Natalia Pakharukova

495 total citations
26 papers, 339 citations indexed

About

Natalia Pakharukova is a scholar working on Molecular Biology, Spectroscopy and Genetics. According to data from OpenAlex, Natalia Pakharukova has authored 26 papers receiving a total of 339 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 8 papers in Spectroscopy and 7 papers in Genetics. Recurrent topics in Natalia Pakharukova's work include Advanced Proteomics Techniques and Applications (8 papers), Metabolomics and Mass Spectrometry Studies (7 papers) and Bacterial Genetics and Biotechnology (5 papers). Natalia Pakharukova is often cited by papers focused on Advanced Proteomics Techniques and Applications (8 papers), Metabolomics and Mass Spectrometry Studies (7 papers) and Bacterial Genetics and Biotechnology (5 papers). Natalia Pakharukova collaborates with scholars based in Finland, Russia and United States. Natalia Pakharukova's co-authors include Minna Tuittila, Anton V. Zavialov, Sari Paavilainen, Stefan D. Knight, Susann Teneberg, Robert J. Lefkowitz, Л. Х. Пастушкова, И. М. Ларина, Stephen Matthews and Ali Masoudi and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Natalia Pakharukova

24 papers receiving 337 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Natalia Pakharukova Finland 8 204 130 110 59 44 26 339
Hubing Lou United Kingdom 6 187 0.9× 145 1.1× 48 0.4× 105 1.8× 47 1.1× 7 364
Eun Seon Chung South Korea 11 237 1.2× 219 1.7× 78 0.7× 79 1.3× 36 0.8× 13 436
B. Siebert Germany 6 224 1.1× 129 1.0× 44 0.4× 61 1.0× 33 0.8× 6 437
Blanche L. Fields United States 6 274 1.3× 109 0.8× 57 0.5× 81 1.4× 42 1.0× 7 374
Michelle C. Swick United States 9 275 1.3× 191 1.5× 66 0.6× 97 1.6× 66 1.5× 10 529
Michael Berger Germany 12 92 0.5× 36 0.3× 117 1.1× 83 1.4× 57 1.3× 37 350
Yohann Duverger France 9 203 1.0× 90 0.7× 49 0.4× 106 1.8× 40 0.9× 11 354
Edward F. Griffin United States 8 194 1.0× 40 0.3× 37 0.3× 40 0.7× 16 0.4× 9 301
Mauro Truglio Italy 13 168 0.8× 61 0.5× 35 0.3× 25 0.4× 14 0.3× 35 491
Shinichiro Hirai Japan 12 161 0.8× 60 0.5× 113 1.0× 21 0.4× 37 0.8× 40 510

Countries citing papers authored by Natalia Pakharukova

Since Specialization
Citations

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

Fields of papers citing papers by Natalia Pakharukova

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Natalia Pakharukova

This figure shows the co-authorship network connecting the top 25 collaborators of Natalia Pakharukova. A scholar is included among the top collaborators of Natalia Pakharukova 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 Natalia Pakharukova. Natalia Pakharukova 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.
Pakharukova, Natalia, et al.. (2026). Antiparallel stacking of Csu pili drives Acinetobacter baumannii 3D biofilm assembly. Nature Communications. 17(1).
2.
Pakharukova, Natalia, et al.. (2026). Cardiomyocyte β-arrestins mediate inflammation and cGAS-STING activation in CVB3 viral myocarditis. American Journal of Physiology-Heart and Circulatory Physiology. 330(2). H499–H514.
3.
Pakharukova, Natalia, Minna Tuittila, Tobias Dahlberg, et al.. (2022). Archaic chaperone–usher pili self-secrete into superelastic zigzag springs. Nature. 609(7926). 335–340. 22 indexed citations
4.
Zang, Yunxiang, Alem W. Kahsai, Natalia Pakharukova, Li-Yin Huang, & Robert J. Lefkowitz. (2021). The GPCR–β-arrestin complex allosterically activates C-Raf by binding its amino terminus. Journal of Biological Chemistry. 297(6). 101369–101369. 13 indexed citations
5.
Pakharukova, Natalia, Ali Masoudi, Biswaranjan Pani, Dean P. Staus, & Robert J. Lefkowitz. (2020). Allosteric activation of proto-oncogene kinase Src by GPCR–beta-arrestin complexes. Journal of Biological Chemistry. 295(49). 16773–16784. 31 indexed citations
6.
Pakharukova, Natalia, Minna Tuittila, Sari Paavilainen, et al.. (2018). Structural basis for Acinetobacter baumannii biofilm formation. Proceedings of the National Academy of Sciences. 115(21). 5558–5563. 129 indexed citations
7.
Pakharukova, Natalia, Minna Tuittila, Sari Paavilainen, et al.. (2018). Archaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information. Journal of Biological Chemistry. 293(44). 17070–17080. 5 indexed citations
8.
Pakharukova, Natalia, Minna Tuittila, Sari Paavilainen, & Anton V. Zavialov. (2017). Methylation, crystallization and SAD phasing of the Csu pilus CsuC–CsuE chaperone–adhesin subunit pre-assembly complex from Acinetobacter baumannii. Acta Crystallographica Section F Structural Biology Communications. 73(8). 450–454. 7 indexed citations
9.
Pakharukova, Natalia, Minna Tuittila, Sari Paavilainen, et al.. (2016). Structural basis for Myf and Psa fimbriae‐mediated tropism of pathogenic strains of Yersinia for host tissues. Molecular Microbiology. 102(4). 593–610. 12 indexed citations
10.
Pakharukova, Natalia, Minna Tuittila, Sari Paavilainen, & Anton V. Zavialov. (2015). Crystallization and preliminary X-ray diffraction analysis of the Csu pili CsuC–CsuA/B chaperone–major subunit pre-assembly complex fromAcinetobacter baumannii. Acta Crystallographica Section F Structural Biology Communications. 71(6). 770–774. 7 indexed citations
11.
Pakharukova, Natalia, James A. Garnett, Minna Tuittila, et al.. (2015). Structural Insight into Archaic and Alternative Chaperone-Usher Pathways Reveals a Novel Mechanism of Pilus Biogenesis. PLoS Pathogens. 11(11). e1005269–e1005269. 29 indexed citations
12.
Berry, Andrea A., Yi Yang, Natalia Pakharukova, et al.. (2014). Structural Insight into Host Recognition by Aggregative Adherence Fimbriae of Enteroaggregative Escherichia coli. PLoS Pathogens. 10(9). e1004404–e1004404. 35 indexed citations
13.
Pakharukova, Natalia, Minna Tuittila, & Anton V. Zavialov. (2013). Crystallization and sulfur SAD phasing of AggA, the major subunit of aggregative adherence fimbriae type I from theEscherichia colistrain that caused an outbreak of haemolytic-uraemic syndrome in Germany. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69(12). 1389–1392. 2 indexed citations
14.
Pakharukova, Natalia, Л. Х. Пастушкова, Sergei A. Moshkovskii, & И. М. Ларина. (2012). Variability of healthy human proteome. Biomeditsinskaya Khimiya. 58(5). 514–529. 4 indexed citations
15.
Пастушкова, Л. Х., et al.. (2012). [Direct proteome profiling of human blood serum in the experiment with 5-day dry immersion].. PubMed. 45(6). 13–8. 2 indexed citations
16.
Пастушкова, Л. Х., et al.. (2011). Variability of urine proteome in healthy humans during a 105-day isolation in a pressurized compartment. Human Physiology. 37(3). 351–354. 6 indexed citations
17.
Pakharukova, Natalia, Л. Х. Пастушкова, Sergei A. Moshkovskii, & И. М. Ларина. (2011). Variability of the healthy human proteome. Biochemistry (Moscow) Supplement Series B Biomedical Chemistry. 5(3). 203–212. 3 indexed citations
18.
Pakharukova, Natalia, et al.. (2010). Study of Normal Human Serum Proteomic Profile under Conditions of Hyperbaric Oxygen-Nitrogen-Argon Exposure. Bulletin of Experimental Biology and Medicine. 149(1). 37–39. 3 indexed citations
19.
Pakharukova, Natalia, Л. Х. Пастушкова, И. М. Ларина, & A.I. Grigoriev. (2009). Changes of human serum proteome profile during 7-day “dry” immersion. Acta Astronautica. 68(9-10). 1523–1528. 8 indexed citations
20.
Pakharukova, Natalia, et al.. (2009). [Optimization of the profiling of blood serum of healthy humans].. PubMed. 35(3). 101–7. 1 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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