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