Per Hägglund

3.6k total citations
106 papers, 2.8k citations indexed

About

Per Hägglund is a scholar working on Molecular Biology, Cell Biology and Biotechnology. According to data from OpenAlex, Per Hägglund has authored 106 papers receiving a total of 2.8k indexed citations (citations by other indexed papers that have themselves been cited), including 57 papers in Molecular Biology, 19 papers in Cell Biology and 16 papers in Biotechnology. Recurrent topics in Per Hägglund's work include Redox biology and oxidative stress (29 papers), Enzyme Production and Characterization (15 papers) and Advanced Proteomics Techniques and Applications (8 papers). Per Hägglund is often cited by papers focused on Redox biology and oxidative stress (29 papers), Enzyme Production and Characterization (15 papers) and Advanced Proteomics Techniques and Applications (8 papers). Per Hägglund collaborates with scholars based in Denmark, Sweden and Chile. Per Hägglund's co-authors include Birte Svensson, Jakob Bunkenborg, Michael J. Davies, Peter Roepstorff, Félix Elortza, Ole N. Jensen, Christine Finnie, Henrik Stålbrand, Kenji Maeda and M.A. Karsdal and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and PLoS ONE.

In The Last Decade

Per Hägglund

99 papers receiving 2.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Per Hägglund Denmark 31 1.6k 443 348 328 312 106 2.8k
Bin Qin China 31 1.9k 1.2× 72 0.2× 212 0.6× 276 0.8× 185 0.6× 127 3.2k
Chantragan Srisomsap Thailand 26 1.2k 0.7× 112 0.3× 172 0.5× 337 1.0× 105 0.3× 134 2.4k
Qiuyan Wang China 29 2.1k 1.3× 132 0.3× 127 0.4× 250 0.8× 166 0.5× 143 3.6k
Alberto Vitali Italy 30 1.2k 0.8× 179 0.4× 74 0.2× 214 0.7× 215 0.7× 87 2.3k
Akiko Kubo Japan 32 1.3k 0.8× 187 0.4× 479 1.4× 916 2.8× 553 1.8× 109 3.5k
K.L. Kavanagh United Kingdom 32 2.8k 1.7× 71 0.2× 125 0.4× 249 0.8× 236 0.8× 56 4.7k
Feng Guan China 29 1.7k 1.1× 153 0.3× 73 0.2× 128 0.4× 178 0.6× 124 2.4k
Takahiro Mori Japan 39 2.6k 1.6× 85 0.2× 465 1.3× 217 0.7× 134 0.4× 165 4.9k
Xuezhi Bi Singapore 29 1.2k 0.7× 148 0.3× 141 0.4× 155 0.5× 144 0.5× 76 2.1k
Masahiro Okada Japan 32 2.2k 1.4× 93 0.2× 241 0.7× 211 0.6× 163 0.5× 85 3.8k

Countries citing papers authored by Per Hägglund

Since Specialization
Citations

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

Fields of papers citing papers by Per Hägglund

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Per Hägglund

This figure shows the co-authorship network connecting the top 25 collaborators of Per Hägglund. A scholar is included among the top collaborators of Per Hägglund 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 Hägglund. Per Hägglund 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.
Gao, Qing, Per Hägglund, Luke F. Gamon, & Michael J. Davies. (2024). Mapping of oxidative modifications on the alpha-keto glutarate dehydrogenase complex induced by singlet oxygen: Effects on structure and activity. Free Radical Biology and Medicine. 224. 723–739. 2 indexed citations
2.
Sanchez‐Alonso, Jose L., et al.. (2024). Mesenteric artery smooth muscle cells from hypertensive rats have increased microtubule acetylation. Biochemical Journal. 481(5). 387–403. 2 indexed citations
3.
Hägglund, Per, et al.. (2022). The cysteine residue in beta-lactoglobulin reacts with oxidized tyrosine residues in beta-casein to give casein-lactoglobulin dimers. Archives of Biochemistry and Biophysics. 733. 109482–109482. 6 indexed citations
4.
Horst, Jennifer van der, Geoffrey W. Abbott, Lijo Cherian Ozhathil, et al.. (2021). Dynein regulates Kv7.4 channel trafficking from the cell membrane. The Journal of General Physiology. 153(3). 13 indexed citations
5.
Jiang, Shuwen, et al.. (2021). Formation of protein cross-links by singlet oxygen-mediated disulfide oxidation. Redox Biology. 41. 101874–101874. 29 indexed citations
6.
Al‐Soud, Waleed Abu, et al.. (2020). Azo dying of α‐keratin material improves microbial keratinase screening and standardization. Microbial Biotechnology. 13(4). 984–996. 13 indexed citations
7.
Tiwari, Manish Kumar, Per Hägglund, Ian Max Møller, Michael J. Davies, & Morten J. Bjerrum. (2019). Copper ion / H2O2 oxidation of Cu/Zn-Superoxide dismutase: Implications for enzymatic activity and antioxidant action. Redox Biology. 26. 101262–101262. 38 indexed citations
8.
Chuang, Christine Y., Astrid Hammer, Gerald Höefler, et al.. (2018). Exposure of tropoelastin to peroxynitrous acid gives high yields of nitrated tyrosine residues, di-tyrosine cross-links and altered protein structure and function. Free Radical Biology and Medicine. 120. S102–S103.
9.
Leinisch, Fabian, et al.. (2018). Structural and functional changes in RNAse A originating from tyrosine and histidine cross-linking and oxidation induced by singlet oxygen and peroxyl radicals. Free Radical Biology and Medicine. 126. 73–86. 27 indexed citations
10.
Karsdal, M.A., et al.. (2018). Tofacitinib and TPCA-1 exert chondroprotective effects on extracellular matrix turnover in bovine articular cartilage ex vivo. Biochemical Pharmacology. 165. 91–98. 18 indexed citations
11.
Stender, Emil G. P., Sanaullah Khan, Richard Ipsen, et al.. (2017). Effect of alginate size, mannuronic/guluronic acid content and pH on particle size, thermodynamics and composition of complexes with β-lactoglobulin. Food Hydrocolloids. 75. 157–163. 32 indexed citations
12.
Herschend, Jakob, Andrea Marion Marquard, Birte Svensson, et al.. (2017). A meta-proteomics approach to study the interspecies interactions affecting microbial biofilm development in a model community. Scientific Reports. 7(1). 16483–16483. 51 indexed citations
13.
Bay‐Jensen, Anne‐Christine, Terkel Christiansen, M.A. Karsdal, et al.. (2017). Establishment of a Human Synovium and Cartilage Co-Culture. Osteoarthritis and Cartilage. 25. S276–S277.
14.
Cuesta-Seijo, J.A., Christian Ruzanski, Sebastián Meier, et al.. (2017). Functional and structural characterization of plastidic starch phosphorylase during barley endosperm development. PLoS ONE. 12(4). e0175488–e0175488. 40 indexed citations
15.
16.
Jacquiod, Samuel, et al.. (2015). Developing of microbial consortia for enzymatic valuable conversion of keratin-rich slaughterhouse waste. Technical University of Denmark, DTU Orbit (Technical University of Denmark, DTU). 1 indexed citations
17.
Svensson, Birte, et al.. (2015). Two Lactococcus lactis thioredoxin paralogues play different roles in responses to arsenate and oxidative stress. Microbiology. 161(3). 528–538. 6 indexed citations
18.
Kristensen, Jacob Hull, Lise Larsen, B. Dasgupta, et al.. (2015). Levels of circulating MMP-7 degraded elastin are elevated in pulmonary disorders. Clinical Biochemistry. 48(16-17). 1083–1088. 27 indexed citations
19.
Maeda, Kenji, Per Hägglund, Olof Björnberg, Jakob R. Winther, & Birte Svensson. (2010). Kinetic and thermodynamic properties of two barley thioredoxin h isozymes, HvTrxh1 and HvTrxh2. FEBS Letters. 584(15). 3376–3380. 14 indexed citations
20.
Ademark, Pia, Ronald P. de Vries, Per Hägglund, Henrik Stålbrand, & Jaap Visser. (2001). Cloning and characterization of Aspergillus niger genes encoding an α‐galactosidase and a β‐mannosidase involved in galactomannan degradation. European Journal of Biochemistry. 268(10). 2982–2990. 77 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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