Kirkegaard, K., Svane, A. S. P., Nielsen, J. S., Hindkjær, J. J., Nielsen, N. C. & Ingerslev, H. J. (2014).
Nuclear magnetic resonance metabolomic profiling of Day 3 and 5 embryo culture medium does not predict pregnancy outcome in good prognosis patients: a prospective cohort study on single transferred embryos.
Human reproduction (Oxford, England),
29(11), 2413-20.
https://doi.org/10.1093/humrep/deu236
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
Sørensen, M. K., Jensen, O.
, Bakharev, O. N., Nyord, T. & Nielsen, N. C. (2015).
NPK NMR Sensor: Online Monitoring of Nitrogen, Phosphorus, and Potassium in Animal Slurry.
Analytical Chemistry,
87(13), 6446-6450.
https://doi.org/10.1021/acs.analchem.5b01924
Bomholdt Ravnsbæk, D., Filinchuk, Y., Cerenius, Y.
, Jakobsen, H. J., Besenbacher, F., Skibsted, J. & Jensen, T. R. (2009).
Novel Zinc-based Hydrogen Storage Materials. Poster session presented at 7
th Annual iNANO Meeting, Århus, Denmark.
Dupont, D. M., Hansen, M., Jensen, J. K.
, Kristiansen, S. K., Mathiasen, L., Pedersen, K. E.
, Skeldal, S., Wind, T., Malmendal, A., Schiøtt, B., Nielsen, N. C. & Andreasen, P. (2006).
Novel conformational probes and activity regulators of plasminogen avtivator inhibitor-1, isolated from phage-displayed disulfide bridge constrained peptide libraries. Poster session presented at Annual Meeting of the "Cancer Degradome", København, Denmark.
Bomholdt Ravnsbæk, D., Filinchuk, Y., Cerenius, Y.
, Jakobsen, H. J., Besenbacher, F., Skibsted, J. & Jensen, T. R. (2010).
Novel alkali zinc borohydrides for hydrogen storage.
Kehlet, C., Del Federico, E., Schahbaz, H., Catalano, A., Dittmer, J.
& Nielsen, N. C. (2013).
Non-invasive characterization of polymeric materials in relation to art conservation using unilateral NMR combined with multivariate data analysis.
Analytical Methods,
5(17), 4480-4486.
https://doi.org/10.1039/c3ay40650d
Nielsen, G., Malmendal, A., Meissner, A.
, Møller, J. V. & Nielsen, N. C. (2003).
NMR studies of the fifth transmembrane segment of sarcoplasmic reticulum Ca2+-ATPase reveals a hinge close to the Ca2+ ligating residues.
FEBS Letters,
544, 50-56.
Underhaug, J., Jakobsen, L. O.
, Esmann, M., Malmendal, A. & Nielsen, N. C. (2006).
NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region.
FEBS Letters,
580, 4777-4783.
Malmendal, A., Amoresano, C., Trotta, R., Lauri, I., De Tito, S., Novellino, E. & Randazzo, A. (2011).
NMR spectrometers as "magnetic tongues": prediction of sensory descriptors in canned tomatoes.
Journal of Agricultural and Food Chemistry,
59(20), 10831-8.
https://doi.org/10.1021/jf203803q
Sørensen, M. K., Vinding, M. S., Bakharev, O. N., Nesgaard, T., Jensen, O.
& Nielsen, N. C. (2014).
NMR Sensor for Onboard Ship Detection of Catalytic Fines in Marine Fuel Oil.
Analytical Chemistry,
86(15), 7205-7208.
https://doi.org/10.1021/ac5014496
Pedersen, M. Ø., Mikkelsen, K., Behrens, M. A., Pedersen, J. S., Enghild, J. J., Skrydstrup, T., Malmendal, A. & Nielsen, N. C. (2010).
NMR reveals two-step association of Congo Red to amyloid β in low-molecular-weight aggregates.
Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical,
114(48), 16003-16010.
https://doi.org/10.1021/jp108035y
Bertram, H. C., Bach Knudsen, K. E., Serena, A.
, Malmendal, A., Nielsen, N. C., Fretté, X. C. & Andersen, H. J. (2006).
NMR-based metabonomic studies reveal changes in the biochemical profile of plasma and urine from pigs fed high fibre rye bread. British J. Nutr.,
65, 955-962.
Bertram, H. C., Malmendal, A., Nielsen, N. C., Straadt, I. K., Larsen, T., Bach Knudsen, K. E. & Lærke, H. N. (2009).
NMR-based metabonomics reveals that plasma betaine increases upon intake of high-fiber rye buns in hypercholesterolemic pigs.
Molecular Nutrition & Food Research,
53, 1055-1062.
https://doi.org/10.1002/mnfr.200800344
Jakobsen, H. J., Song, L., Gan, Z., Hung, I.
, Bildsoe, H., Skibsted, J., Bak, E. N., Finster, K., Nornberg, P. & Jensen, S. K. (2016).
NMR and EPR Studies of Free-Radical Intermediates from Experiments Mimicking the Winds on Mars: A Sink for Methane and Other Gases.
The Journal of Physical Chemistry Part C,
120(45), 26138-26149.
https://doi.org/10.1021/acs.jpcc.6b08847
Nørby, P., Overgaard, J., Sigaard Christensen, P., Richter, B., Song, X., Dong, MD., Han, A., Skibsted, J., Iversen, B. B. & Johnsen, S. (2014).
(NH4)4Sn2S6·3H 2O: Crystal structure, thermal decomposition, and precursor for textured thin film.
Chemistry of Materials,
26(15), 4494-4504.
https://doi.org/10.1021/cm501681r
Jakobsen, H. J., Bildsøe, H. K., Skibsted, J., Brorson, M., Srinivasan, B. R., Näther, C. & Bensch, W. (2009).
New opportunities in acquisition and analysis of natural-abundance complex solid-state 33S MAS NMR spectra: (CH3NH3)2WS4.
Physical Chemistry Chemical Physics,
11, 6981-6986.
Stebbins, J. F., Du, L.-S., Kroeker, S., Neuhoff, P., Rice, D., Frye, J.
& Jakobsen, H. J. (2002).
New Opportunities for High-Resolution Solid-State NMR Spectroscopy of Oxide Materials at 21.1- and 18.8-Tesla Fields.
Solid State Nuclear Magnetic Resonance,
21, 105-115.
Jensen, T. R., Gérentes, N., Jepsen, J.
, Hazell, R. G. & Jakobsen, H. J. (2005).
New Amine-Templated Zinc Phosphates with a Temperature-Induced Increase of Structural Dimensionality.
Inorg. Chem.,
44(3), 658.
Jespersen, S. N., Bjarkam, C. R., Nyengaard, J. R., Mallar, C., Hansen, B., Vosegaard, T., Østergaard, L., Yablonskiy, DA.
, Nielsen, N. C. & Vestergaard-Poulsen, P. (2010).
Neurite density from magnetic resonance diffusion measurements at ultrahigh field: comparison with light microscopy and electron microscopy.
NeuroImage,
49(1), 205-16.
https://doi.org/10.1016/j.neuroimage.2009.08.053
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
Runager, K., Underhaug, J., Basaiawmoit, R. V., Valnickova, Z., Kristensen, T., Otzen, D., Klintworth, G. K.
, Nielsen, N. C. & Enghild, J. J. (2009).
Naturally Occurring Mutations Alter the Structure and Stability of the Fourth Fasciclin Domain of the Transforming Growth Factor Beta Induced Protein (TGFBIp).
Investigative Ophthalmology & Visual Science, (E-Abstract 1016).
Jakobsen, H. J., Bildsøe, H. K., Skibsted, J., Brorson, M. & Schaumburg, K. (2010).
Natural abundance solid-state 95Mo MAS NMR of MoS2 reveals precise 95Mo anisotropic parameters from its central and satellite transitions.
Chemical Communications,
46, 2103-2105.
https://doi.org/10.1039/b926699b
Dansirima, P., Kristensen, L. G., Grinderslev, J. B., Skibsted, J., Utke, R.
& Jensen, T. R. (2024).
Nanoconfinement of an ammine magnesium borohydride composite electrolyte in a mesoporous silica scaffold.
Communications Materials,
5(1), Article 160.
https://doi.org/10.1038/s43246-024-00601-5
Nielsen, T. K., Javadian, P., Polanski, M.
, Besenbacher, F., Bystrzycki, J.
, Skibsted, J. & Jensen, T. R. (2014).
Nanoconfined of NaAlH4: Prolific effects from increased surface area and pore volume.
Nanoscale,
6(1), 599-607.
https://doi.org/10.1039/c3nr03538g
Mortensen, H. G., Madsen, J. K., Andersen, K. K., Vosegaard, T., Deen, G. R.
, Otzen, D. E. & Pedersen, J. S. (2017).
Myoglobin and α-Lactalbumin Form Smaller Complexes with the Biosurfactant Rhamnolipid Than with SDS.
Biophysical Journal,
113(12), 2621-2633.
https://doi.org/10.1016/j.bpj.2017.10.024
Underhaug, J., Koldsø, H., Runager, K., Nielsen, J. T., Sørensen, C. S., Kristensen, T., Otzen, D., Karring, H., Malmendal, A., Schiøtt, B., Enghild, J. J. & Nielsen, N. C. (2013).
Mutation in transforming growth factor beta induced protein associated with granular corneal dystrophy type 1 reduces the proteolytic susceptibility through local structural stabilization.
BBA General Subjects,
1834(12), 2812–2822.
https://doi.org/10.1016/j.bbapap.2013.10.008
Nielsen, N. S., Juhl, D. W., Poulsen, E. T., Lukassen, M. V., Poulsen, E. C., Risør, M. W., Scavenius, C. & Enghild, J. J. (2017).
Mutation-Induced Deamidation of Corneal Dystrophy-Related Transforming Growth Factor β-Induced Protein.
Biochemistry,
56(49), 6470–6480.
https://doi.org/10.1021/acs.biochem.7b00668
Bowen, S., Rybalko, O., Petersen, J. R.
, Vinding, M. S., Ullisch, M. G., Nielsen, N. C. & Ardenkjær-Larsen, J. H. (2017).
Multi-Field Cryogen Free Dissolution-DNP at 3.35, 6.70, and 10.05 T. Abstract from 13th EUROMAR 2017, Warsaw.
Aagaard, A., Bechsgaard, J., Sørensen, J. G., Sandfeld, T., Settepani, V., Bird, T. L.
, Lund, M. B., Malmos, K. G., Falck-Rasmussen, K., Darolti, I.
, Nielsen, K. L., Johannsen, M., Vosegaard, T., Tregenza, T., Verhoeven, K. J. F., Mank, J. E.
, Schramm, A. & Bilde, T. (2024).
Molecular Mechanisms of Temperature Tolerance Plasticity in an Arthropod.
Genome Biology and Evolution,
16(8), Article evae165.
https://doi.org/10.1093/gbe/evae165
Andreasen, M., Nielsen, S. B., Mittag, T., Bjerring, M., Nielsen, J. T., Zhang, S., Nielsen, E. H., Jeppesen, M., Christiansen, G., Besenbacher, F., Dong, M., Nielsen, N. C., Skrydstrup, T. & Otzen, D. E. (2012).
Modulation of fibrillation of hIAPP core fragments by chemical modification of the peptide backbone.
B B A - Proteins and Proteomics,
1824(2), 274-85.
https://doi.org/10.1016/j.bbapap.2011.10.014
Jansang, B., Nonat, A.
& Skibsted, J. (2010).
Modelling of guest-ion incorporation in the anhydrous calcium silicate phaes of Portland cement by periodic density functional theory calculations.
Proceedings of CONMOD–2010, 3rd RILEM Conference on Concrete Modelling, June 22 – 25, 2010, Lausanne, Switzerland., 25-28.
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