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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.

Sehgal, P., Kosaka, O., Doe, H. & Otzen, D. (2009). Interaction and stability of mixed micelle and monolayer of nonionic and cationic surfactant mixtures. Journal of Dispersion Science and Technology, 30, 1050-1058.

Sehgal, P., Mogensen, J. E. & Otzen, D. (2005). Using micellar mole fractions to assess membrane protein stability in mixed micelles. B B A - Biomembranes, 1761, 59-68. https://doi.org/10.1016/j.bbamem.2005.08.006

Sehgal, P., Sharma, M., Larsen, K. L., Wimmer, R., Doe, H. & Otzen, D. (2008). Interactions of γ-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/10.1080/01932690701783390

Sehgal, P. & Otzen, D. (2006). Thermodynamics of unfolding of an integral membrane protein in mixed micelles. Protein Science, 15, 890-899. https://doi.org/10.1110/ps.052031306

Sehgal, P., Sharma, M., Wimmer, R., Larsen, K. L. & Otzen, D. (2006). Interactions between anionic mixed micelles and α-cyclodextrin and their inclusion complexes: conductivity, NMR and fluorescence study. Colloid and Polymer Science, 284(8), 916-926. https://doi.org/10.1007/s00396-006-1466-y

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

Sehgal, P., Doe, H., Sharma, M. & Otzen, D. E. (2004). Interaction between phospholipid vesicular structures with long chain zwitterionic surfactants. Colloid and Polymer Science, 282(7), 677-683. https://doi.org/10.1007/s00396-003-0992-0

Schmüser, L., Trefz, M., Roeters, S. J., Beckner, W., Pfaendtner, J., Otzen, D., Woutersen, S., Bonn, M., Schneider, D. & Weidner, T. (2021). Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy. Langmuir : the ACS journal of surfaces and colloids, 37(45), 13452-13459. https://doi.org/10.1021/acs.langmuir.1c02206

Schafer, N., Truong, H. H., Otzen, D., Lindorff-Larsen, K. & Wolynes, P. G. (2016). Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease. Proceedings of the National Academy of Sciences (PNAS), 113(8), 2098-2103. https://doi.org/10.1073/pnas.1524027113

Scavenius, C., Ghodke, S., Otzen, D. E. & Enghild, J. J. (2011). Hydrogen exchange mass spectrometry as an analytical tool for the analysis of amyloid fibrillogenesis. International Journal of Mass Spectrometry, 302(1-3), 167-173. https://doi.org/10.1016/j.ijms.2010.10.001

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

Sawada, M., Yamaguchi, K., Hirano, M., Noji, M., So, M., Otzen, D. E., Kawata, Y. & Goto, Y. (2020). Amyloid formation of α-synuclein based on the solubility- and supersaturation-dependent mechanism. Langmuir, 36(17), 4671-4681. https://doi.org/10.1021/acs.langmuir.0c00426

Santos, J., Cuellar, J., Pallarès, I., Byrd, E. J., Lends, A., Moro, F., Abdul-Shukkoor, M. B., Pujols, J., Velasco-Carneros, L., Sobott, F., Otzen, D. E., Calabrese, A. N., Muga, A., Pedersen, J. S., Loquet, A., Valpuesta, J. M., Radford, S. E. & Ventura, S. (2024). A Targetable N-Terminal Motif Orchestrates α-Synuclein Oligomer-to-Fibril Conversion. Journal of the American Chemical Society, 146(18), 12702-12711. https://doi.org/10.1021/jacs.4c02262

Sahin, C., Lorenzen, N., Lemminger, L., Christiansen, G., Møller, I. M., Vesterager, L. B., Pedersen, L. Ø., Fog, K., Kallunki, P. & Otzen, D. E. (2017). Antibodies against the C-terminus of α-synuclein modulate its fibrillation. Biophysical Chemistry, 220, 34-41. https://doi.org/10.1016/j.bpc.2016.11.002

Sahin, C., Kjær, L., Christensen, M. S., Nedergaard Pedersen, J., Christiansen, G., Pérez, A.-M. W., Moller, I. M., Enghild, J., Pedersen, J. S., Larsen, K. & Otzen, D. E. (2018). α-synucleins from animal species show low fibrillation propensities and weak oligomer membrane disruption. Biochemistry, 57(34), 5145-5158. https://doi.org/10.1021/acs.biochem.8b00627

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

Rusbjerg-Weberskov, C. E., Johansen, M. L., Nowak, J. S., Otzen, D., Pedersen, J. S., Enghild, J. J. & Nielsen, N. S. (2023). Periostin C-Terminal Is Intrinsically Disordered and Interacts with 143 Proteins in an In Vitro Epidermal Model of Atopic Dermatitis. Biochemistry, 62(19), 2803-2815. https://doi.org/10.1021/acs.biochem.3c00176

Runager, K., Underhaug, J., Basaiawmoit, R. V., Valnickova, Z., Kristensen, T., Otzen, D., Klintworth, G. K., Nielsen, N. C. & Enghild, J. J. (2009). Naturally Occurring Mutations Alter the Structure and Stability of the Fourth Fasciclin Domain of the Transforming Growth Factor Beta Induced Protein (TGFBIp). Investigative Ophthalmology & Visual Science, (E-Abstract 1016).

Runager, K., Basaiawmoit, R. V., Deva, T., Andreasen, M., Valnickova, Z., Sørensen, C. S., Karring, H., Thøgersen, I. B., Christiansen, G., Underhaug, J., Kristensen, T., Nielsen, N. C., Klintworth, G. K., Otzen, D. E. & Enghild, J. J. (2011). Human Phenotypically Distinct TGFBI Corneal Dystrophies Are Linked to the Stability of the Fourth FAS1 Domain of TGFBIp. Journal of Biological Chemistry, 286(7), 4951-8. https://doi.org/10.1074/jbc.M110.181099

Ruiz-Sanz, J., de Prat Gay, G., Otzen, D. E. & Fersht, A. R. (1995). Protein Fragments as Models for Events in Protein Folding Pathways: Protein Engineering Analysis of the Association of Two Complementary Fragments of the Barley Chymotrypsin Inhibitor 2 (CI-2). Biochemistry, 34(5), 1695-1701. https://doi.org/10.1021/bi00005a026

Rouse, S. L., Hawthorne, W. J., Berry, J.-L., Chorev, D. S., Ionescu, S. A., Lambert, S., Stylianou, F., Ewert, W., Mackie, U., Morgan, R. M. L., Otzen, D., Herbst, F.-A., Nielsen, P. H., Dueholm, M., Bayley, H., Robinson, C. V., Hare, S. & Matthews, S. (2017). A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis. Nature Communications, 8(1), Article 263. https://doi.org/10.1038/s41467-017-00361-6

Rotilio, L., Bayer, T., Meinert, H., Teixeira, L. M. C., Johansen, M. B., Sommerfeldt, A., Petersen, A. R., Sandahl, A., Keller, M. B., Holck, J., Paiva, P., Otzen, D. E., Bornscheuer, U. T., Wei, R., Fernandes, P. A., Ramos, M. J., Westh, P. & Morth, J. P. (2024). Structural and Functional Characterization of an Amidase Targeting a Polyurethane for Sustainable Recycling. Angewandte Chemie International Edition, e202419535. Advance online publication. https://doi.org/10.1002/anie.202419535

Roeters, S. J., Strunge, K., Pedersen, K. B., Golbek, T. W., Bregnhøj, M., Zhang, Y., Wang, Y., Dong, M., Nielsen, J., Otzen, D. E., Schiøtt, B. & Weidner, T. (2023). Elevated concentrations cause upright alpha-synuclein conformation at lipid interfaces. Nature Communications, 14(1), Article 5731. https://doi.org/10.1038/s41467-023-39843-1

Risør, M. W., Juhl, D. W., Bjerring, M., Mathiesen, J., Enghild, J. J., Nielsen, N. C. & Otzen, D. E. (2017). Critical Influence of Cosolutes and Surfaces on the Assembly of Serpin-Derived Amyloid Fibrils. Biophysical Journal, 113(3), 580-596. https://doi.org/10.1016/j.bpj.2017.06.030

Reinau, M. E. & Otzen, D. (2009). Stability and structure of the membrane protein transporter Ffh is modulated by substrates and lipids. Archives of Biochemistry and Biophysics, 492, 48-53.

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

Reimer, L., Haikal, C., Gram, H., Theologidis, V., Kovacs, G., Ruesink, H., Baun, A., Nielsen, J., Otzen, D. E., Li, J.-Y. & Jensen, P. H. (2022). Low dose DMSO treatment induces oligomerization and accelerates aggregation of α-synuclein. Scientific Reports, 12, Article 3737. https://doi.org/10.1038/s41598-022-07706-2

Rasmussen, C. B., Christiansen, G., Vad, B. S., Lynggaard, C., Enghild, J. J., Andreasen, M. & Otzen, D. (2019). Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation. Protein Science, 28(3), 633-642. https://doi.org/10.1002/pro.3566

Rasmussen, H. Ø., Enghild, J. J., Otzen, D. E. & Pedersen, J. S. (2020). Unfolding and partial refolding of a cellulase from the SDS-denatured state: From β-sheet to α-helix and back. B B A - General Subjects, 1864(1), 129434 1-12. Article 129434. https://doi.org/10.1016/j.bbagen.2019.129434

Rasmussen, H. Ø., Otzen, D. E. & Pedersen, J. S. (2021). A multimethod approach for analyzing FapC fibrillation and determining mass per length. Biophysical Journal, 120(11), 2262-2275. https://doi.org/10.1016/j.bpj.2021.03.031

Rasmussen, H. Ø., Otzen, D. E. & Pedersen, J. S. (2022). Induction, inhibition, and incorporation: Different roles for anionic and zwitterionic lysolipids in the fibrillation of the functional amyloid FapC. The Journal of Biological Chemistry, 298(2), Article 101569. https://doi.org/10.1016/j.jbc.2022.101569

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

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

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

Rantalainen, K., Christensen, P. A., Hafrén, A., Otzen, D., Kalkkinen, N. & Mäkinen, K. (2009). Interaction of a potyviral VPg with anionic phospholipid vesicles. Virology, 395, 114-120.

Rahimi Aqdam, S., Otzen, D. E., Mahmoodi, N. M. & Morshedi, D. (2021). Adsorption of azo dyes by a novel bio-nanocomposite based on whey protein nanofibrils and nano-clay: Equilibrium isotherm and kinetic modeling. Journal of Colloid and Interface Science, 602, 490-503. https://doi.org/10.1016/j.jcis.2021.05.174

Poulsen, E. T., Runager, K., Risør, M. W., Dyrlund, T. F., Scavenius, C., Karring, H., Praetorius, J., Vorum, H., Otzen, D. E., Klintworth, G. K. & Enghild, J. J. (2014). Comparison of two phenotypically distinct lattice corneal dystrophies caused by mutations in the transforming growth factor beta induced (TGFBI) gene. Proteomics - Clinical Applications, 8(3-4), 168-177. https://doi.org/10.1002/prca.201300058

Poghosyan, A. H., Schafer, N., Lyngsø, J., Shahinyan, A. A., Pedersen, J. S. & Otzen, D. (2019). Molecular dynamics study of ACBP denaturation in alkyl sulfates demonstrates possible pathways of unfolding through fused surfactant clusters. Protein Engineering, Design and Selection, 32(4), 175-190. Article gzz037. https://doi.org/10.1093/protein/gzz037

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

Pirhaghi, M., Frank, S. A., Alam, P., Nielsen, J., Sereikaite, V., Gupta, A., Strømgaard, K., Andreasen, M., Sharma, D., Saboury, A. A. & Otzen, D. E. (2022). A penetratin-derived peptide reduces the membrane permeabilization and cell toxicity of α-synuclein oligomers. Journal of Biological Chemistry, 298(12), Article 102688. https://doi.org/10.1016/j.jbc.2022.102688

Pirhaghi, M., Mamashli, F., Moosavi-Movahedi, F., Arghavani, P., Amiri, A., Davaeil, B., Mohammad-Zaheri, M., Mousavi-Jarrahi, Z., Sharma, D., Langel, Ü., Otzen, D. E. & Saboury, A. A. (2024). Cell-Penetrating Peptides: Promising Therapeutics and Drug-Delivery Systems for Neurodegenerative Diseases. Molecular Pharmaceutics, 21(5), 2097-2117. https://doi.org/10.1021/acs.molpharmaceut.3c01167

Pigolotti, S., Lizana, L., Otzen, D. & Sneppen, K. (2013). Quality control system response to stochastic growth of amyloid fibrils. FEBS Letters, 587(9), 1405-1410. https://doi.org/10.1016/j.febslet.2013.03.018

Peña-Díaz, S., Olsen, W. P., Wang, H. & Otzen, D. E. (2024). Functional Amyloids: The Biomaterials of Tomorrow? Advanced Materials, 36(18), Article 2312823. https://doi.org/10.1002/adma.202312823

Peña-Díaz, S., Ferreira, P., Ramos, M. J. & Otzen, D. E. (2024). Mining and engineering activity in catalytic amyloids. Methods in Enzymology, 697, 345-422. https://doi.org/10.1016/bs.mie.2024.03.002

Pedersen, J. S. & Otzen, D. (2008). Amyloid - a state in many guises: survival of the fittest fibril fold. Protein Science, 17, 1-9.

Pedersen, L. R. L., Nielsen, S. B., Hansted, J. G., Petersen, T. E., Otzen, D. E. & Sørensen, E. S. (2012). PP3 forms stable tetrameric structures through hydrophobic interactions via the C-terminal amphipathic helix and undergoes reversible thermal dissociation and denaturation. FEBS journal, 279(2), 336-47. https://doi.org/10.1111/j.1742-4658.2011.08428.x

Pedersen, J. S., Andersen, C. B. & Otzen, D. (2010). Amyloid structure--one but not the same: the many levels of fibrillar polymorphism. FEBS journal, 277(22), 4591-4601. https://doi.org/10.1111/j.1742-4658.2010.07888.x

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Revised 17.04.2023

Lise Refstrup Linnebjerg Pedersen