Irina I. Protasevich

1.2k total citations
32 papers, 973 citations indexed

About

Irina I. Protasevich is a scholar working on Molecular Biology, Physical and Theoretical Chemistry and Materials Chemistry. According to data from OpenAlex, Irina I. Protasevich has authored 32 papers receiving a total of 973 indexed citations (citations by other indexed papers that have themselves been cited), including 28 papers in Molecular Biology, 8 papers in Physical and Theoretical Chemistry and 8 papers in Materials Chemistry. Recurrent topics in Irina I. Protasevich's work include Protein Structure and Dynamics (11 papers), thermodynamics and calorimetric analyses (8 papers) and Enzyme Structure and Function (8 papers). Irina I. Protasevich is often cited by papers focused on Protein Structure and Dynamics (11 papers), thermodynamics and calorimetric analyses (8 papers) and Enzyme Structure and Function (8 papers). Irina I. Protasevich collaborates with scholars based in Russia, United States and France. Irina I. Protasevich's co-authors include Christie G. Brouillette, Vladimir M. Lobachov, Robert Gilli, Claudette Briand, Alexander Makarov, J.F. Hunt, S. Atwell, Diana Wetmore, Zhengrong Yang and Xun Zhao and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Journal of Molecular Biology.

In The Last Decade

Irina I. Protasevich

32 papers receiving 958 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Irina I. Protasevich Russia	17	699	261	159	116	99	32	973
Carol Perez‐Iratxeta Canada	10	744 1.1×	58 0.2×	79 0.5×	97 0.8×	79 0.8×	13	1.1k
Lynda Dieckman United States	10	691 1.0×	54 0.2×	166 1.0×	160 1.4×	41 0.4×	15	915
P Shenbagamurthi United States	19	656 0.9×	134 0.5×	31 0.2×	60 0.5×	91 0.9×	32	1.0k
Yilmaz Alguel United Kingdom	12	745 1.1×	60 0.2×	207 1.3×	163 1.4×	77 0.8×	17	1.1k
Tanya R. Mealy United States	17	842 1.2×	145 0.6×	44 0.3×	188 1.6×	33 0.3×	17	1.2k
Eiichi Nakano Japan	19	608 0.9×	71 0.3×	75 0.5×	83 0.7×	139 1.4×	53	943
Eric A. Toth United States	23	1.2k 1.7×	63 0.2×	119 0.7×	145 1.3×	40 0.4×	53	1.5k
Beth L. Gillece-Castro United States	15	714 1.0×	39 0.1×	79 0.5×	194 1.7×	81 0.8×	19	1.2k
S. Swaminathan United States	11	446 0.6×	55 0.2×	150 0.9×	72 0.6×	30 0.3×	18	1.0k
Kathleen S. Molnar United States	15	680 1.0×	99 0.4×	55 0.3×	189 1.6×	70 0.7×	18	991

Countries citing papers authored by Irina I. Protasevich

Since Specialization

Citations

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

Fields of papers citing papers by Irina I. Protasevich

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Irina I. Protasevich. 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 Irina I. Protasevich. The network helps show where Irina I. Protasevich may publish in the future.

Co-authorship network of co-authors of Irina I. Protasevich

This figure shows the co-authorship network connecting the top 25 collaborators of Irina I. Protasevich. A scholar is included among the top collaborators of Irina I. Protasevich 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 Irina I. Protasevich. Irina I. Protasevich is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Bai, Jiangping, Douglas J. Swartz, Irina I. Protasevich, et al.. (2011). A Gene Optimization Strategy that Enhances Production of Fully Functional P-Glycoprotein in Pichia pastoris. PLoS ONE. 6(8). e22577–e22577. 83 indexed citations

Protasevich, Irina I., Zhengrong Yang, S. Atwell, et al.. (2010). Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide‐binding domain 1. Protein Science. 19(10). 1917–1931. 102 indexed citations

McDonald, Heather M., Champion Deivanayagam, Irina I. Protasevich, et al.. (2007). Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD⁺synthetase fromBacillus anthracis. Acta Crystallographica Section D Biological Crystallography. 63(8). 891–905. 18 indexed citations

Senkovich, Olga, W. James Cook, Shaper Mirza, et al.. (2007). Structure of a Complex of Human Lactoferrin N-lobe with Pneumococcal Surface Protein A Provides Insight into Microbial Defense Mechanism. Journal of Molecular Biology. 370(4). 701–713. 57 indexed citations

Protasevich, Irina I., Christie G. Brouillette, Mark E. Snow, et al.. (2004). Role of Inhibitor Aliphatic Chain in the Thermodynamics of Inhibitor Binding to Escherichia coli Enoyl-ACP Reductase and the Phe203Leu Mutant: A Proposed Mechanism for Drug Resistance. Biochemistry. 43(42). 13380–13389. 10 indexed citations

Schulga, Alexey, Alexander Makarov, Vladimir M. Lobachov, et al.. (2002). Increased stability of human growth hormone with reduced lactogenic potency. FEBS Letters. 528(1-3). 257–260. 6 indexed citations

Protasevich, Irina I., Alexey Schulga, K. M. Polyakov, et al.. (1999). Key role of barstar Cys‐40 residue in the mechanism of heat denaturation of bacterial ribonuclease complexes with barstar. FEBS Letters. 445(2-3). 384–388. 10 indexed citations

Tsvetkov, Philipp O., Irina I. Protasevich, Robert Gilli, et al.. (1999). Apocalmodulin Binds to the Myosin Light Chain Kinase Calmodulin Target Site. Journal of Biological Chemistry. 274(26). 18161–18164. 35 indexed citations

Schulga, Alexey, Fuat Kurbanov, М. П. Кирпичников, et al.. (1998). Comparative study of binase and barnase: experience in chimeric ribonucleases. Protein Engineering Design and Selection. 11(9). 775–782. 43 indexed citations

10.

Garnier, Cyrille, Irina I. Protasevich, Robert Gilli, et al.. (1998). The Two-Stage Process of the Heat Shock Protein 90 Thermal Denaturation: Effect of Calcium and Magnesium. Biochemical and Biophysical Research Communications. 249(1). 197–201. 20 indexed citations

11.

Dolla, Alain, Pascal Arnoux, Irina I. Protasevich, et al.. (1998). Key Role of Phenylalanine 20 in Cytochrome c₃: Structure, Stability, and Function Studies. Biochemistry. 38(1). 33–41. 22 indexed citations

12.

Protasevich, Irina I., et al.. (1995). Thermal Denaturation of Bacterial and Bovine Dihydrofolate Reductases and their Complexes with NADPH, Trimethoprim and Methotrexate. Journal of Biomolecular Structure and Dynamics. 12(5). 1023–1032. 13 indexed citations

13.

Florens, Laurence, P. Bianco, Jean Haladjian, et al.. (1995). Thermal stability of the polyheme cytochrome c₃ superfamily. FEBS Letters. 373(3). 280–284. 12 indexed citations

14.

Makarov, Alexander, et al.. (1995). Heat denaturation of pepsinogen in a water‐ethanol mixture. FEBS Letters. 357(1). 58–61. 10 indexed citations

15.

Makarov, Alexander А., Ivan Adzhubei, Irina I. Protasevich, Vladimir M. Lobachov, & Gerald D. Fasman. (1994). Melting of the left‐handed helical conformation of charged poly‐L‐lysine. Biopolymers. 34(8). 1123–1124. 11 indexed citations

16.

Makarov, Alexander А., Irina I. Protasevich, Vladimir M. Lobachov, et al.. (1994). Thermostability of the barnase—barstar complex. FEBS Letters. 354(3). 251–254. 13 indexed citations

17.

Makarov, Alexander, Ivan Adzhubei, Irina I. Protasevich, Vladimir M. Lobachov, & Esipova Ng. (1993). Scanning microcalorimetry and circular dichroism study of melting of the natural polypeptides in the left-handed helical conformation. Journal of Protein Chemistry. 12(1). 85–91. 15 indexed citations

18.

Makarov, Alexander, Irina I. Protasevich, Sergey Korolev, et al.. (1993). Comparative Study of Thermostability and Structure of Close Homologues - Barnase and Binase. Journal of Biomolecular Structure and Dynamics. 10(6). 1047–1065. 33 indexed citations

19.

Makarov, Alexander, et al.. (1991). The number of cooperative regions (energetic domains) in a pepsin molecule depends on the pH of the medium. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1078(2). 283–288. 13 indexed citations

20.

Protasevich, Irina I., et al.. (1987). Distribution of Charges inBacillus intermedins 7PRibonuclease Determines the Number of Cooperatively Melting Regions of the Globule. Journal of Biomolecular Structure and Dynamics. 4(5). 885–893. 11 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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