Per Berglund

4.8k total citations
82 papers, 3.9k citations indexed

About

Per Berglund is a scholar working on Molecular Biology, Organic Chemistry and Spectroscopy. According to data from OpenAlex, Per Berglund has authored 82 papers receiving a total of 3.9k indexed citations (citations by other indexed papers that have themselves been cited), including 66 papers in Molecular Biology, 20 papers in Organic Chemistry and 18 papers in Spectroscopy. Recurrent topics in Per Berglund's work include Enzyme Catalysis and Immobilization (59 papers), Microbial Metabolic Engineering and Bioproduction (21 papers) and Analytical Chemistry and Chromatography (17 papers). Per Berglund is often cited by papers focused on Enzyme Catalysis and Immobilization (59 papers), Microbial Metabolic Engineering and Bioproduction (21 papers) and Analytical Chemistry and Chromatography (17 papers). Per Berglund collaborates with scholars based in Sweden, Germany and Italy. Per Berglund's co-authors include Karl Hult, Maria Svedendahl Humble, Fei Guo, Cecilia Branneby, Henrik Land, Tore Brinck, Peter Carlqvist, Karim Engelmark Cassimjee, Mats Holmquist and Uwe T. Bornscheuer and has published in prestigious journals such as Journal of the American Chemical Society, Angewandte Chemie International Edition and Biochemistry.

In The Last Decade

Per Berglund

78 papers receiving 3.8k citations

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Per Berglund 3.3k 1.3k 539 533 435 82 3.9k
Herfried Griengl 3.3k 1.0× 2.0k 1.5× 450 0.8× 557 1.0× 328 0.8× 197 4.7k
Paul N. Devine 2.3k 0.7× 1.5k 1.1× 295 0.5× 191 0.4× 730 1.7× 55 3.4k
Dominik Koszelewski 1.9k 0.6× 1.4k 1.0× 426 0.8× 148 0.3× 340 0.8× 96 2.8k
Stanley M. Roberts 3.6k 1.1× 4.4k 3.3× 552 1.0× 639 1.2× 557 1.3× 380 7.3k
Shô Itô 1.5k 0.4× 2.4k 1.8× 533 1.0× 286 0.5× 228 0.5× 273 3.9k
Jun’ichi Oda 1.5k 0.4× 1.0k 0.8× 340 0.6× 401 0.8× 108 0.2× 146 2.6k
Sybille Franken 1.8k 0.6× 489 0.4× 651 1.2× 373 0.7× 176 0.4× 33 2.8k
Vytas K. Švedas 2.2k 0.7× 782 0.6× 359 0.7× 291 0.5× 316 0.7× 150 2.8k
Ignacio Alfonso 2.2k 0.7× 2.2k 1.7× 650 1.2× 1.4k 2.7× 252 0.6× 154 4.2k
Ari M. P. Koskinen 1.5k 0.5× 3.1k 2.4× 273 0.5× 266 0.5× 197 0.5× 190 4.1k

Countries citing papers authored by Per Berglund

Since Specialization
Citations

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

Fields of papers citing papers by Per Berglund

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Per Berglund

This figure shows the co-authorship network connecting the top 25 collaborators of Per Berglund. A scholar is included among the top collaborators of Per Berglund 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 Per Berglund. Per Berglund 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.
Gautom, Trishnamoni, et al.. (2025). Exploring the Stability and Substrate Profile of Transaminase from Silicibacter pomeroyi with Ancestral Sequence Reconstruction. ChemBioChem. 26(13). e202500155–e202500155. 1 indexed citations
2.
Höhne, Matthias, et al.. (2023). Biosynthesis of Furfurylamines in Batch and Continuous Flow by Immobilized Amine Transaminases. Catalysts. 13(5). 875–875. 9 indexed citations
3.
Gumaelius, Lena, et al.. (2022). Leadership, support and organisation for academics’ participation in engineering education change for sustainable development. European Journal of Engineering Education. 48(2). 240–266. 6 indexed citations
4.
Sheludko, Y. V., et al.. (2022). Enantioselective Synthesis of Pharmaceutically Relevant Bulky Arylbutylamines Using Engineered Transaminases. Advanced Synthesis & Catalysis. 364(17). 2972–2981. 8 indexed citations
5.
Kretschmer, Martin, Rafael Ceña‐Diez, Illia Dobryden, et al.. (2022). Synthetic Mucin Gels with Self‐Healing Properties Augment Lubricity and Inhibit HIV‐1 and HSV‐2 Transmission. Advanced Science. 9(32). e2203898–e2203898. 12 indexed citations
6.
Langen, Luuk M. van, et al.. (2022). The Role of Buffer, Pyridoxal 5’‐Phosphate and Light on the Stability of the Silicibacter Pomeroyi Transaminase. ChemCatChem. 15(2). 6 indexed citations
7.
Fiorati, Andrea, Per Berglund, Maria Svedendahl Humble, & Davide Tessaro. (2020). Application of Transaminases in a Disperse System for the Bioamination of Hydrophobic Substrates. Advanced Synthesis & Catalysis. 362(5). 1156–1166. 10 indexed citations
8.
9.
Marx, Lisa, et al.. (2019). Chemoenzymatic Synthesis of Sertraline. European Journal of Organic Chemistry. 2020(4). 510–513. 14 indexed citations
10.
Langen, Luuk M. van, et al.. (2018). Transaminase‐Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions. ChemCatChem. 10(21). 5012–5018. 11 indexed citations
11.
Chen, Shan, et al.. (2018). Characterization of the stability of Vibrio fluvialis JS17 amine transaminase. Journal of Biotechnology. 282. 10–17. 17 indexed citations
12.
Guo, Fei & Per Berglund. (2016). Transaminase biocatalysis: optimization and application. Green Chemistry. 19(2). 333–360. 372 indexed citations
13.
Steffen‐Munsberg, Fabian, Clare Vickers, Henrik Land, et al.. (2015). Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications. Biotechnology Advances. 33(5). 566–604. 199 indexed citations
14.
Cooney, Jakki C., Fathima Laffir, Karim Engelmark Cassimjee, et al.. (2014). Preparation and characterisation of a Ni2+/Co2+-cyclam modified mesoporous cellular foam for the specific immobilisation of His6-alanine racemase. Journal of Molecular Catalysis B Enzymatic. 109. 154–160. 11 indexed citations
15.
Humble, Maria Svedendahl, Karim Engelmark Cassimjee, M. Håkansson, et al.. (2012). Crystal structures of the Chromobacterium violaceumω‐transaminase reveal major structural rearrangements upon binding of coenzyme PLP. FEBS Journal. 279(5). 779–792. 105 indexed citations
16.
17.
Humble, Maria Svedendahl, Peter Carlqvist, Cecilia Branneby, et al.. (2008). Direct Epoxidation in Candida antarctica Lipase B Studied by Experiment and Theory. ChemBioChem. 9(15). 2443–2451. 62 indexed citations
18.
Hult, Karl & Per Berglund. (2007). Enzyme promiscuity: mechanism and applications. Trends in biotechnology. 25(5). 231–238. 486 indexed citations
19.
Hult, Karl & Per Berglund. (2003). Engineered enzymes for improved organic synthesis. Current Opinion in Biotechnology. 14(4). 395–400. 101 indexed citations
20.
Berglund, Per. (2001). Controlling lipase enantioselectivity for organic synthesis. Biomolecular Engineering. 18(1). 13–22. 110 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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