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

Lindholt, J., Mattle, D., Fedosova, N., Nissen, P. & Schuldt, L. (2016). Isolation, crystallization and crystal structure determination of bovine kidney Na+,K+-ATPase. Acta Crystallographica Section F: Structural Biology Communications, 72(Pt. 4), 282-287. https://doi.org/10.1107/S2053230X1600279X
Montigny, C., Lyons, J., Champeil, P., Nissen, P. & Lenoir, G. (2016). On the molecular mechanism of flippase- and scramblase-mediated phospholipid transport. B B A - Molecular and Cell Biology of Lipids, 1861(8, Part B), 767-783. https://doi.org/10.1016/j.bbalip.2015.12.020
David-Bosne, S., Voldsgaard Clausen, M., Poulsen, H., Møller, J. V., Nissen, P. & le Maire, M. (2016). Reappraising the effects of artemisinin on the ATPase activity of PfATP6 and SERCA1a E255L expressed in Xenopus laevis oocytes. Nature Structural and Molecular Biology, 23(1), 1-2. https://doi.org/10.1038/nsmb.3156
Gregersen, J. L., Fedosova, N., Nissen, P. & Boesen, T. (2016). Reconstitution of Na,K-ATPase in Nanodiscs. Methods in Molecular Biology, 1377, 403-409. https://doi.org/10.1007/978-1-4939-3179-8_36
Horrocks, M. H., Lee, S. F., Gandhi, S., Magdalinou, N. K., Chen, S. W., Devine, M. J., Tosatto, L., Kjaergaard, M., Beckwith, J. S., Zetterberg, H., Iljina, M., Cremades, N., Dobson, C. M., Wood, N. W. & Klenerman, D. (2016). Single-molecule imaging of individual amyloid protein aggregates in human biofluids. ACS Chemical Neuroscience, 7(3), 399–406. https://doi.org/10.1021/acschemneuro.5b00324
Voldsgaard Clausen, M., Nissen, P. & Poulsen, H. (2016). The α4 isoform of the Na+ ,K+ -ATPase is tuned for changing extracellular environments. FEBS journal, 283(2), 282-293. https://doi.org/10.1111/febs.13567
Hilbers, F., Kopec, W., Isaksen, T. J., Holm, T. H., Lykke-Hartmann, K., Nissen, P., Khandelia, H. & Poulsen, H. (2016). Tuning of the Na,K-ATPase by the beta subunit. Scientific Reports, 6(20442), Artikel 20442. https://doi.org/10.1038/srep20442
Vöge, M., Pfaffhuber, A., Auken, E., Kirkegaard, C., Boesen, T., Hendricks, S. & Hunkeler, P. (2015). 5D inversion of sea ice thickness from helicopter EM data. I 1st European Airborne Electromagnetics Conference: Held at Near Surface Geoscience 2015 (s. 41-45). European Association of Geoscientists and Engineers.
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
Shammas, S. L., Garcia, G. A., Kumar, S., Kjaergaard, M., Horrocks, M. H., Shivji, N., Mandelkow, E., Knowles, T. P. J., Mandelkow, E. & Klenerman, D. (2015). A mechanistic model of tau amyloid aggregation based on direct observation of oligomers. Nature Communications, 6, 7025. https://doi.org/10.1038/ncomms8025
Mattle, D., Zhang, L., Sitsel, O., Pedersen, L. T., Moncelli, M. R., Tadini-Buoninsegni, F., Gourdon, P., Rees, D. C., Nissen, P. & Meloni, G. (2015). A sulfur-based transport pathway in Cu+-ATPases. E M B O Reports, 728-740. https://doi.org/10.15252/embr.201439927
Kjærgaard, M. (2015). Can proteins be intrinsically disordered inside a membrane? Intrinsically Disordered Proteins, 3(1), 1-7. Artikel e984570. https://doi.org/10.4161/21690707.2014.984570

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Revideret 13.11.2025
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Helene Eriksen