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- Publications
- Influence
The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pump.
- J. Møller, C. Olesen, A. L. Winther, P. Nissen
- Chemistry, Medicine
- Quarterly reviews of biophysics
- 1 November 2010
The sarcoplasmic (SERCA 1a) Ca2+-ATPase is a membrane protein abundantly present in skeletal muscles where it functions as an indispensable component of the excitation-contraction coupling, being at… Expand
The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm
- A. L. Winther, M. Bublitz, +4 authors M. Buch-Pedersen
- Biology, Medicine
- Nature
- 14 March 2013
The contraction and relaxation of muscle cells is controlled by the successive rise and fall of cytosolic Ca2+, initiated by the release of Ca2+ from the sarcoplasmic reticulum and terminated by… Expand
The structural basis of calcium transport by the calcium pump
The sarcoplasmic reticulum Ca2+-ATPase, a P-type ATPase, has a critical role in muscle function and metabolism. Here we present functional studies and three new crystal structures of the rabbit… Expand
Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation
- M. Quick, A. L. Winther, L. Shi, P. Nissen, H. Weinstein, J. Javitch
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences
- 7 April 2009
The first crystal structure of the neurotransmitter/sodium symporter homolog LeuT revealed an occluded binding pocket containing leucine and 2 Na+; later structures showed tricyclic antidepressants… Expand
Chloride binding site of neurotransmitter sodium symporters
- A. K. Kantcheva, M. Quick, +5 authors P. Nissen
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences
- 2 May 2013
Neurotransmitter:sodium symporters (NSSs) play a critical role in signaling by reuptake of neurotransmitters. Eukaryotic NSSs are chloride-dependent, whereas prokaryotic NSS homologs like LeuT are… Expand
Critical Roles of Hydrophobicity and Orientation of Side Chains for Inactivation of Sarcoplasmic Reticulum Ca2+-ATPase with Thapsigargin and Thapsigargin Analogs*
- A. L. Winther, H. Liu, +7 authors J. Møller
- Chemistry, Medicine
- The Journal of Biological Chemistry
- 15 June 2010
Thapsigargin (Tg), a specific inhibitor of sarco/endoplasmic Ca2+-ATPases (SERCA), binds with high affinity to the E2 conformation of these ATPases. SERCA inhibition leads to elevated calcium levels… Expand
Identification of Antifungal H+-ATPase Inhibitors with Effect on Plasma Membrane Potential
- L. Kjellerup, S. Gordon, K. O. Cohrt, W. D. Brown, A. Fuglsang, A. L. Winther
- Chemistry, Medicine
- Antimicrobial Agents and Chemotherapy
- 24 April 2017
ABSTRACT The plasma membrane H+-ATPase (Pma1) is an essential fungal protein and a proposed target for new antifungal medications. The compounds in a small-molecule library containing ∼191,000… Expand
A first low-resolution difference Fourier map of phosphorus in a membrane protein from near-edge anomalous diffraction.
- P. Boesecke, J. M. Bois, +12 authors H. Stuhrmann
- Chemistry, Medicine
- Journal of synchrotron radiation
- 1 September 2009
Crystal diffraction of three membrane proteins (cytochrome bc(1) complex, sarcoplasmic reticulum Ca(2+) ATPase, ADP-ATP carrier) and of one nucleoprotein complex (leucyl tRNA synthetase bound to… Expand
Tetrahydrocarbazoles are a novel class of potent P-type ATPase inhibitors with antifungal activity
- Maike Bublitz, L. Kjellerup, +8 authors A. L. Winther
- Chemistry, Medicine
- PloS one
- 2 January 2018
We have identified a series of tetrahydrocarbazoles as novel P-type ATPase inhibitors. Using a set of rationally designed analogues, we have analyzed their structure-activity relationship using… Expand