E.V. Blagova

1.7k total citations
54 papers, 1.2k citations indexed

About

E.V. Blagova is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, E.V. Blagova has authored 54 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 31 papers in Molecular Biology, 21 papers in Materials Chemistry and 19 papers in Genetics. Recurrent topics in E.V. Blagova's work include Enzyme Structure and Function (20 papers), Bacterial Genetics and Biotechnology (17 papers) and Enzyme Production and Characterization (10 papers). E.V. Blagova is often cited by papers focused on Enzyme Structure and Function (20 papers), Bacterial Genetics and Biotechnology (17 papers) and Enzyme Production and Characterization (10 papers). E.V. Blagova collaborates with scholars based in United Kingdom, Denmark and United States. E.V. Blagova's co-authors include Anthony J. Wilkinson, V.M. Levdikov, Keith S. Wilson, Olga V. Moroz, J.A. Brannigan, Abraham L. Sonenshein, Mark J. Fogg, Anne‐Kathrin Duhme‐Klair, Igor Bronstein and Pascale Joseph 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

E.V. Blagova

52 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
E.V. Blagova United Kingdom 21 794 293 178 154 147 54 1.2k
Changsoo Chang United States 24 1.1k 1.4× 243 0.8× 283 1.6× 102 0.7× 126 0.9× 64 1.6k
Carole Creuzenet Canada 25 773 1.0× 210 0.7× 188 1.1× 206 1.3× 103 0.7× 46 1.3k
Heather K. Lamb United Kingdom 26 1.1k 1.4× 243 0.8× 248 1.4× 98 0.6× 89 0.6× 62 1.5k
Laurent Aussel France 25 1.1k 1.4× 484 1.7× 147 0.8× 263 1.7× 105 0.7× 42 2.0k
Michael Graninger Austria 17 794 1.0× 234 0.8× 234 1.3× 174 1.1× 95 0.6× 24 1.3k
Mayuree Fuangthong Thailand 22 1.2k 1.5× 546 1.9× 172 1.0× 140 0.9× 150 1.0× 43 2.0k
Andrew Leech United Kingdom 19 696 0.9× 194 0.7× 150 0.8× 166 1.1× 116 0.8× 41 1.1k
Andréa Villarino Uruguay 17 932 1.2× 143 0.5× 120 0.7× 121 0.8× 298 2.0× 31 1.3k
Ohsuk Kwon South Korea 28 1.8k 2.3× 798 2.7× 156 0.9× 207 1.3× 101 0.7× 71 2.4k
Evan W. Skowronski United States 15 874 1.1× 292 1.0× 99 0.6× 120 0.8× 60 0.4× 25 1.5k

Countries citing papers authored by E.V. Blagova

Since Specialization
Citations

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

Fields of papers citing papers by E.V. Blagova

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by E.V. Blagova. 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 E.V. Blagova. The network helps show where E.V. Blagova may publish in the future.

Co-authorship network of co-authors of E.V. Blagova

This figure shows the co-authorship network connecting the top 25 collaborators of E.V. Blagova. A scholar is included among the top collaborators of E.V. Blagova 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 E.V. Blagova. E.V. Blagova 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.
Blagova, E.V., et al.. (2024). Catch-and-Release: The Assembly, Immobilization, and Recycling of Redox-Reversible Artificial Metalloenzymes. ACS Catalysis. 14(5). 3218–3227. 4 indexed citations
2.
3.
Moroz, Olga V., E.V. Blagova, Andrey A. Lebedev, et al.. (2023). Module walking using an SH3-like cell-wall-binding domain leads to a new GH184 family of muramidases. Acta Crystallographica Section D Structural Biology. 79(8). 706–720. 1 indexed citations
4.
Moroz, Olga V., E.V. Blagova, G.J. Davies, et al.. (2023). Structural and functional characterization of a multi-domain GH92 α-1,2-mannosidase from Neobacillus novalis. Acta Crystallographica Section D Structural Biology. 79(5). 387–400. 5 indexed citations
5.
Blagova, E.V., et al.. (2023). Thermostable homologues of the periplasmic siderophore-binding protein CeuE from Geobacillus stearothermophilus and Parageobacillus thermoglucosidasius. Acta Crystallographica Section D Structural Biology. 79(8). 694–705. 3 indexed citations
6.
Moroz, Olga V., E.V. Blagova, Andrey A. Lebedev, et al.. (2021). Multitasking in the gut:X-ray structure of a multidomain BbgIII from Bifidobacterium bifidum offers possible explanations for its alternative functions. White Rose Research Online (University of Leeds, The University of Sheffield, University of York).
7.
Mathieu, Yann, Wendy A. Offen, Luisa Ciano, et al.. (2020). Discovery of a Fungal Copper Radical Oxidase with High Catalytic Efficiency toward 5-Hydroxymethylfurfural and Benzyl Alcohols for Bioprocessing. ACS Catalysis. 10(5). 3042–3058. 46 indexed citations
8.
Roth, Christian, E.V. Blagova, Roderick E. Hubbard, et al.. (2020). Substrate Engagement and Catalytic Mechanisms of N-Acetylglucosaminyltransferase V. ACS Catalysis. 10(15). 8590–8596. 29 indexed citations
9.
Freiesleben, Pernille von, Olga V. Moroz, E.V. Blagova, et al.. (2019). Crystal structure and substrate interactions of an unusual fungal non-CBM carrying GH26 endo-β-mannanase from Yunnania penicillata. Scientific Reports. 9(1). 20 indexed citations
10.
Roth, Christian, Olga V. Moroz, J.P. Turkenburg, et al.. (2019). Structural and Functional Characterization of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance. International Journal of Molecular Sciences. 20(19). 4902–4902. 13 indexed citations
11.
Bule, Pedro, E.V. Blagova, Liang Wu, et al.. (2019). Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action. Nature Communications. 10(1). 4816–4816. 15 indexed citations
12.
Moroz, Olga V., L.F. Sobala, E.V. Blagova, et al.. (2018). Structure of a Talaromyces pinophilus GH62 arabinofuranosidase in complex with AraDNJ at 1.25 Å resolution. Acta Crystallographica Section F Structural Biology Communications. 74(8). 490–495. 4 indexed citations
13.
Blagova, E.V., et al.. (2018). Mimicking salmochelin S1 and the interactions of its Fe(III) complex with periplasmic iron siderophore binding proteins CeuE and VctP. Journal of Inorganic Biochemistry. 190. 75–84. 7 indexed citations
14.
Vind, Jesper, Olga V. Moroz, E.V. Blagova, et al.. (2016). Controlled lid-opening in Thermomyces lanuginosus lipase– An engineered switch for studying lipase function. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1865(1). 20–27. 45 indexed citations
15.
Blagova, E.V., et al.. (2015). Structural characterisation of the virulence-associated protein VapG from the horse pathogen Rhodococcus equi. Veterinary Microbiology. 179(1-2). 42–52. 16 indexed citations
16.
García‐Nafría, Javier, Gabriela Ondrovičová, E.V. Blagova, et al.. (2010). Structure of the catalytic domain of the human mitochondrial Lon protease: Proposed relation of oligomer formation and activity. Protein Science. 19(5). 987–999. 41 indexed citations
17.
Levdikov, V.M., E.V. Blagova, Pascale Joseph, Abraham L. Sonenshein, & Anthony J. Wilkinson. (2006). The Structure of CodY, a GTP- and Isoleucine-responsive Regulator of Stationary Phase and Virulence in Gram-positive Bacteria. Journal of Biological Chemistry. 281(16). 11366–11373. 80 indexed citations
18.
Levdikov, V.M., E.V. Blagova, Mark J. Fogg, et al.. (2005). Structures of two superoxide dismutases fromBacillus anthracisreveal a novel active centre. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(7). 621–624. 9 indexed citations
19.
Blagova, E.V. & И. П. Куранова. (1999). Crystallization and preparation of protein crystals for X-ray diffraction analysis. 44(3). 513–531. 2 indexed citations
20.
Lunin, Vladimir Y., V.M. Levdikov, E.V. Blagova, et al.. (1997). Three‐dimensional structure of Serratiamarcescens nuclease at 1.7 Å resolution and mechanism of its action. FEBS Letters. 412(1). 217–222. 27 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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