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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.

Hjørringgaard, C. U., Vad, B. S., Matchkov, V., Nielsen, S. B., Vosegaard, T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2010). Cyclodextrin Scaffolded Alamethicin with Highly Efficient Channel-forming Properties. Poster session presented at 31st European Peptide Symposium, 31EPS, Copenhagen, Denmark.

Vad, B. S., Thomsen, L. A. H., Bertelsen, K., Franzmann, M., Pedersen, J. M., Nielsen, S. B., Vosegaard, T., Valnickova, Z., Skrydstrup, T., Enghild, J. J., Wimmer, R., Nielsen, N. C. & Otzen, D. (2010). Divorcing folding from function: how acylation affects the membrane-perturbing properties of an antimicrobial peptide. Biochimica et Biophysica Acta - Proteins and Proteomics, 1804(4), 806-20. https://doi.org/10.1016/j.bbapap.2009.12.006

Giehm, L. & Otzen, D. E. (2010). Erratum to Strategies to increase the reproducibility of protein fibrillization in plate reader assays [Anal. Biochem., 400, (2010), 270-281]. Analytical Biochemistry, 406(2). https://doi.org/10.1016/j.ab.2010.06.047

Malmendal, A., Underhaug, J., Otzen, D. E. & Nielsen, N. C. (2010). Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins. PLoS One, 5(4), e10262. https://doi.org/10.1371/journal.pone.0010262

Valnickova, Z., Sanglas, L., Arolas, J. L., Petersen, S. V., Schar, C., Otzen, D., Aviles, F. X., Gomis-Ruth, F. X. & Enghild, J. J. (2010). Flexibility of the thrombin-activatable fibrinolysis inhibitor pro-domain enables productive binding of protein substrates. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.M110.150342

Dueholm, M. S., Petersen, S. V., Sønderkær, M., Larsen, P., Christiansen, G., Hein, K. L., Enghild, J. J., Nielsen, J. L., Nielsen, K. L., Nielsen, P. H. & Otzen, D. E. (2010). Functional amyloid in Pseudomonas. Molecular Microbiology. https://doi.org/10.1111/j.1365-2958.2010.07269.x

Otzen, D. (2010). Functional amyloid: turning swords into plowshares. Prion, 4(4), 256-64.

Otzen, D. (2010). Functional bacterial amyloids in biofilms. Annual Biofilm Highlights.

Andersen, C. B., Hicks, M. R., Vetri, V., Vandahl, B., Rahbek-Nielsen, H., Thøgersen, H., Thøgersen, I., Enghild, J. J., Serpell, L. C., Rischel, C. & Otzen, D. E. (2010). Glucagon fibril polymorphism reflects differences in protofilament backbone structure. Journal of Molecular Biology, 397(4), 932-46. https://doi.org/10.1016/j.jmb.2010.02.012

Otzen, D. & Enghild, J. J. (2010). Human phenotypically distinct TGFI corneal dystrophies are linked to the stability of the fourth Fas1 domain of TGFBIp. Journal of Biological Chemistry.

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

Otzen, D. (2010). Institutional nonconformism: the many levels of glucagon polymorphism. FEBS journal.

Debnath, D., Nielsen, K. L. & Otzen, D. E. (2010). In vitro association of fragments of a beta-sheet membrane protein. Advances in Biophysical Chemistry, 148(1-3), 112-20. https://doi.org/10.1016/j.bpc.2010.03.004

Dorosz, J., Gofman, Y., Kolusheva, S., Otzen, D., Ben-Tal, N., Nielsen, N. C. & Jelinek, R. (2010). Membrane Interactions of Novicidin, a Novel Antimicrobial Peptide: Phosphatidylglycerol Promotes Bilayer Insertion. Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 114(34), 11053-60. https://doi.org/10.1021/jp1052248

Otzen, D. (2010). Occupancy of non-annular lipid binding sites on KcsA greatly increases the stability of the tetrameric protein. Biochemistry.

Triano, I., Barrera, F. N., Renart, M. L., Molina, M. L., Fernández-Ballester, G., Poveda, J. A., Fernández, A. M., Encinar, J. A., Ferrer-Montiel, A. V., Otzen, D. & González-Ros, J. M. (2010). Occupancy of nonannular lipid binding sites on KcsA greatly increases the stability of the tetrameric protein. Biochemistry, 49(25), 5397-5404. https://doi.org/10.1021/bi1003712

Vad, B. S., Bertelsen, K., Johansen, C. H., Pedersen, J. M., Skrydstrup, T., Nielsen, N. C. & Otzen, D. E. (2010). Pardaxin permeabilizes vesicles more efficiently by pore formation than by disruption. Biophysical Journal, 98(4), 576-85. https://doi.org/10.1016/j.bpj.2009.08.063

Giehm, L., Oliveira, C. L. P. D., Christiansen, G., Pedersen, J. S. & Otzen, D. (2010). SDS-Induced Fibrillation of α-Synuclein: An Alternative Fibrillation Pathway. Journal of Molecular Biology, 401, 115-133. https://doi.org/10.1016/j.jmb.2010.05.060

Ferkinghoff-Borg, J., Fonslet, J., Andersen, C. B., Krishna, S., Pigolotti, S., Yagi, H., Goto, Y., Otzen, D. & Jensen, M. H. (2010). Stop-and-go kinetics in amyloid fibrillation. Physical Review E. Statistical, Nonlinear, and Soft Matter Physics, 82(1 Pt 1), 010901.

Giehm, L. & Otzen, D. E. (2010). Strategies to increase the reproducibility of protein fibrillization in plate reader assays. Analytical Biochemistry, 400(2), 270-81. https://doi.org/10.1016/j.ab.2010.02.001

Giehm, L. & Otzen, D. (2010). Strategies to increase the reproducibility of α-synuclein fibrillation in plate reader assays. Analytical Biochemistry, 406(2), 270-281.

Otzen, D. (2010). Surfactants and alcohols as inducers of protein amyloid: aggregation chaperones or membrane simulators? Lipids and membranes in amyloid diseases.

Reinau, M. E., Thøgersen, I. B., Enghild, J. J., Nielsen, K. L. & Otzen, D. E. (2010). The diversity of FtsY-lipid interactions. Biopolymers, 93(7), 595-606. https://doi.org/10.1002/bip.21404

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

Jeppesen, M. D., Westh, P. & Otzen, D. E. (2010). The role of protonation in protein fibrillation. FEBS Letters, 584(4), 780-4. https://doi.org/10.1016/j.febslet.2010.01.002

Huynh, T. H. V., Mantel, M., Mikkelsen, K., Lindhardt, A. T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2009). A Versatile Approach to β-Amyloid Fibril-Binding Compounds Exploiting the Shirakawa/Hayashi Protocol for trans-Alkene Synthesis. Organic Letters, 11, 999-1002.

Displaying results 301 to 350 out of 468

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Lise Refstrup Linnebjerg Pedersen