Konstantin M. Boyko

1.5k total citations
105 papers, 988 citations indexed

About

Konstantin M. Boyko is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, Konstantin M. Boyko has authored 105 papers receiving a total of 988 indexed citations (citations by other indexed papers that have themselves been cited), including 75 papers in Molecular Biology, 51 papers in Materials Chemistry and 25 papers in Biochemistry. Recurrent topics in Konstantin M. Boyko's work include Enzyme Structure and Function (48 papers), Amino Acid Enzymes and Metabolism (24 papers) and Biochemical and Molecular Research (14 papers). Konstantin M. Boyko is often cited by papers focused on Enzyme Structure and Function (48 papers), Amino Acid Enzymes and Metabolism (24 papers) and Biochemical and Molecular Research (14 papers). Konstantin M. Boyko collaborates with scholars based in Russia, China and Germany. Konstantin M. Boyko's co-authors include Vladimir O. Popov, Ekaterina Yu. Bezsudnova, A.Y. Nikolaeva, Tatiana V. Rakitina, K. M. Polyakov, Т.В. Тихонова, R. A. Zvyagilskaya, А. Н. Антипов, В. И. Тимофеев and Artem Bonchuk and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and The Journal of Chemical Physics.

In The Last Decade

Konstantin M. Boyko

90 papers receiving 979 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 M. Boyko Russia 19 661 281 173 117 93 105 988
Andrea Hall United States 15 1.2k 1.7× 175 0.6× 211 1.2× 56 0.5× 121 1.3× 18 1.7k
R.D. Seidel United States 21 1.1k 1.6× 230 0.8× 92 0.5× 66 0.6× 137 1.5× 35 1.4k
T. Joseph Kappock United States 21 1.1k 1.7× 396 1.4× 100 0.6× 55 0.5× 99 1.1× 35 1.5k
Kazuaki Yoshimune Japan 16 718 1.1× 174 0.6× 152 0.9× 113 1.0× 24 0.3× 53 972
Régine Lebrun France 24 863 1.3× 164 0.6× 59 0.3× 131 1.1× 37 0.4× 58 1.4k
E. Joel Loveridge United Kingdom 23 837 1.3× 566 2.0× 60 0.3× 36 0.3× 119 1.3× 52 1.3k
Akiko Kita Japan 18 1.0k 1.5× 341 1.2× 101 0.6× 81 0.7× 85 0.9× 66 1.5k
T. Lundqvist Sweden 18 856 1.3× 275 1.0× 121 0.7× 44 0.4× 70 0.8× 24 1.2k
Martin St. Maurice United States 23 991 1.5× 508 1.8× 267 1.5× 32 0.3× 110 1.2× 49 1.5k
Stefano Ferri Japan 29 1.4k 2.1× 211 0.8× 232 1.3× 114 1.0× 97 1.0× 72 2.2k

Countries citing papers authored by Konstantin M. Boyko

Since Specialization
Citations

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

Fields of papers citing papers by Konstantin M. Boyko

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Konstantin M. Boyko

This figure shows the co-authorship network connecting the top 25 collaborators of Konstantin M. Boyko. A scholar is included among the top collaborators of Konstantin M. Boyko 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 M. Boyko. Konstantin M. Boyko 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.
Slonimskiy, Yury B., Maria A. Sinetova, Georgy V. Tsoraev, et al.. (2025). Structure and quenching of a bundle-shaped phycobilisome. Science Advances. 11(42). eadz6774–eadz6774.
2.
Minyaev, Mikhail E., et al.. (2024). Multifunctionality of arginine residues in the active sites of non-canonical d-amino acid transaminases. Archives of Biochemistry and Biophysics. 756. 110011–110011. 3 indexed citations
3.
Minyaev, Mikhail E., et al.. (2024). Incorporation of pyridoxal-5′-phosphate into the apoenzyme: A structural study of D-amino acid transaminase from Haliscomenobacter hydrossis. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1873(1). 141056–141056.
4.
Bolshakov, М. А., З. К. Махнева, Andrey V. Mardanov, et al.. (2024). Near-atomic cryo-EM structure of the light-harvesting complex LH2 from the sulfur purple bacterium Ectothiorhodospira haloalkaliphila. Structure. 33(2). 311–320.e3.
5.
Popov, Vladimir O., et al.. (2024). Structural basis of selective beta-carotene binding by a soluble protein. Structure. 32(11). 2123–2133.e3.
6.
7.
Boyko, Konstantin M., et al.. (2024). Single-point substitution F97M leads to in cellulo crystallization of the biphotochromic protein moxSAASoti. Biochemical and Biophysical Research Communications. 732. 150419–150419.
8.
Nikolaeva, A.Y., K. V. Anokhin, Kiryl D. Piatkevich, et al.. (2023). Blue-to-Red TagFT, mTagFT, mTsFT, and Green-to-FarRed mNeptusFT2 Proteins, Genetically Encoded True and Tandem Fluorescent Timers. International Journal of Molecular Sciences. 24(4). 3279–3279. 1 indexed citations
9.
Arapidi, Georgij, A.Y. Nikolaeva, Konstantin M. Boyko, et al.. (2023). Crystal Structure of Inhibitor-Bound Bacterial Oligopeptidase B in the Closed State: Similarity and Difference between Protozoan and Bacterial Enzymes. International Journal of Molecular Sciences. 24(3). 2286–2286. 2 indexed citations
10.
Subach, Oksana M., A.Y. Nikolaeva, Kiryl D. Piatkevich, et al.. (2023). FNCaMP, ratiometric green calcium indicator based on mNeonGreen protein. Biochemical and Biophysical Research Communications. 665. 169–177. 6 indexed citations
11.
Zueva, Irina V., Elmira A. Vasilieva, Gulnara A. Gaynanova, et al.. (2023). Can Activation of Acetylcholinesterase by β-Amyloid Peptide Decrease the Effectiveness of Cholinesterase Inhibitors?. International Journal of Molecular Sciences. 24(22). 16395–16395. 7 indexed citations
12.
13.
Sluchanko, Nikolai N., Yury B. Slonimskiy, Anastasia M. Moysenovich, et al.. (2022). Silkworm carotenoprotein as an efficient carotenoid extractor, solubilizer and transporter. International Journal of Biological Macromolecules. 223(Pt A). 1381–1393. 11 indexed citations
14.
Boyko, Konstantin M., A.Y. Nikolaeva, Tatiana V. Rakitina, et al.. (2022). A Puzzling Protein from Variovorax paradoxus Has a PLP Fold Type IV Transaminase Structure and Binds PLP without Catalytic Lysine. Crystals. 12(5). 619–619.
15.
Slonimskiy, Yury B., et al.. (2022). Preparation and Structural Studies of the Silkworm Carotenoid-Binding Protein Complexed with a New Pigment. Crystallography Reports. 67(6). 909–917. 2 indexed citations
16.
Boyko, Konstantin M., et al.. (2022). Three-Dimensional Structure of the S148F Mutant of Blue-to-Red Fluorescent Timer mRubyFT. Crystallography Reports. 67(6). 905–908. 1 indexed citations
17.
Subach, Oksana M., Павел В. Дороватовский, A.Y. Nikolaeva, et al.. (2021). LSSmScarlet, dCyRFP2s, dCyOFP2s and CRISPRed2s, Genetically Encoded Red Fluorescent Proteins with a Large Stokes Shift. International Journal of Molecular Sciences. 22(23). 12887–12887. 12 indexed citations
18.
Boyko, Konstantin M., L. E. Petrovskaya, A.Y. Nikolaeva, et al.. (2021). Structural and Biochemical Characterization of a Cold-Active PMGL3 Esterase with Unusual Oligomeric Structure. Biomolecules. 11(1). 57–57. 7 indexed citations
19.
Nikolaeva, A.Y., Tatiana V. Rakitina, Maria G. Khrenova, et al.. (2021). The Uncommon Active Site of D-Amino Acid Transaminase from Haliscomenobacter hydrossis: Biochemical and Structural Insights into the New Enzyme. Molecules. 26(16). 5053–5053. 18 indexed citations
20.
Сыкилинда, Н. Н., A.Y. Nikolaeva, Mikhail M. Shneider, et al.. (2018). Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal α-Helix with the Proposed Role in Activity against Live Bacterial Cells. Viruses. 10(6). 309–309. 31 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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