 19(2). 37–42. 1 indexed citations
9.
Grigorieva, D. V., И. В. Горудко, С. Н. Черенкевич, et al.. (2019). Celestine blue B as a sensor for hypochlorous acid and HOCL-modified proteins registration. Medical academic journal. 19(2). 63–71. 2 indexed citations
10.
Av, Sokolov, Maxim V. Petoukhov, Gleb Bourenkov, et al.. (2018). Structural Study of the Complex Formed by Ceruloplasmin and Macrophage Migration Inhibitory Factor. Biochemistry (Moscow). 83(6). 701–707. 5 indexed citations
11.
Захарова, Е. Т., Sokolov Av, В. А. Костевич, et al.. (2018). Erythropoietin and Nrf2: key factors in the neuroprotection provided by apo-lactoferrin. BioMetals. 31(3). 425–443. 44 indexed citations
12.
Костевич, В. А. & Sokolov Av. (2018). Oxidation of cysteine by ceruloplasmin leads to formation of hydrogen peroxide, which can be utilized by myeloperoxidase. Biochemical and Biophysical Research Communications. 503(3). 2146–2151. 5 indexed citations
13.
Av, Sokolov, et al.. (2017). Comparison of interaction between ceruloplasmin and lactoferrin/transferrin: to bind or not to bind. Biochemistry (Moscow). 82(9). 1073–1078. 19 indexed citations
14.
Grigorieva, D. V., И. В. Горудко, Sokolov Av, et al.. (2016). Myeloperoxidase Stimulates Neutrophil Degranulation. Bulletin of Experimental Biology and Medicine. 161(4). 495–500. 36 indexed citations
15.
Av, Sokolov, Laura Acquasaliente, В. А. Костевич, et al.. (2015). Thrombin inhibits the anti-myeloperoxidase and ferroxidase functions of ceruloplasmin: relevance in rheumatoid arthritis. Free Radical Biology and Medicine. 86. 279–294. 39 indexed citations
16.
Горудко, И. В., D. V. Grigorieva, В. А. Костевич, et al.. (2014). Hypohalous acid-modified human serum albumin induces neutrophil NADPH oxidase activation, degranulation, and shape change. Free Radical Biology and Medicine. 68. 326–334. 64 indexed citations
17.
Vlasova, Irina I., Sokolov Av, В. А. Костевич, et al.. (2012). PEGylated single-walled carbon nanotubes activate neutrophils to increase production of hypochlorous acid, the oxidant capable of degrading nanotubes. Toxicology and Applied Pharmacology. 264(1). 131–142. 48 indexed citations
18.
Av, Sokolov, et al.. (2010). Interaction of ceruloplasmin and 5-lipoxygenase. Biochemistry (Moscow). 75(12). 1464–1469. 18 indexed citations
19.
Pulina, M. O., Sokolov Av, Е. Т. Захарова, В. А. Костевич, & V. B. Vasilyev. (2010). Effect of Lactoferrin on Consequences of Acute Experimental Hemorrhagic Anemia in Rats. Bulletin of Experimental Biology and Medicine. 149(2). 219–222. 15 indexed citations
20.
Av, Sokolov, et al.. (2010). Revealing binding sites for myeloperoxidase on the surface of human low density lipoproteins. Chemistry and Physics of Lipids. 164(1). 49–53. 16 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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