L. E. Meshalkina

849 total citations
32 papers, 707 citations indexed

About

L. E. Meshalkina is a scholar working on Biochemistry, Neurology and Clinical Biochemistry. According to data from OpenAlex, L. E. Meshalkina has authored 32 papers receiving a total of 707 indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Biochemistry, 21 papers in Neurology and 20 papers in Clinical Biochemistry. Recurrent topics in L. E. Meshalkina's work include Biochemical Acid Research Studies (32 papers), Alcoholism and Thiamine Deficiency (21 papers) and Metabolism and Genetic Disorders (20 papers). L. E. Meshalkina is often cited by papers focused on Biochemical Acid Research Studies (32 papers), Alcoholism and Thiamine Deficiency (21 papers) and Metabolism and Genetic Disorders (20 papers). L. E. Meshalkina collaborates with scholars based in Russia, Germany and Sweden. L. E. Meshalkina's co-authors include G. Schneider, G.A. Kochetov, Ylva Lindqvist, Ulrika Nilsson, Olga N. Solovjeva, Ralph Golbik, Matti Nikkola, M. Sundström, Gerhard Hübner and Vitaly A. Selivanov and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Analytical Biochemistry.

In The Last Decade

L. E. Meshalkina

32 papers receiving 692 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
L. E. Meshalkina Russia 14 584 366 331 294 53 32 707
Olga N. Solovjeva Russia 11 196 0.3× 121 0.3× 94 0.3× 189 0.6× 37 0.7× 26 392
Krishnamoorthy Chandrasekhar United States 8 301 0.5× 129 0.4× 216 0.7× 149 0.5× 14 0.3× 8 374
Sukhdeep Sidhu United States 7 188 0.3× 62 0.2× 125 0.4× 197 0.7× 39 0.7× 7 346
Hetalben Patel United States 10 173 0.3× 77 0.2× 84 0.3× 270 0.9× 26 0.5× 13 460
István Alkonyi Hungary 10 140 0.2× 21 0.1× 214 0.6× 197 0.7× 70 1.3× 24 375
Robert C. Vallari United States 10 77 0.1× 28 0.1× 38 0.1× 258 0.9× 49 0.9× 13 442
Aníbal M. Nervi Argentina 14 255 0.4× 11 0.0× 85 0.3× 327 1.1× 113 2.1× 19 692
David R. Wilken United States 11 88 0.2× 16 0.0× 76 0.2× 227 0.8× 75 1.4× 20 385
Jun Oizumi Japan 12 75 0.1× 28 0.1× 35 0.1× 130 0.4× 17 0.3× 32 358
Payam Baziyar Iran 11 46 0.1× 99 0.3× 35 0.1× 105 0.4× 81 1.5× 24 331

Countries citing papers authored by L. E. Meshalkina

Since Specialization
Citations

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

Fields of papers citing papers by L. E. Meshalkina

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by L. E. Meshalkina. 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 L. E. Meshalkina. The network helps show where L. E. Meshalkina may publish in the future.

Co-authorship network of co-authors of L. E. Meshalkina

This figure shows the co-authorship network connecting the top 25 collaborators of L. E. Meshalkina. A scholar is included among the top collaborators of L. E. Meshalkina 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 L. E. Meshalkina. L. E. Meshalkina 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.
Meshalkina, L. E., et al.. (2012). Computer modeling of transketolase-like protein, TKTL1, a marker of certain tumor tissues. Biochemistry (Moscow). 77(3). 296–299. 10 indexed citations
2.
Meshalkina, L. E., et al.. (2012). Is transketolase-like protein, TKTL1, transketolase?. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1832(3). 387–390. 22 indexed citations
3.
Meshalkina, L. E., Olga N. Solovjeva, & G.A. Kochetov. (2011). Interaction of transketolase from human tissues with substrates. Biochemistry (Moscow). 76(9). 1061–1064. 4 indexed citations
4.
Meshalkina, L. E., et al.. (2010). Isolation and properties of human transketolase. Biochemistry (Moscow). 75(7). 873–880. 7 indexed citations
5.
Esakova, Olga, L. E. Meshalkina, G.A. Kochetov, & Ralph Golbik. (2009). Halogenated pyruvate derivatives as substrates of transketolase from Saccharomyces cerevisiae. Biochemistry (Moscow). 74(11). 1234–1238. 6 indexed citations
6.
Meshalkina, L. E., G.A. Kochetov, Gerhard Hübner, Kai Tittmann, & Ralph Golbik. (2009). New function of the amino group of thiamine diphosphate in thiamine catalysis. Biochemistry (Moscow). 74(3). 293–300. 5 indexed citations
7.
Esakova, Olga, L. E. Meshalkina, Ralph Golbik, et al.. (2007). Which stage of the process of apotransketolase interaction with thiamine diphosphate is affected by the regulatory activity of the donor substrate?. IUBMB Life. 59(2). 104–109. 2 indexed citations
8.
Meshalkina, L. E., et al.. (2007). New evidence for cofactor’s amino group function in thiamin catalysis by transketolase. Biochemical and Biophysical Research Communications. 366(3). 692–697. 10 indexed citations
9.
Esakova, Olga, L. E. Meshalkina, & G.A. Kochetov. (2005). Effects of transketolase cofactors on its conformation and stability. Life Sciences. 78(1). 8–13. 13 indexed citations
10.
Esakova, Olga, et al.. (2005). Effect of Transketolase Substrates on Holoenzyme Reconstitution and Stability. Biochemistry (Moscow). 70(7). 770–776. 5 indexed citations
11.
Selivanov, Vitaly A., L. E. Meshalkina, Olga N. Solovjeva, et al.. (2005). Rapid simulation and analysis of isotopomer distributions using constraints based on enzyme mechanisms: an example from HT29 cancer cells. Computer applications in the biosciences. 21(17). 3558–3564. 30 indexed citations
12.
Kaplun, Alexander, Maria Vyazmensky, Stanislav Engel, et al.. (2005). Monitoring the acetohydroxy acid synthase reaction and related carboligations by circular dichroism spectroscopy. Analytical Biochemistry. 342(1). 126–133. 21 indexed citations
13.
Golbik, Ralph, L. E. Meshalkina, Tatyana Sandalova, et al.. (2005). Effect of coenzyme modification on the structural and catalytic properties of wild‐type transketolase and of the variant E418A from Saccharomyces cerevisiae. FEBS Journal. 272(6). 1326–1342. 13 indexed citations
14.
Selivanov, Vitaly A., et al.. (2004). Kinetic study of the H103A mutant yeast transketolase. FEBS Letters. 567(2-3). 270–274. 15 indexed citations
15.
Esakova, Olga, L. E. Meshalkina, Ralph Golbik, Gerhard Hübner, & G.A. Kochetov. (2004). Donor substrate regulation of transketolase. European Journal of Biochemistry. 271(21). 4189–4194. 12 indexed citations
16.
Solovjeva, Olga N., et al.. (2002). The origin of the absorption band induced through the interaction between apotransketolase and thiamin diphosphate. Biochemical and Biophysical Research Communications. 294(1). 155–160. 13 indexed citations
17.
Solovjeva, Olga N., et al.. (2001). One-Substrate Transketolase-Catalyzed Reaction. Biochemical and Biophysical Research Communications. 280(3). 845–847. 35 indexed citations
18.
Meshalkina, L. E., et al.. (2001). Cleaving of Ketosubstrates by Transketolase and the Nature of the Products Formed. Biochemistry (Moscow). 66(8). 932–936. 16 indexed citations
19.
Meshalkina, L. E., et al.. (1997). Examination of the Thiamin Diphosphate Binding Site in Yeast Transketolase by Site‐Directed Mutagenesis. European Journal of Biochemistry. 244(2). 646–652. 38 indexed citations
20.

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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