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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

Hyldgaard, M., Mygind, T., Vad, B. S., Stenvang, M., Otzen, D. & Meyer, R. L. (2014). The Antimicrobial Mechanism of Action of Epsilon-Poly-L-Lysine. Applied and Environmental Microbiology, 80(24), 7758-7770 . https://doi.org/10.1128/AEM.02204-14

Andreasen, M., Skeby, K. K., Zhang, S., Nielsen, E. H., Klausen, L. H., Frahm, H., Christiansen, G., Skrydstrup, T., Dong, M., Schiøtt, B. & Otzen, D. (2014). The Importance of Being Capped: Terminal Capping of an Amyloidogenic Peptide Affects Fibrillation Propensity and Fibril Morphology. Biochemistry, 53(44), 6968-6980. https://doi.org/10.1021/bi500674u

Stenvang, M. R., Andreasen, M. & Otzen, D. (2014). The Molecular Basis for TGFBIp-Related Corneal Dystrophies. In Bio-nanoimaging : Protein Misfolding and Aggregation (pp. 179-188). Elsevier. https://doi.org/10.1016/B978-0-12-394431-3.00016-X

Lorenzen, N., Lemminger, L., Pedersen, J. N., Nielsen, S. B. & Otzen, D. (2014). The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes. FEBS Letters, 588(3), 497-502. https://doi.org/10.1016/j.febslet.2013.12.015

Lorenzen, N., Nielsen, S. B., Buell, A. K., Kaspersen, J. D., Arosio, P., Vad, B. S., Paslawski, W., Christiansen, G., Valnickova Hansen, Z., Andreasen, M., Enghild, J. J., Pedersen, J. S., Dobson, C. M., Knowles, T. P. J. & Otzen, D. (2014). The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation. Journal of the American Chemical Society, 136(10), 3859-3868. https://doi.org/10.1021/ja411577t

Zhang, S., Andreasen, M., Nielsen, J. T., Liu, L., Nielsen, E. H., Song, J., Ji, G., Sun, F., Skrydstrup, T., Besenbacher, F., Nielsen, N. C., Otzen, D. E. & Dong, M. (2013). Coexistence of ribbon and helical fibrils originating from hIAPP20-29 revealed by quantitative nanomechanical atomic force microscopy. Proceedings of the National Academy of Sciences (PNAS), 110(8), 2798-2803. https://doi.org/10.1073/pnas.1209955110

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.

Dueholm, M. S., Otzen, D. & Nielsen, P. H. (2013). Evolutionary Insight into the Functional Amyloids of the Pseudomonads. PLoS One, 8(10), 1-9. Article e76630. https://doi.org/10.1371/journal.pone.0076630

Giehm, L. & Otzen, D. (2013). Experimental Approaches to Inducing Amyloid Aggregates. In Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties (pp. 295-320). Wiley-VCH. https://doi.org/10.1002/9783527654185.ch14

Dueholm, M. S., Søndergaard, M., Nilsson, M., Christiansen, G., Stensballe, A., Overgaard, M. T., Givskov, M. C., Tolker-Nielsen, T., Otzen, D. & Nielsen, P. H. (2013). Expression of Fap amyloids in Pseudomonas aeruginosa, P. fluorescens, and P. putida results in aggregation and increased biofilm formation. MicrobiologyOpen, 2(3), 365-382. https://doi.org/10.1002/mbo3.81

Fändrich, M., Wulff, M., Pedersen, J. S. & Otzen, D. (2013). Fibrillar Polymorphism. In Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties (pp. 321-343). Wiley-VCH. https://doi.org/10.1002/9783527654185.ch15

Otzen, D. & Andersen, K. K. (2013). Folding of outer membrane proteins. Archives of Biochemistry and Biophysics, 531(1-2), 34-43. https://doi.org/10.1016/j.abb.2012.10.008

Abelein, A., Kaspersen, J. D., Nielsen, S. B., Jensen, G. V., Christiansen, G., Pedersen, J. S., Danielsson, J. A., Otzen, D. & Gräslund, A. (2013). Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates. Journal of Biological Chemistry, 288, 23518-23528. https://doi.org/10.1074/jbc.M113.470450

Dueholm, M. S., Nielsen, P. H., Chapman, M. & Otzen, D. (2013). Functional Amyloids in Bacteria. In Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties (pp. 411-438). Wiley-VCH. https://doi.org/10.1002/9783527654185.ch19

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

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

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

Balakrishnan, V. S., Vad, B. S. & Otzen, D. (2013). Novicidin's membrane permeabilizing activity is driven by membrane partitioning but not by helicity: A biophysical study of the impact of lipid charge and cholesterol. BBA General Subjects, 1834(6), 996-1002. https://doi.org/10.1016/j.bbapap.2013.03.025

Deva, T., Lorenzen, N., Vad, B. S., Petersen, S. V., Thørgersen, I., Enghild, J. J., Kristensen, T. & Otzen, D. (2013). Off-pathway aggregation can inhibit fibrillation at high protein concentrations. BBA General Subjects, 1834(3), 677-687. https://doi.org/10.1016/j.bbapap.2012.12.020

Wang, H., Andersen, K. K., Vad, B. S. & Otzen, D. E. (2013). OmpA can form folded and unfolded oligomers. Biochimica et Biophysica Acta - Proteins and Proteomics, 1834(1), 127-136. https://doi.org/10.1016/j.bbapap.2012.09.002

Wang, H., Andersen, K. K., Sehgal, P., Hagedorn, J., Westh, P., Borch, K. & Otzen, D. E. (2013). pH regulation of the kinetic stability of the lipase from Thermomyces lanuginosus. Biochemistry, 52(1), 264-276. https://doi.org/10.1021/bi301258e

Cohen, S. I. A., Linse, S., Luheshi, L. M., Hellstrand, E., White, D. A., Rajah, L., Otzen, D., Vendruscolo, M., Dobson, C. M. & Knowles, T. P. J. (2013). Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. Proceedings of the National Academy of Sciences (PNAS), 110(24), 9758-9763. https://doi.org/10.1073/pnas.1218402110

Brinkmann, C. R., Thiel, S. & Otzen, D. (2013). Protein:fatty acid complexes: Biochemistry, biophysics and function. FEBS journal, 280(8), 1733–1749. https://doi.org/10.1111/febs.12204

Pigolotti, S., Lizana, L., Otzen, D. & Sneppen, K. (2013). Quality control system response to stochastic growth of amyloid fibrils. FEBS Letters, 587(9), 1405-1410. https://doi.org/10.1016/j.febslet.2013.03.018

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

Helwig, M., Hoshino, A., Berridge, C., Lee, S.-N., Lorenzen, N., Otzen, D., Eriksen, J. & Lindberg, I. (2013). The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins. Journal of Biological Chemistry, 288(2), 1114.

Wang, H., Hagedorn, J., Svendsen, A., Borch, K. & Otzen, D. (2013). Variant of the Thermomyces lanuginosus lipase with improved kinetic stability: a candidate for enzyme replacement therapy. Biophysical Chemistry, 172, 43-52. https://doi.org/10.1016/j.bpc.2012.12.003

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

Andersen, K. K., Wang, H. & Otzen, D. (2012). A Kinetic Analysis of the Folding and Unfolding of OmpA in Urea and Guaninidinium Chloride: Single and Parallel Pathways. Biochemistry, 51(42), 8371-8383. https://doi.org/10.1021/bi300974y

Weber, M., Tome, L., Otzen, D. & Schneider, D. (2012). A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer. BBA General Subjects, 1818(9), 2103-7. https://doi.org/10.1016/j.bbamem.2012.04.003

Dueholm, M. S., Albertsen, M., Otzen, D. & Nielsen, P. H. (2012). Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure. PLoS One, 7(12), e51274. https://doi.org/10.1371/journal.pone.0051274

Hjørringgaard, C. U., Vad, B. S., Matchkov, V., Nielsen, S. B., Vosegaard, T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2012). Cyclodextrin-Scaffolded Alamethicin with Remarkably Efficient Membrane Permeabilizing Properties and Membrane Current Conductance. Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 116(26), 7652-7659. https://doi.org/10.1021/jp2098679

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

Otzen, D., Blans, K., Wang, H., Gilbert, G. E. & Rasmussen, J. T. (2012). Lactadherin binds to phosphatidylserine-containing vesicles in a two-step mechanism sensitive to vesicle size and composition. BBA General Subjects, 1818(4), 1019-1027. https://doi.org/10.1016/j.bbamem.2011.08.032

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

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

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

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

Otzen, D. (2012). N for AsN - O for StrOcture? A strand-loop-strand motif for prokaryotic O-glycosylation. Molecular Oral Microbiology. https://doi.org/10.1111/j.1365-2958.2012.07972.x

Andreasen, M., Nielsen, S. B., Runager, K., Christiansen, G., Nielsen, N. C., Enghild, J. J. & Otzen, D. (2012). Polymorphic Fibrillation of the Destabilized Fourth Fasciclin-1 Domain Mutant A₅₄6T of the Transforming Growth Factor-β-induced Protein (TGFBIp) Occurs through Multiple Pathways with Different Oligomeric Intermediates. Journal of Biological Chemistry, 287(41), 34730-34742. https://doi.org/10.1074/jbc.M112.379552

Pedersen, L. R. L., Nielsen, S. B., Hansted, J. G., Petersen, T. E., Otzen, D. E. & Sørensen, E. S. (2012). PP3 forms stable tetrameric structures through hydrophobic interactions via the C-terminal amphipathic helix and undergoes reversible thermal dissociation and denaturation. FEBS journal, 279(2), 336-47. https://doi.org/10.1111/j.1742-4658.2011.08428.x

Pedersen, L. R. L., Hansted, J. G., Nielsen, S. B., Petersen, T. E., Sørensen, U. S., Otzen, D. & Sørensen, E. S. (2012). Proteolytic activation of proteose peptone component 3 by release of a C-terminal peptide with antibacterial properties. Journal of Dairy Science, 95(6), 2819-2829. https://doi.org/10.3168/jds.2011-4837

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

Kalashnyk, N., Nielsen, J. T., Nielsen, E. H., Skrydstrup, T., Otzen, D., Lægsgaard, E., Wang, C., Besenbacher, F., Nielsen, N. C. & Linderoth, T. R. (2012). Scanning tunneling microscopy reveals single-molecule insights into the self-assembly of amyloid fibrils. A C S Nano, 6(8), 6882-6889. https://doi.org/10.1021/nn301708d

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

Giehm, L., Lorenzen, N. & Otzen, D. (2011). Assays for alpha-synuclein aggregation. Methods, 53(3), 295-305.

Otzen, D. E. (2011). Assembling good amyloid some structures at last. Structure, 19(9), 1207-1209. https://doi.org/10.1016/j.str.2011.08.005

Du, X., Wang, L., Wang, Y., Andreasen, M., Zhan, D., Feng, Y., Li, M., Zhao, M., Otzen, D., Xue, D., Yang, Y. & Liu, R. (2011). Aβ_1-16Can Aggregate and induce the Production of Reactive Oxygen Species, Nitric Oxide, and Inflammatory Cytokines. Journal of Alzheimer's Disease, 27(2), 401-413. https://doi.org/10.3233/JAD-2011-110476

Hansted, J. G., Wejse, P. L., Bertelsen, H. & Otzen, D. E. (2011). Effect of protein-surfactant interactions on aggregation of β-lactoglobulin. BBA General Subjects, 1814(5), 713-723. https://doi.org/10.1016/j.bbapap.2011.03.011

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