A. G. Bobylev

984 total citations
45 papers, 695 citations indexed

About

A. G. Bobylev is a scholar working on Molecular Biology, Physiology and Cell Biology. According to data from OpenAlex, A. G. Bobylev has authored 45 papers receiving a total of 695 indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 15 papers in Physiology and 11 papers in Cell Biology. Recurrent topics in A. G. Bobylev's work include Alzheimer's disease research and treatments (12 papers), Prion Diseases and Protein Misfolding (10 papers) and Fullerene Chemistry and Applications (9 papers). A. G. Bobylev is often cited by papers focused on Alzheimer's disease research and treatments (12 papers), Prion Diseases and Protein Misfolding (10 papers) and Fullerene Chemistry and Applications (9 papers). A. G. Bobylev collaborates with scholars based in Russia, France and United States. A. G. Bobylev's co-authors include I. M. Vikhlyantsev, L. G. Bobyleva, Elmira I. Yakupova, Z. A. Podlubnaya, Pavel A. Troshin, Р. С. Фадеев, И. С. Фадеева, Anton A. Nizhnikov, Anna I. Sulatskaya and Kirill S. Antonets and has published in prestigious journals such as SHILAP Revista de lepidopterología, PLoS ONE and Scientific Reports.

In The Last Decade

A. G. Bobylev

41 papers receiving 685 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
A. G. Bobylev Russia 14 311 275 95 88 81 45 695
Emanuela Cazzaniga Italy 17 340 1.1× 244 0.9× 44 0.5× 86 1.0× 65 0.8× 38 812
L. G. Bobyleva Russia 7 198 0.6× 175 0.6× 70 0.7× 70 0.8× 52 0.6× 25 450
Shenglan Wang China 17 418 1.3× 198 0.7× 57 0.6× 65 0.7× 60 0.7× 62 1.1k
Yuting Wang China 16 471 1.5× 189 0.7× 38 0.4× 42 0.5× 97 1.2× 59 1.0k
I. M. Vikhlyantsev Russia 14 378 1.2× 298 1.1× 33 0.3× 49 0.6× 50 0.6× 72 743
Neeraj Singh United States 18 277 0.9× 189 0.7× 20 0.2× 105 1.2× 60 0.7× 41 958
Yaru Huang China 15 269 0.9× 256 0.9× 19 0.2× 129 1.5× 169 2.1× 59 938
Lian Liu China 20 657 2.1× 74 0.3× 69 0.7× 46 0.5× 85 1.0× 88 1.2k
Harry Fein United States 8 225 0.7× 176 0.6× 40 0.4× 39 0.4× 110 1.4× 12 849

Countries citing papers authored by A. G. Bobylev

Since Specialization
Citations

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

Fields of papers citing papers by A. G. Bobylev

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of A. G. Bobylev

This figure shows the co-authorship network connecting the top 25 collaborators of A. G. Bobylev. A scholar is included among the top collaborators of A. G. Bobylev 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 A. G. Bobylev. A. G. Bobylev 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.
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
3.
Belousov, M. V., Maksim I. Sulatsky, Anna I. Sulatskaya, et al.. (2023). OmpC and OmpF Outer Membrane Proteins of Escherichia coli and Salmonella enterica Form Bona Fide Amyloids. International Journal of Molecular Sciences. 24(21). 15522–15522. 14 indexed citations
4.
Volkov, Kirill V., Julia V. Sopova, A. G. Bobylev, et al.. (2022). Human RAD51 Protein Forms Amyloid-like Aggregates In Vitro. International Journal of Molecular Sciences. 23(19). 11657–11657. 2 indexed citations
5.
Belousov, M. V., Maksim I. Sulatsky, Anna V. Tsyganova, et al.. (2022). RopB protein of Rhizobium leguminosarum bv. viciae adopts amyloid state during symbiotic interactions with pea (Pisum sativum L.). Frontiers in Plant Science. 13. 1014699–1014699. 6 indexed citations
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.
Antonets, Kirill S., M. V. Belousov, Anna I. Sulatskaya, et al.. (2020). Accumulation of storage proteins in plant seeds is mediated by amyloid formation. PLoS Biology. 18(7). e3000564–e3000564. 54 indexed citations
8.
9.
Bobylev, A. G., Elmira I. Yakupova, С. П. Белова, et al.. (2020). Inhibition of Histone Deacetylase 1 Prevents the Decrease in Titin (Connectin) Content and Development of Atrophy in Rat m. soleus after 3-Day Hindlimb Unloading. Bulletin of Experimental Biology and Medicine. 169(4). 450–457. 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., 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
12.
Yakupova, Elmira I., I. M. Vikhlyantsev, M. Yu. Lobanov, Oxana V. Galzitskaya, & A. G. Bobylev. (2017). Amyloid properties of titin. Biochemistry (Moscow). 82(13). 1675–1685. 3 indexed citations
13.
Bobylev, A. G., et al.. (2017). Chronic alcohol intoxication is not accompanied by an increase in calpain proteolytic activity in cardiac muscle of rats. Biochemistry (Moscow). 82(2). 168–175. 2 indexed citations
14.
15.
Бобкова, Н. В., Dmitry N. Lyabin, N. I. Medvinskaya, et al.. (2015). The Y-Box Binding Protein 1 Suppresses Alzheimer’s Disease Progression in Two Animal Models. PLoS ONE. 10(9). e0138867–e0138867. 23 indexed citations
16.
Vikhlyantsev, I. M., et al.. (2013). Method for isolation of intact titin (connectin) molecules from mammalian cardiac muscle. Biochemistry (Moscow). 78(5). 455–462. 3 indexed citations
17.
18.
Podlubnaya, Z. A. & A. G. Bobylev. (2012). On functional amyloids of muscle proteins of titin family. BIOPHYSICS. 57(5). 577–580. 3 indexed citations
19.
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
20.
Bobylev, A. G., et al.. (2010). Effect of nitroderivatives of fullerene C60 on amyloid fibrils of the brain Aβ(1–42) peptide and muscle X-protein. BIOPHYSICS. 55(3). 353–357. 7 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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