Dmitrii I. Levitsky

2.4k total citations
99 papers, 2.0k citations indexed

About

Dmitrii I. Levitsky is a scholar working on Cardiology and Cardiovascular Medicine, Molecular Biology and Cell Biology. According to data from OpenAlex, Dmitrii I. Levitsky has authored 99 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 78 papers in Cardiology and Cardiovascular Medicine, 68 papers in Molecular Biology and 26 papers in Cell Biology. Recurrent topics in Dmitrii I. Levitsky's work include Cardiomyopathy and Myosin Studies (78 papers), Muscle Physiology and Disorders (46 papers) and Cardiovascular Effects of Exercise (35 papers). Dmitrii I. Levitsky is often cited by papers focused on Cardiomyopathy and Myosin Studies (78 papers), Muscle Physiology and Disorders (46 papers) and Cardiovascular Effects of Exercise (35 papers). Dmitrii I. Levitsky collaborates with scholars based in Russia, United Kingdom and Tajikistan. Dmitrii I. Levitsky's co-authors include Olga Nikolaeva, Alexander M. Matyushenko, Nikolai B. Gusev, Natalia A. Chebotareva, Galina V. Kopylova, Daniil V. Shchepkin, Sergey Y. Bershitsky, Nikolai N. Sluchanko, K Schwartz and J.-J. Mercadier and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Journal of Molecular Biology.

In The Last Decade

Dmitrii I. Levitsky

99 papers receiving 2.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Dmitrii I. Levitsky Russia 26 1.5k 1.1k 404 188 146 99 2.0k
Wolfgang M.J. Obermann Germany 19 1.8k 1.2× 562 0.5× 347 0.9× 69 0.4× 232 1.6× 27 2.1k
Etienne Audemard France 23 1.0k 0.7× 1.1k 1.0× 614 1.5× 157 0.8× 45 0.3× 35 1.6k
Morris Burke United States 19 700 0.5× 549 0.5× 259 0.6× 71 0.4× 47 0.3× 33 1.1k
Montserrat Samsó United States 24 1.5k 1.0× 649 0.6× 338 0.8× 86 0.5× 100 0.7× 56 1.8k
Olga Nikolaeva Russia 18 609 0.4× 362 0.3× 200 0.5× 99 0.5× 41 0.3× 40 881
Deborah B. Stone United States 19 607 0.4× 596 0.5× 179 0.4× 124 0.7× 49 0.3× 36 1.0k
FUMIKO EBASHI Japan 13 762 0.5× 749 0.7× 420 1.0× 106 0.6× 17 0.1× 15 1.5k
Kathleen Ue United States 12 455 0.3× 439 0.4× 335 0.8× 102 0.5× 43 0.3× 17 769
Katsuhiko Sakurada Japan 13 525 0.4× 421 0.4× 318 0.8× 226 1.2× 18 0.1× 18 1.0k
Kohji Ito Japan 21 874 0.6× 286 0.2× 343 0.8× 61 0.3× 27 0.2× 67 1.6k

Countries citing papers authored by Dmitrii I. Levitsky

Since Specialization
Citations

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

Fields of papers citing papers by Dmitrii I. Levitsky

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Dmitrii I. Levitsky. 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 Dmitrii I. Levitsky. The network helps show where Dmitrii I. Levitsky may publish in the future.

Co-authorship network of co-authors of Dmitrii I. Levitsky

This figure shows the co-authorship network connecting the top 25 collaborators of Dmitrii I. Levitsky. A scholar is included among the top collaborators of Dmitrii I. Levitsky 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 Dmitrii I. Levitsky. Dmitrii I. Levitsky 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.
Matyushenko, Alexander M., Galina V. Kopylova, Natalia A. Koubassova, et al.. (2023). Novel Mutation Glu98Lys in Cardiac Tropomyosin Alters Its Structure and Impairs Myocardial Relaxation. International Journal of Molecular Sciences. 24(15). 12359–12359. 3 indexed citations
2.
Kleymenov, Sergey Y., et al.. (2023). Effect of neurodegenerative mutations in NEFL gene on thermal denaturation of the neurofilament light chain protein. 88(5). 748–760. 1 indexed citations
3.
Kleymenov, Sergey Y., et al.. (2023). Structural and Functional Properties of Tropomyosin Isoforms Tpm4.1 and Tpm2.1. Biochemistry (Moscow). 88(6). 801–809. 1 indexed citations
4.
Kopylova, Galina V., Daniil V. Shchepkin, Vera A. Borzova, et al.. (2022). Impact of Troponin in Cardiomyopathy Development Caused by Mutations in Tropomyosin. International Journal of Molecular Sciences. 23(24). 15723–15723. 4 indexed citations
5.
Kopylova, Galina V., Daniil V. Shchepkin, Sergey Y. Bershitsky, et al.. (2020). Impact of A134 and E218 Amino Acid Residues of Tropomyosin on Its Flexibility and Function. International Journal of Molecular Sciences. 21(22). 8720–8720. 3 indexed citations
6.
Kleymenov, Sergey Y., et al.. (2019). Thermal unfolding of various human non-muscle isoforms of tropomyosin. Biochemical and Biophysical Research Communications. 514(3). 613–617. 7 indexed citations
7.
Matyushenko, Alexander M., et al.. (2017). Transient interaction between the N-terminal extension of the essential light chain-1 and motor domain of the myosin head during the ATPase cycle. Biochemical and Biophysical Research Communications. 495(1). 163–167. 6 indexed citations
8.
Nikolaeva, Olga, et al.. (2015). Does Interaction between the Motor and Regulatory Domains of the Myosin Head Occur during ATPase Cycle? Evidence from Thermal Unfolding Studies on Myosin Subfragment D.S. Logvinova, D.I. Markov, O.P. Nikolaeva, N.N. Sluchanko, D.S. Ushakov, D.I. Levitsky. PLoS ONE. 10(9). 4 indexed citations
9.
Kopylova, Galina V., Daniil V. Shchepkin, Alexander M. Matyushenko, et al.. (2015). Stabilizing the Central Part of Tropomyosin Increases the Bending Stiffness of the Thin Filament. Biophysical Journal. 109(2). 373–379. 16 indexed citations
10.
Redwood, Charles, et al.. (2008). Effect of mutation Arg91Gly on the thermal stability of β-tropomyosin. BIOPHYSICS. 53(6). 479–481. 1 indexed citations
11.
Timofeev, Vladimir P., et al.. (2007). Nucleotide-induced and actin-induced structural changes in SH1-SH2-modified myosin subfragment 1. Journal of Muscle Research and Cell Motility. 28(1). 67–78. 5 indexed citations
12.
Levitsky, Dmitrii I.. (2004). Actomyosin systems of biological motility. Biochemistry (Moscow). 69(11). 1177–1189. 14 indexed citations
13.
Bobkov, Andrey A., et al.. (1999). Effects of SH1 and SH2 Modifications on Myosin Similarities and Differences. Biophysical Journal. 76(2). 1001–1007. 27 indexed citations
14.
Rostkova, Elena, et al.. (1999). Use of stable analogs of myosin ATPase intermediates for kinetic studies of the "weak" binding of myosin heads to F-actin.. PubMed. 64(8). 875–82. 2 indexed citations
15.
Levitsky, Dmitrii I., et al.. (1998). Differential scanning calorimetric study of the thermal unfolding of the motor domain fragments of Dictyostelium discoideum myosin II. European Journal of Biochemistry. 251(1-2). 275–280. 17 indexed citations
16.
Орлов, В. Н., et al.. (1998). Thermally induced chain exchange of smooth muscle tropomyosin dimers studied by differential scanning calorimetry. FEBS Letters. 433(3). 241–244. 9 indexed citations
17.
Nikolaeva, Olga, et al.. (1996). Interaction of myosin subfragment 1 with F‐actin studied by differential scanning calorimetry. IUBMB Life. 40(4). 653–661. 15 indexed citations
18.
Timofeev, Vladimir P., et al.. (1995). The difference between ADP‐beryllium fluoride and ADP‐aluminium fluoride complexes of the spin‐labeled myosin subfragment 1. FEBS Letters. 371(3). 261–263. 25 indexed citations
19.
Bobkov, Andrey A., et al.. (1995). Structural Basis for Actomyosin Chemomechanical Transduction by Non-Nucleoside Triphosphate Analogs. Biochemistry. 34(38). 12178–12184. 4 indexed citations
20.
Shnyrov, Valery L., et al.. (1992). Thermal denaturation of the alkali light chain‐20 kDa fragment complex obtained from myosin subfragment 1. FEBS Letters. 303(2-3). 255–257. 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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