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
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
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
Martin, J. R.
, Mulder, F. A. A., Karimi-Nejad, Y., van der Zwan, J., Mariani, M., Schipper, D. & Boelens, R. (1997).
The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site.
Structure,
5(4), 521-532.
https://doi.org/10.1016/S0969-2126(97)00208-6
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
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
Lindman, S., Bauer, M. C., Lund, M., Diehl, C.
, Mulder, F. A. A., Akke, M. & Linse, S. (2010).
PKa values for the unfolded state under native conditions explain the pH-dependent stability of PGB1.
Biophysical Journal,
99(10), 3365-3373.
https://doi.org/10.1016/j.bpj.2010.08.078
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
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
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
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
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
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
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
Helgstrand, M., Mandava, C. S.
, Mulder, F. A. A., Liljas, A., Sanyal, S. & Akke, M. (2007).
The Ribosomal Stalk Binds to Translation Factors IF2, EF-Tu, EF-G and RF3 via a Conserved Region of the L12 C-terminal Domain.
Journal of Molecular Biology,
365(2), 468-479.
https://doi.org/10.1016/j.jmb.2006.10.025
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
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
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
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
Düx, P., Rubinstenn, G., Vuister, G. W., Boelens, R.
, Mulder, F. A. A., Hård, K., Hoff, W. D., Kroon, A. R., Crielaard, W., Hellingwerf, K. J. & Kaptein, R. (1998).
Solution structure and backbone dynamics of the photoactive yellow protein.
Biochemistry,
37(37), 12689-12699.
https://doi.org/10.1021/bi9806652
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
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
Brünger, A. T., Karimi-Nejad, Y.
, Mulder, F. A. A., Martin, J. R., Schipper, D. & Boelens, R. (1999).
NMR Studies of the 269 Residue Serine Protease PB92 from Bacillus Alcalophilus.
NMR in Supramolecular Chemistry,
526, 227-246.
https://doi.org/10.1007/978-94-011-4615-9_14
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
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
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