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Otzen, D. E., Kristensen, O., Proctor, M. & Oliveberg, M. (1999). Structural changes in the transition state of protein folding: Alternative interpretations of curved chevron plots. Biochemistry, 38(20), 6499-6511. https://doi.org/10.1021/bi982819j

Otzen, D. E. & Fersht, A. R. (1998). Folding of circular and permuted chymotrypsin inhibitor 2: Retention of the folding nucleus. Biochemistry, 37(22), 8139-8146. https://doi.org/10.1021/bi980250g

Otzen, D. E., Rheinnecker, M. & Fersht, A. R. (1995). Structural Factors Contributing to the Hydrophobic Effect: The Partly Exposed Hydrophobic Minicore in Chymotrypsin Inhibitor. Biochemistry, 34(40), 13051-13058. https://doi.org/10.1021/bi00040a016

Otzen, D. E. & Fersht, A. R. (1995). Side-Chain Determinants of β-Sheet Stability. Biochemistry, 34(17), 5718-5724. https://doi.org/10.1021/bi00017a003

Otzen, D. E., Barciszewski, J. & Clark, B. F. C. (1994). Dual hydrolytic role for Pb(II) ions. Biochimie, 76(1), 15-21. https://doi.org/10.1016/0300-9084(94)90058-2

Otzen, D. E., Itzhaki, L. S., Elmasry, N. F., Jackson, S. E. & Fersht, A. R. (1994). Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding. Proceedings of the National Academy of Sciences, 91(22), 10422-10425. https://doi.org/10.1073/pnas.91.22.10422

Otzen, D. E., Barciszewski, J. & Clark, B. F. C. (1993). Altered lead(II)-cleavage pattern of free Phe-tRNA(Phe) and Phe-tRNA(Phe) in ternary complex with EF-Tu:GTP. Biochemistry and Molecular Biology International, 31(1), 95-103.

Otzen, D. & Riek, R. (2019). Functional Amyloids. Cold Spring Harbor Perspectives in Biology, 11(12), Article a033860. https://doi.org/10.1101/cshperspect.a033860

Otzen, D. E., Morshedi, D., Mohammad-Beigi, H. & Aliakbari, F. (2021). A Triple Role for a Bilayer: Using Nanoliposomes to Cross and Protect Cellular Membranes. Journal of Membrane Biology, 254(1), 29-39. https://doi.org/10.1007/s00232-020-00159-6

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

Otzen, D. (2021). Driving forces in amyloidosis: How does a light chain make a heavy heart? The Journal of Biological Chemistry, 296, 100785. Article 100785. https://doi.org/10.1016/j.jbc.2021.100785

Otzen, D. E., Pedersen, J. N., Somavarapu, A. K., Clement, A., Ji, M., Petersen, E. H., Pedersen, J. S., Urban, S. & Schafer, N. P. (2021). Cys-labelling kinetics of membrane protein GlpG: a role for specific SDS binding and micelle changes? Biophysical Journal, 120(18), 4115-4128. https://doi.org/10.1016/j.bpj.2021.08.001

Otzen, D. E., Dueholm, M. S., Najarzadeh, Z., Knowles, T. P. J. & Ruggeri, F. S. (2021). In situ Sub-Cellular Identification of Functional Amyloids in Bacteria and Archaea by Infrared Nanospectroscopy. Small Methods, 5(6), Article 2001002. https://doi.org/10.1002/smtd.202001002

Otzen, D. E., Pedersen, J. N., Rasmussen, H. Ø. & Pedersen, J. S. (2022). How do surfactants unfold and refold proteins? Advances in Colloid and Interface Science, 308, Article 102754. https://doi.org/10.1016/j.cis.2022.102754

Otzen, D. E. (2022). Functional amyloid in a lipid-like environment: a merry dance of many steps. Essays in Biochemistry, 66(7), 1035-1046. https://doi.org/10.1042/EBC20220062

Otzen, D. E. (2023). Antibodies and α-synuclein: What to target against Parkinson's Disease? B B A - Proteins and Proteomics, 140943. Article 140943. Advance online publication. https://doi.org/10.1016/j.bbapap.2023.140943

Oliveira, C. L. P. D., Behrens, M. A., Pedersen, J. S., Erlacher, K., Otzen, D. & Pedersen, J. S. (2009). SAXS Study of Glucagon Fibrillation: From Monomers to Fibers. Journal of Molecular Biology, 387, 147-161.

Oeemig, J. S., Lynggaard, C., Knudsen, D., Hansen, F. T., Noergaard, K. D., Schneider, T., Vad, B. S., Sandvang, D., Nielsen, L., Neve, S., Kristensen, H-H., Sahl, H-G., Otzen, D. & Wimmer, R. (2012). Eurocin, a new fungal defensin: structure, lipid binding and its mode of action. Journal of Biological Chemistry, 7, 42361-42372. https://doi.org/10.1074/jbc.M112.382028

Noji, M., Samejima, T., Yamaguchi, K., So, M., Yuzu, K., Chatani, E., Akazawa-Ogawa, Y., Hagihara, Y., Kawata, Y., Ikenaka, K., Mochizuki, H., Kardos, J., Otzen, D. E., Bellotti, V., Buchner, J. & Goto, Y. (2021). Breakdown of supersaturation barrier links protein folding to amyloid formation. Communications Biology, 4(1), Article 120. https://doi.org/10.1038/s42003-020-01641-6

Nissen, S. K., Shrivastava, K., Schulte, C., Otzen, D. E., Goldeck, D., Berg, D., Møller, H. J., Maetzler, W. & Romero-Ramos, M. (2019). Alterations in Blood Monocyte Functions in Parkinson's Disease. Movement Disorders, 34(11), 1711-1721. https://doi.org/10.1002/mds.27815

Nielsen, S. B., Wilhelm, K., Vad, B., Schleucher, J., Morozova-Roche, L. A. & Otzen, D. (2010). The interaction of equine lysozyme:oleic acid complexes with lipid membranes suggests a cargo off-loading mechanism. Journal of Molecular Biology, 398(2), 351-61. https://doi.org/10.1016/j.jmb.2010.03.012

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. P L o S 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

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. B B A - 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. B B A - 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, 100055. 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.

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

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