Publications

We publish in a broad array of journals… To view list of publications related to nanoscience/technology by scientists associated with iNANO

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Sist, M., Bindzus, N. & Iversen, B. B. (2014). The structure of tin telluride. Poster-session præsenteret på DanScatt annual meeting, Lyngby, Danmark.

Steiner, E. M., Lyngsø, J., Guy, J. E., Bourenkov, G., Lindqvist, Y., Schneider, T. R., Pedersen, J. S., Schneider, G. & Schnell, R. (2018). The structure of the N-terminal module of the cell wall hydrolase RipA and its role in regulating catalytic activity. Proteins: Structure, Function and Bioinformatics, 86(9), 912-923. https://doi.org/10.1002/prot.25523

Morth, J. P., Poulsen, H., Toustrup-Jensen, M. S., Schack, V. R., Egebjerg, J., Andersen, J. P., Vilsen, B. & Nissen, P. (2009). The structure of the Na⁺,K⁺-ATPase and mapping of isoform differences and disease-related mutations. Philosophical Transactions of the Royal Society B: Biological Sciences, 364(1514), 217-27. https://doi.org/10.1098/rstb.2008.0201

Wahlberg, N. & Iversen, B. B. (2015). The structure of thecotrichite an efflorescent salt on calcareous objects. Poster-session præsenteret på Danscatt Annual meeting 2015, Aarhus, Danmark.

Fester, J., Makoveev, A., Grumelli, D., Gutzler, R., Sun, Z., Rodríguez-Fernández, J., Kern, K. & Lauritsen, J. V. (2018). The Structure of the Cobalt Oxide/Au Catalyst Interface in Electrochemical Water Splitting. Angewandte Chemie - International Edition, 57(37), 11893-11897. https://doi.org/10.1002/anie.201804417

Mangayayam, M., Dideriksen, K., Ceccato, M. & Tobler, D. J. (2019). The Structure of Sulfidized Zero-Valent Iron by One-Pot Synthesis: Impact on Contaminant Selectivity and Long-Term Performance. Environmental Science & Technology, 53(8), 4389-4396. https://doi.org/10.1021/acs.est.8b06480

Jensen, J. E., Foreman, J. C. (red.) & Johansen, T. (red.) (2002). The structure of ligand-gated ion-channels. I Textbook of Receptor Pharmacology (2 udg., s. 111-130)

Filsø, M., Chaaban, I., Al Shehabi, A., Skibsted, J. & Lock, N. (2017). The structure-directing amine changes everything: Structures and optical properties of two-dimensional thiostannates. Acta Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 73, 931-940. https://doi.org/10.1107/S2052520617010630

Thostrup, P., Salmeron, M. & Besenbacher, F. (2012). The structure and reactivity of surfaces revealed by scanning tunneling microscopy. MRS Bulletin, 37(07), 677-681.

Olesen, C., Picard, M., Winther, A.-M. L., Nielsen, C. G., Morth, J. P., Oxvig, C., Møller, J. V. & Nissen, P. (2007). The structural basis of calcium transport by the calcium pump. Nature, 450(7172), 1036-1042. https://doi.org/10.1038/nature06418

Møller, J. V., Olesen, C., Jensen, A.-M. L. & Nissen, P. (2005). The structural basis for coupling of Ca²⁺transport to ATP hydrolysis by the sarcoplasmic reticulum Ca²⁺-ATPase. J. Bioenerg. Biomembr., 37(6), 359-364.

Grube, E. & Nielsen, U. G. (2015). The stoichiometry of synthetic alunite as a function of hydrothermal aging investigated by solid-state NMR spectroscopy, powder X-ray diffraction and infrared spectroscopy. Physics and Chemistry of Minerals, 42(5), 337-345. https://doi.org/10.1007/s00269-014-0724-7

Marvian, A. T., Aliakbari, F., Mohammad-Beigi, H., Ahmadi, Z. A., Mehrpouyan, S., Lermyte, F., Nasouti, M., Collingwood, J. F., Otzen, D. E. & Morshedi, D. (2020). The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization. International Journal of Biological Macromolecules, 155, 543-550. https://doi.org/10.1016/j.ijbiomac.2020.03.238

Sanggaard, K. W., Dyrlund, T. F., Bechsgaard, J. S., Scavenius, C., Wang, T., Bilde, T. & Enghild, J. J. (2016). The spider hemolymph clot proteome reveals high concentrations of hemocyanin and von Willebrand factor-like proteins. B B A - Proteins and Proteomics, 1864(2), 233-241. https://doi.org/10.1016/j.bbapap.2015.11.004

Yatime, L. & Andersen, G. R. (2014). The specificity of DNA recognition by the RAGE receptor. Journal of Experimental Medicine, 211(5), 749-750. https://doi.org/10.1084/jem.20132526

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

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

Brodersen, D. E. & Nissen, P. (2005). The social life of ribosomal proteins. FEBS journal, 272(9), 2098-2108.

Christensen, L. F. B., Hansen, L. M., Finster, K., Christiansen, G., Nielsen, P. H., Otzen, D. E. & Dueholm, M. S. (2018). The Sheaths of Methanospirillum Are Made of a New Type of Amyloid Protein. Frontiers in Microbiology, 9(NOV), Artikel 2729. https://doi.org/10.3389/fmicb.2018.02729, https://doi.org/10.3389/fmicb.2018.02729

Behrens, M. A., Sendall, T. J., Pedersen, J. S., Kjeldgaard, M., Huntington, J. A. & Jensen, J. K. (2014). The Shapes of Z-α1-Antitrypsin Polymers in Solution Support the C-Terminal Domain-Swap Mechanism of Polymerization. Biophysical Journal, 107(8), 1905-1912. https://doi.org/10.1016/j.bpj.2014.08.030

Pedersen, S. M., Nielsen, N. C., Andersen, H. J., Olsson, J., Simrén, M., Öhman, L., Svensson, U., Malmendal, A. & Bertram, H. C. (2010). The Serum Metabolite Response to Diet Intervention with Probiotic Acidified Milk in Irritable Bowel Syndrome Patients is indistiguishanble from that of Non-Probiotic Acidified Milk by 1H NMR-based Metabonomic Analysis. Nutrients, 2, 1141-1155.

Poulsen, E. T., Nielsen, N. S., Scavenius, C., Mogensen, E. H., Risør, M. W., Runager, K., Lukassen, M. V., Rasmussen, C. B., Christiansen, G., Richner, M., Vorum, H. & Enghild, J. J. (2019). The serine protease HtrA1 cleaves misfolded transforming growth factor β-induced protein (TGFBIp) and induces amyloid formation. Journal of Biological Chemistry, 294(31), 11817-11828. https://doi.org/10.1074/jbc.RA119.009050

Baatrup, E. (1984). The sense of taste in the lamprey.

Liu, L., Xia, D., Klausen, L. H. & Dong, MD. (2014). The self-assembled behavior of DNA bases on the interface. International Journal of Molecular Sciences (Online), 15(2), 1901-14. https://doi.org/10.3390/ijms15021901

Nielsen, M., Liljefors, T., Krogsgaard-Larsen, P. & Jensen, J. E. (2003). The selective activation of the glutamate receptor GluR5 by ATPA is controlled by serine 741. Mol. Pharmacol., 63, 19-25.

Nielsen(Holm), M. M., Krogsgaard-Larsen, P., Liljefors, T. & Egebjerg, J. (2003). The selective activation of the glutamate receptor GluR5 by ATPA is controlled by serine 741. Molecular Pharmacology, 63, 19-25.

Schunack, M., Rosei, F. & Besenbacher, F. (2003). The scanning tunneling microscope as a unique tool to investigate the interaction between complex molecules and metal surfaces. Science: Technology and Education of Microscopy - An Overview, 1, 43.

Møller, J. V., Olesen, C. E., Winther, A.-M. L. & Nissen, P. (2010). The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pump. Quarterly Reviews of Biophysics, 43(4), 501-566.

Winther, A.-M. L., Bublitz, M., Karlsen, J. L., Møller, J. V., Hansen, J. B., Nissen, P. & Buch-Pedersen, M. J. (2013). The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm. Nature, 495(7440), 265-269. https://doi.org/10.1038/nature11900

Thøgersen, J., Nielsen, J. B., Jensen, S. K., Keiding, S. R., Odelius, M., Ogden, T., Réhault, J. & Helbing, J. (2013). The rotation of NO₃− as a probe of molecular ion - water interactions. E P J Web of Conferences, 41, Artikel 06002. https://doi.org/10.1051/epjconf/20134106002

Birkedal, H., Andersen, A. M. K., Arakcheeva, A., Chapuis, G., Norby, P. & Pattison, P. (2006). The Room-Temperature Superstructure of ZrP₂O₇ Is Orthorhombic: There are No Unusual 180^o P-O-P Bond Angles. Inorg. Chem., 45(11), 4346-4351.

Enevoldsen, G. H., Pinto, H. P., Besenbacher, F., Lauritsen, J. V. & Foster, A. S. (2009). The role of tip size and orientation, tip-surface relaxations and surface impurities in simultaneous AFM and STM studies on the TiO₂(110) surface. Nanotechnology, 20(26), 264020. https://doi.org/10.1088/0957-4484/20/26/264020

Ramsgaard, L. (2010). The Role of the Receptor for Advanced Glycation End-Products in the Pathogenesis of Silicosis and Acute Lung Injury.

Ramsgaard, L., Englert, J. M., Tobolewski, J., Tomai, L., Fattman, C. L., Leme, A. S., Kaynar, A. M., Shapiro, S. D., Enghild, J. J. & Oury, T. D. (2010). The role of the receptor for advanced glycation end-products in a murine model of silicosis. P L o S One, 5(3), e9604. https://doi.org/10.1371/journal.pone.0009604

Rauls, E. & Hammer, B. (2006). The role of the chiral modifier on the enantioselective hydrogenation of methyl pyruvate on Pt (111). Catal. Lett., 106, 111-114.

Salazar, E. L. (2011). The role of surface and subsurface defects in the adsorption of oxygen and the adhesion of metals on TiO2(110).

Lorenzen, N., Nielsen, S. B., Buell, A. K., Kaspersen, J. D., Arosio, P., Vad, B. S., Paslawski, W., Christiansen, G., Valnickova Hansen, Z., Andreasen, M., Enghild, J. J., Pedersen, J. S., Dobson, C. M., Knowles, T. P. J. & Otzen, D. (2014). The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation. Journal of the American Chemical Society, 136(10), 3859-3868. https://doi.org/10.1021/ja411577t

Kjeldsen, M. K., Pedersen, F. S., Johansen, P., Johnsen, H. E. & Dybkær, K. (2010). The role of SOX4 in malignant lymphopoiesis. Poster-session præsenteret på PhD Day, Århus, Danmark.

Kjeldsen, M. K., Pedersen, F. S., Johansen, P., Johnsen, H. E. & Dybkær, K. (2010). The role of SOX4 in malignant lymphopoiesis. Abstract fra PhD Day, Århus, Danmark.

Liu, L., Busuttil, K., Zhang, S., Yang, Y., Wang, C., Besenbacher, F. & Dong, M. (2011). The role of self-assembling polypeptides in building nanomaterials. Physical Chemistry Chemical Physics, 13, 17435-17444. https://doi.org/10.1039/c1cp21338e

Topsøe, H., Hinnemann, B., Nørskov, J. K., Lauritsen, J. V., Besenbacher, F., Hansen, P. L., Hytoft, G., Egeberg, R. G. & Knudsen, K. G. (2005). The role of reaction pathways and support interactions in the development of high activity hydrotreating catalysts. Catalysis Today, 107-108, 12-22.

Jeppesen, M. D., Westh, P. & Otzen, D. E. (2010). The role of protonation in protein fibrillation. FEBS Letters, 584(4), 780-4. https://doi.org/10.1016/j.febslet.2010.01.002

Gu, T., Just, J., Stenz, K. T., Yan, Y., Sieljacks, P., Wang, J., Groennebaek, T. S., Jakobsgaard, J. E., Rindom, E., Herskind, J., Gravholt, A., Lassen, T. R., Jørgensen, M., Bæk, R., Gutiérrez-Jiménez, E., Iversen, N. K., Rasmussen, P. M., Nyengaard, J. R., Jørgensen, M. M. ... Drasbek, K. R. (2022). The Role of Plasma Extracellular Vesicles in Remote Ischemic Conditioning and Exercise-Induced Ischemic Tolerance. International Journal of Molecular Sciences , 23(6), Artikel 3334. https://doi.org/10.3390/ijms23063334

Khateb, H., Sørensen, R. S., Cramer, K., Eklund, A. S., Kjems, J., Meyer, R. L., Jungmann, R. & Sutherland, D. S. (2022). The Role of Nanoscale Distribution of Fibronectin in the Adhesion of Staphylococcus aureus Studied by Protein Patterning and DNA-PAINT. ACS Nano, 16(7), 10392-10403. https://doi.org/10.1021/acsnano.2c00630

Carmona, F. J., Dal Sasso, G., Bertolotti, F., Ramírez-Rodríguez, G. B., Delgado-López, J. M., Pedersen, J. S., Masciocchi, N. & Guagliardi, A. (2020). The role of nanoparticle structure and morphology in the dissolution kinetics and nutrient release of nitrate-doped calcium phosphate nanofertilizers. Scientific Reports, 10(1), Artikel 12396. https://doi.org/10.1038/s41598-020-69279-2

Gjelstrup, L. C., Kaspersen, J. D., Behrens, M. A., Pedersen, J. S., Thiel, S., Kingshott, P., Oliveira, C. L. P., Thielens, N. M. & Vorup-Jensen, T. (2012). The role of nanometer-scaled ligand patterns in polyvalent binding by large mannan-binding lectin oligomers. Journal of Immunology, 188(3), 1292-306. https://doi.org/10.4049/jimmunol.1103012

Andersen, M. Ø., Dillschneider, P. & Kjems, J. (2013). The Role of MicroRNAs in Natural Tissue Development and Application in Regenerative Medicine. I K. A. Howard (red.), RNA Interference from Biology to Therapeutics (s. 57-78). Springer. https://doi.org/10.1007/978-1-4614-4744-3_3

Debnath, D. K., Basaiawmoit, R. V., Nielsen, K. L. & Otzen, D. E. (2011). The role of membrane properties in Mistic folding and dimerisation. Protein Engineering Design and Selection (Print), 24(1-2), 89-97. https://doi.org/10.1093/protein/gzq095

Suzuki, K., Nagase, H., Ito, A., Enghild, J. J. & Salvesen, G. (1990). The role of matrix metalloproteinase 3 in the stepwise activation of human rheumatoid synovial procollagenase. Biological chemistry Hoppe-Seyler, 371 Suppl, 305-10.

Wendt, S., Sprunger, P., Lira, E., Madsen, G. K. H., Li, Z., Hansen, J. Ø., Matthiesen, J., Blekinge-Rasmussen, A., Lægsgaard, E., Hammer, B. & Besenbacher, F. (2008). The Role of Interstitial Sites in the Ti3d Defect State in the Band Gap of Titania. Science, 320, 1755-1759. https://doi.org/10.1126/science.1159846

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Lise Refstrup Linnebjerg Pedersen