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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
Højgaard, C.
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Can a Charged Surfactant Unfold an Uncharged Protein? Biophysical Journal,
115(11), 2081-2086. Advance online publication.
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. Advance online publication.
https://doi.org/10.1016/j.jmb.2018.03.001
Tiwari, M. K., Leinisch, F.
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& Bjerrum, M. J. (2018).
Early events in copper-ion catalyzed oxidation of α-synuclein.
Free Radical Biology & Medicine,
121, 38-50. Advance online publication.
https://doi.org/10.1016/j.freeradbiomed.2018.04.559
Aliakbari, F., Shabani, A. A., Bardania, H.
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, 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. Advance online publication.
https://doi.org/10.1016/j.colsurfb.2017.11.023
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.
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& 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. Advance online publication.
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.
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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. Advance online publication.
https://doi.org/10.1002/1873-3468.13038
Nedergaard Pedersen, J., Wilhelmus Johannes Maria Frederix, P.
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& Otzen, D. (2018).
Role of charge and hydrophobicity in liprotide formation: a molecular dynamics study with experimental constraints.
ChemBioChem,
19(3), 263–271. Advance online publication.
https://doi.org/10.1002/cbic.201700496
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.
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The potential of zwitterionic nanoliposomes against neurotoxic alpha-synuclein aggregates in Parkinson's Disease.
Nanoscale,
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https://doi.org/10.1039/c8nr00632f
Christensen, L. F. B., Hansen, L. M.
, Finster, K., Christiansen, G., Nielsen, P. H.
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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,
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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,
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Sahin, C., Lorenzen, N., Lemminger, L., Christiansen, G., Møller, I. M., Vesterager, L. B., Pedersen, L. Ø., Fog, K., Kallunki, P.
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Antibodies against the C-terminus of α-synuclein modulate its fibrillation.
Biophysical Chemistry,
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https://doi.org/10.1016/j.bpc.2016.11.002
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
Risør, M. W., Juhl, D. W., Bjerring, M., Mathiesen, J.
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Critical Influence of Cosolutes and Surfaces on the Assembly of Serpin-Derived Amyloid Fibrils.
Biophysical Journal,
113(3), 580-596.
https://doi.org/10.1016/j.bpj.2017.06.030
Madsen, J. K., Kaspersen, J. D., Andersen, C. B., Nedergaard Pedersen, J., Andersen, K. K., Pedersen, J. S. & Otzen, D. E. (2017).
Glycolipid Biosurfactants Activate, Dimerize, and Stabilize Thermomyces lanuginosus Lipase in a pH-Dependent Fashion.
Biochemistry,
56(32), 4256-4268.
https://doi.org/10.1021/acs.biochem.7b00420
Andersen, K. K., Vad, B. S., Scavenius, C., Enghild, J. J. & Otzen, D. E. (2017).
Human lysozyme peptidase resistance is perturbed by the anionic glycolipid biosurfactant rhamnolipid produced by the opportunistic pathogen Pseudomonas aeruginosa.
Biochemistry,
56(1), 260–270. Advance online publication.
https://doi.org/10.1021/acs.biochem.6b01009
Mortensen, H. G., Madsen, J. K., Andersen, K. K., Vosegaard, T., Deen, G. R.
, Otzen, D. E. & Pedersen, J. S. (2017).
Myoglobin and α-Lactalbumin Form Smaller Complexes with the Biosurfactant Rhamnolipid Than with SDS.
Biophysical Journal,
113(12), 2621-2633.
https://doi.org/10.1016/j.bpj.2017.10.024
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Refolding of SDS-Unfolded Proteins by Nonionic Surfactants.
Biophysical Journal,
112(8), 1609-1620.
https://doi.org/10.1016/j.bpj.2017.03.013
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Self-organizing amyloid in bacteria.
European Biophysics Journal,
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Self-organizing amyloid in bacteria.
European Biophysics Journal,
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The Changing Face of Aging: Highly Sulfated Glycosaminoglycans Induce Amyloid Formation in a Lattice Corneal Dystrophy Model Protein.
Journal of Molecular Biology,
429(18), 2755-2764. Advance online publication.
https://doi.org/10.1016/j.jmb.2017.07.014
Christiansen, S. H., Zhang, X., Juul-Madsen, K., Hvam, M. L., Vad, B. S., Behrens, M. A., Thygesen, I. L., Jalilian, B., Pedersen, J. S., Howard, K., Otzen, D. E. & Vorup-Jensen, T. (2017).
The random co-polymer glatiramer acetate rapidly kills primary human leukocytes through sialic-acid-dependent cell membrane damage.
B B A - Biomembranes,
1859(3), 425-437. Advance online publication.
https://doi.org/10.1016/j.bbamem.2017.01.001
Malmos, K., Blancas-Mejia, L. M., Weber, B., Buchner, J., Ramirez-Alvarado, M., Naiki, H.
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ThT 101: a primer on the use of thioflavin T to investigate amyloid formation.
Amyloid: the Journal of Protein Folding Disorders,
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Alpha-synuclein and familial variants affect the chain order and the thermotropic phase behavior of anionic lipid vesicles.
B B A - Proteins and Proteomics,
1864(9), 1206-1214. Advance online publication.
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A Monte Carlo Study of the Early Steps of Functional Amyloid Formation.
PLOS ONE,
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Detection of pathogenic biofilms with bacterial amyloid targeting fluorescent probe, CDy11.
Journal of the American Chemical Society,
138(1), 402-407.
https://doi.org/10.1021/jacs.5b11357
Jordal, P. L.
, Dyrlund, T. F., Winge, K.
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Detection of proteolytic signatures for Parkinson's disease.
Future Neurology,
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, Christiansen, G., Meyer, R. L., Kjelleberg, S.
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Epigallocatechin Gallate Remodels overexpressed Functional Amyloids in Pseudomonas aeruginosa and Increases Biofilm Susceptibility to Antibiotic Treatment.
Journal of Biological Chemistry,
291(51), 26540-26553. Advance online publication.
https://doi.org/10.1074/jbc.M116.739953
Mohammad-Beigi, H., Morshedi, D., Shojaosadati, S. A.
, Pedersen, J. N., Marvian, A. T., Aliakbari, F.
, Christiansen, G., Pedersen, J. S. & Otzen, D. E. (2016).
Gallic acid loaded onto polyethylenimine-coated human serum albumin nanoparticles (PEI-HSA-GA NPs) stabilizes α-synuclein in the unfolded conformation and inhibits aggregation.
RSC Advances,
6(88), 85312-85323.
https://doi.org/10.1039/c6ra08502d
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. (2016).
How Glycosaminoglycans Promote Fibrillation of Salmon Calcitonin.
Journal of Biological Chemistry,
291(32), 16849-16862.
https://doi.org/10.1074/jbc.M116.715466
Madsen, J. L. H., Hjørringgaard, C. U., Vad, B. S., Otzen, D. & Skrydstrup, T. (2016).
Incorporation of β-Silicon-β3-Amino Acids in the Antimicrobial Peptide Alamethicin Provides a 20-Fold Increase in Membrane Permeabilization.
Chemistry: A European Journal,
22(24), 8358-8367.
https://doi.org/10.1002/chem.201600445