L. G. Bobyleva

636 total citations
25 papers, 450 citations indexed

About

L. G. Bobyleva is a scholar working on Physiology, Molecular Biology and Cell Biology. According to data from OpenAlex, L. G. Bobyleva has authored 25 papers receiving a total of 450 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Physiology, 10 papers in Molecular Biology and 7 papers in Cell Biology. Recurrent topics in L. G. Bobyleva's work include Alzheimer's disease research and treatments (11 papers), Prion Diseases and Protein Misfolding (7 papers) and Fullerene Chemistry and Applications (5 papers). L. G. Bobyleva is often cited by papers focused on Alzheimer's disease research and treatments (11 papers), Prion Diseases and Protein Misfolding (7 papers) and Fullerene Chemistry and Applications (5 papers). L. G. Bobyleva collaborates with scholars based in Russia, Belgium and Hungary. L. G. Bobyleva's co-authors include A. G. Bobylev, I. M. Vikhlyantsev, Elmira I. Yakupova, Р. С. Фадеев, Z. A. Podlubnaya, Pavel A. Troshin, И. С. Фадеева, Jan Balzarini, А. Б. Корнев and Nikita V. Penkov and has published in prestigious journals such as Scientific Reports, International Journal of Molecular Sciences and Colloids and Surfaces B Biointerfaces.

In The Last Decade

L. G. Bobyleva

23 papers receiving 446 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
L. G. Bobyleva Russia 7 198 175 70 70 55 25 450
A. G. Bobylev Russia 14 311 1.6× 275 1.6× 88 1.3× 95 1.4× 75 1.4× 45 695
Elmira I. Yakupova Russia 7 203 1.0× 167 1.0× 42 0.6× 27 0.4× 39 0.7× 28 425
Irina Naletova Italy 17 288 1.5× 130 0.7× 96 1.4× 42 0.6× 75 1.4× 39 588
Kubra Kamisoglu United States 11 213 1.1× 132 0.8× 33 0.5× 23 0.3× 42 0.8× 15 547
Yu Feng China 16 315 1.6× 60 0.3× 69 1.0× 52 0.7× 35 0.6× 40 784
Ghazi M. Rahman Bangladesh 14 284 1.4× 42 0.2× 41 0.6× 59 0.8× 27 0.5× 18 523
Yee Ting Wong Singapore 8 186 0.9× 91 0.5× 49 0.7× 30 0.4× 28 0.5× 9 530
Juan R. Tejedo Spain 18 334 1.7× 168 1.0× 21 0.3× 22 0.3× 18 0.3× 42 779
Xinrui Li China 16 320 1.6× 61 0.3× 92 1.3× 34 0.5× 117 2.1× 55 767
Kellen Brunaldi Brazil 11 235 1.2× 111 0.6× 20 0.3× 22 0.3× 21 0.4× 22 485

Countries citing papers authored by L. G. Bobyleva

Since Specialization
Citations

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

Fields of papers citing papers by L. G. Bobyleva

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by L. G. Bobyleva. 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 L. G. Bobyleva. The network helps show where L. G. Bobyleva may publish in the future.

Co-authorship network of co-authors of L. G. Bobyleva

This figure shows the co-authorship network connecting the top 25 collaborators of L. G. Bobyleva. A scholar is included among the top collaborators of L. G. Bobyleva 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 L. G. Bobyleva. L. G. Bobyleva 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.
Bobyleva, L. G., Nikita V. Penkov, Azat Gabdulkhakov, et al.. (2025). Formation of an Amyloid-like Structure During In Vitro Interaction of Titin and Myosin-Binding Protein C. International Journal of Molecular Sciences. 26(14). 6910–6910. 1 indexed citations
2.
Bobyleva, L. G., et al.. (2024). Structural features of skeletal muscle titin aggregates. Молекулярная биология. 58(2). 314–324. 1 indexed citations
3.
Bobyleva, L. G., et al.. (2024). The Structural Features of Skeletal Muscle Titin Aggregates. Molecular Biology. 58(2). 319–327. 1 indexed citations
4.
Bobylev, A. G., Elmira I. Yakupova, L. G. Bobyleva, et al.. (2023). Nonspecific Amyloid Aggregation of Chicken Smooth-Muscle Titin: In Vitro Investigations. International Journal of Molecular Sciences. 24(2). 1056–1056. 1 indexed citations
5.
Bobyleva, L. G., et al.. (2022). Differential Expression of Titin and Obscurin mRNA in Striated Muscles of the Long-Tailed Ground Squirrel Urocitellus undulatus. Journal of Evolutionary Biochemistry and Physiology. 58(5). 1332–1340.
6.
Bobylev, A. G., et al.. (2021). Amyloid Aggregates of Smooth-Muscle Titin Impair Cell Adhesion. International Journal of Molecular Sciences. 22(9). 4579–4579. 6 indexed citations
7.
Yakupova, Elmira I., et al.. (2021). Amyloids: The History of Toxicity and Functionality. Biology. 10(5). 394–394. 19 indexed citations
8.
Bobyleva, L. G., Elmira I. Yakupova, Alexey K. Surin, et al.. (2021). Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro. International Journal of Molecular Sciences. 22(2). 731–731. 4 indexed citations
9.
Bobyleva, L. G., et al.. (2021). Stable Level of Giant Sarcomeric Cytoskeletal Proteins in Striated Muscles of the Edible Dormouse Glis glis during Hibernation. Journal of Evolutionary Biochemistry and Physiology. 57(4). 886–895. 2 indexed citations
10.
Rogachevsky, Vadim V., et al.. (2020). Predominant synthesis of giant myofibrillar proteins in striated muscles of the long-tailed ground squirrel Urocitellus undulatus during interbout arousal. Scientific Reports. 10(1). 15185–15185. 5 indexed citations
11.
Bobylev, A. G., Elmira I. Yakupova, L. G. Bobyleva, et al.. (2020). Changes in Titin Structure during Its Aggregation. Molecular Biology. 54(4). 578–585. 3 indexed citations
12.
Bobylev, A. G., Olga A. Kraevaya, L. G. Bobyleva, et al.. (2019). Anti-amyloid activities of three different types of water-soluble fullerene derivatives. Colloids and Surfaces B Biointerfaces. 183. 110426–110426. 18 indexed citations
13.
Yakupova, Elmira I., A. G. Bobylev, L. G. Bobyleva, & I. M. Vikhlyantsev. (2019). Study of the complement activation by amyloid aggregates of smooth muscle titin in vitro. Journal of Immunoassay and Immunochemistry. 41(2). 132–143. 1 indexed citations
14.
Yakupova, Elmira I., I. M. Vikhlyantsev, L. G. Bobyleva, et al.. (2017). Different amyloid aggregation of smooth muscles titin in vitro. Journal of Biomolecular Structure and Dynamics. 36(9). 2237–2248. 16 indexed citations
15.
Galzitskaya, Oxana V., Р. С. Фадеев, L. G. Bobyleva, et al.. (2016). Smooth muscle titin formsin vitroamyloid aggregates. Bioscience Reports. 36(3). 16 indexed citations
16.
Bobylev, A. G., Yu. V. Shatalin, I. M. Vikhlyantsev, et al.. (2014). Interaction of C60 fullerene-polyvinylpyrrolidone complex and brain Aβ(1–42)-peptide in vitro. BIOPHYSICS. 59(5). 685–688. 4 indexed citations
18.
Bobylev, A. G., et al.. (2012). Study of cytotoxicity of fullerene C60 derivatives. BIOPHYSICS. 57(5). 572–576. 6 indexed citations
19.
Bobylev, A. G., et al.. (2012). Antiamyloid properties of fullerene C60 derivatives. BIOPHYSICS. 57(3). 300–304. 9 indexed citations
20.
Bobylev, A. G., А. Б. Корнев, L. G. Bobyleva, et al.. (2011). Fullerenolates: metallated polyhydroxylated fullerenes with potent anti-amyloid activity. Organic & Biomolecular Chemistry. 9(16). 5714–5714. 52 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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