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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(1), Article 74. https://doi.org/10.1186/s12974-016-0532-8

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

Alam, P., Bousset, L., Melki, R. & Otzen, D. E. (2019). α-synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicities. Journal of Neurochemistry, 150(5), 522-534. https://doi.org/10.1111/jnc.14808

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

Otzen, D., Sehgal, P. & Westh, P. (2009). α-lactalbumin is unfolded by all classes of detergents but with different mechanisms. Journal of Colloid and Interface Science, 329, 273-283.

Nielsen, S. B., Macchi, F., Raccosta, S., Langkilde, A. E., Giehm, L., Kyrsting, A., Svane, A. S. P., Manno, M., Christiansen, G., Nielsen, N. C., Oddershede, L., Vestergaard, B. & Otzen, D. (2013). Wildtype and A30P Mutant Alpha-Synuclein Form Different Fibril Structures. P L o S One, 8(7), Article e67713. https://doi.org/10.1371/journal.pone.0067713

Jensen, P. L., Dueholm, M. S., Larsen, P., Petersen, S. V., Enghild, J. J., Christiansen, G., Højrup, P., Nielsen, P. H. & Otzen, D. (2009). Widespread abundance of Functional Bacterial Amyloid in Mycolata and other Gram positive Bacteria. Applied and Environmental Microbiology, 75, 4101-4110.

Madsen, J. K., Kaspersen, J. D., Andersen, K. K., Pedersen, J. S. & Otzen, D. E. (2016). When Enzymes and Green Surfactants Meet. Biophysical Journal, 110(3), 211A. https://doi.org/10.1016/j.bpj.2015.11.1171

Otzen, D. & Nielsen, P. H. (2007). We find them here, we find them there: Functional bacterial amyloid. Cell. Mol. Life Sci.

Otzen, D. & Nielsen, P. H. (2008). We find them here, we find them there: Functional bacterial amyloid. Cellular and Molecular Life Sciences, 65, 910-927.

Andersen, K. K., Vad, B. S., Roelants, S., van Bogaert, I. N. A. & Otzen, D. E. (2016). Weak and Saturable Protein-Surfactant Interactions in the Denaturation of Apo-α-Lactalbumin by Acidic and Lactonic Sophorolipid. Frontiers in Microbiology, 7(NOV), Article 1711. https://doi.org/10.3389/fmicb.2016.01711

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

Pedersen, J. N., Frislev, H. K. S., Pedersen, J. S. & Otzen, D. E. (2016). Using protein-fatty acid complexes to improve vitamin D stability. Journal of Dairy Science, 99(10), 7755–7767. https://doi.org/10.3168/jds.2016-11343

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

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

Nielsen, J. T., Bjerring, M., Jeppesen, M., Pedersen, R. O., Pedersen, J. M., Hein, K. L., Vosegaard, T., Skrydstrup, T., Otzen, D. & Nielsen, N. C. (2009). Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy. Angewandte Chemie International Edition, 48, 2118-2121.

Nielsen, J. T., Bjerring, M., Jeppesen, M., Pedersen, R. O., Pedersen, J. M., Hein, K. L., Vosegaard, T., Skrydstrup, T., Otzen, D. & Nielsen, N. C. (2009). Unique Identification of Supramolecular Structures in Amyloid Fibrils by Solid-State NMR. Poster session presented at 50th Experimental NMR Conference (ENC), Asilomar, CA, United States.

Nielsen, M. M., Andersen, K. K., Westh, P. & Otzen, D. (2007). Unfolding of ß-sheet proteins in SDS. Biophysical Journal, (92), 3674-3685.

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

Meisl, G., Xu, C. K., Taylor, J. D., Michaels, T. C. T., Levin, A., Otzen, D., Klenerman, D., Matthews, S., Linse, S., Andreasen, M. & Knowles, T. P. J. (2022). Uncovering the universality of self-replication in protein aggregation and its link to disease. Science Advances, 8(32), Article eabn6831. https://doi.org/10.1126/sciadv.abn6831

Mortensen, H. G., Otzen, D. E. & Pedersen, J. S. (2021). Ubiquitin forms conventional decorated micelle structures with sodium dodecyl sulfate at saturation. Journal of Colloid and Interface Science, 596, 233-244. https://doi.org/10.1016/j.jcis.2021.03.110

Monti, M., Milanetti, E., Frans, M. T., Miotto, M., Di Rienzo, L., Baranov, M. V., Gosti, G., Somavarapu, A. K., Nagaraj, M., Golbek, T. W., Rossing, E., Moons, S. J., Boltje, T. J., van den Bogaart, G., Weidner, T., Otzen, D. E., Tartaglia, G. G., Ruocco, G. & Roeters, S. J. (2024). Two Receptor Binding Strategy of SARS-CoV-2 Is Mediated by Both the N-Terminal and Receptor-Binding Spike Domain. The journal of physical chemistry. B, 128(2), 451-464. https://doi.org/10.1021/acs.jpcb.3c06258

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

Melo, E. P., Chen, L. Y., Cabral, J. M. S., Fojan, P., Petersen, S. B. & Otzen, D. E. (2003). Trehalose favors a cutinase compact intermediate off-folding pathway. Biochemistry, 42(24), 7611-7617. https://doi.org/10.1021/bi034267x

Otzen, D. E. & Oliveberg, M. (2004). Transient formation of nano-crystalline structures during fibrillation of an Aβ-like peptide. Protein Science, 13(5), 1417-1421. https://doi.org/10.1110/ps.03538904

Otzen, D. E., Miron, S., Akke, M. & Oliveberg, M. (2004). Transient aggregation and stable dimerization induced by introducing an Alzheimer sequence into a water-soluble protein. Biochemistry, 43(41), 12964-12978. https://doi.org/10.1021/bi048509k

Pathak, G. S., Hinge, M. & Otzen, D. (2023). Transdisciplinary Pragmatic Melioration for the Plastic Life Cycle: Why the Social, Natural, and Technical Sciences Should Prioritize Reducing Harm. Science of the Total Environment, 895, Article 165154. https://doi.org/10.1016/j.scitotenv.2023.165154

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, 113(8), 2098-2103. https://doi.org/10.1073/pnas.1524027113

Malmos, K., Blancas-Mejia, L. M., Weber, B., Buchner, J., Ramirez-Alvarado, M., Naiki, H. & Otzen, D. (2017). ThT 101: a primer on the use of thioflavin T to investigate amyloid formation. Amyloid: the Journal of Protein Folding Disorders, 24(1), 1-16. https://doi.org/10.1080/13506129.2017.1304905

Madsen, J. K., Giehm, L. & Otzen, D. E. (2018). The Use of Surfactants to Solubilise a Glucagon Analogue. Pharmaceutical Research, 35(12), Article 235. https://doi.org/10.1007/s11095-018-2494-2

Pedersen, J. N., Pedersen, J. S. & Otzen, D. E. (2015). The Use of Liprotides To Stabilize and Transport Hydrophobic Molecules. Biochemistry, 54(31), 4815-4823. https://doi.org/10.1021/acs.biochem.5b00547

Basaiawmoit, R. V., Deva, T., Runager, K., Kristensen, T., Enghild, J. J. & Otzen, D. (2009). The Underlying Mechanisms of TGFBIp-mediated Corneal Dystrophies. Abstract from Asia ARVO, International Meeting on Research in Vision and Ophthalmology, Hyderabad International Convention Center. Abstract number: PAP05.01, Hyderabad, India.

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

Agerschou, E. D., Christiansen, G., Schafer, N. P., Madsen, D. J., Brodersen, D. E., Semsey, S. & Otzen, D. E. (2016). The transcriptional regulator GalR self-assembles to form highly regular tubular structures. Scientific Reports, 6, Article 27672. https://doi.org/10.1038/srep27672

Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995). The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding. Journal of Molecular Biology, 254(2), 260-288. https://doi.org/10.1006/jmbi.1995.0616

Marvian, A. T., Aliakbari, F., Mohammad-Beigi, H., Ahmadi, Z. A., Mehrpouyan, S., Lermyte, F., Nasouti, M., Collingwood, J. F., Otzen, D. E. & Morshedi, D. (2020). The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization. International Journal of Biological Macromolecules, 155, 543-550. https://doi.org/10.1016/j.ijbiomac.2020.03.238

Cavallin, A., Arozenius, H., Kristensson, K., Antonsson, P., Otzen, D. E., Björk, P. & Forsberg, G. (2000). The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function. Journal of Biological Chemistry, 275(3), 1665-1672. https://doi.org/10.1074/jbc.275.3.1665

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(NOV), Article 2729. https://doi.org/10.3389/fmicb.2018.02729, https://doi.org/10.3389/fmicb.2018.02729

Lorenzen, N., Nielsen, S. B., Buell, A. K., Kaspersen, J. D., Arosio, P., Vad, B. S., Paslawski, W., Christiansen, G., Valnickova Hansen, Z., Andreasen, M., Enghild, J. J., Pedersen, J. S., Dobson, C. M., Knowles, T. P. J. & Otzen, D. (2014). The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation. Journal of the American Chemical Society, 136(10), 3859-3868. https://doi.org/10.1021/ja411577t

Jeppesen, M. D., Westh, P. & Otzen, D. E. (2010). The role of protonation in protein fibrillation. FEBS Letters, 584(4), 780-4. https://doi.org/10.1016/j.febslet.2010.01.002

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

Andersen, K., Oliveira, C. L. P. D., Larsen, K. L., Poulsen, F., Callisen, T., Westh, P., Pedersen, J. S. & Otzen, D. (2009). The role of decorated SDS micelles in sub-cmc protein denaturation and association. Journal of Molecular Biology, 391, 207-226.

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

Baptista, R. P., Pedersen, S. H., Cabrita, G. J. M., Otzen, D., Cabral, J. M. & Melo, E. P. (2008). Thermodynamics and mechanism of cutinase stabilization by trehalose. Biopolymers, 89, 538-547.

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

Aliakbari, F., Mohammad-Beigi, H., Rezaei-Ghaleh, N., Becker, S., Dehghani Esmatabad, F., Eslampanah Seyedi, H. A., Bardania, H., Tayaranian Marvian, A., Collingwood, J. F., Christiansen, G., Zweckstetter, M., Otzen, D. E. & Morshedi, D. (2018). The potential of zwitterionic nanoliposomes against neurotoxic alpha-synuclein aggregates in Parkinson's Disease. Nanoscale, 10(19), 9174-9185. https://doi.org/10.1039/c8nr00632f

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, 119(25), Article e2203098119. https://doi.org/10.1073/pnas.2203098119

Lorenzen, N., Lemminger, L., Pedersen, J. N., Nielsen, S. B. & Otzen, D. (2014). The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes. FEBS Letters, 588(3), 497-502. https://doi.org/10.1016/j.febslet.2013.12.015

Helwig, M., Hoshino, A., Berridge, C., Lee, S.-N., Lorenzen, N., Otzen, D., Eriksen, J. & Lindberg, I. (2013). The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins. Journal of Biological Chemistry, 288(2), 1114.

Jarvela, T. S., Lam, H. A., Helwig, M., Lorenzen, N., Otzen, D. E., McLean, P. J., Maidment, N. T. & Lindberg, I. (2016). The neural chaperone proSAAS blocks α-synuclein fibrillation and neurotoxicity. Proceedings of the National Academy of Sciences, 113(32), E4708-E4715. https://doi.org/10.1073/pnas.1601091113

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