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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.

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

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.

Otzen, D. E., Morshedi, D., Mohammad-Beigi, H. & Aliakbari, F. (2021). A Triple Role for a Bilayer: Using Nanoliposomes to Cross and Protect Cellular Membranes. Journal of Membrane Biology, 254(1), 29-39. https://doi.org/10.1007/s00232-020-00159-6

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

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

Giehm, L., Lorenzen, N. & Otzen, D. E. (2010). Assays for α-synuclein aggregation. Methods. https://doi.org/10.1016/j.ymeth.2010.12.008

Giehm, L., Lorenzen, N. & Otzen, D. (2011). Assays for alpha-synuclein aggregation. Methods, 53(3), 295-305.

Otzen, D. E. & Oliveberg, M. (2001). A simple way to measure protein refolding rates in water. Journal of Molecular Biology, 313(3), 479-483. https://doi.org/10.1006/jmbi.2001.5039

Weber, M., Tome, L., Otzen, D. & Schneider, D. (2012). A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer. BBA General Subjects, 1818(9), 2103-7. https://doi.org/10.1016/j.bbamem.2012.04.003

Choong, F. X., Huzell, S., Rosenberg, M., Eckert, J. A., Nagaraj, M., Zhang, T., Melican, K., Otzen, D. E. & Richter-Dahlfors, A. (2021). A semi high-throughput method for real-time monitoring of curli producing Salmonella biofilms on air-solid interfaces. Biofilm, 3, Article 100060. https://doi.org/10.1016/j.bioflm.2021.100060

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

Mohammad-Beigi, H., Zanganeh, M., Scavenius, C., Eskandari, H., Farzadfard, A., Shojaosadati, S. A., Enghild, J. J., Otzen, D. E., Buell, A. K. & Sutherland, D. S. (2022). A Protein Corona Modulates Interactions of α-Synuclein with Nanoparticles and Alters the Rates of the Microscopic Steps of Amyloid Formation. ACS Nano, 16(1), 1102-1118. https://doi.org/10.1021/acsnano.1c08825

Mohammad-Beigi, H., Kjær, L., Eskandari, H., Aliakbari, F., Christiansen, G., Ruvo, G., L. Ward, J. & Otzen, D. (2019). A Possible Connection Between Plant Longevity and the Absence of Protein Fibrillation: Basis for Identifying Aggregation Inhibitors in Plants. Frontiers in Plant Science, 10(148), Article 148. https://doi.org/10.3389/fpls.2019.00148

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

Haaning, S., Radutoiu, S., Hoffmann, S. V., Dittmer, J., Giehm, L., Otzen, D. & Stougaard, J. (2008). An unusual intrinsically disordered protein from the model legume Lotus japonicus stabilizes proteins in vitro. Journal of Biological Chemistry, 283(45), 31142-52. https://doi.org/10.1074/jbc.M805024200

Otzen, D. E. (2023). Antibodies and α-synuclein: What to target against Parkinson's Disease? B B A - Proteins and Proteomics, 140943. Article 140943. Advance online publication. https://doi.org/10.1016/j.bbapap.2023.140943

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

Otzen, D. (2005). Antagonism, non-native interactions and non-two-state folding in S6 revealed by double-mutant cycle analysis. Protein Engineering, Design and Selection, 18(11), 547-557. https://doi.org/10.1093/protein/gzi063

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

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

Giehm, L., Dal Degan, F., Fraser, P., Klysner, S. & Otzen, D. E. (2010). An Aß concatemer with altered aggregation propensities. BBA General Subjects, 1804(10), 2025-35. https://doi.org/10.1016/j.bbapap.2010.06.023

Otzen, D. E. & Fersht, A. R. (1999). Analysis of protein-protein interactions by mutagenesis: Direct versus indirect effects. Protein Engineering, 12(1), 41-45.

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

Larsen, P., Nielsen, J. L. & Otzen, D. (2008). Amyloid-like adhesins in floc-forming and filamentous bacteria in activated sludge. Applied and Environmental Microbiology, 74, 1517-1526.

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

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

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

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

Larsen, P., Dueholm, M. S., Christiansen, G., Nielsen, J. L., Otzen, D. & Nielsen, P. H. (2007). Amyloid adhesins are abundant in natural biofilms. Env. Microbiol., (9), 3077-3090.

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

Tian, P., Lindorff-Larsen, K., Boomsma, W., Jensen, M. H. & Otzen, D. E. (2016). A Monte Carlo Study of the Early Steps of Functional Amyloid Formation. PLOS ONE, 11(1), Article e0146096. https://doi.org/10.1371/journal.pone.0146096

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

Ali, S. A., Chung, K. H. K., Forgham, H., Olsen, W. P., Kakinen, A., Balaji, A., Otzen, D. E., Davis, T. P. & Javed, I. (2023). Alzheimer's Progenitor Amyloid-β Targets and Dissolves Microbial Amyloids and Impairs Biofilm Function. Advanced Science, 10(29), Article e2301423. https://doi.org/10.1002/advs.202301423

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