Poul Nissen

A collection of P-type ATPase structures from the Nissen lab. Figure courtesy of Dr. Oleg Sitsel.

Research

Nissen group - Structural and Functional Studies of Membrane Proteins in Brain

The Nissen group investigates molecular mechanisms of membrane transport processes, receptors, and biomembrane ultrastructure. Activities are mainly focused on cryo-electron microscopy (Cryo-EM), protein crystallography, biochemistry, electrophysiology, and include also small-angle X-ray scattering and cryo-electron tomography. Main subjects of research concern membrane transporters and receptors involved with neurological and psychiatric disorders, i.e. P-type ATPase (Na,K-ATPase, Ca-ATPases, lipid flippases, P5-ATPases), Na+ dependent neurotransmitter and chloride transporters, and insulin receptor signaling. studies include also structure based drug discovery and protein engineering. Biomembrane ultrastructures of neurons focus on axons and synapses associated with memory.

Our investigations link also to translational studies of neurological and psychiatric disorders associated with perturbed ion transport or metabolic control.

Methods development and integrative structural biology and bioimaging is also of great interest to the group.

Research Areas: Membrane proteins, Membrane transport and signaling, single-particle Cryo-EM, Cryo-Electron Tomography, Crystallography, Biochemistry, Drug discovery

Movies

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Group photo Nissen lab (2025)

Structural Biology - past, present and future by Peter Moore

Read the article by Peter Moore

Publications

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Hjorth-Jensen, S. J., Oksanen, E., Nissen, P. & Sørensen, T. L. M. (2020). Prospects for membrane protein crystals in NMX. I P. C. E. Moody (red.), Neutron Crystallography in Structural Biology (s. 47-68). Elsevier. https://doi.org/10.1016/bs.mie.2019.11.019

Dyla, M., Kjærgaard, M., Poulsen, H. & Nissen, P. (2020). Structure and Mechanism of P-Type ATPase Ion Pumps. Annual Review of Biochemistry, 89, 583-603. https://doi.org/10.1146/annurev-biochem-010611-112801

Nissen, P. (2020). The a-minor motif. I Structural Insights into Gene Expression and Protein Synthesis (s. 461-463). World Scientific. https://doi.org/10.1142/9789811215865_0055

Geurts, M. M. G., Clausen, J. D., Arnou, B., Montigny, C., Lenoir, G., Corey, R. A., Jaxel, C., Møller, J. V., Nissen, P., Andersen, J. P., Le Maire, M. & Bublitz, M. (2020). The SERCA residue Glu340 mediates interdomain communication that guides Ca²⁺transport. Proceedings of the National Academy of Sciences (PNAS), 117(49), 31114-31122. https://doi.org/10.1073/pnas.2014896117

Ravishankar, H., Pedersen, M. N., Eklund, M., Sitsel, A., Li, C., Duelli, A., Levantino, M., Wulff, M., Barth, A., Olesen, C., Nissen, P. & Andersson, M. (2020). Tracking Ca²⁺ ATPase intermediates in real time by x-ray solution scattering. Science Advances, 6(12), Artikel eaaz0981. https://doi.org/10.1126/sciadv.aaz0981

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Affiliated researcher of DANDRITE

The Danish Research Institute of Translational Neuroscience (DANDRITE) is the Danish node of the Nordic EMBL Partnership for Molecular Medicine. DANDRITE was established by Lundbeckfonden and Aarhus University in 2013 and performs basic and translational research in brain and the nervous system.

Partner of PROMEMO

PROMEMO is a Danish National Research Foundation Center of Excellence, studying the fundamental traits of learning and memory in healty and diseased brains.