Dmitri Tolkatchev

603 total citations
27 papers, 479 citations indexed

About

Dmitri Tolkatchev is a scholar working on Molecular Biology, Cardiology and Cardiovascular Medicine and Cell Biology. According to data from OpenAlex, Dmitri Tolkatchev has authored 27 papers receiving a total of 479 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 10 papers in Cardiology and Cardiovascular Medicine and 7 papers in Cell Biology. Recurrent topics in Dmitri Tolkatchev's work include Cardiomyopathy and Myosin Studies (10 papers), Cardiovascular Effects of Exercise (6 papers) and Muscle Physiology and Disorders (5 papers). Dmitri Tolkatchev is often cited by papers focused on Cardiomyopathy and Myosin Studies (10 papers), Cardiovascular Effects of Exercise (6 papers) and Muscle Physiology and Disorders (5 papers). Dmitri Tolkatchev collaborates with scholars based in United States, Canada and Italy. Dmitri Tolkatchev's co-authors include Feng Ni, Ping Xu, Alla S. Kostyukova, Suneil Malik, H.P.J. Bennett, Ping Wang, Zhigang Chen, Andrew Bateman, Wim Vranken and Carol C. Gregorio and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Dmitri Tolkatchev

26 papers receiving 468 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Dmitri Tolkatchev United States 14 292 100 97 62 60 27 479
Zeynep A. Oztug Durer United States 11 162 0.6× 94 0.9× 77 0.8× 61 1.0× 135 2.3× 14 458
Sylvia Varland Norway 9 610 2.1× 15 0.1× 52 0.5× 46 0.7× 106 1.8× 12 830
K Titani Japan 12 361 1.2× 20 0.2× 21 0.2× 33 0.5× 100 1.7× 15 587
Kevin R. Parker United States 10 833 2.9× 61 0.6× 39 0.4× 16 0.3× 120 2.0× 10 1.1k
Stefan Schüchner Austria 12 506 1.7× 34 0.3× 13 0.1× 35 0.6× 175 2.9× 15 793
Greg Slodkowicz United Kingdom 8 553 1.9× 18 0.2× 24 0.2× 25 0.4× 37 0.6× 10 740
Danielle G. May United States 9 362 1.2× 24 0.2× 15 0.2× 22 0.4× 272 4.5× 15 553
W. Mathias Howell Sweden 10 593 2.0× 14 0.1× 20 0.2× 55 0.9× 63 1.1× 16 782
Yin Yao Dong United Kingdom 9 487 1.7× 11 0.1× 69 0.7× 138 2.2× 97 1.6× 19 796
Lenka Řežábková Czechia 17 606 2.1× 10 0.1× 43 0.4× 60 1.0× 237 4.0× 20 727

Countries citing papers authored by Dmitri Tolkatchev

Since Specialization
Citations

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

Fields of papers citing papers by Dmitri Tolkatchev

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Dmitri Tolkatchev

This figure shows the co-authorship network connecting the top 25 collaborators of Dmitri Tolkatchev. A scholar is included among the top collaborators of Dmitri Tolkatchev 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 Dmitri Tolkatchev. Dmitri Tolkatchev 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.
Tolkatchev, Dmitri, et al.. (2022). Ca2+ attenuates nucleation activity of leiomodin. Protein Science. 31(7). e4358–e4358. 2 indexed citations
2.
Tolkatchev, Dmitri, et al.. (2020). Leiomodin creates a leaky cap at the pointed end of actin-thin filaments. PLoS Biology. 18(9). e3000848–e3000848. 18 indexed citations
3.
Tolkatchev, Dmitri, et al.. (2019). Role of intrinsic disorder in muscle sarcomeres. Progress in molecular biology and translational science. 166. 311–340. 4 indexed citations
4.
Tolkatchev, Dmitri. (2018). Nuclear Magnetic Resonance Spectroscopy in Analysis of Granulin Three-Dimensional Structure and Cysteine Bridging. Methods in molecular biology. 1806. 65–80. 1 indexed citations
5.
Tolkatchev, Dmitri. (2018). Large-Scale Generation of Recombinant Granulin Peptides in E. coli. Methods in molecular biology. 1806. 51–64.
6.
Tolkatchev, Dmitri, Daniel Elnatan, Leonardo Nogara, et al.. (2018). Piperine, an alkaloid inhibiting the super-relaxed state of myosin, binds to the myosin regulatory light chain. Archives of Biochemistry and Biophysics. 659. 75–84. 7 indexed citations
7.
Tolkatchev, Dmitri, et al.. (2017). The cardiomyopathy-associated K15N mutation in tropomyosin alters actin filament pointed end dynamics. Archives of Biochemistry and Biophysics. 630. 18–26. 16 indexed citations
8.
Krieger, Inna V., Dmitri Tolkatchev, Timothy W. Moural, et al.. (2017). Structural destabilization of tropomyosin induced by the cardiomyopathy‐linked mutation R21H. Protein Science. 27(2). 498–508. 7 indexed citations
9.
Moroz, Natalia, Christopher T. Pappas, Stefanie M. Novak, et al.. (2016). The N-terminal tropomyosin- and actin-binding sites are important for leiomodin 2’s function. Molecular Biology of the Cell. 27(16). 2565–2575. 21 indexed citations
10.
Tolkatchev, Dmitri, et al.. (2016). Localization of the binding interface between leiomodin-2 and α-tropomyosin. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1864(5). 523–530. 17 indexed citations
11.
Tolkatchev, Dmitri, et al.. (2011). Molecular imaging of breast tumors using a near‐infrared fluorescently labeled clusterin binding peptide. International Journal of Cancer. 131(5). E681–92. 10 indexed citations
12.
Tolkatchev, Dmitri, et al.. (2010). Binding of human angiogenin inhibits actin polymerization. Archives of Biochemistry and Biophysics. 495(1). 74–81. 13 indexed citations
13.
Jin, Albert, et al.. (2009). Development of Polyvalent Peptide-Conjugated Magnetic Nanoparticles for Targeted In-Vivo Imaging of Micro-Thrombi. Advances in experimental medicine and biology. 611. 415–416. 1 indexed citations
14.
Tolkatchev, Dmitri, Suneil Malik, Ping Wang, et al.. (2008). Structure dissection of human progranulin identifies well‐folded granulin/epithelin modules with unique functional activities. Protein Science. 17(4). 711–724. 134 indexed citations
15.
Tolkatchev, Dmitri, Rustem Shaykhutdinov, Ping Xu, et al.. (2006). Three‐dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni. Protein Science. 15(10). 2381–2394. 16 indexed citations
16.
Tolkatchev, Dmitri, et al.. (2005). Transforming bivalent ligands into retractable enzyme inhibitors through polypeptide–protein interactions. Bioorganic & Medicinal Chemistry Letters. 15(23). 5120–5123. 4 indexed citations
17.
Tolkatchev, Dmitri, et al.. (2004). Rational design and selection of bivalent peptide ligands of thrombin incorporating P4-P1 tetrapeptide sequences: from good substrates to potent inhibitors. Protein Engineering Design and Selection. 17(8). 647–657. 14 indexed citations
18.
Vranken, Wim, Dmitri Tolkatchev, Ping Xu, et al.. (2002). Solution Structure of a Llama Single-Domain Antibody with Hydrophobic Residues Typical of the VH/VL Interface. Biochemistry. 41(27). 8570–8579. 37 indexed citations
20.
Tolkatchev, Dmitri, Linda Yu, & Chang‐An Yu. (1996). Potential Induced Redox Reactions in Mitochondrial and Bacterial Cytochrome b-c1 Complexes. Journal of Biological Chemistry. 271(21). 12356–12363. 10 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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