Sergei E. Permyakov

2.3k total citations
103 papers, 1.8k citations indexed

About

Sergei E. Permyakov is a scholar working on Molecular Biology, Physiology and Oncology. According to data from OpenAlex, Sergei E. Permyakov has authored 103 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 87 papers in Molecular Biology, 17 papers in Physiology and 15 papers in Oncology. Recurrent topics in Sergei E. Permyakov's work include Protein Structure and Dynamics (23 papers), S100 Proteins and Annexins (21 papers) and Enzyme Structure and Function (11 papers). Sergei E. Permyakov is often cited by papers focused on Protein Structure and Dynamics (23 papers), S100 Proteins and Annexins (21 papers) and Enzyme Structure and Function (11 papers). Sergei E. Permyakov collaborates with scholars based in Russia, United States and Finland. Sergei E. Permyakov's co-authors include Eugene A. Permyakov, Vladimir N. Uversky, Alexander I. Denesyuk, Ekaterina L. Knyazeva, Anthony L. Fink, John Goers, Evgeni Yu. Zernii, Pavel P. Philippov, Ivan I. Senin and Alexei S. Kazakov and has published in prestigious journals such as Journal of Biological Chemistry, SHILAP Revista de lepidopterología and PLoS ONE.

In The Last Decade

Sergei E. Permyakov

100 papers receiving 1.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Sergei E. Permyakov Russia 25 1.2k 277 228 215 207 103 1.8k
Barbara Spolaore Italy 25 1.5k 1.2× 130 0.5× 152 0.7× 170 0.8× 128 0.6× 45 2.2k
Roberto Fattorusso Italy 29 1.9k 1.5× 179 0.6× 227 1.0× 139 0.6× 225 1.1× 129 2.7k
Joseph F. Leykam United States 25 1.5k 1.2× 143 0.5× 99 0.4× 179 0.8× 174 0.8× 39 2.4k
Minh Lam United States 29 1.3k 1.1× 114 0.4× 357 1.6× 132 0.6× 116 0.6× 55 2.4k
Jui‐Yoa Chang United States 29 1.8k 1.5× 148 0.5× 261 1.1× 138 0.6× 190 0.9× 93 2.8k
Luís Maurício T. R. Lima Brazil 27 1.3k 1.1× 228 0.8× 329 1.4× 304 1.4× 53 0.3× 102 2.0k
Peilong Lu China 17 1.4k 1.1× 66 0.2× 210 0.9× 378 1.8× 130 0.6× 32 2.1k
Yuying Zhang China 24 1.0k 0.8× 89 0.3× 123 0.5× 86 0.4× 65 0.3× 92 1.8k
Irantzu Pallarès Spain 19 972 0.8× 84 0.3× 128 0.6× 357 1.7× 96 0.5× 44 1.4k
Chi L.L. Pham Australia 25 926 0.7× 97 0.4× 107 0.5× 844 3.9× 216 1.0× 48 1.8k

Countries citing papers authored by Sergei E. Permyakov

Since Specialization
Citations

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

Fields of papers citing papers by Sergei E. Permyakov

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Sergei E. Permyakov. 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 Sergei E. Permyakov. The network helps show where Sergei E. Permyakov may publish in the future.

Co-authorship network of co-authors of Sergei E. Permyakov

This figure shows the co-authorship network connecting the top 25 collaborators of Sergei E. Permyakov. A scholar is included among the top collaborators of Sergei E. Permyakov 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 Sergei E. Permyakov. Sergei E. Permyakov 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.
Luginina, Aleksandra, Ivan Maslov, Marina P. Shevelyova, et al.. (2025). Unlocking GPCR–ligand interactions: Measuring binding affinities with thermal shift assay. Protein Science. 34(5). e70120–e70120.
2.
Chistyakov, Dmitry V., Olga Gancharova, Viktoriia E. Baksheeva, et al.. (2024). Targeting Oxidative Stress and Inflammation in the Eye: Insights from a New Model of Experimental Autoimmune Uveitis. International Journal of Molecular Sciences. 25(23). 12910–12910. 3 indexed citations
3.
Denessiouk, Konstantin, Alexander I. Denesyuk, Sergei E. Permyakov, et al.. (2023). The active site of the SGNH hydrolase-like fold proteins: Nucleophile–oxyanion (Nuc-Oxy) and Acid–Base zones. SHILAP Revista de lepidopterología. 7. 100123–100123. 3 indexed citations
4.
Permyakov, Sergei E., et al.. (2020). Mouse S100G protein exhibits properties characteristic of a calcium sensor. Cell Calcium. 87. 102185–102185. 4 indexed citations
5.
Kazakov, Alexei S., Andrey S. Sokolov, Victor Marchenkov, et al.. (2019). The binding of monomeric amyloid β peptide to serum albumin is affected by major plasma unsaturated fatty acids. Biochemical and Biophysical Research Communications. 510(2). 248–253. 24 indexed citations
6.
Zernii, Evgeni Yu., Viktoriia E. Baksheeva, Alexei S. Kazakov, et al.. (2018). Photoreceptor calcium sensor proteins in detergent-resistant membrane rafts are regulated via binding to caveolin-1. Cell Calcium. 73. 55–69. 11 indexed citations
7.
Kazakov, Alexei S., et al.. (2017). Calcium-dependent interaction of monomeric S100P protein with serum albumin. International Journal of Biological Macromolecules. 108. 143–148. 3 indexed citations
8.
Kazakov, Alexei S., et al.. (2017). In search for globally disordered apo-parvalbumins: Case of parvalbumin β-1 from coho salmon. Cell Calcium. 67. 53–64. 11 indexed citations
9.
Permyakov, Eugene A., Vladimir N. Uversky, & Sergei E. Permyakov. (2016). Interleukin-11: A Multifunctional Cytokine with Intrinsically Disordered Regions. Cell Biochemistry and Biophysics. 74(3). 285–296. 14 indexed citations
10.
Breydo, Leonid, Amanda Sales Conniff, Luísa A. Ferreira, et al.. (2015). Effects of osmolytes on protein-solvent interactions in crowded environment: Analyzing the effect of TMAO on proteins in crowded solutions. Archives of Biochemistry and Biophysics. 570. 66–74. 19 indexed citations
11.
Kaspersen, Jørn Døvling, Jannik Nedergaard Pedersen, Søren B. Nielsen, et al.. (2014). Generic Structures of Cytotoxic Liprotides: Nano‐Sized Complexes with Oleic Acid Cores and Shells of Disordered Proteins. ChemBioChem. 15(18). 2693–2702. 35 indexed citations
12.
Permyakov, Sergei E., et al.. (2014). Parvalbumin as a metal-dependent antioxidant. Cell Calcium. 55(5). 261–268. 6 indexed citations
13.
Zernii, Evgeni Yu., Ilya I. Grigoriev, Konstantin E. Komolov, et al.. (2013). New mechanisms of regulatory activity of photoreceptor calcium sensors. FEBS Journal. 280. 438–439. 2 indexed citations
14.
Permyakov, Sergei E., et al.. (2011). Intrinsic disorder in S100 proteins. Molecular BioSystems. 7(7). 2164–2180. 29 indexed citations
15.
Permyakov, Sergei E., Evgeni Yu. Zernii, Ekaterina L. Knyazeva, et al.. (2011). Oxidation mimicking substitution of conservative cysteine in recoverin suppresses its membrane association. Amino Acids. 42(4). 1435–1442. 29 indexed citations
16.
Permyakov, Sergei E., et al.. (2010). Analysis of Ca2+/Mg2+ selectivity in α‐lactalbumin and Ca2+‐binding lysozyme reveals a distinct Mg2+‐specific site in lysozyme. Proteins Structure Function and Bioinformatics. 78(12). 2609–2624. 9 indexed citations
17.
Knyazeva, Ekaterina L., et al.. (2009). Interaction of antitumor α-lactalbumin—oleic acid complexes with artificial and natural membranes. Journal of Bioenergetics and Biomembranes. 41(3). 229–237. 33 indexed citations
18.
Permyakov, Sergei E., et al.. (2009). Metal-controlled interdomain cooperativity in parvalbumins. Cell Calcium. 46(3). 163–175. 19 indexed citations
19.
Permyakov, Sergei E., et al.. (2006). Calcium‐binding and temperature induced transitions in equine lysozyme: New insights from the pCa–temperature “phase diagrams”. Proteins Structure Function and Bioinformatics. 65(4). 984–998. 11 indexed citations
20.
Permyakov, Sergei E., Vladimir N. Uversky, Dmitry B. Veprintsev, et al.. (2001). Mutating aspartate in the calcium-binding site of α-lactalbumin: effects on the protein stability and cation binding. Protein Engineering Design and Selection. 14(10). 785–789. 23 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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