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