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, [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, [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, [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, [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, [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
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
Chu, B. C. H., Otten, R., Krewulak, K. D.
, Mulder, F. A. A. & Vogel, H. J. (2014).
The Solution Structure, Binding Properties, and Dynamics of the Bacterial Siderophore-binding Protein FepB.
Journal of Biological Chemistry,
289(42), 29219-29234.
https://doi.org/10.1074/jbc.M114.564021
Pool, T. J., Oktaviani, N. A., Kamikubo, H., Kataoka, M.
& Mulder, F. A. A. (2013).
1H, 13C, and 15N resonance assignment of photoactive yellow protein.
Biomolecular N M R Assignments,
7(1), 97-100.
https://doi.org/10.1007/s12104-012-9387-9
Avanti, C., Oktaviani, N. A., Hinrichs, W. L. J., Frijlink, H. W.
& Mulder, F. A. A. (2013).
Aspartate buffer and divalent metal ions affect oxytocin in aqueous solution and protect it from degradation.
International Journal of Pharmaceutics,
444(1-2), 139-145.
https://doi.org/10.1016/j.ijpharm.2013.01.051
Roodbeen, R., Paaske, B., Jiang, L.
, Jensen, J. K., Christensen, A., Nielsen, J. T., Huang, M.
, Mulder, F. A. A., Nielsen, N. C., Andreasen, P. & Jensen, K. J. (2013).
Bicyclic Peptide Inhibitor of Urokinase-Type Plasminogen Activator: Mode of Action.
ChemBioChem,
14(16), 2179–2188.
https://doi.org/10.1002/cbic.201300335