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Somavarapu, A. K., Kleijwegt, G., Nagaraj, M., Alam, P., Nielsen, J. & Otzen, D. E. (2023). Drug repurposing screens identify compounds that inhibit α-synuclein oligomers' membrane disruption and block antibody interactions. Chemical Science, 14(11), 3030-3047. https://doi.org/10.1039/d2sc05534a

Alijanvand, S. H., Ladefoged, L. K., Zubrienė, A., Sakalauskas, A., Christiansen, G., Dudutiene, V., Schiøtt, B., Matulis, D., Smirnovas, V. & Otzen, D. E. (2023). Inhibitory effects of fluorinated benzenesulfonamides on insulin fibrillation. International Journal of Biological Macromolecules, 227, 590-600. https://doi.org/10.1016/j.ijbiomac.2022.12.105

Pirhaghi, M., Najarzadeh, Z., Moosavi-Movahedi, F., Shafizadeh, M., Mamashli, F., Atarod, D., Ghasemi, A., Morshedi, D., Meratan, A. A., Otzen, D. E. & Saboury, A. A. (2023). The anti-platelet drug ticlopidine inhibits FapC fibrillation and biofilm production: Highlighting its antibiotic activity. B B A - Proteins and Proteomics, 1871(2), 140883. [140883]. https://doi.org/10.1016/j.bbapap.2022.140883

Hourfar, H., Aliakbari, F., Aqdam, S. R., Nayeri, Z., Bardania, H., Otzen, D. E. & Morshedi, D. (2023). The impact of α-synuclein aggregates on blood-brain barrier integrity in the presence of neurovascular unit cells. International Journal of Biological Macromolecules, 229, 305-320. https://doi.org/10.1016/j.ijbiomac.2022.12.134

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

Kjærgaard, M., Rasmussen, L. S., Vinther, J. N., Andersen, K. R., Andersen, E. S., Lorentzen, E., Thirup, S. S., Otzen, D. & Brodersen, D. E. (2022). A Semester-Long Learning Path Teaching Computational Skills via Molecular Graphics in PyMOL. The Biophysicist, 3(2), 106–114. https://doi.org/10.35459/tbp.2022.000219

Pirhaghi, M., Frank, S. A., Alam, P., Nielsen, J., Sereikaite, V., Gupta, A., Strømgaard, K., Andreasen, M., Sharma, D., Saboury, A. A. & Otzen, D. E. (2022). A penetratin-derived peptide reduces the membrane permeabilization and cell toxicity of α-synuclein oligomers. Journal of Biological Chemistry, 298(12), [102688]. https://doi.org/10.1016/j.jbc.2022.102688

He, J., Steffen, J. H., Thulstrup, P. W., Pedersen, J. N., Sauerland, M. B., Otzen, D. E., Hawkins, C. L., Gourdon, P., Davies, M. J. & Hägglund, P. (2022). Anastellin impacts on the processing of extracellular matrix fibronectin and stimulates release of cytokines from coronary artery smooth muscle cells. Scientific Reports, 12(1), [22051]. https://doi.org/10.1038/s41598-022-26359-9

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

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

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), [4080]. https://doi.org/10.3390/molecules27134080

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

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

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, [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), [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

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), [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), [102142]. https://doi.org/10.1016/j.jbc.2022.102142

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

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), [eabn6831]. https://doi.org/10.1126/sciadv.abn6831

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

Displaying results 1 to 50 out of 405

Revised 07.04.2021

Lise Refstrup Linnebjerg Pedersen