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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

Peña-Díaz, S., Jiang, Y., Zhang, Z., Daugberg, A., Ferreira, P., López Hernández, M., Mittal, C., Ramos, M. J., Pedersen, J. S., Dueholm, M. K. D., Qin, C., Wang, H. & Otzen, D. E. (2026). The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid. Advanced Science, 13(4), Article e17090. https://doi.org/10.1002/advs.202517090

Peña Díaz, S., Zhang, Z., Jiang, Y., Daugberg, A. O. H., López Hernández, M., Nielsen, J., Dueholm, M. K. D., Dong, MD., Pedersen, J. S., Otzen, D. E. & Wang, H. (2025). Natural Design of a Stabilized Cross-β Fold: Structure of the FuA FapC from Pseudomonas Sp. UK4 Reveals a Critical Role for Stacking of Imperfect Repeats. Advanced Materials, 37(34), Article 2505503. https://doi.org/10.1002/adma.202505503

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

Pedersen, L. R. L., Hansted, J. G., Nielsen, S. B., Petersen, T. E., Sørensen, U. S., Otzen, D. & Sørensen, E. S. (2012). Proteolytic activation of proteose peptone component 3 by release of a C-terminal peptide with antibacterial properties. Journal of Dairy Science, 95(6), 2819-2829. https://doi.org/10.3168/jds.2011-4837

Pedersen, J. S., Dikov, D. & Otzen, D. (2006). N- and C-Terminal Hydrophobic Patches Are Involved in Fibrillation of Glucagon. Biochemistry, 45(48), 14503-14512. https://doi.org/10.1021/bi061228n

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

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

Pedersen, J. N., Frislev, H. K. S., Pedersen, J. S. & Otzen, D. (2016). Liprotides: a New Class of Protein Lipid-Complexes. Abstract from Biophysical Society 60th Annual Meeting, Los Angeles, United States. https://doi.org/10.1016/j.bpj.2015.11.3085

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

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

Pedersen, J. N., Jiang, Z., Christiansen, G., Lee, J. C., Pedersen, J. S. & Otzen, D. E. (2019). Lysophospholipids induce fibrillation of the repeat domain of Pmel17 through intermediate core-shell structures. Biochimica et Biophysica Acta - Proteins and Proteomics, 1867(5), 519-528. https://doi.org/10.1016/j.bbapap.2018.11.007

Pedersen, J. S., Christensen, G. & Otzen, D. E. (2004). Modulation of S6 fibrillation by unfolding rates and gatekeeper residues. Journal of Molecular Biology, 341(2), 575-588. https://doi.org/10.1016/j.jmb.2004.06.020

Pedersen, J. N., Lyngsø, J., Zinn, T., Otzen, D. & Pedersen, J. S. (2020). A complete picture of protein unfolding and refolding in surfactants. Chemical Science, 11(3), 699-712. https://doi.org/10.1039/C9SC04831F

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

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

Paslawski, W., Mysling, S., Thomsen, K., Jørgensen, T. J. D. & Otzen, D. (2014). Co-existence of Two Different α-Synuclein Oligomers with Different Core Structures Determined by Hydrogen/Deuterium Exchange Mass Spectrometry. Angewandte Chemie International Edition, 53(29), 7560-7563. https://doi.org/10.1002/anie.201400491

Paslawski, W., Andreasen, M., Nielsen, S. B., Lorenzen, N., Thomsen, K., Kaspersen, J. D., Pedersen, J. S. & Otzen, D. (2014). High stability and cooperative unfolding of cytotoxic α-synuclein oligomers. Biochemistry, 53(39), 6252-6263. https://doi.org/10.1021/bi5007833

Paslawski, W., Lillelund, O. K., Kristensen, J. V., Schafer, N. P., Baker, R. P., Urban, S. & Otzen, D. E. (2015). Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops. Proceedings of the National Academy of Sciences (PNAS), 112(6), 7978-7983. https://doi.org/10.1073/pnas.1424751112

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

Pantusa, M., Vad, B., Lillelund, O., Kjær, L., Otzen, D. & Bartucci, R. (2016). Alpha-synuclein and familial variants affect the chain order and the thermotropic phase behavior of anionic lipid vesicles. Biochimica et Biophysica Acta - Proteins and Proteomics, 1864(9), 1206-1214. https://doi.org/10.1016/j.bbapap.2016.05.003

Paiva, P., Teixeira, L. M. C., Wei, R., Liu, W., Weber, G., Morth, J. P., Westh, P., Petersen, A. R., Johansen, M. B., Sommerfeldt, A., Sandahl, A., Otzen, D. E., Fernandes, P. A. & Ramos, M. J. (2025). Unveiling the enzymatic pathway of UMG-SP2 urethanase: insights into polyurethane degradation at the atomic level. Chemical Science, 16(5), 2437-2452. https://doi.org/10.1039/d4sc06688j

Paiva, P., Teixeira, L. M. C., Ferreira, P., Otzen, D. E., Fernandes, P. A. & Ramos, M. J. (2025). Transforming Computational Power into Environmental Solutions: HPC-driven Research on Urethanase-mediated Plastic Degradation. Procedia Computer Science, 267, 207-217. https://doi.org/10.1016/j.procs.2025.08.247

Otzen, D., Sehgal, P. & Nesgaard, L. (2007). Alternative membrane protein conformations in alcohol. Biochemistry, (46), 4348-4359.

Otzen, D. & Nielsen, P. H. (2007). We find them here, we find them there: Functional bacterial amyloid. Cellular and Molecular Life Sciences, 65, 910-927.

Otzen, D. (2008). Differential adsorption of variants of the thermomyces lanuginosus lipase on a hydrophobic surface suggests a role for local flexibility. Colloids and Surfaces B: Biointerfaces, (64), 223-228.

Otzen, D., Nesgaard, L., Andersen, K. K., Hansen, J. H., Christiansen, G., Doe, H. & Sehgal, P. (2008). Aggregation of S6 in a quasi-native state by monomeric SDS. Biochimica et Biophysica Acta - Biomembranes, (1784), 400-414.

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.

Otzen, D. E. (2011). Mapping the folding pathway of the transmembrane protein DsbB by protein engineering. Protein Engineering, Design and Selection, 24(1-2), 139-149. https://doi.org/10.1093/protein/gzq079

Otzen, D. E. (2010). Amyloid formation in surfactants and alcohols: membrane mimetics or structural switchers? Current protein & peptide science, 11(5), 355-71.

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

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

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

Otzen, D. (2010). Institutional nonconformism: the many levels of glucagon polymorphism. FEBS journal.

Otzen, D. & Enghild, J. J. (2010). Human phenotypically distinct TGFI corneal dystrophies are linked to the stability of the fourth Fas1 domain of TGFBIp. Journal of Biological Chemistry.

Otzen, D. (2010). Occupancy of non-annular lipid binding sites on KcsA greatly increases the stability of the tetrameric protein. Biochemistry.

Otzen, D. E. (2011). Assembling good amyloid some structures at last. Structure, 19(9), 1207-1209. https://doi.org/10.1016/j.str.2011.08.005

Otzen, D. (2011). Protein-surfactant interactions a tale of many states. BBA General Subjects, 1814(5), 562-91. https://doi.org/10.1016/j.bbapap.2011.03.003

Otzen, D. (2012). N for AsN - O for StrOcture? A strand-loop-strand motif for prokaryotic O-glycosylation. Molecular Oral Microbiology. https://doi.org/10.1111/j.1365-2958.2012.07972.x

Otzen, D., Blans, K., Wang, H., Gilbert, G. E. & Rasmussen, J. T. (2012). Lactadherin binds to phosphatidylserine-containing vesicles in a two-step mechanism sensitive to vesicle size and composition. BBA General Subjects, 1818(4), 1019-1027. https://doi.org/10.1016/j.bbamem.2011.08.032

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

Otzen, D. (2014). Membrane protein folding and stability. Archives of Biochemistry and Biophysics, 564, 262-264. https://doi.org/10.1016/j.abb.2014.10.014

Otzen, D. (2015). Protein aggregation: Close encounters of the greasy kind. Nature Chemical Biology, 11(3), 176-177. https://doi.org/10.1038/nchembio.1759

Otzen, D. E. (2015). Proteins in a brave new surfactant world. Current Opinion in Colloid & Interface Science, 20(3), 161-169. https://doi.org/10.1016/j.cocis.2015.07.003

Otzen, D. (2017). Biosurfactants and surfactants interacting with membranes and proteins: Same but different? Biochimica et Biophysica Acta - Biomembranes, 1859(4), 639–649. https://doi.org/10.1016/j.bbamem.2016.09.024

Otzen, D. E., Vad, B. S., Dueholm, M. S., Nielsen, P. H., Rouse, S. L. & Matthews, S. J. (2017). Self-organizing amyloid in bacteria. European Biophysics Journal, 46, S98-S98.

Otzen, D. E., Vad, B. S., Dueholm, M. S., Nielsen, P. H., Rouse, S. L. & Matthews, S. J. (2017). Self-organizing amyloid in bacteria. European Biophysics Journal, 46(supp 1), S341-S341. https://doi.org/10.1007/s00249-017-1222-x

Displaying results 101 to 150 out of 473

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Revised 08.12.2025

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Lise Refstrup Linnebjerg Pedersen