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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.

Otzen, D. & Schülein, M. (2001). Stability and Folding of Endoglucanase I (CEL7B) from Humicoia Insolens. Biocatalysis and Biotransformation, 19(42130), 469-487. https://doi.org/10.3109/10242420108992031

Christensen, P. A., Pedersen, J. S., Christiansen, G. & Otzen, D. (2008). Spectroscopic Evidence for the Existence of an Obligate Pre-Fibrillar Oligonomer during Glucagon Fibrillation. FEBS Letters, (582), 1341-1345.

Adam, L., Kumar, R., Arroyo-Garcia, L. E., Molenkamp, W. H., Nowak, J. S., Klute, H., Farzadfard, A., Alkenayeh, R., Nielsen, J., Biverstål, H., Otzen, D. E., Johansson, J. & Abelein, A. (2024). Specific inhibition of α-synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS. Protein Science, 33(8), Article e5091. https://doi.org/10.1002/pro.5091

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., 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.

Wang, J., Jensen, U. B., Jensen, G. V., Shipovskov, S., Balakrishnan, V. S., Otzen, D., Pedersen, J. S., Besenbacher, F. & Sutherland, D. S. (2011). Soft Interactions at Nanoparticles Alter Protein Function and Conformation in a Size Dependent Manner. Nano Letters, 11(11), 4985-4991. https://doi.org/10.1021/nl202940k

Juul-Madsen, K., Qvist, P., Bendtsen, K. L., Langkilde, A. E., Vestergaard, B., Howard, K., Dehesa-Etxebeste, M., Paludan, S. R., Andersen, G. R., Jensen, P. H., Otzen, D. E., Romero-Ramos, M. & Vorup-Jensen, T. (2020). Size-Selective Phagocytic Clearance of Fibrillar α-Synuclein through Conformational Activation of Complement Receptor 4. Journal of Immunology, 204(5), 1345-1361. https://doi.org/10.4049/jimmunol.1900494

Fersht, A. R., Itzhaki, L. S., Elmasry, N. F., Matthews, J. M. & Otzen, D. E. (1994). Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. Proceedings of the National Academy of Sciences, 91(22), 10426-10429. https://doi.org/10.1073/pnas.91.22.10426

Otzen, D. E. & Fersht, A. R. (1995). Side-Chain Determinants of β-Sheet Stability. Biochemistry, 34(17), 5718-5724. https://doi.org/10.1021/bi00017a003

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

Sønderby, T. V., Louros, N. N., Khodaparast, L., Khodaparast, L., Madsen, D. J., Olsen, W. P., Moonen, N., Nagaraj, M., Sereikaite, V., Strømgaard, K., Rousseau, F., Schymkowitz, J. & Otzen, D. E. (2023). Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation. Journal of Molecular Biology, 435(11), 168039. Article 168039. https://doi.org/10.1016/j.jmb.2023.168039

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

Krainer, G., Hartmann, A., Bogatyr, V., Nielsen, J., Schlierf, M. & Otzen, D. E. (2020). SDS-induced multi-stage unfolding of a small globular protein through different denatured states revealed by single-molecule fluorescence. Chemical Science, 11(34), 9141-9153. https://doi.org/10.1039/d0sc02100h

Giehm, L., Oliveira, C. L. P. D., Christiansen, G., Pedersen, J. S. & Otzen, D. (2010). SDS-Induced Fibrillation of α-Synuclein: An Alternative Fibrillation Pathway. Journal of Molecular Biology, 401, 115-133. https://doi.org/10.1016/j.jmb.2010.05.060

Weber, M., Schneider, D., Prodöhl, A., Dreher, C., Becker, C., Underhaug, J., Svane, A. S. P., Malmendal, A., Nielsen, N. C. & Otzen, D. (2011). SDS-facilitated in vitro formation of a transmembrane B-type cytochrome is mediated by changes in local pH. Journal of Molecular Biology, 407(4), 594-606. https://doi.org/10.1016/j.jmb.2011.02.005

Kalashnyk, N., Nielsen, J. T., Nielsen, E. H., Skrydstrup, T., Otzen, D., Lægsgaard, E., Wang, C., Besenbacher, F., Nielsen, N. C. & Linderoth, T. R. (2012). Scanning tunneling microscopy reveals single-molecule insights into the self-assembly of amyloid fibrils. A C S Nano, 6(8), 6882-6889. https://doi.org/10.1021/nn301708d

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

Oliveira, C. L. P. D., Behrens, M. A., Pedersen, J. S., Erlacher, K., Otzen, D. & Pedersen, J. S. (2009). SAXS Study of Glucagon Fibrillation: From Monomers to Fibers. Journal of Molecular Biology, 387, 147-161.

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

Otzen, D. E. & Oliveberg, M. (1999). Salt-induced detour through compact regions of the protein folding landscape. Proceedings of the National Academy of Sciences, 96(21), 11746-11751. https://doi.org/10.1073/pnas.96.21.11746

Lorenzen, N., Cohen, S. I. A., Nielsen, S. B., Herling, T. W., Christiansen, G., Dobson, C. M., T. P. Knowles, T. & Otzen, D. (2012). Role of elongation and secondary pathways in S6 amyloid fibril growth. Biophysical Journal, 102(9), 2167-2175. https://doi.org/10.1016/j.bpj.2012.03.047

Nedergaard Pedersen, J., Wilhelmus Johannes Maria Frederix, P., Skov Pedersen, J., Marrink, S. J. & Otzen, D. (2018). Role of charge and hydrophobicity in liprotide formation: a molecular dynamics study with experimental constraints. ChemBioChem, 19(3), 263–271. https://doi.org/10.1002/cbic.201700496

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

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. FEBS Letters, 318, 186-188.

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

Tan, Y. J., Oliveberg, M., Otzen, D. E. & Fersht, A. R. (1997). Rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2. Journal of Molecular Biology, 269(4), 611-622. https://doi.org/10.1006/jmbi.1997.1043

Hovgaard, M. B., Dong, M., Otzen, D. & Besenbacher, F. (2007). Quartz crystal microbalance studies of multilayer glucagons fibrillation at the solid-liquid interface. Biophysical Journal, 93(6), 2162.

Hovgaard, M. B., Dong, M., Otzen, D. E. & Besenbacher, F. (2007). Quartz crystal microbalance studies of multilayer glucagon fibrillation at the solid-liquid interface. Biophysical Journal, 93(6), 2162-9. https://doi.org/10.1529/biophysj.107.109686

Nielsen, S. B. & Otzen, D. E. (2019). Quartz Crystal Microbalances as Tools for Probing Protein-Membrane Interactions. In J. H. Kleinschmidt (Ed.), Methods in Molecular Biology: Methods and Protocols (Vol. 2003, pp. 31-52). Springer. https://doi.org/10.1007/978-1-4939-9512-7_2

Nielsen, S. B. & Otzen, D. (2013). Quartz crystal microbalances as tools for probing protein-membrane interactions. In J. Kleinschmidt (Ed.), Lipid-Protein Interactions: Methods and Protocols: Methods in Molecular Biology (Vol. 974, pp. 1-21). https://doi.org/10.1007/978-1-62703-275-9_1

Franzmann, M., Otzen, D. & Wimmer, R. (2009). Quantitative use of paramagnetic relaxation enhancements for determining orientation and insertion depth of peptides in micelles. ChemBioChem, 10, 2339-2347.

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. Journal of Biological Chemistry, 295(37), 13036-13041. https://doi.org/10.1074/jbc.ra120.013396

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

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

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

Kilic, N., Stensballe, A., Otzen, D. & Dönmez, G. (2009). Proteomic changes in response to chromium(VI) toxicity in Pseudomonas aeruginosa . Bioresource Technology, 101, 2134-2140.

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

Otzen, D. E. (2002). Protein unfolding in detergents: Effect of micelle structure, ionic strength, pH, and temperature. Biophysical Journal, 83(4), 2219-2230. https://doi.org/10.1016/S0006-3495(02)73982-9

Otzen, D. (2011). Protein-surfactant interactions a tale of many states. BBA General Subjects, 1814(5), 562-91. https://doi.org/10.1016/j.bbapap.2011.03.003

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

López Hernández, M., Pedersen, J. S. & Otzen, D. E. (2023). Proteins and biosurfactants: Structures, functions, and recent applications. Current Opinion in Colloid and Interface Science, 68, Article 101746. https://doi.org/10.1016/j.cocis.2023.101746

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

Brinkmann, C. R., Thiel, S. & Otzen, D. (2013). Protein:fatty acid complexes: Biochemistry, biophysics and function. FEBS 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

Frøkjær, S. & Otzen, D. (2005). Protein drug stability: a formulation challenge. Nature Reviews. Drug Discovery, 4, 298-306. https://doi.org/10.1038/nrd1695

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

Sneppen, K., Lizana, G. L., Jensen, M. H., Pigolotti, S. & Otzen, D. (2009). Proteasome-Fibrillation Antagonism in a Dynamic Model for Parkinson’s Disease. Physical Biology, 6, 36005.

Fatum, T. M., Olsen, A. A., Fuglsang, C. C. & Otzen, D. (1998). Properties of PEG-modified microbial proteases. Activity and stability studies. Progress in Biotechnology, 15(C), 147-150. https://doi.org/10.1016/S0921-0423(98)80024-5

Displaying results 101 to 150 out of 432

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Lise Refstrup Linnebjerg Pedersen