Institut for Molekylærbiologi og Genetik

Aarhus Universitets segl

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Paslawski, W., Mysling, S., Thomsen, K., Jørgensen, T. J. D. & Otzen, D. (2014). Co-existence of Two Different α-Synuclein Oligomers with Different Core Structures Determined by Hydrogen/Deuterium Exchange Mass Spectrometry. Angewandte Chemie International Edition, 53(29), 7560-7563. https://doi.org/10.1002/anie.201400491
Poulsen, E. T., Runager, K., Risør, M. W., Dyrlund, T. F., Scavenius, C., Karring, H., Praetorius, J., Vorum, H., Otzen, D. E., Klintworth, G. K. & Enghild, J. J. (2014). Comparison of two phenotypically distinct lattice corneal dystrophies caused by mutations in the transforming growth factor beta induced (TGFBI) gene. Proteomics - Clinical Applications, 8(3-4), 168-177. https://doi.org/10.1002/prca.201300058
Knudsen, A. D., Bennike, T., Kjeldal, H., Birkelund, S., Otzen, D. & Stensballe, A. (2014). Condenser: A statistical aggregation tool for multi-sample quantitative proteomic data from Matrix Science Mascot Distiller™. Journal of Proteomics, 103, 261-266. https://doi.org/10.1016/j.jprot.2014.02.001
Andersen, K. K. & Otzen, D. (2014). Denaturation of α-lactalbumin and myoglobin by the anionic biosurfactant rhamnolipid. Biochimica et biophysica acta. Bioenergeticss, 1844(12), 2338-2345. https://doi.org/10.1016/j.bbapap.2014.10.005
Lopes, P., Dyrnesli, H., Lorenzen, N., Otzen, D. & Ferapontova, E. (2014). Electrochemical Analysis of the Fibrillation of Parkinson's Disease α-synuclein. Analyst, 139(4), 749-756. https://doi.org/10.1039/C3AN01616A
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
Andersen, K. K. & Otzen, D. (2014). Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid. FEBS Letters, 588(10), 1955-1960. https://doi.org/10.1016/j.febslet.2014.04.004
Kaspersen, J. D., Pedersen, J. N., Hansted, J. G., Nielsen, S. B., Sakthivel, S., Wilhelm, K., Nemashkalova, E. L., Permyakov, S. E., Permyakov, E. A., Pinto Oliveira, C. L., Morozova-Roche, L. A., Otzen, D. & Pedersen, J. S. (2014). Generic Structures of Cytotoxic Liprotides: Nano-Sized Complexes with Oleic Acid Cores and Shells of Disordered Proteins. ChemBioChem, 10(18), 2693-2702. https://doi.org/10.1002/cbic.201402407
Paslawski, W., Andreasen, M., Nielsen, S. B., Lorenzen, N., Thomsen, K., Kaspersen, J. D., Pedersen, J. S. & Otzen, D. (2014). High stability and cooperative unfolding of cytotoxic α-synuclein oligomers. Biochemistry, 53(39), 6252-6263. https://doi.org/10.1021/bi5007833
Lorenzen, N., Nielsen, S. B., Yoshimura, Y., Vad, B. S., Andersen, C. B., Betzer, C., Kaspersen, J. D., Christiansen, G., Pedersen, J. S., Jensen, P. H., Mulder, F. A. A. & Otzen, D. E. (2014). How epigallocatechin gallate can inhibit α-synuclein oligomer toxicity in vitro. Journal of Biological Chemistry, 289(31), 21299-21310. https://doi.org/10.1074/jbc.M114.554667
Kaspersen, J., Moestrup Jessen, C., Stougaard Vad, B., Skipper Sørensen, E., Kleiner Andersen, K., Glasius, M., Pinto Oliveira, C. L., Otzen, D. & Pedersen, J. S. (2014). Low-Resolution Structures of OmpA⋅DDM Protein-Detergent Complexes. ChemBioChem, 15(14), 2113-2124. https://doi.org/10.1002/cbic.201402162
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
Lorenzen, N. & Otzen, D. (2014). Oligomers of α-synuclein: picking the culprit in the line-up. Essays in Biochemistry, 56(1), 137-148. https://doi.org/10.1042/bse0560137
Ghodke, S. D., Jensen, G. V., Svane, A. S. P., Weise, K., Søndergaard, A., Behrens, M. A., Pedersen, J. S., Nielsen, N. C., Pedersen, J. S., Winter, R. & Otzen, D. (2014). Polymorphism, metastable species and interconversion: the many states of glucagon fibrils. I V. Uversky & Y. Lyubchenko (red.), Bio-nanoimaging: Protein misfolding and aggregation (s. 373-386). Elsevier. https://doi.org/10.1016/B978-0-12-394431-3.00034-1
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, Artikel 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. I Bio-nanoimaging : Protein Misfolding and Aggregation (s. 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 fra 6th International Workshop on Surface Modification for Chemical and Biochemical Sensing, Warsaw, Polen.
Dueholm, M. S., Otzen, D. & Nielsen, P. H. (2013). Evolutionary Insight into the Functional Amyloids of the Pseudomonads. PLoS One, 8(10), 1-9. Artikel e76630. https://doi.org/10.1371/journal.pone.0076630
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
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
Lorenzen, N., E. Wanker, E. & Otzen, D. (2013). Inhibitors of amyloid and oligomer formation. I D. E. Otzen (red.), Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties (s. 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. I J. Kleinschmidt (red.), Lipid-Protein Interactions: Methods and Protocols: Methods in Molecular Biology (Bind 974, s. 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), Artikel 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

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Revideret 01.07.2026
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Viktor Hauge Ladegaard