Ke, P. C., Zhou, R., Serpell, L. C., Riek, R., Knowles, T. P. J., Lashuel, H. A., Gazit, E., Hamley, I. W., Davis, T. P., Fändrich, M., Otzen, D. E., Chapman, M. R., Dobson, C. M., Eisenberg, D. S. & Mezzenga, R. (2020). Half a century of amyloids: past, present and future. Chemical Society Reviews, 49(15), 5473-5509. https://doi.org/10.1039/c9cs00199a

Malmos, K. G. & Otzen, D. E. (2013). Glycosaminoglycans and Fibrillar Polymorphism. In Bio-nanoimaging: Protein Misfolding and Aggregation (pp. 281-290). Elsevier Inc.. https://doi.org/10.1016/B978-0-12-394431-3.00026-2

Madsen, J. K., Kaspersen, J. D., Andersen, C. B., Nedergaard Pedersen, J., Andersen, K. K., Pedersen, J. S. & Otzen, D. E. (2017). Glycolipid Biosurfactants Activate, Dimerize, and Stabilize Thermomyces lanuginosus Lipase in a pH-Dependent Fashion. Biochemistry, 56(32), 4256-4268. https://doi.org/10.1021/acs.biochem.7b00420

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

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

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

Kaspersen, J. D., Pedersen, J. N., Hansted, J. G., Nielsen, S. B., Sakthivel, S., Wilhelm, K., Nemashkalova, E. L., Permyakov, S. E., Permyakov, E. A., Pinto Oliveira, C. L., Morozova-Roche, L. A., Otzen, D. & Pedersen, J. S. (2014). Generic Structures of Cytotoxic Liprotides: Nano-Sized Complexes with Oleic Acid Cores and Shells of Disordered Proteins. ChemBioChem, 10(18), 2693-2702. https://doi.org/10.1002/cbic.201402407

Mohammad-Beigi, H., Morshedi, D., Shojaosadati, S. A., Pedersen, J. N., Marvian, A. T., Aliakbari, F., Christiansen, G., Pedersen, J. S. & Otzen, D. E. (2016). Gallic acid loaded onto polyethylenimine-coated human serum albumin nanoparticles (PEI-HSA-GA NPs) stabilizes α-synuclein in the unfolded conformation and inhibits aggregation. RSC Advances, 6(88), 85312-85323. https://doi.org/10.1039/c6ra08502d

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

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

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

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

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

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

Otzen, D. & Riek, R. (2019). Functional Amyloids. Cold Spring Harbor Perspectives in Biology, 11(12), Article a033860. https://doi.org/10.1101/cshperspect.a033860

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. E. (2022). Functional amyloid in a lipid-like environment: a merry dance of many steps. Essays in Biochemistry, 66(7), 1035-1046. https://doi.org/10.1042/EBC20220062

Aliakbari, F., Shabani, A. A., Bardania, H., Mohammad-Beigi, H., Tayaranian Marvian, A., Dehghani Esmatabad, F., Vafaei, A. A., Shojaosadati, S. A., Saboury, A. A., Christiansen, G., Otzen, D. E. & Morshedi, D. (2018). Formulation and anti-neurotoxic activity of baicalein-incorporating neutral nanoliposome. Colloids and surfaces. B, Biointerfaces, 161, 578-587. https://doi.org/10.1016/j.colsurfb.2017.11.023

Abelein, A., Kaspersen, J. D., Nielsen, S. B., Jensen, G. V., Christiansen, G., Pedersen, J. S., Danielsson, J. A., Otzen, D. & Gräslund, A. (2013). Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates. Journal of Biological Chemistry, 288, 23518-23528. https://doi.org/10.1074/jbc.M113.470450

Paslawski, W., Lorenzen, N. & Otzen, D. E. (2016). Formation and Characterization of α-Synuclein Oligomers. Methods in molecular biology (Clifton, N.J.), 1345, 133-150. https://doi.org/10.1007/978-1-4939-2978-8_9

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

Otzen, D. & Andersen, K. K. (2013). Folding of outer membrane proteins. Archives of Biochemistry and Biophysics, 531(1-2), 34-43. https://doi.org/10.1016/j.abb.2012.10.008

Andersen, K. K. & Otzen, D. (2014). Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid. FEBS Letters, 588(10), 1955-1960. https://doi.org/10.1016/j.febslet.2014.04.004

Otzen, D. E. (2003). Folding of DsbB in mixed micelles: a kinetic analysis of the stability of a bacterial membrane protein. Journal of Molecular Biology, 330(4), 641-649. https://doi.org/10.1016/S0022-2836(03)00624-7

Lindberg, M. O., Tångrot, J., Otzen, D. E., Dolgikh, D. A., Finkelstein, A. V. & Oliveberg, M. (2001). Folding of circular permutants with decreased contact order: General trend balanced by protein stability. Journal of Molecular Biology, 314(4), 891-900. https://doi.org/10.1006/jmbi.2001.5186

Otzen, D. E. & Fersht, A. R. (1998). Folding of circular and permuted chymotrypsin inhibitor 2: Retention of the folding nucleus. Biochemistry, 37(22), 8139-8146. https://doi.org/10.1021/bi980250g

Neumann, J., Klein, N., Otzen, D. & Schneider, D. (2014). Folding energetics and oligomerization of polytopic α-helical transmembrane proteins. Archives of Biochemistry and Biophysics, 564, 281–296. https://doi.org/10.1016/j.abb.2014.07.017

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

Basaiawmoit, R. V., Oliveira, C. L. P. D., Runager, K., Kristensen, T., Enghild, J. J., Pedersen, J. S. & Otzen, D. (2009). First Low Resolution Structural Evidence of Full-length TGFBIp and Its Implications in TGFBI-linked Corneal Dystrophy. Abstract from ARVO 2009 Annual Meeting, nr. 2009, Fort Lauderdale, USA, 3. maj - 7. maj 2009, Investigative Ophthalmology & Visual Science. 2009. E-Abstract 4311. Association for Research in Vision and Ophthalmology..

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

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

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. P L o S One, 5(4), e10262. https://doi.org/10.1371/journal.pone.0010262

Rasmussen, H. Ø., Kumar, A., Shin, B., Stylianou, F., Sewell, L., Xu, Y., Otzen, D. E., Pedersen, J. S. & Matthews, S. J. (2023). FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC. Journal of Molecular Biology, 435(2), Article 167878. https://doi.org/10.1016/j.jmb.2022.167878

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

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

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Lise Refstrup Linnebjerg Pedersen