Igor Polikarpov
About
Igor Polikarpov is a scholar working on Molecular Biology, Biomedical Engineering and Biotechnology.
According to data from OpenAlex, Igor Polikarpov has authored 333 papers receiving a total of 10.5k indexed citations (citations by other indexed papers that have themselves been cited), including 156 papers in Molecular Biology, 122 papers in Biomedical Engineering and 91 papers in Biotechnology. Recurrent topics in Igor Polikarpov's work include Biofuel production and bioconversion (116 papers), Enzyme Production and Characterization (87 papers) and Enzyme Structure and Function (52 papers). Igor Polikarpov is often cited by papers focused on Biofuel production and bioconversion (116 papers), Enzyme Production and Characterization (87 papers) and Enzyme Structure and Function (52 papers). Igor Polikarpov collaborates with scholars based in Brazil, United States and United Kingdom. Igor Polikarpov's co-authors include A. F. Craievich, Hannes Fischer, Camila A. Rezende, Munir S. Skaf, Eduardo R. deAzevedo, Mário de Oliveira Neto, Lindsay Sawyer, Alessandro S. Nascimento, Paul Webb and Sharon Brownlow 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
Igor Polikarpov
325 papers receiving 10.4k citations
Hit Papers
Peers — A (Enhanced Table)
Peers by citation overlap · career bar shows stage (early→late) cites · hero ref
| Name | h | Career | Trend | Papers | Cites | |||||
|---|---|---|---|---|---|---|---|---|---|---|
| Igor Polikarpov Brazil | 52 | 5.1k | 3.1k | 1.9k | 1.3k | 1.0k | 333 | 10.5k | ||
| Mario De Rosa Italy | 55 | 6.4k 1.3× | 1.0k 0.3× | 1.1k 0.6× | 648 0.5× | 1.2k 1.1× | 321 | 11.9k | ||
| Jesús Jiménez‐Barbero Spain | 71 | 13.1k 2.6× | 2.7k 0.9× | 1.8k 1.0× | 2.3k 1.7× | 1.4k 1.4× | 670 | 20.9k | ||
| Peng George Wang United States | 58 | 8.7k 1.7× | 1.3k 0.4× | 1.1k 0.6× | 547 0.4× | 1.1k 1.1× | 511 | 15.7k | ||
| José L. Garcı́a Spain | 63 | 7.7k 1.5× | 1.5k 0.5× | 1.2k 0.6× | 875 0.7× | 911 0.9× | 339 | 12.7k | ||
| Lars K. Nielsen Australia | 63 | 9.7k 1.9× | 4.0k 1.3× | 756 0.4× | 787 0.6× | 359 0.4× | 297 | 13.8k | ||
| Fuming Zhang United States | 62 | 6.4k 1.2× | 1.1k 0.4× | 530 0.3× | 1.5k 1.1× | 609 0.6× | 437 | 14.0k | ||
| Karl‐Erich Jaeger Germany | 65 | 14.0k 2.7× | 2.8k 0.9× | 1.9k 1.0× | 1.4k 1.1× | 1.1k 1.1× | 327 | 17.9k | ||
| Alois Jungbauer Austria | 59 | 8.0k 1.6× | 2.7k 0.9× | 445 0.2× | 612 0.5× | 712 0.7× | 389 | 12.7k | ||
| Michael L. Shuler United States | 68 | 7.2k 1.4× | 9.0k 2.9× | 1.3k 0.7× | 922 0.7× | 518 0.5× | 335 | 18.7k | ||
| Tadayuki Imanaka Japan | 58 | 8.4k 1.7× | 1.5k 0.5× | 2.6k 1.4× | 1.3k 1.0× | 2.3k 2.2× | 382 | 12.1k |
Countries citing papers authored by Igor Polikarpov
Since
Specialization
Citations
This map shows the geographic impact of Igor Polikarpov'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 Igor Polikarpov with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Igor Polikarpov more than expected).
Fields of papers citing papers by Igor Polikarpov
Since
Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences
This network shows the impact of papers produced by Igor Polikarpov. 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 Igor Polikarpov. The network helps show where Igor Polikarpov may publish in the future.
Co-authorship network of co-authors of Igor Polikarpov
This figure shows the co-authorship network connecting the top 25 collaborators of Igor Polikarpov. A scholar is included among the top collaborators of Igor Polikarpov 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 Igor Polikarpov. Igor Polikarpov is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
1.
Polikarpov, Igor, et al.. (2025). Bio-engineered silver nanoparticles suppress flic-mediated motility and induce argI-driven metabolic rewiring in Escherichia coli. Biocatalysis and Agricultural Biotechnology. 68. 103712–103712.
2.
Liberato, M.V., et al.. (2025). Recombinant GH5_8 mannanase from Hungateiclostridium cellulolyticum: Biochemical and structural characteristics and applications for mannooligosaccharides production from spent coffee grounds. Food and Bioproducts Processing. 151. 44–53.
3.
Ngom, B.D., et al.. (2025). Green Synthesis of ZnO Nanoparticles Using Licania tomentosa Benth (Oiti) Leaf Extract: Characterization and Applications for the Photocatalytic Degradation of Crystal Violet Dye. Processes. 13(3). 880–880.
4.
Godoy, André S., et al.. (2024). Structures of Bl Est2 from Bacillus licheniformis in its propeptide and mature forms reveal autoinhibitory effects of the C ‐terminal domain. FEBS Journal. 291(22). 4930–4950.
5.
Pratavieira, Sebastião, Luís Antônio Esmerino, Mário de Oliveira Neto, et al.. (2024). Thermothelomyces thermophilus exo- and endo-glucanases as tools for pathogenic E. coli biofilm degradation. Scientific Reports. 14(1). 22576–22576.
6.
Peixoto, Guilherme, Gustavo Mockaitis, Daniel Moureira Fontes Lima, et al.. (2023). Acidogenesis of Pentose Liquor to Produce Biohydrogen and Organic Acids Integrated with 1G–2G Ethanol Production in Sugarcane Biorefineries. SHILAP Revista de lepidopterología. 1(3). 672–688.
7.
Oliva, Bianca, B. Alves Franca, Thiago Augusto Gonçalves, et al.. (2020). Functional characterization of a novel thermophilic exo-arabinanase from Thermothielavioides terrestris. Applied Microbiology and Biotechnology. 104(19). 8309–8326.
8.
Sonoda, Milton T., André S. Godoy, Vanessa O.A. Pellegrini, et al.. (2019). Structure and dynamics of Trichoderma harzianum Cel7B suggest molecular architecture adaptations required for a wide spectrum of activities on plant cell wall polysaccharides. Biochimica et Biophysica Acta (BBA) - General Subjects. 1863(6). 1015–1026.
9.
Araújo, Evandro Ares de, Mário de Oliveira Neto, & Igor Polikarpov. (2018). Biochemical characterization and low-resolution SAXS structure of two-domain endoglucanase BlCel9 from Bacillus licheniformis. Applied Microbiology and Biotechnology. 103(3). 1275–1287.
10.
Kadowaki, Marco Antônio Seiki, et al.. (2017). Biochemical and structural insights into a thermostable cellobiohydrolase from Myceliophthora thermophila. FEBS Journal. 285(3). 559–579.
11.
Souza, Paulo C. T., Ana C. Puhl, Leandro Martı́nez, et al.. (2014). Identification of a New Hormone-Binding Site on the Surface of Thyroid Hormone Receptor. Molecular Endocrinology. 28(4). 534–545.
12.
Camilo, César M. & Igor Polikarpov. (2014). High-throughput cloning, expression and purification of glycoside hydrolases using Ligation-Independent Cloning (LIC). Protein Expression and Purification. 99. 35–42.
13.
Mafud, Ana Carolina, et al.. (2013). Structure-based identification of novel PPAR gamma ligands. Bioorganic & Medicinal Chemistry Letters. 23(21). 5795–5802.
14.
Pereira‐Filho, Edenir Rodrigues, Maria Fátima das Graças Fernandes da Silva, João Batista Fernandes, et al.. (2012). Poly-ε-caprolactone nanoparticles loaded with hydrocortisone: preparation using factorial design and evaluation. SHILAP Revista de lepidopterología. 4(2). 54–76.
15.
Puhl, Ana C., Igor Polikarpov, María de Fátima, et al.. (2012). Preparation and characterization of polymeric nanoparticles loaded with the flavonoid luteolin, by using factorial design. International Journal of Phytomedicine. 3(4). 683–698.
16.
Rezende, Camila A., et al.. (2011). Chemical and morphological characterization of sugarcane bagasse submitted to a delignification process for enhanced enzymatic digestibility. Biotechnology for Biofuels. 4(1). 54–54.
17.
Golubev, Alexander M., Adriana L. Rojas, Alessandro S. Nascimento, et al.. (2008). Crystallization and Preliminary Crystallographic Analysis of Laminarinase from Rhodothermus marinus: A Case of Pseudomerohedral Twinning. Protein and Peptide Letters. 15(10). 1142–1144.
18.
Valadares, Napoleão Fonseca, Marcelo S. Castilho, Igor Polikarpov, & Richard Charles Garratt. (2007). 2D QSAR studies on thyroid hormone receptor ligands. Bioorganic & Medicinal Chemistry. 15(13). 4609–4617.
19.
Polikarpov, Igor, et al.. (1999). Stability of l-asparaginase: an enzyme used in leukemia treatment. Pharmaceutica Acta Helvetiae. 74(1). 1–9.
20.
Isupov, Michail N., G. Obmolova, Marie‐Ange Badet‐Denisot, et al.. (1996). Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 å crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase. Structure. 4(7). 801–810.
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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