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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. P L o S 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. P L o S 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. B B A - 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. B B A - 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

Dueholm, M. S., Nielsen, S. B., Hein, K. L., Nissen, P., Chapman, M., Christiansen, G., Nielsen, P. H. & Otzen, D. E. (2011). Fibrillation of the major curli subunit CsgA under a wide range of conditions implies a robust design of aggregation. Biochemistry, 50(39), 8281-90. https://doi.org/10.1021/bi200967c

Runager, K., Basaiawmoit, R. V., Deva, T., Andreasen, M., Valnickova, Z., Sørensen, C. S., Karring, H., Thøgersen, I. B., Christiansen, G., Underhaug, J., Kristensen, T., Nielsen, N. C., Klintworth, G. K., Otzen, D. E. & Enghild, J. J. (2011). Human Phenotypically Distinct TGFBI Corneal Dystrophies Are Linked to the Stability of the Fourth FAS1 Domain of TGFBIp. Journal of Biological Chemistry, 286(7), 4951-8. https://doi.org/10.1074/jbc.M110.181099

Scavenius, C., Ghodke, S., Otzen, D. E. & Enghild, J. J. (2011). Hydrogen exchange mass spectrometry as an analytical tool for the analysis of amyloid fibrillogenesis. International Journal of Mass Spectrometry, 302(1-3), 167-173. https://doi.org/10.1016/j.ijms.2010.10.001

Bertelsen, K., Vad, B., Nielsen, E. H. T., Hansen, S. K., Skrydstrup, T., Otzen, D., Vosegaard, T. & Nielsen, N. C. (2011). Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR: altered structural information in studies of antimicrobial peptides. Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 115(8), 1767-1774. https://doi.org/10.1021/jp110866g

Giehm, L., Svergun, D. I., Otzen, D. E. & Vestergaard, B. (2011). Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation. Proceedings of the National Academy of Sciences (PNAS), 108(8), 3246-3251. https://doi.org/10.1073/pnas.1013225108

Otzen, D. E. (2011). Mapping the folding pathway of the transmembrane protein DsbB by protein engineering. Protein Engineering Design and Selection (Print), 24(1-2), 139-149. https://doi.org/10.1093/protein/gzq079

Macchi, F., Hoffmann, S. V., Carlsen, M., Vad, B. S., Imparato, A., Rischel, C. & Otzen, D. (2011). Mechanical stress affects glucagon fibrillation kinetics and fibril structure. Langmuir, 27(20), 12539–12549. https://doi.org/10.1021/la202125c

Otzen, D. (2011). Protein-surfactant interactions a tale of many states. BBA General Subjects, 1814(5), 562-91. https://doi.org/10.1016/j.bbapap.2011.03.003

Basaiawmoit, R. V., Oliveira, C. L. P., Runager, K., Sørensen, C. S., Behrens, M. A., Jonsson, B.-H., Kristensen, T., Klintworth, G. K., Enghild, J. J., Pedersen, J. S. & Otzen, D. E. (2011). SAXS models of TGFBIp reveal a trimeric structure and show that the overall shape is not affected by the Arg124His mutation. Journal of Molecular Biology, 408(3), 503-513. https://doi.org/10.1016/j.jmb.2011.02.052

Weber, M., Schneider, D., Prodöhl, A., Dreher, C., Becker, C., Underhaug, J., Svane, A. S. P., Malmendal, A., Nielsen, N. C. & Otzen, D. (2011). SDS-facilitated in vitro formation of a transmembrane B-type cytochrome is mediated by changes in local pH. Journal of Molecular Biology, 407(4), 594-606. https://doi.org/10.1016/j.jmb.2011.02.005

Wang, J., Jensen, U. B., Jensen, G. V., Shipovskov, S., Balakrishnan, V. S., Otzen, D., Pedersen, J. S., Besenbacher, F. & Sutherland, D. S. (2011). Soft Interactions at Nanoparticles Alter Protein Function and Conformation in a Size Dependent Manner. Nano Letters, 11(11), 4985-4991. https://doi.org/10.1021/nl202940k

Debnath, D. K., Basaiawmoit, R. V., Nielsen, K. L. & Otzen, D. E. (2011). The role of membrane properties in Mistic folding and dimerisation. Protein Engineering Design and Selection (Print), 24(1-2), 89-97. https://doi.org/10.1093/protein/gzq095

Otzen, D. E. (2010). Amyloid formation in surfactants and alcohols: membrane mimetics or structural switchers? Current protein & peptide science, 11(5), 355-71.

Pedersen, J. S., Andersen, C. B. & Otzen, D. (2010). Amyloid structure--one but not the same: the many levels of fibrillar polymorphism. FEBS journal, 277(22), 4591-4601. https://doi.org/10.1111/j.1742-4658.2010.07888.x

Giehm, L., Dal Degan, F., Fraser, P., Klysner, S. & Otzen, D. E. (2010). An Aß concatemer with altered aggregation propensities. BBA General Subjects, 1804(10), 2025-35. https://doi.org/10.1016/j.bbapap.2010.06.023

Giehm, L., Lorenzen, N. & Otzen, D. E. (2010). Assays for α-synuclein aggregation. Methods. https://doi.org/10.1016/j.ymeth.2010.12.008

Jeppesen, M. D., Hein, K., Nissen, P., Westh, P. & Otzen, D. E. (2010). A thermodynamic analysis of fibrillar polymorphism. Advances in Biophysical Chemistry, 149(1-2), 40-6. https://doi.org/10.1016/j.bpc.2010.03.016

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

Debnath, D. K. & Otzen, D. E. (2010). Cell-free synthesis and folding of transmembrane OmpA reveals higher order structures and premature truncations. Advances in Biophysical Chemistry, 152(1-3), 80-8. https://doi.org/10.1016/j.bpc.2010.08.003

Hein, K. L., Kragh-Hansen, U., Morth, J. P., Jeppesen, M., Otzen, D., Møller, J. V. & Nissen, P. (2010). Crystallographic analysis reveals a unique lidocaine binding site on human serum albumin. Journal of Structural Biology, 171, 353-360.

Hjørringgaard, C. U., Vad, B., Nielsen, S. B., Matchkov, V., Vosegaard, T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2010). Cyclodextrin scaffolded alamethicin with highly efficient channel-forming properties. Journal of Peptide Science, 16, 148.

Displaying results 251 to 300 out of 444

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Lise Refstrup Linnebjerg Pedersen