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.
, Otzen, D. E. & Nielsen, P. H. (2016).
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.
Biochimica et Biophysica Acta - 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,
10(1), 25-29.
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.
, Otzen, D. E., Sanggaard, K. W. & Enghild, J. J. (2016).
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 (PNAS),
113(32), E4708-E4715.
https://doi.org/10.1073/pnas.1601091113Agerschou, E. D., Christiansen, G., Schafer, N. P., Madsen, D. J., Brodersen, D. E., Semsey, S.
& Otzen, D. E. (2016).
The transcriptional regulator GalR self-assembles to form highly regular tubular structures.
Scientific Reports,
6, Article 27672.
https://doi.org/10.1038/srep27672
Schafer, N., Truong, H. H.
, Otzen, D., Lindorff-Larsen, K. & Wolynes, P. G. (2016).
Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease.
Proceedings of the National Academy of Sciences (PNAS),
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.
, Otzen, D., Oddershede, L. B. & Jensen, M. H. (2015).
A monomer-trimer model supports intermittent glucagon fibril growth.
Scientific Reports,
5, 1-6. Article 9005.
https://doi.org/10.1038/srep09005Paslawski, W., Lillelund, O. K., Kristensen, J. V.
, Schafer, N. P., Baker, R. P., Urban, S.
& Otzen, D. E. (2015).
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 (PNAS),
112(6), 7978-7983.
https://doi.org/10.1073/pnas.1424751112
Seviour, T., Hansen, S. H., Yang, L., Yau, Y. H., Wang, V. B.
, Stenvang, M. R., Christiansen, G., Marsili, E., Givskov, M., Chen, Y.
, Otzen, D., Nielsen, P. H., Shochat, S. G., Kjelleberg, S. & Dueholm, M. S. (2015).
Functional Amyloids Keep Quorum Sensing Molecules in Check.
Journal of Biological Chemistry,
290, 6457-6469.
https://doi.org/10.1074/jbc.M114.613810Zeng, 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.
, Kaspersen, J. D., Silow, M. B., Vind, J.
, Pedersen, J. S., Svendsen, A.
& Otzen, D. E. (2015).
Promoting protein self-association in non-glycosylated Thermomyces lanuginosus lipase based on crystal lattice contacts.
Biochimica et Biophysica Acta - 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.
Biochimica et Biophysica Acta - Proteins and Proteomics,
1854(12), 1890-1897.
https://doi.org/10.1016/j.bbapap.2015.08.005Mohammad-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/ja5093634Estrela, N., Franquelim, H. G., Lopes, C., Tavares, E., Macedo, J. A.
, Christiansen, G., Otzen, D. E. & Melo, E. P. (2015).
Sucrose prevents protein fibrillation through compaction of the tertiary structure but hardly affects the secondary structure.
Proteins: Structure, Function, and Bioinformatics,
83(11), 2039-2051.
https://doi.org/10.1002/prot.24921Madsen, J., Pihl, R., Møller, A. H., Tranberg Madsen, A., Otzen, D. & Andersen, K. K. (2015).
The anionic biosurfactant rhamnolipid does not denature industrial enzymes.
Frontiers in Microbiology,
6, Article 292.
https://doi.org/10.3389/fmicb.2015.00292
Michaels, T. C. T., Yde, P., Willis, J. C. W., Jensen, M. H.
, Otzen, D., Dobson, C. M., Buell, A. K. & Knowles, T. P. J. (2015).
The length distribution of frangible biofilaments.
Journal of Chemical Physics,
143(16), 1-15. Article 164901.
https://doi.org/10.1063/1.4933230Frahm, H., Hansen, S. K., Vad, B. S., Nielsen, E. H., Nielsen, J. T., Vosegaard, T., Skrydstrup, T. & Otzen, D. E. (2015).
The natural, peptaibolic peptide SPF-5506-A4 adopts a β-bend spiral structure, shows low hemolytic activity and targets membranes through formation of large pores.
Biochimica et Biophysica Acta - Proteins and Proteomics,
1854(8), 882-889.
https://doi.org/10.1016/j.bbapap.2015.03.003
Dueholm, M. S., Larsen, P.
, Finster, K., Stenvang, M. R., Christiansen, G., Vad, B. S., Bøggild, A., Otzen, D. E. & Halkjær Nielsen, P. (2015).
The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids.
Journal of Biological Chemistry,
290, 20590-26600.
https://doi.org/10.1074/jbc.M115.654780
Skals, M., Bjaelde, R. G., Reinholdt, J., Poulsen, K., Vad, B. S., Otzen, D., Leipziger, J. & Praetorius, H. A. (2014).
Bacterial RTX Toxins Allow Acute ATP Release from Human Erythrocytes Directly through the Toxin Pore.
Journal of Biological Chemistry,
289, 19098-19109.
https://doi.org/10.1074/jbc.M114.571414
Paslawski, W., Mysling, S.
, Thomsen, K., Jørgensen, T. J. D.
& Otzen, D. (2014).
Co-existence of Two Different α-Synuclein Oligomers with Different Core Structures Determined by Hydrogen/Deuterium Exchange Mass Spectrometry.
Angewandte Chemie International Edition,
53(29), 7560-7563.
https://doi.org/10.1002/anie.201400491
Poulsen, E. T., Runager, K., Risør, M. W., Dyrlund, T. F., Scavenius, C., Karring, H., Praetorius, J., Vorum, H., Otzen, D. E., Klintworth, G. K.
& Enghild, J. J. (2014).
Comparison of two phenotypically distinct lattice corneal dystrophies caused by mutations in the transforming growth factor beta induced (TGFBI) gene.
Proteomics - Clinical Applications,
8(3-4), 168-177.
https://doi.org/10.1002/prca.201300058
Knudsen, A. D., Bennike, T., Kjeldal, H.
, Birkelund, S., Otzen, D. & Stensballe, A. (2014).
Condenser: A statistical aggregation tool for multi-sample quantitative proteomic data from Matrix Science Mascot Distiller™.
Journal of Proteomics,
103, 261-266.
https://doi.org/10.1016/j.jprot.2014.02.001
Lopes, P., Dyrnesli, H.
, Lorenzen, N., Otzen, D. & Ferapontova, E. (2014).
Electrochemical Analysis of the Fibrillation of Parkinson's Disease α-synuclein.
Analyst,
139(4), 749-756.
https://doi.org/10.1039/C3AN01616A
Kaspersen, J. D., Pedersen, J. N., Hansted, J. G., Nielsen, S. B., Sakthivel, S., Wilhelm, K., Nemashkalova, E. L., Permyakov, S. E., Permyakov, E. A., Pinto Oliveira, C. L., Morozova-Roche, L. A.
, Otzen, D. & Pedersen, J. S. (2014).
Generic Structures of Cytotoxic Liprotides: Nano-Sized Complexes with Oleic Acid Cores and Shells of Disordered Proteins.
ChemBioChem,
10(18), 2693-2702.
https://doi.org/10.1002/cbic.201402407
Paslawski, W., Andreasen, M., Nielsen, S. B., Lorenzen, N., Thomsen, K., Kaspersen, J. D., Pedersen, J. S. & Otzen, D. (2014).
High stability and cooperative unfolding of cytotoxic α-synuclein oligomers.
Biochemistry,
53(39), 6252-6263.
https://doi.org/10.1021/bi5007833
Lorenzen, N., Nielsen, S. B., Yoshimura, Y., Vad, B. S., Andersen, C. B., Betzer, C., Kaspersen, J. D., Christiansen, G., Pedersen, J. S., Jensen, P. H., Mulder, F. A. A. & Otzen, D. E. (2014).
How epigallocatechin gallate can inhibit α-synuclein oligomer toxicity in vitro.
Journal of Biological Chemistry,
289(31), 21299-21310.
https://doi.org/10.1074/jbc.M114.554667
