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Christophersen, C., Otzen, D. E., Norman, B. E., Christensen, S. & Schäfer, T. (1998). Enzymatic characterisation of novamyl®, a thermostable α-amylase. Starch/Staerke, 50(1), 39-45. https://doi.org/10.1002/(SICI)1521-379X(199801)50:1<39::AID-STAR39>3.0.CO;2-S
Bendtsen, M. K., Møllebjerg, A., Peña-Díaz, S., Graham, R., Petersen, N. C., Isaksen, B. N., Carstensen, M., Johansen, M. B., Sommerfeldt, A., Petersen, A. R., Chuma, I. K., Ryberg, C., Wittenborn, T. R., Gichuru, V., Wang, H., Scavenius, C., Sandahl, A. & Otzen, D. E. (2026). Environmental Identification of Novel Enzymes for Polyurethane and Polyamide Degradation. Angewandte Chemie International Edition, 65(35), Article e6159643. https://doi.org/10.1002/anie.6159643
Nielsen, J. E., Beier, L., Otzen, D., Borchert, T. V., Frantzen, H. B., Andersen, K. V. & Svendsen, A. (1999). Electrostatics in the active site of an α-amylase. European Journal of Biochemistry, 264(3), 816-824. https://doi.org/10.1046/j.1432-1327.1999.00664.x
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.
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.
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
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
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
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.
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
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