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A structural overview of the plasma membrane Na+,K+-ATPase and H+-ATPase ion pumps. / Morth, Jens Preben ; Pedersen, Bjørn Panella ; Buch-Pedersen, Morten Jeppe ; Andersen, Jens Peter ; Vilsen, Bente ; Palmgren, Michael G ; Nissen, Poul.
In: Nature Reviews. Molecular Cell Biology, Vol. 12, 01.2011, p. 60-70.Publication: Research - peer-review › Journal article
Crystal structure of a copper-transporting PIB-type ATPase. / Gourdon, Pontus ; Liu, Xiang-Yu ; Skjørringe, Tina ; Morth, J Preben ; Møller, Lisbeth Birk ; Pedersen, Bjørn Panyella ; Nissen, Poul.
In: Nature, Vol. 475, No. 7354, 2011, p. 59-64.Publication: Research - peer-review › Journal article
Crystal structure of a plasma membrane proton pump. / Pedersen, Bjørn Panyella (Inventor) ; Buch-Pedersen, Morten (Inventor) ; Palmgren, Michael G. (Inventor) ; Nissen, Poul (Inventor).
Patent No.: PCT/DK2008/050305. Dec 12, 2008.Publication: Research › Patent
Structural identification of cation binding pockets in the plasma membrane proton pump. / Ekberg, Kira ; Pedersen, Bjørn Panella ; Sørensen, Danny Mollerup ; Veierskov, Bjarke ; Nissen, Poul ; Palmgren, Michael ; Buch-Pedersen, Morten Jeppe.
In: National Academy of Sciences. Proceedings, Vol. 107, 2010, p. 21400-21405.Publication: Research - peer-review › Journal article
Structural identification of cation binding pockets in the plasma membrane proton pump. / Ekberg, Kira ; Pedersen, Bjørn P ; Sørensen, Danny Mollerup ; Nielsen, Ann Kallehauge ; Veierskov, Bjarke ; Nissen, Poul ; Palmgren, Michael G ; Buch-Pedersen, Morten Jeppe.
In: National Academy of Sciences. Proceedings, Vol. 107, No. 50, 2010, p. 21400-5.Publication: Research - peer-review › Journal article
Structure determination using poorly diffracting membrane protein crystals - Lessons from the H+ and Na+,K+-ATPases. / Pedersen, Bjørn Panyella ; Morth, Jens Preben ; Nissen, Poul.
In: Acta Crystallographica. Section D: Biological Crystallography, Vol. 66, 2010, p. 309-313.Publication: Research - peer-review › Journal article
Automatic classification of P-Type ATPases using SLR. / Liboriussen, Poul ; Pedersen, Bjørn Panyella ; Ifrim, Georgiana ; Nissen, Poul ; Pedersen, Christian Storm.
2009. Poster session presented at 17th Annual International Conference on Intelligent Systems for Molecular Biology (ISMB) & 8th European Conference on Computational Biology (ECCB), Stockholm, Sweden.Publication: Research › Poster
P-type ATPases as drug targets: Tools for medicine and science. / Yatime, Laure ; Buch-Pedersen, Morten Jeppe ; Musgaard, Maria ; Morth, Jens Preben ; Winther, Anne-Marie Lund ; Pedersen, Bjørn Panyella ; Olesen, Claus Elsborg ; Andersen, Jens Peter ; Vilsen, Bente ; Schiøtt, Hanne Birgit ; Palmgren, Michael ; Møller, Jesper Vuust ; Nissen, Poul ; Fedosova, Natalya.
In: B B A - Bioenergetics, Vol. 1787, No. 4, 2009, p. 207-20.Publication: Research - peer-review › Journal article
Protons and how they are transported by proton pumps. / Buch-Pedersen, Morten Jeppe ; Pedersen, Bjørn Panyella ; Nissen, Poul ; Palmgren, Michael.
In: Pfluegers Archiv, Vol. 457, No. 3, 06.05.2008, p. 573-9.Publication: Research - peer-review › Journal article
Structural and biochemical strudies of a proton ATPase and a heavy metal ATPase. / Pedersen, Bjørn Panyella.
2008. 228 p.Publication: Research › Ph.d. thesis
Crystal structure of the plasma membrane proton pump.. / Pedersen, Bjørn Panyella ; Buch-Pedersen, Morten J ; Morth, Jens Preben ; Palmgren, Mickey G ; Nissen, Poul.
In: Nature, Vol. 450, No. 7172, 2007, p. 1111-1114.Publication: Research - peer-review › Journal article
The university’s website is being redesigned. The design and content will therefore change, and you may experience for a while that old and new sections are mixed together, and that the content is not in its usual place.
We hope that the new website will make up for any inconvenience, and that you will enjoy greater coherence throughout and find the website simpler to use.
In the time ahead, you will notice a mixture of old and new designs in the pages on the website.
In spring 2011, Aarhus University’s nine main academic areas were reduced to four, and the fifty-five departments became twenty-six. This was to unify the organisation and to strengthen the university’s interdisciplinary approach. We are now following suit by restructuring the entire website to ensure more coherence in the content and design.
Such an exercise takes time – and we hope you will bear with us!
Under the HOT KEY at the top right, you can find links to the most frequently used content on the website, as well as the two new universes for staff and students.

Use the new mega dropdowns to get an overview of the website’s content. They open when you run your mouse over the navigation at the top.
