Institut for Molekylærbiologi og Genetik

Aarhus Universitets segl

Neurobiologi

DANDRITE's logo

The Section for Neurobiology is part of the Danish Research Institute of Translational Neuroscience – DANDRITE 

- the Danish node of the Nordic EMBL Partnership for Molecular Medicine, which performs basic and translational research in brain and the nervous system.  

Groups at DANDRITE encompass ambitious research programs that include:

  • Molecular and cellular mechanisms of memory
  • Effort-based decision making
  • Neuronal development and stem cells
  • Motor control
  • Brain processing of vision
  • Neurological and neurodegenerative diseases
  • Psychiatric disorders
  • Neurotrophic receptors, sorting
  • Structural biology of membrane transporters and receptors

Read more about the research at DANDRITE.

Below you see the list of researchers at DANDRITE affiliated with the Department of Molecular Biology and Genetics.

Professor

Lektorer

Tenure Track Adjunkt

Peer-reviewed publikationer

Sortér efter: Dato | Forfatter | Titel

Saleh, N., Wang, Y., Nissen, P. & Lindorff-Larsen, K. (2019). Allosteric modulation of the sarcoplasmic reticulum Ca2+ ATPase by thapsigargin via decoupling of functional motions. Physical Chemistry Chemical Physics, 21(39), 21991-21995. https://doi.org/10.1039/c9cp04736k
Yamamoto, S., Nakamura, H., Kawamura, Y. K., Kitazawa, T., Kimura, M. & Kitazawa, Y. (2024). Alkoxy Substituted Brominated closo-Dodecaborates with Functionalized Aliphatic Spacers. Chemistry, 6(6), 1635-1644. https://doi.org/10.3390/chemistry6060099
Azouaoui, H., Montigny, C., Ash, M.-R., Fijalkowski, F., Jacquot, A., Grønberg, C., López-Marqués, R. L., Palmgren, M. G., Garrigos, M., le Maire, M., Decottignies, P., Gourdon, P., Nissen, P., Champeil, P. & Lenoir, G. (2014). A high-yield co-expression system for the purification of an intact drs2p-cdc50p lipid flippase complex, critically dependent on and stabilized by phosphatidylinositol-4-phosphate. PLoS One, 9(11), Artikel e112176. https://doi.org/10.1371/journal.pone.0112176
Azouaoui, H., Montigny, C., Dieudonné, T., Champeil, P., Jacquot, A., Vázquez-Ibar, J. L., le Maréchal, P., Ulstrup, J., Ash, M.-R., Lyons, J. A., Nissen, P. & Lenoir, G. (2017). A High and Phosphatidylinositol-4-phosphate (PI4P)-dependent ATPase Activity for the Drs2p/Cdc50p Flippase after Removal of its N- and C-terminal Extensions. Journal of Biological Chemistry, 292(19), 7954-7970. https://doi.org/10.1074/jbc.M116.751487
Gorgel, M., Bøggild, A., Ulstrup, J., Weiss, M. S., Müller, U., Nissen, P. & Boesen, T. (2015). Against the odds? De novo structure determination of a pilin with two cysteine residues by sulfur SAD. Acta crystallographica Section D: Structural biology , 71(5), 1095-1101. https://doi.org/10.1107/S1399004715003272
Kjærgaard, M., Andersen, L., Nielsen, L. D. & Teilum, K. (2013). A folded excited state of ligand-free nuclear coactivator binding domain (NCBD) underlies plasticity in ligand recognition. Biochemistry, 52(10), 1686-93. https://doi.org/10.1021/bi4001062
Mertens, H. D. T., Kjærgaard, M., Mysling, S., Gårdsvoll, H., Jørgensen, T. J. D., Svergun, D. I. & Ploug, M. (2012). A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR). Journal of Biological Chemistry, 287(41), 34304-15. https://doi.org/10.1074/jbc.M112.398404
Boesecke, P., Bois, J. M., Crëpin, T., Hunte, C., Kahn, R., Kao, W.-C., Nauton, L., Winther, A.-M. L., Møller, J. V., Nissen, P., Nury, H., Olesen, C. E., Pebay-Peyroula, E., Vicat, J. & Stuhrmann, H. (2009). A first low-resolution difference Fourier map of phosphorus in a membrane protein from near-edge anomalous diffraction. Journal of Synchrotron Radiation, 16(5), 658-665.
Dach, I., Olesen, C., Signor, L., Nissen, P., le Maire, M., Møller, J. V. & Ebel, C. (2012). Active Detergent-solubilized H+,K+-ATPase Is a Monomer. Journal of Biological Chemistry, 287, 41963-41978. https://doi.org/10.1074/jbc.M112.398768
Hourez, R., Azdad, K., Vanwalleghem, G., Roussel, C., Gall, D. & Schiffmann, S. N. (2005). Activation of protein kinase C and inositol 1,4,5-triphosphate receptors antagonistically modulate voltage-gated sodium channels in striatal neurons. G E P, 1059(2), 189-196. https://doi.org/10.1016/j.brainres.2005.08.031
Dieudonné, T., Kümmerer, F., Laursen, M. J., Stock, C., Flygaard, R. K., Khalid, S., Lenoir, G., Lyons, J. A., Lindorff-Larsen, K. & Nissen, P. (2023). Activation and substrate specificity of the human P4-ATPase ATP8B1. Nature Communications, 14, Artikel 7492. https://doi.org/10.1038/s41467-023-42828-9
Fruergaard, M. U., Nielsen, C. J. F., Kjeldsen, C. R., Iversen, L., Andersen, J. L. & Nissen, P. (2023). Activation and inhibition of the C-terminal kinase domain of p90 ribosomal S6 kinases. Life Science Alliance, 6(5), Artikel e202201425. https://doi.org/10.26508/lsa.202201425

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Revideret 13.11.2025
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Helene Eriksen