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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

Christensen, L. F. B., Otzen, D. & Dueholm, M. S. (2018). High-quality draft genome sequence of Sphaerisporangium cinnabarinum ATCC 31213. Genome Announcements, 6(21), [e00456-18]. https://doi.org/10.1128/genomeA.00456-18

Christensen, L. F. B., Hansen, L. M., Finster, K., Christiansen, G., Nielsen, P. H., Otzen, D. E. & Dueholm, M. S. (2018). The Sheaths of Methanospirillum Are Made of a New Type of Amyloid Protein. Frontiers in Microbiology, 9, [2729]. https://doi.org/10.3389/fmicb.2018.02729, https://doi.org/10.3389/fmicb.2018.02729

Christensen, L. F. B., Jensen, K. F., Nielsen, J., Vad, B. S., Christiansen, G. & Otzen, D. E. (2019). Reducing the Amyloidogenicity of Functional Amyloid Protein FapC Increases Its Ability To Inhibit α-Synuclein Fibrillation. ACS Omega, 4(2), 4029-4039. https://doi.org/10.1021/acsomega.8b03590

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.), Biological and Bio-inspired Nanomaterials (pp. 113-159). Springer. Advances in Experimental Medicine and Biology Vol. 1174 https://doi.org/10.1007/978-981-13-9791-2_4

Christensen, L. F. B., Nowak, J. S., Sønderby, T. V., Frank, S. A. & Otzen, D. E. (2020). Quantitating denaturation by formic acid: Imperfect repeats are essential to the stability of the functional amyloid protein FapC. The Journal of biological chemistry, 295(37), 13031–13046. https://doi.org/10.1074/jbc.RA120.013396

Christensen, L. F. B., Alijanvand, S. H., Burdukiewicz, M., Herbst, F-A., Kjeldal, H., Dueholm, M. S. & Otzen, D. E. (2021). Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats. Protein Science, 30(9), 1854-1870. https://doi.org/10.1002/pro.4137

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), [103808]. https://doi.org/10.1016/j.isci.2022.103808

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, [100060]. https://doi.org/10.1016/j.bioflm.2021.100060

Chen, L., Cabrita, G. J. M., Otzen, D. & Melo, E. P. (2005). Stabilization of the Ribosomal Protein S6 by Trehalose is Counterbalanced by the Formation of a Putative Off-pathway Species. Journal of Molecular Biology, 351, 402-416. https://doi.org/10.1016/j.jmb.2005.05.056

Cavallin, A., Arozenius, H., Kristensson, K., Antonsson, P., Otzen, D. E., Björk, P. & Forsberg, G. (2000). The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function. Journal of Biological Chemistry, 275(3), 1665-1672. https://doi.org/10.1074/jbc.275.3.1665

Calcutta, A., Jessen, C. M., Behrens, M. A., Oliveira, C. L. P., Renart, M. L., González-Ros, J. M., Otzen, D., Pedersen, J. S., Malmendal, A. & Nielsen, N. C. (2012). Mapping of unfolding states of integral helical membrane proteins by GPS-NMR and scattering techniques: TFE-induced unfolding of KcsA in DDM surfactant. B B A - Biomembranes, 1818(9), 2290-301. https://doi.org/10.1016/j.bbamem.2012.04.005

Cabré, E., Malmström, J., Sutherland, D., Perez-Gil, J. & Otzen, D. (2009). Surfactant protein SP-B strongly modifies surface collapse of phospholipid vesicles: Insights from a quartz crystal microbalance with dissipation. Biophysical Journal, 97(3), 768-76. https://doi.org/10.1016/j.bpj.2009.04.057

Brinkmann, C. R., Thiel, S. & Otzen, D. (2013). Protein:fatty acid complexes: Biochemistry, biophysics and function. F E B S Journal, 280(8), 1733–1749. https://doi.org/10.1111/febs.12204

Bleem, A., Christiansen, G., Madsen, D. J., Maric, H., Strømgaard, K., Bryers, J. D., Daggett, V., Meyer, R. L. & Otzen, D. E. (2018). Protein Engineering Reveals Mechanisms of Functional Amyloid Formation in Pseudomonas aeruginosa Biofilms. Journal of Molecular Biology, 430(20), 3751-3763. https://doi.org/10.1016/j.jmb.2018.06.043

Bisiak, F., Chrenková, A., Zhang, S. D., Pedersen, J. N., Otzen, D. E., Zhang, Y. E. & Brodersen, D. E. (2022). Structural variations between small alarmone hydrolase dimers support different modes of regulation of the stringent response. Journal of Biological Chemistry, 298(7), [102142]. https://doi.org/10.1016/j.jbc.2022.102142

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

Bertelsen, K., Vad, B., Nielsen, E. H. T., Hansen, S. K., Skrydstrup, T., Otzen, D., Vosegaard, T. & Nielsen, N. C. (2011). Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR: altered structural information in studies of antimicrobial peptides. Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 115(8), 1767-1774. https://doi.org/10.1021/jp110866g

Basaiawmoit, R. V., Oliveira, C. L. P. D., Runager, K., Kristensen, T., Enghild, J. J., Pedersen, J. S. & Otzen, D. (2009). First Low Resolution Structural Evidence of Full-length TGFBIp and Its Implications in TGFBI-linked Corneal Dystrophy. Abstract from ARVO 2009 Annual Meeting, nr. 2009, Fort Lauderdale, USA, 3. maj - 7. maj 2009, Investigative Ophthalmology & Visual Science. 2009. E-Abstract 4311. Association for Research in Vision and Ophthalmology..

Basaiawmoit, R. V., Deva, T., Runager, K., Kristensen, T., Enghild, J. J. & Otzen, D. (2009). The Underlying Mechanisms of TGFBIp-mediated Corneal Dystrophies. Abstract from Asia ARVO, International Meeting on Research in Vision and Ophthalmology, Hyderabad International Convention Center. Abstract number: PAP05.01, Hyderabad, India.

Basaiawmoit, R. V., Oliveira, C. L. P., Runager, K., Sørensen, C. S., Behrens, M. A., Jonsson, B-H., Kristensen, T., Klintworth, G. K., Enghild, J. J., Pedersen, J. S. & Otzen, D. E. (2011). SAXS models of TGFBIp reveal a trimeric structure and show that the overall shape is not affected by the Arg124His mutation. Journal of Molecular Biology, 408(3), 503-513. https://doi.org/10.1016/j.jmb.2011.02.052

Barciszewski, J., Rattan, S., Otzen, D. & Clark, B. F. C. (1992). Specific incorportation of kinetin into eukaryotic and prokaryotic transfer ribonucleic acid molecules. Biochemistry international, 28, 805-811.

Barciszewski, J., Rattan, S., Siboska, G., Otzen, D. & Clark, B. F. C. (1993). Reduction in the amount of 8-hydroxy-2´-deoxyguanosine in the DNA of SV40-transformed human fibroblasts as compared with normal cells in culture. F E B S Letters, 318, 186-188.

Barciszewski, J., Otzen, D., Rattan, S. I. S. & Clark, B. F. C. (1992). Specific incorporation of kinetin into eukaryotic and prokaryotic transfer ribonucleic acid molecules. Biochemistry international, 28(5), 805-811.

Baptista, R. P., Pedersen, S. H., Cabrita, G. J. M., Otzen, D., Cabral, J. M. & Melo, E. P. (2008). Thermodynamics and mechanism of cutinase stabilization by trehalose. Biopolymers, 89, 538-547.

Baldry, M., Bojer, M. S., Najarzadeh, Z., Vestergaard, M., Meyer, R. L., Otzen, D. E. & Ingmer, H. (2020). Phenol-Soluble Modulins Modulate Persister Cell Formation in Staphylococcus aureus. Frontiers in Microbiology, 11, [573253]. https://doi.org/10.3389/fmicb.2020.573253

Balakrishnan, V. S., Vad, B. S. & Otzen, D. (2013). Novicidin's membrane permeabilizing activity is driven by membrane partitioning but not by helicity: A biophysical study of the impact of lipid charge and cholesterol. BBA General Subjects, 1834(6), 996-1002. https://doi.org/10.1016/j.bbapap.2013.03.025

Andreasen, M., Nielsen, S. B., Mittag, T., Bjerring, M., Nielsen, J. T., Zhang, S., Nielsen, E. H., Jeppesen, M., Christiansen, G., Besenbacher, F., Dong, M., Nielsen, N. C., Skrydstrup, T. & Otzen, D. E. (2012). Modulation of fibrillation of hIAPP core fragments by chemical modification of the peptide backbone. B B A - Proteins and Proteomics, 1824(2), 274-85. https://doi.org/10.1016/j.bbapap.2011.10.014

Andreasen, M., Nielsen, S. B., Runager, K., Christiansen, G., Nielsen, N. C., Enghild, J. J. & Otzen, D. (2012). Polymorphic Fibrillation of the Destabilized Fourth Fasciclin-1 Domain Mutant A₅₄6T of the Transforming Growth Factor-β-induced Protein (TGFBIp) Occurs through Multiple Pathways with Different Oligomeric Intermediates. Journal of Biological Chemistry, 287(41), 34730-34742. https://doi.org/10.1074/jbc.M112.379552

Andreasen, M., Skeby, K. K., Zhang, S., Nielsen, E. H., Klausen, L. H., Frahm, H., Christiansen, G., Skrydstrup, T., Dong, M., Schiøtt, B. & Otzen, D. (2014). The Importance of Being Capped: Terminal Capping of an Amyloidogenic Peptide Affects Fibrillation Propensity and Fibril Morphology. Biochemistry, 53(44), 6968-6980. https://doi.org/10.1021/bi500674u

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

Andreasen, M., Meisl, G., Taylor, J. D., Michaels, T. C. T., Levin, A., Otzen, D. E., Chapman, M. R., Dobson, C. M., Matthews, S. J. & Knowles, T. P. J. (2019). Physical Determinants of Amyloid Assembly in Biofilm Formation. mBio, 10(1), [e02279-18]. https://doi.org/10.1128/mBio.02279-18

Andersen, K. K., Westh, P. & Otzen, D. (2008). A global study of myoglobin-surfactant interactions. Langmuir, 15, 399-407.

Andersen, K. & Otzen, D. (2009). How chain length and charge affect surfactant denaturation of ACBP. Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 113, 13942-13952.

Andersen, K., Oliveira, C. L. P. D., Larsen, K. L., Poulsen, F., Callisen, T., Westh, P., Pedersen, J. S. & Otzen, D. (2009). The role of decorated SDS micelles in sub-cmc protein denaturation and association. Journal of Molecular Biology, 391, 207-226.

Andersen, C. B., Hicks, M. R., Vetri, V., Vandahl, B., Rahbek-Nielsen, H., Thøgersen, H., Thøgersen, I., Enghild, J. J., Serpell, L. C., Rischel, C. & Otzen, D. E. (2010). Glucagon fibril polymorphism reflects differences in protofilament backbone structure. Journal of Molecular Biology, 397(4), 932-46. https://doi.org/10.1016/j.jmb.2010.02.012

Andersen, K. K., Wang, H. & Otzen, D. (2012). A Kinetic Analysis of the Folding and Unfolding of OmpA in Urea and Guaninidinium Chloride: Single and Parallel Pathways. Biochemistry, 51(42), 8371-8383. https://doi.org/10.1021/bi300974y

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

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

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, [1711]. https://doi.org/10.3389/fmicb.2016.01711

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

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

Andersen, K. K., Vad, B. S., Kjaer, L., Tolker-Nielsen, T., Christiansen, G. & Otzen, D. E. (2018). Pseudomonas aeruginosa rhamnolipid induces fibrillation of human α-synuclein and modulates its effect on biofilm formation. FEBS Letters, 592(9), 1484-1496. https://doi.org/10.1002/1873-3468.13038

Andersen, C. B., Yoshimura, Y., Nielsen, J., Otzen, D. E. & Mulder, F. A. A. (2021). How epigallocatechin gallate binds and assembles oligomeric forms of human alpha-synuclein. The Journal of Biological Chemistry, 296, [100788]. https://doi.org/10.1016/j.jbc.2021.100788

Andersen, C., Grønnemose, A. L., Pedersen, J. N., Nowak, J. S., Christiansen, G., Nielsen, J., Mulder, F. A. A., Otzen, D. E. & Jørgensen, T. J. D. (2021). Lipid Peroxidation Products HNE and ONE Promote and Stabilize Alpha-Synuclein Oligomers by Chemical Modifications. Biochemistry, 60(47), 3644-3658. https://doi.org/10.1021/acs.biochem.1c00478

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), [8744]. https://doi.org/10.1038/s41598-021-88157-z

Alijanvand, S. H., Christensen, M. H., Christiansen, G., Harikandei, K. B., Salehi, P., Schiøtt, B., Moosavi-Movahedi, A. A. & Otzen, D. E. (2020). Novel noscapine derivatives stabilize the native state of insulin against fibrillation. International Journal of Biological Macromolecules, 147, 98-108. https://doi.org/10.1016/j.ijbiomac.2020.01.061

Alijanvand, S. H., Ladefoged, L. K., Zubrienė, A., Sakalauskas, A., Christiansen, G., Dudutiene, V., Schiøtt, B., Matulis, D., Smirnovas, V. & Otzen, D. E. (2023). Inhibitory effects of fluorinated benzenesulfonamides on insulin fibrillation. International Journal of Biological Macromolecules, 227, 590-600. https://doi.org/10.1016/j.ijbiomac.2022.12.105

Aliakbari, F., Shabani, A. A., Bardania, H., Mohammad-Beigi, H., Tayaranian Marvian, A., Dehghani Esmatabad, F., Vafaei, A. A., Shojaosadati, S. A., Saboury, A. A., Christiansen, G., Otzen, D. E. & Morshedi, D. (2018). Formulation and anti-neurotoxic activity of baicalein-incorporating neutral nanoliposome. Colloids and surfaces. B, Biointerfaces, 161, 578-587. https://doi.org/10.1016/j.colsurfb.2017.11.023

Aliakbari, F., Mohammad-Beigi, H., Rezaei-Ghaleh, N., Becker, S., Dehghani Esmatabad, F., Eslampanah Seyedi, H. A., Bardania, H., Tayaranian Marvian, A., Collingwood, J. F., Christiansen, G., Zweckstetter, M., Otzen, D. E. & Morshedi, D. (2018). The potential of zwitterionic nanoliposomes against neurotoxic alpha-synuclein aggregates in Parkinson's Disease. Nanoscale, 10(19), 9174-9185. https://doi.org/10.1039/c8nr00632f

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Lise Refstrup Linnebjerg Pedersen