А. В. Липкин

818 total citations
36 papers, 626 citations indexed

About

А. В. Липкин is a scholar working on Molecular Biology, Genetics and Materials Chemistry. According to data from OpenAlex, А. В. Липкин has authored 36 papers receiving a total of 626 indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 10 papers in Genetics and 5 papers in Materials Chemistry. Recurrent topics in А. В. Липкин's work include Venomous Animal Envenomation and Studies (7 papers), Enzyme Structure and Function (5 papers) and Ion channel regulation and function (4 papers). А. В. Липкин is often cited by papers focused on Venomous Animal Envenomation and Studies (7 papers), Enzyme Structure and Function (5 papers) and Ion channel regulation and function (4 papers). А. В. Липкин collaborates with scholars based in Russia, United Kingdom and Sweden. А. В. Липкин's co-authors include Eugene V. Grishin, A. N. Fedorov, Sergey Filkin, Sergey A. Kozlov, Kirill A. Pluzhnikov, E. D. Nosyreva, Yuliya V. Korolkova, Kamilla Angelo, Søren‐Peter Olesen and Tatiana V. Rakitina and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Power Sources and Scientific Reports.

In The Last Decade

А. В. Липкин

35 papers receiving 611 citations

Peers

А. В. Липкин
Yue Qiu China
Hoi Jong Jung South Korea
Irina Dementieva United States
C. Eric Hodgman United States
Joost W. Gouw Netherlands
А. В. Липкин
Citations per year, relative to А. В. Липкин А. В. Липкин (= 1×) peers Michael Hoffmann

Countries citing papers authored by А. В. Липкин

Since Specialization
Citations

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

Fields of papers citing papers by А. В. Липкин

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by А. В. Липкин. 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 А. В. Липкин. The network helps show where А. В. Липкин may publish in the future.

Co-authorship network of co-authors of А. В. Липкин

This figure shows the co-authorship network connecting the top 25 collaborators of А. В. Липкин. A scholar is included among the top collaborators of А. В. Липкин 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 А. В. Липкин. А. В. Липкин 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.
Власова, Н. Н., et al.. (2024). A method for producing protease pS273R of the African swine fever virus. Journal of Virological Methods. 330. 115037–115037.
2.
Filkin, Sergey, et al.. (2020). Expression, purification and biophysical characterization of recombinant Streptomyces violaceoruber phospholipase PLA2 overproduced in Pichia pastoris. Preparative Biochemistry & Biotechnology. 50(6). 549–555. 5 indexed citations
3.
Boyko, Konstantin M., Yu. M. Chesnokov, Michael Hons, et al.. (2018). 3D structure of the natural tetrameric form of human butyrylcholinesterase as revealed by cryoEM, SAXS and MD. Biochimie. 156. 196–205. 28 indexed citations
4.
Nikolaeva, A.Y., et al.. (2015). Isolation, purification, crystallization, and preliminary X-ray diffraction study of the crystals of HU protein from M. gallisepticum. Crystallography Reports. 60(6). 880–883. 9 indexed citations
5.
Тимофеев, В. И., M.A. Gorbacheva, Konstantin M. Boyko, et al.. (2015). Structure of recombinant prolidase fromThermococcus sibiricusin space groupP21221. Acta Crystallographica Section F Structural Biology Communications. 71(8). 951–957. 4 indexed citations
6.
Nekrasov, A. N., et al.. (2015). Truncated variants of Serratia proteamaculans oligopeptidase B having different activities. Biochemistry (Moscow). 80(10). 1331–1343. 8 indexed citations
7.
Machulin, Andrey V., et al.. (2015). New insight into formation of DNA-containing microparticles during PCR: the scaffolding role of magnesium pyrophosphate crystals. Journal of Biomolecular Structure and Dynamics. 34(3). 625–639. 6 indexed citations
8.
Pankratov, Dmitry, Javier Sotres, Ivan Maximov, et al.. (2015). Transparent and flexible, nanostructured and mediatorless glucose/oxygen enzymatic fuel cells. Journal of Power Sources. 294. 501–506. 38 indexed citations
9.
Boyko, Konstantin M., et al.. (2014). Identification of the ligand in the structure of the protein with unknown function STM4435 from Salmonella typhimurium. Doklady Biochemistry and Biophysics. 457(1). 121–124. 2 indexed citations
10.
Boyko, Konstantin M., M.A. Gorbacheva, Tatiana V. Rakitina, et al.. (2014). Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein fromSpiroplasma melliferumKC3. Acta Crystallographica Section F Structural Biology Communications. 71(1). 24–27. 24 indexed citations
11.
Смирнова, Е. В., et al.. (2011). Novel protein haponin regulates cellular response to oxidative stress. Doklady Biochemistry and Biophysics. 440(1). 225–227. 7 indexed citations
12.
Lassot, Irina, Ian Robbins, Mark Kristiansen, et al.. (2010). Trim17, a novel E3 ubiquitin-ligase, initiates neuronal apoptosis. Cell Death and Differentiation. 17(12). 1928–1941. 39 indexed citations
14.
Липкин, А. В., Ekaterina Barsova, Elena Leychenko, et al.. (2006). Amino acid sequence of RTX-A's isoform actinoporin from the sea anemone, Radianthus macrodactylus. Toxicon. 47(5). 517–520. 20 indexed citations
15.
Липкин, А. В., et al.. (2005). An antimicrobial peptide Ar-AMP from amaranth (Amaranthus retroflexus L.) seeds. Phytochemistry. 66(20). 2426–2431. 73 indexed citations
16.
Desagher, Solange, Dany Séverac, А. В. Липкин, et al.. (2004). Genes Regulated in Neurons Undergoing Transcription-dependent Apoptosis Belong to Signaling Pathways Rather than the Apoptotic Machinery. Journal of Biological Chemistry. 280(7). 5693–5702. 39 indexed citations
17.
Korolkova, Yuliya V., Eduard V. Bocharov, Kamilla Angelo, et al.. (2002). New Binding Site on Common Molecular Scaffold Provides HERG Channel Specificity of Scorpion Toxin BeKm-1. Journal of Biological Chemistry. 277(45). 43104–43109. 53 indexed citations
18.
Липкин, А. В., et al.. (2002). Novel insecticidal toxins from the venom of the spider Segestria florentina. Toxicon. 40(2). 125–130. 23 indexed citations
19.
Korolkova, Yuliya V., Sergey A. Kozlov, А. В. Липкин, et al.. (2001). An ERG Channel Inhibitor from the Scorpion Buthus eupeus. Journal of Biological Chemistry. 276(13). 9868–9876. 81 indexed citations
20.
Kiyatkin, N.I., et al.. (1992). Structure of the low molecular weight protein copurified with α-latrotoxin. Toxicon. 30(7). 771–774. 38 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026