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Sahin, C., Kjær, L., Christensen, M. S., Nedergaard Pedersen, J., Christiansen, G., Pérez, A-M. W., Moller, I. M., Enghild, J., Pedersen, J. S., Larsen, K. & Otzen, D. E. (2018). α-synucleins from animal species show low fibrillation propensities and weak oligomer membrane disruption. Biochemistry, 57(34), 5145-5158. https://doi.org/10.1021/acs.biochem.8b00627

Alam, P., Bousset, L., Melki, R. & Otzen, D. E. (2019). α-synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicities. Journal of Neurochemistry, 150(5), 522-534. https://doi.org/10.1111/jnc.14808

Otzen, D., Sehgal, P. & Westh, P. (2009). α-lactalbumin is unfolded by all classes of detergents but with different mechanisms. Journal of Colloid and Interface Science, 329, 273-283.

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, [74]. https://doi.org/10.1186/s12974-016-0532-8

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

Wang, H., Andersen, K. K., Sehgal, P., Hagedorn, J., Westh, P., Borch, K. & Otzen, D. E. (2013). pH regulation of the kinetic stability of the lipase from Thermomyces lanuginosus. Biochemistry, 52(1), 264-276. https://doi.org/10.1021/bi301258e

Song, Y. J. C., Lundvig, D. M. S., Huang, Y., Wei, P. G., Blumbergs, P. C., Højrup, P., Otzen, D., Halliday, G. M. & Jensen, P. H. (2007). p25α relocalizes in oligodendroglia from myelin to cytoplasmic inclusions in multiple system atrophy. American Journal of Pathology, 171(4), 1291-1303. https://doi.org/10.2353/ajpath.2007.070201

Song, Y. J. C., Lundvig, D. M. S., Huang, Y., Gai, W. P., Blumbergs, P. C., Højrup, P., Otzen, D., Halliday, G. M. & Jensen, P. H. (2007). p25a Relocalizes in Oligodendroglia from Myelin to Cytoplasmic Inclusions in Multiple System Atrophy. Am. J. Path., (171), 1291-1303.

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

Nielsen, S. B., Macchi, F., Raccosta, S., Langkilde, A. E., Giehm, L., Kyrsting, A., Svane, A. S. P., Manno, M., Christiansen, G., Nielsen, N. C., Oddershede, L., Vestergaard, B. & Otzen, D. (2013). Wildtype and A30P Mutant Alpha-Synuclein Form Different Fibril Structures. P L o S One, 8(7), [e67713]. https://doi.org/10.1371/journal.pone.0067713

Jensen, P. L., Dueholm, M. S., Larsen, P., Petersen, S. V., Enghild, J. J., Christiansen, G., Højrup, P., Nielsen, P. H. & Otzen, D. (2009). Widespread abundance of Functional Bacterial Amyloid in Mycolata and other Gram positive Bacteria. Applied and Environmental Microbiology, 75, 4101-4110.

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

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

Otzen, D. & Nielsen, P. H. (2007). We find them here, we find them there: Functional bacterial amyloid. Cell. Mol. Life Sci.

Otzen, D. & Nielsen, P. H. (2008). We find them here, we find them there: Functional bacterial amyloid. Cellular and Molecular Life Sciences, 65, 910-927.

Wang, H., Hagedorn, J., Svendsen, A., Borch, K. & Otzen, D. (2013). Variant of the Thermomyces lanuginosus lipase with improved kinetic stability: a candidate for enzyme replacement therapy. Biophysical Chemistry, 172, 43-52. https://doi.org/10.1016/j.bpc.2012.12.003

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

Sehgal, P., Mogensen, J. E. & Otzen, D. (2005). Using micellar mole fractions to assess membrane protein stability in mixed micelles. B B A - Biomembranes, 1761, 59-68. https://doi.org/10.1016/j.bbamem.2005.08.006

Frislev, H. S., Nielsen, J., Nylandsted, J. & Otzen, D. (2018). Using Liprotides to Deliver Cholesterol to the Plasma Membrane. Journal of Membrane Biology, 25(4), 581-592. https://doi.org/10.1007/s00232-018-0034-y

Nielsen, J. T., Bjerring, M., Jeppesen, M., Pedersen, R. O., Pedersen, J. M., Hein, K. L., Vosegaard, T., Skrydstrup, T., Otzen, D. & Nielsen, N. C. (2009). Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy. Angewandte Chemie International Edition, 48, 2118-2121.

Nielsen, J. T., Bjerring, M., Jeppesen, M., Pedersen, R. O., Pedersen, J. M., Hein, K. L., Vosegaard, T., Skrydstrup, T., Otzen, D. & Nielsen, N. C. (2009). Unique Identification of Supramolecular Structures in Amyloid Fibrils by Solid-State NMR. Poster session presented at 50th Experimental NMR Conference (ENC), Asilomar, CA, United States.

Nielsen, M. M., Andersen, K. K., Westh, P. & Otzen, D. (2007). Unfolding of ß-sheet proteins in SDS. Biophysical Journal, (92), 3674-3685.

Rasmussen, H. Ø., Enghild, J. J., Otzen, D. E. & Pedersen, J. S. (2020). Unfolding and partial refolding of a cellulase from the SDS-denatured state: From β-sheet to α-helix and back. B B A - General Subjects, 1864(1), 129434 1-12. [129434]. https://doi.org/10.1016/j.bbagen.2019.129434

Meisl, G., Xu, C. K., Taylor, J. D., Michaels, T. C. T., Levin, A., Otzen, D., Klenerman, D., Matthews, S., Linse, S., Andreasen, M. & Knowles, T. P. J. (2022). Uncovering the universality of self-replication in protein aggregation and its link to disease. Science Advances, 8(32), [eabn6831]. https://doi.org/10.1126/sciadv.abn6831

Mortensen, H. G., Otzen, D. E. & Pedersen, J. S. (2021). Ubiquitin forms conventional decorated micelle structures with sodium dodecyl sulfate at saturation. Journal of Colloid and Interface Science, 596, 233-244. https://doi.org/10.1016/j.jcis.2021.03.110

van Diggelen, F., Hrle, D., Apetri, M., Christiansen, G., Rammes, G., Tepper, A. & Otzen, D. E. (2019). Two conformationally distinct α-synuclein oligomers share common epitopes and the ability to impair long-term potentiation. PLOS ONE, 14(3), [0213663]. https://doi.org/10.1371/journal.pone.0213663

Melo, E. P., Chen, L. Y., Cabral, J. M. S., Fojan, P., Petersen, S. B. & Otzen, D. E. (2003). Trehalose favors a cutinase compact intermediate off-folding pathway. Biochemistry, 42(24), 7611-7617. https://doi.org/10.1021/bi034267x

Otzen, D. E. & Oliveberg, M. (2004). Transient formation of nano-crystalline structures during fibrillation of an Aβ-like peptide. Protein Science, 13(5), 1417-1421. https://doi.org/10.1110/ps.03538904

Otzen, D. E., Miron, S., Akke, M. & Oliveberg, M. (2004). Transient aggregation and stable dimerization induced by introducing an Alzheimer sequence into a water-soluble protein. Biochemistry, 43(41), 12964-12978. https://doi.org/10.1021/bi048509k

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 of the United States of America, 113(8), 2098-2103. https://doi.org/10.1073/pnas.1524027113

Sehgal, P. & Otzen, D. (2006). Thermodynamics of unfolding of an integral membrane protein in mixed micelles. Protein Science, 15, 890-899. https://doi.org/10.1110/ps.052031306

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.

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, [27672]. https://doi.org/10.1038/srep27672

Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995). The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding. Journal of Molecular Biology, 254(2), 260-288. https://doi.org/10.1006/jmbi.1995.0616

Marvian, A. T., Aliakbari, F., Mohammad-Beigi, H., Ahmadi, Z. A., Mehrpouyan, S., Lermyte, F., Nasouti, M., Collingwood, J. F., Otzen, D. E. & Morshedi, D. (2020). The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization. International Journal of Biological Macromolecules, 155, 543-550. https://doi.org/10.1016/j.ijbiomac.2020.03.238

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

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

Jeppesen, M. D., Westh, P. & Otzen, D. E. (2010). The role of protonation in protein fibrillation. FEBS Letters, 584(4), 780-4. https://doi.org/10.1016/j.febslet.2010.01.002

Debnath, D. K., Basaiawmoit, R. V., Nielsen, K. L. & Otzen, D. E. (2011). The role of membrane properties in Mistic folding and dimerisation. Protein Engineering Design and Selection (Print), 24(1-2), 89-97. https://doi.org/10.1093/protein/gzq095

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.

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

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

Dyla, M., González Foutel, N. S., Otzen, D. E. & Kjaergaard, M. (2022). The optimal docking strength for reversibly tethered kinases. Proceedings of the National Academy of Sciences of the United States of America, 119(25), [e2203098119]. https://doi.org/10.1073/pnas.2203098119

Helwig, M., Hoshino, A., Berridge, C., Lee, S-N., Lorenzen, N., Otzen, D., Eriksen, J. & Lindberg, I. (2013). The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins. Journal of Biological Chemistry, 288(2), 1114.

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 of the United States of America, 113(32). https://doi.org/10.1073/pnas.1601091113

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

Mogensen, J. E., Wimmer, R., Larsen, J. N., Spangfort, M. D. & Otzen, D. E. (2002). The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands. Journal of Biological Chemistry, 277(26), 23684-23692. https://doi.org/10.1074/jbc.M202065200

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. [164901]. https://doi.org/10.1063/1.4933230

van Diggelen, F., Frank, S. A., Somavarapu, A. K., Scavenius, C., Apetri, M. M., Nielsen, J., Tepper, A. W. J. W., Enghild, J. J. & Otzen, D. E. (2020). The interactome of stabilized α-synuclein oligomers and neuronal proteins. The FEBS Journal, 287(10), 2037-2054. https://doi.org/10.1111/febs.15124

Nielsen, S. B., Wilhelm, K., Vad, B., Schleucher, J., Morozova-Roche, L. A. & Otzen, D. (2010). The interaction of equine lysozyme:oleic acid complexes with lipid membranes suggests a cargo off-loading mechanism. Journal of Molecular Biology, 398(2), 351-61. https://doi.org/10.1016/j.jmb.2010.03.012

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