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Matouschek, A., Otzen, D. E., Itzhaki, L. S., Jackson, S. E. & Fersht, A. R. (1995). Movement of the Position of the Transition State in Protein Folding. Biochemistry, 34(41), 13656-13662. https://doi.org/10.1021/bi00041a047
Marzookian, K., Aliakbari, F., Hourfar, H., Sabouni, F., Otzen, D. E. & Morshedi, D. (2025). The neuroprotective effect of human umbilical cord MSCs-derived secretome against α-synuclein aggregates on the blood-brain barrier. International Journal of Biological Macromolecules, 304(Part 1), Article 140387. https://doi.org/10.1016/j.ijbiomac.2025.140387
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
Martins, P. M., Navarro, S., Silva, A., Pinto, M. F., Sárkány, Z., Figueiredo, F., Pereira, P. J. B., Pinheiro, F., Bednarikova, Z., Burdukiewicz, M., Galzitskaya, O. V., Gazova, Z., Gomes, C. M., Pastore, A., Serpell, L. C., Skrabana, R., Smirnovas, V., Ziaunys, M., Otzen, D. E. ... Macedo-Ribeiro, S. (2020). MIRRAGGE - Minimum Information Required for Reproducible AGGregation Experiments. Frontiers in Molecular Neuroscience, 13, Article 582488. https://doi.org/10.3389/fnmol.2020.582488
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
Malmos, K. G. & Otzen, D. E. (2013). Glycosaminoglycans and Fibrillar Polymorphism. In Bio-nanoimaging: Protein Misfolding and Aggregation (pp. 281-290). Elsevier Inc.. https://doi.org/10.1016/B978-0-12-394431-3.00026-2
Macchi, F., Eisenkolb, M., Kiefer, H. & Otzen, D. (2012). The effect of osmolytes on protein fibrillation. International Journal of Molecular Sciences (Online), 13(3), 3801-3819. https://doi.org/10.3390/ijms13033801
Lorenzen, N., E. Wanker, E. & Otzen, D. (2013). Inhibitors of amyloid and oligomer formation. In D. E. Otzen (Ed.), Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties (pp. 345-372). Wiley-VCH. https://doi.org/10.1002/9783527654185
Lorenzen, N., Cohen, S. I. A., Nielsen, S. B., Herling, T. W., Christiansen, G., Dobson, C. M., T. P. Knowles, T. & Otzen, D. (2012). Role of elongation and secondary pathways in S6 amyloid fibril growth. Biophysical Journal, 102(9), 2167-2175. https://doi.org/10.1016/j.bpj.2012.03.047
Lopes, P., Dyrnesli, H., Lorenzen, N., Otzen, D. & Ferapontova, E. (2013). Electroanalysis of Amyloid Formation of Parkinson's Disease alpha-Synuclein. Abstract from 6th International Workshop on Surface Modification for Chemical and Biochemical Sensing, Warsaw, Poland.
Lindberg, M. O., Tångrot, J., Otzen, D. E., Dolgikh, D. A., Finkelstein, A. V. & Oliveberg, M. (2001). Folding of circular permutants with decreased contact order: General trend balanced by protein stability. Journal of Molecular Biology, 314(4), 891-900. https://doi.org/10.1006/jmbi.2001.5186
Larsen, P., Dueholm, M. S., Christiansen, G., Nielsen, J. L., Otzen, D. & Nielsen, P. H. (2007). Amyloid adhesins are abundant in natural biofilms. Env. Microbiol., (9), 3077-3090.
Larsen, P., Nielsen, J. L. & Otzen, D. (2008). Amyloid-like adhesins in floc-forming and filamentous bacteria in activated sludge. Applied and Environmental Microbiology, 74, 1517-1526.
Kronqvist, N., Otikovs, M., Chmyrov, V., Chen, G., Andersson, M., Nordling, K., Landreh, M., Sarr, M., Jörnvall, H., Wennmalm, S., Widengren, J., Meng, Q., Rising, A., Otzen, D., Knight, S. D., Jaudzems, K. & Johansson, J. (2014). Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation. Nature Communications, 5, Article 3254. https://doi.org/10.1038/ncomms4254
Košmrlj, A., Cordsen, P., Kyrsting, A., Otzen, D., Oddershede, L. B. & Jensen, M. H. (2015). A monomer-trimer model supports intermittent glucagon fibril growth. Scientific Reports, 5, 1-6. Article 9005. https://doi.org/10.1038/srep09005
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.
Knudsen, L. J., Nielsen, S. D.-H., Rauh, V., Otzen, D., Dekker, P. J. T. & Larsen, L. B. (2019). Interrelations between chemical changes in lactose-free UHT milk. Abstract from 16th Symposium on Milk Genomics and Human Health, Aarhus, Denmark.
Knudsen, L. J., Nielsen, S. D.-H., Rauh, V., Otzen, D. & Larsen, L. B. (2019). New Lactase Enzymes. Abstract from Sandbjerg Seminar 2019, Sønderborg, Denmark.
Knudsen, L. J., Nielsen, S. D., Rauh, V., Otzen, D., Dekker, P. J. T. & Larsen, L. B. (2019). Interrelations between chemical changes in lactose-free UHT milk. Abstract from Sandbjerg Seminar 2019, Sønderborg, Denmark.
Kjær, L., Giehm, L., Heimburg, T. R. & Otzen, D. (2009). The influence of vesicle composition and size on a-synuclein structure and stability. Biophysical Journal, 96.
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