K. M. Polyakov

1.4k total citations
67 papers, 1.2k citations indexed

About

K. M. Polyakov is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, K. M. Polyakov has authored 67 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 47 papers in Molecular Biology, 36 papers in Materials Chemistry and 14 papers in Biochemistry. Recurrent topics in K. M. Polyakov's work include Enzyme Structure and Function (36 papers), Biochemical and Molecular Research (18 papers) and Protein Structure and Dynamics (15 papers). K. M. Polyakov is often cited by papers focused on Enzyme Structure and Function (36 papers), Biochemical and Molecular Research (18 papers) and Protein Structure and Dynamics (15 papers). K. M. Polyakov collaborates with scholars based in Russia, Germany and France. K. M. Polyakov's co-authors include Vladimir O. Popov, Т.В. Тихонова, Т. В. Федорова, Konstantin M. Boyko, А. Н. Попов, Victor S. Lamzin, A.G. Pavlovsky, О. В. Королева, Guy Dodson and Ruslan Sanishvili and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Trends in Biochemical Sciences.

In The Last Decade

K. M. Polyakov

66 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
K. M. Polyakov Russia	20	746	323	238	161	138	67	1.2k
Akiko Kita Japan	18	1.0k 1.4×	341 1.1×	277 1.2×	186 1.2×	98 0.7×	66	1.5k
Neela H. Yennawar United States	25	1.1k 1.5×	315 1.0×	315 1.3×	106 0.7×	119 0.9×	68	1.9k
Moshe Goldsmith Israel	22	1.4k 1.9×	232 0.7×	516 2.2×	160 1.0×	168 1.2×	35	2.2k
Carlos Frazão Portugal	25	1.2k 1.7×	318 1.0×	229 1.0×	202 1.3×	109 0.8×	68	1.9k
Sergio Martínez‐Rodríguez Spain	21	1.1k 1.5×	400 1.2×	314 1.3×	138 0.9×	101 0.7×	77	1.8k
Shuhei Zenno Japan	22	1.2k 1.6×	152 0.5×	155 0.7×	108 0.7×	186 1.3×	38	1.7k
Gustav Oberdorfer Austria	18	1.2k 1.7×	408 1.3×	108 0.5×	67 0.4×	51 0.4×	37	1.7k
E. Bitto United States	21	946 1.3×	192 0.6×	148 0.6×	47 0.3×	197 1.4×	38	1.4k
T. Lundqvist Sweden	18	856 1.1×	275 0.9×	101 0.4×	77 0.5×	63 0.5×	24	1.2k
T. Joseph Kappock United States	21	1.1k 1.5×	396 1.2×	64 0.3×	61 0.4×	101 0.7×	35	1.5k

Countries citing papers authored by K. M. Polyakov

Since Specialization

Citations

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

Fields of papers citing papers by K. M. Polyakov

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of K. M. Polyakov

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

All Works

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20 of 20 papers shown

Gavryushov, Sergei, Nikolay Kuzmich, & K. M. Polyakov. (2023). Quantum Mechanical Study of Oxygen Ligands Protonation for the Stable States of the Laccase Active Site. International Journal of Molecular Sciences. 24(3). 2990–2990. 3 indexed citations

Glazunova, Olga A., et al.. (2018). Structure-function study of two new middle-redox potential laccases from basidiomycetes Antrodiella faginea and Steccherinum murashkinskyi. International Journal of Biological Macromolecules. 118(Pt A). 406–418. 23 indexed citations

Polyakov, K. M., et al.. (2015). Structural study of the X-ray-induced enzymatic reaction of octahaem cytochromecnitrite reductase. Acta Crystallographica Section D Biological Crystallography. 71(5). 1087–1094. 8 indexed citations

Polyakov, K. M., Т.В. Тихонова, Roman Kittl, et al.. (2015). Incorporation of copper ions into crystals of T2 copper-depleted laccase fromBotrytis aclada. Acta Crystallographica Section F Structural Biology Communications. 71(12). 1465–1469. 17 indexed citations

Polyakov, K. M., Roman Kittl, Sergey Shleev, et al.. (2014). Effect of the L499M mutation of the ascomycetousBotrytis acladalaccase on redox potential and catalytic properties. Acta Crystallographica Section D Biological Crystallography. 70(11). 2913–2923. 31 indexed citations

Polyakov, K. M., Ekaterina Yu. Bezsudnova, Павел В. Дороватовский, et al.. (2013). Structures of β-glycosidase from Acidilobus saccharovorans in complexes with tris and glycerol. Doklady Biochemistry and Biophysics. 449(1). 99–101. 8 indexed citations

Тихонова, Т.В., K. M. Polyakov, Konstantin M. Boyko, et al.. (2012). Comparative structural and functional analysis of two octaheme nitrite reductases from closely related Thioalkalivibrio species. FEBS Journal. 279(21). 4052–4061. 25 indexed citations

Polyakov, K. M., et al.. (2012). Covalent modifications of catalytic tyrosine in octaheme cytochrome c nitrite reductase and their effect on the enzyme activity. Acta Crystallographica Section A Foundations of Crystallography. 68. 144–153. 1 indexed citations

Polyakov, K. M., et al.. (2012). Crystallization of uridine phosphorylase from Shewanella oneidensis MR-1 in the laboratory and under microgravity and preliminary X-ray diffraction analysis. Acta Crystallographica Section A Foundations of Crystallography. 68. 1387–1389. 3 indexed citations

10.

Федорова, Т. В., et al.. (2012). Purification, biochemical characterization, and structure of recombinant endo-1,4-β-xylanase XylE. Biochemistry (Moscow). 77(10). 1190–1198. 17 indexed citations

11.

Polyakov, K. M., et al.. (2012). Influence of intermolecular contacts on the structure of recombinant prolidase fromThermococcus sibiricus. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(11). 1275–1278. 6 indexed citations

12.

Polyakov, K. M., et al.. (2010). Structures of complexes of octahaem cytochromecnitrite reductase fromThioalkalivibrio nitratireducenswith sulfite and cyanide. Acta Crystallographica Section D Biological Crystallography. 66(10). 1043–1047. 9 indexed citations

13.

Polyakov, K. M., et al.. (2010). Structure of octaheme cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens in a complex with phosphate. Crystallography Reports. 55(1). 58–64. 6 indexed citations

14.

Polyakov, K. M., Т. В. Федорова, Elena V. Stepanova, et al.. (2009). Structure of native laccase fromTrametes hirsutaat 1.8 Å resolution. Acta Crystallographica Section D Biological Crystallography. 65(6). 611–617. 55 indexed citations

15.

Тихонова, Т.В., Konstantin M. Boyko, S. Yu. Kleimenov, et al.. (2008). Isolation and oligomeric composition of cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens. Biochemistry (Moscow). 73(2). 164–170. 5 indexed citations

16.

Тихонова, Т.В., А. Н. Антипов, Konstantin M. Boyko, et al.. (2006). Molecular and catalytic properties of a novel cytochrome c nitrite reductase from nitrate-reducing haloalkaliphilic sulfur-oxidizing bacterium Thioalkalivibrio nitratireducens. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1764(4). 715–723. 55 indexed citations

17.

Darii, Ekaterina, N.P. Fomenkova, Igor Pechik, et al.. (2005). Structure ofEscherichia coliglutamate decarboxylase (GADα) in complex with glutarate at 2.05 Å resolution. Acta Crystallographica Section D Biological Crystallography. 61(3). 230–235. 35 indexed citations

18.

Polyakov, K. M., Andrey A. Lebedev, Andrei L. Okorokov, et al.. (2002). The structure of substrate-free microbial ribonuclease binase and of its complexes with 3′GMP and sulfate ions. Acta Crystallographica Section D Biological Crystallography. 58(5). 744–750. 20 indexed citations

19.

Okorokov, Andrei L., Kostya I. Panov, M.Ya. Karpeisky, et al.. (1996). Site‐directed mutagenesis of the base recognition loop of ribonuclease from Bacillus intermedius (binase). FEBS Letters. 384(2). 143–146. 7 indexed citations

20.

Sanishvili, Ruslan, et al.. (1990). Comparison of active sites of some microbial ribonucleases: structural basis for guanylic specificity. Trends in Biochemical Sciences. 15(4). 158–162. 64 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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