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Frislev, H. K. S., Pedersen, J. N., Pedersen, J. S. & Otzen, D. E. (2016). Liprotides: Nano-Sized Cytotoxic Protein-Fatty Acid Complexes with a Core-Shell or Multi-Layer Structure. Biophysical Journal, 110(3), 577A. https://doi.org/10.1016/j.bpj.2015.11.3087

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

Frislev, H. K. S., Jessen, C. M., Oliveira, C. L. P., Pedersen, J. S. & Otzen, D. E. (2016). Liprotides made of α-lactalbumin and cis fatty acids form core-shell and multi-layer structures with a common membrane-targeting mechanism. B B A - Proteins and Proteomics, 1864(7), 847-859. https://doi.org/10.1016/j.bbapap.2016.04.003

Frislev, H. K. S., Pedersen, J. N., Pedersen, J. S. & Otzen, D. (2016). Liprotides: Nano-Sized Cytotoxic Protein-Fatty Acid Complexes with a Core-Shell or Multi-Layer Structure. Poster session presented at Biophysical Society 60th Annual Meeting, Los Angeles, United States. http://www.cell.com/biophysj/fulltext/S0006-3495%2815%2904270-8

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

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

Scavenius, C., Nikolajsen, C. L., Stenvang, M., Thøgersen, I., Wyrozemski, L., Wisniewski, H-G., Otzen, D. E., Sanggaard, K. W. & Enghild, J. J. (2016). The compact and biologically relevant structure of inter-α-inhibitor is maintained by the chondroitin sulfate chain and divalent cations. Journal of Biological Chemistry, 291(9), 4658-4670. https://doi.org/10.1074/jbc.M115.678748

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

Agerschou, E. D., Christiansen, G., Schafer, N. P., Madsen, D. J., Brodersen, D. E., Semsey, S. & Otzen, D. E. (2016). The transcriptional regulator GalR self-assembles to form highly regular tubular structures. Scientific Reports, 6, Article 27672. https://doi.org/10.1038/srep27672

Schafer, N., Truong, H. H., Otzen, D., Lindorff-Larsen, K. & Wolynes, P. G. (2016). Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease. Proceedings of the National Academy of Sciences, 113(8), 2098-2103. Advance online publication. https://doi.org/10.1073/pnas.1524027113

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. Advance online publication. https://doi.org/10.3168/jds.2016-11343

Andersen, K. K., Vad, B. S., Roelants, S., van Bogaert, I. N. A. & Otzen, D. E. (2016). Weak and Saturable Protein-Surfactant Interactions in the Denaturation of Apo-α-Lactalbumin by Acidic and Lactonic Sophorolipid. Frontiers in Microbiology, 7(NOV), Article 1711. https://doi.org/10.3389/fmicb.2016.01711

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

Christiansen, J. R., Olesen, M. N., Otzen, D. E., Romero-Ramos, M. & Sanchez-Guajardo, V. (2016). α-Synuclein vaccination modulates regulatory T cell activation and microglia in the absence of brain pathology. Journal of Neuroinflammation, 13(1), Article 74. https://doi.org/10.1186/s12974-016-0532-8

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

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, 112(6), 7978-7983. https://doi.org/10.1073/pnas.1424751112

Seviour, T., Hansen, S. H., Yang, L., Yau, Y. H., Wang, V. B., Stenvang, M. R., Christiansen, G., Marsili, E., Givskov, M., Chen, Y., Otzen, D., Nielsen, P. H., Shochat, S. G., Kjelleberg, S. & Dueholm, M. S. (2015). Functional Amyloids Keep Quorum Sensing Molecules in Check. Journal of Biological Chemistry, 290, 6457-6469. https://doi.org/10.1074/jbc.M114.613810

Zeng, G., Vad, B. S., Dueholm, M. S., Christiansen, G., Nilsson, M., Tolker-Nielsen, T., Nielsen, P. H., Meyer, R. L. & Otzen, D. E. (2015). Functional bacterial amyloid increases Pseudomonas biofilm hydrophobicity and stiffness. Frontiers in Microbiology, 6, 1099. https://doi.org/10.3389/fmicb.2015.01099

Andreasen, M., Lorenzen, N. & Otzen, D. (2015). Interactions between misfolded protein oligomers and membranes: A central topic in neurodegenerative diseases? B B A - Molecular and Cell Biology of Lipids, 1848(9), 1897-1907. Advance online publication. https://doi.org/10.1016/j.bbamem.2015.01.018

Vad, B. S., Balakrishnan, V. S., Nielsen, S. B. & Otzen, D. (2015). Phospholipid Ether Linkages Significantly Modulate the Membrane Affinity of the Antimicrobial Peptide Novicidin. Journal of Membrane Biology, 487-496. https://doi.org/10.1007/s00232-015-9792-y

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

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

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

Christoffersen, H. F., Andreasen, M., Zhang, S., Nielsen, E. H., Christiansen, G., Dong, M., Skrydstrup, T. & Otzen, D. E. (2015). Scaffolded multimers of hIAPP20-29 peptide fragments fibrillate faster and lead to different fibrils compared to the free hIAPP20-29 peptide fragment. B B A - Proteins and Proteomics, 1854(12), 1890-1897. https://doi.org/10.1016/j.bbapap.2015.08.005

Mohammad-Beigi, H., Shojaosadati, S. A., Marvian, A. T., Pedersen, J. N., Klausen, L. H., Christiansen, G., Pedersen, J. S., Dong, M., Morshedi, D. & Otzen, D. E. (2015). Strong interactions with polyethylenimine-coated human serum albumin nanoparticles (PEI-HSA NPs) alter α-synuclein conformation and aggregation kinetics. Nanoscale, 7, 19627-19640. https://doi.org/10.1039/c5nr05663b

Tian, P., Boomsma, W., Wang, Y., Otzen, D., Jensen, M. H. & Lindorff-Larsen, K. (2015). Structure of a Functional Amyloid Protein Subunit Computed Using Sequence Variation. Journal of the American Chemical Society, 137(1), 22-25. https://doi.org/10.1021/ja5093634

Estrela, N., Franquelim, H. G., Lopes, C., Tavares, E., Macedo, J. A., Christiansen, G., Otzen, D. E. & Melo, E. P. (2015). Sucrose prevents protein fibrillation through compaction of the tertiary structure but hardly affects the secondary structure. Proteins: Structure, Function, and Bioinformatics, 83(11), 2039-2051. https://doi.org/10.1002/prot.24921

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

Michaels, T. C. T., Yde, P., Willis, J. C. W., Jensen, M. H., Otzen, D., Dobson, C. M., Buell, A. K. & Knowles, T. P. J. (2015). The length distribution of frangible biofilaments. Journal of Chemical Physics, 143(16), 1-15. Article 164901. https://doi.org/10.1063/1.4933230

Frahm, H., Hansen, S. K., Vad, B. S., Nielsen, E. H., Nielsen, J. T., Vosegaard, T., Skrydstrup, T. & Otzen, D. E. (2015). The natural, peptaibolic peptide SPF-5506-A4 adopts a β-bend spiral structure, shows low hemolytic activity and targets membranes through formation of large pores. B B A - Proteins and Proteomics, 1854(8), 882-889. https://doi.org/10.1016/j.bbapap.2015.03.003

Dueholm, M. S., Larsen, P., Finster, K., Stenvang, M. R., Christiansen, G., Vad, B. S., Bøggild, A., Otzen, D. E. & Halkjær Nielsen, P. (2015). The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids. Journal of Biological Chemistry, 290, 20590-26600. https://doi.org/10.1074/jbc.M115.654780

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

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

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

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

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. & 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

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

Neumann, J., Klein, N., Otzen, D. & Schneider, D. (2014). Folding energetics and oligomerization of polytopic α-helical transmembrane proteins. Archives of Biochemistry and Biophysics, 564, 281–296. https://doi.org/10.1016/j.abb.2014.07.017

Andersen, K. K. & Otzen, D. (2014). Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid. FEBS Letters, 588(10), 1955-1960. https://doi.org/10.1016/j.febslet.2014.04.004

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

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

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

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

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

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

Ghodke, S. D., Jensen, G. V., Svane, A. S. P., Weise, K., Søndergaard, A., Behrens, M. A., Pedersen, J. S., Nielsen, N. C., Pedersen, J. S., Winter, R. & Otzen, D. (2014). Polymorphism, metastable species and interconversion: the many states of glucagon fibrils. In V. Uversky & Y. Lyubchenko (Eds.), Bio-nanoimaging: Protein misfolding and aggregation (pp. 373-386). Elsevier. https://doi.org/10.1016/B978-0-12-394431-3.00034-1

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

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

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