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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

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

Otzen, D. E., Kristensen, O. & Oliveberg, M. (2000). Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly. Proceedings of the National Academy of Sciences (PNAS), 97(18), 9907-9912. https://doi.org/10.1073/pnas.160086297

Giehm, L., Christensen, C., Boas, U., Heegaard, P. M. H. & Otzen, D. (2008). Dendrimers destabilize proteins in a generation-dependent manner involving eletrostatic interactions. Biopolymers, 89, 522-529.

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

Andersen, K. K. & Otzen, D. (2014). Denaturation of α-lactalbumin and myoglobin by the anionic biosurfactant rhamnolipid. B B A - Bioenergetics, 1844(12), 2338-2345. https://doi.org/10.1016/j.bbapap.2014.10.005

Otzen, D. E., Pedersen, J. N., Somavarapu, A. K., Clement, A., Ji, M., Petersen, E. H., Pedersen, J. S., Urban, S. & Schafer, N. P. (2021). Cys-labelling kinetics of membrane protein GlpG: a role for specific SDS binding and micelle changes? Biophysical Journal, 120(18), 4115-4128. https://doi.org/10.1016/j.bpj.2021.08.001

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

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., 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.

Dueholm, M. S., Albertsen, M., Otzen, D. & Nielsen, P. H. (2012). Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure. P L o S One, 7(12), e51274. https://doi.org/10.1371/journal.pone.0051274

Amodeo, G. F., Lee, B. Y., Krilyuk, N., Filice, C. T., Valyuk, D., Otzen, D. E., Noskov, S., Leonenko, Z. & Pavlov, E. V. (2021). C subunit of the ATP synthase is an amyloidogenic calcium dependent channel-forming peptide with possible implications in mitochondrial permeability transition. Scientific Reports, 11(1), Article 8744. https://doi.org/10.1038/s41598-021-88157-z

Olsen, W. P., Courtade, G., Peña-Díaz, S., Nagaraj, M., Sønderby, T. V., Mulder, F. A. A., Malle, M. G. & Otzen, D. E. (2024). CsgA gatekeeper residues control nucleation but not stability of functional amyloid. Protein Science, 33(10), Article e5178. https://doi.org/10.1002/pro.5178

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.

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

Otzen, D. E. & Oliveberg, M. (2004). Correspondence between anomalous m- and ΔC_p-values in protein folding. Protein Science, 13(12), 3253-3263. https://doi.org/10.1110/ps.04991004

Malmos, K. G., Bjerring, M., Jessen, C. M., Nielsen, E. H. T., Poulsen, E. T., Christiansen, G., Vosegaard, T., Skrydstrup, T., Enghild, J. J., Pedersen, J. S. & Otzen, D. E. (2017). Correction to: How glycosaminoglycans promote fibrillation of salmon calcitonin. Journal of Biological Chemistry, 292(38), 15992. https://doi.org/10.1074/jbc.A116.715466

Stenvang, M., Schafer, N. P., Malmos, K. G., Pérez, A.-M. W., Niembro, O., Sormanni, P., Basaiawmoit, R. V., Christiansen, G., Andreasen, M. & Otzen, D. E. (2018). Corneal dystrophy mutations drive pathogenesis by targeting TGFBIp stability and solubility in a latent amyloid-forming domain. Journal of Molecular Biology, 430(8), 1116-1140. https://doi.org/10.1016/j.jmb.2018.03.001

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

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

Otzen, D. E. & Oliveberg, M. (2002). Conformational plasticity in folding of the split β-α-β protein S6: Evidence for burst-phase disruption of the native state. Journal of Molecular Biology, 317(4), 613-627. https://doi.org/10.1006/jmbi.2002.5423

De Prat Gay, G., Ruiz-Sanz, J., Neira, J. L., Corrales, F. J., Otzen, D. E., Ladurner, A. G. & Fersht, A. R. (1995). Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway. Journal of Molecular Biology, 254(5), 968-979. https://doi.org/10.1006/jmbi.1995.0669

Otzen, D. E. (2005). Conformational detours during folding of a collapsed state. Biochimica et Biophysica Acta - Proteins and Proteomics, 1750(2), 146-153. https://doi.org/10.1016/j.bbapap.2005.05.006

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

Andersen, K. K., Vad, B., Omer, S. & Otzen, D. E. (2016). Concatemers of Outer Membrane Protein A Take Detours in the Folding Landscape. Biochemistry, 55(51), 7123–7140. https://doi.org/10.1021/acs.biochem.6b01153

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

Bendtsen, M. K., Nowak, J. S., Paiva, P., López Hernández, M., Ferreira, P., Pedersen, J. S., Bekker, N. S., Viezzi, E., Bisiak, F., Brodersen, D. E., Pedersen, L. H., Zervas, A., Fernandes, P. A., Ramos, M. J., Stougaard, P., Thøgersen, M. S. & Otzen, D. E. (2025). Cold-Active Starch-Degrading Enzymes from a Cold and Alkaline Greenland Environment: Role of Ca 2+ Ions and Conformational Dynamics in Psychrophilicity. Biomolecules, 15(3), Article 415. https://doi.org/10.3390/biom15030415

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

Zhang, S., Andreasen, M., Nielsen, J. T., Liu, L., Nielsen, E. H., Song, J., Ji, G., Sun, F., Skrydstrup, T., Besenbacher, F., Nielsen, N. C., Otzen, D. E. & Dong, M. (2013). Coexistence of ribbon and helical fibrils originating from hIAPP20-29 revealed by quantitative nanomechanical atomic force microscopy. Proceedings of the National Academy of Sciences (PNAS), 110(8), 2798-2803. https://doi.org/10.1073/pnas.1209955110

Nayeri, Z., Aliakbari, F., Afzali, F., Parsafar, S., Gharib, E., Otzen, D. E. & Morshedi, D. (2022). Characterization of exogenous αSN response genes and their relation to Parkinson's disease using network analyses. Frontiers in Pharmacology, 13, Article 966760. https://doi.org/10.3389/fphar.2022.966760

Nesgaard, L. W., Hoffmann, S. V., Andersen, C. B., Malmendal, A. & Otzen, D. (2008). Characterization of Dry Globular Proteins and Protein Fibrils by Synchrotron Radiation Vacuum UV Circular Dichroism. Biopolymers, 89(9), 779-795.

Nagaraj, M., Najarzadeh, Z., Pansieri, J., Biverstål, H., Musteikyte, G., Smirnovas, V., Matthews, S., Emanuelsson, C., Johansson, J., Buxbaum, J. N., Morozova-Roche, L. & Otzen, D. E. (2022). Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation. Chemical Science, 13(2), 536-553. https://doi.org/10.1039/d1sc05790a

Dalsgaard, T. K., Otzen, D., Nielsen, J. H. & Larsen, L. B. (2007). Changes in structures of milk proteins upon photo-oxidation. J. Agr. Food Chem., (55), 10968-10976.

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

Debnath, D. K. & Otzen, D. E. (2010). Cell-free synthesis and folding of transmembrane OmpA reveals higher order structures and premature truncations. Advances in Biophysical Chemistry, 152(1-3), 80-8. https://doi.org/10.1016/j.bpc.2010.08.003

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

Otzen, D. E. & Oliveberg, M. (2002). Burst-phase expansion of native protein prior to global unfolding in SDS. Journal of Molecular Biology, 315(5), 1231-1240. https://doi.org/10.1006/jmbi.2001.5300

Noji, M., Samejima, T., Yamaguchi, K., So, M., Yuzu, K., Chatani, E., Akazawa-Ogawa, Y., Hagihara, Y., Kawata, Y., Ikenaka, K., Mochizuki, H., Kardos, J., Otzen, D. E., Bellotti, V., Buchner, J. & Goto, Y. (2021). Breakdown of supersaturation barrier links protein folding to amyloid formation. Communications Biology, 4(1), Article 120. https://doi.org/10.1038/s42003-020-01641-6

Beyschau Andersen, C., Yagi, H., Manno, M., Martorana, V., Ban, T., Christiansen, G., Otzen, D., Goto, Y. & Rischel, C. (2009). Branching in amyloid fibril growth. Biophysical Journal, 96(4), 1529-36. https://doi.org/10.1016/j.bpj.2008.11.024

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

Nielsen, N. S., Poulsen, E. T., Lukassen, M. V., Chao Shern, C., Mogensen, E. H., Weberskov, C. E., DeDionisio, L., Schauser, L., Moore, T. C. B., Otzen, D. E., Hjortdal, J. & Enghild, J. J. (2020). Biochemical mechanisms of aggregation in TGFBI-linked corneal dystrophies. Progress in Retinal and Eye Research, 77, Article 100843. https://doi.org/10.1016/j.preteyeres.2020.100843

Christensen, N. R., Pedersen, C. P., Sereikaite, V., Pedersen, J. N., Vistrup-Parry, M., Sørensen, A. T., Otzen, D., Teilum, K., Madsen, K. L. & Strømgaard, K. (2022). Bidirectional protein-protein interactions control liquid-liquid phase separation of PSD-95 and its interaction partners. iScience, 25(2), Article 103808. https://doi.org/10.1016/j.isci.2022.103808

Nielsen, S. B., Franzmann, M., Basaiawmoit, R. V., Wimmer, R., Mikkelsen, J. D. & Otzen, D. E. (2010). beta-Sheet aggregation of kisspeptin-10 is stimulated by heparin but inhibited by amphiphiles. Biopolymers, 93(8), 678-89. https://doi.org/10.1002/bip.21434

Otzen, D. & d'Angelo, J. (2024). BBA: 2024 and beyond. Biochimica et Biophysica Acta - General Subjects, 1868(2), Article 130524. https://doi.org/10.1016/j.bbagen.2023.130524

Mogensen, J. E., Tapadar, D., Schmidt, M. A. & Otzen, D. (2005). Barriers to Folding of the Transmembrane Domain of the Escherichia coli Autotransporter Adhesin Involved in Diffuse Adherence. Biochemistry, 44, 4533-4545. https://doi.org/10.1021/bi0475121

Skals, M., Bjaelde, R. G., Reinholdt, J., Poulsen, K., Vad, B. S., Otzen, D., Leipziger, J. & Praetorius, H. A. (2014). Bacterial RTX Toxins Allow Acute ATP Release from Human Erythrocytes Directly through the Toxin Pore. Journal of Biological Chemistry, 289, 19098-19109. https://doi.org/10.1074/jbc.M114.571414

Christensen, L. F. B., Schafer, N., Wolf-Perez, A., Madsen, D. J. & Otzen, D. E. (2019). Bacterial Amyloids: Biogenesis and Biomaterials. In S. Perrett, A. K. Buell & T. P. J. Knowles (Eds.), Advances in Experimental Medicine and Biology (pp. 113-159). Springer. https://doi.org/10.1007/978-981-13-9791-2_4

Najarzadeh, Z., Pedersen, J. N., Christiansen, G., Shojaosadati, S. A., Pedersen, J. S. & Otzen, D. E. (2019). Bacterial amphiphiles as amyloid inducers: Effect of Rhamnolipid and Lipopolysaccharide on FapC fibrillation. B B A - Proteins and Proteomics, 1867(11), Article 140263. https://doi.org/10.1016/j.bbapap.2019.140263

Du, X., Wang, L., Wang, Y., Andreasen, M., Zhan, D., Feng, Y., Li, M., Zhao, M., Otzen, D., Xue, D., Yang, Y. & Liu, R. (2011). Aβ_1-16Can Aggregate and induce the Production of Reactive Oxygen Species, Nitric Oxide, and Inflammatory Cytokines. Journal of Alzheimer's Disease, 27(2), 401-413. https://doi.org/10.3233/JAD-2011-110476

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.

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Lise Refstrup Linnebjerg Pedersen