Leonid M. Vinokurov

912 total citations
24 papers, 746 citations indexed

About

Leonid M. Vinokurov is a scholar working on Molecular Biology, Biophysics and Genetics. According to data from OpenAlex, Leonid M. Vinokurov has authored 24 papers receiving a total of 746 indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 11 papers in Biophysics and 6 papers in Genetics. Recurrent topics in Leonid M. Vinokurov's work include Advanced Fluorescence Microscopy Techniques (9 papers), RNA and protein synthesis mechanisms (6 papers) and Bacterial Genetics and Biotechnology (5 papers). Leonid M. Vinokurov is often cited by papers focused on Advanced Fluorescence Microscopy Techniques (9 papers), RNA and protein synthesis mechanisms (6 papers) and Bacterial Genetics and Biotechnology (5 papers). Leonid M. Vinokurov collaborates with scholars based in Russia, Germany and Tajikistan. Leonid M. Vinokurov's co-authors include Alexander V. Yakhnin, Andrey Yu. Gorokhovatsky, Yu.B. Alakhov, Sergey Lukyanov, Kseniya N. Markvicheva, Natalia M. Mishina, Vsevolod V. Belousov, Dmitry S. Bilan, Evgeny Kulesskiy and Yu.A. Ovchinnikov and has published in prestigious journals such as Biochemistry, Analytical Biochemistry and Scientific Reports.

In The Last Decade

Leonid M. Vinokurov

24 papers receiving 716 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Leonid M. Vinokurov Russia 14 581 139 82 73 69 24 746
Desiree A. Thayer United States 11 668 1.1× 50 0.4× 39 0.5× 63 0.9× 62 0.9× 13 868
Jean‐René Alattia Canada 13 504 0.9× 80 0.6× 59 0.7× 34 0.5× 25 0.4× 18 694
Dennis M. Mishler United States 10 643 1.1× 67 0.5× 16 0.2× 139 1.9× 48 0.7× 13 759
F.G. Prendergast United States 10 388 0.7× 166 1.2× 33 0.4× 44 0.6× 9 0.1× 12 566
Montse Morell Spain 10 584 1.0× 34 0.2× 17 0.2× 105 1.4× 69 1.0× 12 723
Fu‐Sen Liang United States 15 727 1.3× 25 0.2× 27 0.3× 94 1.3× 29 0.4× 37 933
Robin Hurst United States 17 848 1.5× 39 0.3× 16 0.2× 47 0.6× 97 1.4× 34 1.1k
Roberta Spadaccini Italy 21 666 1.1× 24 0.2× 22 0.3× 56 0.8× 47 0.7× 41 996
Alexander S. Paramonov Russia 19 846 1.5× 17 0.1× 184 2.2× 104 1.4× 39 0.6× 72 1.0k
Iwan Zimmermann Switzerland 15 723 1.2× 23 0.2× 24 0.3× 76 1.0× 238 3.4× 19 1.0k

Countries citing papers authored by Leonid M. Vinokurov

Since Specialization
Citations

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

Fields of papers citing papers by Leonid M. Vinokurov

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Leonid M. Vinokurov. 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 Leonid M. Vinokurov. The network helps show where Leonid M. Vinokurov may publish in the future.

Co-authorship network of co-authors of Leonid M. Vinokurov

This figure shows the co-authorship network connecting the top 25 collaborators of Leonid M. Vinokurov. A scholar is included among the top collaborators of Leonid M. Vinokurov 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 Leonid M. Vinokurov. Leonid M. Vinokurov 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.
Chizhik, Alexey I., Leonid M. Vinokurov, Т. В. Ивашина, et al.. (2018). Monomerization of the photoconvertible fluorescent protein SAASoti by rational mutagenesis of single amino acids. Scientific Reports. 8(1). 15542–15542. 11 indexed citations
2.
Ивашина, Т. В., et al.. (2011). Induction-resonance energy transfer between the terbium-binding peptide and the red fluorescent proteins DsRed2 and TagRFP. BIOPHYSICS. 56(3). 381–386. 3 indexed citations
3.
Русанов, А. Л., et al.. (2010). FRET-sensor for imaging with lifetime resolution. Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE. 7376. 737611–737611. 7 indexed citations
4.
Русанов, А. Л., Т. В. Ивашина, Leonid M. Vinokurov, et al.. (2010). Lifetime imaging of FRET between red fluorescent proteins. Journal of Biophotonics. 3(12). 774–783. 23 indexed citations
5.
Markvicheva, Kseniya N., Dmitry S. Bilan, Natalia M. Mishina, et al.. (2010). A genetically encoded sensor for H2O2 with expanded dynamic range. Bioorganic & Medicinal Chemistry. 19(3). 1079–1084. 149 indexed citations
6.
Ивашина, Т. В., et al.. (2010). Genetically encoded FRET-pair on the basis of terbium-binding peptide and red fluorescent protein. Applied Biochemistry and Microbiology. 46(2). 154–158. 6 indexed citations
7.
Zvyagin, Ivan V., et al.. (2008). Universal and rapid method for purification of GFP-like proteins by the ethanol extraction. Protein Expression and Purification. 65(1). 108–113. 24 indexed citations
8.
Ксензенко, В. Н., et al.. (2007). Barnase–barstar high affinity interaction phenomenon as the base for the heterogenous bioluminescence pseudorabies virus' immunoassay. Journal of Biochemical and Biophysical Methods. 70(4). 605–611. 4 indexed citations
9.
Zhang, Lijuan, Nadya G. Gurskaya, Ekaterina M. Merzlyak, et al.. (2007). Method for Real-Time Monitoring of Protein Degradation at the Single Cell Level. BioTechniques. 42(4). 446–450. 72 indexed citations
10.
Gorokhovatsky, Andrey Yu., Victor Marchenkov, Т. В. Ивашина, et al.. (2004). Fusion of Aequorea victoria GFP and aequorin provides their Ca2+-induced interaction that results in red shift of GFP absorption and efficient bioluminescence energy transfer. Biochemical and Biophysical Research Communications. 320(3). 703–711. 46 indexed citations
11.
Kulesskiy, Evgeny, et al.. (2003). Expression of the recombinant antibacterial peptide sarcotoxin IA in Escherichia coli cells. Protein Expression and Purification. 28(2). 350–356. 65 indexed citations
12.
Есикова, Т. З., et al.. (2003). A Catecholic Siderophore Produced by the Thermoresistant Bacilluslicheniformis VK21 Strain. Russian Journal of Bioorganic Chemistry. 29(6). 542–549. 22 indexed citations
13.
Gorokhovatsky, Andrey Yu., et al.. (2003). Homogeneous assay for biotin based on Aequorea victoria bioluminescence resonance energy transfer system. Analytical Biochemistry. 313(1). 68–75. 17 indexed citations
14.
Yakhnin, Alexander V., et al.. (2002). EGFP as a fusion partner for the expression and organic extraction of small polypeptides. Protein Expression and Purification. 27(1). 55–62. 48 indexed citations
15.
Vinokurov, Leonid M., et al.. (2001). The Dependence of Stability of the Green Fluorescent Protein–Obelin Hybrids on the Nature of Their Constituent Modules and the Structure of the Amino Acid Linker. Russian Journal of Bioorganic Chemistry. 27(5). 323–329. 3 indexed citations
16.
Yakhnin, Alexander V., et al.. (1998). Green Fluorescent Protein Purification by Organic Extraction. Protein Expression and Purification. 14(3). 382–386. 82 indexed citations
17.
Matveev, Sergey V., et al.. (1996). Effect of the ATP level on the overall protein biosynthesis rate in a wheat germ cell-free system. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1293(2). 207–212. 19 indexed citations
18.
Ryabova, Lyubov A., et al.. (1995). Acetyl Phosphate as an Energy Source for Bacterial Cell-Free Translation Systems. Analytical Biochemistry. 226(1). 184–186. 56 indexed citations
19.
Ovchinnikov, Yu.A., et al.. (1982). The primary structure of elongation factor from Escherichia coli. FEBS Letters. 139(1). 130–135. 41 indexed citations
20.
Vinokurov, Leonid M., et al.. (1976). The primary structure of protein L10 from Escherichia coli ribosomes. FEBS Letters. 67(1). 58–61. 13 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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