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
van Tilborg, P. J.
, Mulder, F. A. A., de Backer, M. M., Nair, M., van Heerde, E. C., Folkers, G., van der Saag, P. T., Karimi-Nejad, Y., Boelens, R. & Kaptein, R. (1999).
Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation.
Biochemistry,
38(7), 1951-1956.
https://doi.org/10.1021/bi982526q
Mulder, F. A. A., Skrynnikov, N. R., Hon, B., Dahlquist, F. W. & Kay, L. E. (2001).
Measurement of slow (μs-ms) time scale dynamics in protein side chains by 15N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
Journal of the American Chemical Society,
123(5), 967-975.
https://doi.org/10.1021/ja003447g
Meinema, A. C., Laba, J. K., Hapsari, R. A., Otten, R.
, Mulder, F. A. A., Kralt, A., van den Bogaart, G., Lusk, C. P., Poolman, B. & Veenhoff, L. M. (2011).
Long unfolded linkers facilitate membrane protein import through the nuclear pore complex.
Science,
333(6038), 90-3.
https://doi.org/10.1126/science.1205741
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
Ayed, A.
, Mulder, F. A., Yi, G. S., Lu, Y., Kay, L. E. & Arrowsmith, C. H. (2001).
Latent and active p53 are identical in conformation.
Nature Structural and Molecular Biology,
8(9), 756-760.
https://doi.org/10.1038/nsb0901-756
Mulder, F. A. A., Spronk, C. A. E. M., Slijper, M., Kaptein, R. & Boelens, R. (1996).
Improved HSQC experiments for the observation of exchange broadened signals.
Journal of Biomolecular N M R,
8(2), 223-228.
https://doi.org/10.1007/BF00211169
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
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
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
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
Brath, U., Akke, M., Yang, D., Kay, L. E.
& Mulder, F. A. A. (2006).
Functional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy.
Journal of the American Chemical Society,
128(17), 5718-5727.
https://doi.org/10.1021/ja0570279
Mulder, F. A. A., Hon, B., Muhandiram, D. R., Dahlquist, F. W. & Kay, L. E. (2000).
Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR.
Biochemistry,
39(41), 12614-12622.
https://doi.org/10.1021/bi001351t
Choy, W. Y.
, Mulder, F. A. A., Crowhurst, K. A., Muhandiram, D. R., Millett, I. S., Doniach, S., Forman-Kay, J. D. & Kay, L. E. (2002).
Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques.
Journal of Molecular Biology,
316(1), 101-112.
https://doi.org/10.1006/jmbi.2001.5328
Hansen, D. F., Neudecker, P., Vallurupalli, P.
, Mulder, F. A. A. & Kay, L. E. (2010).
Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion.
Journal of the American Chemical Society,
132(1), 42-43.
https://doi.org/10.1021/ja909294n
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
Karasawa, A., Erkens, G. B., Berntsson, R. P.-A., Otten, R., Schuurman-Wolters, G. K.
, Mulder, F. A. A. & Poolman, B. (2011).
Cystathionine β-synthase (CBS) domains 1 and 2 fulfill different roles in ionic strength sensing of the ATP-binding cassette (ABC) transporter OpuA.
Journal of Biological Chemistry,
286(43), 37280-91.
https://doi.org/10.1074/jbc.M111.284059
Mulder, F. A. A., Bouakaz, L., Lundell, A., Venkataramana, M., Liljas, A., Akke, M. & Sanyal, S. (2004).
Conformation and dynamics of ribosomal stalk protein L12 in solution and on the ribosome.
Biochemistry,
43(20), 5930-5936.
https://doi.org/10.1021/bi0495331
Oktaviani, N. A., Pool, T. J., Kamikubo, H., Slager, J., Scheek, R. M., Kataoka, M.
& Mulder, F. A. A. (2012).
Comprehensive determination of protein tyrosine pKa values for photoactive yellow protein using indirect 13C NMR spectroscopy.
Biophysical Journal,
102(3), 579-86.
https://doi.org/10.1016/j.bpj.2011.12.024
Otten, R., Chu, B., Krewulak, K. D., Vogel, H. J.
& Mulder, F. A. A. (2010).
Comprehensive and cost-effective NMR spectroscopy of methyl groups in large proteins.
Journal of the American Chemical Society,
132(9), 2952-2960.
https://doi.org/10.1021/ja907706a
van Tilborg, P. J., Czisch, M.
, Mulder, F. A. A., Folkers, G. E., Bonvin, A. M., Nair, M., Boelens, R. & Kaptein, R. (2000).
Changes in dynamical behavior of the retinoid X receptor DNA-binding domain upon binding to a 14 base-pair DNA half site.
Biochemistry,
39(30), 8747-8757.
https://doi.org/10.1021/bi991550g
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
Paz, A., Zeev-Ben-Mordehai, T., Lundqvist, M., Sherman, E., Mylonas, E., Weiner, K. L., Haran, G., Svergun, D. I.
, Mulder, F. A. A., Sussman, J. L. & Silman, I. (2008).
Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3.
Biophysical Journal,
95(4), 1928-1944.
https://doi.org/10.1529/biophysj.107.126995
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
Wood, K., Paz, A., Dijkstra, K., Scheek, R. M., Otten, R., Silman, I., Sussman, J. L.
& Mulder, F. A. A. (2012).
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Biomolecular N M R Assignments,
6(1), 15-8.
https://doi.org/10.1007/s12104-011-9315-4
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
Mulder, F. A., Ayed, A., Yang, D., Arrowsmith, C. H. & Kay, L. E. (2000).
Assignment of 1H(N), 15N, 13C(alpha), 13CO and 13C(beta) resonances in a 67 kDa p53 dimer using 4D-TROSY NMR spectroscopy.
Journal of Biomolecular N M R,
18(2), 173-176.
https://doi.org/10.1023/A:1008317825976
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
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
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