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.0c00426Hajipour, M. J.
, Mohammad-Beigi, H., Nabipour, I., Mahmoudi, N., Azhdarzadeh, M., Derakhshankhah, H., El Dawud, D., Mohammadinejad, R.
& Otzen, D. (2020).
Amyloid fibril inhibition, acceleration, or fragmentation: Are nano-based approaches advance in the right direction? Nano Today,
35(December), Article 100983.
https://doi.org/10.1016/j.nantod.2020.100983Larsen, P., Dueholm, M. S., Christiansen, G., Nielsen, J. L.
, Otzen, D. & Nielsen, P. H. (2007).
Amyloid adhesins are abundant in natural biofilms.
Env. Microbiol., (9), 3077-3090.
Tian, P., Lindorff-Larsen, K., Boomsma, W., Jensen, M. H.
& Otzen, D. E. (2016).
A Monte Carlo Study of the Early Steps of Functional Amyloid Formation.
PLoS One,
11(1), Article e0146096.
https://doi.org/10.1371/journal.pone.0146096Košmrlj, A., Cordsen, P., Kyrsting, A.
, Otzen, D., Oddershede, L. B. & Jensen, M. H. (2015).
A monomer-trimer model supports intermittent glucagon fibril growth.
Scientific Reports,
5, 1-6. Article 9005.
https://doi.org/10.1038/srep09005Ali, S. A., Chung, K. H. K., Forgham, H., Olsen, W. P., Kakinen, A., Balaji, A.
, Otzen, D. E., Davis, T. P. & Javed, I. (2023).
Alzheimer's Progenitor Amyloid-β Targets and Dissolves Microbial Amyloids and Impairs Biofilm Function.
Advanced Science,
10(29), Article e2301423.
https://doi.org/10.1002/advs.202301423Nissen, 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
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.
Biochimica et Biophysica Acta - Proteins and Proteomics,
1864(9), 1206-1214.
https://doi.org/10.1016/j.bbapap.2016.05.003Otzen, 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.
Biochimica et Biophysica Acta - Biomembranes, (1784), 400-414.
Dong, M., Hovgaard, M. B., Mamdouh, W., Xu, S., Otzen, D. & Besenbacher, F. (2008).
AFM-based force spectroscopy measurements of mature amyloid fibrils of the peptide glucagon.
Nanotechnology,
19, 384013.
https://doi.org/10.1088/0957-4484/19/38/384013
Dong, M. D., Hovgaard, M. B., Mamdouh, W., Xu, S. L., Otzen, D. E. & Besenbacher, F. (2008).
AFM-based force spectroscopy measurements of mature amyloid fibrils of the peptide glucagon: Nanotechnology.
Nanotechnology,
19(38).
Ramos Docampo, M. A., Abild Meyer, C., Ryberg, C., Otzen, D. E., Hirsch, C. & Städler, B. (2025).
Actin Polymerizing Motors to Assist Cytoskeleton-like Networks Formation in Artificial Cells.
ACS Nano,
19(42), 37324-37338.
https://doi.org/10.1021/acsnano.5c12624
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
Javed, I., Zhang, Z., Adamcik, J., Andrikopoulos, N., Li, Y.
, Otzen, D. E., Lin, S., Mezzenga, R., Davis, T. P., Ding, F. & Ke, P. C. (2020).
Accelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC.
Advanced Science,
7(18), Article 2001299.
https://doi.org/10.1002/advs.202001299Andersen, C. B., Lausdahl, A. K.
, Nielsen, J., Clausen, M. P.
, Mulder, F. A. A., Otzen, D. E. & Arnspang, E. C. (2023).
4-Oxo-2-nonenal-Induced α-Synuclein Oligomers Interact with Membranes in the Cell, Leading to Mitochondrial Fragmentation.
Biochemistry,
62(16), 2417-2425.
https://doi.org/10.1021/acs.biochem.3c00114
