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Nielsen, S. B. & Otzen, D. E. (2010). Impact of the antimicrobial peptide Novicidin on membrane structure and integrity. Journal of Colloid and Interface Science, 345(2), 248-256. https://doi.org/10.1016/j.jcis.2010.01.065

Nielsen, M. M., Andersen, K. K., Westh, P. & Otzen, D. (2007). Unfolding of ß-sheet proteins in SDS. Biophysical Journal, (92), 3674-3685.

Nielsen, J. T., Bjerring, M., Jeppesen, M., Pedersen, R. O., Pedersen, J. M., Hein, K. L., Vosegaard, T., Skrydstrup, T., Otzen, D. & Nielsen, N. C. (2009). Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy. Angewandte Chemie International Edition, 48, 2118-2121.

Nielsen, J. T., Bjerring, M., Jeppesen, M., Pedersen, R. O., Pedersen, J. M., Hein, K. L., Vosegaard, T., Skrydstrup, T., Otzen, D. & Nielsen, N. C. (2009). Unique Identification of Supramolecular Structures in Amyloid Fibrils by Solid-State NMR. Poster session presented at 50th Experimental NMR conference (ENC), Asilomar, CA, United States.

Nielsen, S. B., Franzmann, M., Basaiawmoit, R. V., Wimmer, R., Mikkelsen, J. D. & Otzen, D. E. (2010). beta-Sheet aggregation of kisspeptin-10 is stimulated by heparin but inhibited by amphiphiles. Biopolymers, 93(8), 678-89. https://doi.org/10.1002/bip.21434

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

Nielsen, S. B. & Otzen, D. (2013). Quartz crystal microbalances as tools for probing protein-membrane interactions. In J. Kleinschmidt (Ed.), Lipid-Protein Interactions: Methods and Protocols: Methods in Molecular Biology (Vol. 974, pp. 1-21). https://doi.org/10.1007/978-1-62703-275-9_1

Nielsen, S. B., Macchi, F., Raccosta, S., Langkilde, A. E., Giehm, L., Kyrsting, A., Svane, A. S. P., Manno, M., Christiansen, G., Nielsen, N. C., Oddershede, L., Vestergaard, B. & Otzen, D. (2013). Wildtype and A30P Mutant Alpha-Synuclein Form Different Fibril Structures. PLoS One, 8(7), Article e67713. https://doi.org/10.1371/journal.pone.0067713

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

Nielsen, S. B. & Otzen, D. E. (2019). Quartz Crystal Microbalances as Tools for Probing Protein-Membrane Interactions. In J. H. Kleinschmidt (Ed.), Methods in Molecular Biology: Methods and Protocols (Vol. 2003, pp. 31-52). Springer. https://doi.org/10.1007/978-1-4939-9512-7_2

Nielsen, N. S., Poulsen, E. T., Lukassen, M. V., Chao Shern, C., Mogensen, E. H., Weberskov, C. E., DeDionisio, L., Schauser, L., Moore, T. C. B., Otzen, D. E., Hjortdal, J. & Enghild, J. J. (2020). Biochemical mechanisms of aggregation in TGFBI-linked corneal dystrophies. Progress in Retinal and Eye Research, 77, Article 100843. https://doi.org/10.1016/j.preteyeres.2020.100843

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

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

Neumann, J., Klein, N., Otzen, D. & Schneider, D. (2014). Folding energetics and oligomerization of polytopic α-helical transmembrane proteins. Archives of Biochemistry and Biophysics, 564, 281–296. https://doi.org/10.1016/j.abb.2014.07.017

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.

Nesgaard, L. W., Vad, B., Christiansen, G. & Otzen, D. (2009). Kinetic partitioning between aggregation and vesicle permeabilization by modified ADan. Biochimica et Biophysica Acta. Molecular Cell Research, 1794, 84-93.

Neira, J. L., Itzhaki, L. S., Otzen, D. E., Davis, B. & Fersht, A. R. (1997). Hydrogen exchange in chymotrypsin inhibitor 2 probed by mutagenesis. Journal of Molecular Biology, 270(1), 99-110. https://doi.org/10.1006/jmbi.1997.1088

Nedergaard Pedersen, J., Wilhelmus Johannes Maria Frederix, P., Skov Pedersen, J., Marrink, S. J. & Otzen, D. (2018). Role of charge and hydrophobicity in liprotide formation: a molecular dynamics study with experimental constraints. ChemBioChem, 19(3), 263–271. https://doi.org/10.1002/cbic.201700496

Nedergaard Pedersen, J., Skov Pedersen, J. & Otzen, D. E. (2018). Liprotides assist in folding of outer membrane proteins. Protein Science, 27(2), 451-462. https://doi.org/10.1002/pro.3337

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

Najarzadeh, Z., Pedersen, J. N., Christiansen, G., Shojaosadati, S. A., Pedersen, J. S. & Otzen, D. E. (2019). Bacterial amphiphiles as amyloid inducers: Effect of Rhamnolipid and Lipopolysaccharide on FapC fibrillation. Biochimica et Biophysica Acta - Proteins and Proteomics, 1867(11), Article 140263. https://doi.org/10.1016/j.bbapap.2019.140263

Najarzadeh, Z., Mohammad-Beigi, H., Pedersen, J. N., Christiansen, G., Sønderby, T. V., Shojaosadati, S. A., Morshedi, D., Strømgaard, K., Meisl, G., Sutherland, D., Pedersen, J. S. & Otzen, D. (2019). Plant polyphenols inhibit functional amyloid and biofilm formation in Pseudomonas strains by directing monomers to off-pathway oligomers. Biomolecules, 9(11), Article 659. https://doi.org/10.3390/biom9110659

Najarzadeh, Z., Zaman, M., Sereikaite, V., Strømgaard, K., Andreasen, M. & Otzen, D. E. (2021). Heparin promotes fibrillation of most phenol-soluble modulin virulence peptides from Staphylococcus aureus. The Journal of Biological Chemistry, 297(2), 100953. Article 100953. https://doi.org/10.1016/j.jbc.2021.100953

Najarzadeh, Z., Nielsen, J., Farzadfard, A., Sereikaite, V., Strømgaard, K., Meyer, R. L. & Otzen, D. E. (2021). Human Fibrinogen Inhibits Amyloid Assembly of Most Phenol-Soluble Modulins from Staphylococcus aureus. ACS Omega, 6(34), 21960-21970. https://doi.org/10.1021/acsomega.1c02333

Najarzadeh, Z., Mohammad-Beigi, H., Pedersen, J. N., Christiansen, G., Pedersen, J. S., Nielsen, J. & Otzen, D. E. (2022). Interaction of membrane vesicles with the Pseudomonas functional amyloid protein FapC facilitates amyloid formation. BBA advances, 2, Article 100055. https://doi.org/10.1016/j.bbadva.2022.100055

Nagaraj, M., Ahmed, M., Lyngsø, J., Vad, B. S., Bøggild, A., Fillipsen, A., Pedersen, J. S., Otzen, D. E. & Akbey, Ü. (2020). Predicted Loop Regions Promote Aggregation: A Study of Amyloidogenic Domains in the Functional Amyloid FapC. Journal of Molecular Biology, 432(7), 2232-2252. https://doi.org/10.1016/j.jmb.2020.01.044

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

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

Mortensen, H. G., Otzen, D. E. & Pedersen, J. S. (2021). Ubiquitin forms conventional decorated micelle structures with sodium dodecyl sulfate at saturation. Journal of Colloid and Interface Science, 596, 233-244. https://doi.org/10.1016/j.jcis.2021.03.110

Morgensen, JE., Ferreras, M., Wimmer, R., Petersen, S. V., Enghild, J. J. & Otzen, D. (2007). The Major Allergen from Birch Tree Pollen, Bet v 1, Binds and Permeabilizes Membranes. Biochemistry.

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

Mohammad-Beigi, H., Shojaosadati, S. A., Marvian, A. T., Pedersen, J. N., Klausen, L. H., Christiansen, G., Pedersen, J. S., Dong, M., Morshedi, D. & Otzen, D. E. (2015). Strong interactions with polyethylenimine-coated human serum albumin nanoparticles (PEI-HSA NPs) alter α-synuclein conformation and aggregation kinetics. Nanoscale, 7, 19627-19640. https://doi.org/10.1039/c5nr05663b

Mohammad-Beigi, H., Morshedi, D., Shojaosadati, S. A., Pedersen, J. N., Marvian, A. T., Aliakbari, F., Christiansen, G., Pedersen, J. S. & Otzen, D. E. (2016). Gallic acid loaded onto polyethylenimine-coated human serum albumin nanoparticles (PEI-HSA-GA NPs) stabilizes α-synuclein in the unfolded conformation and inhibits aggregation. RSC Advances, 6(88), 85312-85323. https://doi.org/10.1039/c6ra08502d

Mohammad-Beigi, H., Aliakbari, F., Sahin, C., Lomax, C., Tawfike, A., P. Schafer, N., Amiri-Nowdijeh, A., Eskandari, H., Møller, I. M., Hosseini-Mazinani, M., Christiansen, G., Ward, J. L., Morshedi, D. & Otzen, D. (2019). Oleuropein derivatives from olive fruit extracts reduce α-synuclein fibrillation and oligomer toxicity. Journal of Biological Chemistry, 294(11), 4215-4232. https://doi.org/10.1074/jbc.RA118.005723

Mohammad-Beigi, H., Kjær, L., Eskandari, H., Aliakbari, F., Christiansen, G., Ruvo, G., L. Ward, J. & Otzen, D. (2019). A Possible Connection Between Plant Longevity and the Absence of Protein Fibrillation: Basis for Identifying Aggregation Inhibitors in Plants. Frontiers in Plant Science, 10(148), Article 148. https://doi.org/10.3389/fpls.2019.00148

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

Mohammad-Beigi, H., Zanganeh, M., Scavenius, C., Eskandari, H., Farzadfard, A., Shojaosadati, S. A., Enghild, J. J., Otzen, D. E., Buell, A. K. & Sutherland, D. S. (2022). A Protein Corona Modulates Interactions of α-Synuclein with Nanoparticles and Alters the Rates of the Microscopic Steps of Amyloid Formation. ACS Nano, 16(1), 1102-1118. https://doi.org/10.1021/acsnano.1c08825

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

Mogensen, J. E., Tapadar, D., Schmidt, M. A. & Otzen, D. (2005). Barriers to Folding of the Transmembrane Domain of the Escherichia coli Autotransporter Adhesin Involved in Diffuse Adherence. Biochemistry, 44, 4533-4545. https://doi.org/10.1021/bi0475121

Mogensen, J. E., Sehgal, P. & Otzen, D. (2005). Activation, Inhibition, and Destabilization of Thermomyces lanuginosus Lipase by Detergents. Biochemistry, 44(5), 1719-1730. https://doi.org/10.1021/bi0479757

Mogensen, J. E. & Otzen, D. E. (2005). Interactions between folding factors and bacterial outer membrane proteins. Molecular Microbiology, 57(2), 326-346. https://doi.org/10.1111/j.1365-2958.2005.04674.x

Mogensen, J. E., Ipsen, H., Holm, J. & Otzen, D. E. (2004). Elimination of A Misfolded Folding Intermediate by A Single Point Mutation. Biochemistry, 43(12), 3357-3367. https://doi.org/10.1021/bi0358622

Mogensen, J. E., Wimmer, R., Larsen, J. N., Spangfort, M. D. & Otzen, D. E. (2002). The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands. Journal of Biological Chemistry, 277(26), 23684-23692. https://doi.org/10.1074/jbc.M202065200

Mittag, T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2009). Synthesis of a Ketomethylene Isostere of the Fibrillating Peptide SNNFGAILSS. Journal of Organic Chemistry, 74, 7955-7957.

Mishra, A., Golbek, T. W., Thomassen, A. B., Zuzic, L., Schmüser, L., Saeed, K. H., Madzharova, F., Nielsen, J., Schiøtt, B., Otzen, D. E. & Weidner, T. (2025). Pathological Folding of α-Synuclein on Polystyrene Nanoplastic Revealed by Sum Frequency Scattering and 2D Infrared Spectroscopy. The Journal of Physical Chemistry Letters, 16(45), 11893-11900. https://doi.org/10.1021/acs.jpclett.5c02526

Mirab, F., Pirhaghi, M., Otzen, D. E. & Saboury, A. A. (2025). Parkinson's disease and gut microbiota metabolites: The dual impact of vitamins and functional amyloids. B B A - Molecular Basis of Disease, 1871(6), Article 167862. https://doi.org/10.1016/j.bbadis.2025.167862

Minero, G. A. S., Møllebjerg, A., Thiesen, C., Johansen, M. I., Jørgensen, N. P., Birkedal, V., Otzen, D. E. & Meyer, R. L. (2024). Extracellular G-quadruplexes and Z-DNA protect biofilms from DNase I, and G-quadruplexes form a DNAzyme with peroxidase activity. Nucleic Acids Research, 52(4), 1575-1590. https://doi.org/10.1093/nar/gkae034

Milanetti, E., Miotto, M., Di Rienzo, L., Nagaraj, M., Monti, M., Golbek, T. W., Gosti, G., Roeters, S. J., Weidner, T., Otzen, D. E. & Ruocco, G. (2021). In-Silico Evidence for a Two Receptor Based Strategy of SARS-CoV-2. Frontiers in Molecular Biosciences, 8, Article 690655. https://doi.org/10.3389/fmolb.2021.690655

Michaels, T. C. T., Yde, P., Willis, J. C. W., Jensen, M. H., Otzen, D., Dobson, C. M., Buell, A. K. & Knowles, T. P. J. (2015). The length distribution of frangible biofilaments. Journal of Chemical Physics, 143(16), 1-15. Article 164901. https://doi.org/10.1063/1.4933230

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

Displaying results 201 to 250 out of 469

Revised 08.12.2025

Lise Refstrup Linnebjerg Pedersen