A.M. Mikhailov

780 total citations
51 papers, 648 citations indexed

About

A.M. Mikhailov is a scholar working on Molecular Biology, Materials Chemistry and Plant Science. According to data from OpenAlex, A.M. Mikhailov has authored 51 papers receiving a total of 648 indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 23 papers in Materials Chemistry and 13 papers in Plant Science. Recurrent topics in A.M. Mikhailov's work include Enzyme Structure and Function (23 papers), Biochemical and Molecular Research (20 papers) and Enzyme-mediated dye degradation (8 papers). A.M. Mikhailov is often cited by papers focused on Enzyme Structure and Function (23 papers), Biochemical and Molecular Research (20 papers) and Enzyme-mediated dye degradation (8 papers). A.M. Mikhailov collaborates with scholars based in Russia, Germany and United Kingdom. A.M. Mikhailov's co-authors include Christian Betzel, Wolfgang Voelter, Ekaterina Morgunova, Azat Gabdulkhakov, В. Н. Зайцев, А. С. Миронов, Ch. Betzel, В. В. Лунин, B. K. Vaǐnshteǐn and Michael B. Sherman and has published in prestigious journals such as Journal of Virology, Biochemical and Biophysical Research Communications and FEBS Letters.

In The Last Decade

A.M. Mikhailov

46 papers receiving 633 citations

Peers

A.M. Mikhailov
Susan K. Boehlein United States
G. Cohen Israel
Qingjia Yao United States
J. Todd Hoopes United States
Ruud Luiten Netherlands
A.M. Mikhailov
Citations per year, relative to A.M. Mikhailov A.M. Mikhailov (= 1×) peers Jarmila Dušková

Countries citing papers authored by A.M. Mikhailov

Since Specialization
Citations

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

Fields of papers citing papers by A.M. Mikhailov

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of A.M. Mikhailov

This figure shows the co-authorship network connecting the top 25 collaborators of A.M. Mikhailov. A scholar is included among the top collaborators of A.M. Mikhailov 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 A.M. Mikhailov. A.M. Mikhailov 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.
Mikhailov, A.M., et al.. (2024). Comparison of Multi-resonant Patch Antenna Topologies. 1–7.
2.
Mikhailov, A.M., et al.. (2024). Comparison of Circular Polarized Patch Antenna Topologies. 1–8.
3.
Mikhailov, A.M., et al.. (2024). Optimization of an Extended Antenna Field. 1–5.
4.
Gabdulkhakov, Azat, et al.. (2018). Structural and Functional Analysis of Pyrimidine Nucleoside Phosphorylases of the NP-I and NP-II Families in Complexes with 6-Methyluracil. Crystallography Reports. 63(3). 418–427. 2 indexed citations
7.
Gabdulkhakov, Azat, et al.. (2012). Expression, purification, crystallization and preliminary X-ray structure analysis ofVibrio choleraeuridine phosphorylase in complex with thymidine. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(11). 1394–1397. 7 indexed citations
8.
Gabdulkhakov, Azat, et al.. (2011). Purification, crystallization and preliminary X-ray structure analysis of the laccase fromGanoderma lucidum. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(8). 926–929. 8 indexed citations
9.
Shtil, Аlexander А., et al.. (2009). The X-ray structure ofSalmonella typhimuriumuridine nucleoside phosphorylase complexed with 2,2′-anhydrouridine, phosphate and potassium ions at 1.86 Å resolution. Acta Crystallographica Section D Biological Crystallography. 66(1). 51–60. 19 indexed citations
10.
Bento, Isabel, Ekaterina Morgunova, Wolfgang Voelter, et al.. (2006). X-ray structural studies of the fungal laccase from Cerrena maxima. JBIC Journal of Biological Inorganic Chemistry. 11(8). 963–973. 45 indexed citations
11.
Bento, Isabel, Elena V. Stepanova, Г.С. Качалова, et al.. (2006). Purification, crystallization and preliminary X-ray study of the fungal laccase fromCerrena maxima. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62(10). 954–957. 25 indexed citations
12.
Wacker, Roland, Raghuvir K. Arni, T.P. Singh, et al.. (2004). Mistletoe lectin I in complex with galactose and lactose reveals distinct sugar-binding properties. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(1). 17–25. 23 indexed citations
13.
Rypniewski, W., et al.. (2002). Crystallisation under microgravity of mistletoe lectin I from Viscum album with adenine monophosphate and the crystal structure at 1.9 Å resolution. Acta Crystallographica Section D Biological Crystallography. 58(10). 1704–1707. 24 indexed citations
14.
Лунин, В. В., et al.. (2000). Magnesium-dependent Serratia marcescens endonuclease: three-dimensional structure at 1.1 Å resolution and molecular mechanism of enzyme action. Acta Crystallographica Section A Foundations of Crystallography. 56(s1). s280–s280. 4 indexed citations
15.
Лунин, В. В., K. M. Polyakov, Vladimir Y. Lunin, et al.. (2000). Atomic structure of theSerratia marcescensendonuclease at 1.1 Å resolution and the enzyme reaction mechanism. Acta Crystallographica Section D Biological Crystallography. 56(5). 567–572. 36 indexed citations
16.
Mikhailov, A.M., et al.. (1999). Crystallization and X-ray study of the artificial TBI protein, an experimental multiple-epitope vaccine against type 1 human immunodeficiency virus. Crystallography Reports. 44(5). 868–870. 1 indexed citations
17.
Fedorov, Roman, N. Nevskaya, Svetlana Tishchenko, et al.. (1999). Structure of ribosomal protein L30 from Thermus thermophilus at 1.9 Å resolution: conformational flexibility of the molecule. Acta Crystallographica Section D Biological Crystallography. 55(11). 1827–1833. 5 indexed citations
18.
Lunin, Vladimir Y., V.M. Levdikov, E.V. Blagova, et al.. (1997). Three‐dimensional structure of Serratiamarcescens nuclease at 1.7 Å resolution and mechanism of its action. FEBS Letters. 412(1). 217–222. 27 indexed citations
19.
Morgunova, Ekaterina, A.M. Mikhailov, А. Н. Попов, et al.. (1995). Atomic structure at 2.5 Å resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal lattice. FEBS Letters. 367(2). 183–187. 45 indexed citations
20.
Mikhailov, A.M., et al.. (1990). Crystallization and preliminary x‐ray diffraction study of neurotoxin‐I from Naja naja oxiana VENOM. FEBS Letters. 269(1). 255–257. 3 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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