Aarhus Universitets segl

Neurobiologi

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

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
Nass, K., Foucar, L., Barends, T. R. M., Hartmann, E., Botha, S., Shoeman, R. L., Doak, R. B., Alonso-Mori, R., Aquila, A., Bajt, S., Barty, A., Bean, R., Beyerlein, K. R., Bublitz, M., Drachmann, N., Gregersen, J., Jönsson, H. O., Kabsch, W., Kassemeyer, S. ... Schlichting, I. (2015). Indications of radiation damage in ferredoxin microcrystals using high-intensity X-FEL beams. Journal of Synchrotron Radiation, 22(2), 225-238. https://doi.org/10.1107/S1600577515002349
Valle, M., Zavialov, A., Li, W., Stagg, S. M., Sengupta, J., Nielsen, R. C., Nissen, P., Harvey, S. C., Ehrenberg, M. & Frank, J. (2003). Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy. Nat. Struct. Biol. ,10, 899-906.