A. Henriksen

5.0k total citations · 2 hit papers
57 papers, 4.1k citations indexed

About

A. Henriksen is a scholar working on Molecular Biology, Plant Science and Biotechnology. According to data from OpenAlex, A. Henriksen has authored 57 papers receiving a total of 4.1k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 25 papers in Plant Science and 14 papers in Biotechnology. Recurrent topics in A. Henriksen's work include Enzyme-mediated dye degradation (14 papers), Enzyme Production and Characterization (12 papers) and Enzyme Structure and Function (11 papers). A. Henriksen is often cited by papers focused on Enzyme-mediated dye degradation (14 papers), Enzyme Production and Characterization (12 papers) and Enzyme Structure and Function (11 papers). A. Henriksen collaborates with scholars based in Denmark, United Kingdom and France. A. Henriksen's co-authors include Michael Gajhede, Andrew Smith, David J. Schuller, G.I. Berglund, Gunilla Carlsson, H. Szöke, János Hajdu, T.L. Poulos, Karen G. Welinder and Osman Mirza and has published in prestigious journals such as Nature, Journal of Biological Chemistry and The Journal of Immunology.

In The Last Decade

A. Henriksen

57 papers receiving 4.0k citations

Hit Papers

The catalytic pathway of horseradish peroxidase at high r... 1997 2026 2006 2016 2002 1997 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
A. Henriksen Denmark 30 2.0k 1.3k 638 607 486 57 4.1k
Rosangela Marchelli Italy 50 3.4k 1.7× 1.7k 1.3× 538 0.8× 334 0.6× 311 0.6× 239 7.6k
Karen G. Welinder Denmark 41 3.0k 1.5× 3.2k 2.5× 365 0.6× 841 1.4× 639 1.3× 113 6.1k
J.P. Turkenburg United Kingdom 43 5.2k 2.5× 872 0.7× 863 1.4× 1.4k 2.3× 422 0.9× 121 7.1k
Francesco Bonomi Italy 40 2.0k 1.0× 813 0.6× 470 0.7× 405 0.7× 89 0.2× 190 5.1k
Monica M. Palcic Canada 53 6.3k 3.1× 752 0.6× 419 0.7× 1.2k 2.0× 139 0.3× 257 9.0k
Kengo Sakaguchi Japan 46 5.3k 2.6× 1.7k 1.3× 520 0.8× 304 0.5× 200 0.4× 332 7.9k
Bunzo Mikami Japan 45 3.6k 1.7× 1.9k 1.4× 784 1.2× 2.0k 3.3× 92 0.2× 285 7.5k
David L. Ollis Australia 47 5.4k 2.6× 1.0k 0.8× 1.2k 1.9× 412 0.7× 184 0.4× 140 7.9k
Bijan Ranjbar Iran 34 2.6k 1.3× 537 0.4× 777 1.2× 695 1.1× 334 0.7× 162 4.2k
Takashi Takahashi Japan 41 3.1k 1.5× 466 0.4× 788 1.2× 481 0.8× 382 0.8× 331 7.0k

Countries citing papers authored by A. Henriksen

Since Specialization
Citations

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

Fields of papers citing papers by A. Henriksen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of A. Henriksen

This figure shows the co-authorship network connecting the top 25 collaborators of A. Henriksen. A scholar is included among the top collaborators of A. Henriksen 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 A. Henriksen. A. Henriksen 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.
Sim, Lyann, Sophie R. Beeren, David Dauvillée, et al.. (2014). Crystal Structure of the Chlamydomonas Starch Debranching Enzyme Isoamylase ISA1 Reveals Insights into the Mechanism of Branch Trimming and Complex Assembly. Journal of Biological Chemistry. 289(33). 22991–23003. 46 indexed citations
2.
Carciofi, Massimiliano, Andreas Blennow, Susanne L. Jensen, et al.. (2012). Concerted suppression of all starch branching enzyme genes in barley produces amylose-only starch granules. BMC Plant Biology. 12(1). 223–223. 193 indexed citations
3.
Pye, Valerie E., Caspar Christensen, James H. Dyer, S. Arent, & A. Henriksen. (2010). Peroxisomal Plant 3-Ketoacyl-CoA Thiolase Structure and Activity Are Regulated by a Sensitive Redox Switch. Journal of Biological Chemistry. 285(31). 24078–24088. 37 indexed citations
4.
Arent, S., et al.. (2010). The Multifunctional Protein in Peroxisomal β-Oxidation. Journal of Biological Chemistry. 285(31). 24066–24077. 41 indexed citations
5.
Arent, S., Valerie E. Pye, & A. Henriksen. (2008). Structure and function of plant acyl-CoA oxidases. Plant Physiology and Biochemistry. 46(3). 292–301. 48 indexed citations
6.
Olsen, Johan G., et al.. (2008). Barley aldose reductase: Structure, cofactor binding, and substrate recognition in the aldo/keto reductase 4C family. Proteins Structure Function and Bioinformatics. 71(3). 1572–1581. 12 indexed citations
7.
Christensen, Caspar, Birthe B. Kragelund, Penny von Wettstein‐Knowles, & A. Henriksen. (2007). Structure of the human β‐ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase. Protein Science. 16(2). 261–272. 62 indexed citations
8.
Pedersen, Lise, et al.. (2006). Controlling Electron Transfer in Acyl-CoA Oxidases and Dehydrogenases. Journal of Biological Chemistry. 281(41). 31012–31020. 18 indexed citations
9.
Wettstein‐Knowles, Penny von, Johan G. Olsen, Kirsten Arnvig McGuire, & A. Henriksen. (2006). Fatty acid synthesis. FEBS Journal. 273(4). 695–710. 68 indexed citations
10.
Holm, Jens‐Christian, Michael Gajhede, Mercedes Ferreras, et al.. (2004). Allergy Vaccine Engineering: Epitope Modulation of Recombinant Bet v 1 Reduces IgE Binding but Retains Protein Folding Pattern for Induction of Protective Blocking-Antibody Responses. The Journal of Immunology. 173(8). 5258–5267. 61 indexed citations
11.
Pedersen, Lise & A. Henriksen. (2004). Expression, purification and crystallization of two peroxisomal acyl-CoA oxidases fromArabidopsis thaliana. Acta Crystallographica Section D Biological Crystallography. 60(6). 1125–1128. 6 indexed citations
12.
Olsen, Johan G., Claus Flensburg, Ole Olsen, G. Bricogne, & A. Henriksen. (2004). Solving the structure of the bubble protein using the anomalous sulfur signal from single-crystal in-house Cu Kα diffraction data only. Acta Crystallographica Section D Biological Crystallography. 60(2). 250–255. 30 indexed citations
13.
Teilum, Kaare, et al.. (2002). Purification, crystallization and preliminary X-ray diffraction analysis of the carbohydrate-binding domain of flocculin, a cell-adhesion molecule fromSaccharomyces carlsbergensis. Acta Crystallographica Section D Biological Crystallography. 58(12). 2135–2137. 10 indexed citations
14.
Henriksen, A., Te Piao King, Osman Mirza, et al.. (2001). Major venom allergen of yellow jackets, Ves v 5: Structural characterization of a pathogenesis‐related protein superfamily. Proteins Structure Function and Bioinformatics. 45(4). 438–448. 124 indexed citations
15.
Henriksen, A., Osman Mirza, Chiara Indiani, et al.. (2001). Structure of soybean seed coat peroxidase: A plant peroxidase with unusual stability and haem‐apoprotein interactions. Protein Science. 10(1). 108–115. 116 indexed citations
16.
Mirza, Osman, Lars K. Skov, A. Henriksen, et al.. (2000). Structural analysis of substrate binding by the glucan synthesizing enzyme amylosucrase. Acta Crystallographica Section A Foundations of Crystallography. 56(s1). s245–s245. 2 indexed citations
17.
Skov, Lars K., Osman Mirza, A. Henriksen, et al.. (2000). Crystallization and preliminary X-ray studies of recombinant amylosucrase fromNeisseria polysaccharea. Acta Crystallographica Section D Biological Crystallography. 56(2). 203–205. 24 indexed citations
18.
Henriksen, A., Andrew Smith, & Michael Gajhede. (1999). The Structures of the Horseradish Peroxidase C-Ferulic Acid Complex and the Ternary Complex with Cyanide Suggest How Peroxidases Oxidize Small Phenolic Substrates. Journal of Biological Chemistry. 274(49). 35005–35011. 189 indexed citations
19.
Henriksen, A., Karen G. Welinder, & Michael Gajhede. (1998). Structure of Barley Grain Peroxidase Refined at 1.9-Å Resolution. Journal of Biological Chemistry. 273(4). 2241–2248. 72 indexed citations
20.
Gajhede, Michael, David J. Schuller, A. Henriksen, Andrew Smith, & T.L. Poulos. (1997). Crystal structure of horseradish peroxidase C at 2.15 Å resolution. Nature Structural Biology. 4(12). 1032–1038. 606 indexed citations breakdown →

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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