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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

Tian, P., Boomsma, W., Wang, Y., Otzen, D., Jensen, M. H. & Lindorff-Larsen, K. (2015). Structure of a Functional Amyloid Protein Subunit Computed Using Sequence Variation. Journal of the American Chemical Society, 137(1), 22-25. https://doi.org/10.1021/ja5093634

Estrela, N., Franquelim, H. G., Lopes, C., Tavares, E., Macedo, J. A., Christiansen, G., Otzen, D. E. & Melo, E. P. (2015). Sucrose prevents protein fibrillation through compaction of the tertiary structure but hardly affects the secondary structure. Proteins: Structure, Function, and Bioinformatics, 83(11), 2039-2051. https://doi.org/10.1002/prot.24921

Madsen, J., Pihl, R., Møller, A. H., Tranberg Madsen, A., Otzen, D. & Andersen, K. K. (2015). The anionic biosurfactant rhamnolipid does not denature industrial enzymes. Frontiers in Microbiology, 6, Article 292. https://doi.org/10.3389/fmicb.2015.00292

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

Frahm, H., Hansen, S. K., Vad, B. S., Nielsen, E. H., Nielsen, J. T., Vosegaard, T., Skrydstrup, T. & Otzen, D. E. (2015). The natural, peptaibolic peptide SPF-5506-A4 adopts a β-bend spiral structure, shows low hemolytic activity and targets membranes through formation of large pores. B B A - Proteins and Proteomics, 1854(8), 882-889. https://doi.org/10.1016/j.bbapap.2015.03.003

Dueholm, M. S., Larsen, P., Finster, K., Stenvang, M. R., Christiansen, G., Vad, B. S., Bøggild, A., Otzen, D. E. & Halkjær Nielsen, P. (2015). The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids. Journal of Biological Chemistry, 290, 20590-26600. https://doi.org/10.1074/jbc.M115.654780

Pedersen, J. N., Pedersen, J. S. & Otzen, D. E. (2015). The Use of Liprotides To Stabilize and Transport Hydrophobic Molecules. Biochemistry, 54(31), 4815-4823. https://doi.org/10.1021/acs.biochem.5b00547

Skals, M., Bjaelde, R. G., Reinholdt, J., Poulsen, K., Vad, B. S., Otzen, D., Leipziger, J. & Praetorius, H. A. (2014). Bacterial RTX Toxins Allow Acute ATP Release from Human Erythrocytes Directly through the Toxin Pore. Journal of Biological Chemistry, 289, 19098-19109. https://doi.org/10.1074/jbc.M114.571414

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. B B A - Bioenergetics, 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. In V. Uversky & Y. Lyubchenko (Eds.), Bio-nanoimaging: Protein misfolding and aggregation (pp. 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, 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. B B A - 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.

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Lise Refstrup Linnebjerg Pedersen