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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 (PNAS), 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 (PNAS), 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 (PNAS), 91(22), 10422-10425. https://doi.org/10.1073/pnas.91.22.10422

Otzen, D. E., Barciszewski, J. & Clark, B. F. C. (1993). Altered lead(II)-cleavage pattern of free Phe-tRNA(Phe) and Phe-tRNA(Phe) in ternary complex with EF-Tu:GTP. Biochemistry and Molecular Biology International, 31(1), 95-103.

Otzen, D. & Riek, R. (2019). Functional Amyloids. Cold Spring Harbor Perspectives in Biology, 11(12), Article a033860. https://doi.org/10.1101/cshperspect.a033860

Otzen, D. E., Morshedi, D., Mohammad-Beigi, H. & Aliakbari, F. (2021). A Triple Role for a Bilayer: Using Nanoliposomes to Cross and Protect Cellular Membranes. Journal of Membrane Biology, 254(1), 29-39. https://doi.org/10.1007/s00232-020-00159-6

Otzen, D. E., Buell, A. K. & Jensen, H. (2021). Microfluidics and the quantification of biomolecular interactions. Current Opinion in Structural Biology, 70, 8-15. https://doi.org/10.1016/j.sbi.2021.02.006

Otzen, D. (2021). Driving forces in amyloidosis: How does a light chain make a heavy heart? The Journal of Biological Chemistry, 296, 100785. Article 100785. https://doi.org/10.1016/j.jbc.2021.100785

Otzen, D. E., Pedersen, J. N., Somavarapu, A. K., Clement, A., Ji, M., Petersen, E. H., Pedersen, J. S., Urban, S. & Schafer, N. P. (2021). Cys-labelling kinetics of membrane protein GlpG: a role for specific SDS binding and micelle changes? Biophysical Journal, 120(18), 4115-4128. https://doi.org/10.1016/j.bpj.2021.08.001

Otzen, D. E., Dueholm, M. S., Najarzadeh, Z., Knowles, T. P. J. & Ruggeri, F. S. (2021). In situ Sub-Cellular Identification of Functional Amyloids in Bacteria and Archaea by Infrared Nanospectroscopy. Small Methods, 5(6), Article 2001002. https://doi.org/10.1002/smtd.202001002

Otzen, D. E., Pedersen, J. N., Rasmussen, H. Ø. & Pedersen, J. S. (2022). How do surfactants unfold and refold proteins? Advances in Colloid and Interface Science, 308, Article 102754. https://doi.org/10.1016/j.cis.2022.102754

Otzen, D. E. (2022). Functional amyloid in a lipid-like environment: a merry dance of many steps. Essays in Biochemistry, 66(7), 1035-1046. https://doi.org/10.1042/EBC20220062

Otzen, D. E. (2024). Antibodies and α-synuclein: What to target against Parkinson's Disease? Biochimica et Biophysica Acta - Proteins and Proteomics, 1872(2), Article 140943. https://doi.org/10.1016/j.bbapap.2023.140943

Otzen, D. E., Møllebjerg, A., Hinge, M. & Pathak, G. S. (2024). Hvordan opnår vi en bæredygtig plastikkultur? Aktuel Naturvidenskab, 2024(1), 15-18.

Otzen, D. & d'Angelo, J. (2024). BBA: 2024 and beyond. Biochimica et Biophysica Acta - General Subjects, 1868(2), Article 130524. https://doi.org/10.1016/j.bbagen.2023.130524

Otzen, D. E. (2024). Editorial: Research methods in biochemistry and biophysics. BBA advances, 6, Article 100121. https://doi.org/10.1016/j.bbadva.2024.100121

Otzen, D. E., Peña-Díaz, S., Widmann, J., Daugberg, A. O. H., Zhang, Z., Jiang, Y., Mittal, C., Dueholm, M. K. D., Louros, N., Wang, H. & Javed, I. (2025). Interactions between pathological and functional amyloid: A match made in Heaven or Hell? Molecular Aspects of Medicine, 103, 101351. Article 101351. https://doi.org/10.1016/j.mam.2025.101351

Otzen, D. E., Gamon, L. F., Hägglund, P., Nielsen, J., Pedersen, J. N., Nybo, T., Nowak, J. S., Amstrup, S. K., Pirhaghi, M. & Davies, M. J. (2026). Nitrated products formed on α-synuclein are preferentially incorporated into oligomers but excluded from fibrils: A mechanism for accumulation of neurotoxic species. Biochimica et Biophysica Acta - Proteins and Proteomics, 1874(2), Article 141118. https://doi.org/10.1016/j.bbapap.2025.141118

Olsen, W. P., Courtade, G., Peña-Díaz, S., Nagaraj, M., Sønderby, T. V., Mulder, F. A. A., Malle, M. G. & Otzen, D. E. (2024). CsgA gatekeeper residues control nucleation but not stability of functional amyloid. Protein Science, 33(10), Article e5178. https://doi.org/10.1002/pro.5178

Olsen, W. P., Larsen, A.-K. K., Christensen, J. L., Malle, M. G. & Otzen, D. E. (2025). Investigating strategies for creating cross-linked amyloid fibril networks through branching of amyloid growth. Colloids and surfaces. B, Biointerfaces, 251, 114617. Article 114617. https://doi.org/10.1016/j.colsurfb.2025.114617

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.

Oeemig, J. S., Lynggaard, C., Knudsen, D., Hansen, F. T., Noergaard, K. D., Schneider, T., Vad, B. S., Sandvang, D., Nielsen, L., Neve, S., Kristensen, H.-H., Sahl, H.-G., Otzen, D. & Wimmer, R. (2012). Eurocin, a new fungal defensin: structure, lipid binding and its mode of action. Journal of Biological Chemistry, 7, 42361-42372. https://doi.org/10.1074/jbc.M112.382028

Nybo, T., Gamon, L. F., Fuentes-Lemus, E., Otzen, D. E., Davies, M. J. & Hägglund, P. (2025). Dimethyl labeling of N-terminal amines allows unambiguous identification of protein crosslinks. Free Radical Biology & Medicine, 227, 629-637. https://doi.org/10.1016/j.freeradbiomed.2024.12.002

Nowak, J. S. & Otzen, D. E. (2024). Helping proteins come in from the cold: 5 burning questions about cold-active enzymes. BBA advances, 5, Article 100104. https://doi.org/10.1016/j.bbadva.2023.100104

Nowak, J. S., Olesen, S., Tian, P., Bærentsen, R. L., Brodersen, D. E. & Otzen, D. E. (2025). Role of electrostatics in cold adaptation: A comparative study of eury- and stenopsychrophilic triose phosphate isomerase. Biochimica et Biophysica Acta - Proteins and Proteomics, 1873(4), Article 141072. https://doi.org/10.1016/j.bbapap.2025.141072

Nowak, J. S., Kruuse, N., Rasmussen, H. Ø., Tian, P., Astono, J., Schultz-Nielsen, S., Thøgersen, M. S., Stougaard, P., Pedersen, J. S. & Otzen, D. E. (2025). Quaternary stabilization of a GH2 β-galactosidase from the psychrophile A. ikkensis, a flexible and unstable dimeric enzyme. Protein Science, 34(5), Article e70141. https://doi.org/10.1002/pro.70141

Noji, M., Samejima, T., Yamaguchi, K., So, M., Yuzu, K., Chatani, E., Akazawa-Ogawa, Y., Hagihara, Y., Kawata, Y., Ikenaka, K., Mochizuki, H., Kardos, J., Otzen, D. E., Bellotti, V., Buchner, J. & Goto, Y. (2021). Breakdown of supersaturation barrier links protein folding to amyloid formation. Communications Biology, 4(1), Article 120. https://doi.org/10.1038/s42003-020-01641-6

Nissen, S. K., Shrivastava, K., Schulte, C., Otzen, D. E., Goldeck, D., Berg, D., Møller, H. J., Maetzler, W. & Romero-Ramos, M. (2019). Alterations in Blood Monocyte Functions in Parkinson's Disease. Movement Disorders, 34(11), 1711-1721. https://doi.org/10.1002/mds.27815

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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Lise Refstrup Linnebjerg Pedersen