Publications

Recent publications

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), Article 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

Nayeri, Z., Aliakbari, F., Afzali, F., Parsafar, S., Gharib, E., Otzen, D. E. & Morshedi, D. (2022). Characterization of exogenous αSN response genes and their relation to Parkinson's disease using network analyses. Frontiers in Pharmacology, 13, Article 966760. https://doi.org/10.3389/fphar.2022.966760

Grønnemose, A. L., Østerlund, E. C., Otzen, D. E. & Jørgensen, T. J. D. (2022). EGCG has Dual and Opposing Effects on the N-terminal Region of Self-associating α-synuclein Oligomers. Journal of Molecular Biology, 434(23), Article 167855. https://doi.org/10.1016/j.jmb.2022.167855

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), Article 167337. https://doi.org/10.1016/j.jmb.2021.167337

Otzen, D. E. (2022). Functional amyloid in a lipid-like environment: a merry dance of many steps. Essays in Biochemistry, 66(7), 1035-1046. https://doi.org/10.1042/EBC20220062

Sønderby, T. V., Najarzadeh, Z. & Otzen, D. E. (2022). Functional Bacterial Amyloids: Understanding Fibrillation, Regulating Biofilm Fibril Formation and Organizing Surface Assemblies. Molecules, 27(13), Article 4080. https://doi.org/10.3390/molecules27134080

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), Article 101848. https://doi.org/10.1016/j.jbc.2022.101848

Otzen, D. E., Pedersen, J. N., Rasmussen, H. Ø. & Pedersen, J. S. (2022). How do surfactants unfold and refold proteins? Advances in Colloid and Interface Science, 308, Article 102754. https://doi.org/10.1016/j.cis.2022.102754

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), Article 101569. https://doi.org/10.1016/j.jbc.2022.101569

Najarzadeh, Z., Mohammad-Beigi, H., Pedersen, J. N., Christiansen, G., Pedersen, J. S., Nielsen, J. & Otzen, D. E. (2022). Interaction of membrane vesicles with the Pseudomonas functional amyloid protein FapC facilitates amyloid formation. BBA advances, 2, Article 100055. https://doi.org/10.1016/j.bbadva.2022.100055

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, Article 3737. https://doi.org/10.1038/s41598-022-07706-2

Sønderby, T. V., Zou, Y., Wang, P., Wang, C. & Otzen, D. E. (2022). Molecular-level insights into the surface-induced assembly of Functional Bacterial Amyloid. Biophysical Journal, 121(18), 3422-3434. https://doi.org/10.1016/j.bpj.2022.08.013

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), Article 37. https://doi.org/10.1186/s12987-022-00334-y

Sahin, C., Østerlund, E. C., Österlund, N., Costeira-Paulo, J., Pedersen, J. N., Christiansen, G., Nielsen, J., Grønnemose, A. L., Amstrup, S. K., Tiwari, M. K., Rao, R. S. P., Bjerrum, M. J., Ilag, L. L., Davies, M. J., Marklund, E. G., Pedersen, J. S., Landreh, M., Møller, I. M., Jørgensen, T. J. D. & Otzen, D. E. (2022). Structural Basis for Dityrosine-Mediated Inhibition of α-Synuclein Fibrillization. Journal of the American Chemical Society, 144(27), 11949-11954. https://doi.org/10.1021/jacs.2c03607

Bisiak, F., Chrenková, A., Zhang, S. D., Pedersen, J. N., Otzen, D. E., Zhang, Y. E. & Brodersen, D. E. (2022). Structural variations between small alarmone hydrolase dimers support different modes of regulation of the stringent response. Journal of Biological Chemistry, 298(7), Article 102142. https://doi.org/10.1016/j.jbc.2022.102142

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

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. Article 123. https://doi.org/10.1038/s42003-022-03059-8

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 (PNAS), 119(25), Article e2203098119. https://doi.org/10.1073/pnas.2203098119

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

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), Article 167231. https://doi.org/10.1016/j.jmb.2021.167231

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, Article 100060. https://doi.org/10.1016/j.bioflm.2021.100060

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

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), Article 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), Article 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. Article 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. Article 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, Article 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

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, Article 690655. https://doi.org/10.3389/fmolb.2021.690655

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

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), Article 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), Article 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

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.202001299

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

Displaying results 51 to 100 out of 448

Revised 17.04.2023

Lise Refstrup Linnebjerg Pedersen