Publications

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Olsen, W. P., Courtade, G., Peña-Díaz, S., Nagaraj, M., Sønderby, T. V., Mulder, F. A. A., Malle, M. G. & Otzen, D. E. (2024). CsgA gatekeeper residues control nucleation but not stability of functional amyloid. Protein Science, 33(10), Article e5178. https://doi.org/10.1002/pro.5178

Andersen, C. B., Lausdahl, A. K., Nielsen, J., Clausen, M. P., Mulder, F. A. A., Otzen, D. E. & Arnspang, E. C. (2023). 4-Oxo-2-nonenal-Induced α-Synuclein Oligomers Interact with Membranes in the Cell, Leading to Mitochondrial Fragmentation. Biochemistry, 62(16), 2417-2425. https://doi.org/10.1021/acs.biochem.3c00114

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

Sette, M., Johnson, L. A., Jimenez, R. & Mulder, F. A. A. (2023). Backbone ¹H, ¹⁵N and ¹³C resonance assignments of the 27kDa fluorescent protein mCherry. Biomolecular NMR Assignments, 17(2), 243-247. https://doi.org/10.1007/s12104-023-10149-z

Mulder, F. A. A., Tenori, L., Licari, C. & Luchinat, C. (2023). Practical considerations for rapid and quantitative NMR-based metabolomics. Journal of Magnetic Resonance, 352, Article 107462. https://doi.org/10.1016/j.jmr.2023.107462

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

Hoffmann, F., Mulder, F. A. A. & Schäfer, L. V. (2022). How Much Entropy Is Contained in NMR Relaxation Parameters? Journal of Physical Chemistry B, 126(1), 54-68. https://doi.org/10.1021/acs.jpcb.1c07786

Ali, A. A. A. I., Hoffmann, F., Schäfer, L. V. & Mulder, F. A. . A. (2022). Probing Methyl Group Dynamics in Proteins by NMR Cross-Correlated Dipolar Relaxation and Molecular Dynamics Simulations. Journal of Chemical Theory and Computation, 18(12), 7722-7732. https://doi.org/10.1021/acs.jctc.2c00568

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, Article 803004. https://doi.org/10.3389/fcimb.2022.803004

Lenard, A. J., Mulder, F. A. A. & Madl, T. (2022). Solvent paramagnetic relaxation enhancement as a versatile method for studying structure and dynamics of biomolecular systems. Progress in Nuclear Magnetic Resonance Spectroscopy, 132-133, 113-139. https://doi.org/10.1016/j.pnmrs.2022.09.001

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

Nielsen, J. T. & Mulder, F. A. A. (2021). CheSPI: chemical shift secondary structure population inference. Journal of Biomolecular NMR, 75(6-7), 273-291. https://doi.org/10.1007/s10858-021-00374-w

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

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

Mulder, F. A. A. (2021). NMR spectroscopy charges into protein surface electrostatics. Proceedings of the National Academy of Sciences (PNAS), 118(30), Article 2110176118. https://doi.org/10.1073/pnas.2110176118

Dass, R., Corlianò, E. & Mulder, F. A. A. (2021). The contribution of electrostatics to hydrogen exchange in the unfolded protein state. Biophysical Journal, 120(18), 4107-4114. https://doi.org/10.1016/j.bpj.2021.08.003

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

Dass, R., Mulder, F. A. A. & Nielsen, J. T. (2020). ODiNPred: comprehensive prediction of protein order and disorder. Scientific Reports, 10(1), Article 14780. https://doi.org/10.1038/s41598-020-71716-1

Dass, R. & Mulder, F. A. A. (2020). Paris-DÉCOR: A Protocol for the Determination of Fast Protein Backbone Amide Hydrogen Exchange Rates. In B. B. Kragelund & K. Skriver (Eds.), Intrinsically Disordered Proteins (pp. 337-344). Humana Press. https://doi.org/10.1007/978-1-0716-0524-0_17

Hoffmann, F., Mulder, F. A. A. & Schäfer, L. V. (2020). Predicting NMR relaxation of proteins from molecular dynamics simulations with accurate methyl rotation barriers. Journal of Chemical Physics, 152(8), Article 084102. https://doi.org/10.1063/1.5135379

Nielsen, J. T. & Mulder, F. A. A. (2020). Quantitative Protein Disorder Assessment Using NMR Chemical Shifts. In B. B. Kragelund & K. Skriver (Eds.), Intrinsically Disordered Proteins (pp. 303-317). Humana Press. https://doi.org/10.1007/978-1-0716-0524-0_15

Yoshimura, Y. & Mulder, F. A. A. (2020). Sensitive and simplified: a combinatorial acquisition of five distinct 2D constant-time ¹³C− ¹H NMR protein correlation spectra. Journal of Biomolecular NMR, 74(12), 695-706. https://doi.org/10.1007/s10858-020-00341-x

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

Mulder, F. A. A., Tenori, L. & Luchinat, C. (2019). Fast and Quantitative NMR Metabolite Analysis Afforded by a Paramagnetic Co-Solute. Angewandte Chemie - International Edition, 58(43), 15283-15286. https://doi.org/10.1002/anie.201908006

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 (PNAS), 116(42), 21031-21036. https://doi.org/10.1073/pnas.1911181116

Dass, R., Corlianò, E. & Mulder, F. A. A. (2019). Measurement of Very Fast Exchange Rates of Individual Amide Protons in Proteins by NMR Spectroscopy. ChemPhysChem, 20(2), 231-235. https://doi.org/10.1002/cphc.201801044

Nielsen, J. T. & Mulder, F. A. A. (2019). Quality and bias of protein disorder predictors. Scientific Reports, 9, Article 5137. https://doi.org/10.1038/s41598-019-41644-w

Hoffmann, F., Mulder, F. A. A. & Schaefer, L. V. (2018). Accurate Methyl Group Dynamics in Protein Simulations with AMBER Force Fields. Journal of Physical Chemistry B, 122(19), 5038-5048. https://doi.org/10.1021/acs.jpcb.8b02769

Mulder, F. A. A. (2018). Fuzzy and fast nuclear transport. Journal of Biological Chemistry, 293(12), 4564-4565. https://doi.org/10.1074/jbc.H118.002129

Hoffmann, F., Xue, M., Schäfer, L. V. & Mulder, F. A. A. (2018). Narrowing the gap between experimental and computational determination of methyl group dynamics in proteins. Physical Chemistry Chemical Physics, 20(38), 24577-24590. https://doi.org/10.1039/c8cp03915a

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

Tamiola, K., Scheek, R. M., Van Der Meulen, P. & Mulder, F. A. A. (2018). PepKalc: Scalable and comprehensive calculation of electrostatic interactions in random coil polypeptides. Bioinformatics, 34(12), 2053-2060. https://doi.org/10.1093/bioinformatics/bty033

Nielsen, J. T. & Mulder, F. A. A. (2018). POTENCI: prediction of temperature, neighbor and pH-corrected chemical shifts for intrinsically disordered proteins. Journal of Biomolecular NMR, 70(3), 141-165. https://doi.org/10.1007/s10858-018-0166-5

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

Madl, T. & Mulder, F. A. A. (2018). Small Paramagnetic Co-solute Molecules. In C. Luchinat, G. Parigi & E. Ravera (Eds.), Paramagnetism in Experimental Biomolecular NMR (Vol. 2018/16, pp. 283-309). Royal Society of Chemistry. https://doi.org/10.1039/9781788013291-00283

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

Xue, M., Kitahara, R., Yoshimura, Y. & Mulder, F. A. A. (2016). Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation. Biochemical and Biophysical Research Communications, 478(3), 1185-1188. https://doi.org/10.1016/j.bbrc.2016.08.092

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

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

Nielsen, J. T. & Mulder, F. A. A. (2016). There is Diversity in Disorder-"In all Chaos there is a Cosmos, in all Disorder a Secret Order". Frontiers in Molecular Biosciences, 3(FEB), Article 4. https://doi.org/10.3389/fmolb.2016.00004

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

Hass, M. A. S. & Mulder, F. A. A. (2015). Contemporary NMR Studies of Protein Electrostatics. Annual Review of Biophysics, 44, 53-75. https://doi.org/10.1146/annurev-biophys-083012-130351

Yoshimura, Y., Kulminskaya, N. V. & Mulder, F. A. A. (2015). Easy and unambiguous sequential assignments of intrinsically disordered proteins by correlating the backbone (15)N or (13)C' chemical shifts of multiple contiguous residues in highly resolved 3D spectra. Journal of Biomolecular N M R, 61(2), 109-121. https://doi.org/10.1007/s10858-014-9890-7

Kitahara, R. & Mulder, F. A. A. (2015). Is pressure-induced signal loss in NMR spectra for the Leu99Ala cavity mutant of T₄ lysozyme due to unfolding? Proceedings of the National Academy of Sciences (PNAS), 112(9), Article E923. https://doi.org/10.1073/pnas.1423279112

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

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Revised 17.04.2023

Lise Refstrup Linnebjerg Pedersen

Interdisciplinary Nanoscience Center

Danish Center for Ultrahigh Field NMR Spectroscopy

Publications