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Krainer, G., Hartmann, A., Bogatyr, V., Nielsen, J., Schlierf, M. & Otzen, D. E. (2020). SDS-induced multi-stage unfolding of a small globular protein through different denatured states revealed by single-molecule fluorescence. Chemical Science, 11(34), 9141-9153. https://doi.org/10.1039/d0sc02100h

Košmrlj, A., Cordsen, P., Kyrsting, A., Otzen, D., Oddershede, L. B. & Jensen, M. H. (2015). A monomer-trimer model supports intermittent glucagon fibril growth. Scientific Reports, 5, 1-6. Article 9005. https://doi.org/10.1038/srep09005

Knudsen, S. K., Westergaard, U. B., Frantzmann, M., Stensballe, A. & Otzen, D. (2008). Effect of glycosylation on biphysical and flocculative properties of the extracellular domain of Ag43. Biochemical Journal, (412), 563-577.

Knudsen, A. D., Bennike, T., Kjeldal, H., Birkelund, S., Otzen, D. & Stensballe, A. (2014). Condenser: A statistical aggregation tool for multi-sample quantitative proteomic data from Matrix Science Mascot Distiller™. Journal of Proteomics, 103, 261-266. https://doi.org/10.1016/j.jprot.2014.02.001

Knudsen, L. J., Nielsen, S. D-H., Rauh, V., Otzen, D., Dekker, P. J. T. & Larsen, L. B. (2019). Interrelations between chemical changes in lactose-free UHT milk. Abstract from 16th Symposium on Milk Genomics and Human Health, Aarhus, Denmark.

Knudsen, L. J., Nielsen, S. D-H., Rauh, V., Otzen, D. & Larsen, L. B. (2019). New Lactase Enzymes. Abstract from Sandbjerg Seminar 2019, Sønderborg, Denmark.

Knudsen, L. J., Nielsen, S. D., Rauh, V., Otzen, D., Dekker, P. J. T. & Larsen, L. B. (2019). Interrelations between chemical changes in lactose-free UHT milk. Abstract from Sandbjerg Seminar 2019, Sønderborg, Denmark.

Kjærgaard, M., Rasmussen, L. S., Vinther, J. N., Andersen, K. R., Andersen, E. S., Lorentzen, E., Thirup, S. S., Otzen, D. & Brodersen, D. E. (2022). A Semester-Long Learning Path Teaching Computational Skills via Molecular Graphics in PyMOL. The Biophysicist, 3(2), 106–114. https://doi.org/10.35459/tbp.2022.000219

Kjær, L., Giehm, L., Heimburg, T. R. & Otzen, D. (2009). The influence of vesicle composition and size on a-synuclein structure and stability. Biophysical Journal, 96.

Kim, J-Y., Sahu, S., Yau, Y-H., Wang, X., Shochat, S. G., Nielsen, P. H., Dueholm, M. S., Otzen, D. E., Lee, J., Delos Santos, M. M. S., Yam, J. K. H., Kang, N-Y., Park, S-J., Kwon, H., Seviour, T. W., Yang, L., Givskov, M. & Chang, Y-T. (2016). Detection of pathogenic biofilms with bacterial amyloid targeting fluorescent probe, CDy11. Journal of the American Chemical Society, 138(1), 402-407. https://doi.org/10.1021/jacs.5b11357

Kilic, N., Stensballe, A., Otzen, D. & Dönmez, G. (2009). Proteomic changes in response to chromium(VI) toxicity in Pseudomonas aeruginosa . Bioresource Technology, 101, 2134-2140.

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

Kaspersen, J., Moestrup Jessen, C., Stougaard Vad, B., Skipper Sørensen, E., Kleiner Andersen, K., Glasius, M., Pinto Oliveira, C. L., Otzen, D. & Pedersen, J. S. (2014). Low-Resolution Structures of OmpA⋅DDM Protein-Detergent Complexes. ChemBioChem, 15(14), 2113-2124. https://doi.org/10.1002/cbic.201402162

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

Kaspersen, J. D., Søndergaard, A., Madsen, D. J., Otzen, D. E. & Pedersen, J. S. (2017). Refolding of SDS-Unfolded Proteins by Nonionic Surfactants. Biophysical Journal, 112(8), 1609-1620. https://doi.org/10.1016/j.bpj.2017.03.013

Kalashnyk, N., Nielsen, J. T., Nielsen, E. H., Skrydstrup, T., Otzen, D., Lægsgaard, E., Wang, C., Besenbacher, F., Nielsen, N. C. & Linderoth, T. R. (2012). Scanning tunneling microscopy reveals single-molecule insights into the self-assembly of amyloid fibrils. A C S Nano, 6(8), 6882-6889. https://doi.org/10.1021/nn301708d

Juul-Madsen, K., Qvist, P., Bendtsen, K. L., Langkilde, A. E., Vestergaard, B., Howard, K., Dehesa-Etxebeste, M., Paludan, S. R., Andersen, G. R., Jensen, P. H., Otzen, D. E., Romero-Ramos, M. & Vorup-Jensen, T. (2020). Size-Selective Phagocytic Clearance of Fibrillar α-Synuclein through Conformational Activation of Complement Receptor 4. Journal of Immunology, 204(5), 1345-1361. https://doi.org/10.4049/jimmunol.1900494

Justesen, P. H., Kristensen, T., Ebdrup, T. & Otzen, D. (2004). Investigating porcine pancreatic phospholipase A ₂ action on vesicles and supported planar bilayers using a quartz crystal microbalance with dissipation. Journal of Colloid and Interface Science, 279(2), 399-409. https://doi.org/10.1016/j.jcis.2004.06.083

Juhl, D. W., Risør, M. W., Scavenius, C., Rasmussen, C. B., Otzen, D., Nielsen, N. C. & Enghild, J. J. (2019). Conservation of the Amyloid Interactome Across Diverse Fibrillar Structures. Scientific Reports, 9(1), Article 3863. https://doi.org/10.1038/s41598-019-40483-z

Jordal, P. L., Dyrlund, T. F., Winge, K., Larsen, M. R., Danielsen, E. H., Wells, J. A., Otzen, D. E. & Enghild, J. J. (2016). Detection of proteolytic signatures for Parkinson's disease. Future Neurology, 11(1), 15-32. https://doi.org/10.2217/fnl.16.3

Jeppesen, M. D., Hein, K., Nissen, P., Westh, P. & Otzen, D. E. (2010). A thermodynamic analysis of fibrillar polymorphism. Advances in Biophysical Chemistry, 149(1-2), 40-6. https://doi.org/10.1016/j.bpc.2010.03.016

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

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.

Jensen, G. V., Pedersen, J. N., Otzen, D. E. & Pedersen, J. S. (2020). Multi-Step Unfolding and Rearrangement of α-Lactalbumin by SDS Revealed by Stopped-Flow SAXS. Frontiers in Molecular Biosciences, 7, Article 125. https://doi.org/10.3389/fmolb.2020.00125

Javed, I., Zhang, Z., Adamcik, J., Andrikopoulos, N., Li, Y., Otzen, D. E., Lin, S., Mezzenga, R., Davis, T. P., Ding, F. & Ke, P. C. (2020). Accelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC. Advanced Science, 7(18), Article 2001299. https://doi.org/10.1002/advs.202001299

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

Jakob, D. S., Wang, H., Zeng, G., Otzen, D. E., Yan, Y. & Xu, X. (2020). Peak Force Infrared - Kelvin Probe Force Microscopy. Angewandte Chemie International Edition, 59(37), 16083-16090. https://doi.org/10.1002/anie.202004211

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

Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995). Nature and Consequences of GroEL-Protein Interactions. Biochemistry, 34(44), 14581-14587. https://doi.org/10.1021/bi00044a037

Hyldgaard, M., Mygind, T., Vad, B. S., Stenvang, M., Otzen, D. & Meyer, R. L. (2014). The Antimicrobial Mechanism of Action of Epsilon-Poly-L-Lysine. Applied and Environmental Microbiology, 80(24), 7758-7770 . https://doi.org/10.1128/AEM.02204-14

Huynh, T. H. V., Mantel, M., Mikkelsen, K., Lindhardt, A. T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2009). A Versatile Approach to β-Amyloid Fibril-Binding Compounds Exploiting the Shirakawa/Hayashi Protocol for trans-Alkene Synthesis. Organic Letters, 11, 999-1002.

Huma, Z-E., Javed, I., Zhang, Z., Bilal, H., Sun, Y., Hussain, S. Z., Davis, T. P., Otzen, D. E., Landersdorfer, C. B., Ding, F., Hussain, I. & Ke, P. C. (2020). Nanosilver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition. Small (Weinheim an der Bergstrasse, Germany), 16(21), Article 1906674. https://doi.org/10.1002/smll.201906674

Hovgaard, M. B., Dong, M., Otzen, D. & Besenbacher, F. (2007). Quartz crystal microbalance studies of multilayer glucagons fibrillation at the solid-liquid interface. Biophysical Journal, 93(6), 2162.

Hovgaard, M. B., Dong, M., Otzen, D. E. & Besenbacher, F. (2007). Quartz crystal microbalance studies of multilayer glucagon fibrillation at the solid-liquid interface. Biophysical Journal, 93(6), 2162-9. https://doi.org/10.1529/biophysj.107.109686

Hourfar, H., Aliakbari, F., Aqdam, S. R., Nayeri, Z., Bardania, H., Otzen, D. E. & Morshedi, D. (2023). The impact of α-synuclein aggregates on blood-brain barrier integrity in the presence of neurovascular unit cells. International Journal of Biological Macromolecules, 229, 305-320. https://doi.org/10.1016/j.ijbiomac.2022.12.134

Højgaard, C., Sørensen, H. V., Pedersen, J. S., Winther, J. R. & Otzen, D. E. (2018). Can a Charged Surfactant Unfold an Uncharged Protein? Biophysical Journal, 115(11), 2081-2086. https://doi.org/10.1016/j.bpj.2018.10.022

Hjorth, C. F., Hubálek, F., Andersson, J., Poulsen, C., Otzen, D. & Naver, H. (2015). Purification and Identification of High Molecular Weight Products Formed During Storage of Neutral Formulation of Human Insulin. Pharmaceutical Research, 32(6), 2072-2085. https://doi.org/10.1007/s11095-014-1600-3

Hjorth, C. F., Norrman, M., Wahlund, P-O., Benie, A. J., Petersen, B. O., Jessen, C. M., Pedersen, T. Å., Vestergaard, K., Steensgaard, D. B., Pedersen, J. S., Naver, H., Hubálek, F., Poulsen, C. & Otzen, D. (2016). Structure, Aggregation, and Activity of a Covalent Insulin Dimer Formed During Storage of Neutral Formulation of Human Insulin. Journal of Pharmaceutical Sciences, 105(4), 1376-1386. https://doi.org/10.1016/j.xphs.2016.01.003

Hjørringgaard, C. U., Vad, B., Nielsen, S. B., Matchkov, V., Vosegaard, T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2010). Cyclodextrin scaffolded alamethicin with highly efficient channel-forming properties. Journal of Peptide Science, 16, 148.

Hjørringgaard, C. U., Vad, B. S., Nielsen, S. B., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2009). Templated Multimers of Antimicrobial Peptides. Poster session presented at 8th Australian Peptide Conference, Peptides - Tools, Targets & Therapeutics , Australia.

Hjørringgaard, C. U., Vad, B. S., Matchkov, V., Nielsen, S. B., Vosegaard, T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2010). Cyclodextrin Scaffolded Alamethicin with Highly Efficient Channel-forming Properties. Poster session presented at 31st European Peptide Symposium, 31EPS, Copenhagen, Denmark.

Hjørringgaard, C. U., Vad, B. S., Matchkov, V., Nielsen, S. B., Vosegaard, T., Nielsen, N. C., Otzen, D. & Skrydstrup, T. (2012). Cyclodextrin-Scaffolded Alamethicin with Remarkably Efficient Membrane Permeabilizing Properties and Membrane Current Conductance. Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 116(26), 7652-7659. https://doi.org/10.1021/jp2098679

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.

Hein, K. L., Kragh-Hansen, U., Morth, J. P., Jeppesen, M., Otzen, D., Møller, J. V. & Nissen, P. (2010). Crystallographic analysis reveals a unique lidocaine binding site on human serum albumin. Journal of Structural Biology, 171, 353-360.

Heegaard, P. M. P., Boas, U. & Otzen, D. (2007). Dendrimer effects on peptide and protein fibrillation. Macromolecular Bioscience, (7), 1047-1059.

He, J., Becares, E. R., Thulstrup, P. W., Gamon, L. F., Pedersen, J. N., Otzen, D., Gourdon, P., Davies, M. J. & Hägglund, P. (2020). Peroxynitrous acid (ONOOH) modifies the structure of anastellin and influences its capacity to polymerize fibronectin. Redox Biology, 36, Article 101631. https://doi.org/10.1016/j.redox.2020.101631

He, J., Steffen, J. H., Thulstrup, P. W., Pedersen, J. N., Sauerland, M. B., Otzen, D. E., Hawkins, C. L., Gourdon, P., Davies, M. J. & Hägglund, P. (2022). Anastellin impacts on the processing of extracellular matrix fibronectin and stimulates release of cytokines from coronary artery smooth muscle cells. Scientific Reports, 12(1), Article 22051. https://doi.org/10.1038/s41598-022-26359-9

Hansted, J. G., Wejse, P. L., Bertelsen, H. & Otzen, D. E. (2011). Effect of protein-surfactant interactions on aggregation of β-lactoglobulin. BBA General Subjects, 1814(5), 713-723. https://doi.org/10.1016/j.bbapap.2011.03.011

Hansen, J. H., Petersen, S. V., Andersen, K. K., Enghild, J. J., Damhus, T. & Otzen, D. (2009). Stable intermediates determine proteins' primary unfolding sites in the presence of surfactants. Biopolymers, 91(3), 221-31. https://doi.org/10.1002/bip.21125

Hajipour, M. J., Mohammad-Beigi, H., Nabipour, I., Mahmoudi, N., Azhdarzadeh, M., Derakhshankhah, H., El Dawud, D., Mohammadinejad, R. & Otzen, D. (2020). Amyloid fibril inhibition, acceleration, or fragmentation: Are nano-based approaches advance in the right direction? Nano Today, 35(December), Article 100983. https://doi.org/10.1016/j.nantod.2020.100983

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Lise Refstrup Linnebjerg Pedersen