А. П. Синицын

4.9k total citations
181 papers, 3.7k citations indexed

About

А. П. Синицын is a scholar working on Biomedical Engineering, Biotechnology and Molecular Biology. According to data from OpenAlex, А. П. Синицын has authored 181 papers receiving a total of 3.7k indexed citations (citations by other indexed papers that have themselves been cited), including 130 papers in Biomedical Engineering, 117 papers in Biotechnology and 94 papers in Molecular Biology. Recurrent topics in А. П. Синицын's work include Biofuel production and bioconversion (128 papers), Enzyme Production and Characterization (112 papers) and Enzyme Catalysis and Immobilization (41 papers). А. П. Синицын is often cited by papers focused on Biofuel production and bioconversion (128 papers), Enzyme Production and Characterization (112 papers) and Enzyme Catalysis and Immobilization (41 papers). А. П. Синицын collaborates with scholars based in Russia, Tajikistan and Germany. А. П. Синицын's co-authors include Alexander V. Gusakov, А. М. Рожкова, О. Н. Окунев, И. Н. Зоров, О. А. Синицына, Anatole A. Klyosov, Elena Vlasenko, А. В. Марков, М. В. Семенова and Anna S. Dotsenko and has published in prestigious journals such as SHILAP Revista de lepidopterología, PLoS ONE and Applied and Environmental Microbiology.

In The Last Decade

А. П. Синицын

173 papers receiving 3.6k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
А. П. Синицын Russia	32	2.7k	1.9k	1.8k	860	599	181	3.7k
Alexander V. Gusakov Russia	31	2.4k 0.9×	1.7k 0.9×	1.5k 0.9×	792 0.9×	477 0.8×	90	3.2k
Edivaldo Ximenes Ferreira Filho Brazil	32	2.1k 0.8×	1.6k 0.9×	1.7k 0.9×	924 1.1×	452 0.8×	96	3.2k
Henrik Stålbrand Sweden	36	2.2k 0.8×	1.5k 0.8×	1.6k 0.9×	1.2k 1.4×	897 1.5×	87	3.8k
F. I. Javier Pastor Spain	35	1.5k 0.6×	1.5k 0.8×	1.2k 0.7×	753 0.9×	299 0.5×	98	3.1k
Gurinder Singh Hoondal India	24	1.8k 0.7×	1.8k 1.0×	1.9k 1.1×	1.1k 1.3×	321 0.5×	37	3.2k
Maria de Lourdes Teixeira de Moraes Polizeli Brazil	35	3.0k 1.1×	2.5k 1.3×	2.7k 1.5×	1.4k 1.7×	866 1.4×	200	4.9k
Fábio M. Squina Brazil	34	2.5k 0.9×	1.8k 0.9×	1.9k 1.0×	973 1.1×	483 0.8×	159	3.9k
Eduardo Ximenes United States	28	3.3k 1.2×	2.0k 1.0×	826 0.5×	789 0.9×	224 0.4×	67	3.9k
Akihiko Kosugi Japan	31	2.0k 0.8×	1.5k 0.8×	1.1k 0.6×	607 0.7×	308 0.5×	134	3.2k
Matti Siika‐aho Finland	43	4.3k 1.6×	2.5k 1.3×	2.1k 1.2×	1.6k 1.9×	622 1.0×	134	5.8k

Countries citing papers authored by А. П. Синицын

Since Specialization

Citations

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

Fields of papers citing papers by А. П. Синицын

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of А. П. Синицын

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

All Works

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20 of 20 papers shown

Семенова, М. В., et al.. (2025). Efficient Hydrolysis of Sugar Beet Pulp Using Novel Enzyme Complexes. Agronomy. 15(1). 101–101. 1 indexed citations

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.

Dotsenko, Anna S., et al.. (2025). Increased activity under acidic conditions and improved thermostability of Aspergillus niger phytase A. Bioresource Technology Reports. 30. 102161–102161.

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

Синицын, А. П., et al.. (2024). Transcription Factors ClrB and XlnR and Their Effect on the Transcription of Cellulase Genes in the Filamentous Fungus Penicillium verruculosum. International Journal of Molecular Sciences. 25(24). 13373–13373. 1 indexed citations

Dotsenko, Anna S., et al.. (2023). The role of intracellular β-glucosidase in cellulolytic response induction in filamentous fungus Penicillium verruculosum. Research in Microbiology. 175(4). 104178–104178. 1 indexed citations

Dotsenko, Anna S., et al.. (2023). Stabilization of elements of secondary structure in Aspergillus awamori exo-inulinase for thermostability improvement. Bioresource Technology Reports. 24. 101644–101644. 1 indexed citations

Dotsenko, Anna S., et al.. (2023). Flexibility of active center affects thermostability and activity of Penicillium canescens xylanase E. Biochimie. 216. 83–89.

Чухчин, Д. Г., A. V. Mal’kov, А. М. Рожкова, et al.. (2023). Enzymatic Hydrolysis of Kraft and Sulfite Pulps: What Is the Best Cellulosic Substrate for Industrial Saccharification?. Fermentation. 9(11). 936–936. 3 indexed citations

10.

Dotsenko, Anna S., et al.. (2022). Single substitution in α-helix of active center enhanced thermostability of Aspergillus awamori exo-inulinase. Journal of Molecular Graphics and Modelling. 119. 108381–108381. 6 indexed citations

11.

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

12.

Contreras, Francisca, Subrata Pramanik, А. М. Рожкова, et al.. (2020). Engineering Robust Cellulases for Tailored Lignocellulosic Degradation Cocktails. International Journal of Molecular Sciences. 21(5). 1589–1589. 79 indexed citations

13.

Contreras, Francisca, Subrata Pramanik, А. М. Рожкова, et al.. (2020). KnowVolution of a GH5 Cellulase from Penicillium verruculosum to Improve Thermal Stability for Biomass Degradation. ACS Sustainable Chemistry & Engineering. 8(33). 12388–12399. 37 indexed citations

14.

Короткова, О. Г., et al.. (2018). Comparison Analysis of the Composition and Properties of Fodder Enzyme Preparations. Kataliz v promyshlennosti. 18(4). 72–78. 3 indexed citations

15.

Dotsenko, Anna S., А. М. Рожкова, Alexander V. Gusakov, & А. П. Синицын. (2017). Improving the efficiency of the bioconversion of plant raw materials with mutant cellulases of Penicillium verruculosum. Catalysis in Industry. 9(1). 71–76. 4 indexed citations

16.

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

17.

Синицын, А. П., et al.. (2013). Comparing the efficiency of plant material bioconversion processes using biocatalysts based on Trichoderma and Penicillium verruculosum enzyme preparations. Catalysis in Industry. 5(1). 98–104. 17 indexed citations

18.

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

19.

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

20.

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

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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