Christiansen, J. R., Olesen, M. N., Otzen, D. E., Romero-Ramos, M. & Sanchez-Guajardo, V. (2016).
α-Synuclein vaccination modulates regulatory T cell activation and microglia in the absence of brain pathology.
Journal of Neuroinflammation,
13(1), Article 74.
https://doi.org/10.1186/s12974-016-0532-8
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
Nielsen, S. B., Macchi, F., Raccosta, S., Langkilde, A. E.
, Giehm, L., Kyrsting, A.
, Svane, A. S. P., Manno, M.
, Christiansen, G., Nielsen, N. C., Oddershede, L., Vestergaard, B.
& Otzen, D. (2013).
Wildtype and A30P Mutant Alpha-Synuclein Form Different Fibril Structures.
P L o S One,
8(7), Article e67713.
https://doi.org/10.1371/journal.pone.0067713
Jensen, P. L., Dueholm, M. S., Larsen, P.
, Petersen, S. V., Enghild, J. J., Christiansen, G., Højrup, P., Nielsen, P. H.
& Otzen, D. (2009).
Widespread abundance of Functional Bacterial Amyloid in Mycolata and other Gram positive Bacteria.
Applied and Environmental Microbiology,
75, 4101-4110.
Madsen, J. K., Kaspersen, J. D., Andersen, K. K., Pedersen, J. S. & Otzen, D. E. (2016).
When Enzymes and Green Surfactants Meet.
Biophysical Journal,
110(3), 211A.
https://doi.org/10.1016/j.bpj.2015.11.1171
Andersen, K. K., Vad, B. S., Roelants, S., van Bogaert, I. N. A.
& Otzen, D. E. (2016).
Weak and Saturable Protein-Surfactant Interactions in the Denaturation of Apo-α-Lactalbumin by Acidic and Lactonic Sophorolipid.
Frontiers in Microbiology,
7(NOV), Article 1711.
https://doi.org/10.3389/fmicb.2016.01711
Wang, H., Hagedorn, J., Svendsen, A., Borch, K.
& Otzen, D. (2013).
Variant of the Thermomyces lanuginosus lipase with improved kinetic stability: a candidate for enzyme replacement therapy.
Biophysical Chemistry,
172, 43-52.
https://doi.org/10.1016/j.bpc.2012.12.003
Nielsen, J. T., Bjerring, M., Jeppesen, M., Pedersen, R. O.
, Pedersen, J. M., Hein, K. L., Vosegaard, T., Skrydstrup, T., Otzen, D. & Nielsen, N. C. (2009).
Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy.
Angewandte Chemie International Edition,
48, 2118-2121.
Nielsen, J. T., Bjerring, M., Jeppesen, M., Pedersen, R. O., Pedersen, J. M., Hein, K. L., Vosegaard, T., Skrydstrup, T., Otzen, D. & Nielsen, N. C. (2009).
Unique Identification of Supramolecular Structures in Amyloid Fibrils by Solid-State NMR. Poster session presented at 50th Experimental NMR Conference (ENC), Asilomar, CA, United States.
Meisl, G., Xu, C. K., Taylor, J. D., Michaels, T. C. T., Levin, A.
, Otzen, D., Klenerman, D., Matthews, S., Linse, S.
, Andreasen, M. & Knowles, T. P. J. (2022).
Uncovering the universality of self-replication in protein aggregation and its link to disease.
Science Advances,
8(32), Article eabn6831.
https://doi.org/10.1126/sciadv.abn6831
Monti, M., Milanetti, E., Frans, M. T., Miotto, M., Di Rienzo, L., Baranov, M. V., Gosti, G.
, Somavarapu, A. K., Nagaraj, M., Golbek, T. W., Rossing, E., Moons, S. J., Boltje, T. J., van den Bogaart, G.
, Weidner, T., Otzen, D. E., Tartaglia, G. G., Ruocco, G.
& Roeters, S. J. (2024).
Two Receptor Binding Strategy of SARS-CoV-2 Is Mediated by Both the N-Terminal and Receptor-Binding Spike Domain.
The journal of physical chemistry. B,
128(2), 451-464.
https://doi.org/10.1021/acs.jpcb.3c06258
van Diggelen, F., Hrle, D., Apetri, M.
, Christiansen, G., Rammes, G., Tepper, A.
& Otzen, D. E. (2019).
Two conformationally distinct α-synuclein oligomers share common epitopes and the ability to impair long-term potentiation.
PLOS ONE,
14(3), Article 0213663.
https://doi.org/10.1371/journal.pone.0213663
Melo, E. P., Chen, L. Y., Cabral, J. M. S., Fojan, P.
, Petersen, S. B. & Otzen, D. E. (2003).
Trehalose favors a cutinase compact intermediate off-folding pathway.
Biochemistry,
42(24), 7611-7617.
https://doi.org/10.1021/bi034267x
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 (PNAS),
113(8), 2098-2103.
https://doi.org/10.1073/pnas.1524027113
Malmos, K., Blancas-Mejia, L. M., Weber, B., Buchner, J., Ramirez-Alvarado, M., Naiki, H.
& Otzen, D. (2017).
ThT 101: a primer on the use of thioflavin T to investigate amyloid formation.
Amyloid: the Journal of Protein Folding Disorders,
24(1), 1-16.
https://doi.org/10.1080/13506129.2017.1304905
Basaiawmoit, R. V., Deva, T., Runager, K., Kristensen, T., Enghild, J. J. & Otzen, D. (2009).
The Underlying Mechanisms of TGFBIp-mediated Corneal Dystrophies. Abstract from Asia ARVO, International Meeting on Research in Vision and Ophthalmology, Hyderabad International Convention Center. Abstract number: PAP05.01, Hyderabad, India.
Dueholm, M. S., Larsen, P.
, Finster, K., Stenvang, M. R., Christiansen, G., Vad, B. S., Bøggild, A., Otzen, D. E. & Halkjær Nielsen, P. (2015).
The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids.
Journal of Biological Chemistry,
290, 20590-26600.
https://doi.org/10.1074/jbc.M115.654780
Agerschou, E. D., Christiansen, G., Schafer, N. P., Madsen, D. J., Brodersen, D. E., Semsey, S.
& Otzen, D. E. (2016).
The transcriptional regulator GalR self-assembles to form highly regular tubular structures.
Scientific Reports,
6, Article 27672.
https://doi.org/10.1038/srep27672
Marvian, A. T.
, Aliakbari, F., Mohammad-Beigi, H., Ahmadi, Z. A., Mehrpouyan, S., Lermyte, F., Nasouti, M., Collingwood, J. F.
, Otzen, D. E. & Morshedi, D. (2020).
The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization.
International Journal of Biological Macromolecules,
155, 543-550.
https://doi.org/10.1016/j.ijbiomac.2020.03.238
Cavallin, A., Arozenius, H., Kristensson, K., Antonsson, P.
, Otzen, D. E., Björk, P. & Forsberg, G. (2000).
The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function.
Journal of Biological Chemistry,
275(3), 1665-1672.
https://doi.org/10.1074/jbc.275.3.1665
Christensen, L. F. B., Hansen, L. M.
, Finster, K., Christiansen, G., Nielsen, P. H.
, Otzen, D. E. & Dueholm, M. S. (2018).
The Sheaths of Methanospirillum Are Made of a New Type of Amyloid Protein.
Frontiers in Microbiology,
9(NOV), Article 2729.
https://doi.org/10.3389/fmicb.2018.02729,
https://doi.org/10.3389/fmicb.2018.02729
Lorenzen, N., Nielsen, S. B., Buell, A. K.
, Kaspersen, J. D., Arosio, P.
, Vad, B. S., Paslawski, W., Christiansen, G., Valnickova Hansen, Z., Andreasen, M., Enghild, J. J., Pedersen, J. S., Dobson, C. M., Knowles, T. P. J.
& Otzen, D. (2014).
The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation.
Journal of the American Chemical Society,
136(10), 3859-3868.
https://doi.org/10.1021/ja411577t
Andersen, K., Oliveira, C. L. P. D., Larsen, K. L., Poulsen, F., Callisen, T., Westh, P.
, Pedersen, J. S. & Otzen, D. (2009).
The role of decorated SDS micelles in sub-cmc protein denaturation and association.
Journal of Molecular Biology,
391, 207-226.
Baptista, R. P., Pedersen, S. H., Cabrita, G. J. M.
, Otzen, D., Cabral, J. M. & Melo, E. P. (2008).
Thermodynamics and mechanism of cutinase stabilization by trehalose.
Biopolymers,
89, 538-547.
Christiansen, S. H., Zhang, X., Juul-Madsen, K., Hvam, M. L., Vad, B. S., Behrens, M. A., Thygesen, I. L., Jalilian, B., Pedersen, J. S., Howard, K., Otzen, D. E. & Vorup-Jensen, T. (2017).
The random co-polymer glatiramer acetate rapidly kills primary human leukocytes through sialic-acid-dependent cell membrane damage.
B B A - Biomembranes,
1859(3), 425-437.
https://doi.org/10.1016/j.bbamem.2017.01.001
Aliakbari, F., Mohammad-Beigi, H., Rezaei-Ghaleh, N., Becker, S., Dehghani Esmatabad, F., Eslampanah Seyedi, H. A., Bardania, H., Tayaranian Marvian, A., Collingwood, J. F.
, Christiansen, G., Zweckstetter, M.
, Otzen, D. E. & Morshedi, D. (2018).
The potential of zwitterionic nanoliposomes against neurotoxic alpha-synuclein aggregates in Parkinson's Disease.
Nanoscale,
10(19), 9174-9185.
https://doi.org/10.1039/c8nr00632f
Lorenzen, N., Lemminger, L., Pedersen, J. N., Nielsen, S. B. & Otzen, D. (2014).
The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes.
FEBS Letters,
588(3), 497-502.
https://doi.org/10.1016/j.febslet.2013.12.015
Helwig, M., Hoshino, A., Berridge, C., Lee, S.-N.
, Lorenzen, N., Otzen, D., Eriksen, J. & Lindberg, I. (2013).
The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins.
Journal of Biological Chemistry,
288(2), 1114.
Jarvela, T. S., Lam, H. A., Helwig, M.
, Lorenzen, N., Otzen, D. E., McLean, P. J., Maidment, N. T. & Lindberg, I. (2016).
The neural chaperone proSAAS blocks α-synuclein fibrillation and neurotoxicity.
Proceedings of the National Academy of Sciences (PNAS),
113(32), E4708-E4715.
https://doi.org/10.1073/pnas.1601091113