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

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
Malinauskaite, L., Quick, M., Reinhard, L., Lyons, J. A., Yano, H., Javitch, J. A. & Nissen, P. (2014). A mechanism for intracellular release of Na(+) by neurotransmitter/sodium symporters. Nature Structural and Molecular Biology, 21(11), 1006-1012. https://doi.org/10.1038/nsmb.2894
Drachmann, N. D., Olesen, C., Møller, J. V., Guo, Z., Bublitz, M. & Nissen, P. (2014). Comparing crystal structures of Ca2+-ATPase in the presence of different lipids. FEBS journal, 281(18), 4249-4262. https://doi.org/10.1111/febs.12957
Andersson, M., Mattle, D., Sitsel, O., Klymchuk, T., Nielsen, A. M., Møller, L. B., White, S. H., Nissen, P. & Gourdon, P. (2014). Copper-transporting P-type ATPases use a unique ion-release pathway. Nature Structural and Molecular Biology, 21, 43-48. https://doi.org/10.1038/nsmb.2721
Huliciak, M., Reinhard, L., Laursen, M., Fedosova, N., Nissen, P. & Kubala, M. (2014). Crystals of Na(+)/K(+)-ATPase with bound cisplatin. Biochemical Pharmacology, 92(3), 494-498. https://doi.org/10.1016/j.bcp.2014.08.029
Iešmantavičius, V., Dogan, J., Jemth, P., Teilum, K. & Kjærgaard, M. (2014). Helical propensity in an intrinsically disordered protein accelerates ligand binding. Angewandte Chemie International Edition, 53(6), 1548-51. https://doi.org/10.1002/anie.201307712
Penner, R., Andersen, E. S., Jensen, J. L., Kantcheva, A. K., Bublitz, M., Nissen, P., Rasmussen, A. M. H., Svane, K. L., Hammer, B., Rezazadegan, R., Nielsen, N. C., Nielsen, J. T. & Andersen, J. E. (2014). Hydrogen bond rotations as a uniform structural tool for analyzing protein architecture. Nature Communications, 5, Artikel 5803. https://doi.org/10.1038/ncomms6803
Bianchini, E., Testoni, S., Gentile, A., Calì, T., Ottolini, D., Villa, A., Brini, M., Betto, R., Mascarello, F., Sandonà, D., Sacchetto, R. & Nissen, P. (2014). Inhibition of Ubiquitin Proteasome System Rescues the Defective Sarco(endo)plasmic Reticulum Ca2+-ATPase (SERCA1) Protein Causing Chianina Cattle Pseudomyotonia. Journal of Biological Chemistry, 289(48), 33073-33082. https://doi.org/10.1074/jbc.M114.576157
Pedersen, B. P., Ifrim, G., Liboriussen, P., Axelsen, K. B., Palmgren, M. G., Nissen, P., Wiuf, C. H. & Pedersen, C. N. S. (2014). Large Scale Identification and Categorization of Protein Sequences Using Structured Logistic Regression. PLoS One, 9(1), Artikel e85139. https://doi.org/10.1371/journal.pone.0085139
Weigand, K., Laursen, M., Swarts, H. G. P., Engwerda, A. H. J., Prufert, C., Sandrock, J., Nissen, P., Fedosova, N., Russel, F. G. M. & Koenderink, J. B. (2014). Na(+),K(+)-ATPase Isoform Selectivity for Digitalis-Like Compounds Is Determined by Two Amino Acids in the First Extracellular Loop. Chemical Research in Toxicology, 27(12), 2082-2092. https://doi.org/10.1021/tx500290k
Quistgaard, E. M., Grøftehauge, M. K., Madsen, P., Pallesen, L. T., Christensen, B. S., Sørensen, E. S., Nissen, P., Petersen, C. M. & Thirup, S. S. (2014). Revisiting the structure of the Vps10 domain of human sortilin and its interaction with neurotensin. Protein Science, 23(9), 1291-1300. https://doi.org/10.1002/pro.2512
Montigny, C., Decottignies, P., le Maréchal, P., Capy, P., Bublitz, M., Olesen, C., Møller, J. V., le Maire, M. & Nissen, P. (2014). S-Palmitoylation and S-Oleoylation of Rabbit and Pig Sarcolipin. Journal of Biological Chemistry, 289, 33850-33861. https://doi.org/10.1074/jbc.M114.590307

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Revideret 13.11.2025
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Helene Eriksen