Konstantin S. Vassilenko

667 total citations
15 papers, 519 citations indexed

About

Konstantin S. Vassilenko is a scholar working on Molecular Biology, Plant Science and Cardiology and Cardiovascular Medicine. According to data from OpenAlex, Konstantin S. Vassilenko has authored 15 papers receiving a total of 519 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 4 papers in Plant Science and 3 papers in Cardiology and Cardiovascular Medicine. Recurrent topics in Konstantin S. Vassilenko's work include RNA and protein synthesis mechanisms (10 papers), RNA modifications and cancer (4 papers) and Protein Structure and Dynamics (4 papers). Konstantin S. Vassilenko is often cited by papers focused on RNA and protein synthesis mechanisms (10 papers), RNA modifications and cancer (4 papers) and Protein Structure and Dynamics (4 papers). Konstantin S. Vassilenko collaborates with scholars based in Russia and United States. Konstantin S. Vassilenko's co-authors include S.Yu. Venyaminov, Vladimir N. Uversky, Alexander S. Spirin, Sergey E. Dmitriev, Ivan N. Shatsky, Vladimir V. Rogov, A.T. Gudkov, Anne E. Simon, Konstantin К. Turoverov and Sofia Khaitlina and has published in prestigious journals such as Nucleic Acids Research, Analytical Biochemistry and Biophysical Journal.

In The Last Decade

Konstantin S. Vassilenko

15 papers receiving 516 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Konstantin S. Vassilenko Russia 13 432 91 63 60 43 15 519
Anil Thakur India 10 439 1.0× 78 0.9× 23 0.4× 34 0.6× 31 0.7× 22 576
Sébastien Violot France 13 384 0.9× 97 1.1× 44 0.7× 36 0.6× 21 0.5× 25 594
Chris H. Hill United Kingdom 17 655 1.5× 86 0.9× 53 0.8× 49 0.8× 102 2.4× 29 919
Jörg A. Schenk Germany 13 330 0.8× 42 0.5× 88 1.4× 43 0.7× 43 1.0× 40 521
Stanley C. Kwok United States 13 419 1.0× 39 0.4× 54 0.9× 138 2.3× 27 0.6× 22 561
Alastair Muir United Kingdom 8 234 0.5× 44 0.5× 46 0.7× 28 0.5× 17 0.4× 10 334
Jesper Lykkegaard Karlsen Denmark 8 471 1.1× 51 0.6× 52 0.8× 50 0.8× 92 2.1× 12 694
Christopher T. Jurgenson United States 10 382 0.9× 101 1.1× 28 0.4× 52 0.9× 135 3.1× 12 631
Fernanda L. Sirota Singapore 13 407 0.9× 60 0.7× 15 0.2× 28 0.5× 73 1.7× 21 550
Lenin Domínguez‐Ramírez Mexico 11 413 1.0× 49 0.5× 13 0.2× 21 0.3× 46 1.1× 42 568

Countries citing papers authored by Konstantin S. Vassilenko

Since Specialization
Citations

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

Fields of papers citing papers by Konstantin S. Vassilenko

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Konstantin S. Vassilenko. 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 Konstantin S. Vassilenko. The network helps show where Konstantin S. Vassilenko may publish in the future.

Co-authorship network of co-authors of Konstantin S. Vassilenko

This figure shows the co-authorship network connecting the top 25 collaborators of Konstantin S. Vassilenko. A scholar is included among the top collaborators of Konstantin S. Vassilenko 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 Konstantin S. Vassilenko. Konstantin S. Vassilenko is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

15 of 15 papers shown
1.
Vassilenko, Konstantin S., et al.. (2023). High-Resolution Structure and Internal Mobility of a Plant 40S Ribosomal Subunit. International Journal of Molecular Sciences. 24(24). 17453–17453. 3 indexed citations
2.
Vassilenko, Konstantin S., et al.. (2021). Non-Canonical Translation Initiation Mechanisms Employed by Eukaryotic Viral mRNAs. Biochemistry (Moscow). 86(9). 1060–1094. 37 indexed citations
3.
Maksimova, Elena, et al.. (2021). RbfA Is Involved in Two Important Stages of 30S Subunit Assembly: Formation of the Central Pseudoknot and Docking of Helix 44 to the Decoding Center. International Journal of Molecular Sciences. 22(11). 6140–6140. 17 indexed citations
4.
Gao, Feng, et al.. (2018). Unusual dicistronic expression from closely spaced initiation codons in an umbravirus subgenomic RNA. Nucleic Acids Research. 46(22). 11726–11742. 12 indexed citations
5.
Du, Zhiyou, et al.. (2017). Concerted action of two 3′ cap-independent translation enhancers increases the competitive strength of translated viral genomes. Nucleic Acids Research. 45(16). 9558–9572. 22 indexed citations
6.
Nikonorova, Inna A., et al.. (2014). Identification of a Mg2+-sensitive ORF in the 5′-leader of TRPM7 magnesium channel mRNA. Nucleic Acids Research. 42(20). 12779–12788. 17 indexed citations
7.
Vassilenko, Konstantin S., et al.. (2012). Translation initiation in eukaryotes: Versatility of the scanning model. Biochemistry (Moscow). 77(13). 1465–1477. 16 indexed citations
8.
Vassilenko, Konstantin S., et al.. (2011). Unidirectional constant rate motion of the ribosomal scanning particle during eukaryotic translation initiation. Nucleic Acids Research. 39(13). 5555–5567. 62 indexed citations
9.
Shirokikh, Nikolay E., et al.. (2009). Quantitative analysis of ribosome–mRNA complexes at different translation stages. Nucleic Acids Research. 38(3). e15–e15. 33 indexed citations
10.
Vassilenko, Konstantin S., et al.. (2007). Translation of non-capped mRNAs in a eukaryotic cell-free system: acceleration of initiation rate in the course of polysome formation. Nucleic Acids Research. 35(19). 6547–6559. 26 indexed citations
11.
Vassilenko, Konstantin S. & Vladimir N. Uversky. (2002). Native-like secondary structure of molten globules. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1594(1). 168–177. 64 indexed citations
12.
Uversky, Vladimir N., Ziedulla Abdullaev, Eduard V. Bocharov, et al.. (1999). Structure and stability of recombinant protein depend on the extra N-terminal methionine residue: S6 permutein from direct and fusion expression systems. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1432(2). 324–332. 4 indexed citations
13.
Kuznetsova, Irina М., et al.. (1999). Effect of Self-Association on the Structural Organization of Partially Folded Proteins: Inactivated Actin. Biophysical Journal. 77(5). 2788–2800. 41 indexed citations
14.
15.
Venyaminov, S.Yu. & Konstantin S. Vassilenko. (1994). Determination of Protein Tertiary Structure Class from Circular Dichroism Spectra. Analytical Biochemistry. 222(1). 176–184. 107 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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