T. Petrova

839 total citations
46 papers, 687 citations indexed

About

T. Petrova is a scholar working on Materials Chemistry, Molecular Biology and Radiation. According to data from OpenAlex, T. Petrova has authored 46 papers receiving a total of 687 indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Materials Chemistry, 19 papers in Molecular Biology and 9 papers in Radiation. Recurrent topics in T. Petrova's work include Enzyme Structure and Function (28 papers), Protein Structure and Dynamics (10 papers) and Advanced X-ray Imaging Techniques (8 papers). T. Petrova is often cited by papers focused on Enzyme Structure and Function (28 papers), Protein Structure and Dynamics (10 papers) and Advanced X-ray Imaging Techniques (8 papers). T. Petrova collaborates with scholars based in Russia, France and United States. T. Petrova's co-authors include A. Podjarny, A. Mitschler, Vladimir Y. Lunin, Michael L. Jones, A. Thomas DiCioccio, Janet Sredy, Diane R. Sawicki, David Gunn, Leo S. Geraci and J. Howard Jones and has published in prestigious journals such as Journal of Molecular Biology, Journal of Medicinal Chemistry and Reports on Progress in Physics.

In The Last Decade

T. Petrova

41 papers receiving 622 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. Petrova Russia 14 252 219 185 111 83 46 687
I. Ascone France 17 419 1.7× 408 1.9× 76 0.4× 80 0.7× 133 1.6× 59 926
P. A. Machin United Kingdom 8 328 1.3× 334 1.5× 80 0.4× 36 0.3× 76 0.9× 13 547
M. Elder United Kingdom 9 215 0.9× 208 0.9× 103 0.6× 18 0.2× 56 0.7× 24 484
Toshiyuki Chatake Japan 17 565 2.2× 413 1.9× 21 0.1× 49 0.4× 81 1.0× 54 779
Isabelle Hazemann France 19 860 3.4× 278 1.3× 68 0.4× 212 1.9× 62 0.7× 34 1.2k
Torsten Becker Germany 14 570 2.3× 139 0.6× 270 1.5× 31 0.3× 12 0.1× 24 747
Takekiyo Matsuo Japan 21 206 0.8× 134 0.6× 112 0.6× 83 0.7× 27 0.3× 64 1.1k
Erik Malmerberg Sweden 11 356 1.4× 175 0.8× 27 0.1× 53 0.5× 43 0.5× 14 538
Ivana Adamovic United States 10 194 0.8× 109 0.5× 103 0.6× 41 0.4× 4 0.0× 13 672
H. Lami France 18 342 1.4× 192 0.9× 99 0.5× 36 0.3× 34 0.4× 33 775

Countries citing papers authored by T. Petrova

Since Specialization
Citations

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

Fields of papers citing papers by T. Petrova

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of T. Petrova

This figure shows the co-authorship network connecting the top 25 collaborators of T. Petrova. A scholar is included among the top collaborators of T. Petrova 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. Petrova. T. Petrova 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.
Petrova, T., M. Yu. Rubtsova, I. V. Uporov, et al.. (2022). Crystal structures of the molecular class A β-lactamase TEM-171 and its complexes with tazobactam. Acta Crystallographica Section D Structural Biology. 78(7). 825–834. 1 indexed citations
2.
Petrova, T. & Vladimir Y. Lunin. (2020). Determination of the Structure of Biological Macromolecular Particles Using X-Ray Lasers. Achievements and Prospects. Mathematical Biology and Bioinformatics. 15(2). 195–234. 2 indexed citations
3.
Lunin, Vladimir Y., et al.. (2020). Mask-Based Approach in Phasing and Restoring of Single-Particle Diffraction Data. Mathematical Biology and Bioinformatics. 15(1). 57–72. 4 indexed citations
4.
Lunin, Vladimir Y., et al.. (2019). Single Particle Study by X-Ray Diffraction: Crystallographic Approach. Mathematical Biology and Bioinformatics. 14(2). 500–516. 4 indexed citations
5.
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8.
Lunin, Vladimir Y., et al.. (2015). Mask-based approach to phasing of single-particle diffraction data. Acta Crystallographica Section D Structural Biology. 72(1). 147–157. 11 indexed citations
9.
Lunin, Vladimir Y., Alexei N. Grum-Grzhimailo, Elena V. Gryzlova, et al.. (2015). Efficient calculation of diffracted intensities in the case of nonstationary scattering by biological macromolecules under XFEL pulses. Acta Crystallographica Section D Biological Crystallography. 71(2). 293–303. 13 indexed citations
10.
Kleymenov, Sergey Y., et al.. (2015). Heat-induced conformational changes of TET peptidase from crenarchaeon Desulfurococcus kamchatkensis. European Biophysics Journal. 44(8). 667–675. 2 indexed citations
11.
Petrova, T., Konstantin M. Boyko, Olga S. Sokolova, et al.. (2015). Structure of the dodecamer of the aminopeptidase APDkam598 from the archaeonDesulfurococcus kamchatkensis. Acta Crystallographica Section F Structural Biology Communications. 71(3). 277–285. 8 indexed citations
12.
Petrova, T., Vladimir Y. Lunin, Stephan L. Ginell, et al.. (2012). X-ray-induced overall structural changes in a protein molecule at cryogenic temperatures. Acta Crystallographica Section A Foundations of Crystallography. 68(a1). s266–s266. 2 indexed citations
13.
Cousido-Siah, A., Daniel Ayoub, Graciela Berberián, et al.. (2012). Structural and functional studies of ReP1-NCXSQ, a protein regulating the squid nerve Na+/Ca2+exchanger. Acta Crystallographica Section D Biological Crystallography. 68(9). 1098–1107. 8 indexed citations
14.
Petrova, T., Ekaterina Yu. Bezsudnova, Konstantin M. Boyko, et al.. (2012). ATP-dependent DNA ligase fromThermococcussp. 1519 displays a new arrangement of the OB-fold domain. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(12). 1440–1447. 16 indexed citations
15.
Petrova, T., Ekaterina Yu. Bezsudnova, K. M. Polyakov, et al.. (2012). Expression, purification, crystallization and preliminary crystallographic analysis of a thermostable DNA ligase from the archaeonThermococcus sibiricus. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(2). 163–165. 8 indexed citations
16.
Howard, Eduardo, Matthew P. Blakeley, Michael Haertlein, et al.. (2011). Neutron structure of type‐III antifreeze protein allows the reconstruction of AFP–ice interface. Journal of Molecular Recognition. 24(4). 724–732. 59 indexed citations
17.
Petrova, T., Stephan L. Ginell, A. Mitschler, et al.. (2010). X-ray-induced deterioration of disulfide bridges at atomic resolution. Acta Crystallographica Section D Biological Crystallography. 66(10). 1075–1091. 18 indexed citations
18.
Lunin, Vladimir Y., et al.. (2000). Low-resolution ab initio phasing: problems and advances. Acta Crystallographica Section D Biological Crystallography. 56(10). 1223–1232. 9 indexed citations
19.
Petrova, T., Vladimir Y. Lunin, & A. Podjarny. (2000). Ab initio low-resolution phasing in crystallography of macromolecules by maximization of likelihood. Acta Crystallographica Section D Biological Crystallography. 56(10). 1245–1252. 6 indexed citations
20.
Lunin, Vladimir Y., et al.. (1995). On theab initiosolution of the phase problem for macromolecules at very low resolution: the few atoms model method. Acta Crystallographica Section D Biological Crystallography. 51(6). 896–903. 13 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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