Alexander A. Baykov

5.2k total citations · 1 hit paper
152 papers, 4.2k citations indexed

About

Alexander A. Baykov is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, Alexander A. Baykov has authored 152 papers receiving a total of 4.2k indexed citations (citations by other indexed papers that have themselves been cited), including 126 papers in Molecular Biology, 28 papers in Materials Chemistry and 26 papers in Oncology. Recurrent topics in Alexander A. Baykov's work include ATP Synthase and ATPases Research (99 papers), Biochemical and Molecular Research (31 papers) and Protein Structure and Dynamics (28 papers). Alexander A. Baykov is often cited by papers focused on ATP Synthase and ATPases Research (99 papers), Biochemical and Molecular Research (31 papers) and Protein Structure and Dynamics (28 papers). Alexander A. Baykov collaborates with scholars based in Russia, Finland and United States. Alexander A. Baykov's co-authors include Reijo Lahti, С.М. Аваева, Barry S. Cooperman, Adrian Goldman, Anssi M. Malinen, Anu Salminen, Heidi Tuominen, Natalia P. Bakuleva, Vladimir N. Kasho and А. С. Шестаков and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Alexander A. Baykov

146 papers receiving 4.1k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

A malachite green procedure for orthophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay

1988 688 citations Alexander A. Baykov et al. Analytical Biochemistry profile →

Peers

Alexander A. Baykov

ONCOL

Reijo Lahti Finland

Sun‐Shin Cha South Korea

K.L. Kavanagh United Kingdom

Vilmos Fülöp United Kingdom

Heidi Schubert United States

Parimal Karmakar India

Yasuo Hata Japan

Weimin Gong China

S. Turley United States

Eduardo Méndez Spain

Reijo Lahti Finland

Alexander A. Baykov

3.0k ×0.9

913 ×1.0

551 ×0.9

ONCOL

623 ×2.2

227 ×1.2

Citations per year, relative to Alexander A. Baykov Alexander A. Baykov (= 1×) peers Reijo Lahti

Countries citing papers authored by Alexander A. Baykov

Since Specialization

Citations

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

Fields of papers citing papers by Alexander A. Baykov

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Alexander A. Baykov

This figure shows the co-authorship network connecting the top 25 collaborators of Alexander A. Baykov. A scholar is included among the top collaborators of Alexander A. Baykov 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 Alexander A. Baykov. Alexander A. Baykov 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

Bertsova, Yulia V., et al.. (2024). Acrylate reductase of an anaerobic electron transport chain of the marine bacterium shewanella woodyi. 89(4). 666–676. 1 indexed citations

Moiseenko, Andrey, et al.. (2023). The Structure and Nucleotide-Binding Characteristics of Regulated Cystathionine β-Synthase Domain-Containing Pyrophosphatase without One Catalytic Domain. International Journal of Molecular Sciences. 24(24). 17160–17160. 1 indexed citations

Salminen, Anu, et al.. (2020). The tetrameric structure of nucleotide-regulated pyrophosphatase and its modulation by deletion mutagenesis and ligand binding. Archives of Biochemistry and Biophysics. 692. 108537–108537. 4 indexed citations

Baykov, Alexander A., et al.. (2019). DYNAMICS OF INTERNATIONAL ALLIANCES IN AN UNBALANCED WORLD STRUCTURE. World Economy and International Relations. 63(1). 34–48. 10 indexed citations

Serebryakova, Marina V., Yulia V. Bertsova, С. С. Соколов, et al.. (2018). Catalytically important flavin linked through a phosphoester bond in a eukaryotic fumarate reductase. Biochimie. 149. 34–40. 11 indexed citations

Salminen, Anu, et al.. (2015). Cystathionine β-Synthase (CBS) Domain-containing Pyrophosphatase as a Target for Diadenosine Polyphosphates in Bacteria. Journal of Biological Chemistry. 290(46). 27594–27603. 17 indexed citations

Baykov, Alexander A., et al.. (2013). Membrane-integral pyrophosphatase subfamily capable of translocating both Na ⁺ and H ⁺. Proceedings of the National Academy of Sciences. 110(4). 1255–1260. 50 indexed citations

Bertsova, Yulia V., et al.. (2013). Localization-controlled specificity of FAD:threonine flavin transferases in Klebsiella pneumoniae and its implications for the mechanism of Na+-translocating NADH:quinone oxidoreductase. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1837(7). 1122–1129. 19 indexed citations

Baykov, Alexander A., et al.. (2012). Fast kinetics of nucleotide binding to Clostridium perfringens family II pyrophosphatase containing CBS and DRTGG domains. Biochemistry (Moscow). 77(2). 165–170. 2 indexed citations

10.

Baykov, Alexander A., et al.. (2012). The evolutionary history of membrane-integral pyrophosphatases supports Na+ as the ancestral coupling ion in membrane bioenergetics. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817. S35–S36. 1 indexed citations

11.

Belogurov, Georgiy A., et al.. (2011). Na+-translocating Membrane Pyrophosphatases Are Widespread in the Microbial World and Evolutionarily Precede H+-translocating Pyrophosphatases. Journal of Biological Chemistry. 286(24). 21633–21642. 48 indexed citations

12.

Uchiumi, Toshio, et al.. (2001). Directed mutagenesis studies of the C‐terminal fingerprint region of Bacillus subtilis pyrophosphatase. European Journal of Biochemistry. 268(22). 5771–5775. 3 indexed citations

13.

Merckel, M.C., Anu Salminen, Nisse Kalkkinen, et al.. (2001). Crystal Structure of Streptococcus mutans Pyrophosphatase. Structure. 9(4). 289–297. 62 indexed citations

14.

Baykov, Alexander A., Teppo Hyytiä, Maria V. Turkina, et al.. (1999). Functional characterization of Escherichia coli inorganic pyrophosphatase in zwitterionic buffers. European Journal of Biochemistry. 260(2). 308–317. 9 indexed citations

15.

Baykov, Alexander A., et al.. (1996). Kinetic Characterization of the Hydrolytic Activity of the H⁺‐Pyrophosphatase of Rhodospirillum rubrum in Membrane‐Bound and Isolated States. European Journal of Biochemistry. 236(1). 121–127. 15 indexed citations

16.

Heikinheimo, Pirkko, et al.. (1996). A Site‐Directed Mutagenesis Study of Saccharomyces cerevisiae Pyrophosphatase. European Journal of Biochemistry. 239(1). 138–143. 49 indexed citations

17.

Baykov, Alexander A., Natalia P. Bakuleva, & Philip A. Rea. (1993). Steady‐state kinetics of substrate hydrolysis by vacuolar H⁺‐pyrophosphatase. European Journal of Biochemistry. 217(2). 755–762. 66 indexed citations

18.

Baykov, Alexander A., et al.. (1993). Differential sensitivity of membrane‐associated pyrophosphatases to inhibition by diphosphonates and fluoride delineates two classes of enzyme. FEBS Letters. 327(2). 199–202. 41 indexed citations

19.

Baykov, Alexander A., et al.. (1990). Tightly bound pyrophosphate inEscherichia coliinorganic pyrophosphatase. FEBS Letters. 262(2). 194–196. 6 indexed citations

20.

Vener, Alexander V., et al.. (1990). Use of biotinylated inorganic pyrophosphatase for detection of biotin bound to solid support. Analytical Biochemistry. 191(1). 65–69. 7 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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