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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

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

Mogensen, J. E., Wimmer, R., Larsen, J. N., Spangfort, M. D. & Otzen, D. E. (2002). The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands. Journal of Biological Chemistry, 277(26), 23684-23692. https://doi.org/10.1074/jbc.M202065200

Morgensen, JE., Ferreras, M., Wimmer, R., Petersen, S. V., Enghild, J. J. & Otzen, D. (2007). The Major Allergen from Birch Tree Pollen, Bet v 1, Binds and Permeabilizes Membranes. Biochemistry.

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

van Diggelen, F., Frank, S. A., Somavarapu, A. K., Scavenius, C., Apetri, M. M., Nielsen, J., Tepper, A. W. J. W., Enghild, J. J. & Otzen, D. E. (2020). The interactome of stabilized α-synuclein oligomers and neuronal proteins. FEBS journal, 287(10), 2037-2054. https://doi.org/10.1111/febs.15124

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

Kjær, L., Giehm, L., Heimburg, T. R. & Otzen, D. (2009). The influence of vesicle composition and size on a-synuclein structure and stability. Biophysical Journal, 96.

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

Hourfar, H., Aliakbari, F., Aqdam, S. R., Nayeri, Z., Bardania, H., Otzen, D. E. & Morshedi, D. (2023). The impact of α-synuclein aggregates on blood-brain barrier integrity in the presence of neurovascular unit cells. International Journal of Biological Macromolecules, 229, 305-320. https://doi.org/10.1016/j.ijbiomac.2022.12.134

Aliakbari, F., Marzookian, K., Parsafar, S., Hourfar, H., Nayeri, Z., Fattahi, A., Raeiji, M., Boroujeni, N. N., Otzen, D. E. & Morshedi, D. (2024). The impact of hUC MSC-derived exosome-nanoliposome hybrids on α-synuclein fibrillation and neurotoxicity. Science Advances, 10(14), eadl3406. Article eadl3406. https://doi.org/10.1126/sciadv.adl3406

van Gils, J. H. M., van Dijk, E., Peduzzo, A., Hofmann, A., Vettore, N., Schützmann, M. P., Groth, G., Mouhib, H., Otzen, D. E., Buell, A. K. & Abeln, S. (2020). The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth. PLOS Computational Biology, 16(5), Article e1007767. https://doi.org/10.1371/journal.pcbi.1007767

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

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

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), Article 123. https://doi.org/10.1038/s42003-022-03059-8

Scavenius, C., Nikolajsen, C. L., Stenvang, M., Thøgersen, I., Wyrozemski, L., Wisniewski, H.-G., Otzen, D. E., Sanggaard, K. W. & Enghild, J. J. (2016). The compact and biologically relevant structure of inter-α-inhibitor is maintained by the chondroitin sulfate chain and divalent cations. Journal of Biological Chemistry, 291(9), 4658-4670. https://doi.org/10.1074/jbc.M115.678748

Rasmussen, H. Ø., Wollenberg, D. T. W., Wang, H., Andersen, K. K., Oliveira, C. L. P., Jørgensen, C. I., Jørgensen, T. J. D., Otzen, D. E. & Pedersen, J. S. (2022). The changing face of SDS denaturation: Complexes of Thermomyces lanuginosus lipase with SDS at pH 4.0, 6.0 and 8.0. Journal of Colloid and Interface Science, 614, 214-232. https://doi.org/10.1016/j.jcis.2021.12.188

Malmos, K. G., Stenvang, M., Sahin, C., Christiansen, G. & Otzen, D. E. (2017). The Changing Face of Aging: Highly Sulfated Glycosaminoglycans Induce Amyloid Formation in a Lattice Corneal Dystrophy Model Protein. Journal of Molecular Biology, 429(18), 2755-2764. https://doi.org/10.1016/j.jmb.2017.07.014

Haikal, C., Pascual, L. O., Najarzadeh, Z., Bernfur, K., Svanbergsson, A., Otzen, D. E., Linse, S. & Li, J. Y. (2021). The bacterial amyloids phenol soluble modulins from staphylococcus aureus catalyze alpha-synuclein aggregation. International Journal of Molecular Sciences , 22(21), Article 11594. https://doi.org/10.3390/ijms222111594

Pirhaghi, M., Najarzadeh, Z., Moosavi-Movahedi, F., Shafizadeh, M., Mamashli, F., Atarod, D., Ghasemi, A., Morshedi, D., Meratan, A. A., Otzen, D. E. & Saboury, A. A. (2023). The anti-platelet drug ticlopidine inhibits FapC fibrillation and biofilm production: Highlighting its antibiotic activity. Biochimica et Biophysica Acta - Proteins and Proteomics, 1871(2), Article 140883. https://doi.org/10.1016/j.bbapap.2022.140883

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

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

Hjørringgaard, C. U., Vad, B. S., Nielsen, S. B., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2009). Templated Multimers of Antimicrobial Peptides. Poster session presented at 8th Australian Peptide Conference, Peptides - Tools, Targets & Therapeutics , Australia.

Rasmussen, H. Ø., Nielsen, J., de Poli, A., Otzen, D. E. & Pedersen, J. S. (2023). Tau Fibrillation Induced by Heparin or a Lysophospholipid Show Different Initial Oligomer Formation. Journal of Molecular Biology, 435(17), Article 168194. https://doi.org/10.1016/j.jmb.2023.168194

Sørensen, H. V., Pedersen, J. N., Pedersen, J. S. & Otzen, D. E. (2017). Tailoring thermal treatment to form liprotide complexes between oleic acid and different proteins. BBA Proteins and Proteomics, 1865(6), 682–693. https://doi.org/10.1016/j.bbapap.2017.03.011

Mittag, T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2009). Synthesis of a Ketomethylene Isostere of the Fibrillating Peptide SNNFGAILSS. Journal of Organic Chemistry, 74, 7955-7957.

Sehgal, P., Doe, H., Sharma, M. & Otzen, D. E. (2005). Synergistic behavior of sodiumdodecylsulfate and 1,2-diheptanoyl-sn- glycero-3-phosphocholine in an aqueous medium: Interfacial and bulk behavior. Colloid and Polymer Science, 283(11), 1219-1225. https://doi.org/10.1007/s00396-005-1315-4

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

Cabré, E., Malmström, J., Sutherland, D., Perez-Gil, J. & Otzen, D. (2009). Surfactant protein SP-B strongly modifies surface collapse of phospholipid vesicles: Insights from a quartz crystal microbalance with dissipation. Biophysical Journal, 97(3), 768-76. https://doi.org/10.1016/j.bpj.2009.04.057

Pedersen, J. S., Flink, J. M., Dikov, D. & Otzen, D. (2006). Sulfates Dramatically Stabilize a Salt-Dependent Type of Glucagon Fibrils. Biophysical Journal, 90(11), 4181-4194. https://doi.org/10.1529/biophysj.105.070912

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

Pedersen, J. N., Frislev, H. K. S., Pedersen, J. S. & Otzen, D. (2020). Structures and mechanisms of formation of liprotides. B B A - Proteins and Proteomics, 1868(11), Article 140505. https://doi.org/10.1016/j.bbapap.2020.140505

Otzen, D. E., Itzhaki, L. S., Elmasry, N. F., Jackson, S. E. & Fersht, A. R. (1994). Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding. Proceedings of the National Academy of Sciences, 91(22), 10422-10425. https://doi.org/10.1073/pnas.91.22.10422

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

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

Hjorth, C. F., Norrman, M., Wahlund, P.-O., Benie, A. J., Petersen, B. O., Jessen, C. M., Pedersen, T. Å., Vestergaard, K., Steensgaard, D. B., Pedersen, J. S., Naver, H., Hubálek, F., Poulsen, C. & Otzen, D. (2016). Structure, Aggregation, and Activity of a Covalent Insulin Dimer Formed During Storage of Neutral Formulation of Human Insulin. Journal of Pharmaceutical Sciences, 105(4), 1376-1386. https://doi.org/10.1016/j.xphs.2016.01.003

Žvirblis, M., Sakalauskas, A., Janvand, S. H. A., Dudutienė, V., Žiaunys, M., Sniečkutė, R., Otzen, D. E., Smirnovas, V. & Matulis, D. (2024). Structure-Activity Relationship of Fluorinated Benzenesulfonamides as Inhibitors of Amyloid-β Aggregation. Chemistry - A European Journal, e202402330. Advance online publication. https://doi.org/10.1002/chem.202402330

Bisiak, F., Chrenková, A., Zhang, S. D., Pedersen, J. N., Otzen, D. E., Zhang, Y. E. & Brodersen, D. E. (2022). Structural variations between small alarmone hydrolase dimers support different modes of regulation of the stringent response. Journal of Biological Chemistry, 298(7), Article 102142. https://doi.org/10.1016/j.jbc.2022.102142

Otzen, D. E., Rheinnecker, M. & Fersht, A. R. (1995). Structural Factors Contributing to the Hydrophobic Effect: The Partly Exposed Hydrophobic Minicore in Chymotrypsin Inhibitor. Biochemistry, 34(40), 13051-13058. https://doi.org/10.1021/bi00040a016

Otzen, D. E., Kristensen, O., Proctor, M. & Oliveberg, M. (1999). Structural changes in the transition state of protein folding: Alternative interpretations of curved chevron plots. Biochemistry, 38(20), 6499-6511. https://doi.org/10.1021/bi982819j

Sahin, C., Østerlund, E. C., Österlund, N., Costeira-Paulo, J., Pedersen, J. N., Christiansen, G., Nielsen, J., Grønnemose, A. L., Amstrup, S. K., Tiwari, M. K., Rao, R. S. P., Bjerrum, M. J., Ilag, L. L., Davies, M. J., Marklund, E. G., Pedersen, J. S., Landreh, M., Møller, I. M., Jørgensen, T. J. D. & Otzen, D. E. (2022). Structural Basis for Dityrosine-Mediated Inhibition of α-Synuclein Fibrillization. Journal of the American Chemical Society, 144(27), 11949-11954. https://doi.org/10.1021/jacs.2c03607

Otzen, D. E., Knudsen, B. R., Aachmann, F., Larsen, K. L. & Wimmer, R. (2002). Structural basis for cyclodextrins' suppression of human growth hormone aggregation. Protein Science, 11(7), 1779-1787. https://doi.org/10.1110/ps.0202702

Aachmann, F. L., Otzen, D. E., Larsen, K. L. & Wimmer, R. (2003). Structural background of cyclodextrin-protein interactions. Protein Engineering, 16(12), 905-912.

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

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

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

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.

Hansen, J. H., Petersen, S. V., Andersen, K. K., Enghild, J. J., Damhus, T. & Otzen, D. (2009). Stable intermediates determine proteins' primary unfolding sites in the presence of surfactants. Biopolymers, 91(3), 221-31. https://doi.org/10.1002/bip.21125

Pedersen, J. N., Sørensen, H. V. & Otzen, D. E. (2018). Stabilizing vitamin D₃ using the molten globule state of α-lactalbumin. Journal of Dairy Science, 101(3), 1817–1826. https://doi.org/10.3168/jds.2017-13818

Chen, L., Cabrita, G. J. M., Otzen, D. & Melo, E. P. (2005). Stabilization of the Ribosomal Protein S6 by Trehalose is Counterbalanced by the Formation of a Putative Off-pathway Species. Journal of Molecular Biology, 351, 402-416. https://doi.org/10.1016/j.jmb.2005.05.056

Displaying results 51 to 100 out of 436

Revised 17.04.2023

Lise Refstrup Linnebjerg Pedersen