I. V. Uporov

923 total citations
58 papers, 754 citations indexed

About

I. V. Uporov is a scholar working on Molecular Biology, Materials Chemistry and Molecular Medicine. According to data from OpenAlex, I. V. Uporov has authored 58 papers receiving a total of 754 indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 14 papers in Materials Chemistry and 9 papers in Molecular Medicine. Recurrent topics in I. V. Uporov's work include Enzyme Structure and Function (14 papers), Protein Structure and Dynamics (12 papers) and Antibiotic Resistance in Bacteria (9 papers). I. V. Uporov is often cited by papers focused on Enzyme Structure and Function (14 papers), Protein Structure and Dynamics (12 papers) and Antibiotic Resistance in Bacteria (9 papers). I. V. Uporov collaborates with scholars based in Russia, United States and Tajikistan. I. V. Uporov's co-authors include Kathryn A. Thomasson, Harvey R. Knull, С. Д. Варфоломеев, Irina M. Le‐Deygen, Еlena V. Kudryashova, Neocles B. Leontis, В. И. Тишков, E.V. Fedorov, Н.Н. Угарова and Irina G. Gazaryan and has published in prestigious journals such as The Journal of Chemical Physics, ACS Nano and PLoS ONE.

In The Last Decade

I. V. Uporov

56 papers receiving 731 citations

Peers

I. V. Uporov

EEE

CMN

Jesús Mendieta Spain

Jan Slavı́k Czechia

Ernst Grell Germany

Marc B. Taraban United States

Barbara Biondi Italy

Atanu Acharya United States

Jean‐Marc Millot France

Yves‐Marie Coïc France

Zhengding Su China

Jesús Mendieta Spain

I. V. Uporov

540 ×1.2

183 ×1.4

126 ×1.4

97 ×1.2

EEE

60 ×0.8

CMN

Citations per year, relative to I. V. Uporov I. V. Uporov (= 1×) peers Jesús Mendieta

Countries citing papers authored by I. V. Uporov

Since Specialization

Citations

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

Fields of papers citing papers by I. V. Uporov

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by I. V. Uporov. 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 I. V. Uporov. The network helps show where I. V. Uporov may publish in the future.

Co-authorship network of co-authors of I. V. Uporov

This figure shows the co-authorship network connecting the top 25 collaborators of I. V. Uporov. A scholar is included among the top collaborators of I. V. Uporov 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 I. V. Uporov. I. V. Uporov 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

Le‐Deygen, Irina M., Marina Sokolsky‐Papkov, Yuri I. Golovin, et al.. (2025). In Situ Observation of Chymotrypsin Catalytic Activity Change Actuated by Nonheating Low-Frequency Magnetic Field. UNC Libraries.

Korostin, Dmitriy, I. V. Uporov, Steven M. Dudek, et al.. (2024). Effect of ACE mutations on blood ACE phenotype parameters. PLoS ONE. 19(10). e0308289–e0308289. 2 indexed citations

Uporov, I. V., Maria V. Efremova, Irina M. Le‐Deygen, et al.. (2022). Modulation of α-Chymotrypsin Conjugated to Magnetic Nanoparticles by the Non-Heating Low-Frequency Magnetic Field: Molecular Dynamics, Reaction Kinetics, and Spectroscopy Analysis. ACS Omega. 7(24). 20644–20655. 6 indexed citations

Petrova, T., M. Yu. Rubtsova, I. V. Uporov, et al.. (2022). Crystal structures of the molecular class A β-lactamase TEM-171 and its complexes with tazobactam. Acta Crystallographica Section D Structural Biology. 78(7). 825–834. 1 indexed citations

Gusakov, Alexander V., I. V. Uporov, & О. А. Синицына. (2020). Molecular dynamics simulations of two GH74 endo-processive xyloglucanases and the mutated variants to understand better the mechanism of the enzyme action. Biochimica et Biophysica Acta (BBA) - General Subjects. 1864(12). 129721–129721. 1 indexed citations

Efremova, Maria V., Aleksandr Barulin, Irina M. Le‐Deygen, et al.. (2018). In Situ Observation of Chymotrypsin Catalytic Activity Change Actuated by Nonheating Low-Frequency Magnetic Field. ACS Nano. 12(4). 3190–3199. 35 indexed citations

Gusakov, Alexander V., et al.. (2017). Site-directed mutagenesis of GH10 xylanase A from Penicillium canescens for determining factors affecting the enzyme thermostability. International Journal of Biological Macromolecules. 104(Pt A). 665–671. 30 indexed citations

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

Алексеева, А. В., et al.. (2012). Stabilization of plant formate dehydrogenase by rational design. Biochemistry (Moscow). 77(10). 1199–1209. 7 indexed citations

10.

Uporov, I. V., et al.. (2006). Theoretical study of interactions between muscle aldolase and F‐actin: Insight into different species. Biopolymers. 85(1). 60–71. 14 indexed citations

11.

Угарова, Н.Н., et al.. (2005). Bioluminescence Spectra of Native and Mutant Firefly Luciferases as a Function of pH. Biochemistry (Moscow). 70(11). 1262–1267. 52 indexed citations

12.

Орлова, М. А., T. A. Chubar, О. В. Игнатенко, et al.. (2003). Conformational Differences between Native and Recombinant Horseradish Peroxidase Revealed by Tritium Planigraphy. Biochemistry (Moscow). 68(11). 1225–1230. 6 indexed citations

13.

Lowe, Stephen L., et al.. (2003). Brownian dynamics simulations of glycolytic enzyme subsets with F‐actin. Biopolymers. 70(4). 456–470. 16 indexed citations

14.

Варфоломеев, С. Д., I. V. Uporov, & E.V. Fedorov. (2002). Bioinformatics and Molecular Modeling in Chemical Enzymology. Active Sites of Hydrolases. Biochemistry (Moscow). 67(10). 1099–1108. 41 indexed citations

15.

Uporov, I. V., Harvey R. Knull, Amanda K. Huber, & Kathryn A. Thomasson. (2001). Brownian Dynamics Simulations of Aldolase Binding Glyceraldehyde 3-Phosphate Dehydrogenase and the Possibility of Substrate Channeling. Biophysical Journal. 80(6). 2527–2535. 23 indexed citations

16.

Uporov, I. V., et al.. (2000). Computer Simulations of Glycolytic Enzyme Interactions with F-actin. Journal of Biomolecular Structure and Dynamics. 18(2). 311–323. 14 indexed citations

17.

Uporov, I. V., Harvey R. Knull, & Kathryn A. Thomasson. (1999). Brownian Dynamics Simulations of Interactions between Aldolase and G- or F-Actin. Biophysical Journal. 76(1). 17–27. 49 indexed citations

18.

Leontis, Neocles B., Michael Hills, Martial Piotto, et al.. (1995). Helical stacking in DNA three-way junctions containing two unpaired pyrimidines: proton NMR studies. Biophysical Journal. 68(1). 251–265. 24 indexed citations

19.

Uporov, I. V. & Neocles B. Leontis. (1995). Refinement of the solution structure of a branched DNA three-way junction. Biophysical Journal. 68(1). 266–274. 20 indexed citations

20.

Михайлов, А. С. & I. V. Uporov. (1980). Noise-induced phase transition and the percolation problem for fluctuating media with diffusion. Journal of Experimental and Theoretical Physics. 52. 989. 1 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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