M. O. Pulina

614 total citations
18 papers, 555 citations indexed

About

M. O. Pulina is a scholar working on Nutrition and Dietetics, Immunology and Hematology. According to data from OpenAlex, M. O. Pulina has authored 18 papers receiving a total of 555 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Nutrition and Dietetics, 7 papers in Immunology and 6 papers in Hematology. Recurrent topics in M. O. Pulina's work include Trace Elements in Health (12 papers), Infant Nutrition and Health (10 papers) and Neutrophil, Myeloperoxidase and Oxidative Mechanisms (6 papers). M. O. Pulina is often cited by papers focused on Trace Elements in Health (12 papers), Infant Nutrition and Health (10 papers) and Neutrophil, Myeloperoxidase and Oxidative Mechanisms (6 papers). M. O. Pulina collaborates with scholars based in Russia, United Kingdom and Italy. M. O. Pulina's co-authors include Sokolov Av, V. B. Vasilyev, Е. Т. Захарова, В. Р. Самыгина, О. М. Панасенко, H.D. Bartunik, Dmitri I. Svergun, Irina I. Vlasova, Maxim V. Petoukhov and Gleb Bourenkov and has published in prestigious journals such as PLoS ONE, Journal of Molecular Biology and Archives of Biochemistry and Biophysics.

In The Last Decade

M. O. Pulina

18 papers receiving 545 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
M. O. Pulina Russia	16	287	259	161	125	99	18	555
Е. Т. Захарова Russia	20	405 1.4×	345 1.3×	220 1.4×	172 1.4×	149 1.5×	38	839
Luciana Costa Portugal	10	121 0.4×	49 0.2×	81 0.5×	115 0.9×	52 0.5×	26	375
Catharina Van Elssen Netherlands	13	149 0.5×	289 1.1×	174 1.1×	63 0.5×	13 0.1×	29	664
Tomofusa Usui Japan	14	73 0.3×	90 0.3×	120 0.7×	47 0.4×	48 0.5×	33	403
Richard D. Horniblow United Kingdom	10	76 0.3×	20 0.1×	184 1.1×	90 0.7×	25 0.3×	20	458
Yoshikazu Sukenaga Japan	12	85 0.3×	96 0.4×	225 1.4×	11 0.1×	34 0.3×	22	435
Peggy Charbonnier France	12	113 0.4×	150 0.6×	190 1.2×	11 0.1×	38 0.4×	20	595
Christopher J. De Feo United States	9	356 1.2×	24 0.1×	114 0.7×	58 0.5×	24 0.2×	10	564
George X. Song‐Zhao Canada	5	35 0.1×	202 0.8×	144 0.9×	13 0.1×	86 0.9×	6	414
Judit Cserepes Hungary	7	51 0.2×	24 0.1×	416 2.6×	34 0.3×	42 0.4×	10	786

Countries citing papers authored by M. O. Pulina

Since Specialization

Citations

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

Fields of papers citing papers by M. O. Pulina

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by M. O. Pulina. 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 M. O. Pulina. The network helps show where M. O. Pulina may publish in the future.

Co-authorship network of co-authors of M. O. Pulina

This figure shows the co-authorship network connecting the top 25 collaborators of M. O. Pulina. A scholar is included among the top collaborators of M. O. Pulina 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 M. O. Pulina. M. O. Pulina is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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18 of 18 papers shown

Самыгина, В. Р., Sokolov Av, Gleb Bourenkov, et al.. (2013). Ceruloplasmin: Macromolecular Assemblies with Iron-Containing Acute Phase Proteins. PLoS ONE. 8(7). e67145–e67145. 83 indexed citations

Av, Sokolov, В. А. Костевич, M. O. Pulina, et al.. (2012). Protection of ceruloplasmin by lactoferrin against hydroxyl radicals is pH dependent¹This article is part of a Special Issue entitled Lactoferrin and has undergone the Journal’s usual peer review process.. Biochemistry and Cell Biology. 90(3). 397–404. 20 indexed citations

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

Av, Sokolov, et al.. (2010). Identification and properties of complexes formed by myeloperoxidase with lipoproteins and ceruloplasmin. Chemistry and Physics of Lipids. 163(4-5). 347–355. 44 indexed citations

Av, Sokolov, et al.. (2009). Identification of complexes formed by ceruloplasmin with matrix metalloproteinases 2 and 12. Biochemistry (Moscow). 74(12). 1388–1392. 15 indexed citations

Av, Sokolov, et al.. (2009). Effect of lactoferrin on oxidative features of ceruloplasmin. BioMetals. 22(3). 521–529. 29 indexed citations

Горудко, И. В., Sokolov Av, M. O. Pulina, et al.. (2009). New approaches to the measurement of the concentration and peroxidase activity of myeloperoxidase in human blood plasma. Russian Journal of Bioorganic Chemistry. 35(5). 566–575. 31 indexed citations

Панасенко, О. М., et al.. (2008). Influence of ceruloplasmin and lactoferrin on the chlorination activity of leukocyte myeloperoxidase assayed by chemiluminescence. BIOPHYSICS. 53(4). 268–272. 18 indexed citations

Av, Sokolov, M. O. Pulina, В. Р. Самыгина, et al.. (2008). Ceruloplasmin and myeloperoxidase in complex affect the enzymatic properties of each other. Free Radical Research. 42(11-12). 989–998. 62 indexed citations

10.

Самыгина, В. Р., et al.. (2008). X-ray diffraction study of highly purified human ceruloplasmin. Crystallography Reports. 53(4). 655–662. 18 indexed citations

11.

Av, Sokolov, et al.. (2007). Identification of leukocyte cationic proteins that interact with ceruloplasmin. Biochemistry (Moscow). 72(8). 872–877. 25 indexed citations

12.

Sabatucci, Annalaura, Patrice Vachette, V. B. Vasilyev, et al.. (2007). Structural Characterization of the Ceruloplasmin: Lactoferrin Complex in Solution. Journal of Molecular Biology. 371(4). 1038–1046. 30 indexed citations

13.

Av, Sokolov, et al.. (2007). Interaction of ceruloplasmin, lactoferrin, and myeloperoxidase. Biochemistry (Moscow). 72(4). 409–415. 40 indexed citations

14.

Av, Sokolov, et al.. (2006). Identification and isolation from breast milk of ceruloplasmin-lactoferrin complex. Biochemistry (Moscow). 71(2). 160–166. 28 indexed citations

15.

Av, Sokolov, et al.. (2006). A study of recombinant human lactoferrin secreted in milk of transgenic mice. Doklady Biochemistry and Biophysics. 411(1). 336–338. 9 indexed citations

16.

Av, Sokolov, et al.. (2005). Effect of Lactoferrin on the Ferroxidase Activity of Ceruloplasmin. Biochemistry (Moscow). 70(9). 1015–1019. 19 indexed citations

17.

Pulina, M. O., et al.. (2002). Studies of the ceruloplasmin-lactoferrin complex. Biochemistry and Cell Biology. 80(1). 35–39. 27 indexed citations

18.

Захарова, Е. Т., M. O. Pulina, Vincenzo De Filippis, et al.. (2000). Interaction of Lactoferrin with Ceruloplasmin. Archives of Biochemistry and Biophysics. 374(2). 222–228. 42 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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