Т. В. Ротанова

1.1k total citations
41 papers, 843 citations indexed

About

Т. В. Ротанова is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Т. В. Ротанова has authored 41 papers receiving a total of 843 indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Biology, 26 papers in Materials Chemistry and 18 papers in Genetics. Recurrent topics in Т. В. Ротанова's work include Enzyme Structure and Function (26 papers), Bacterial Genetics and Biotechnology (18 papers) and RNA and protein synthesis mechanisms (15 papers). Т. В. Ротанова is often cited by papers focused on Enzyme Structure and Function (26 papers), Bacterial Genetics and Biotechnology (18 papers) and RNA and protein synthesis mechanisms (15 papers). Т. В. Ротанова collaborates with scholars based in Russia, United States and Italy. Т. В. Ротанова's co-authors include Edward E. Melnikov, Alla Gustchina, Alexander Wlodawer, Istvan Botos, Fatima Rasulova, Michael R. Maurizi, Joseph E. Tropea, Scott Cherry, V.K. Antonov and Zbigniew Dauter and has published in prestigious journals such as Journal of Biological Chemistry, SHILAP Revista de lepidopterología and Journal of Molecular Biology.

In The Last Decade

Т. В. Ротанова

38 papers receiving 830 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Т. В. Ротанова Russia 15 726 357 315 113 84 41 843
Edward E. Melnikov Russia 10 509 0.7× 234 0.7× 219 0.7× 86 0.8× 68 0.8× 19 598
Matthias Rose Germany 16 857 1.2× 315 0.9× 97 0.3× 114 1.0× 63 0.8× 24 1.0k
P R Waller United States 6 1.1k 1.5× 501 1.4× 128 0.4× 142 1.3× 39 0.5× 9 1.3k
Paul Wolfe United States 9 740 1.0× 516 1.4× 128 0.4× 101 0.9× 48 0.6× 11 886
Thomas E. Shrader United States 15 1.3k 1.8× 313 0.9× 148 0.5× 93 0.8× 40 0.5× 17 1.4k
Nathalie Sassoon France 14 500 0.7× 222 0.6× 93 0.3× 51 0.5× 36 0.4× 16 676
Richard P. Moerschell United States 10 1.1k 1.5× 225 0.6× 156 0.5× 106 0.9× 48 0.6× 12 1.2k
Sreedevi Nallamsetty United States 10 572 0.8× 160 0.4× 72 0.2× 46 0.4× 58 0.7× 10 711
Lynn G. Kleina United States 8 923 1.3× 397 1.1× 133 0.4× 22 0.2× 44 0.5× 9 1.0k
Evelyne Richet France 22 1.0k 1.4× 747 2.1× 167 0.5× 33 0.3× 86 1.0× 33 1.4k

Countries citing papers authored by Т. В. Ротанова

Since Specialization
Citations

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

Fields of papers citing papers by Т. В. Ротанова

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Т. В. Ротанова. 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 Т. В. Ротанова. The network helps show where Т. В. Ротанова may publish in the future.

Co-authorship network of co-authors of Т. В. Ротанова

This figure shows the co-authorship network connecting the top 25 collaborators of Т. В. Ротанова. A scholar is included among the top collaborators of Т. В. Ротанова 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 Т. В. Ротанова. Т. В. Ротанова 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.
Wlodawer, Alexander, B. Sekula, Alla Gustchina, & Т. В. Ротанова. (2022). Structure and the Mode of Activity of Lon Proteases from Diverse Organisms. Journal of Molecular Biology. 434(7). 167504–167504. 19 indexed citations
2.
Gustchina, Alla, et al.. (2020). Involvement of the N Domain Residues E34, K35, and R38 in the Functionally Active Structure of Escherichia coli Lon Protease. Acta Naturae. 12(4). 86–97. 3 indexed citations
3.
Botos, Istvan, G.T. Lountos, Weimin Wu, et al.. (2019). Cryo-EM structure of substrate-free E. coli Lon protease provides insights into the dynamics of Lon machinery. SHILAP Revista de lepidopterología. 1. 13–20. 19 indexed citations
4.
Серова, О. В., et al.. (2016). Роль фрагмента (1-106) в функционировании АТР-зависимой Lon-протеазыE. coli. Биоорганическая химия. 42(4). 421–430.
5.
Ротанова, Т. В., et al.. (2013). Уникальная структурная организация АТР-зависимых Lon-протеиназ подсемейства А. Биоорганическая химия. 39(3). 303–319.
6.
Melnikov, Edward E. & Т. В. Ротанова. (2010). Molecular chaperones. Russian Journal of Bioorganic Chemistry. 36(1). 1–10. 9 indexed citations
7.
Li, Mi, Alla Gustchina, Fatima Rasulova, et al.. (2010). Structure of the N-terminal fragment ofEscherichia coliLon protease. Acta Crystallographica Section D Biological Crystallography. 66(8). 865–873. 30 indexed citations
8.
Ротанова, Т. В., Istvan Botos, Edward E. Melnikov, et al.. (2006). Slicing a protease: Structural features of the ATP‐dependent Lon proteases gleaned from investigations of isolated domains. Protein Science. 15(8). 1815–1828. 73 indexed citations
9.
Botos, Istvan, Edward E. Melnikov, Scott Cherry, et al.. (2005). Atomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases. Journal of Molecular Biology. 351(1). 144–157. 43 indexed citations
10.
Li, Mi, Fatima Rasulova, Edward E. Melnikov, et al.. (2005). Crystal structure of the N‐terminal domain of E. coli Lon protease. Protein Science. 14(11). 2895–2900. 44 indexed citations
11.
Ротанова, Т. В., et al.. (2004). Classification of ATP‐dependent proteases Lon and comparison of the active sites of their proteolytic domains. European Journal of Biochemistry. 271(23-24). 4865–4871. 79 indexed citations
12.
Botos, Istvan, Edward E. Melnikov, Scott Cherry, et al.. (2004). The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site. Journal of Biological Chemistry. 279(9). 8140–8148. 152 indexed citations
13.
Botos, Istvan, Edward E. Melnikov, Scott Cherry, et al.. (2003). Crystal structure of the AAA+ α domain of E. coli Lon protease at 1.9Å resolution. Journal of Structural Biology. 146(1-2). 113–122. 69 indexed citations
14.
Melnikov, Edward E., et al.. (2003). Proteolysis Coupled to ATP Hydrolysis: Regulation of the Activity of Proteolytic Sites of Lon Protease from Escherichia coli. Russian Journal of Bioorganic Chemistry. 29(5). 441–449. 2 indexed citations
15.
Melnikov, Edward E., et al.. (2001). Coupling of Proteolysis to ATP Hydrolysis upon Escherichia coliLon Protease Functioning: II. Hydrolysis of ATP and Activity of the Enzyme Peptide Hydrolase Sites. Russian Journal of Bioorganic Chemistry. 27(2). 101–109. 6 indexed citations
16.
Манухов, И. В., et al.. (1999). [A test system based on the lux-regulon from Vibrio fischeri for studying the functional activity of mutant forms of Escherichia coli lon-proteinase].. PubMed. 25(5). 365–8. 2 indexed citations
17.
Koroleva, Ekaterina P., et al.. (1998). Mutations in the proteolytic domain of Escherichia coli protease Lon impair the ATPase activity of the enzyme. FEBS Letters. 422(2). 218–220. 37 indexed citations
18.
Antonov, V.K., et al.. (1988). Catalytic activity and association of pancreatic lipase. Biochimie. 70(9). 1235–1244. 13 indexed citations
19.
Ротанова, Т. В., et al.. (1976). Kinetic studies of the alkaline mesentericopeptidase. Study on the active centre topography of alkaline mesentericopeptidase by means of bifunctional reversible inhibition.. Munich Personal RePEc Archive (Ludwig Maximilian University of Munich). 8(3). 225–31. 3 indexed citations
20.
Ротанова, Т. В., et al.. (1976). KINETIC STUDIES OF THE ALKALINE MESENTERICOPEPTIDASE.. International journal of peptide & protein research. 8(3). 225–231. 3 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Edward E. Melnikov Breakdown of academic impact, for papers by Matthias Rose Breakdown of academic impact, for papers by P R Waller Breakdown of academic impact, for papers by Paul Wolfe Breakdown of academic impact, for papers by Thomas E. Shrader Breakdown of academic impact, for papers by Nathalie Sassoon Breakdown of academic impact, for papers by Richard P. Moerschell Breakdown of academic impact, for papers by Sreedevi Nallamsetty Breakdown of academic impact, for papers by Lynn G. Kleina Breakdown of academic impact, for papers by Evelyne Richet
Rankless by CCL
2026