T. A. Muranova

656 total citations
30 papers, 538 citations indexed

About

T. A. Muranova is a scholar working on Molecular Biology, Food Science and Aquatic Science. According to data from OpenAlex, T. A. Muranova has authored 30 papers receiving a total of 538 indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 6 papers in Food Science and 5 papers in Aquatic Science. Recurrent topics in T. A. Muranova's work include Protein Hydrolysis and Bioactive Peptides (8 papers), Aquaculture Nutrition and Growth (5 papers) and Peptidase Inhibition and Analysis (5 papers). T. A. Muranova is often cited by papers focused on Protein Hydrolysis and Bioactive Peptides (8 papers), Aquaculture Nutrition and Growth (5 papers) and Peptidase Inhibition and Analysis (5 papers). T. A. Muranova collaborates with scholars based in Russia, United Kingdom and Japan. T. A. Muranova's co-authors include Svetlana E. Sedelnikova, I.A. Eliseikina, Maria Garber, С.В. Никонов, Anders Liljas, N.P. Fomenkova, N. Nevskaya, L.A. Svensson, А. И. Мирошников and Д. В. Зинченко and has published in prestigious journals such as The EMBO Journal, Journal of Molecular Biology and Applied and Environmental Microbiology.

In The Last Decade

T. A. Muranova

30 papers receiving 528 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
T. A. Muranova Russia 11 424 125 95 54 51 30 538
David W. Hibler United States 7 357 0.8× 60 0.5× 216 2.3× 64 1.2× 48 0.9× 8 623
Takao Torikata Japan 17 390 0.9× 110 0.9× 44 0.5× 21 0.4× 191 3.7× 57 625
Jacob Verghese Germany 9 683 1.6× 73 0.6× 27 0.3× 34 0.6× 59 1.2× 9 859
Stuart J. Jamieson United Kingdom 8 533 1.3× 60 0.5× 110 1.2× 145 2.7× 33 0.6× 11 751
Chi-Min Ho United States 9 332 0.8× 36 0.3× 73 0.8× 48 0.9× 56 1.1× 10 610
Louis P. Visentin Canada 19 600 1.4× 64 0.5× 269 2.8× 166 3.1× 41 0.8× 45 763
Benoı̂t Odaert France 15 572 1.3× 38 0.3× 90 0.9× 71 1.3× 84 1.6× 27 648
Samuel Zinker Mexico 12 527 1.2× 17 0.1× 41 0.4× 43 0.8× 61 1.2× 23 709
Željka Maglica Switzerland 10 537 1.3× 147 1.2× 127 1.3× 36 0.7× 33 0.6× 17 711

Countries citing papers authored by T. A. Muranova

Since Specialization
Citations

This map shows the geographic impact of T. A. Muranova'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 T. A. Muranova with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites T. A. Muranova more than expected).

Fields of papers citing papers by T. A. Muranova

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of T. A. Muranova

This figure shows the co-authorship network connecting the top 25 collaborators of T. A. Muranova. A scholar is included among the top collaborators of T. A. Muranova 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 T. A. Muranova. T. A. Muranova 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.
Кононова, С. В., et al.. (2019). Intestinal microbiota of salmonids and its changes upon introduction of soy proteins to fish feed. Aquaculture International. 27(2). 475–496. 39 indexed citations
2.
Muranova, T. A., et al.. (2018). Hydrolysis of Soybean Proteins with Kamchatka Crab Hepatopancreas Enzyme Complex. Applied Biochemistry and Microbiology. 54(1). 76–82. 5 indexed citations
3.
Muranova, T. A., et al.. (2014). Lytic Peptidase L5 of <b><i>Lysobacter </i></b>sp. XL1 with Broad Antimicrobial Spectrum. Microbial Physiology. 24(1). 59–66. 31 indexed citations
4.
Stepnaya, O. A., et al.. (2008). Extracellular yeast-lytic enzyme of the bacterium Lysobacter sp. XL 1. Biochemistry (Moscow). 73(3). 310–314. 8 indexed citations
5.
Yamamoto, Naoki, Naoko Takahashi, Hiroyuki Kakinuma, et al.. (2007). Mechanistic Analysis of the Phosphonate Transition-state Analogue-derived Catalytic and Non-catalytic Antibody. The Journal of Biochemistry. 142(4). 421–433. 1 indexed citations
6.
Stepnaya, O. A., et al.. (2005). Isolation and Characterization of a New Extracellular Bacteriolytic Endopeptidase of Lysobacter sp. XL1. Biochemistry (Moscow). 70(9). 1031–1037. 21 indexed citations
7.
Muranova, T. A., et al.. (2004). Structural Investigations and Identification of the Extracellular Bacteriolytic Endopeptidase L1 from Lysobacter sp. XL1. Biochemistry (Moscow). 69(5). 501–505. 12 indexed citations
8.
Muranova, T. A., Svetlana E. Sedelnikova, Philip M. Leonard, et al.. (2003). Crystallization of RusA Holliday junction resolvase fromEscherichia coli. Acta Crystallographica Section D Biological Crystallography. 59(12). 2262–2264. 1 indexed citations
9.
Rafferty, John B., Edward L. Bolt, T. A. Muranova, et al.. (2003). The Structure of Escherichia coli RusA Endonuclease Reveals a New Holliday Junction DNA Binding Fold. Structure. 11(12). 1557–1567. 20 indexed citations
10.
Ruzheinikov, S.N., T. A. Muranova, Svetlana E. Sedelnikova, et al.. (2003). High-resolution Crystal Structure of the Fab-fragments of a Family of Mouse Catalytic Antibodies with Esterase Activity. Journal of Molecular Biology. 332(2). 423–435. 11 indexed citations
11.
Muranova, T. A., S.N. Ruzheinikov, Adrian Higginbottom, et al.. (2003). Crystallization of a carbamatase catalytic antibody Fab fragment and its complex with a transition-state analogue. Acta Crystallographica Section D Biological Crystallography. 60(1). 172–174. 3 indexed citations
12.
Muranova, T. A., S.N. Ruzheinikov, Svetlana E. Sedelnikova, et al.. (2002). Crystallization and preliminary X-ray analysis of substrate complexes of leucine dehydrogenase fromThermoactinomyces intermedius. Acta Crystallographica Section D Biological Crystallography. 58(6). 1059–1062. 2 indexed citations
13.
Muranova, T. A., S.N. Ruzheinikov, Svetlana E. Sedelnikova, et al.. (2001). The preparation and crystallization of Fab fragments of a family of mouse esterolytic catalytic antibodies and their complexes with a transition-state analogue. Acta Crystallographica Section D Biological Crystallography. 57(8). 1192–1195. 2 indexed citations
14.
Kukhtina, Viktoria, Christoph Weise, T. A. Muranova, et al.. (2000). Muscarinic toxin-like proteins from cobra venom. European Journal of Biochemistry. 267(23). 6784–6789. 3 indexed citations
15.
Muranova, T. A., et al.. (2000). Proteolytic specificity of plasmin toward adhesive proteins. Russian Journal of Bioorganic Chemistry. 26(5). 317–321. 2 indexed citations
16.
Kukhtina, Viktoria, Christoph Weise, T. A. Muranova, et al.. (2000). Muscarinic toxin‐like proteins from cobra venom. European Journal of Biochemistry. 267(23). 6784–6789. 38 indexed citations
17.
Sedelnikova, Svetlana E., et al.. (1994). Proteins of the Thermus thermophilus ribosome. Purification of proteins from the large ribosomal subunit. Biochimie. 76(5). 440–451. 5 indexed citations
18.
Svensson, L.A., Anders Liljas, Svetlana E. Sedelnikova, et al.. (1994). Crystal structure of the ribosomal protein S6 from Thermus thermophilus.. The EMBO Journal. 13(6). 1249–1254. 125 indexed citations
19.
Lindahl, Martin, L.A. Svensson, Anders Liljas, et al.. (1994). Crystal structure of the ribosomal protein S6 from Thermus thermophilus.. PubMed. 13(6). 1249–54. 129 indexed citations
20.
Amons, Reinout, et al.. (1993). The complete primary structure of ribosomal protein L1 fromThermus thermophilus. Journal of Protein Chemistry. 12(6). 725–734. 4 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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