Alexey Silakov

3.8k total citations
68 papers, 3.1k citations indexed

About

Alexey Silakov is a scholar working on Renewable Energy, Sustainability and the Environment, Inorganic Chemistry and Molecular Biology. According to data from OpenAlex, Alexey Silakov has authored 68 papers receiving a total of 3.1k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Renewable Energy, Sustainability and the Environment, 25 papers in Inorganic Chemistry and 23 papers in Molecular Biology. Recurrent topics in Alexey Silakov's work include Metalloenzymes and iron-sulfur proteins (37 papers), Metal-Catalyzed Oxygenation Mechanisms (24 papers) and Electrocatalysts for Energy Conversion (21 papers). Alexey Silakov is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (37 papers), Metal-Catalyzed Oxygenation Mechanisms (24 papers) and Electrocatalysts for Energy Conversion (21 papers). Alexey Silakov collaborates with scholars based in United States, Germany and Russia. Alexey Silakov's co-authors include Wolfgang Lubitz, E.J. Reijerse, Thomas Happe, Michael T. Green, Carsten Krebs, Edward J. Reijerse, Elizabeth L. Onderko, Timothy H. Yosca, J. Martin Bollinger and Courtney M. Krest and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Alexey Silakov

65 papers receiving 3.1k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Alexey Silakov United States	30	1.8k	1.2k	781	708	475	68	3.1k
Giuseppe Zampella Italy	35	2.1k 1.2×	1.1k 0.9×	539 0.7×	904 1.3×	555 1.2×	107	3.5k
Ricardo García‐Serres France	28	948 0.5×	1.1k 0.9×	743 1.0×	621 0.9×	105 0.2×	59	2.2k
Jeffrey J. Warren Canada	29	1.6k 0.9×	1.4k 1.2×	655 0.8×	1.1k 1.5×	557 1.2×	74	4.0k
Yutaka Hitomi Japan	29	634 0.3×	741 0.6×	509 0.7×	1.2k 1.7×	299 0.6×	99	2.4k
Yisong Guo United States	35	1.2k 0.7×	1.8k 1.5×	906 1.2×	849 1.2×	270 0.6×	129	3.4k
Codrina V. Popescu United States	22	854 0.5×	605 0.5×	368 0.5×	402 0.6×	128 0.3×	35	1.6k
Marie‐Hélène Charon France	11	1.3k 0.7×	459 0.4×	639 0.8×	424 0.6×	209 0.4×	19	2.0k
Bruno Guigliarelli France	32	719 0.4×	369 0.3×	1.2k 1.5×	618 0.9×	249 0.5×	88	2.7k
Bruno Guigliarelli France	34	2.2k 1.2×	645 0.5×	753 1.0×	603 0.9×	607 1.3×	62	3.0k
Esther M. Johnston United States	9	308 0.2×	975 0.8×	582 0.7×	520 0.7×	146 0.3×	9	2.0k

Countries citing papers authored by Alexey Silakov

Since Specialization

Citations

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

Fields of papers citing papers by Alexey Silakov

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Alexey Silakov. 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 Alexey Silakov. The network helps show where Alexey Silakov may publish in the future.

Co-authorship network of co-authors of Alexey Silakov

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

Onderko, Elizabeth L., et al.. (2025). Importance of the Ferryl Quintet State in Determining the Electronic Properties of P450 Compound I. Journal of the American Chemical Society. 147(11). 9147–9158. 1 indexed citations

Silakov, Alexey, et al.. (2025). Design and characterization of a tunable open TE011 resonator for Q-band pulse EPR experiments. Journal of Magnetic Resonance. 378. 107921–107921.

Martinie, Ryan J., Richiro Ushimaru, Christopher J. Pollock, et al.. (2024). Optimized Substrate Positioning Enables Switches in the C–H Cleavage Site and Reaction Outcome in the Hydroxylation–Epoxidation Sequence Catalyzed by Hyoscyamine 6β-Hydroxylase. Journal of the American Chemical Society. 146(35). 24271–24287. 8 indexed citations

Baker, Carol S., et al.. (2024). Light-induced H ₂ generation in a photosystem I-O ₂ -tolerant [FeFe] hydrogenase nanoconstruct. Proceedings of the National Academy of Sciences. 121(34). e2400267121–e2400267121. 6 indexed citations

Silakov, Alexey, et al.. (2023). Evidence for Porphyrin-Mediated Electron Transfer in the Radical SAM Enzyme HutW. Biochemistry. 62(6). 1191–1196. 5 indexed citations

Silakov, Alexey, et al.. (2021). Mechanism of Reduction of an Aminyl Radical Intermediate in the Radical SAM GTP 3′,8-Cyclase MoaA. Journal of the American Chemical Society. 143(34). 13835–13844. 12 indexed citations

Silakov, Alexey, et al.. (2020). Investigation of the Unusual Ability of the [FeFe] Hydrogenase from Clostridium beijerinckii to Access an O₂-Protected State. Journal of the American Chemical Society. 142(28). 12409–12419. 38 indexed citations

Martinie, Ryan J., Juan Pan, Squire J. Booker, et al.. (2019). Analysis of RNA Methylation by Phylogenetically Diverse Cfr Radical S -Adenosylmethionine Enzymes Reveals an Iron-Binding Accessory Domain in a Clostridial Enzyme. Biochemistry. 58(29). 3169–3184. 2 indexed citations

Esakova, Olga, Alexey Silakov, Tyler L. Grove, et al.. (2019). An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase. Journal of the American Chemical Society. 141(36). 14142–14151. 6 indexed citations

10.

Maggiolo, Ailiena O., Christopher J. Pollock, Elizabeth J. Blaesi, et al.. (2018). Structural Basis for Superoxide Activation of Flavobacterium johnsoniae Class I Ribonucleotide Reductase and for Radical Initiation by Its Dimanganese Cofactor. Biochemistry. 57(18). 2679–2693. 34 indexed citations

11.

Martinie, Ryan J., Elizabeth J. Blaesi, Carsten Krebs, et al.. (2017). Evidence for a Di-μ-oxo Diamond Core in the Mn(IV)/Fe(IV) Activation Intermediate of Ribonucleotide Reductase from Chlamydia trachomatis. Journal of the American Chemical Society. 139(5). 1950–1957. 29 indexed citations

12.

Mitchell, Andrew J., Noah P. Dunham, Ryan J. Martinie, et al.. (2017). Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase. Journal of the American Chemical Society. 139(39). 13830–13836. 107 indexed citations

13.

Martinie, Ryan J., Christopher J. Pollock, Megan L. Matthews, et al.. (2017). Vanadyl as a Stable Structural Mimic of Reactive Ferryl Intermediates in Mononuclear Nonheme-Iron Enzymes. Inorganic Chemistry. 56(21). 13382–13389. 23 indexed citations

14.

Silakov, Alexey, Tyler L. Grove, Matthew I. Radle, et al.. (2014). Characterization of a Cross-Linked Protein–Nucleic Acid Substrate Radical in the Reaction Catalyzed by RlmN. Journal of the American Chemical Society. 136(23). 8221–8228. 37 indexed citations

15.

Yosca, Timothy H., Jonathan Rittle, Courtney M. Krest, et al.. (2013). Iron(IV)hydroxide p K _a and the Role of Thiolate Ligation in C–H Bond Activation by Cytochrome P450. Science. 342(6160). 825–829. 269 indexed citations

16.

Wörsdörfer, Bigna, Kenichi Yokoyama, Jovan Livada, et al.. (2013). Function of the Diiron Cluster of Escherichia coli Class Ia Ribonucleotide Reductase in Proton-Coupled Electron Transfer. DSpace@MIT (Massachusetts Institute of Technology). 1 indexed citations

17.

Grove, Tyler L., Jovan Livada, Erica L. Schwalm, et al.. (2013). A substrate radical intermediate in catalysis by the antibiotic resistance protein Cfr. Nature Chemical Biology. 9(7). 422–427. 39 indexed citations

18.

Erdem, Özlen F., Lennart Schwartz, Matthias Stein, et al.. (2011). A Model of the [FeFe] Hydrogenase Active Site with a Biologically Relevant Azadithiolate Bridge: A Spectroscopic and Theoretical Investigation. Angewandte Chemie International Edition. 50(6). 1439–1443. 120 indexed citations

19.

Silakov, Alexey, et al.. (2009). The [FeFe]‐hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN⁻ ligated iron cofactor. FEBS Letters. 584(3). 638–642. 81 indexed citations

20.

Silakov, Alexey, et al.. (2008). Isolation and first EPR characterization of the [FeFe]-hydrogenases from green algae. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1777(5). 410–416. 100 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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