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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

Christensen, L. F. B., Schafer, N., Wolf-Perez, A., Madsen, D. J. & Otzen, D. E. (2019). Bacterial Amyloids: Biogenesis and Biomaterials. In S. Perrett, A. K. Buell & T. P. J. Knowles (Eds.), Advances in Experimental Medicine and Biology (pp. 113-159). Springer. https://doi.org/10.1007/978-981-13-9791-2_4

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

Knudsen, L. J., Nielsen, S. D.-H., Rauh, V., Otzen, D., Dekker, P. J. T. & Larsen, L. B. (2019). Interrelations between chemical changes in lactose-free UHT milk. Abstract from 16th Symposium on Milk Genomics and Human Health, Aarhus, Denmark.

Knudsen, L. J., Nielsen, S. D., Rauh, V., Otzen, D., Dekker, P. J. T. & Larsen, L. B. (2019). Interrelations between chemical changes in lactose-free UHT milk. Abstract from Sandbjerg Seminar 2019, Sønderborg, Denmark.

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

Knudsen, L. J., Nielsen, S. D.-H., Rauh, V., Otzen, D. & Larsen, L. B. (2019). New Lactase Enzymes. Abstract from Sandbjerg Seminar 2019, Sønderborg, Denmark.

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

Nielsen, S. B. & Otzen, D. E. (2019). Quartz Crystal Microbalances as Tools for Probing Protein-Membrane Interactions. In J. H. Kleinschmidt (Ed.), Methods in Molecular Biology: Methods and Protocols (Vol. 2003, pp. 31-52). Springer. https://doi.org/10.1007/978-1-4939-9512-7_2

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

Christensen, L. F. B., Otzen, D. & Dueholm, M. S. (2018). High-quality draft genome sequence of Sphaerisporangium cinnabarinum ATCC 31213. Genome Announcements, 6(21), Article e00456-18. https://doi.org/10.1128/genomeA.00456-18

Nedergaard Pedersen, J., Skov Pedersen, J. & Otzen, D. E. (2018). Liprotides assist in folding of outer membrane proteins. Protein Science, 27(2), 451-462. https://doi.org/10.1002/pro.3337

Kurnik, M., Sahin, C., Andersen, C. B., Lorenzen, N., Giehm, L., Mohammad-Beigi, H., Jessen, C. M., Pedersen, J. S., Christiansen, G., Petersen, S. V., Staal, R., Krishnamurthy, G., Pitts, K., Reinhart, P. H., Mulder, F. A. A., Mente, S., Hirst, W. D. & Otzen, D. E. (2018). Potent α-Synuclein Aggregation Inhibitors, Identified by High-Throughput Screening, Mainly Target the Monomeric State. Cell Chemical Biology, 25(11), 1389-1402. https://doi.org/10.1016/j.chembiol.2018.08.005

Bleem, A., Christiansen, G., Madsen, D. J., Maric, H., Strømgaard, K., Bryers, J. D., Daggett, V., Meyer, R. L. & Otzen, D. E. (2018). Protein Engineering Reveals Mechanisms of Functional Amyloid Formation in Pseudomonas aeruginosa Biofilms. Journal of Molecular Biology, 430(20), 3751-3763. https://doi.org/10.1016/j.jmb.2018.06.043

Andersen, K. K., Vad, B. S., Kjaer, L., Tolker-Nielsen, T., Christiansen, G. & Otzen, D. E. (2018). Pseudomonas aeruginosa rhamnolipid induces fibrillation of human α-synuclein and modulates its effect on biofilm formation. FEBS Letters, 592(9), 1484-1496. https://doi.org/10.1002/1873-3468.13038

Nedergaard Pedersen, J., Wilhelmus Johannes Maria Frederix, P., Skov Pedersen, J., Marrink, S. J. & Otzen, D. (2018). Role of charge and hydrophobicity in liprotide formation: a molecular dynamics study with experimental constraints. ChemBioChem, 19(3), 263–271. https://doi.org/10.1002/cbic.201700496

Pedersen, J. N., Sørensen, H. V. & Otzen, D. E. (2018). Stabilizing vitamin D₃ using the molten globule state of α-lactalbumin. Journal of Dairy Science, 101(3), 1817–1826. https://doi.org/10.3168/jds.2017-13818

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

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

Madsen, J. K., Giehm, L. & Otzen, D. E. (2018). The Use of Surfactants to Solubilise a Glucagon Analogue. Pharmaceutical Research, 35(12), Article 235. https://doi.org/10.1007/s11095-018-2494-2

Frislev, H. S., Nielsen, J., Nylandsted, J. & Otzen, D. (2018). Using Liprotides to Deliver Cholesterol to the Plasma Membrane. Journal of Membrane Biology, 25(4), 581-592. https://doi.org/10.1007/s00232-018-0034-y

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

Rouse, S. L., Hawthorne, W. J., Berry, J.-L., Chorev, D. S., Ionescu, S. A., Lambert, S., Stylianou, F., Ewert, W., Mackie, U., Morgan, R. M. L., Otzen, D., Herbst, F.-A., Nielsen, P. H., Dueholm, M., Bayley, H., Robinson, C. V., Hare, S. & Matthews, S. (2017). A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis. Nature Communications, 8(1), Article 263. https://doi.org/10.1038/s41467-017-00361-6

Sahin, C., Lorenzen, N., Lemminger, L., Christiansen, G., Møller, I. M., Vesterager, L. B., Pedersen, L. Ø., Fog, K., Kallunki, P. & Otzen, D. E. (2017). Antibodies against the C-terminus of α-synuclein modulate its fibrillation. Biophysical Chemistry, 220, 34-41. https://doi.org/10.1016/j.bpc.2016.11.002

Otzen, D. (2017). Biosurfactants and surfactants interacting with membranes and proteins: Same but different? BBA Biomembranes, 1859(4), 639–649. https://doi.org/10.1016/j.bbamem.2016.09.024

Malmos, K. G., Bjerring, M., Jessen, C. M., Nielsen, E. H. T., Poulsen, E. T., Christiansen, G., Vosegaard, T., Skrydstrup, T., Enghild, J. J., Pedersen, J. S. & Otzen, D. E. (2017). Correction to: How glycosaminoglycans promote fibrillation of salmon calcitonin. Journal of Biological Chemistry, 292(38), 15992. https://doi.org/10.1074/jbc.A116.715466

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Lise Refstrup Linnebjerg Pedersen