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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
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
Knudsen, S. K., Westergaard, U. B., Frantzmann, M., Stensballe, A. & Otzen, D. (2008). Effect of glycosylation on biphysical and flocculative properties of the extracellular domain of Ag43. Biochemical Journal, (412), 563-577.
Otzen, D. E. (2024). Editorial: Research methods in biochemistry and biophysics. BBA advances, 6, Article 100121. https://doi.org/10.1016/j.bbadva.2024.100121
Svane, A. S. P., Jahn, K., Deva, T., Malmendal, A., Otzen, D., Dittmer, J. & Nielsen, N. C. (2008). Early Stages of Amyloid Fibril Formation Studied by Liquid-State NMR: The Peptide Hormone Glucagon. Biophysical Journal, 95(1), 366 – 377. https://doi.org/10.1529/biophysj.107.122895
Tiwari, M. K., Leinisch, F., Sahin, C., Møller, I. M., Otzen, D., Davies, M. J. & Bjerrum, M. J. (2018). Early events in copper-ion catalyzed oxidation of α-synuclein. Free Radical Biology & Medicine, 121, 38-50. https://doi.org/10.1016/j.freeradbiomed.2018.04.559
Zhang, T., Bär, J., Risberg, L., Gómez Mejia, A., Hammar, H., Löffler, S., Otzen, D. E., Andreasen, M., Meyer, R. L., Melican, K., Zinkernagel, A. S. & Richter-Dahlfors, A. (2025). Dynamic visualization of extracellular matrix components in S. aureus colony biofilms reveals functional amyloids leading to the formation of cap-like structures. Biofilm, 10, Article 100318. https://doi.org/10.1016/j.bioflm.2025.100318
Frislev, H. S., Jakobsen, S. C. L., Frank, S. A. & Otzen, D. E. (2018). Dynamic content exchange between liprotides. Biophysical Chemistry, 233, 13-18. https://doi.org/10.1016/j.bpc.2017.11.006
Otzen, D. E., Barciszewski, J. & Clark, B. F. C. (1994). Dual hydrolytic role for Pb(II) ions. Biochimie, 76(1), 15-21. https://doi.org/10.1016/0300-9084(94)90058-2
Somavarapu, A. K., Kleijwegt, G., Nagaraj, M., Alam, P., Nielsen, J. & Otzen, D. E. (2023). Drug repurposing screens identify compounds that inhibit α-synuclein oligomers' membrane disruption and block antibody interactions. Chemical Science, 14(11), 3030-3047. https://doi.org/10.1039/d2sc05534a
Otzen, D. (2021). Driving forces in amyloidosis: How does a light chain make a heavy heart? The Journal of Biological Chemistry, 296, 100785. Article 100785. https://doi.org/10.1016/j.jbc.2021.100785
Vad, B. S., Thomsen, L. A. H., Bertelsen, K., Franzmann, M., Pedersen, J. M., Nielsen, S. B., Vosegaard, T., Valnickova, Z., Skrydstrup, T., Enghild, J. J., Wimmer, R., Nielsen, N. C. & Otzen, D. (2010). Divorcing folding from function: how acylation affects the membrane-perturbing properties of an antimicrobial peptide. Biochimica et Biophysica Acta - Proteins and Proteomics, 1804(4), 806-20. https://doi.org/10.1016/j.bbapap.2009.12.006
López Hernández, M., Scavenius, C., Otzen, D. E. & Pedersen, J. S. (2026). Divergent effects of anionic surfactants on laundry enzymes: Structural stability, activity modulation, and self-cleavage mechanisms. International Journal of Biological Macromolecules, 335(1), Article 149069. https://doi.org/10.1016/j.ijbiomac.2025.149069
Nybo, T., Gamon, L. F., Fuentes-Lemus, E., Otzen, D. E., Davies, M. J. & Hägglund, P. (2025). Dimethyl labeling of N-terminal amines allows unambiguous identification of protein crosslinks. Free Radical Biology & Medicine, 227, 629-637. https://doi.org/10.1016/j.freeradbiomed.2024.12.002
Otzen, D. (2008). Differential adsorption of variants of the thermomyces lanuginosus lipase on a hydrophobic surface suggests a role for local flexibility. Colloids and Surfaces B: Biointerfaces, (64), 223-228.
Adão, R., Cruz, P. F., Vaz, D. C., Fonseca, F., Pedersen, J. N., Ferreira-da-Silva, F., Brito, R. M. M., Ramos, C. H. I., Otzen, D., Keller, S. & Bastos, M. (2020). DIBMA nanodiscs keep α-synuclein folded. Biochimica et biophysica acta - Biomembranes, 1862(9), Article 183314. https://doi.org/10.1016/j.bbamem.2020.183314
Jordal, P. L., Dyrlund, T. F., Winge, K., Larsen, M. R., Danielsen, E. H., Wells, J. A., Otzen, D. E. & Enghild, J. J. (2016). Detection of proteolytic signatures for Parkinson's disease. Future Neurology, 11(1), 15-32. https://doi.org/10.2217/fnl.16.3
Kim, J.-Y., Sahu, S., Yau, Y.-H., Wang, X., Shochat, S. G., Nielsen, P. H., Dueholm, M. S., Otzen, D. E., Lee, J., Delos Santos, M. M. S., Yam, J. K. H., Kang, N.-Y., Park, S.-J., Kwon, H., Seviour, T. W., Yang, L., Givskov, M. & Chang, Y.-T. (2016). Detection of pathogenic biofilms with bacterial amyloid targeting fluorescent probe, CDy11. Journal of the American Chemical Society, 138(1), 402-407. https://doi.org/10.1021/jacs.5b11357
Otzen, D. E., Kristensen, O. & Oliveberg, M. (2000). Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly. Proceedings of the National Academy of Sciences (PNAS), 97(18), 9907-9912. https://doi.org/10.1073/pnas.160086297
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.
Heegaard, P. M. P., Boas, U. & Otzen, D. (2007). Dendrimer effects on peptide and protein fibrillation. Macromolecular Bioscience, (7), 1047-1059.
Andersen, K. K. & Otzen, D. (2014). Denaturation of α-lactalbumin and myoglobin by the anionic biosurfactant rhamnolipid. Biochimica et biophysica acta. Bioenergeticss, 1844(12), 2338-2345. https://doi.org/10.1016/j.bbapap.2014.10.005
Otzen, D. E., Pedersen, J. N., Somavarapu, A. K., Clement, A., Ji, M., Petersen, E. H., Pedersen, J. S., Urban, S. & Schafer, N. P. (2021). Cys-labelling kinetics of membrane protein GlpG: a role for specific SDS binding and micelle changes? Biophysical Journal, 120(18), 4115-4128. https://doi.org/10.1016/j.bpj.2021.08.001
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
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., 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.
Dueholm, M. S., Albertsen, M., Otzen, D. & Nielsen, P. H. (2012). Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure. PLoS One, 7(12), e51274. https://doi.org/10.1371/journal.pone.0051274
Amodeo, G. F., Lee, B. Y., Krilyuk, N., Filice, C. T., Valyuk, D., Otzen, D. E., Noskov, S., Leonenko, Z. & Pavlov, E. V. (2021). C subunit of the ATP synthase is an amyloidogenic calcium dependent channel-forming peptide with possible implications in mitochondrial permeability transition. Scientific Reports, 11(1), Article 8744. https://doi.org/10.1038/s41598-021-88157-z
Olsen, W. P., Courtade, G., Peña-Díaz, S., Nagaraj, M., Sønderby, T. V., Mulder, F. A. A., Malle, M. G. & Otzen, D. E. (2024). CsgA gatekeeper residues control nucleation but not stability of functional amyloid. Protein Science, 33(10), Article e5178. https://doi.org/10.1002/pro.5178
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.
Risør, M. W., Juhl, D. W., Bjerring, M., Mathiesen, J., Enghild, J. J., Nielsen, N. C. & Otzen, D. E. (2017). Critical Influence of Cosolutes and Surfaces on the Assembly of Serpin-Derived Amyloid Fibrils. Biophysical Journal, 113(3), 580-596. https://doi.org/10.1016/j.bpj.2017.06.030
Marzookian, K., Aliakbari, F., Hourfar, H., Sabouni, F., Otzen, D. E. & Morshedi, D. (2025). Corrigendum to "The neuroprotective effect of human umbilical cord MSCs-derived secretome against α-synuclein aggregates on the blood-brain barrier" [Int. J. Biol. Macromol. Volume 290 (2025), 140387]. International Journal of Biological Macromolecules, Article 149909. Advance online publication. https://doi.org/10.1016/j.ijbiomac.2025.149909
Otzen, D. E. & Oliveberg, M. (2004). Correspondence between anomalous m- and ΔCp-values in protein folding. Protein Science, 13(12), 3253-3263. https://doi.org/10.1110/ps.04991004
Malmos, K. G., Bjerring, M., Jessen, C. M., Nielsen, E. H. T., Poulsen, E. T., Christiansen, G., Vosegaard, T., Skrydstrup, T., Enghild, J. J., Pedersen, J. S. & Otzen, D. E. (2017). Correction to: How glycosaminoglycans promote fibrillation of salmon calcitonin. Journal of Biological Chemistry, 292(38), 15992. https://doi.org/10.1074/jbc.A116.715466
Stenvang, M., Schafer, N. P., Malmos, K. G., Pérez, A.-M. W., Niembro, O., Sormanni, P., Basaiawmoit, R. V., Christiansen, G., Andreasen, M. & Otzen, D. E. (2018). Corneal dystrophy mutations drive pathogenesis by targeting TGFBIp stability and solubility in a latent amyloid-forming domain. Journal of Molecular Biology, 430(8), 1116-1140. https://doi.org/10.1016/j.jmb.2018.03.001
Paslawski, W., Lillelund, O. K., Kristensen, J. V., Schafer, N. P., Baker, R. P., Urban, S. & Otzen, D. E. (2015). Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops. Proceedings of the National Academy of Sciences (PNAS), 112(6), 7978-7983. https://doi.org/10.1073/pnas.1424751112
Juhl, D. W., Risør, M. W., Scavenius, C., Rasmussen, C. B., Otzen, D., Nielsen, N. C. & Enghild, J. J. (2019). Conservation of the Amyloid Interactome Across Diverse Fibrillar Structures. Scientific Reports, 9(1), Article 3863. https://doi.org/10.1038/s41598-019-40483-z
Otzen, D. E. & Oliveberg, M. (2002). Conformational plasticity in folding of the split β-α-β protein S6: Evidence for burst-phase disruption of the native state. Journal of Molecular Biology, 317(4), 613-627. https://doi.org/10.1006/jmbi.2002.5423
De Prat Gay, G., Ruiz-Sanz, J., Neira, J. L., Corrales, F. J., Otzen, D. E., Ladurner, A. G. & Fersht, A. R. (1995). Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway. Journal of Molecular Biology, 254(5), 968-979. https://doi.org/10.1006/jmbi.1995.0669
Otzen, D. E. (2005). Conformational detours during folding of a collapsed state. Biochimica et Biophysica Acta - Proteins and Proteomics, 1750(2), 146-153. https://doi.org/10.1016/j.bbapap.2005.05.006
Knudsen, A. D., Bennike, T., Kjeldal, H., Birkelund, S., Otzen, D. & Stensballe, A. (2014). Condenser: A statistical aggregation tool for multi-sample quantitative proteomic data from Matrix Science Mascot Distiller™. Journal of Proteomics, 103, 261-266. https://doi.org/10.1016/j.jprot.2014.02.001
Andersen, K. K., Vad, B., Omer, S. & Otzen, D. E. (2016). Concatemers of Outer Membrane Protein A Take Detours in the Folding Landscape. Biochemistry, 55(51), 7123–7140. https://doi.org/10.1021/acs.biochem.6b01153
Poulsen, E. T., Runager, K., Risør, M. W., Dyrlund, T. F., Scavenius, C., Karring, H., Praetorius, J., Vorum, H., Otzen, D. E., Klintworth, G. K. & Enghild, J. J. (2014). Comparison of two phenotypically distinct lattice corneal dystrophies caused by mutations in the transforming growth factor beta induced (TGFBI) gene. Proteomics - Clinical Applications, 8(3-4), 168-177. https://doi.org/10.1002/prca.201300058
Bendtsen, M. K., Nowak, J. S., Paiva, P., López Hernández, M., Ferreira, P., Pedersen, J. S., Bekker, N. S., Viezzi, E., Bisiak, F., Brodersen, D. E., Pedersen, L. H., Zervas, A., Fernandes, P. A., Ramos, M. J., Stougaard, P., Thøgersen, M. S. & Otzen, D. E. (2025). Cold-Active Starch-Degrading Enzymes from a Cold and Alkaline Greenland Environment: Role of Ca2+ Ions and Conformational Dynamics in Psychrophilicity. Biomolecules, 15(3), Article 415. https://doi.org/10.3390/biom15030415
Paslawski, W., Mysling, S., Thomsen, K., Jørgensen, T. J. D. & Otzen, D. (2014). Co-existence of Two Different α-Synuclein Oligomers with Different Core Structures Determined by Hydrogen/Deuterium Exchange Mass Spectrometry. Angewandte Chemie International Edition, 53(29), 7560-7563. https://doi.org/10.1002/anie.201400491
Zhang, S., Andreasen, M., Nielsen, J. T., Liu, L., Nielsen, E. H., Song, J., Ji, G., Sun, F., Skrydstrup, T., Besenbacher, F., Nielsen, N. C., Otzen, D. E. & Dong, M. (2013). Coexistence of ribbon and helical fibrils originating from hIAPP20-29 revealed by quantitative nanomechanical atomic force microscopy. Proceedings of the National Academy of Sciences (PNAS), 110(8), 2798-2803. https://doi.org/10.1073/pnas.1209955110
Nayeri, Z., Aliakbari, F., Afzali, F., Parsafar, S., Gharib, E., Otzen, D. E. & Morshedi, D. (2022). Characterization of exogenous αSN response genes and their relation to Parkinson's disease using network analyses. Frontiers in Pharmacology, 13, Article 966760. https://doi.org/10.3389/fphar.2022.966760
Nesgaard, L. W., Hoffmann, S. V., Andersen, C. B., Malmendal, A. & Otzen, D. (2008). Characterization of Dry Globular Proteins and Protein Fibrils by Synchrotron Radiation Vacuum UV Circular Dichroism. Biopolymers, 89(9), 779-795.
Nagaraj, M., Najarzadeh, Z., Pansieri, J., Biverstål, H., Musteikyte, G., Smirnovas, V., Matthews, S., Emanuelsson, C., Johansson, J., Buxbaum, J. N., Morozova-Roche, L. & Otzen, D. E. (2022). Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation. Chemical Science, 13(2), 536-553. https://doi.org/10.1039/d1sc05790a
Dalsgaard, T. K., Otzen, D., Nielsen, J. H. & Larsen, L. B. (2007). Changes in structures of milk proteins upon photo-oxidation. J. Agr. Food Chem., (55), 10968-10976.

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Lise Refstrup Linnebjerg Pedersen