The structure of the membrane-integrated components of a unique substrate decarboxylation-driven primary-active sodium pump provides insights into its transport mechanism.
Biochemical and genetic tests have revealed that a liver protein called NTCP is a functional receptor for hepatitis B and D viruses, which should lead to an improved understanding of the infections caused by these viruses and assist the development of new intervention strategies.
Kinetic interactions between sodium channels and auxiliary factors create a molecular computational engine that can sense and regulate cellular excitability.
Not all members of the bacteria sodium channel family are sodium channels - those found in Bacillus are highly adaptable and can be converted into many selectivity types.
The high-resolution x-ray structure of an asymmetrical SeCitS dimer, present in the inward- and outward-facing state, provides a complete mechanism of substrate and ion translocation in a sodium-dependent symporter.
Modifying membrane potential by an 'inhibitory' chloride conductance such as PSAM4-GlyR is inherently unstable because the normally low intracellular concentration of chloride is readily increased by influx of chloride.
The first structure of the human epithelial sodium channel provides vital insight into the assembly, stoichiometry and molecular mechanism of the ion channel central to sodium homeostasis.
The mRNA that encodes a Drosophila sodium channel enables neurons to adapt to acute temperature changes, via a mechanism independent of its protein-coding role.
A cationic molecule derived from an uncharged Cav2.2 calcium channel inhibitor powerfully inhibits both sodium and calcium channels with extracellular application and inhibits both pain and neurogenic inflammation.
