Find

For students
For PhDs
For employees

Interdisciplinary Nanoscience Center

Publications

Recent publications

Sort by: Date | Author | Title

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

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, 1206-1214. https://doi.org/10.1016/j.bbapap.2016.05.003

Otzen, D., Sehgal, P. & Nesgaard, L. (2007). Alternative membrane protein conformations in alcohol. Biochemistry, (46), 4348-4359.

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

Otzen, D. (2008). Differential adsorption of variants of the thermomyces lanuginosus lipase on a hydrophobic surface suggests a role for local flexibility. Colloids and Surfaces B: Biointerfaces, (64), 223-228.

Otzen, D., Nesgaard, L., Andersen, K. K., Hansen, J. H., Christiansen, G., Doe, H. & Sehgal, P. (2008). Aggregation of S6 in a quasi-native state by monomeric SDS. B B A - Biomembranes, (1784), 400-414.

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.

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.

Otzen, D. E. (2011). Mapping the folding pathway of the transmembrane protein DsbB by protein engineering. Protein Engineering Design and Selection (Print), 24(1-2), 139-149. https://doi.org/10.1093/protein/gzq079

Otzen, D. E. (2010). Amyloid formation in surfactants and alcohols: membrane mimetics or structural switchers? Current protein & peptide science, 11(5), 355-71.

Otzen, D. (2010). Functional amyloid: turning swords into plowshares. Prion, 4(4), 256-64.

Otzen, D. (2010). Functional bacterial amyloids in biofilms. Annual Biofilm Highlights.

Otzen, D. (2010). Surfactants and alcohols as inducers of protein amyloid: aggregation chaperones or membrane simulators? Lipids and membranes in amyloid diseases.

Otzen, D. (2010). Institutional nonconformism: the many levels of glucagon polymorphism. F E B S Journal.

Otzen, D. & Enghild, J. J. (2010). Human phenotypically distinct TGFI corneal dystrophies are linked to the stability of the fourth Fas1 domain of TGFBIp. Journal of Biological Chemistry.

Otzen, D. (2010). Occupancy of non-annular lipid binding sites on KcsA greatly increases the stability of the tetrameric protein. Biochemistry.

Otzen, D. E. (2011). Assembling good amyloid some structures at last. Structure, 19(9), 1207-1209. https://doi.org/10.1016/j.str.2011.08.005

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. (2012). N for AsN - O for StrOcture? A strand-loop-strand motif for prokaryotic O-glycosylation. Molecular Oral Microbiology. https://doi.org/10.1111/j.1365-2958.2012.07972.x

Otzen, D., Blans, K., Wang, H., Gilbert, G. E. & Rasmussen, J. T. (2012). Lactadherin binds to phosphatidylserine-containing vesicles in a two-step mechanism sensitive to vesicle size and composition. BBA General Subjects, 1818(4), 1019-1027. https://doi.org/10.1016/j.bbamem.2011.08.032

Otzen, D. & Andersen, K. K. (2013). Folding of outer membrane proteins. Archives of Biochemistry and Biophysics, 531(1-2), 34-43. https://doi.org/10.1016/j.abb.2012.10.008

Otzen, D. (2014). Membrane protein folding and stability. Archives of Biochemistry and Biophysics, 564, 262-264. https://doi.org/10.1016/j.abb.2014.10.014

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

Otzen, D. (2017). Biosurfactants and surfactants interacting with membranes and proteins: Same but different? BBA Biomembranes, 1859(4), 639–649. https://doi.org/10.1016/j.bbamem.2016.09.024

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

Otzen, D. (2005). Antagonism, non-native interactions and non-two-state folding in S6 revealed by double-mutant cycle analysis. Protein Engineering, Design and Selection, 18(11), 547-557. https://doi.org/10.1093/protein/gzi063

Otzen, D. E. (2005). Conformational detours during folding of a collapsed state. Biochimica et Biophysica Acta - Proteins and Proteomics, 1750(2), 146-153. https://doi.org/10.1016/j.bbapap.2005.05.006

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

Otzen, D. E. & Oliveberg, M. (2004). Correspondence between anomalous m- and ΔC_p-values in protein folding. Protein Science, 13(12), 3253-3263. https://doi.org/10.1110/ps.04991004

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., Oliveberg, M. & Höök, F. (2003). Adsorption of a small protein to a methyl-terminated hydrophobic surfaces: Effect of protein-folding thermodynamics and kinetics. Colloids and Surfaces B: Biointerfaces, 29(1), 67-73. https://doi.org/10.1016/S0927-7765(02)00186-8

Otzen, D. E. (2003). Folding of DsbB in mixed micelles: a kinetic analysis of the stability of a bacterial membrane protein. Journal of Molecular Biology, 330(4), 641-649. https://doi.org/10.1016/S0022-2836(03)00624-7

Otzen, D. E. & Oliveberg, M. (2002). Conformational plasticity in folding of the split β-α-β protein S6: Evidence for burst-phase disruption of the native state. Journal of Molecular Biology, 317(4), 613-627. https://doi.org/10.1006/jmbi.2002.5423

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. E. & Oliveberg, M. (2002). Burst-phase expansion of native protein prior to global unfolding in SDS. Journal of Molecular Biology, 315(5), 1231-1240. https://doi.org/10.1006/jmbi.2001.5300

Otzen, D. E., Knudsen, B. R., Aachmann, F., Larsen, K. L. & Wimmer, R. (2002). Structural basis for cyclodextrins' suppression of human growth hormone aggregation. Protein Science, 11(7), 1779-1787. https://doi.org/10.1110/ps.0202702

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

Otzen, D. E. & Oliveberg, M. (2001). A simple way to measure protein refolding rates in water. Journal of Molecular Biology, 313(3), 479-483. https://doi.org/10.1006/jmbi.2001.5039

Otzen, D. E., Kristensen, O. & Oliveberg, M. (2000). Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly. Proceedings of the National Academy of Sciences, 97(18), 9907-9912. https://doi.org/10.1073/pnas.160086297

Otzen, D. E., Christiansen, L. & Schülein, M. (1999). A comparative study of the unfolding of the endoglucanase Ce145 from Humicola insolens in denaturant and surfactant. Protein Science, 8(9), 1878-1887. https://doi.org/10.1110/ps.8.9.1878

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

Otzen, D. E. & Fersht, A. R. (1999). Analysis of protein-protein interactions by mutagenesis: Direct versus indirect effects. Protein Engineering, 12(1), 41-45.

Otzen, D. E., Kristensen, O., Proctor, M. & Oliveberg, M. (1999). Structural changes in the transition state of protein folding: Alternative interpretations of curved chevron plots. Biochemistry, 38(20), 6499-6511. https://doi.org/10.1021/bi982819j

Otzen, D. E. & Fersht, A. R. (1998). Folding of circular and permuted chymotrypsin inhibitor 2: Retention of the folding nucleus. Biochemistry, 37(22), 8139-8146. https://doi.org/10.1021/bi980250g

Otzen, D. E., Rheinnecker, M. & Fersht, A. R. (1995). Structural Factors Contributing to the Hydrophobic Effect: The Partly Exposed Hydrophobic Minicore in Chymotrypsin Inhibitor. Biochemistry, 34(40), 13051-13058. https://doi.org/10.1021/bi00040a016

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

Otzen, D. E., Barciszewski, J. & Clark, B. F. C. (1994). Dual hydrolytic role for Pb(II) ions. Biochimie, 76(1), 15-21. https://doi.org/10.1016/0300-9084(94)90058-2

Otzen, D. E., Itzhaki, L. S., Elmasry, N. F., Jackson, S. E. & Fersht, A. R. (1994). Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding. Proceedings of the National Academy of Sciences, 91(22), 10422-10425. https://doi.org/10.1073/pnas.91.22.10422

Displaying results 101 to 150 out of 407

3

Revised 17.04.2023

-

Lise Refstrup Linnebjerg Pedersen