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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

Sehgal, P., Sharma, M., Wimmer, R., Larsen, K. L. & Otzen, D. (2006). Interactions between anionic mixed micelles and α-cyclodextrin and their inclusion complexes: conductivity, NMR and fluorescence study. Colloid and Polymer Science, 284(8), 916-926. https://doi.org/10.1007/s00396-006-1466-y

Sehgal, P., Doe, H., Sharma, M. & Otzen, D. E. (2005). Synergistic behavior of sodiumdodecylsulfate and 1,2-diheptanoyl-sn- glycero-3-phosphocholine in an aqueous medium: Interfacial and bulk behavior. Colloid and Polymer Science, 283(11), 1219-1225. https://doi.org/10.1007/s00396-005-1315-4

Sehgal, P., Doe, H., Sharma, M. & Otzen, D. E. (2004). Interaction between phospholipid vesicular structures with long chain zwitterionic surfactants. Colloid and Polymer Science, 282(7), 677-683. https://doi.org/10.1007/s00396-003-0992-0

Schmüser, L., Trefz, M., Roeters, S. J., Beckner, W., Pfaendtner, J., Otzen, D., Woutersen, S., Bonn, M., Schneider, D. & Weidner, T. (2021). Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy. Langmuir : the ACS journal of surfaces and colloids, 37(45), 13452-13459. https://doi.org/10.1021/acs.langmuir.1c02206

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. https://doi.org/10.1073/pnas.1524027113

Scavenius, C., Ghodke, S., Otzen, D. E. & Enghild, J. J. (2011). Hydrogen exchange mass spectrometry as an analytical tool for the analysis of amyloid fibrillogenesis. International Journal of Mass Spectrometry, 302(1-3), 167-173. https://doi.org/10.1016/j.ijms.2010.10.001

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

Sawada, M., Yamaguchi, K., Hirano, M., Noji, M., So, M., Otzen, D. E., Kawata, Y. & Goto, Y. (2020). Amyloid formation of α-synuclein based on the solubility- and supersaturation-dependent mechanism. Langmuir, 36(17), 4671-4681. https://doi.org/10.1021/acs.langmuir.0c00426

Sahin, C., Lorenzen, N., Lemminger, L., Christiansen, G., Møller, I. M., Vesterager, L. B., Pedersen, L. Ø., Fog, K., Kallunki, P. & Otzen, D. E. (2017). Antibodies against the C-terminus of α-synuclein modulate its fibrillation. Biophysical Chemistry, 220, 34-41. https://doi.org/10.1016/j.bpc.2016.11.002

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

Sahin, C., Østerlund, E. C., Österlund, N., Costeira-Paulo, J., Pedersen, J. N., Christiansen, G., Nielsen, J., Grønnemose, A. L., Amstrup, S. K., Tiwari, M. K., Rao, R. S. P., Bjerrum, M. J., Ilag, L. L., Davies, M. J., Marklund, E. G., Pedersen, J. S., Landreh, M., Møller, I. M., Jørgensen, T. J. D. & Otzen, D. E. (2022). Structural Basis for Dityrosine-Mediated Inhibition of α-Synuclein Fibrillization. Journal of the American Chemical Society, 144(27), 11949-11954. https://doi.org/10.1021/jacs.2c03607

Runager, K., Underhaug, J., Basaiawmoit, R. V., Valnickova, Z., Kristensen, T., Otzen, D., Klintworth, G. K., Nielsen, N. C. & Enghild, J. J. (2009). Naturally Occurring Mutations Alter the Structure and Stability of the Fourth Fasciclin Domain of the Transforming Growth Factor Beta Induced Protein (TGFBIp). Investigative Ophthalmology & Visual Science, (E-Abstract 1016).

Runager, K., Basaiawmoit, R. V., Deva, T., Andreasen, M., Valnickova, Z., Sørensen, C. S., Karring, H., Thøgersen, I. B., Christiansen, G., Underhaug, J., Kristensen, T., Nielsen, N. C., Klintworth, G. K., Otzen, D. E. & Enghild, J. J. (2011). Human Phenotypically Distinct TGFBI Corneal Dystrophies Are Linked to the Stability of the Fourth FAS1 Domain of TGFBIp. Journal of Biological Chemistry, 286(7), 4951-8. https://doi.org/10.1074/jbc.M110.181099

Ruiz-Sanz, J., de Prat Gay, G., Otzen, D. E. & Fersht, A. R. (1995). Protein Fragments as Models for Events in Protein Folding Pathways: Protein Engineering Analysis of the Association of Two Complementary Fragments of the Barley Chymotrypsin Inhibitor 2 (CI-2). Biochemistry, 34(5), 1695-1701. https://doi.org/10.1021/bi00005a026

Rouse, S. L., Hawthorne, W. J., Berry, J-L., Chorev, D. S., Ionescu, S. A., Lambert, S., Stylianou, F., Ewert, W., Mackie, U., Morgan, R. M. L., Otzen, D., Herbst, F-A., Nielsen, P. H., Dueholm, M., Bayley, H., Robinson, C. V., Hare, S. & Matthews, S. (2017). A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis. Nature Communications, 8(1), [263]. https://doi.org/10.1038/s41467-017-00361-6

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

Reinau, M. E. & Otzen, D. (2009). Stability and structure of the membrane protein transporter Ffh is modulated by substrates and lipids. Archives of Biochemistry and Biophysics, 492, 48-53.

Reinau, M. E., Thøgersen, I. B., Enghild, J. J., Nielsen, K. L. & Otzen, D. E. (2010). The diversity of FtsY-lipid interactions. Biopolymers, 93(7), 595-606. https://doi.org/10.1002/bip.21404

Reimer, L., Haikal, C., Gram, H., Theologidis, V., Kovacs, G., Ruesink, H., Baun, A., Nielsen, J., Otzen, D. E., Li, J-Y. & Jensen, P. H. (2022). Low dose DMSO treatment induces oligomerization and accelerates aggregation of α-synuclein. Scientific Reports, 12, [3737]. https://doi.org/10.1038/s41598-022-07706-2

Rasmussen, C. B., Christiansen, G., Vad, B. S., Lynggaard, C., Enghild, J. J., Andreasen, M. & Otzen, D. (2019). Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation. Protein Science, 28(3), 633-642. https://doi.org/10.1002/pro.3566

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

Rasmussen, H. Ø., Otzen, D. E. & Pedersen, J. S. (2021). A multimethod approach for analyzing FapC fibrillation and determining mass per length. Biophysical Journal, 120(11), 2262-2275. https://doi.org/10.1016/j.bpj.2021.03.031

Rasmussen, H. Ø., Otzen, D. E. & Pedersen, J. S. (2022). Induction, inhibition, and incorporation: Different roles for anionic and zwitterionic lysolipids in the fibrillation of the functional amyloid FapC. The Journal of Biological Chemistry, 298(2), [101569]. https://doi.org/10.1016/j.jbc.2022.101569

Rasmussen, H. Ø., Wollenberg, D. T. W., Wang, H., Andersen, K. K., Oliveira, C. L. P., Jørgensen, C. I., Jørgensen, T. J. D., Otzen, D. E. & Pedersen, J. S. (2022). The changing face of SDS denaturation: Complexes of Thermomyces lanuginosus lipase with SDS at pH 4.0, 6.0 and 8.0. Journal of Colloid and Interface Science, 614, 214-232. https://doi.org/10.1016/j.jcis.2021.12.188

Rasmussen, H. Ø., Kumar, A., Shin, B., Stylianou, F., Sewell, L., Xu, Y., Otzen, D. E., Pedersen, J. S. & Matthews, S. J. (2023). FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC. Journal of Molecular Biology, 435(2), [167878]. https://doi.org/10.1016/j.jmb.2022.167878

Rantalainen, K., Christensen, P. A., Hafrén, A., Otzen, D., Kalkkinen, N. & Mäkinen, K. (2009). Interaction of a potyviral VPg with anionic phospholipid vesicles. Virology, 395, 114-120.

Rahimi Aqdam, S., Otzen, D. E., Mahmoodi, N. M. & Morshedi, D. (2021). Adsorption of azo dyes by a novel bio-nanocomposite based on whey protein nanofibrils and nano-clay: Equilibrium isotherm and kinetic modeling. Journal of Colloid and Interface Science, 602, 490-503. https://doi.org/10.1016/j.jcis.2021.05.174

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

Poghosyan, A. H., Schafer, N., Lyngsø, J., Shahinyan, A. A., Pedersen, J. S. & Otzen, D. (2019). Molecular dynamics study of ACBP denaturation in alkyl sulfates demonstrates possible pathways of unfolding through fused surfactant clusters. Protein Engineering, Design and Selection, 32(4), 175-190. [gzz037]. https://doi.org/10.1093/protein/gzz037

Pirhaghi, M., Najarzadeh, Z., Moosavi-Movahedi, F., Shafizadeh, M., Mamashli, F., Atarod, D., Ghasemi, A., Morshedi, D., Meratan, A. A., Otzen, D. E. & Saboury, A. A. (2023). The anti-platelet drug ticlopidine inhibits FapC fibrillation and biofilm production: Highlighting its antibiotic activity. B B A - Proteins and Proteomics, 1871(2), 140883. [140883]. https://doi.org/10.1016/j.bbapap.2022.140883

Pirhaghi, M., Frank, S. A., Alam, P., Nielsen, J., Sereikaite, V., Gupta, A., Strømgaard, K., Andreasen, M., Sharma, D., Saboury, A. A. & Otzen, D. E. (2022). A penetratin-derived peptide reduces the membrane permeabilization and cell toxicity of α-synuclein oligomers. Journal of Biological Chemistry, 298(12), [102688]. https://doi.org/10.1016/j.jbc.2022.102688

Pigolotti, S., Lizana, L., Otzen, D. & Sneppen, K. (2013). Quality control system response to stochastic growth of amyloid fibrils. F E B S Letters, 587(9), 1405-1410. https://doi.org/10.1016/j.febslet.2013.03.018

Pedersen, J. S. & Otzen, D. (2008). Amyloid - a state in many guises: survival of the fittest fibril fold. Protein Science, 17, 1-9.

Pedersen, L. R. L., Nielsen, S. B., Hansted, J. G., Petersen, T. E., Otzen, D. E. & Sørensen, E. S. (2012). PP3 forms stable tetrameric structures through hydrophobic interactions via the C-terminal amphipathic helix and undergoes reversible thermal dissociation and denaturation. F E B S Journal, 279(2), 336-47. https://doi.org/10.1111/j.1742-4658.2011.08428.x

Pedersen, J. S., Andersen, C. B. & Otzen, D. (2010). Amyloid structure--one but not the same: the many levels of fibrillar polymorphism. The F E B S Journal (Online), 277(22), 4591-4601. https://doi.org/10.1111/j.1742-4658.2010.07888.x

Pedersen, L. R. L., Hansted, J. G., Nielsen, S. B., Petersen, T. E., Sørensen, U. S., Otzen, D. & Sørensen, E. S. (2012). Proteolytic activation of proteose peptone component 3 by release of a C-terminal peptide with antibacterial properties. Journal of Dairy Science, 95(6), 2819-2829. https://doi.org/10.3168/jds.2011-4837

Pedersen, J. S., Dikov, D. & Otzen, D. (2006). N- and C-Terminal Hydrophobic Patches Are Involved in Fibrillation of Glucagon. Biochemistry, 45(48), 14503-14512. https://doi.org/10.1021/bi061228n

Pedersen, J. S., Flink, J. M., Dikov, D. & Otzen, D. (2006). Sulfates Dramatically Stabilize a Salt-Dependent Type of Glucagon Fibrils. Biophysical Journal, 90(11), 4181-4194. https://doi.org/10.1529/biophysj.105.070912

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

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

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

Pedersen, J. N., Sørensen, H. V. & Otzen, D. E. (2018). Stabilizing vitamin D₃ using the molten globule state of α-lactalbumin. Journal of Dairy Science, 101(3), 1817–1826. https://doi.org/10.3168/jds.2017-13818

Pedersen, J. N., Jiang, Z., Christiansen, G., Lee, J. C., Pedersen, J. S. & Otzen, D. E. (2019). Lysophospholipids induce fibrillation of the repeat domain of Pmel17 through intermediate core-shell structures. Biochimica et Biophysica Acta - Proteins and Proteomics, 1867(5), 519-528. https://doi.org/10.1016/j.bbapap.2018.11.007

Pedersen, J. S., Christensen, G. & Otzen, D. E. (2004). Modulation of S6 fibrillation by unfolding rates and gatekeeper residues. Journal of Molecular Biology, 341(2), 575-588. https://doi.org/10.1016/j.jmb.2004.06.020

Pedersen, J. N., Lyngsø, J., Zinn, T., Otzen, D. & Pedersen, J. S. (2020). A complete picture of protein unfolding and refolding in surfactants. Chemical Science, 11(3), 699-712. https://doi.org/10.1039/C9SC04831F

Pedersen, J. N., Frislev, H. K. S., Pedersen, J. S. & Otzen, D. (2020). Structures and mechanisms of formation of liprotides. B B A - Proteins and Proteomics, 1868(11), [140505]. https://doi.org/10.1016/j.bbapap.2020.140505

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

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

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

Displaying results 51 to 100 out of 407

Revised 17.04.2023

Lise Refstrup Linnebjerg Pedersen