Olsen, W. P., Courtade, G.
, Peña-Díaz, S., Nagaraj, M., Sønderby, T. V., Mulder, F. A. A., Malle, M. G. & Otzen, D. E. (2024).
CsgA gatekeeper residues control nucleation but not stability of functional amyloid.
Protein Science,
33(10), Article e5178.
https://doi.org/10.1002/pro.5178
Andersen, C. B., Lausdahl, A. K.
, Nielsen, J., Clausen, M. P.
, Mulder, F. A. A., Otzen, D. E. & Arnspang, E. C. (2023).
4-Oxo-2-nonenal-Induced α-Synuclein Oligomers Interact with Membranes in the Cell, Leading to Mitochondrial Fragmentation.
Biochemistry,
62(16), 2417-2425.
https://doi.org/10.1021/acs.biochem.3c00114
Laursen, K. R., Christensen, N. V., Mulder, F. A., Schullehner, J., Hoffmann, H. J., Jensen, A., Møller, P., Loft, S., Olin, A.-C.
, Rasmussen, B. B., Rosati, B., Strandberg, B.
, Glasius, M., Bilde, M., Sigsgaard, T. & Climate Chamber Group (2023).
Airway and systemic biomarkers of health effects after short-term exposure to indoor ultrafine particles from cooking and candles: A randomized controlled double-blind crossover study among mild asthmatic subjects.
Particle and Fibre Toxicology,
20(1), Article 26.
https://doi.org/10.1186/s12989-023-00537-7
Møller, K. V., Nguyen, H. T. T.
, Mørch, M. G. M., Hesselager, M. O., Mulder, F. A. A., Fuursted, K. & Olsen, A. (2022).
A Lactobacilli diet that confers MRSA resistance causes amino acid depletion and increased antioxidant levels in the C. elegans host.
Frontiers in Microbiology,
13, Article 886206.
https://doi.org/10.3389/fmicb.2022.886206
Stødkilde, K., Nielsen, J. T., Petersen, S. V., Paetzold, B.
, Brüggemann, H., Mulder, F. A. A. & Andersen, C. B. F. (2022).
Solution Structure of the Cutibacterium acnes-Specific Protein RoxP and Insights Into Its Antioxidant Activity.
Frontiers in cellular and infection microbiology,
12, Article 803004.
https://doi.org/10.3389/fcimb.2022.803004
Hansen, A. R. E., Enemark-Rasmussen, K.
, Mulder, F. A. A., Jensen, P. R. & Meier, S. (2022).
Versatile Procedures for Reliable NMR Quantification of CO2 Electroreduction Products.
Journal of Physical Chemistry C,
126(27), 11026-11032.
https://doi.org/10.1021/acs.jpcc.2c03448
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, Article 100788.
https://doi.org/10.1016/j.jbc.2021.100788
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
Guo, X., Sarup, P. M., Jensen, J. D., Jihad, O., Kristensen, N. H.
, Mulder, F. A. A., Jahoor, A.
& Jensen, J. (2020).
Genetic Variance of Metabolomic Features and Their Relationship With Malting Quality Traits in Spring Barley.
Frontiers in Plant Science,
11, Article 575467.
https://doi.org/10.3389/fpls.2020.575467
Hansen, B. K., Larsen, C. K., Nielsen, J. T., Svenningsen, E. B., Van, L. B., Jacobsen, K. M., Bjerring, M., Flygaard, R. K., Jenner, L. B.
, Nejsum, L. N., Brodersen, D. E., Mulder, F. A. A., Tørring, T. & Poulsen, T. B. (2020).
Structure and Function of the Bacterial Protein Toxin Phenomycin.
Structure,
28(5), 528-539.e9.
https://doi.org/10.1016/j.str.2020.03.003
Xue, M., Wakamoto, T.
, Kejlberg, C., Yoshimura, Y., Nielsen, T. A., Risør, M. W., Sanggaard, K. W., Kitahara, R.
& Mulder, F. A. A. (2019).
How internal cavities destabilize a protein.
Proceedings of the National Academy of Sciences,
116(42), 21031-21036.
https://doi.org/10.1073/pnas.1911181116
Kitahara, R., Sakuraba, S., Kameda, T., Okuda, S.
, Xue, M. & Mulder, F. A. A. (2018).
Nuclear magnetic resonance-based determination of dioxygen binding sites in protein cavities.
Protein Science,
27(3), 769-779.
https://doi.org/10.1002/pro.3371
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.
, Mulder, F. A. A., Mente, S., Hirst, W. D.
& 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.
https://doi.org/10.1016/j.chembiol.2018.08.005
Oktaviani, N. A., Pool, T. J.
, Yoshimura, Y., Kamikubo, H., Scheek, R. M., Kataoka, M.
& Mulder, F. A. A. (2017).
Active-Site pKa Determination for Photoactive Yellow Protein Rationalizes Slow Ground-State Recovery.
Biophysical Journal,
112(10), 2109-2116.
https://doi.org/10.1016/j.bpj.2017.04.008
Yoshimura, Y., Holmberg, M., Kukic, P.
, Andersen, C. B., Mata-Cabana, A., Falsone, S. F., Vendruscolo, M., Nollen, E. A. A.
& Mulder, F. (2017).
MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions.
Journal of Biological Chemistry,
292(20), 8269-8278.
https://doi.org/10.1074/jbc.M116.764886
Yoshimura, Y., Oktaviani, N. A., Yonezawa, K., Kamikubo, H.
& Mulder, F. A. A. (2017).
Unambiguous Determination of Protein Arginine Ionization States in Solution by NMR Spectroscopy.
Angewandte Chemie International Edition,
56(1), 239–242.
https://doi.org/10.1002/anie.201609605
Kitahara, R.
, Yoshimura, Y., Xue, M., Kameda, T.
& Mulder, F. A. A. (2016).
Detecting O2 binding sites in protein cavities.
Scientific Reports,
6, Article 20534.
https://doi.org/10.1038/srep20534
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
Maeno, A., Sindhikara, D., Hirata, F., Otten, R., Dahlquist, F. W., Yokoyama, S., Akasaka, K.
, Mulder, F. A. A. & Kitahara, R. (2015).
Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Biophysical Journal,
108(1), 133-45.
https://doi.org/10.1016/j.bpj.2014.11.012
Oktaviani, N. A.
, Risør, M. W., Lee, Y.-H., Megens, R. P., de Jong, D. H., Otten, R., Scheek, R. M.
, Enghild, J. J., Nielsen, N. C., Ikegami, T.
& Mulder, F. A. A. (2015).
Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide.
Journal of Biomolecular N M R,
62(2), 129-142.
https://doi.org/10.1007/s10858-015-9925-8
Olesen, H. G., Mohr, D., Seweryn, P., Yoshimura, Y., Kutlubaeva, Z.
, Dolman, F., Chelchessa, B., Chetverin, A. B.
, Mulder, F. A. A., Brodersen, D. E. & Knudsen, C. R. (2015).
Structural basis for RNA-genome recognition during bacteriophage Qβ replication.
Nucleic Acids Research,
43(22), 10893-10906.
https://doi.org/10.1093/nar/gkv1212
Hong, Z., Nowakowski, M., Spronk, C.
, Petersen, S. V., Andreasen, P., Koźmiński, W.
, Mulder, F. & Jensen, J. K. (2015).
The solution structure of the MANEC-type domain from Hepatocyte Growth Factor Activator Inhibitor 1 reveals an unexpected PAN/apple domain-type fold.
Biochemical Journal,
466(2), 299-309.
https://doi.org/10.1042/BJ20141236
O'Malley, T. T., Oktaviani, N. A., Zhang, D., Lomakin, A., O'Nuallain, B., Linse, S., Benedek, G. B., Rowan, M. J.
, Mulder, F. A. A. & Walsh, D. M. (2014).
Aβ dimers differ from monomers in structural propensity, aggregation paths and population of synaptotoxic assemblies.
Biochemical Journal,
461(3), 413-426.
https://doi.org/10.1042/BJ20140219