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van Diggelen, F., Tepper, A., Petri, M. & Otzen, D. (2017). α-Synuclein Oligomers: A Study in Diversity. Israel Journal of Chemistry, 57(7), 699-723. https://doi.org/10.1002/ijch.201600116
Otzen, D., Sehgal, P. & Westh, P. (2009). α-lactalbumin is unfolded by all classes of detergents but with different mechanisms. Journal of Colloid and Interface Science, 329, 273-283.
Otzen, D. & Nielsen, P. H. (2008). We find them here, we find them there: Functional bacterial amyloid. Cellular and Molecular Life Sciences, 65, 910-927.
Sehgal, P., Mogensen, J. E. & Otzen, D. (2005). Using micellar mole fractions to assess membrane protein stability in mixed micelles. Biochimica et biophysica acta - Biomembranes, 1761, 59-68. https://doi.org/10.1016/j.bbamem.2005.08.006
Paiva, P., Teixeira, L. M. C., Wei, R., Liu, W., Weber, G., Morth, J. P., Westh, P., Petersen, A. R., Johansen, M. B., Sommerfeldt, A., Sandahl, A., Otzen, D. E., Fernandes, P. A. & Ramos, M. J. (2025). Unveiling the enzymatic pathway of UMG-SP2 urethanase: insights into polyurethane degradation at the atomic level. Chemical Science, 16(5), 2437-2452. https://doi.org/10.1039/d4sc06688j
Nielsen, M. M., Andersen, K. K., Westh, P. & Otzen, D. (2007). Unfolding of ß-sheet proteins in SDS. Biophysical Journal, (92), 3674-3685.
Meisl, G., Xu, C. K., Taylor, J. D., Michaels, T. C. T., Levin, A., Otzen, D., Klenerman, D., Matthews, S., Linse, S., Andreasen, M. & Knowles, T. P. J. (2022). Uncovering the universality of self-replication in protein aggregation and its link to disease. Science Advances, 8(32), Article eabn6831. https://doi.org/10.1126/sciadv.abn6831
Monti, M., Milanetti, E., Frans, M. T., Miotto, M., Di Rienzo, L., Baranov, M. V., Gosti, G., Somavarapu, A. K., Nagaraj, M., Golbek, T. W., Rossing, E., Moons, S. J., Boltje, T. J., van den Bogaart, G., Weidner, T., Otzen, D. E., Tartaglia, G. G., Ruocco, G. & Roeters, S. J. (2024). Two Receptor Binding Strategy of SARS-CoV-2 Is Mediated by Both the N-Terminal and Receptor-Binding Spike Domain. The journal of physical chemistry. B, 128(2), 451-464. https://doi.org/10.1021/acs.jpcb.3c06258
Melo, E. P., Chen, L. Y., Cabral, J. M. S., Fojan, P., Petersen, S. B. & Otzen, D. E. (2003). Trehalose favors a cutinase compact intermediate off-folding pathway. Biochemistry, 42(24), 7611-7617. https://doi.org/10.1021/bi034267x
Paiva, P., Teixeira, L. M. C., Ferreira, P., Otzen, D. E., Fernandes, P. A. & Ramos, M. J. (2025). Transforming Computational Power into Environmental Solutions: HPC-driven Research on Urethanase-mediated Plastic Degradation. Procedia Computer Science, 267, 207-217. https://doi.org/10.1016/j.procs.2025.08.247
Schafer, N., Truong, H. H., Otzen, D., Lindorff-Larsen, K. & Wolynes, P. G. (2016). Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease. Proceedings of the National Academy of Sciences (PNAS), 113(8), 2098-2103. https://doi.org/10.1073/pnas.1524027113
Malmos, K., Blancas-Mejia, L. M., Weber, B., Buchner, J., Ramirez-Alvarado, M., Naiki, H. & Otzen, D. (2017). ThT 101: a primer on the use of thioflavin T to investigate amyloid formation. Amyloid: the Journal of Protein Folding Disorders, 24(1), 1-16. https://doi.org/10.1080/13506129.2017.1304905
Basaiawmoit, R. V., Deva, T., Runager, K., Kristensen, T., Enghild, J. J. & Otzen, D. (2009). The Underlying Mechanisms of TGFBIp-mediated Corneal Dystrophies. Abstract from Asia ARVO, International Meeting on Research in Vision and Ophthalmology, Hyderabad International Convention Center. Abstract number: PAP05.01, Hyderabad, India.
Marvian, A. T., Aliakbari, F., Mohammad-Beigi, H., Ahmadi, Z. A., Mehrpouyan, S., Lermyte, F., Nasouti, M., Collingwood, J. F., Otzen, D. E. & Morshedi, D. (2020). The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization. International Journal of Biological Macromolecules, 155, 543-550. https://doi.org/10.1016/j.ijbiomac.2020.03.238
Cavallin, A., Arozenius, H., Kristensson, K., Antonsson, P., Otzen, D. E., Björk, P. & Forsberg, G. (2000). The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function. Journal of Biological Chemistry, 275(3), 1665-1672. https://doi.org/10.1074/jbc.275.3.1665
Andersen, K., Oliveira, C. L. P. D., Larsen, K. L., Poulsen, F., Callisen, T., Westh, P., Pedersen, J. S. & Otzen, D. (2009). The role of decorated SDS micelles in sub-cmc protein denaturation and association. Journal of Molecular Biology, 391, 207-226.
Baptista, R. P., Pedersen, S. H., Cabrita, G. J. M., Otzen, D., Cabral, J. M. & Melo, E. P. (2008). Thermodynamics and mechanism of cutinase stabilization by trehalose. Biopolymers, 89, 538-547.
Aliakbari, F., Mohammad-Beigi, H., Rezaei-Ghaleh, N., Becker, S., Dehghani Esmatabad, F., Eslampanah Seyedi, H. A., Bardania, H., Tayaranian Marvian, A., Collingwood, J. F., Christiansen, G., Zweckstetter, M., Otzen, D. E. & Morshedi, D. (2018). The potential of zwitterionic nanoliposomes against neurotoxic alpha-synuclein aggregates in Parkinson's Disease. Nanoscale, 10(19), 9174-9185. https://doi.org/10.1039/c8nr00632f
Dyla, M., González Foutel, N. S., Otzen, D. E. & Kjaergaard, M. (2022). The optimal docking strength for reversibly tethered kinases. Proceedings of the National Academy of Sciences (PNAS), 119(25), Article e2203098119. https://doi.org/10.1073/pnas.2203098119