Roman Fedorov

1.9k total citations
50 papers, 1.5k citations indexed

About

Roman Fedorov is a scholar working on Molecular Biology, Organic Chemistry and Cardiology and Cardiovascular Medicine. According to data from OpenAlex, Roman Fedorov has authored 50 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 9 papers in Organic Chemistry and 8 papers in Cardiology and Cardiovascular Medicine. Recurrent topics in Roman Fedorov's work include RNA and protein synthesis mechanisms (11 papers), RNA modifications and cancer (9 papers) and Cardiomyopathy and Myosin Studies (8 papers). Roman Fedorov is often cited by papers focused on RNA and protein synthesis mechanisms (11 papers), RNA modifications and cancer (9 papers) and Cardiomyopathy and Myosin Studies (8 papers). Roman Fedorov collaborates with scholars based in Germany, Russia and United Kingdom. Roman Fedorov's co-authors include Ilme Schlichting, Dietmar J. Manstein, Elisabeth Hartmann, Tatiana Domratcheva, Peter Hegemann, Dipak Ghosh, Markus Fuhrmann, Michael A. Geeves, Hans‐Joachim Knölker and Herwig O. Gutzeit and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Roman Fedorov

47 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Roman Fedorov Germany 24 971 339 270 195 175 50 1.5k
Koji Tomoo Japan 25 1.2k 1.3× 206 0.6× 166 0.6× 138 0.7× 134 0.8× 78 1.8k
Joanne Widom United States 17 1.0k 1.1× 486 1.4× 495 1.8× 150 0.8× 140 0.8× 23 1.8k
Hsiau‐Wei Lee United States 25 1.2k 1.2× 175 0.5× 129 0.5× 99 0.5× 99 0.6× 64 1.9k
Barbara Spolaore Italy 25 1.5k 1.6× 134 0.4× 128 0.5× 331 1.7× 108 0.6× 45 2.2k
Jan Willem Thuring United States 22 1.1k 1.2× 396 1.2× 125 0.5× 505 2.6× 413 2.4× 53 2.2k
Maulik Patel United States 25 981 1.0× 73 0.2× 181 0.7× 275 1.4× 148 0.8× 73 1.7k
Tapas K. Mal Canada 21 1.4k 1.4× 120 0.4× 357 1.3× 256 1.3× 138 0.8× 35 1.9k
Dung Le‐Nguyen France 22 1.4k 1.4× 177 0.5× 141 0.5× 86 0.4× 351 2.0× 38 1.7k
Farida S. Sharief United States 18 1.5k 1.6× 157 0.5× 182 0.7× 211 1.1× 47 0.3× 27 2.0k
Lucy Malinina United States 25 2.2k 2.2× 344 1.0× 42 0.2× 228 1.2× 88 0.5× 60 2.5k

Countries citing papers authored by Roman Fedorov

Since Specialization
Citations

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

Fields of papers citing papers by Roman Fedorov

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Roman Fedorov

This figure shows the co-authorship network connecting the top 25 collaborators of Roman Fedorov. A scholar is included among the top collaborators of Roman Fedorov 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 Roman Fedorov. Roman Fedorov 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
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Kazmierski, Julia, Carina Elsner, Katinka Döhner, et al.. (2022). A Baseline Cellular Antiviral State Is Maintained by cGAS and Its Most Frequent Naturally Occurring Variant rs610913. The Journal of Immunology. 209(3). 535–547. 1 indexed citations
3.
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Никулин, А.Д., et al.. (2015). The Activation Mechanism of 2′-5′-Oligoadenylate Synthetase Gives New Insights Into OAS/cGAS Triggers of Innate Immunity. Structure. 23(5). 851–862. 58 indexed citations
5.
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Fedorov, Roman, et al.. (2014). Expression, purification and crystallization of a dye-decolourizing peroxidase from Dictyostelium discoideum. Acta Crystallographica Section F Structural Biology Communications. 70(2). 252–255. 2 indexed citations
7.
Damerow, Sebastian, et al.. (2012). Octamerization is essential for enzymatic function of human UDP-glucose pyrophosphorylase. Glycobiology. 23(4). 426–437. 23 indexed citations
8.
Chinthalapudi, Krishna, Manuel H. Taft, René Martin, et al.. (2011). Mechanism and Specificity of Pentachloropseudilin-mediated Inhibition of Myosin Motor Activity. Journal of Biological Chemistry. 286(34). 29700–29708. 53 indexed citations
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Nikonov, Oleg, Elena Stolboushkina, А.Д. Никулин, et al.. (2007). New Insights into the Interactions of the Translation Initiation Factor 2 from Archaea with Guanine Nucleotides and Initiator tRNA. Journal of Molecular Biology. 373(2). 328–336. 26 indexed citations
11.
Witte, Gregor, Roman Fedorov, & Ute Curth. (2007). Biophysical Analysis of Thermus aquaticus Single-Stranded DNA Binding Protein. Biophysical Journal. 94(6). 2269–2279. 21 indexed citations
12.
Fedorov, Roman, Gregor Witte, Claus Urbanke, Dietmar J. Manstein, & Ute Curth. (2006). 3D structure of Thermus aquaticus single-stranded DNA-binding protein gives insight into the functioning of SSB proteins. Nucleic Acids Research. 34(22). 6708–6717. 32 indexed citations
13.
Geeves, Michael A., Roman Fedorov, & Dietmar J. Manstein. (2005). Molecular mechanism of actomyosin-based motility. Cellular and Molecular Life Sciences. 62(13). 1462–1477. 80 indexed citations
14.
Fedorov, Roman, Ilme Schlichting, Elisabeth Hartmann, et al.. (2003). Crystal Structures and Molecular Mechanism of a Light-Induced Signaling Switch: The Phot-LOV1 Domain from Chlamydomonas reinhardtii. Biophysical Journal. 84(4). 2474–2482. 235 indexed citations
15.
Nevskaya, N., Svetlana Tishchenko, Mikhail Paveliev, et al.. (2002). Structure of ribosomal protein L1 fromMethanococcus thermolithotrophicus. Functionally important structural invariants on the L1 surface. Acta Crystallographica Section D Biological Crystallography. 58(6). 1023–1029. 12 indexed citations
16.
Davydova, Natalia, Roman Fedorov, Victor A. Streltsov, Anders Liljas, & Maria Garber. (2001). Crystals of a mutant form of ribosomal protein L22 rendering bacterial ribosomes resistant to erythromycin. Acta Crystallographica Section D Biological Crystallography. 57(8). 1150–1152. 1 indexed citations
17.
Fedorov, Roman, V. A. Meshcheryakov, G. M. Gongadze, et al.. (2001). Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins. Acta Crystallographica Section D Biological Crystallography. 57(7). 968–976. 35 indexed citations
18.
Nevskaya, N., Svetlana Tishchenko, Roman Fedorov, et al.. (2000). Archaeal ribosomal protein L1: the structure provides new insights into RNA binding of the L1 protein family. Structure. 8(4). 363–371. 30 indexed citations
19.
Fedorov, Roman, N. Nevskaya, Svetlana Tishchenko, et al.. (1999). Structure of ribosomal protein L30 from Thermus thermophilus at 1.9 Å resolution: conformational flexibility of the molecule. Acta Crystallographica Section D Biological Crystallography. 55(11). 1827–1833. 5 indexed citations
20.
Никонов, С.В., N. Nevskaya, Roman Fedorov, et al.. (1998). Structural Studies of Ribosomal Proteins. Biological Chemistry. 379(7). 795–806. 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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