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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

Zhang, S., Andreasen, M., Nielsen, J. T., Liu, L., Nielsen, E. H., Song, J., Ji, G., Sun, F., Skrydstrup, T., Besenbacher, F., Nielsen, N. C., Otzen, D. E. & Dong, M. (2013). Coexistence of ribbon and helical fibrils originating from hIAPP20-29 revealed by quantitative nanomechanical atomic force microscopy. Proceedings of the National Academy of Sciences, 110(8), 2798-2803. https://doi.org/10.1073/pnas.1209955110

Zeng, G., Vad, B. S., Dueholm, M. S., Christiansen, G., Nilsson, M., Tolker-Nielsen, T., Nielsen, P. H., Meyer, R. L. & Otzen, D. E. (2015). Functional bacterial amyloid increases Pseudomonas biofilm hydrophobicity and stiffness. Frontiers in Microbiology, 6, 1099. https://doi.org/10.3389/fmicb.2015.01099

Wolf Pérez, A.-M., Sormanni, P., Andersen, J. S., Sakhnini, L. I., Rodriguez-Leon, I., Bjelke, J. R., Gajhede, A. J., De Maria, L., Otzen, D. E., Vendruscolo, M. & Lorenzen, N. (2019). In vitro and in silico assessment of the developability of a designed monoclonal antibody library. mAbs, 11(2), 388-400. https://doi.org/10.1080/19420862.2018.1556082

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

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

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

Wang, H., Andersen, K. K., Vad, B. S. & Otzen, D. E. (2013). OmpA can form folded and unfolded oligomers. B B A - Proteins and Proteomics, 1834(1), 127-136. https://doi.org/10.1016/j.bbapap.2012.09.002

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

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

Walther, R., Monge, P., Pedersen, A., Benderoth, A., Pedersen, J., Farzadfard, A., Mandrup, O., Howard, K., Otzen, D. & Zelikin, A. N. (2021). Per-glycosylation of the Surface-Accessible Lysines: One-Pot Aqueous Route to Stabilized Proteins with Native Activity. ChemBioChem, 22(14), 2478-2485. https://doi.org/10.1002/cbic.202100228

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

van Diggelen, F., Tepper, A., Petri, M. & Otzen, D. (2017). α-Synuclein Oligomers: A Study in Diversity. Israel Journal of Chemistry, 57(7-8), 699-723. https://doi.org/10.1002/ijch.201600116

van Diggelen, F., Hrle, D., Apetri, M., Christiansen, G., Rammes, G., Tepper, A. & Otzen, D. E. (2019). Two conformationally distinct α-synuclein oligomers share common epitopes and the ability to impair long-term potentiation. PLOS ONE, 14(3), Article 0213663. https://doi.org/10.1371/journal.pone.0213663

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

Valnickova, Z., Petersen, S. V., Nielsen, SB., Otzen, D. & Enghild, J. J. (2007). Heparin binding induces a conformational change of pigment epithelium-derived factor (PEDF). Journal of Biological Chemistry.

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

Valnickova, Z., Petersen, S. V., Nielsen, S. B., Otzen, D. E. & Enghild, J. J. (2007). Heparin binding induces a conformational change in pigment epithelium-derived factor. Journal of Biological Chemistry, 282(9), 6661-6667. https://doi.org/10.1074/jbc.M610471200

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. B B A - Proteins and Proteomics, 1804(4), 806-20. https://doi.org/10.1016/j.bbapap.2009.12.006

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

Vad, B. S., Balakrishnan, V. S., Nielsen, S. B. & Otzen, D. (2015). Phospholipid Ether Linkages Significantly Modulate the Membrane Affinity of the Antimicrobial Peptide Novicidin. Journal of Membrane Biology, 487-496. https://doi.org/10.1007/s00232-015-9792-y

Underhaug, J., Koldsø, H., Runager, K., Nielsen, J. T., Sørensen, C. S., Kristensen, T., Otzen, D., Karring, H., Malmendal, A., Schiøtt, B., Enghild, J. J. & Nielsen, N. C. (2013). Mutation in transforming growth factor beta induced protein associated with granular corneal dystrophy type 1 reduces the proteolytic susceptibility through local structural stabilization. BBA General Subjects, 1834(12), 2812–2822. https://doi.org/10.1016/j.bbapap.2013.10.008

Umakoshi, H., Persson, J., Kroon, M., Johansson, H. O., Otzen, D. E., Kuboi, R. & Tjerneld, F. (2000). Model process for separation based on unfolding and refolding of chymotrypsin inhibitor 2 in thermoseparating polymer two-phase systems. Journal of Chromatography B: Biomedical Sciences and Applications, 743(1-2), 13-19. https://doi.org/10.1016/S0378-4347(00)00190-0

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

Tiwari, M. K., Leinisch, F., Sahin, C., Møller, I. M., Otzen, D., Davies, M. J. & Bjerrum, M. J. (2018). Early events in copper-ion catalyzed oxidation of α-synuclein. Free Radical Biology & Medicine, 121, 38-50. https://doi.org/10.1016/j.freeradbiomed.2018.04.559

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

Tian, P., Lindorff-Larsen, K., Boomsma, W., Jensen, M. H. & Otzen, D. E. (2016). A Monte Carlo Study of the Early Steps of Functional Amyloid Formation. PLOS ONE, 11(1), Article e0146096. https://doi.org/10.1371/journal.pone.0146096

Tan, Y. J., Oliveberg, M., Otzen, D. E. & Fersht, A. R. (1997). Rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2. Journal of Molecular Biology, 269(4), 611-622. https://doi.org/10.1006/jmbi.1997.1043

Svane, A. S. P., Jahn, K., Deva, T., Malmendal, A., Otzen, D., Dittmer, J. & Nielsen, N. C. (2008). Early Stages of Amyloid Fibril Formation Studied by Liquid-State NMR: The Peptide Hormone Glucagon. Biophysical Journal, 95(1), 366 – 377. https://doi.org/10.1529/biophysj.107.122895

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

Stenvang, M., Christiansen, G. & Otzen, D. E. (2016). Epigallocatechin gallate remodels fibrils of Lattice Corneal Dystrophy protein, facilitating proteolytic degradation and preventing formation of membrane-permeabilizing species. Biochemistry, 55(16), 2344-2357. https://doi.org/10.1021/acs.biochem.6b00063

Stenvang, M., Dueholm, M. S., Vad, B. S., Seviour, T. W., Zeng, G., Geifman-Shochat, S., Søndergaard, M. T., Christiansen, G., Meyer, R. L., Kjelleberg, S., Otzen, D. E. & Nielsen, P. H. (2016). Epigallocatechin Gallate Remodels overexpressed Functional Amyloids in Pseudomonas aeruginosa and Increases Biofilm Susceptibility to Antibiotic Treatment. Journal of Biological Chemistry, 291(51), 26540-26553. https://doi.org/10.1074/jbc.M116.739953

Stenvang, M., Schafer, N. P., Malmos, K. G., Pérez, A.-M. W., Niembro, O., Sormanni, P., Basaiawmoit, R. V., Christiansen, G., Andreasen, M. & Otzen, D. E. (2018). Corneal dystrophy mutations drive pathogenesis by targeting TGFBIp stability and solubility in a latent amyloid-forming domain. Journal of Molecular Biology, 430(8), 1116-1140. https://doi.org/10.1016/j.jmb.2018.03.001

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

Song, Y. J. C., Lundvig, D. M. S., Huang, Y., Gai, W. P., Blumbergs, P. C., Højrup, P., Otzen, D., Halliday, G. M. & Jensen, P. H. (2007). p25a Relocalizes in Oligodendroglia from Myelin to Cytoplasmic Inclusions in Multiple System Atrophy. Am. J. Path., (171), 1291-1303.

Song, Y. J. C., Lundvig, D. M. S., Huang, Y., Wei, P. G., Blumbergs, P. C., Højrup, P., Otzen, D., Halliday, G. M. & Jensen, P. H. (2007). p25α relocalizes in oligodendroglia from myelin to cytoplasmic inclusions in multiple system atrophy. American Journal of Pathology, 171(4), 1291-1303. https://doi.org/10.2353/ajpath.2007.070201

Sønderby, T. V., Rasmussen, H. Ø., Frank, S. A., Skov Pedersen, J. & Otzen, D. E. (2022). Folding steps in the fibrillation of functional amyloid: denaturant sensitivity reveals common features in nucleation and elongation. Journal of Molecular Biology, 434(2), Article 167337. https://doi.org/10.1016/j.jmb.2021.167337

Sønderby, T. V., Zou, Y., Wang, P., Wang, C. & Otzen, D. E. (2022). Molecular-level insights into the surface-induced assembly of Functional Bacterial Amyloid. Biophysical Journal, 121(18), 3422-3434. https://doi.org/10.1016/j.bpj.2022.08.013

Sønderby, T. V., Najarzadeh, Z. & Otzen, D. E. (2022). Functional Bacterial Amyloids: Understanding Fibrillation, Regulating Biofilm Fibril Formation and Organizing Surface Assemblies. Molecules, 27(13), Article 4080. https://doi.org/10.3390/molecules27134080

Sønderby, T. V., Louros, N. N., Khodaparast, L., Khodaparast, L., Madsen, D. J., Olsen, W. P., Moonen, N., Nagaraj, M., Sereikaite, V., Strømgaard, K., Rousseau, F., Schymkowitz, J. & Otzen, D. E. (2023). Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation. Journal of Molecular Biology, 435(11), 168039. Article 168039. https://doi.org/10.1016/j.jmb.2023.168039

Somavarapu, A. K., Kleijwegt, G., Nagaraj, M., Alam, P., Nielsen, J. & Otzen, D. E. (2023). Drug repurposing screens identify compounds that inhibit α-synuclein oligomers' membrane disruption and block antibody interactions. Chemical Science, 14(11), 3030-3047. https://doi.org/10.1039/d2sc05534a

Sneppen, K., Lizana, G. L., Jensen, M. H., Pigolotti, S. & Otzen, D. (2009). Proteasome-Fibrillation Antagonism in a Dynamic Model for Parkinson’s Disease. Physical Biology, 6, 36005.

Skals, M., Bjaelde, R. G., Reinholdt, J., Poulsen, K., Vad, B. S., Otzen, D., Leipziger, J. & Praetorius, H. A. (2014). Bacterial RTX Toxins Allow Acute ATP Release from Human Erythrocytes Directly through the Toxin Pore. Journal of Biological Chemistry, 289, 19098-19109. https://doi.org/10.1074/jbc.M114.571414

Singh, Y., Trautwein, C., Romani, J., Salker, M. S., Neckel, P. H., Fraccaroli, I., Abeditashi, M., Woerner, N., Admard, J., Dhariwal, A., Dueholm, M. K. D., Schäfer, K. H., Lang, F., Otzen, D. E., Lashuel, H. A., Riess, O. & Casadei, N. (2023). Overexpression of human alpha-Synuclein leads to dysregulated microbiome/metabolites with ageing in a rat model of Parkinson disease. Molecular Neurodegeneration, 18(1), Article 44. https://doi.org/10.1186/s13024-023-00628-1

Seviour, T., Hansen, S. H., Yang, L., Yau, Y. H., Wang, V. B., Stenvang, M. R., Christiansen, G., Marsili, E., Givskov, M., Chen, Y., Otzen, D., Nielsen, P. H., Shochat, S. G., Kjelleberg, S. & Dueholm, M. S. (2015). Functional Amyloids Keep Quorum Sensing Molecules in Check. Journal of Biological Chemistry, 290, 6457-6469. https://doi.org/10.1074/jbc.M114.613810

Serpell, L. C., Radford, S. E. & Otzen, D. (2021). AlphaFold: A Special Issue and a Special time for Protein Science. Journal of Molecular Biology, 433(20), Article 167231. https://doi.org/10.1016/j.jmb.2021.167231

Sehgal, P., Bang Nielsen, S., Pedersen, S., Wimmer, R. & Otzen, D. (2007). Modulation of cutinase structure and stability by phospholipid detergents. Biochim. Biophys. Acta., (1774), 1544-1554.

Sehgal, P., Sharma, D., Larsen, K. L., Wimmer, R., Otzen, D. & Doe, H. (2008). Influence of beta-Cyclodextrin on the Mixed Micellization Process of Sodium Dodecyl Sulfate and Sodium Lauroyl Sarcosine and Formation of Inclusion Complexes. Journal of Dispersion Science and Technology, 29, 128-133.

Sehgal, P., Sharma, M., Larsen, K. L., Wimmer, R., Doe, H. & Otzen, D. (2008). Interactions of g-Cyclodextrin with the Mixed Micelles of Anionic Surfactants and Their Inclusion Complexes Formation. Journal of Dispersion Science and Technology, 29, 885-890. https://doi.org/10.1007/s00396-006-1466-y

Sehgal, P., Mizuki, T., Doe, H., Wimmer, R., Larsen, K. L. & Otzen, D. (2009). Interactions and Influence of a-Cyclodextrin on the Aggregation and Interfacial Properties of Mixtures of Nonionic and Zwitterionic Surfactants. Colloid and Polymer Science, 287, 1243-1252.

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Lise Refstrup Linnebjerg Pedersen