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.
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
Kaspersen, J. D., Søndergaard, A., Madsen, D. J., Otzen, D. E. & Pedersen, J. S. (2017).
Refolding of SDS-Unfolded Proteins by Nonionic Surfactants.
Biophysical Journal,
112(8), 1609-1620.
https://doi.org/10.1016/j.bpj.2017.03.013
Otzen, D. E., Vad, B. S., Dueholm, M. S., Nielsen, P. H., Rouse, S. L. & Matthews, S. J. (2017).
Self-organizing amyloid in bacteria.
European Biophysics Journal,
46, S98-S98.
Otzen, D. E., Vad, B. S., Dueholm, M. S., Nielsen, P. H., Rouse, S. L. & Matthews, S. J. (2017).
Self-organizing amyloid in bacteria.
European Biophysics Journal,
46(supp 1), S341-S341.
https://doi.org/10.1007/s00249-017-1222-x
Malmos, K. G., Stenvang, M., Sahin, C., Christiansen, G. & Otzen, D. E. (2017).
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.
https://doi.org/10.1016/j.jmb.2017.07.014
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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.
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.
& Otzen, D. (2017).
ThT 101: a primer on the use of thioflavin T to investigate amyloid formation.
Amyloid: the Journal of Protein Folding Disorders,
24(1), 1-16.
https://doi.org/10.1080/13506129.2017.1304905
Pantusa, M.
, Vad, B., Lillelund, O., Kjær, L., Otzen, D. & Bartucci, R. (2016).
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.
https://doi.org/10.1016/j.bbapap.2016.05.003
Tian, P., Lindorff-Larsen, K., Boomsma, W., Jensen, M. H.
& Otzen, D. E. (2016).
A Monte Carlo Study of the Early Steps of Functional Amyloid Formation.
PLOS ONE,
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https://doi.org/10.1371/journal.pone.0146096
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, Otzen, D. E., Lee, J., Delos Santos, M. M. S., Yam, J. K. H., Kang, N.-Y., Park, S.-J., Kwon, H., Seviour, T. W., Yang, L., Givskov, M. & Chang, Y.-T. (2016).
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,
11(1), 15-32.
https://doi.org/10.2217/fnl.16.3
Stenvang, M., Dueholm, M. S.
, Vad, B. S., Seviour, T. W., Zeng, G., Geifman-Shochat, S., Søndergaard, M. T.
, 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.
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
Frislev, H. K. S., Jessen, C. M., Oliveira, C. L. P., Pedersen, J. S. & Otzen, D. E. (2016).
Liprotides made of α-lactalbumin and cis fatty acids form core-shell and multi-layer structures with a common membrane-targeting mechanism.
B B A - Proteins and Proteomics,
1864(7), 847-859.
https://doi.org/10.1016/j.bbapap.2016.04.003
Kulminskaya, N. V., Yoshimura, Y., Runager, K., Sørensen, C. S., Bjerring, M., Andreasen, M., Otzen, D. E., Enghild, J. J., Nielsen, N. C. & Mulder, F. A. A. (2016).
Near-complete 1H, 13C, 15N resonance assignments of dimethylsulfoxide-denatured TGFBIp FAS1-4 A546T.
Biomolecular N M R Assignments,
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https://doi.org/10.1007/s12104-015-9630-2
Hjorth, C. F., Norrman, M., Wahlund, P.-O., Benie, A. J., Petersen, B. O.
, Jessen, C. M., Pedersen, T. Å., Vestergaard, K., Steensgaard, D. B.
, Pedersen, J. S., Naver, H., Hubálek, F., Poulsen, C.
& Otzen, D. (2016).
Structure, Aggregation, and Activity of a Covalent Insulin Dimer Formed During Storage of Neutral Formulation of Human Insulin.
Journal of Pharmaceutical Sciences,
105(4), 1376-1386.
https://doi.org/10.1016/j.xphs.2016.01.003
Scavenius, C., Nikolajsen, C. L., Stenvang, M., Thøgersen, I., Wyrozemski, L., Wisniewski, H.-G.
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The compact and biologically relevant structure of inter-α-inhibitor is maintained by the chondroitin sulfate chain and divalent cations.
Journal of Biological Chemistry,
291(9), 4658-4670.
https://doi.org/10.1074/jbc.M115.678748
Jarvela, T. S., Lam, H. A., Helwig, M.
, Lorenzen, N., Otzen, D. E., McLean, P. J., Maidment, N. T. & Lindberg, I. (2016).
The neural chaperone proSAAS blocks α-synuclein fibrillation and neurotoxicity.
Proceedings of the National Academy of Sciences,
113(32), E4708-E4715.
https://doi.org/10.1073/pnas.1601091113
Agerschou, E. D., Christiansen, G., Schafer, N. P., Madsen, D. J., Brodersen, D. E., Semsey, S.
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The transcriptional regulator GalR self-assembles to form highly regular tubular structures.
Scientific Reports,
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https://doi.org/10.1038/srep27672
Schafer, N., Truong, H. H.
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Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease.
Proceedings of the National Academy of Sciences,
113(8), 2098-2103.
https://doi.org/10.1073/pnas.1524027113
Andersen, K. K., Vad, B. S., Roelants, S., van Bogaert, I. N. A.
& Otzen, D. E. (2016).
Weak and Saturable Protein-Surfactant Interactions in the Denaturation of Apo-α-Lactalbumin by Acidic and Lactonic Sophorolipid.
Frontiers in Microbiology,
7(NOV), Article 1711.
https://doi.org/10.3389/fmicb.2016.01711
Madsen, J. K., Kaspersen, J. D., Andersen, K. K., Pedersen, J. S. & Otzen, D. E. (2016).
When Enzymes and Green Surfactants Meet.
Biophysical Journal,
110(3), 211A.
https://doi.org/10.1016/j.bpj.2015.11.1171
Christiansen, J. R., Olesen, M. N., Otzen, D. E., Romero-Ramos, M. & Sanchez-Guajardo, V. (2016).
α-Synuclein vaccination modulates regulatory T cell activation and microglia in the absence of brain pathology.
Journal of Neuroinflammation,
13(1), Article 74.
https://doi.org/10.1186/s12974-016-0532-8
Košmrlj, A., Cordsen, P., Kyrsting, A.
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A monomer-trimer model supports intermittent glucagon fibril growth.
Scientific Reports,
5, 1-6. Article 9005.
https://doi.org/10.1038/srep09005
Paslawski, W., Lillelund, O. K., Kristensen, J. V.
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Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops.
Proceedings of the National Academy of Sciences,
112(6), 7978-7983.
https://doi.org/10.1073/pnas.1424751112
Seviour, T., Hansen, S. H., Yang, L., Yau, Y. H., Wang, V. B.
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Functional Amyloids Keep Quorum Sensing Molecules in Check.
Journal of Biological Chemistry,
290, 6457-6469.
https://doi.org/10.1074/jbc.M114.613810
Zeng, G., Vad, B. S., Dueholm, M. S., Christiansen, G., Nilsson, M., Tolker-Nielsen, T., Nielsen, P. H.
, Meyer, R. L. & Otzen, D. E. (2015).
Functional bacterial amyloid increases Pseudomonas biofilm hydrophobicity and stiffness.
Frontiers in Microbiology,
6, 1099.
https://doi.org/10.3389/fmicb.2015.01099
Madsen, J., Sørensen, T. R.
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& Otzen, D. E. (2015).
Promoting protein self-association in non-glycosylated Thermomyces lanuginosus lipase based on crystal lattice contacts.
BBA Proteins and Proteomics,
154(12), 1914-1921.
https://doi.org/10.1016/j.bbapap.2015.09.007
Hjorth, C. F., Hubálek, F., Andersson, J., Poulsen, C.
, Otzen, D. & Naver, H. (2015).
Purification and Identification of High Molecular Weight Products Formed During Storage of Neutral Formulation of Human Insulin.
Pharmaceutical Research,
32(6), 2072-2085.
https://doi.org/10.1007/s11095-014-1600-3
Christoffersen, H. F.
, Andreasen, M., Zhang, S., Nielsen, E. H., Christiansen, G., Dong, M., Skrydstrup, T. & Otzen, D. E. (2015).
Scaffolded multimers of hIAPP20-29 peptide fragments fibrillate faster and lead to different fibrils compared to the free hIAPP20-29 peptide fragment.
B B A - Proteins and Proteomics,
1854(12), 1890-1897.
https://doi.org/10.1016/j.bbapap.2015.08.005
Mohammad-Beigi, H., Shojaosadati, S. A., Marvian, A. T.
, Pedersen, J. N., Klausen, L. H., Christiansen, G., Pedersen, J. S., Dong, M., Morshedi, D.
& Otzen, D. E. (2015).
Strong interactions with polyethylenimine-coated human serum albumin nanoparticles (PEI-HSA NPs) alter α-synuclein conformation and aggregation kinetics.
Nanoscale,
7, 19627-19640.
https://doi.org/10.1039/c5nr05663b
Tian, P., Boomsma, W., Wang, Y.
, Otzen, D., Jensen, M. H. & Lindorff-Larsen, K. (2015).
Structure of a Functional Amyloid Protein Subunit Computed Using Sequence Variation.
Journal of the American Chemical Society,
137(1), 22-25.
https://doi.org/10.1021/ja5093634