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  • Mutation
  • This project used whole cell voltage clamp of heterologously-expressed NaV1.1-5A and 5N to compare the intrinsic properties of the splice variants, their modulation by AEDs, their interaction with a published epilepsy mutation (R1648H), their modulation by G-proteins and how they responded to co-expression of sodium channel β subunits. (ucl.ac.uk)
  • Inclusion of the mutation R1648H also eradicated the difference by disproportionately slowing the recovery of NaV1.1-5N. (ucl.ac.uk)
  • Function
  • Here we review the current pre-clinical and clinical evidence to reveal how the nine NaV channel family members (NaV1.1-NaV1.9) contribute to abdominal visceral function in normal and disease states. (edu.au)
  • interactions
  • Additionally, investigators studied the varying behavioral phenotypes and found that deletion of Nav1.1 in SST-expressing interneurons contributes to hyperactivity while deletion in PV-expressing interneurons results in impaired social interactions. (pediatricneurologybriefs.com)
  • several
  • This difference in recovery was conferred by a single amino acid substitution that is conserved in several sodium channels that are alternatively spliced at this site, and the difference was obscured in the presence of the common AED, phenytoin. (ucl.ac.uk)
  • component
  • It acts by shifting the voltage dependence of channel activation to more depolarized potentials and by blocking the inward component of the sodium current (PubMed:16267209). (rcsb.org)
  • state
  • Interestingly, inhibitory compounds often exhibit different pharmacological profiles dependent upon the conformational state of the ion channel. (sophion.com)