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Jin, Z., Olsen, W. P., Mörman, C., Leppert, A., Kumar, R., Møllebjerg, A., Nielsen, L. G., Moshynets, O. V., Frasinyuk, M. S., Elosua, J. Y., Ferreira, D., Abelein, A., Landreh, M., Knight, S. D., Johansson, J., Otzen, D. E. & Chen, G. (2025). Helicobacter pylori CagA protein is a potent and broad-spectrum amyloid inhibitor. Science Advances, 11(24), Article eads7525. https://doi.org/10.1126/sciadv.ads7525

Jeppesen, M. D., Hein, K., Nissen, P., Westh, P. & Otzen, D. E. (2010). A thermodynamic analysis of fibrillar polymorphism. Advances in Biophysical Chemistry, 149(1-2), 40-6. https://doi.org/10.1016/j.bpc.2010.03.016

Jeppesen, M. D., Westh, P. & Otzen, D. E. (2010). The role of protonation in protein fibrillation. FEBS Letters, 584(4), 780-4. https://doi.org/10.1016/j.febslet.2010.01.002

Jensen, P. L., Dueholm, M. S., Larsen, P., Petersen, S. V., Enghild, J. J., Christiansen, G., Højrup, P., Nielsen, P. H. & Otzen, D. (2009). Widespread abundance of Functional Bacterial Amyloid in Mycolata and other Gram positive Bacteria. Applied and Environmental Microbiology, 75, 4101-4110.

Jensen, G. V., Pedersen, J. N., Otzen, D. E. & Pedersen, J. S. (2020). Multi-Step Unfolding and Rearrangement of α-Lactalbumin by SDS Revealed by Stopped-Flow SAXS. Frontiers in Molecular Biosciences, 7, Article 125. https://doi.org/10.3389/fmolb.2020.00125

Javed, I., Zhang, Z., Adamcik, J., Andrikopoulos, N., Li, Y., Otzen, D. E., Lin, S., Mezzenga, R., Davis, T. P., Ding, F. & Ke, P. C. (2020). Accelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC. Advanced Science, 7(18), Article 2001299. https://doi.org/10.1002/advs.202001299

Jarvela, T. S., Lam, H. A., Helwig, M., Lorenzen, N., Otzen, D. E., McLean, P. J., Maidment, N. T. & Lindberg, I. (2016). The neural chaperone proSAAS blocks α-synuclein fibrillation and neurotoxicity. Proceedings of the National Academy of Sciences (PNAS), 113(32), E4708-E4715. https://doi.org/10.1073/pnas.1601091113

Jakob, D. S., Wang, H., Zeng, G., Otzen, D. E., Yan, Y. & Xu, X. (2020). Peak Force Infrared - Kelvin Probe Force Microscopy. Angewandte Chemie International Edition, 59(37), 16083-16090. https://doi.org/10.1002/anie.202004211

Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995). The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding. Journal of Molecular Biology, 254(2), 260-288. https://doi.org/10.1006/jmbi.1995.0616

Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995). Nature and Consequences of GroEL-Protein Interactions. Biochemistry, 34(44), 14581-14587. https://doi.org/10.1021/bi00044a037

Hyldgaard, M., Mygind, T., Vad, B. S., Stenvang, M., Otzen, D. & Meyer, R. L. (2014). The Antimicrobial Mechanism of Action of Epsilon-Poly-L-Lysine. Applied and Environmental Microbiology, 80(24), 7758-7770 . https://doi.org/10.1128/AEM.02204-14

Huynh, T. H. V., Mantel, M., Mikkelsen, K., Lindhardt, A. T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2009). A Versatile Approach to β-Amyloid Fibril-Binding Compounds Exploiting the Shirakawa/Hayashi Protocol for trans-Alkene Synthesis. Organic Letters, 11, 999-1002.

Huma, Z.-E., Javed, I., Zhang, Z., Bilal, H., Sun, Y., Hussain, S. Z., Davis, T. P., Otzen, D. E., Landersdorfer, C. B., Ding, F., Hussain, I. & Ke, P. C. (2020). Nanosilver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition. Small (Weinheim an der Bergstrasse, Germany), 16(21), Article 1906674. https://doi.org/10.1002/smll.201906674

Hovgaard, M. B., Dong, M., Otzen, D. & Besenbacher, F. (2007). Quartz crystal microbalance studies of multilayer glucagons fibrillation at the solid-liquid interface. Biophysical Journal, 93(6), 2162.

Hovgaard, M. B., Dong, M., Otzen, D. E. & Besenbacher, F. (2007). Quartz crystal microbalance studies of multilayer glucagon fibrillation at the solid-liquid interface. Biophysical Journal, 93(6), 2162-9. https://doi.org/10.1529/biophysj.107.109686

Hourfar, H., Aliakbari, F., Aqdam, S. R., Nayeri, Z., Bardania, H., Otzen, D. E. & Morshedi, D. (2023). The impact of α-synuclein aggregates on blood-brain barrier integrity in the presence of neurovascular unit cells. International Journal of Biological Macromolecules, 229, 305-320. https://doi.org/10.1016/j.ijbiomac.2022.12.134

Højgaard, C., Sørensen, H. V., Pedersen, J. S., Winther, J. R. & Otzen, D. E. (2018). Can a Charged Surfactant Unfold an Uncharged Protein? Biophysical Journal, 115(11), 2081-2086. https://doi.org/10.1016/j.bpj.2018.10.022

Hjorth, C. F., Hubálek, F., Andersson, J., Poulsen, C., Otzen, D. & Naver, H. (2015). Purification and Identification of High Molecular Weight Products Formed During Storage of Neutral Formulation of Human Insulin. Pharmaceutical Research, 32(6), 2072-2085. https://doi.org/10.1007/s11095-014-1600-3

Hjorth, C. F., Norrman, M., Wahlund, P.-O., Benie, A. J., Petersen, B. O., Jessen, C. M., Pedersen, T. Å., Vestergaard, K., Steensgaard, D. B., Pedersen, J. S., Naver, H., Hubálek, F., Poulsen, C. & Otzen, D. (2016). Structure, Aggregation, and Activity of a Covalent Insulin Dimer Formed During Storage of Neutral Formulation of Human Insulin. Journal of Pharmaceutical Sciences, 105(4), 1376-1386. https://doi.org/10.1016/j.xphs.2016.01.003

Hjørringgaard, C. U., Vad, B., Nielsen, S. B., Matchkov, V., Vosegaard, T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2010). Cyclodextrin scaffolded alamethicin with highly efficient channel-forming properties. Journal of Peptide Science, 16, 148.

Hjørringgaard, C. U., Vad, B. S., Nielsen, S. B., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2009). Templated Multimers of Antimicrobial Peptides. Poster session presented at 8th Australian Peptide Conference, Peptides - Tools, Targets & Therapeutics , Australia.

Hjørringgaard, C. U., Vad, B. S., Matchkov, V., Nielsen, S. B., Vosegaard, T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2010). Cyclodextrin Scaffolded Alamethicin with Highly Efficient Channel-forming Properties. Poster session presented at 31st European Peptide Symposium, 31EPS, Copenhagen, Denmark.

Hjørringgaard, C. U., Vad, B. S., Matchkov, V., Nielsen, S. B., Vosegaard, T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2012). Cyclodextrin-Scaffolded Alamethicin with Remarkably Efficient Membrane Permeabilizing Properties and Membrane Current Conductance. Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 116(26), 7652-7659. https://doi.org/10.1021/jp2098679

Helwig, M., Hoshino, A., Berridge, C., Lee, S.-N., Lorenzen, N., Otzen, D., Eriksen, J. & Lindberg, I. (2013). The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins. Journal of Biological Chemistry, 288(2), 1114.

Hein, K. L., Kragh-Hansen, U., Morth, J. P., Jeppesen, M., Otzen, D., Møller, J. V. & Nissen, P. (2010). Crystallographic analysis reveals a unique lidocaine binding site on human serum albumin. Journal of Structural Biology, 171, 353-360.

Heegaard, P. M. P., Boas, U. & Otzen, D. (2007). Dendrimer effects on peptide and protein fibrillation. Macromolecular Bioscience, (7), 1047-1059.

He, J., Becares, E. R., Thulstrup, P. W., Gamon, L. F., Pedersen, J. N., Otzen, D., Gourdon, P., Davies, M. J. & Hägglund, P. (2020). Peroxynitrous acid (ONOOH) modifies the structure of anastellin and influences its capacity to polymerize fibronectin. Redox Biology, 36, Article 101631. https://doi.org/10.1016/j.redox.2020.101631

He, J., Steffen, J. H., Thulstrup, P. W., Pedersen, J. N., Sauerland, M. B., Otzen, D. E., Hawkins, C. L., Gourdon, P., Davies, M. J. & Hägglund, P. (2022). Anastellin impacts on the processing of extracellular matrix fibronectin and stimulates release of cytokines from coronary artery smooth muscle cells. Scientific Reports, 12(1), Article 22051. https://doi.org/10.1038/s41598-022-26359-9

Hansted, J. G., Wejse, P. L., Bertelsen, H. & Otzen, D. E. (2011). Effect of protein-surfactant interactions on aggregation of β-lactoglobulin. BBA General Subjects, 1814(5), 713-723. https://doi.org/10.1016/j.bbapap.2011.03.011

Hansen, J. H., Petersen, S. V., Andersen, K. K., Enghild, J. J., Damhus, T. & Otzen, D. (2009). Stable intermediates determine proteins' primary unfolding sites in the presence of surfactants. Biopolymers, 91(3), 221-31. https://doi.org/10.1002/bip.21125

Hajipour, M. J., Mohammad-Beigi, H., Nabipour, I., Mahmoudi, N., Azhdarzadeh, M., Derakhshankhah, H., El Dawud, D., Mohammadinejad, R. & Otzen, D. (2020). Amyloid fibril inhibition, acceleration, or fragmentation: Are nano-based approaches advance in the right direction? Nano Today, 35(December), Article 100983. https://doi.org/10.1016/j.nantod.2020.100983

Haikal, C., Pascual, L. O., Najarzadeh, Z., Bernfur, K., Svanbergsson, A., Otzen, D. E., Linse, S. & Li, J. Y. (2021). The bacterial amyloids phenol soluble modulins from staphylococcus aureus catalyze alpha-synuclein aggregation. International Journal of Molecular Sciences , 22(21), Article 11594. https://doi.org/10.3390/ijms222111594

Haaning, S., Radutoiu, S., Hoffmann, S. V., Dittmer, J., Giehm, L., Otzen, D. & Stougaard, J. (2008). An unusual intrinsically disordered protein from the model legume Lotus japonicus stabilizes proteins in vitro. Journal of Biological Chemistry, 283(45), 31142-52. https://doi.org/10.1074/jbc.M805024200

Grønnemose, A. L., Østerlund, E. C., Otzen, D. E. & Jørgensen, T. J. D. (2022). EGCG has Dual and Opposing Effects on the N-terminal Region of Self-associating α-synuclein Oligomers. Journal of Molecular Biology, 434(23), Article 167855. https://doi.org/10.1016/j.jmb.2022.167855

Golan, N., Parizat, A., Tabachnikov, O., Barnea, E., Olsen, W. P., Otzen, D. E. & Landau, M. (2025). Resilience and Charge-Dependent Fibrillation of functional amyloid: Interactions of Pseudomonas Biofilm-Associated FapB and FapC Amyloids. The Journal of Biological Chemistry, 301(2), Article 108096. https://doi.org/10.1016/j.jbc.2024.108096

Giehm, L., Christensen, C., Boas, U., Heegaard, P. M. H. & Otzen, D. (2008). Dendrimers destabilize proteins in a generation-dependent manner involving eletrostatic interactions. Biopolymers, 89, 522-529.

Giehm, L. & Otzen, D. (2010). Strategies to increase the reproducibility of α-synuclein fibrillation in plate reader assays. Analytical Biochemistry, 406(2), 270-281.

Giehm, L., Oliveira, C. L. P. D., Christiansen, G., Pedersen, J. S. & Otzen, D. (2010). SDS-Induced Fibrillation of α-Synuclein: An Alternative Fibrillation Pathway. Journal of Molecular Biology, 401, 115-133. https://doi.org/10.1016/j.jmb.2010.05.060

Giehm, L., Dal Degan, F., Fraser, P., Klysner, S. & Otzen, D. E. (2010). An Aß concatemer with altered aggregation propensities. BBA General Subjects, 1804(10), 2025-35. https://doi.org/10.1016/j.bbapap.2010.06.023

Giehm, L., Lorenzen, N. & Otzen, D. E. (2010). Assays for α-synuclein aggregation. Methods. https://doi.org/10.1016/j.ymeth.2010.12.008

Giehm, L. & Otzen, D. E. (2010). Strategies to increase the reproducibility of protein fibrillization in plate reader assays. Analytical Biochemistry, 400(2), 270-81. https://doi.org/10.1016/j.ab.2010.02.001

Giehm, L., Svergun, D. I., Otzen, D. E. & Vestergaard, B. (2011). Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation. Proceedings of the National Academy of Sciences (PNAS), 108(8), 3246-3251. https://doi.org/10.1073/pnas.1013225108

Giehm, L., Lorenzen, N. & Otzen, D. (2011). Assays for alpha-synuclein aggregation. Methods, 53(3), 295-305.

Giehm, L. & Otzen, D. E. (2010). Erratum to Strategies to increase the reproducibility of protein fibrillization in plate reader assays [Anal. Biochem., 400, (2010), 270-281]. Analytical Biochemistry, 406(2). https://doi.org/10.1016/j.ab.2010.06.047

Giehm, L. & Otzen, D. (2013). Experimental Approaches to Inducing Amyloid Aggregates. In Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties (pp. 295-320). Wiley-VCH. https://doi.org/10.1002/9783527654185.ch14

Ghodke, S., Nielsen, S. B., Christiansen, G., Hjuler, H. A., Flink, J., Otzen, D. & Nielsen, S. B. (2012). Mapping out the multistage fibrillation of glucagon. FEBS journal, 279(5), 752-765. https://doi.org/10.1111/j.1742-4658.2011.08465.x

Ghodke, S. D., Jensen, G. V., Svane, A. S. P., Weise, K., Søndergaard, A., Behrens, M. A., Pedersen, J. S., Nielsen, N. C., Pedersen, J. S., Winter, R. & Otzen, D. (2014). Polymorphism, metastable species and interconversion: the many states of glucagon fibrils. In V. Uversky & Y. Lyubchenko (Eds.), Bio-nanoimaging: Protein misfolding and aggregation (pp. 373-386). Elsevier. https://doi.org/10.1016/B978-0-12-394431-3.00034-1

Frøkjær, S. & Otzen, D. (2005). Protein drug stability: a formulation challenge. Nature Reviews. Drug Discovery, 4, 298-306. https://doi.org/10.1038/nrd1695

Frislev, H. K. S., Pedersen, J. N., Pedersen, J. S. & Otzen, D. (2016). Liprotides: Nano-Sized Cytotoxic Protein-Fatty Acid Complexes with a Core-Shell or Multi-Layer Structure. Poster session presented at Biophysical Society 60th Annual Meeting, Los Angeles, United States. http://www.cell.com/biophysj/fulltext/S0006-3495%2815%2904270-8

Frislev, H. K. S., Jessen, C. M., Oliveira, C. L. P., Pedersen, J. S. & Otzen, D. E. (2016). Liprotides made of α-lactalbumin and cis fatty acids form core-shell and multi-layer structures with a common membrane-targeting mechanism. B B A - Proteins and Proteomics, 1864(7), 847-859. https://doi.org/10.1016/j.bbapap.2016.04.003

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