Alexander A. Ishchenko

2.9k total citations
96 papers, 2.4k citations indexed

About

Alexander A. Ishchenko is a scholar working on Molecular Biology, Oncology and Genetics. According to data from OpenAlex, Alexander A. Ishchenko has authored 96 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 90 papers in Molecular Biology, 14 papers in Oncology and 10 papers in Genetics. Recurrent topics in Alexander A. Ishchenko's work include DNA Repair Mechanisms (76 papers), DNA and Nucleic Acid Chemistry (39 papers) and Advanced biosensing and bioanalysis techniques (16 papers). Alexander A. Ishchenko is often cited by papers focused on DNA Repair Mechanisms (76 papers), DNA and Nucleic Acid Chemistry (39 papers) and Advanced biosensing and bioanalysis techniques (16 papers). Alexander A. Ishchenko collaborates with scholars based in France, Russia and Kazakhstan. Alexander A. Ishchenko's co-authors include Murat Saparbaev, Olga S. Fedorova, Dmitry O. Zharkov, Georgy A. Nevinsky, Bakhyt Matkarimov, Nikita A. Kuznetsov, Olga I. Lavrik, Inga R. Grin, Didier Gasparutto and Laurent Gros and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Alexander A. Ishchenko

92 papers receiving 2.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Alexander A. Ishchenko France 30 2.0k 503 264 215 157 96 2.4k
Murat Saparbaev France 34 3.3k 1.6× 513 1.0× 600 2.3× 399 1.9× 116 0.7× 118 3.8k
Carlo M. Nalin United States 23 2.3k 1.1× 531 1.1× 160 0.6× 148 0.7× 229 1.5× 29 2.8k
J. Symerský United States 18 1.3k 0.6× 252 0.5× 384 1.5× 176 0.8× 80 0.5× 47 2.0k
Jean‐Baptiste Charbonnier France 29 2.2k 1.1× 322 0.6× 122 0.5× 196 0.9× 258 1.6× 74 2.7k
Susan E. Tsutakawa United States 34 2.6k 1.3× 313 0.6× 186 0.7× 327 1.5× 56 0.4× 66 2.8k
Alexey Bochkarev Canada 28 2.2k 1.1× 751 1.5× 147 0.6× 521 2.4× 179 1.1× 42 3.1k
Scott Classen United States 16 1.6k 0.8× 364 0.7× 131 0.5× 148 0.7× 72 0.5× 20 2.0k
Peggy Hsieh United States 28 3.0k 1.5× 459 0.9× 529 2.0× 482 2.2× 55 0.4× 34 3.5k
M. Hammarstrom Sweden 22 1.3k 0.6× 269 0.5× 70 0.3× 173 0.8× 317 2.0× 29 1.7k

Countries citing papers authored by Alexander A. Ishchenko

Since Specialization
Citations

This map shows the geographic impact of Alexander A. Ishchenko'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. Ishchenko 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. Ishchenko more than expected).

Fields of papers citing papers by Alexander A. Ishchenko

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

This figure shows the co-authorship network connecting the top 25 collaborators of Alexander A. Ishchenko. A scholar is included among the top collaborators of Alexander A. Ishchenko 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. Ishchenko. Alexander A. Ishchenko 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.
Zhao, Mingxing, et al.. (2025). Role of Individual Amino Acid Residues Directly Involved in Damage Recognition in Active Demethylation by ABH2 Dioxygenase. International Journal of Molecular Sciences. 26(14). 6912–6912.
2.
Ishchenko, Alexander A., et al.. (2024). Enhanced thermal stability enables human mismatch-specific thymine–DNA glycosylase to catalyse futile DNA repair. PLoS ONE. 19(10). e0304818–e0304818.
3.
Baranova, Svetlana V., et al.. (2023). Abasic site–peptide cross-links are blocking lesions repaired by AP endonucleases. Nucleic Acids Research. 51(12). 6321–6336. 8 indexed citations
5.
Кузнецова, А. А., et al.. (2023). The Impact of Human DNA Glycosylases on the Activity of DNA Polymerase β toward Various Base Excision Repair Intermediates. International Journal of Molecular Sciences. 24(11). 9594–9594. 8 indexed citations
6.
Кузнецова, А. А., et al.. (2023). Coordination between human DNA polymerase β and apurinic/apyrimidinic endonuclease 1 in the course of DNA repair. Biochimie. 216. 126–136. 3 indexed citations
7.
Кузнецова, А. А., et al.. (2022). The Kinetic Mechanism of 3′-5′ Exonucleolytic Activity of AP Endonuclease Nfo from E. coli. Cells. 11(19). 2998–2998. 3 indexed citations
8.
Кузнецова, А. А., et al.. (2022). Kinetic Features of 3′–5′–Exonuclease Activity of Apurinic/Apyrimidinic Endonuclease Apn2 from Saccharomyces cerevisiae. International Journal of Molecular Sciences. 23(22). 14404–14404. 2 indexed citations
9.
Ishchenko, Alexander A., et al.. (2022). Conformational Dynamics of Human ALKBH2 Dioxygenase in the Course of DNA Repair as Revealed by Stopped-Flow Fluorescence Spectroscopy. Molecules. 27(15). 4960–4960. 2 indexed citations
10.
Кузнецова, А. А., Д. С. Новопашина, Alexander A. Ishchenko, et al.. (2022). Comparative Analysis of Exo- and Endonuclease Activities of APE1-like Enzymes. International Journal of Molecular Sciences. 23(5). 2869–2869. 4 indexed citations
11.
Кузнецова, А. А., et al.. (2021). Common Kinetic Mechanism of Abasic Site Recognition by Structurally Different Apurinic/Apyrimidinic Endonucleases. International Journal of Molecular Sciences. 22(16). 8874–8874. 6 indexed citations
13.
Belousova, E. A., Alexander A. Ishchenko, & Olga I. Lavrik. (2018). Dna is a New Target of Parp3. Scientific Reports. 8(1). 4176–4176. 57 indexed citations
14.
Кузнецова, А. А., et al.. (2017). Pre-steady-state kinetic analysis of damage recognition by human single-strand selective monofunctional uracil-DNA glycosylase SMUG1. Molecular BioSystems. 13(12). 2638–2649. 26 indexed citations
15.
Кузнецова, А. А., Nikita A. Kuznetsov, Alexander A. Ishchenko, Murat Saparbaev, & Olga S. Fedorova. (2014). Pre-steady-state fluorescence analysis of damaged DNA transfer from human DNA glycosylases to AP endonuclease APE1. Biochimica et Biophysica Acta (BBA) - General Subjects. 1840(10). 3042–3051. 28 indexed citations
16.
Talhaoui, Ibtissam, Sophie Couvé, Alexander A. Ishchenko, et al.. (2012). 7,8-dihydro-8-oxoadenine, a highly mutagenic adduct, is repaired by Escherichia coli and human mismatch-specific uracil/thymine-DNA glycosylases. Nucleic Acids Research. 41(2). 912–923. 25 indexed citations
17.
Koval, Vladimir V., D.G. Knorre, Dmitry O. Zharkov, et al.. (2009). Conformational Dynamics of Human AP Endonuclease in Base Excision and Nucleotide Incision Repair Pathways. Journal of Biomolecular Structure and Dynamics. 26(5). 637–652. 43 indexed citations
18.
Ishchenko, Alexander A., Eric Deprez, Andrei Maksimenko, et al.. (2006). Uncoupling of the base excision and nucleotide incision repair pathways reveals their respective biological roles. Proceedings of the National Academy of Sciences. 103(8). 2564–2569. 71 indexed citations
19.
Ishchenko, Alexander A., et al.. (2006). High Resolution Characterization of Formamidopyrimidine-DNA Glycosylase Interaction with Its Substrate by Chemical Cross-linking and Mass Spectrometry Using Substrate Analogs. Journal of Biological Chemistry. 281(43). 32353–32365. 7 indexed citations
20.
Ishchenko, Alexander A., Vladimir V. Koval, Olga S. Fedorova, Kenneth T. Douglas, & Georgy A. Nevinsky. (1999). Structural Requirements of Double and Single Stranded DNA Substrates and Inhibitors, Including a Photoaffinity Label, of Fpg Protein From Escherichia Coli. Journal of Biomolecular Structure and Dynamics. 17(2). 301–310. 16 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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