Issues
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Cover Image
Cover Image
Cover picture: Crystal structure of the sodium–proton antiporter, NhaA homodimer (green and brown), simulated in a 1-palmitoyl-2-oleoylphosphatidylcholine (POPC) lipid bilayer (white). The image shows the periplasmic-facing side after about 1 μs of molecular dynamics simulation. The roles of conserved charged residues (shown in sticks) in the transport mechanism were elucidated using a combination of x-ray crystallography and MD simulations (see research article by Lee et al., 529–544).
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Generally Physiological
Editorial
Commentary
Article
Stargazin promotes closure of the AMPA receptor ligand-binding domain
Stargazin enhances closure of the AMPA receptor ligand-binding domain, thereby facilitating channel activation.
Capturing distinct KCNQ2 channel resting states by metal ion bridges in the voltage-sensor domain
The KCNQ2 channel can exist in multiple resting conformations.
Crystal structure of the sodium–proton antiporter NhaA dimer and new mechanistic insights
A dimeric structure of the sodium–proton antiporter NhaA provides insight into the roles of Asp163 and Lys300 in the transport mechanism.
Volatile anesthetics inhibit sodium channels without altering bulk lipid bilayer properties
Volatile anesthetics act directly on neuronal sodium channels, independently of effects on the lipid bilayer.
Communication
Juxtaposition of the changes in intracellular calcium and force during staircase potentiation at 30 and 37°C
Temperature-dependent changes in basal calcium and in the calcium transient contribute to force potentiation during repetitive stimulation.
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