Åsmund K. Røhr

4.0k total citations · 1 hit paper
58 papers, 3.0k citations indexed

About

Åsmund K. Røhr is a scholar working on Molecular Biology, Plant Science and Biomedical Engineering. According to data from OpenAlex, Åsmund K. Røhr has authored 58 papers receiving a total of 3.0k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 17 papers in Plant Science and 17 papers in Biomedical Engineering. Recurrent topics in Åsmund K. Røhr's work include Biofuel production and bioconversion (17 papers), Metal-Catalyzed Oxygenation Mechanisms (16 papers) and Enzyme-mediated dye degradation (12 papers). Åsmund K. Røhr is often cited by papers focused on Biofuel production and bioconversion (17 papers), Metal-Catalyzed Oxygenation Mechanisms (16 papers) and Enzyme-mediated dye degradation (12 papers). Åsmund K. Røhr collaborates with scholars based in Norway, United States and France. Åsmund K. Røhr's co-authors include Vincent G. H. Eijsink, Bastien Bissaro, Zarah Forsberg, Morten Sørlie, Gustav Vaaje‐Kolstad, Anikó Várnai, K. Kristoffer Andersson, Piotr Chylenski, Svein Jarle Horn and Sophanit Mekasha and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Åsmund K. Røhr

53 papers receiving 3.0k citations

Hit Papers

Oxidative cleavage of polysaccharides by monocopper enzym... 2017 2026 2020 2023 2017 100 200 300 400

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Åsmund K. Røhr Norway 26 1.6k 1.5k 1.1k 904 471 58 3.0k
G.R. Hemsworth United Kingdom 21 1.2k 0.8× 1.5k 1.0× 827 0.7× 878 1.0× 258 0.5× 35 2.6k
Zarah Forsberg Norway 27 2.1k 1.3× 1.5k 1.0× 1.3k 1.2× 1.2k 1.4× 283 0.6× 45 3.0k
Leila Lo Leggio Denmark 34 2.5k 1.6× 3.9k 2.6× 3.1k 2.8× 2.1k 2.3× 267 0.6× 119 6.5k
Theodora Tryfona United Kingdom 28 1.8k 1.2× 1.7k 1.2× 2.2k 2.0× 941 1.0× 142 0.3× 48 3.8k
Zui Fujimoto Japan 34 700 0.4× 1.5k 1.0× 707 0.6× 1.3k 1.4× 207 0.4× 120 3.0k
Anu Koivula Finland 39 2.8k 1.8× 2.5k 1.7× 1.4k 1.3× 1.9k 2.1× 145 0.3× 98 4.8k
Yingang Feng China 30 760 0.5× 2.0k 1.3× 230 0.2× 330 0.4× 117 0.2× 155 3.0k
Markku Saloheimo Finland 45 2.7k 1.7× 3.8k 2.6× 2.1k 1.9× 2.4k 2.6× 96 0.2× 110 6.0k
Wataru Ogasawara Japan 26 1.1k 0.7× 1.2k 0.8× 238 0.2× 541 0.6× 105 0.2× 89 2.0k
Joel R. Cherry United States 19 1.7k 1.1× 2.3k 1.5× 1.0k 0.9× 1.1k 1.2× 64 0.1× 29 3.3k

Countries citing papers authored by Åsmund K. Røhr

Since Specialization
Citations

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

Fields of papers citing papers by Åsmund K. Røhr

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Åsmund K. Røhr. 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 Åsmund K. Røhr. The network helps show where Åsmund K. Røhr may publish in the future.

Co-authorship network of co-authors of Åsmund K. Røhr

This figure shows the co-authorship network connecting the top 25 collaborators of Åsmund K. Røhr. A scholar is included among the top collaborators of Åsmund K. Røhr 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 Åsmund K. Røhr. Åsmund K. Røhr 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.
Sengupta, Kushal, Sergio A. V. Jannuzzi, Morten Sørlie, et al.. (2025). Structural and electronic modulations of lytic polysaccharide monooxygenase (LPMO) upon chitin binding: insights from X-ray spectroscopy. Chemical Science. 16(48). 22952–22969.
2.
3.
Ayuso‐Fernández, Iván, Anton A. Stepnov, Roland Ludwig, et al.. (2024). Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO). Nature Communications. 15(1). 3975–3975. 7 indexed citations
4.
Ayuso‐Fernández, Iván, et al.. (2023). Reductants fuel lytic polysaccharide monooxygenase activity in a pH‐dependent manner. FEBS Letters. 597(10). 1363–1374. 23 indexed citations
5.
Røhr, Åsmund K., et al.. (2023). Initial characterization of an iron superoxide dismutase from Thermobifida fusca. JBIC Journal of Biological Inorganic Chemistry. 28(7). 689–698. 3 indexed citations
6.
Røhr, Åsmund K., et al.. (2022). The extracellular domain of site-2-metalloprotease RseP is important for sensitivity to bacteriocin EntK1. Journal of Biological Chemistry. 298(11). 102593–102593. 8 indexed citations
7.
Askarian, Fatemeh, Satoshi Uchiyama, Sophanit Mekasha, et al.. (2021). The lytic polysaccharide monooxygenase CbpD promotes Pseudomonas aeruginosa virulence in systemic infection. Nature Communications. 12(1). 1230–1230. 63 indexed citations
8.
Røhr, Åsmund K., et al.. (2021). Characterization of a lytic polysaccharide monooxygenase from Aspergillus fumigatus shows functional variation among family AA11 fungal LPMOs. Journal of Biological Chemistry. 297(6). 101421–101421. 11 indexed citations
9.
Michalak, Leszek, Gabriel Vasconcelos Pereira, Åsmund K. Røhr, et al.. (2021). Human Gut Faecalibacterium prausnitzii Deploys a Highly Efficient Conserved System To Cross-Feed on β-Mannan-Derived Oligosaccharides. mBio. 12(3). e0362820–e0362820. 55 indexed citations
10.
Sæther, Thomas, et al.. (2021). Methylation-dependent SUMOylation of the architectural transcription factor HMGA2. Biochemical and Biophysical Research Communications. 552. 91–97. 6 indexed citations
11.
Michalak, Leszek, et al.. (2020). A pair of esterases from a commensal gut bacterium remove acetylations from all positions on complex β-mannans. Proceedings of the National Academy of Sciences. 117(13). 7122–7130. 31 indexed citations
12.
Bissaro, Bastien, Bennett R. Streit, Vincent G. H. Eijsink, et al.. (2020). Molecular mechanism of the chitinolytic peroxygenase reaction. Proceedings of the National Academy of Sciences. 117(3). 1504–1513. 111 indexed citations
13.
Bissaro, Bastien, et al.. (2020). Controlled depolymerization of cellulose by light-driven lytic polysaccharide oxygenases. Nature Communications. 11(1). 890–890. 69 indexed citations
14.
Eijsink, Vincent G. H., Dejan Petrović, Zarah Forsberg, et al.. (2019). On the functional characterization of lytic polysaccharide monooxygenases (LPMOs). Biotechnology for Biofuels. 12(1). 58–58. 127 indexed citations
15.
Forsberg, Zarah, Morten Sørlie, Dejan Petrović, et al.. (2019). Polysaccharide degradation by lytic polysaccharide monooxygenases. Current Opinion in Structural Biology. 59. 54–64. 117 indexed citations
16.
Bissaro, Bastien, Anikó Várnai, Åsmund K. Røhr, & Vincent G. H. Eijsink. (2018). Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass. Microbiology and Molecular Biology Reviews. 82(4). 217 indexed citations
17.
Forsberg, Zarah, Cassandra E. Nelson, Bjørn Dalhus, et al.. (2016). Structural and Functional Analysis of a Lytic Polysaccharide Monooxygenase Important for Efficient Utilization of Chitin in Cellvibrio japonicus. Journal of Biological Chemistry. 291(14). 7300–7312. 108 indexed citations
18.
Backe, Paul Hoff, Åsmund K. Røhr, Brian Fowler, et al.. (2013). Novel Deletion Mutation Identified in a Patient with Late-Onset Combined Methylmalonic Acidemia and Homocystinuria, cblC Type. JIMD Reports. 11. 79–85. 13 indexed citations
19.
Sandvik, Guro K., Jonas Bergan, Giorgio Zoppellaro, et al.. (2012). Studies of Ribonucleotide Reductase in Crucian Carp—An Oxygen Dependent Enzyme in an Anoxia Tolerant Vertebrate. PLoS ONE. 7(8). e42784–e42784. 11 indexed citations
20.
Hersleth, H.-P., Takeshi Uchida, Åsmund K. Røhr, et al.. (2005). Structure of the intermediates in the myoglobin-peroxide reaction. Acta Crystallographica Section A Foundations of Crystallography. 61(a1). c214–c214. 1 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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