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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

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

Andersen, K. K., Vad, B. S., Scavenius, C., Enghild, J. J. & Otzen, D. E. (2017). Human lysozyme peptidase resistance is perturbed by the anionic glycolipid biosurfactant rhamnolipid produced by the opportunistic pathogen Pseudomonas aeruginosa. Biochemistry, 56(1), 260–270. https://doi.org/10.1021/acs.biochem.6b01009

Frislev, H. S., Boye, T. L., Nylandsted, J. & Otzen, D. (2017). Liprotides kill cancer cells by disrupting the plasma membrane. Scientific Reports, 7(1), Article 15129. https://doi.org/10.1038/s41598-017-15003-6

Mortensen, H. G., Madsen, J. K., Andersen, K. K., Vosegaard, T., Deen, G. R., Otzen, D. E. & Pedersen, J. S. (2017). Myoglobin and α-Lactalbumin Form Smaller Complexes with the Biosurfactant Rhamnolipid Than with SDS. Biophysical Journal, 113(12), 2621-2633. https://doi.org/10.1016/j.bpj.2017.10.024

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

Otzen, D. E., Vad, B. S., Dueholm, M. S., Nielsen, P. H., Rouse, S. L. & Matthews, S. J. (2017). Self-organizing amyloid in bacteria. European Biophysics Journal, 46, S98-S98.

Otzen, D. E., Vad, B. S., Dueholm, M. S., Nielsen, P. H., Rouse, S. L. & Matthews, S. J. (2017). Self-organizing amyloid in bacteria. European Biophysics Journal, 46(supp 1), S341-S341. https://doi.org/10.1007/s00249-017-1222-x

Sørensen, H. V., Pedersen, J. N., Pedersen, J. S. & Otzen, D. E. (2017). Tailoring thermal treatment to form liprotide complexes between oleic acid and different proteins. BBA Proteins and Proteomics, 1865(6), 682–693. https://doi.org/10.1016/j.bbapap.2017.03.011

Malmos, K. G., Stenvang, M., Sahin, C., Christiansen, G. & Otzen, D. E. (2017). The Changing Face of Aging: Highly Sulfated Glycosaminoglycans Induce Amyloid Formation in a Lattice Corneal Dystrophy Model Protein. Journal of Molecular Biology, 429(18), 2755-2764. https://doi.org/10.1016/j.jmb.2017.07.014

Christiansen, S. H., Zhang, X., Juul-Madsen, K., Hvam, M. L., Vad, B. S., Behrens, M. A., Thygesen, I. L., Jalilian, B., Pedersen, J. S., Howard, K., Otzen, D. E. & Vorup-Jensen, T. (2017). The random co-polymer glatiramer acetate rapidly kills primary human leukocytes through sialic-acid-dependent cell membrane damage. B B A - Biomembranes, 1859(3), 425-437. https://doi.org/10.1016/j.bbamem.2017.01.001

Malmos, K., Blancas-Mejia, L. M., Weber, B., Buchner, J., Ramirez-Alvarado, M., Naiki, H. & Otzen, D. (2017). ThT 101: a primer on the use of thioflavin T to investigate amyloid formation. Amyloid: the Journal of Protein Folding Disorders, 24(1), 1-16. https://doi.org/10.1080/13506129.2017.1304905

van Diggelen, F., Tepper, A., Petri, M. & Otzen, D. (2017). α-Synuclein Oligomers: A Study in Diversity. Israel Journal of Chemistry, 57(7-8), 699-723. https://doi.org/10.1002/ijch.201600116

Christensen, L. F. B., Malmos, K. G., Christiansen, G. & Otzen, D. E. (2016). A Complex Dance: The Importance of Glycosaminoglycans and Zinc in the Aggregation of Human Prolactin. Biochemistry, 55(26), 3674–3684. https://doi.org/10.1021/acs.biochem.6b00153

Pantusa, M., Vad, B., Lillelund, O., Kjær, L., Otzen, D. & Bartucci, R. (2016). Alpha-synuclein and familial variants affect the chain order and the thermotropic phase behavior of anionic lipid vesicles. B B A - Proteins and Proteomics, 1864(9), 1206-1214. https://doi.org/10.1016/j.bbapap.2016.05.003

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

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

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

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

Stenvang, M., Christiansen, G. & Otzen, D. E. (2016). Epigallocatechin gallate remodels fibrils of Lattice Corneal Dystrophy protein, facilitating proteolytic degradation and preventing formation of membrane-permeabilizing species. Biochemistry, 55(16), 2344-2357. https://doi.org/10.1021/acs.biochem.6b00063

Stenvang, M., Dueholm, M. S., Vad, B. S., Seviour, T. W., Zeng, G., Geifman-Shochat, S., Søndergaard, M. T., Christiansen, G., Meyer, R. L., Kjelleberg, S., Otzen, D. E. & Nielsen, P. H. (2016). Epigallocatechin Gallate Remodels overexpressed Functional Amyloids in Pseudomonas aeruginosa and Increases Biofilm Susceptibility to Antibiotic Treatment. Journal of Biological Chemistry, 291(51), 26540-26553. https://doi.org/10.1074/jbc.M116.739953

Paslawski, W., Lorenzen, N. & Otzen, D. E. (2016). Formation and Characterization of α-Synuclein Oligomers. Methods in molecular biology (Clifton, N.J.), 1345, 133-150. https://doi.org/10.1007/978-1-4939-2978-8_9

Mohammad-Beigi, H., Morshedi, D., Shojaosadati, S. A., Pedersen, J. N., Marvian, A. T., Aliakbari, F., Christiansen, G., Pedersen, J. S. & Otzen, D. E. (2016). Gallic acid loaded onto polyethylenimine-coated human serum albumin nanoparticles (PEI-HSA-GA NPs) stabilizes α-synuclein in the unfolded conformation and inhibits aggregation. RSC Advances, 6(88), 85312-85323. https://doi.org/10.1039/c6ra08502d

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. (2016). How Glycosaminoglycans Promote Fibrillation of Salmon Calcitonin. Journal of Biological Chemistry, 291(32), 16849-16862. https://doi.org/10.1074/jbc.M116.715466

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

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 (PNAS), 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 (PNAS), 113(8), 2098-2103. 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. 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 (PNAS), 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. 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

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