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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

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

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., 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

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

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

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

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

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

Frøkjær, S. & Otzen, D. (2005). Protein drug stability: a formulation challenge. Nature Reviews. Drug Discovery, 4, 298-306. https://doi.org/10.1038/nrd1695

Frislev, H. K. S., Pedersen, J. N., Pedersen, J. S. & Otzen, D. (2016). Liprotides: Nano-Sized Cytotoxic Protein-Fatty Acid Complexes with a Core-Shell or Multi-Layer Structure. Poster session presented at Biophysical Society 60th Annual Meeting, Los Angeles, United States. http://www.cell.com/biophysj/fulltext/S0006-3495%2815%2904270-8

Frislev, H. K. S., Jessen, C. M., Oliveira, C. L. P., Pedersen, J. S. & Otzen, D. E. (2016). Liprotides made of α-lactalbumin and cis fatty acids form core-shell and multi-layer structures with a common membrane-targeting mechanism. Biochimica et Biophysica Acta - Proteins and Proteomics, 1864(7), 847-859. https://doi.org/10.1016/j.bbapap.2016.04.003

Frislev, H. K. S., Pedersen, J. N., Pedersen, J. S. & Otzen, D. E. (2016). Liprotides: Nano-Sized Cytotoxic Protein-Fatty Acid Complexes with a Core-Shell or Multi-Layer Structure. Biophysical Journal, 110(3), 577A. https://doi.org/10.1016/j.bpj.2015.11.3087

Frislev, H. S., Boye, T. L., Nylandsted, J. & Otzen, D. (2017). Liprotides kill cancer cells by disrupting the plasma membrane. Scientific Reports, 7(1), Article 15129. https://doi.org/10.1038/s41598-017-15003-6

Frislev, H. S., Jakobsen, S. C. L., Frank, S. A. & Otzen, D. E. (2018). Dynamic content exchange between liprotides. Biophysical Chemistry, 233, 13-18. https://doi.org/10.1016/j.bpc.2017.11.006

Frislev, H. S., Nielsen, J., Nylandsted, J. & Otzen, D. (2018). Using Liprotides to Deliver Cholesterol to the Plasma Membrane. Journal of Membrane Biology, 25(4), 581-592. https://doi.org/10.1007/s00232-018-0034-y

Franzmann, M., Otzen, D. & Wimmer, R. (2009). Quantitative use of paramagnetic relaxation enhancements for determining orientation and insertion depth of peptides in micelles. ChemBioChem, 10, 2339-2347.

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. Biochimica et Biophysica Acta - Proteins and Proteomics, 1854(8), 882-889. https://doi.org/10.1016/j.bbapap.2015.03.003

Fersht, A. R., Itzhaki, L. S., Elmasry, N. F., Matthews, J. M. & Otzen, D. E. (1994). Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. Proceedings of the National Academy of Sciences (PNAS), 91(22), 10426-10429. https://doi.org/10.1073/pnas.91.22.10426

Ferreira, N., Gram, H., Sorrentino, Z. A., Gregersen, E., Schmidt, S. I., Reimer, L., Betzer, C., Perez-Gozalbo, C., Beltoja, M., Nagaraj, M., Wang, J., Nowak, J. S., Dong, M., Willén, K., Cholak, E., Bjerregaard-Andersen, K., Mendez, N., Rabadia, P., Shahnawaz, M. ... Jensen, P. H. (2021). Multiple system atrophy-associated oligodendroglial protein p25α stimulates formation of novel α-synuclein strain with enhanced neurodegenerative potential. Acta Neuropathologica, 142, 87-115. https://doi.org/10.1007/s00401-021-02316-0

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.

Fatum, T. M., Olsen, A. A., Fuglsang, C. C. & Otzen, D. (1998). Properties of PEG-modified microbial proteases. Activity and stability studies. Progress in Biotechnology, 15(C), 147-150. https://doi.org/10.1016/S0921-0423(98)80024-5

Farzadfard, A., Pedersen, J. N., Meisl, G., Somavarapu, A. K., Alam, P., Goksøyr, L., Nielsen, M. A., Sander, A. F., Knowles, T. P. J., Pedersen, J. S. & Otzen, D. E. (2022). The C-terminal tail of α-synuclein protects against aggregate replication but is critical for oligomerization. Communications Biology, 5(1), 123. Article 123. https://doi.org/10.1038/s42003-022-03059-8

Farzadfard, A., König, A., Petersen, S. V., Nielsen, J., Vasili, E., Dominguez-Meijide, A., Buell, A. K., Outeiro, T. F. & Otzen, D. E. (2022). Glycation modulates alpha-synuclein fibrillization kinetics: a sweet spot for inhibition. The Journal of Biological Chemistry, 298(5), Article 101848. https://doi.org/10.1016/j.jbc.2022.101848

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

Evans, D. C. S., Khamas, A. B., Marcussen, L., Rasmussen, K. S., Klitgaard, J. K., Kallipolitis, B. H., Nielsen, J., Otzen, D. E., Leake, M. C. & Meyer, R. L. (2023). GFP fusions of Sec-routed extracellular proteins in Staphylococcus aureusreveal surface-associated coagulase in biofilms. Microbial Cell, 10(7), 145-156. https://doi.org/10.15698/mic2023.07.800

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

Eskandari, H., Ghanadian, M., Noleto-Dias, C., Lomax, C., Tawfike, A., Christiansen, G., Sutherland, D. S., Ward, J. L., Mohammad-Beigi, H. & Otzen, D. E. (2020). Inhibitors of α-Synuclein fibrillation and oligomer toxicity in Rosa damascena: the all-pervading powers of flavonoids and phenolic glycosides. ACS Chemical Neuroscience, 11(19), 3161–3173. https://doi.org/10.1021/acschemneuro.0c00528

Dyla, M., González Foutel, N. S., Otzen, D. E. & Kjaergaard, M. (2022). The optimal docking strength for reversibly tethered kinases. Proceedings of the National Academy of Sciences (PNAS), 119(25), Article e2203098119. https://doi.org/10.1073/pnas.2203098119

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

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

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

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

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

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

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

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

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

Dong, M., Hovgaard, M. B., Mamdouh, W., Xu, S., Otzen, D. & Besenbacher, F. (2008). AFM-based force spectroscopy measurements of mature amyloid fibrils of the peptide glucagon. Nanotechnology, 19, 384013. https://doi.org/10.1088/0957-4484/19/38/384013

Dong, M. D., Hovgaard, M. B., Mamdouh, W., Xu, S. L., Otzen, D. E. & Besenbacher, F. (2008). AFM-based force spectroscopy measurements of mature amyloid fibrils of the peptide glucagon: Nanotechnology. Nanotechnology, 19(38).

Dilamian, M., Montazer, M., Yousefi, H., Otzen, D. E. & Morshedi, D. (2024). Functional porous protein nanofibrils/polysaccharides aerogel beads for efficient dyes removal from water. Materials Advances, 5(18), 7199-7221. https://doi.org/10.1039/d4ma00380b

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

De Prat Gay, G., Ruiz-Sanz, J., Neira, J. L., Corrales, F. J., Otzen, D. E., Ladurner, A. G. & Fersht, A. R. (1995). Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway. Journal of Molecular Biology, 254(5), 968-979. https://doi.org/10.1006/jmbi.1995.0669

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

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

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

Dalsgaard, T. K., Otzen, D., Nielsen, J. H. & Larsen, L. B. (2007). Changes in structures of milk proteins upon photo-oxidation. J. Agr. Food Chem., (55), 10968-10976.

Daggett, V., Li, A., Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1996). Structure of the transition state for folding of a protein derived from experiment and simulation. Journal of Molecular Biology, 257(2), 430-440. https://doi.org/10.1006/jmbi.1996.0173

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

Displaying results 351 to 400 out of 469

Revised 08.12.2025

Lise Refstrup Linnebjerg Pedersen