Mohammad-Beigi, H., Zanganeh, M., Scavenius, C., Eskandari, H., Farzadfard, A., Shojaosadati, S. A., Enghild, J. J., Otzen, D. E., Buell, A. K. & Sutherland, D. S. (2022). A Protein Corona Modulates Interactions of α-Synuclein with Nanoparticles and Alters the Rates of the Microscopic Steps of Amyloid Formation. ACS Nano, 16(1), 1102-1118. https://doi.org/10.1021/acsnano.1c08825

Christensen, N. R., Pedersen, C. P., Sereikaite, V., Pedersen, J. N., Vistrup-Parry, M., Sørensen, A. T., Otzen, D., Teilum, K., Madsen, K. L. & Strømgaard, K. (2022). Bidirectional protein-protein interactions control liquid-liquid phase separation of PSD-95 and its interaction partners. iScience, 25(2), [103808]. https://doi.org/10.1016/j.isci.2022.103808

Nagaraj, M., Najarzadeh, Z., Pansieri, J., Biverstål, H., Musteikyte, G., Smirnovas, V., Matthews, S., Emanuelsson, C., Johansson, J., Buxbaum, J. N., Morozova-Roche, L. & Otzen, D. E. (2022). Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation. Chemical Science, 13(2), 536-553. https://doi.org/10.1039/d1sc05790a

Sønderby, T. V., Rasmussen, H. Ø., Frank, S. A., Skov Pedersen, J. & Otzen, D. E. (2022). Folding steps in the fibrillation of functional amyloid: denaturant sensitivity reveals common features in nucleation and elongation. Journal of Molecular Biology, 434(2), [167337]. https://doi.org/10.1016/j.jmb.2021.167337

Farzadfard, A., König, A., Petersen, S. V., Nielsen, J., Vasili, E., Dominguez-Meijide, A., Buell, A. K., Outeiro, T. F. & Otzen, D. E. (2022). Glycation modulates alpha-synuclein fibrillization kinetics: a sweet spot for inhibition. The Journal of Biological Chemistry, 298(5), [101848]. https://doi.org/10.1016/j.jbc.2022.101848

Rasmussen, H. Ø., Otzen, D. E. & Pedersen, J. S. (2022). Induction, inhibition, and incorporation: Different roles for anionic and zwitterionic lysolipids in the fibrillation of the functional amyloid FapC. The Journal of Biological Chemistry, 298(2), [101569]. https://doi.org/10.1016/j.jbc.2022.101569

Reimer, L., Haikal, C., Gram, H., Theologidis, V., Kovacs, G., Ruesink, H., Baun, A., Nielsen, J., Otzen, D. E., Li, J-Y. & Jensen, P. H. (2022). Low dose DMSO treatment induces oligomerization and accelerates aggregation of α-synuclein. Scientific Reports, 12, [3737]. https://doi.org/10.1038/s41598-022-07706-2

Alam, P., Holst, M. R., Lauritsen, L., Nielsen, J., Nielsen, S. S. E., Jensen, P. H., Brewer, J. R., Otzen, D. E. & Nielsen, M. S. (2022). Polarized α-synuclein trafficking and transcytosis across brain endothelial cells via Rab7-decorated carriers. Fluids and Barriers of the CNS, 19(1), 37. https://doi.org/10.1186/s12987-022-00334-y

Farzadfard, A., Pedersen, J. N., Meisl, G., Somavarapu, A. K., Alam, P., Goksøyr, L., Nielsen, M. A., Sander, A. F., Knowles, T. P. J., Pedersen, J. S. & Otzen, D. E. (2022). The C-terminal tail of α-synuclein protects against aggregate replication but is critical for oligomerization. Communications Biology, 5(1), [123]. https://doi.org/10.1038/s42003-022-03059-8

Rasmussen, H. Ø., Wollenberg, D. T. W., Wang, H., Andersen, K. K., Oliveira, C. L. P., Jørgensen, C. I., Jørgensen, T. J. D., Otzen, D. E. & Pedersen, J. S. (2022). The changing face of SDS denaturation: Complexes of Thermomyces lanuginosus lipase with SDS at pH 4.0, 6.0 and 8.0. Journal of Colloid and Interface Science, 614, 214-232. https://doi.org/10.1016/j.jcis.2021.12.188

Dyla, M., González Foutel, N. S., Otzen, D. E. & Kjaergaard, M. (2022). The optimal docking strength for reversibly tethered kinases. Proceedings of the National Academy of Sciences of the United States of America, 119(25), e2203098119. https://doi.org/10.1073/pnas.2203098119

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

Rasmussen, H. Ø., Otzen, D. E. & Pedersen, J. S. (2021). A multimethod approach for analyzing FapC fibrillation and determining mass per length. Biophysical Journal, 120(11), 2262-2275. https://doi.org/10.1016/j.bpj.2021.03.031

Choong, F. X., Huzell, S., Rosenberg, M., Eckert, J. A., Nagaraj, M., Zhang, T., Melican, K., Otzen, D. E. & Richter-Dahlfors, A. (2021). A semi high-throughput method for real-time monitoring of curli producing Salmonella biofilms on air-solid interfaces. Biofilm, 3, [100060]. https://doi.org/10.1016/j.bioflm.2021.100060

Rahimi Aqdam, S., Otzen, D. E., Mahmoodi, N. M. & Morshedi, D. (2021). Adsorption of azo dyes by a novel bio-nanocomposite based on whey protein nanofibrils and nano-clay: Equilibrium isotherm and kinetic modeling. Journal of Colloid and Interface Science, 602, 490-503. https://doi.org/10.1016/j.jcis.2021.05.174

Serpell, L. C., Radford, S. E. & Otzen, D. (2021). AlphaFold: A Special Issue and a Special time for Protein Science. Journal of Molecular Biology, 433(20), [167231]. https://doi.org/10.1016/j.jmb.2021.167231

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), [120]. https://doi.org/10.1038/s42003-020-01641-6

Amodeo, G. F., Lee, B. Y., Krilyuk, N., Filice, C. T., Valyuk, D., Otzen, D. E., Noskov, S., Leonenko, Z. & Pavlov, E. V. (2021). C subunit of the ATP synthase is an amyloidogenic calcium dependent channel-forming peptide with possible implications in mitochondrial permeability transition. Scientific Reports, 11(1), [8744]. https://doi.org/10.1038/s41598-021-88157-z

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

Najarzadeh, Z., Zaman, M., Sereikaite, V., Strømgaard, K., Andreasen, M. & Otzen, D. E. (2021). Heparin promotes fibrillation of most phenol-soluble modulin virulence peptides from Staphylococcus aureus. The Journal of Biological Chemistry, 297(2), 100953. https://doi.org/10.1016/j.jbc.2021.100953

Andersen, C. B., Yoshimura, Y., Nielsen, J., Otzen, D. E. & Mulder, F. A. A. (2021). How epigallocatechin gallate binds and assembles oligomeric forms of human alpha-synuclein. The Journal of Biological Chemistry, 296, [100788]. https://doi.org/10.1016/j.jbc.2021.100788

Najarzadeh, Z., Nielsen, J., Farzadfard, A., Sereikaite, V., Strømgaard, K., Meyer, R. L. & Otzen, D. E. (2021). Human Fibrinogen Inhibits Amyloid Assembly of Most Phenol-Soluble Modulins from Staphylococcus aureus. ACS Omega, 6(34), 21960-21970. https://doi.org/10.1021/acsomega.1c02333

Christensen, L. F. B., Alijanvand, S. H., Burdukiewicz, M., Herbst, F-A., Kjeldal, H., Dueholm, M. S. & Otzen, D. E. (2021). Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats. Protein Science, 30(9), 1854-1870. https://doi.org/10.1002/pro.4137

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), [2001002]. https://doi.org/10.1002/smtd.202001002

Milanetti, E., Miotto, M., Di Rienzo, L., Nagaraj, M., Monti, M., Golbek, T. W., Gosti, G., Roeters, S. J., Weidner, T., Otzen, D. E. & Ruocco, G. (2021). In-Silico Evidence for a Two Receptor Based Strategy of SARS-CoV-2. Frontiers in Molecular Biosciences, 8, [690655]. https://doi.org/10.3389/fmolb.2021.690655

Andersen, C., Grønnemose, A. L., Pedersen, J. N., Nowak, J. S., Christiansen, G., Nielsen, J., Mulder, F. A. A., Otzen, D. E. & Jørgensen, T. J. D. (2021). Lipid Peroxidation Products HNE and ONE Promote and Stabilize Alpha-Synuclein Oligomers by Chemical Modifications. Biochemistry, 60(47), 3644-3658. https://doi.org/10.1021/acs.biochem.1c00478

Schmüser, L., Trefz, M., Roeters, S. J., Beckner, W., Pfaendtner, J., Otzen, D., Woutersen, S., Bonn, M., Schneider, D. & Weidner, T. (2021). Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy. Langmuir : the ACS journal of surfaces and colloids, 37(45), 13452-13459. https://doi.org/10.1021/acs.langmuir.1c02206

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

Larsen, K., Bæk, R., Sahin, C., Kjær, L., Christiansen, G., Nielsen, J., Farajzadeh, L. & Otzen, D. E. (2021). Molecular characteristics of porcine alpha-synuclein splicing variants. Biochimie, 180, 121-133. https://doi.org/10.1016/j.biochi.2020.10.019

Aliakbari, F., Mohammad-Beigi, H., Abbasi, S., Rezaei-Ghaleh, N., Lermyte, F., Parsafar, S., Becker, S., Tafreshi, A. P., O'Connor, P. B., Collingwood, J. F., Christiansen, G., Sutherland, D. S., Jensen, P. H., Morshedi, D. & Otzen, D. E. (2021). Multiple Protective Roles of Nanoliposome-Incorporated Baicalein against Alpha-Synuclein Aggregates. Advanced Functional Materials, 31(7), [2007765]. https://doi.org/10.1002/adfm.202007765

Ferreira, N., Gram, H., Sorrentino, Z. A., Gregersen, E., Schmidt, S. I., Reimer, L., Betzer, C., Perez-Gozalbo, C., Beltoja, M., Nagaraj, M., Wang, J., Nowak, J. S., Dong, M., Willén, K., Cholak, E., Bjerregaard-Andersen, K., Mendez, N., Rabadia, P., Shahnawaz, M. ... Jensen, P. H. (2021). Multiple system atrophy-associated oligodendroglial protein p25α stimulates formation of novel α-synuclein strain with enhanced neurodegenerative potential. Acta Neuropathologica, 142, 87-115. https://doi.org/10.1007/s00401-021-02316-0

Walther, R., Monge, P., Pedersen, A., Benderoth, A., Pedersen, J., Farzadfard, A., Mandrup, O., Howard, K., Otzen, D. & Zelikin, A. N. (2021). Per-glycosylation of the Surface-Accessible Lysines: One-Pot Aqueous Route to Stabilized Proteins with Native Activity. ChemBioChem, 22(14), 2478-2485. https://doi.org/10.1002/cbic.202100228

Haikal, C., Pascual, L. O., Najarzadeh, Z., Bernfur, K., Svanbergsson, A., Otzen, D. E., Linse, S. & Li, J. Y. (2021). The bacterial amyloids phenol soluble modulins from staphylococcus aureus catalyze alpha-synuclein aggregation. International Journal of Molecular Sciences , 22(21), [11594]. https://doi.org/10.3390/ijms222111594

Mortensen, H. G., Otzen, D. E. & Pedersen, J. S. (2021). Ubiquitin forms conventional decorated micelle structures with sodium dodecyl sulfate at saturation. Journal of Colloid and Interface Science, 596, 233-244. https://doi.org/10.1016/j.jcis.2021.03.110

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), [2001299]. https://doi.org/10.1002/advs.202001299

Hajipour, 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), [100983]. https://doi.org/10.1016/j.nantod.2020.100983

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.0c00426

Nielsen, N. S., Poulsen, E. T., Lukassen, M. V., Chao Shern, C., Mogensen, E. H., Weberskov, C. E., DeDionisio, L., Schauser, L., Moore, T. C. B., Otzen, D. E., Hjortdal, J. & Enghild, J. J. (2020). Biochemical mechanisms of aggregation in TGFBI-linked corneal dystrophies. Progress in Retinal and Eye Research, 77, [100843]. https://doi.org/10.1016/j.preteyeres.2020.100843

Adão, R., Cruz, P. F., Vaz, D. C., Fonseca, F., Pedersen, J. N., Ferreira-da-Silva, F., Brito, R. M. M., Ramos, C. H. I., Otzen, D., Keller, S. & Bastos, M. (2020). DIBMA nanodiscs keep α-synuclein folded. Biochimica et Biophysica Acta - Biomembranes, 1862(9), [183314]. https://doi.org/10.1016/j.bbamem.2020.183314

Ke, P. C., Zhou, R., Serpell, L. C., Riek, R., Knowles, T. P. J., Lashuel, H. A., Gazit, E., Hamley, I. W., Davis, T. P., Fändrich, M., Otzen, D. E., Chapman, M. R., Dobson, C. M., Eisenberg, D. S. & Mezzenga, R. (2020). Half a century of amyloids: past, present and future. Chemical Society Reviews, 49(15), 5473-5509. https://doi.org/10.1039/c9cs00199a

Eskandari, H., Ghanadian, M., Noleto-Dias, C., Lomax, C., Tawfike, A., Christiansen, G., Sutherland, D. S., Ward, J. L., Mohammad-Beigi, H. & Otzen, D. E. (2020). Inhibitors of α-Synuclein fibrillation and oligomer toxicity in Rosa damascena: the all-pervading powers of flavonoids and phenolic glycosides. ACS Chemical Neuroscience, 11(19), 3161–3173. https://doi.org/10.1021/acschemneuro.0c00528

Martins, P. M., Navarro, S., Silva, A., Pinto, M. F., Sárkány, Z., Figueiredo, F., Pereira, P. J. B., Pinheiro, F., Bednarikova, Z., Burdukiewicz, M., Galzitskaya, O. V., Gazova, Z., Gomes, C. M., Pastore, A., Serpell, L. C., Skrabana, R., Smirnovas, V., Ziaunys, M., Otzen, D. E. ... Macedo-Ribeiro, S. (2020). MIRRAGGE - Minimum Information Required for Reproducible AGGregation Experiments. Frontiers in Molecular Neuroscience, 13, [582488]. https://doi.org/10.3389/fnmol.2020.582488

Jensen, G. V., Pedersen, J. N., Otzen, D. E. & Pedersen, J. S. (2020). Multi-Step Unfolding and Rearrangement of α-Lactalbumin by SDS Revealed by Stopped-Flow SAXS. Frontiers in Molecular Biosciences, 7, [125]. https://doi.org/10.3389/fmolb.2020.00125

Huma, Z-E., Javed, I., Zhang, Z., Bilal, H., Sun, Y., Hussain, S. Z., Davis, T. P., Otzen, D. E., Landersdorfer, C. B., Ding, F., Hussain, I. & Ke, P. C. (2020). Nanosilver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition. Small (Weinheim an der Bergstrasse, Germany), 16(21), [1906674]. https://doi.org/10.1002/smll.201906674

Alijanvand, S. H., Christensen, M. H., Christiansen, G., Harikandei, K. B., Salehi, P., Schiøtt, B., Moosavi-Movahedi, A. A. & Otzen, D. E. (2020). Novel noscapine derivatives stabilize the native state of insulin against fibrillation. International Journal of Biological Macromolecules, 147, 98-108. https://doi.org/10.1016/j.ijbiomac.2020.01.061

Jakob, D. S., Wang, H., Zeng, G., Otzen, D. E., Yan, Y. & Xu, X. (2020). Peak Force Infrared - Kelvin Probe Force Microscopy. Angewandte Chemie International Edition, 59(37), 16083-16090. https://doi.org/10.1002/anie.202004211

He, J., Becares, E. R., Thulstrup, P. W., Gamon, L. F., Pedersen, J. N., Otzen, D., Gourdon, P., Davies, M. J. & Hägglund, P. (2020). Peroxynitrous acid (ONOOH) modifies the structure of anastellin and influences its capacity to polymerize fibronectin. Redox Biology, 36, [101631]. https://doi.org/10.1016/j.redox.2020.101631

Baldry, M., Bojer, M. S., Najarzadeh, Z., Vestergaard, M., Meyer, R. L., Otzen, D. E. & Ingmer, H. (2020). Phenol-Soluble Modulins Modulate Persister Cell Formation in Staphylococcus aureus. Frontiers in Microbiology, 11, [573253]. https://doi.org/10.3389/fmicb.2020.573253