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Binding and Orientation of Tricyclic Antidepressants within the Central Substrate Site of the Human Serotonin Transporter*
Tricyclic antidepressants (TCAs) have been used for decades, but their orientation within and molecular interactions with their primary target is yet unsettled. The recent finding of a TCA bindingExpand
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Ion Pathways in the Sarcoplasmic Reticulum Ca2+-ATPase*
The sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) is a transmembrane ion transporter belonging to the PII-type ATPase family. It performs the vital task of re-sequestering cytoplasmic Ca2+ to theExpand
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Distinct Structural Pathways Coordinate the Activation of AMPA Receptor-Auxiliary Subunit Complexes
Summary Neurotransmitter-gated ion channels adopt different gating modes to fine-tune signaling at central synapses. At glutamatergic synapses, high and low activity of AMPA receptors (AMPARs) isExpand
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P-type ATPases as drug targets: tools for medicine and science.
P-type ATPases catalyze the selective active transport of ions like H+, Na+, K+, Ca2+, Zn2+, and Cu2+ across diverse biological membrane systems. Many members of the P-type ATPase protein family,Expand
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Tracing cytoplasmic Ca(2+) ion and water access points in the Ca(2+)-ATPase.
Sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) transports two Ca(2+) ions across the membrane of the sarco(endo)plasmic reticulum against the concentration gradient, harvesting the requiredExpand
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Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes.
The structural elucidation of membrane proteins continues to gather pace, but we know little about their molecular interactions with the lipid environment or how they interact with the surroundingExpand
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Role of the Cys Loop and Transmembrane Domain in the Allosteric Modulation of α4β2 Nicotinic Acetylcholine Receptors*
Allosteric modulators of pentameric ligand-gated ion channels are thought to act on elements of the pathways that couple agonist binding to channel gating. Using α4β2 nicotinic acetylcholineExpand
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Ion Pathways in the Sarcoplasmic Reticulum
Published, JBC Papers in Press, February 11, 2013, DOI 10.1074/jbc.R112.436550 Maike Bublitz, Maria Musgaard, Hanne Poulsen, Lea Thøgersen , Claus Olesen**, Birgit Schiøtt, J. Preben Morth, JesperExpand
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Kainate receptor pore‐forming and auxiliary subunits regulate channel block by a novel mechanism
Key points Kainate receptor heteromerization and auxiliary subunits, Neto1 and Neto2, attenuate polyamine ion‐channel block by facilitating blocker permeation. Relief of polyamine block inExpand
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Promiscuous attraction of ligands within the ATP binding site of RyR2 promotes diverse gating behaviour
ATP is an essential constitutive regulator of cardiac ryanodine receptors (RyR2), enabling small changes in cytosolic Ca2+ to trigger large changes in channel activity. With recent landmarkExpand
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