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Lipid Peroxidation Products HNE and ONE Promote and Stabilize Alpha-Synuclein Oligomers by Chemical Modifications.
Biochemistry,
60(47), 3644-3658. Advance online publication.
https://doi.org/10.1021/acs.biochem.1c00478
Schmüser, L., Trefz, M.
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& 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. Advance online publication.
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Larsen, K., Bæk, R.
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Molecular characteristics of porcine alpha-synuclein splicing variants.
Biochimie,
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Multiple Protective Roles of Nanoliposome-Incorporated Baicalein against Alpha-Synuclein Aggregates.
Advanced Functional Materials,
31(7), Article 2007765.
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Multiple system atrophy-associated oligodendroglial protein p25α stimulates formation of novel α-synuclein strain with enhanced neurodegenerative potential.
Acta Neuropathologica,
142, 87-115. Advance online publication.
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. Advance online publication.
https://doi.org/10.1002/cbic.202100228
Haikal, C., Pascual, L. O.
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The bacterial amyloids phenol soluble modulins from staphylococcus aureus catalyze alpha-synuclein aggregation.
International Journal of Molecular Sciences ,
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Javed, I., Zhang, Z., Adamcik, J., Andrikopoulos, N., Li, Y.
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Accelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC.
Advanced Science,
7(18), Article 2001299.
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Pedersen, J. N., Lyngsø, J., Zinn, T.
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A complete picture of protein unfolding and refolding in surfactants.
Chemical Science,
11(3), 699-712. Advance online publication.
https://doi.org/10.1039/C9SC04831F
Hajipour, M. J.
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Amyloid fibril inhibition, acceleration, or fragmentation: Are nano-based approaches advance in the right direction? Nano Today,
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Sawada, M., Yamaguchi, K., Hirano, M., Noji, M., So, M.
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Amyloid formation of α-synuclein based on the solubility- and supersaturation-dependent mechanism.
Langmuir,
36(17), 4671-4681. Advance online publication.
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.
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DIBMA nanodiscs keep α-synuclein folded.
Biochimica et Biophysica Acta - Biomembranes,
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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.
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Half a century of amyloids: past, present and future.
Chemical Society Reviews,
49(15), 5473-5509. Advance online publication.
https://doi.org/10.1039/c9cs00199a
Eskandari, H., Ghanadian, M., Noleto-Dias, C., Lomax, C., Tawfike, A.
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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. Advance online publication.
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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.
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MIRRAGGE - Minimum Information Required for Reproducible AGGregation Experiments.
Frontiers in Molecular Neuroscience,
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Huma, Z-E., Javed, I., Zhang, Z., Bilal, H., Sun, Y., Hussain, S. Z., Davis, T. P.
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Nanosilver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition.
Small (Weinheim an der Bergstrasse, Germany),
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Alijanvand, S. H., Christensen, M. H., Christiansen, G., Harikandei, K. B., Salehi, P.
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Novel noscapine derivatives stabilize the native state of insulin against fibrillation.
International Journal of Biological Macromolecules,
147, 98-108. Advance online publication.
https://doi.org/10.1016/j.ijbiomac.2020.01.061
Jakob, D. S., Wang, H., Zeng, G.
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Peak Force Infrared - Kelvin Probe Force Microscopy.
Angewandte Chemie International Edition,
59(37), 16083-16090. Advance online publication.
https://doi.org/10.1002/anie.202004211
He, J., Becares, E. R., Thulstrup, P. W., Gamon, L. F.
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Peroxynitrous acid (ONOOH) modifies the structure of anastellin and influences its capacity to polymerize fibronectin.
Redox Biology,
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Phenol-Soluble Modulins Modulate Persister Cell Formation in Staphylococcus aureus.
Frontiers in Microbiology,
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Predicted Loop Regions Promote Aggregation: A Study of Amyloidogenic Domains in the Functional Amyloid FapC.
Journal of Molecular Biology,
432(7), 2232-2252. Advance online publication.
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.
The Journal of biological chemistry,
295(37), 13031–13046. Advance online publication.
https://doi.org/10.1074/jbc.RA120.013396
Krainer, G., Hartmann, A., Bogatyr, V.
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SDS-induced multi-stage unfolding of a small globular protein through different denatured states revealed by single-molecule fluorescence.
Chemical Science,
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Juul-Madsen, K., Qvist, P., Bendtsen, K. L., Langkilde, A. E., Vestergaard, B.
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Size-Selective Phagocytic Clearance of Fibrillar α-Synuclein through Conformational Activation of Complement Receptor 4.
Journal of Immunology,
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The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth.
PLOS Computational Biology,
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The interactome of stabilized α-synuclein oligomers and neuronal proteins.
The FEBS Journal,
287(10), 2037-2054. Advance online publication.
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. Advance online publication.
https://doi.org/10.1016/j.ijbiomac.2020.03.238
Nissen, S. K., Shrivastava, K., Schulte, C.
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Alterations in Blood Monocyte Functions in Parkinson's Disease.
Movement Disorders,
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https://doi.org/10.1002/mds.27815
Mohammad-Beigi, H., Kjær, L., Eskandari, H., Aliakbari, F., Christiansen, G., Ruvo, G., L. Ward, J.
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A Possible Connection Between Plant Longevity and the Absence of Protein Fibrillation: Basis for Identifying Aggregation Inhibitors in Plants.
Frontiers in Plant Science,
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Najarzadeh, Z., Pedersen, J. N., Christiansen, G., Shojaosadati, S. A.
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Bacterial amphiphiles as amyloid inducers: Effect of Rhamnolipid and Lipopolysaccharide on FapC fibrillation.
B B A - Proteins and Proteomics,
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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.),
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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,
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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Physical Determinants of Amyloid Assembly in Biofilm Formation.
mBio,
10(1), Article e02279-18.
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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