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Malmendal, A., Underhaug, J., Otzen, D. E. & Nielsen, N. C. (2010). Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins. P L o S One, 5(4), e10262. https://doi.org/10.1371/journal.pone.0010262

Madsen, J., Pihl, R., Møller, A. H., Tranberg Madsen, A., Otzen, D. & Andersen, K. K. (2015). The anionic biosurfactant rhamnolipid does not denature industrial enzymes. Frontiers in Microbiology, 6, Article 292. https://doi.org/10.3389/fmicb.2015.00292

Madsen, J., Sørensen, T. R., Kaspersen, J. D., Silow, M. B., Vind, J., Pedersen, J. S., Svendsen, A. & Otzen, D. E. (2015). Promoting protein self-association in non-glycosylated Thermomyces lanuginosus lipase based on crystal lattice contacts. BBA Proteins and Proteomics, 154(12), 1914-1921. https://doi.org/10.1016/j.bbapap.2015.09.007

Madsen, J. L. H., Hjørringgaard, C. U., Vad, B. S., Otzen, D. & Skrydstrup, T. (2016). Incorporation of β-Silicon-β3-Amino Acids in the Antimicrobial Peptide Alamethicin Provides a 20-Fold Increase in Membrane Permeabilization. Chemistry: A European Journal, 22(24), 8358-8367. https://doi.org/10.1002/chem.201600445

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

Madsen, J. K., Kaspersen, J. D., Andersen, C. B., Nedergaard Pedersen, J., Andersen, K. K., Pedersen, J. S. & Otzen, D. E. (2017). Glycolipid Biosurfactants Activate, Dimerize, and Stabilize Thermomyces lanuginosus Lipase in a pH-Dependent Fashion. Biochemistry, 56(32), 4256-4268. https://doi.org/10.1021/acs.biochem.7b00420

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

Macchi, F., Hoffmann, S. V., Carlsen, M., Vad, B. S., Imparato, A., Rischel, C. & Otzen, D. (2011). Mechanical stress affects glucagon fibrillation kinetics and fibril structure. Langmuir, 27(20), 12539–12549. https://doi.org/10.1021/la202125c

Macchi, F., Eisenkolb, M., Kiefer, H. & Otzen, D. (2012). The effect of osmolytes on protein fibrillation. International Journal of Molecular Sciences (Online), 13(3), 3801-3819. https://doi.org/10.3390/ijms13033801

Lorenzen, N., E. Wanker, E. & Otzen, D. (2013). Inhibitors of amyloid and oligomer formation. In D. E. Otzen (Ed.), Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties (pp. 345-372). Wiley-VCH. https://doi.org/10.1002/9783527654185

Lorenzen, N., Cohen, S. I. A., Nielsen, S. B., Herling, T. W., Christiansen, G., Dobson, C. M., T. P. Knowles, T. & Otzen, D. (2012). Role of elongation and secondary pathways in S6 amyloid fibril growth. Biophysical Journal, 102(9), 2167-2175. https://doi.org/10.1016/j.bpj.2012.03.047

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

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

Lorenzen, N. & Otzen, D. (2014). Oligomers of α-synuclein: picking the culprit in the line-up. Essays in Biochemistry, 56(1), 137-148. https://doi.org/10.1042/bse0560137

Lorenzen, N., Nielsen, S. B., Yoshimura, Y., Vad, B. S., Andersen, C. B., Betzer, C., Kaspersen, J. D., Christiansen, G., Pedersen, J. S., Jensen, P. H., Mulder, F. A. A. & Otzen, D. E. (2014). How epigallocatechin gallate can inhibit α-synuclein oligomer toxicity in vitro. Journal of Biological Chemistry, 289(31), 21299-21310. https://doi.org/10.1074/jbc.M114.554667

López Hernández, M., Pedersen, J. S. & Otzen, D. E. (2023). Proteins and biosurfactants: Structures, functions, and recent applications. Current Opinion in Colloid and Interface Science, 68, Article 101746. https://doi.org/10.1016/j.cocis.2023.101746

López Hernández, M., Otzen, D. E. & Pedersen, J. S. (2025). Investigating the interactions between an industrial lipase and anionic (bio)surfactants. Journal of Colloid and Interface Science, 679(B), 294-306. https://doi.org/10.1016/j.jcis.2024.10.060

Lopes, P., Dyrnesli, H., Lorenzen, N., Otzen, D. & Ferapontova, E. (2014). Electrochemical Analysis of the Fibrillation of Parkinson's Disease α-synuclein. Analyst, 139(4), 749-756. https://doi.org/10.1039/C3AN01616A

Lopes, P., Dyrnesli, H., Lorenzen, N., Otzen, D. & Ferapontova, E. (2013). Electroanalysis of Amyloid Formation of Parkinson's Disease alpha-Synuclein. Abstract from 6th International Workshop on Surface Modification for Chemical and Biochemical Sensing, Warsaw, Poland.

Lindberg, M. O., Tångrot, J., Otzen, D. E., Dolgikh, D. A., Finkelstein, A. V. & Oliveberg, M. (2001). Folding of circular permutants with decreased contact order: General trend balanced by protein stability. Journal of Molecular Biology, 314(4), 891-900. https://doi.org/10.1006/jmbi.2001.5186

Li, Y., Dong, M., Otzen, D., Yao, Y., Liu, B., Besenbacher, F. & Mamdouh, W. (2009). Influence of tunable external stimuli on the self-assembly of guanosine supramolecular nanostructures studied by atomic force microscope. Langmuir, 25.

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.

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.

Larsen, K., Bæk, R., Sahin, C., Kjær, L., Christiansen, G., Nielsen, J., Farajzadeh, L. & Otzen, D. E. (2021). Molecular characteristics of porcine alpha-synuclein splicing variants. Biochimie, 180, 121-133. https://doi.org/10.1016/j.biochi.2020.10.019

Kurnik, M., Sahin, C., Andersen, C. B., Lorenzen, N., Giehm, L., Mohammad-Beigi, H., Jessen, C. M., Pedersen, J. S., Christiansen, G., Petersen, S. V., Staal, R., Krishnamurthy, G., Pitts, K., Reinhart, P. H., Mulder, F. A. A., Mente, S., Hirst, W. D. & Otzen, D. E. (2018). Potent α-Synuclein Aggregation Inhibitors, Identified by High-Throughput Screening, Mainly Target the Monomeric State. Cell Chemical Biology, 25(11), 1389-1402. https://doi.org/10.1016/j.chembiol.2018.08.005

Kulminskaya, N. V., Yoshimura, Y., Runager, K., Sørensen, C. S., Bjerring, M., Andreasen, M., Otzen, D. E., Enghild, J. J., Nielsen, N. C. & Mulder, F. A. A. (2016). Near-complete ¹H, ¹³C, ¹⁵N resonance assignments of dimethylsulfoxide-denatured TGFBIp FAS1-4 A546T. Biomolecular N M R Assignments, 10(1), 25-29. https://doi.org/10.1007/s12104-015-9630-2

Kronqvist, N., Otikovs, M., Chmyrov, V., Chen, G., Andersson, M., Nordling, K., Landreh, M., Sarr, M., Jörnvall, H., Wennmalm, S., Widengren, J., Meng, Q., Rising, A., Otzen, D., Knight, S. D., Jaudzems, K. & Johansson, J. (2014). Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation. Nature Communications, 5, Article 3254. https://doi.org/10.1038/ncomms4254

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.

Knudsen, L. J., Nielsen, S. D.-H., Dekker, P., Otzen, D. E., Rauh, V. & Larsen, L. B. (2024). Impact of hydrolysis method and lactase preparation on proteolysis and glycation in long-term stored lactose-hydrolysed UHT milk. International Dairy Journal, 154, Article 105946. https://doi.org/10.1016/j.idairyj.2024.105946

Knudsen, L. J., Rauh, V., Pedersen, J. N., Dekker, P., Otzen, D. E., Larsen, L. B. & Nielsen, S. D. H. (2024). Insight into protein crosslinking and casein polymerization in pre- and posthydrolyzed lactose-free ultra-high-temperature milk during long-term storage. Journal of Dairy Science, 107(12), 10497-10511. https://doi.org/10.3168/jds.2024-25103

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

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