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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

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), Article 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, Article 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), Article 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, Article 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, Article 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), Article 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, Article 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, Article 573253. https://doi.org/10.3389/fmicb.2020.573253

Nagaraj, M., Ahmed, M., Lyngsø, J., Vad, B. S., Bøggild, A., Fillipsen, A., Pedersen, J. S., Otzen, D. E. & Akbey, Ü. (2020). Predicted Loop Regions Promote Aggregation: A Study of Amyloidogenic Domains in the Functional Amyloid FapC. Journal of Molecular Biology, 432(7), 2232-2252. https://doi.org/10.1016/j.jmb.2020.01.044

Christensen, L. F. B., Nowak, J. S., Sønderby, T. V., Frank, S. A. & Otzen, D. E. (2020). Quantitating denaturation by formic acid: Imperfect repeats are essential to the stability of the functional amyloid protein FapC. Journal of Biological Chemistry, 295(37), 13036-13041. https://doi.org/10.1074/jbc.ra120.013396

Krainer, G., Hartmann, A., Bogatyr, V., Nielsen, J., Schlierf, M. & Otzen, D. E. (2020). SDS-induced multi-stage unfolding of a small globular protein through different denatured states revealed by single-molecule fluorescence. Chemical Science, 11(34), 9141-9153. https://doi.org/10.1039/d0sc02100h

Juul-Madsen, K., Qvist, P., Bendtsen, K. L., Langkilde, A. E., Vestergaard, B., Howard, K., Dehesa-Etxebeste, M., Paludan, S. R., Andersen, G. R., Jensen, P. H., Otzen, D. E., Romero-Ramos, M. & Vorup-Jensen, T. (2020). Size-Selective Phagocytic Clearance of Fibrillar α-Synuclein through Conformational Activation of Complement Receptor 4. Journal of Immunology, 204(5), 1345-1361. https://doi.org/10.4049/jimmunol.1900494

Pedersen, J. N., Frislev, H. K. S., Pedersen, J. S. & Otzen, D. (2020). Structures and mechanisms of formation of liprotides. B B A - Proteins and Proteomics, 1868(11), Article 140505. https://doi.org/10.1016/j.bbapap.2020.140505

van Gils, J. H. M., van Dijk, E., Peduzzo, A., Hofmann, A., Vettore, N., Schützmann, M. P., Groth, G., Mouhib, H., Otzen, D. E., Buell, A. K. & Abeln, S. (2020). The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth. PLOS Computational Biology, 16(5), Article e1007767. https://doi.org/10.1371/journal.pcbi.1007767

van Diggelen, F., Frank, S. A., Somavarapu, A. K., Scavenius, C., Apetri, M. M., Nielsen, J., Tepper, A. W. J. W., Enghild, J. J. & Otzen, D. E. (2020). The interactome of stabilized α-synuclein oligomers and neuronal proteins. FEBS journal, 287(10), 2037-2054. https://doi.org/10.1111/febs.15124

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

Rasmussen, H. Ø., Enghild, J. J., Otzen, D. E. & Pedersen, J. S. (2020). Unfolding and partial refolding of a cellulase from the SDS-denatured state: From β-sheet to α-helix and back. B B A - General Subjects, 1864(1), 129434 1-12. Article 129434. https://doi.org/10.1016/j.bbagen.2019.129434

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

Mohammad-Beigi, H., Kjær, L., Eskandari, H., Aliakbari, F., Christiansen, G., Ruvo, G., L. Ward, J. & Otzen, D. (2019). A Possible Connection Between Plant Longevity and the Absence of Protein Fibrillation: Basis for Identifying Aggregation Inhibitors in Plants. Frontiers in Plant Science, 10(148), Article 148. https://doi.org/10.3389/fpls.2019.00148

Najarzadeh, Z., Pedersen, J. N., Christiansen, G., Shojaosadati, S. A., Pedersen, J. S. & Otzen, D. E. (2019). Bacterial amphiphiles as amyloid inducers: Effect of Rhamnolipid and Lipopolysaccharide on FapC fibrillation. B B A - Proteins and Proteomics, 1867(11), Article 140263. https://doi.org/10.1016/j.bbapap.2019.140263

Juhl, D. W., Risør, M. W., Scavenius, C., Rasmussen, C. B., Otzen, D., Nielsen, N. C. & Enghild, J. J. (2019). Conservation of the Amyloid Interactome Across Diverse Fibrillar Structures. Scientific Reports, 9(1), Article 3863. https://doi.org/10.1038/s41598-019-40483-z

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

Rasmussen, C. B., Christiansen, G., Vad, B. S., Lynggaard, C., Enghild, J. J., Andreasen, M. & Otzen, D. (2019). Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation. Protein Science, 28(3), 633-642. https://doi.org/10.1002/pro.3566

Wolf Pérez, A.-M., Sormanni, P., Andersen, J. S., Sakhnini, L. I., Rodriguez-Leon, I., Bjelke, J. R., Gajhede, A. J., De Maria, L., Otzen, D. E., Vendruscolo, M. & Lorenzen, N. (2019). In vitro and in silico assessment of the developability of a designed monoclonal antibody library. mAbs, 11(2), 388-400. https://doi.org/10.1080/19420862.2018.1556082

Pedersen, J. N., Jiang, Z., Christiansen, G., Lee, J. C., Pedersen, J. S. & Otzen, D. E. (2019). Lysophospholipids induce fibrillation of the repeat domain of Pmel17 through intermediate core-shell structures. Biochimica et Biophysica Acta - Proteins and Proteomics, 1867(5), 519-528. https://doi.org/10.1016/j.bbapap.2018.11.007

Mohammad-Beigi, H., Hosseini, A., Adeli, M., Ejtehadi, M. R., Christiansen, G., Sahin, C., Tu, Z., Tavakol, M., Dilmaghani-Marand, A., Nabipour, I., Farzadfar, F., Otzen, D. E., Mahmoudi, M. & Hajipour, M. J. (2019). Mechanistic Understanding of the Interactions between Nano-Objects with Different Surface Properties and α-Synuclein. ACS Nano, 13(3), 3243-3256. https://doi.org/10.1021/acsnano.8b08983

Poghosyan, A. H., Schafer, N., Lyngsø, J., Shahinyan, A. A., Pedersen, J. S. & Otzen, D. (2019). Molecular dynamics study of ACBP denaturation in alkyl sulfates demonstrates possible pathways of unfolding through fused surfactant clusters. Protein Engineering, Design and Selection, 32(4), 175-190. Article gzz037. https://doi.org/10.1093/protein/gzz037

Mohammad-Beigi, H., Aliakbari, F., Sahin, C., Lomax, C., Tawfike, A., P. Schafer, N., Amiri-Nowdijeh, A., Eskandari, H., Møller, I. M., Hosseini-Mazinani, M., Christiansen, G., Ward, J. L., Morshedi, D. & Otzen, D. (2019). Oleuropein derivatives from olive fruit extracts reduce α-synuclein fibrillation and oligomer toxicity. Journal of Biological Chemistry, 294(11), 4215-4232. https://doi.org/10.1074/jbc.RA118.005723

Andreasen, M., Meisl, G., Taylor, J. D., Michaels, T. C. T., Levin, A., Otzen, D. E., Chapman, M. R., Dobson, C. M., Matthews, S. J. & Knowles, T. P. J. (2019). Physical Determinants of Amyloid Assembly in Biofilm Formation. mBio, 10(1), Article e02279-18. https://doi.org/10.1128/mBio.02279-18

Najarzadeh, Z., Mohammad-Beigi, H., Pedersen, J. N., Christiansen, G., Sønderby, T. V., Shojaosadati, S. A., Morshedi, D., Strømgaard, K., Meisl, G., Sutherland, D., Pedersen, J. S. & Otzen, D. (2019). Plant polyphenols inhibit functional amyloid and biofilm formation in Pseudomonas strains by directing monomers to off-pathway oligomers. Biomolecules, 9(11), Article 659. https://doi.org/10.3390/biom9110659

Christensen, L. F. B., Jensen, K. F., Nielsen, J., Vad, B. S., Christiansen, G. & Otzen, D. E. (2019). Reducing the Amyloidogenicity of Functional Amyloid Protein FapC Increases Its Ability To Inhibit α-Synuclein Fibrillation. ACS Omega, 4(2), 4029-4039. https://doi.org/10.1021/acsomega.8b03590

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

Alam, P., Bousset, L., Melki, R. & Otzen, D. E. (2019). α-synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicities. Journal of Neurochemistry, 150(5), 522-534. https://doi.org/10.1111/jnc.14808

Højgaard, C., Sørensen, H. V., Pedersen, J. S., Winther, J. R. & Otzen, D. E. (2018). Can a Charged Surfactant Unfold an Uncharged Protein? Biophysical Journal, 115(11), 2081-2086. https://doi.org/10.1016/j.bpj.2018.10.022

Stenvang, M., Schafer, N. P., Malmos, K. G., Pérez, A.-M. W., Niembro, O., Sormanni, P., Basaiawmoit, R. V., Christiansen, G., Andreasen, M. & Otzen, D. E. (2018). Corneal dystrophy mutations drive pathogenesis by targeting TGFBIp stability and solubility in a latent amyloid-forming domain. Journal of Molecular Biology, 430(8), 1116-1140. https://doi.org/10.1016/j.jmb.2018.03.001

Frislev, H. S., Jakobsen, S. C. L., Frank, S. A. & Otzen, D. E. (2018). Dynamic content exchange between liprotides. Biophysical Chemistry, 233, 13-18. https://doi.org/10.1016/j.bpc.2017.11.006

Tiwari, M. K., Leinisch, F., Sahin, C., Møller, I. M., Otzen, D., Davies, M. J. & Bjerrum, M. J. (2018). Early events in copper-ion catalyzed oxidation of α-synuclein. Free Radical Biology & Medicine, 121, 38-50. https://doi.org/10.1016/j.freeradbiomed.2018.04.559

Aliakbari, F., Shabani, A. A., Bardania, H., Mohammad-Beigi, H., Tayaranian Marvian, A., Dehghani Esmatabad, F., Vafaei, A. A., Shojaosadati, S. A., Saboury, A. A., Christiansen, G., Otzen, D. E. & Morshedi, D. (2018). Formulation and anti-neurotoxic activity of baicalein-incorporating neutral nanoliposome. Colloids and surfaces. B, Biointerfaces, 161, 578-587. https://doi.org/10.1016/j.colsurfb.2017.11.023