О. А. Синицына

1.0k total citations
76 papers, 799 citations indexed

About

О. А. Синицына is a scholar working on Biotechnology, Biomedical Engineering and Molecular Biology. According to data from OpenAlex, О. А. Синицына has authored 76 papers receiving a total of 799 indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Biotechnology, 45 papers in Biomedical Engineering and 34 papers in Molecular Biology. Recurrent topics in О. А. Синицына's work include Biofuel production and bioconversion (45 papers), Enzyme Production and Characterization (45 papers) and Microbial Metabolites in Food Biotechnology (19 papers). О. А. Синицына is often cited by papers focused on Biofuel production and bioconversion (45 papers), Enzyme Production and Characterization (45 papers) and Microbial Metabolites in Food Biotechnology (19 papers). О. А. Синицына collaborates with scholars based in Russia, Tajikistan and United States. О. А. Синицына's co-authors include А. П. Синицын, Alexander V. Gusakov, А. М. Рожкова, О. Н. Окунев, И. Н. Зоров, М. В. Семенова, А. В. Марков, É. A. Fedorova, Lorène Aeschbach and Jean-François Manen and has published in prestigious journals such as Applied and Environmental Microbiology, Bioresource Technology and International Journal of Molecular Sciences.

In The Last Decade

О. А. Синицына

71 papers receiving 758 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. Синицына Russia 18 435 395 320 272 201 76 799
Marina Kimiko Kadowaki Brazil 17 365 0.8× 399 1.0× 416 1.3× 214 0.8× 115 0.6× 64 865
Marie Couturier France 18 824 1.9× 485 1.2× 599 1.9× 453 1.7× 159 0.8× 24 1.3k
Dayanand Agsar India 13 178 0.4× 327 0.8× 291 0.9× 272 1.0× 76 0.4× 33 771
Artur Rogowski United Kingdom 14 535 1.2× 404 1.0× 568 1.8× 602 2.2× 296 1.5× 15 1.2k
Amanjot Kaur India 13 291 0.7× 195 0.5× 142 0.4× 155 0.6× 38 0.2× 33 501
Renato Graciano de Paula Brazil 17 394 0.9× 137 0.3× 536 1.7× 367 1.3× 36 0.2× 31 1.0k
Eduardo Scopel Ferreira da Costa Brazil 5 245 0.6× 153 0.4× 306 1.0× 117 0.4× 55 0.3× 6 565
Hisashi Kimoto Japan 19 85 0.2× 306 0.8× 560 1.8× 207 0.8× 63 0.3× 49 846
Harivony Rakotoarivonina France 14 287 0.7× 158 0.4× 231 0.7× 78 0.3× 65 0.3× 24 500
H.J. Gilbert United Kingdom 10 448 1.0× 404 1.0× 368 1.1× 232 0.9× 95 0.5× 10 707

Countries citing papers authored by О. А. Синицына

Since Specialization
Citations

This map shows the geographic impact of О. А. Синицына'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. Синицына 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. Синицына more than expected).

Fields of papers citing papers by О. А. Синицына

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

This figure shows the co-authorship network connecting the top 25 collaborators of О. А. Синицына. A scholar is included among the top collaborators of О. А. Синицына 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. Синицына. О. А. Синицына 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.
Синицын, А. П., et al.. (2025). Anti-Inflammatory Effects of Helianthus Tuberosus L. Polysaccharide and Its Limited Gene Expression Profile. International Journal of Molecular Sciences. 26(16). 7885–7885.
2.
Синицына, О. А., И. Н. Зоров, А. М. Рожкова, et al.. (2025). Physico-chemical properties and substrate specificity of α-(1→3)- d -glucan degrading recombinant mutanase from Trichoderma harzianum expressed in Penicillium verruculosum. Applied and Environmental Microbiology. 91(2). e0022624–e0022624. 1 indexed citations
3.
Боголицын, К. Г., et al.. (2024). Enzymatic hydrolysis of cellulose-rich fraction of Arctic seaweeds using Penicillium- and Myceliophtora-based glycoside hydrolases. Biomass Conversion and Biorefinery. 15(23). 30281–30292. 2 indexed citations
4.
Чухчин, Д. Г., A. V. Mal’kov, А. М. Рожкова, et al.. (2023). Production of Biomodified Bleached Kraft Pulp by Catalytic Conversion Using Penicillium verruculosum Enzymes: Composition, Properties, Structure, and Application. Catalysts. 13(1). 103–103. 3 indexed citations
5.
Короткова, О. Г., et al.. (2023). New Feed Enzyme Preparations for The Destruction of Nonstarch Polysaccharides and Phytates. Moscow University Chemistry Bulletin. 78(2). 63–68. 2 indexed citations
6.
Короткова, О. Г., et al.. (2023). NEW FEED ENZYME PREPARATIONS FOR THE DESTRUCTION OF NON-STARCH POLYSACCHARIDES AND PHYTATES. 64(№2, 2023). 178–186. 1 indexed citations
7.
Синицын, А. П., О. А. Синицына, И. Н. Зоров, & А. М. Рожкова. (2023). Carbohydrases: 50 Years of Research at the Department of Chemical Enzymology of Moscow State University—History and Prospects. Moscow University Chemistry Bulletin. 78(4). 170–186. 1 indexed citations
8.
Зоров, И. Н., Ulrich Schwaneberg, Mehdi D. Davari, et al.. (2021). Expression and Refolding of the Plant Chitinase From Drosera capensis for Applications as a Sustainable and Integrated Pest Management. Frontiers in Bioengineering and Biotechnology. 9. 728501–728501. 6 indexed citations
9.
Shcherbakova, Larisa, А. М. Рожкова, И. Н. Зоров, et al.. (2020). Effective Zearalenone Degradation in Model Solutions and Infected Wheat Grain Using a Novel Heterologous Lactonohydrolase Secreted by Recombinant Penicillium canescens. Toxins. 12(8). 475–475. 23 indexed citations
10.
Синицын, А. П., et al.. (2017). Preparation and Properties of New Biocatalysts for Destruction of Plant non-Starch Polysaccharides. Kataliz v promyshlennosti. 17(4). 331–338. 9 indexed citations
11.
12.
Синицын, А. П., et al.. (2016). Preparation of a Biocatalyst Based on Recombinant Cellulolytic Enzymatic Agents Penicillium verruculosum and its Application for Pulp and Paper Industry. Kataliz v promyshlennosti. 15(6). 84–89. 2 indexed citations
13.
Синицын, А. П., et al.. (2015). Parchment as a Potential Feedstock for Production of Sugars by Enzymatic Hydroly. Kataliz v promyshlennosti. 15(5). 74–77. 1 indexed citations
14.
Gusakov, Alexander V., О. А. Синицына, А. М. Рожкова, & А. П. Синицын. (2013). N-Glycosylation patterns in two α-l-arabinofuranosidases from Penicillium canescens belonging to the glycoside hydrolase families 51 and 54. Carbohydrate Research. 382. 71–76. 9 indexed citations
15.
Синицына, О. А., É. A. Fedorova, А. М. Рожкова, et al.. (2010). Isolation and properties of xyloglucanases of Penicillium sp.. Biochemistry (Moscow). 75(1). 41–49. 22 indexed citations
16.
Синицына, О. А., et al.. (2008). Isolation and characterization of extracellular α-galactosidases from Penicillium canescens. Biochemistry (Moscow). 73(1). 97–106. 21 indexed citations
17.
Синицына, О. А., É. A. Fedorova, М. В. Семенова, et al.. (2007). Isolation and characterization of extracellular pectin lyase from Penicillium canescens. Biochemistry (Moscow). 72(5). 565–571. 39 indexed citations
18.
Manen, Jean-François, О. А. Синицына, Lorène Aeschbach, А. В. Марков, & А. П. Синицын. (2005). A fully automatable enzymatic method for DNA extraction from plant tissues. BMC Plant Biology. 5(1). 23–23. 48 indexed citations
19.
Gusakov, Alexander V., et al.. (2001). Study of protein adsorption on indigo particles confirms the existence of enzyme–indigo interaction sites in cellulase molecules. Journal of Biotechnology. 87(1). 83–90. 34 indexed citations
20.
Yamada, Akio, et al.. (1992). Genetic evidence for variant selection in the course of dilute passaging of mumps vaccine virus. Research in Virology. 143(4). 279–283. 10 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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