Olga V. Stepanenko

1.1k total citations
64 papers, 833 citations indexed

About

Olga V. Stepanenko is a scholar working on Molecular Biology, Materials Chemistry and Cellular and Molecular Neuroscience. According to data from OpenAlex, Olga V. Stepanenko has authored 64 papers receiving a total of 833 indexed citations (citations by other indexed papers that have themselves been cited), including 47 papers in Molecular Biology, 21 papers in Materials Chemistry and 15 papers in Cellular and Molecular Neuroscience. Recurrent topics in Olga V. Stepanenko's work include Protein Structure and Dynamics (18 papers), Enzyme Structure and Function (18 papers) and Alzheimer's disease research and treatments (11 papers). Olga V. Stepanenko is often cited by papers focused on Protein Structure and Dynamics (18 papers), Enzyme Structure and Function (18 papers) and Alzheimer's disease research and treatments (11 papers). Olga V. Stepanenko collaborates with scholars based in Russia, United States and Finland. Olga V. Stepanenko's co-authors include Konstantin К. Turoverov, Irina М. Kuznetsova, Olesya V. Stepanenko, Vladislav V. Verkhusha, Daria M. Shcherbakova, Anna I. Sulatskaya, Vladimir N. Uversky, Olga I. Povarova, Maksim I. Sulatsky and Li Zhu and has published in prestigious journals such as PLoS ONE, Analytical Chemistry and The Journal of Physical Chemistry B.

In The Last Decade

Olga V. Stepanenko

62 papers receiving 829 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Olga V. Stepanenko Russia 16 567 156 134 128 121 64 833
M. Sameer Al‐Abdul‐Wahid Canada 18 837 1.5× 223 1.4× 55 0.4× 88 0.7× 207 1.7× 38 1.4k
Adil R. Abduragimov United States 21 524 0.9× 61 0.4× 68 0.5× 131 1.0× 58 0.5× 52 1.3k
Andrey Yu. Gorokhovatsky Russia 13 680 1.2× 51 0.3× 239 1.8× 72 0.6× 148 1.2× 25 914
Alexander V. Fonin Russia 12 543 1.0× 150 1.0× 35 0.3× 62 0.5× 52 0.4× 59 794
Chris S. Gandhi United States 15 1.1k 2.0× 78 0.5× 63 0.5× 80 0.6× 499 4.1× 17 1.4k
Massimo Bellanda Italy 18 629 1.1× 87 0.6× 31 0.2× 121 0.9× 88 0.7× 43 1.0k
Irene Coin Germany 21 1.5k 2.6× 127 0.8× 48 0.4× 54 0.4× 262 2.2× 38 1.8k
Amit Kessel Israel 19 992 1.7× 109 0.7× 24 0.2× 47 0.4× 85 0.7× 38 1.3k
Laura Baciou France 21 786 1.4× 118 0.8× 47 0.4× 103 0.8× 234 1.9× 62 1.1k
Karine Moncoq France 12 560 1.0× 75 0.5× 90 0.7× 19 0.1× 85 0.7× 20 730

Countries citing papers authored by Olga V. Stepanenko

Since Specialization
Citations

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

Fields of papers citing papers by Olga V. Stepanenko

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Olga V. Stepanenko

This figure shows the co-authorship network connecting the top 25 collaborators of Olga V. Stepanenko. A scholar is included among the top collaborators of Olga V. Stepanenko 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 Olga V. Stepanenko. Olga V. Stepanenko 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.
Sulatsky, Maksim I., et al.. (2025). Cathepsin B prevents cell death by fragmentation and destruction of pathological amyloid fibrils. Cell Death Discovery. 11(1). 61–61. 5 indexed citations
2.
Stepanenko, Olga V., et al.. (2025). Comprehensive picture of β-barrel transformation in the fibrillogenesis of odorant-binding proteins. International Journal of Biological Macromolecules. 309(Pt 1). 142709–142709. 1 indexed citations
3.
Stepanenko, Olga V., Maksim I. Sulatsky, Anna I. Sulatskaya, & Olesya V. Stepanenko. (2025). An unexpected insight into the cause of olfactory dysfunction: fibrillogenesis of odorant-binding proteins. Cell Death Discovery. 11(1). 370–370.
4.
Sulatsky, Maksim I., et al.. (2025). From protective enzyme to facilitator of amyloid propagation: Cathepsin D-mediated amyloid fibril fragmentation. International Journal of Biological Macromolecules. 304(Pt 2). 140971–140971. 1 indexed citations
5.
Sulatskaya, Anna I., Olga V. Stepanenko, Maksim I. Sulatsky, et al.. (2024). Structural determinants of odorant-binding proteins affecting their ability to form amyloid fibrils. International Journal of Biological Macromolecules. 264(8). 130699–130699. 3 indexed citations
6.
Stepanenko, Olga V., et al.. (2024). Degradation of pathogenic amyloids induced by matrix metalloproteinase-9. International Journal of Biological Macromolecules. 281(Pt 3). 136362–136362. 2 indexed citations
7.
Sulatsky, Maksim I., Olga V. Stepanenko, Olesya V. Stepanenko, et al.. (2024). Broken but not beaten: Challenge of reducing the amyloids pathogenicity by degradation. Journal of Advanced Research. 70. 45–62. 10 indexed citations
8.
Sulatsky, Maksim I., Olga V. Stepanenko, Olesya V. Stepanenko, et al.. (2023). Amyloid fibrils degradation: the pathway to recovery or aggravation of the disease?. Frontiers in Molecular Biosciences. 10. 1208059–1208059. 11 indexed citations
9.
Stepanenko, Olga V., Maksim I. Sulatsky, Olesya V. Stepanenko, et al.. (2020). Alpha-B-Crystallin Effect on Mature Amyloid Fibrils: Different Degradation Mechanisms and Changes in Cytotoxicity. International Journal of Molecular Sciences. 21(20). 7659–7659. 16 indexed citations
10.
Sulatskaya, Anna I., Maksim I. Sulatsky, Olga V. Stepanenko, et al.. (2020). Denaturing Effect of Guanidine Hydrohloride on Amyloid Fibrils. Biophysical Journal. 118(3). 509a–509a. 1 indexed citations
11.
Fonin, Alexander V., Olga V. Stepanenko, Iuliia A. Antifeeva, et al.. (2018). Folding of poly-amino acids and intrinsically disordered proteins in overcrowded milieu induced by pH change. International Journal of Biological Macromolecules. 125. 244–255. 10 indexed citations
12.
Stepanenko, Olesya V., Olga V. Stepanenko, Irina М. Kuznetsova, Vladislav V. Verkhusha, & Konstantin К. Turoverov. (2014). Sensitivity of Superfolder GFP to Ionic Agents. PLoS ONE. 9(10). e110750–e110750. 19 indexed citations
13.
Stepanenko, Olga V., Olesya V. Stepanenko, Maria Staiano, et al.. (2014). The Quaternary Structure of the Recombinant Bovine Odorant-Binding Protein Is Modulated by Chemical Denaturants. PLoS ONE. 9(1). e85169–e85169. 9 indexed citations
14.
Ostroumova, Olga S., Evgeny G. Chulkov, Olga V. Stepanenko, & Ludmila V. Schagina. (2013). Effect of flavonoids on the phase separation in giant unilamellar vesicles formed from binary lipid mixtures. Chemistry and Physics of Lipids. 178. 77–83. 20 indexed citations
15.
Stepanenko, Olesya V., Olga V. Stepanenko, Irina М. Kuznetsova, et al.. (2012). Distinct Effects of Guanidine Thiocyanate on the Structure of Superfolder GFP. PLoS ONE. 7(11). e48809–e48809. 21 indexed citations
16.
Fonin, Alexander V., et al.. (2011). Interaction between non-histone chromatin protein HMGB1 and linker histone H1. Cell and Tissue Biology. 5(2). 120–122. 3 indexed citations
17.
Fonin, Alexander V., et al.. (2010). Interaction between linker histone H1 and non-histone chromatin protein HMGB1. Spectroscopy An International Journal. 24(1-2). 165–168. 2 indexed citations
18.
Stepanenko, Olga V., Olga I. Povarova, Olesya V. Stepanenko, et al.. (2010). Structure and stability of D-galactose/D-glucose-binding protein. The role of D-glucose binding and Ca ion depletion. Spectroscopy An International Journal. 24(3-4). 355–359. 2 indexed citations
19.
Verkhusha, Vladislav V., et al.. (2003). Expression of recombinant GFP-actin fusion protein in the methylotrophic yeast. FEMS Yeast Research. 3(1). 105–111. 5 indexed citations
20.
Kuznetsova, Irina М., Olga V. Stepanenko, Konstantin К. Turoverov, et al.. (2002). Unraveling multistate unfolding of rabbit muscle creatine kinase. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1596(1). 138–155. 95 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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