Publications

Recent publications

Sort by: Date | Author | Title

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

Nielsen, J., Pedersen, J. N., Kleijwegt, G., Nowak, J. S., Nami, F., Johansen, C., Sassetti, E., Berg, B. B., Lyngsø, N. M., Brøchner, B. H., Holm Carlson, J., Simonsen, A. J., Pallisgaard Olsen, W., Simonsen, B. W., Mikkelsen, J. H., Sereika-Bejder, V., Lauritsen, J. A., Merrild, K. F., Malle, M. G. ... Otzen, D. E. (2025). Nanobodies raised against the cytotoxic α-synuclein oligomer are oligomer-specific and promote its cellular uptake. npj biosensing, 2, Article 23. https://doi.org/10.1038/s44328-025-00042-1

Pedersen, J. S., Dikov, D. & Otzen, D. (2006). N- and C-Terminal Hydrophobic Patches Are Involved in Fibrillation of Glucagon. Biochemistry, 45(48), 14503-14512. https://doi.org/10.1021/bi061228n

Mortensen, H. G., Madsen, J. K., Andersen, K. K., Vosegaard, T., Deen, G. R., Otzen, D. E. & Pedersen, J. S. (2017). Myoglobin and α-Lactalbumin Form Smaller Complexes with the Biosurfactant Rhamnolipid Than with SDS. Biophysical Journal, 113(12), 2621-2633. https://doi.org/10.1016/j.bpj.2017.10.024

Underhaug, J., Koldsø, H., Runager, K., Nielsen, J. T., Sørensen, C. S., Kristensen, T., Otzen, D., Karring, H., Malmendal, A., Schiøtt, B., Enghild, J. J. & Nielsen, N. C. (2013). Mutation in transforming growth factor beta induced protein associated with granular corneal dystrophy type 1 reduces the proteolytic susceptibility through local structural stabilization. BBA General Subjects, 1834(12), 2812–2822. https://doi.org/10.1016/j.bbapap.2013.10.008

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

Ferreira, N., Gram, H., Sorrentino, Z. A., Gregersen, E., Schmidt, S. I., Reimer, L., Betzer, C., Perez-Gozalbo, C., Beltoja, M., Nagaraj, M., Wang, J., Nowak, J. S., Dong, M., Willén, K., Cholak, E., Bjerregaard-Andersen, K., Mendez, N., Rabadia, P., Shahnawaz, M. ... Jensen, P. H. (2021). Multiple system atrophy-associated oligodendroglial protein p25α stimulates formation of novel α-synuclein strain with enhanced neurodegenerative potential. Acta Neuropathologica, 142, 87-115. https://doi.org/10.1007/s00401-021-02316-0

Nielsen, S. B., Yde, P., Giehm, L., Sundbye, S., Christiansen, G., Matthiesen, J., Jensen, M. H., Jensen, P. H. & Otzen, D. E. (2012). Multiple Roles of Heparin in the Aggregation of p25α. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2012.01.050

Aliakbari, F., Mohammad-Beigi, H., Abbasi, S., Rezaei-Ghaleh, N., Lermyte, F., Parsafar, S., Becker, S., Tafreshi, A. P., O'Connor, P. B., Collingwood, J. F., Christiansen, G., Sutherland, D. S., Jensen, P. H., Morshedi, D. & Otzen, D. E. (2021). Multiple Protective Roles of Nanoliposome-Incorporated Baicalein against Alpha-Synuclein Aggregates. Advanced Functional Materials, 31(7), Article 2007765. https://doi.org/10.1002/adfm.202007765

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

Nielsen, J., Lauritsen, J., Pedersen, J. N., Nowak, J. S., Bendtsen, M. K., Kleijwegt, G., Lusser, K., Pitarch, L. C., Moreno, J. V., Schneider, M. M., Krainer, G., Goksøyr, L., Khalifé, P., Kaalund, S. S., Aznar, S., Kjærgaard, M., Sereikaité, V., Strømgaard, K., Knowles, T. P. J. ... Otzen, D. E. (2024). Molecular properties and diagnostic potential of monoclonal antibodies targeting cytotoxic α-synuclein oligomers. npj Parkinson's Disease , 10(1), Article 139. https://doi.org/10.1038/s41531-024-00747-6

Sønderby, T. V., Zou, Y., Wang, P., Wang, C. & Otzen, D. E. (2022). Molecular-level insights into the surface-induced assembly of Functional Bacterial Amyloid. Biophysical Journal, 121(18), 3422-3434. https://doi.org/10.1016/j.bpj.2022.08.013

Poghosyan, A. H., Schafer, N., Lyngsø, J., Shahinyan, A. A., Pedersen, J. S. & Otzen, D. (2019). Molecular dynamics study of ACBP denaturation in alkyl sulfates demonstrates possible pathways of unfolding through fused surfactant clusters. Protein Engineering, Design and Selection, 32(4), 175-190. Article gzz037. https://doi.org/10.1093/protein/gzz037

Larsen, K., Bæk, R., Sahin, C., Kjær, L., Christiansen, G., Nielsen, J., Farajzadeh, L. & Otzen, D. E. (2021). Molecular characteristics of porcine alpha-synuclein splicing variants. Biochimie, 180, 121-133. https://doi.org/10.1016/j.biochi.2020.10.019

Pedersen, J. S., Christensen, G. & Otzen, D. E. (2004). Modulation of S6 fibrillation by unfolding rates and gatekeeper residues. Journal of Molecular Biology, 341(2), 575-588. https://doi.org/10.1016/j.jmb.2004.06.020

Andreasen, M., Nielsen, S. B., Mittag, T., Bjerring, M., Nielsen, J. T., Zhang, S., Nielsen, E. H., Jeppesen, M., Christiansen, G., Besenbacher, F., Dong, M., Nielsen, N. C., Skrydstrup, T. & Otzen, D. E. (2012). Modulation of fibrillation of hIAPP core fragments by chemical modification of the peptide backbone. Biochimica et Biophysica Acta - Proteins and Proteomics, 1824(2), 274-85. https://doi.org/10.1016/j.bbapap.2011.10.014

Sehgal, P., Bang Nielsen, S., Pedersen, S., Wimmer, R. & Otzen, D. (2007). Modulation of cutinase structure and stability by phospholipid detergents. Biochim. Biophys. Acta., (1774), 1544-1554.

Umakoshi, H., Persson, J., Kroon, M., Johansson, H. O., Otzen, D. E., Kuboi, R. & Tjerneld, F. (2000). Model process for separation based on unfolding and refolding of chymotrypsin inhibitor 2 in thermoseparating polymer two-phase systems. Journal of Chromatography B: Biomedical Sciences and Applications, 743(1-2), 13-19. https://doi.org/10.1016/S0378-4347(00)00190-0

Mogensen, J. E., Kleinschmidt, J. H., Schmidt, M. A. & Otzen, D. (2005). Misfolding of a bacterial autotransporter. Protein Science, 14, 2814-2827. https://doi.org/10.1110/ps.051628705

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

Peña-Díaz, S., Ferreira, P., Ramos, M. J. & Otzen, D. E. (2024). Mining and engineering activity in catalytic amyloids. Methods in Enzymology, 697, 345-422. https://doi.org/10.1016/bs.mie.2024.03.002

Otzen, D. E., Buell, A. K. & Jensen, H. (2021). Microfluidics and the quantification of biomolecular interactions. Current Opinion in Structural Biology, 70, 8-15. https://doi.org/10.1016/j.sbi.2021.02.006

Schmüser, L., Trefz, M., Roeters, S. J., Beckner, W., Pfaendtner, J., Otzen, D., Woutersen, S., Bonn, M., Schneider, D. & Weidner, T. (2021). Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy. Langmuir : the ACS journal of surfaces and colloids, 37(45), 13452-13459. https://doi.org/10.1021/acs.langmuir.1c02206

Otzen, D. (2014). Membrane protein folding and stability. Archives of Biochemistry and Biophysics, 564, 262-264. https://doi.org/10.1016/j.abb.2014.10.014

Dorosz, J., Gofman, Y., Kolusheva, S., Otzen, D., Ben-Tal, N., Nielsen, N. C. & Jelinek, R. (2010). Membrane Interactions of Novicidin, a Novel Antimicrobial Peptide: Phosphatidylglycerol Promotes Bilayer Insertion. Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 114(34), 11053-60. https://doi.org/10.1021/jp1052248

Mohammad-Beigi, H., Hosseini, A., Adeli, M., Ejtehadi, M. R., Christiansen, G., Sahin, C., Tu, Z., Tavakol, M., Dilmaghani-Marand, A., Nabipour, I., Farzadfar, F., Otzen, D. E., Mahmoudi, M. & Hajipour, M. J. (2019). Mechanistic Understanding of the Interactions between Nano-Objects with Different Surface Properties and α-Synuclein. ACS Nano, 13(3), 3243-3256. https://doi.org/10.1021/acsnano.8b08983

Macchi, F., Hoffmann, S. V., Carlsen, M., Vad, B. S., Imparato, A., Rischel, C. & Otzen, D. (2011). Mechanical stress affects glucagon fibrillation kinetics and fibril structure. Langmuir, 27(20), 12539–12549. https://doi.org/10.1021/la202125c

Otzen, D. E. (2011). Mapping the folding pathway of the transmembrane protein DsbB by protein engineering. Protein Engineering Design and Selection (Print), 24(1-2), 139-149. https://doi.org/10.1093/protein/gzq079

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

Calcutta, A., Jessen, C. M., Behrens, M. A., Oliveira, C. L. P., Renart, M. L., González-Ros, J. M., Otzen, D., Pedersen, J. S., Malmendal, A. & Nielsen, N. C. (2012). Mapping of unfolding states of integral helical membrane proteins by GPS-NMR and scattering techniques: TFE-induced unfolding of KcsA in DDM surfactant. Biochimica et biophysica acta - Biomembranes, 1818(9), 2290-301. https://doi.org/10.1016/j.bbamem.2012.04.005

Shahsavari, S., Rad, M. B., Hajiaghajani, A., Rostami, M., Hakimian, F., Jafarzadeh, S., Hasany, M., Collingwood, J. F., Aliakbari, F., Fouladiha, H., Bardania, H., Otzen, D. E. & Morshedi, D. (2024). Magnetoresponsive liposomes applications in nanomedicine: A comprehensive review. Biomedicine & Pharmacotherapy, 181, Article 117665. https://doi.org/10.1016/j.biopha.2024.117665

Pedersen, J. N., Jiang, Z., Christiansen, G., Lee, J. C., Pedersen, J. S. & Otzen, D. E. (2019). Lysophospholipids induce fibrillation of the repeat domain of Pmel17 through intermediate core-shell structures. Biochimica et Biophysica Acta - Proteins and Proteomics, 1867(5), 519-528. https://doi.org/10.1016/j.bbapap.2018.11.007