Jane W. Agger

2.6k total citations
49 papers, 2.0k citations indexed

About

Jane W. Agger is a scholar working on Biomedical Engineering, Biotechnology and Molecular Biology. According to data from OpenAlex, Jane W. Agger has authored 49 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Biomedical Engineering, 25 papers in Biotechnology and 23 papers in Molecular Biology. Recurrent topics in Jane W. Agger's work include Biofuel production and bioconversion (30 papers), Enzyme Production and Characterization (20 papers) and Enzyme-mediated dye degradation (14 papers). Jane W. Agger is often cited by papers focused on Biofuel production and bioconversion (30 papers), Enzyme Production and Characterization (20 papers) and Enzyme-mediated dye degradation (14 papers). Jane W. Agger collaborates with scholars based in Denmark, Norway and Netherlands. Jane W. Agger's co-authors include Vincent G. H. Eijsink, Bjørge Westereng, Anne S. Meyer, Svein Jarle Horn, Roland Ludwig, Finn L. Aachmann, Anikó Várnai, William G. T. Willats, Jesper Holck and Silvia Vidal‐Melgosa and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Jane W. Agger

47 papers receiving 2.0k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Jane W. Agger Denmark	22	1.4k	877	853	724	249	49	2.0k
Gashaw Mamo Sweden	23	863 0.6×	361 0.4×	947 1.1×	769 1.1×	98 0.4×	41	1.7k
Ken K. Y. Wong Canada	23	1.8k 1.3×	745 0.8×	1.1k 1.3×	1.2k 1.7×	260 1.0×	50	2.5k
P. Prema India	28	1.4k 1.0×	768 0.9×	1.1k 1.3×	1.5k 2.0×	185 0.7×	63	2.8k
Edivaldo Ximenes Ferreira Filho Brazil	32	2.1k 1.5×	924 1.1×	1.6k 1.9×	1.7k 2.3×	206 0.8×	96	3.2k
Caroline Rémond France	25	935 0.7×	319 0.4×	590 0.7×	533 0.7×	218 0.9×	71	1.6k
Harald J. Ruijssenaars Netherlands	22	1.0k 0.7×	445 0.5×	1.2k 1.4×	423 0.6×	113 0.5×	33	2.0k
Irina Kataeva United States	22	1.4k 1.0×	353 0.4×	1.2k 1.4×	939 1.3×	222 0.9×	31	2.0k
Brenna A. Black United States	23	1.2k 0.9×	296 0.3×	794 0.9×	376 0.5×	197 0.8×	29	1.8k
Bastien Bissaro France	30	1.9k 1.4×	1.5k 1.7×	1.6k 1.9×	1.2k 1.7×	247 1.0×	55	3.2k
D. Kekos Greece	26	1.3k 1.0×	374 0.4×	1.1k 1.3×	813 1.1×	117 0.5×	60	2.1k

Countries citing papers authored by Jane W. Agger

Since Specialization

Citations

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

Fields of papers citing papers by Jane W. Agger

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jane W. Agger. 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 Jane W. Agger. The network helps show where Jane W. Agger may publish in the future.

Co-authorship network of co-authors of Jane W. Agger

This figure shows the co-authorship network connecting the top 25 collaborators of Jane W. Agger. A scholar is included among the top collaborators of Jane W. Agger 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 Jane W. Agger. Jane W. Agger 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

Luterbacher, Jeremy S., et al.. (2025). Glucuronoyl esterases improve cellulose hydrolysis by lignocellulose degrading enzymes and enhance lignin extraction. International Journal of Biological Macromolecules. 314. 144218–144218. 2 indexed citations

Barrett, Kristian, Mark Sanders, Willem J. H. van Berkel, et al.. (2024). Polyphenol Oxidase Activity on Guaiacyl and Syringyl Lignin Units. Angewandte Chemie International Edition. 63(48). e202409324–e202409324. 8 indexed citations

Barrett, Kristian, Mark Sanders, Willem J. H. van Berkel, et al.. (2024). Polyphenol Oxidase Activity on Guaiacyl and Syringyl Lignin Units. Angewandte Chemie. 136(48). 6 indexed citations

Lin, Shang, Jesper Holck, Jane W. Agger, et al.. (2023). Soluble, Diferuloylated Corn Bran Glucuronoarabinoxylans Modulate the Human Gut Microbiota In Vitro. Journal of Agricultural and Food Chemistry. 71(8). 3885–3897. 9 indexed citations

Vuillemin, M. Paul, et al.. (2023). Polyphenol Oxidase Products Are Priming Agents for LPMO Peroxygenase Activity. ChemSusChem. 16(18). e202300559–e202300559. 10 indexed citations

Westereng, Bjørge, Magnus Ø. Arntzen, Heidi Østby, et al.. (2023). Analyzing Activities of Lytic Polysaccharide Monooxygenases by Liquid Chromatography and Mass Spectrometry. Methods in molecular biology. 2657. 27–51. 1 indexed citations

Lin, Shang, Jesper Brask, Line Munk, et al.. (2022). Enzymatic Cleavage of Diferuloyl Cross-Links in Corn Bran Arabinoxylan by Two Bacterial Feruloyl Esterases. Journal of Agricultural and Food Chemistry. 70(41). 13349–13357. 9 indexed citations

Agger, Jane W. & Birgitte Zeuner. (2022). Bio-based surfactants: enzymatic functionalization and production from renewable resources. Current Opinion in Biotechnology. 78. 102842–102842. 16 indexed citations

Agger, Jane W., et al.. (2019). Laccase Induced Lignin Radical Formation Kinetics Evaluated by Electron Paramagnetic Resonance Spectroscopy. ACS Sustainable Chemistry & Engineering. 7(12). 10425–10434. 22 indexed citations

10.

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

11.

Liu, Zhanliang, Laurie M. Gay, Tina R. Tuveng, et al.. (2017). Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4. Scientific Reports. 7(1). 1746–1746. 60 indexed citations

12.

Westereng, Bjørge, Magnus Ø. Arntzen, Jane W. Agger, Gustav Vaaje‐Kolstad, & Vincent G. H. Eijsink. (2017). Analyzing Activities of Lytic Polysaccharide Monooxygenases by Liquid Chromatography and Mass Spectrometry. Methods in molecular biology. 1588. 71–92. 25 indexed citations

13.

Agger, Jane W., et al.. (2017). A comparative study on the activity of fungal lytic polysaccharide monooxygenases for the depolymerization of cellulose in soybean spent flakes. Carbohydrate Research. 449. 85–94. 17 indexed citations

14.

Agger, Jane W., Peter Kamp Busk, Bo Pilgaard, Anne S. Meyer, & Lene Lange. (2017). A New Functional Classification of Glucuronoyl Esterases by Peptide Pattern Recognition. Frontiers in Microbiology. 8. 309–309. 19 indexed citations

15.

Westereng, Bjørge, Magnus Ø. Arntzen, Finn L. Aachmann, et al.. (2016). Simultaneous analysis of C1 and C4 oxidized oligosaccharides, the products of lytic polysaccharide monooxygenases acting on cellulose. Journal of Chromatography A. 1445. 46–54. 83 indexed citations

16.

Mathiesen, Geir, Alasdair Mackenzie, Jane W. Agger, et al.. (2016). Display of a β-mannanase and a chitosanase on the cell surface of Lactobacillus plantarum towards the development of whole-cell biocatalysts. Microbial Cell Factories. 15(1). 169–169. 28 indexed citations

17.

Puchart, Vladimı́r, Jane W. Agger, Jean‐Guy Berrin, et al.. (2016). Comparison of fungal carbohydrate esterases of family CE16 on artificial and natural substrates. Journal of Biotechnology. 233. 228–236. 21 indexed citations

18.

Bauer, Alexander, Javier Lizasoain, Franz Theuretzbacher, et al.. (2014). Steam explosion pretreatment for enhancing biogas production of late harvested hay. Bioresource Technology. 166. 403–410. 95 indexed citations

19.

Agger, Jane W., Katja S. Johansen, & Anne S. Meyer. (2010). pH catalyzed pretreatment of corn bran for enhanced enzymatic arabinoxylan degradation. New Biotechnology. 28(2). 125–135. 15 indexed citations

20.

Agger, Jane W., Anders Viksø‐Nielsen, & Anne S. Meyer. (2010). Enzymatic Xylose Release from Pretreated Corn Bran Arabinoxylan: Differential Effects of Deacetylation and Deferuloylation on Insoluble and Soluble Substrate Fractions. Journal of Agricultural and Food Chemistry. 58(10). 6141–6148. 106 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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