Jukka Kervinen

1.8k total citations
45 papers, 1.5k citations indexed

About

Jukka Kervinen is a scholar working on Molecular Biology, Immunology and Immunology and Allergy. According to data from OpenAlex, Jukka Kervinen has authored 45 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 13 papers in Immunology and 11 papers in Immunology and Allergy. Recurrent topics in Jukka Kervinen's work include Mast cells and histamine (12 papers), Food Allergy and Anaphylaxis Research (10 papers) and Phytase and its Applications (8 papers). Jukka Kervinen is often cited by papers focused on Mast cells and histamine (12 papers), Food Allergy and Anaphylaxis Research (10 papers) and Phytase and its Applications (8 papers). Jukka Kervinen collaborates with scholars based in United States, Finland and Sweden. Jukka Kervinen's co-authors include Alexander Wlodawer, Alexander Zdanov, Eileen K. Jaffe, Júlia Costa, Gregory J. Tobin, Jacob Martins, Nisse Kalkkinen, Pia Runeberg‐Roos, Roland L. Dunbrack and Lawrence de Garavilla and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and SHILAP Revista de lepidopterología.

In The Last Decade

Jukka Kervinen

41 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jukka Kervinen United States 22 870 370 286 191 116 45 1.5k
Olga V. Moroz United Kingdom 21 1.3k 1.5× 199 0.5× 196 0.7× 190 1.0× 113 1.0× 52 1.8k
Alexander E. Aleshin United States 28 1.3k 1.4× 179 0.5× 615 2.2× 178 0.9× 236 2.0× 53 2.5k
Sujata Sharma India 26 1.2k 1.4× 171 0.5× 161 0.6× 358 1.9× 174 1.5× 100 2.1k
Dale T. Blankenship United States 21 997 1.1× 92 0.2× 109 0.4× 144 0.8× 58 0.5× 26 1.8k
Shuichi Kusano Japan 26 1.1k 1.3× 126 0.3× 93 0.3× 346 1.8× 107 0.9× 78 2.1k
Dominique Boivin Canada 20 1.1k 1.3× 159 0.4× 93 0.3× 177 0.9× 80 0.7× 37 1.8k
Rodrigo V. Honorato Brazil 18 1.0k 1.2× 143 0.4× 148 0.5× 108 0.6× 113 1.0× 36 1.6k
Noriyuki Habuka Japan 20 1.3k 1.4× 252 0.7× 296 1.0× 412 2.2× 296 2.6× 36 2.5k
Andrew Binkowski United States 4 1.2k 1.4× 146 0.4× 86 0.3× 93 0.5× 174 1.5× 4 1.8k
Jean‐Michel Bruneau France 15 602 0.7× 217 0.6× 55 0.2× 162 0.8× 251 2.2× 19 1.3k

Countries citing papers authored by Jukka Kervinen

Since Specialization
Citations

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

Fields of papers citing papers by Jukka Kervinen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jukka Kervinen

This figure shows the co-authorship network connecting the top 25 collaborators of Jukka Kervinen. A scholar is included among the top collaborators of Jukka Kervinen 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 Jukka Kervinen. Jukka Kervinen 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.
Li, Tianyu, et al.. (2025). Preparative choline-based anion-exchange chromatography for enrichment of full adeno-associated virus capsids. Journal of Chromatography A. 1760. 466319–466319.
2.
Li, Tianyu, et al.. (2023). Separation of full and empty adeno-associated virus capsids by anion-exchange chromatography using choline-type salts. Analytical Biochemistry. 686. 115421–115421. 19 indexed citations
3.
Fu, Zhirong, Srinivas Akula, Chang Qiao, et al.. (2021). Duodenases are a small subfamily of ruminant intestinal serine proteases that have undergone a remarkable diversification in cleavage specificity. PLoS ONE. 16(5). e0252624–e0252624. 6 indexed citations
4.
Akula, Srinivas, Zhirong Fu, Lawrence de Garavilla, et al.. (2019). Extended Cleavage Specificities of Rabbit and Guinea Pig Mast Cell Chymases: Two Highly Specific Leu-Ases. International Journal of Molecular Sciences. 20(24). 6340–6340. 8 indexed citations
5.
Kettunen, Kimmo, et al.. (2018). Creating and using ground truth OCR sample data for Finnish historical newspapers and journals. SHILAP Revista de lepidopterología. 1(1). 162–169. 5 indexed citations
6.
Fu, Zhirong, Srinivas Akula, Michael Thorpe, et al.. (2018). Extended cleavage specificity of sheep mast cell protease-2: A classical chymase with preference to aromatic P1 substrate residues. Developmental & Comparative Immunology. 92. 160–169. 4 indexed citations
7.
Thorpe, Michael, Zhirong Fu, Srinivas Akula, et al.. (2018). Extended cleavage specificities of mast cell proteases 1 and 2 from golden hamster: Classical chymase and an elastolytic protease comparable to rat and mouse MCP-5. PLoS ONE. 13(12). e0207826–e0207826. 9 indexed citations
8.
Thorpe, Michael, Zhirong Fu, Srinivas Akula, et al.. (2018). Extended cleavage specificity of human neutrophil cathepsin G: A low activity protease with dual chymase and tryptase-type specificities. PLoS ONE. 13(4). e0195077–e0195077. 32 indexed citations
9.
Fu, Zhirong, Michael Thorpe, Ananya Roy, et al.. (2017). Highly Selective Cleavage of Cytokines and Chemokines by the Human Mast Cell Chymase and Neutrophil Cathepsin G. The Journal of Immunology. 198(4). 1474–1483. 61 indexed citations
10.
Kervinen, Jukka, et al.. (2016). Historiallisten digitoitujen sanoma- ja aikakauslehtien avaaminen avoimena datana tutkijoille. SHILAP Revista de lepidopterología.
11.
Kervinen, Jukka, Carl Crysler, Shariff Bayoumy, et al.. (2010). Potency variation of small-molecule chymase inhibitors across species. Biochemical Pharmacology. 80(7). 1033–1041. 21 indexed citations
12.
Breinig, Sabine, Jukka Kervinen, Linda Stith, et al.. (2003). Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase. Nature Structural & Molecular Biology. 10(9). 757–763. 90 indexed citations
13.
Jaffe, Eileen K., Jacob Martins, Jian Li, Jukka Kervinen, & Roland L. Dunbrack. (2001). The Molecular Mechanism of Lead Inhibition of Human Porphobilinogen Synthase. Journal of Biological Chemistry. 276(2). 1531–1537. 87 indexed citations
14.
Kervinen, Jukka, J. Łubkowski, Alexander Zdanov, et al.. (1998). Toward a universal inhibitor of retroviral proteases: Comparative analysis of the interactions of LP‐130 complexed with proteases from HIV‐1, FIV, and EIAV. Protein Science. 7(11). 2314–2323. 25 indexed citations
15.
Wlodawer, Alexander, Jukka Kervinen, Narmada Thanki, et al.. (1996). Structural Analysis of the Native and Drug Resistant HIV-1 Proteinases Complexed With an Aminodiol Inhibitor. Protein and Peptide Letters. 3(6). 399–406. 16 indexed citations
16.
Kervinen, Jukka, Kirsi Törmäkangas, Pia Runeberg‐Roos, et al.. (1995). Structure and Possible Function of Aspartic Proteinases in Barley and other Plants. Advances in experimental medicine and biology. 362. 241–254. 21 indexed citations
17.
Runeberg‐Roos, Pia, Jukka Kervinen, Valentina Kovaleva, Natasha V. Raikhel, & Susannah Gal. (1994). The Aspartic Proteinase of Barley Is a Vacuolar Enzyme That Processes Probarley Lectin in Vitro. PLANT PHYSIOLOGY. 105(1). 321–329. 105 indexed citations
18.
Guruprasad, Kunchur, Kirsi Törmäkangas, Jukka Kervinen, & Tom L. Blundell. (1994). Comparative modelling of barley‐grain aspartic proteinase: A structural rationale for observed hydrolytic specificity. FEBS Letters. 352(2). 131–136. 74 indexed citations
19.
Törmäkangas, Kirsi, Pia Runeberg‐Roos, Arne Östman, et al.. (1991). Aspartic Proteinase from Barley Seeds is Related to Animal Cathepsin D. Advances in experimental medicine and biology. 306. 355–359. 7 indexed citations
20.
Kervinen, Jukka, Markku Kontturi, & Juhani Mikola. (1990). Changes in the proteinase composition of barley leaves during senescence in field conditions. Cereal Research Communications. 18(3). 191–197. 13 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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