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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. F E B S 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

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

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. B B A - 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, [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. B B A - 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 of the United States of America, 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]. 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), [101848]. https://doi.org/10.1016/j.jbc.2022.101848

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 of the United States of America, 119(25), [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. P L o S 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. [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. The Journal of Physical Chemistry B, 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).

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

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

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

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. PNAS (Proceedings of the National Academy of Sciences of the United States of America), 110(24), 9758-9763. https://doi.org/10.1073/pnas.1218402110

Christophersen, C., Otzen, D. E., Norman, B. E., Christensen, S. & Schäfer, T. (1998). Enzymatic characterisation of novamyl®, a thermostable α-amylase. Starch/Staerke, 50(1), 39-45. https://doi.org/10.1002/(SICI)1521-379X(199801)50:1<39::AID-STAR39>3.0.CO;2-S

Christoffersen, H. F., Andreasen, M., Zhang, S., Nielsen, E. H., Christiansen, G., Dong, M., Skrydstrup, T. & Otzen, D. E. (2015). Scaffolded multimers of hIAPP20-29 peptide fragments fibrillate faster and lead to different fibrils compared to the free hIAPP20-29 peptide fragment. B B A - Proteins and Proteomics, 1854(12), 1890-1897. https://doi.org/10.1016/j.bbapap.2015.08.005

Christiansen, J. R., Olesen, M. N., Otzen, D. E., Romero-Ramos, M. & Sanchez-Guajardo, V. (2016). α-Synuclein vaccination modulates regulatory T cell activation and microglia in the absence of brain pathology. Journal of Neuroinflammation, 13, [74]. https://doi.org/10.1186/s12974-016-0532-8

Christiansen, S. H., Zhang, X., Juul-Madsen, K., Hvam, M. L., Vad, B. S., Behrens, M. A., Thygesen, I. L., Jalilian, B., Pedersen, J. S., Howard, K., Otzen, D. E. & Vorup-Jensen, T. (2017). The random co-polymer glatiramer acetate rapidly kills primary human leukocytes through sialic-acid-dependent cell membrane damage. B B A - Biomembranes, 1859(3), 425-437. https://doi.org/10.1016/j.bbamem.2017.01.001

Christensen, P. A., Pedersen, J. S., Christiansen, G. & Otzen, D. (2008). Spectroscopic Evidence for the Existence of an Obligate Pre-Fibrillar Oligonomer during Glucagon Fibrillation. F E B S Letters, (582), 1341-1345.

Christensen, L. F. B., Malmos, K. G., Christiansen, G. & Otzen, D. E. (2016). A Complex Dance: The Importance of Glycosaminoglycans and Zinc in the Aggregation of Human Prolactin. Biochemistry, 55(26), 3674–3684. https://doi.org/10.1021/acs.biochem.6b00153

Christensen, L. F. B., Otzen, D. & Dueholm, M. S. (2018). High-quality draft genome sequence of Sphaerisporangium cinnabarinum ATCC 31213. Genome Announcements, 6(21), [e00456-18]. https://doi.org/10.1128/genomeA.00456-18

Christensen, L. F. B., Hansen, L. M., Finster, K., Christiansen, G., Nielsen, P. H., Otzen, D. E. & Dueholm, M. S. (2018). The Sheaths of Methanospirillum Are Made of a New Type of Amyloid Protein. Frontiers in Microbiology, 9, [2729]. https://doi.org/10.3389/fmicb.2018.02729, https://doi.org/10.3389/fmicb.2018.02729

Christensen, L. F. B., Jensen, K. F., Nielsen, J., Vad, B. S., Christiansen, G. & Otzen, D. E. (2019). Reducing the Amyloidogenicity of Functional Amyloid Protein FapC Increases Its Ability To Inhibit α-Synuclein Fibrillation. ACS Omega, 4(2), 4029-4039. https://doi.org/10.1021/acsomega.8b03590

Displaying results 301 to 350 out of 403

Revised 07.04.2021

Lise Refstrup Linnebjerg Pedersen