Recombinant Rat Sodium channel protein type 4 subunit alpha (Scn4a), partial

1. Intramolecular distances computed from the LRET signals define a geometrical map of Nav1.4 with the bound toxins, and reveal voltage-dependent structural changes related to channel gating PMID: 28202723
2. the role of the intracellular IFM motif of rNav1.4 (skeletal muscle isoform of the rat Na(+) channel) on the alpha-beta1 functional interaction PMID: 28012039
3. Role of Asparagines in Coupling the Pore and Votage-Sensor Domain in Voltage-Gated Sodium Channels PMID: 26636939
4. The study constructs a homology model for the pore domain of the NaV1.4 channel and uses the functional data for the binding of micro-conotoxin GIIIA to NaV1.4 to validate the model. PMID: 25133704
5. The relationships between voltage sensors and pore conformations in an inactivation deficient Nav1.4 channel, were investigated. PMID: 23322038
6. Effectiveness of SkM1-based antiarrhythmic therapy critically depends on the delivery vehicle, with viral gene delivery seeming to be superior. PMID: 22722661
7. SkM1 gene transfer reduces the incidence of inducible ventricular tachycardia / ventricular fibrillation. PMID: 22374989
8. Anthopleurin elicited opposing effects on the gating mode, kinetics and charge immobilized during open- versus closed-state fast inactivation of Nav1.4 channels. PMID: 21099342
9. amino acid Ile-1575 in the middle of transmembrane segment 6 of domain IV in the adult rat skeletal muscle isoform of rNa(V)1.4 may act as molecular switch allowing for interaction between outer and inner vestibules PMID: 20926383
10. Our results demonstrated the unique permeability of guanidine through NaV1.4 gating pores, and defined voltage-dependent and voltage-independent block by divalent and trivalent cations, respectively. PMID: 20660662
11. To examine the block by mu-conotoxin KIIIA and its analogs of a sodium channel isoform, nine disulfide-depleted KIIIA-peptides are tested on NaV1.4. When mu-conotoxin binds to NaV1.4, it blocks the sodium current essentially completely. PMID: 20459109
12. Role of a conserved neighbouring tryptophan residue at position 736 (W736) of Na(V)1.4 in the pore formation was examined. W736 contributes to the formation of the pore, close to the mouth of the channel, but is not part of the selectivity filter. PMID: 12397382
13. Chimeric channels of NaV1.4 and NaV1.5 also indicated that the C-terminal domain is largely responsible for calmodulin effects on inactivation PMID: 15746172
14. We studied the properties of a sodium channel comprised only of S5-P-S6 region of the rat sodium channel alpha-subunit Nav1.4 (micro1pore). PMID: 15992775
15. low but significant levels of heme-specific transcriptional activity were observed at the hmuO promoter in the chrAS mutants, suggesting that an additional heme-dependent activator is involved in hmuO expression PMID: 16239540
16. Data suggest that modulation of the sodium current by the expression of the highly sialylated beta1-subunit may alter the channel gating by increasing the density of surface negative charges in the vicinity of the sodium channel voltage sensing machinery. PMID: 16432696
17. We demonstrate that a pH-independent current is found in Na(V)1.4, but not in the cardiac isoform (Na(V)1.5). PMID: 16873405
18. an energetically equivalent cation-pi interaction underlies both use-dependent and tonic block of Nav1.4 by TTX PMID: 17237232
19. The mutation R663H permits transmembrane permeation of protons, but not larger cations, similar to the conductance displayed by histidine substitution at Shaker K(+) channel S4 sites. PMID: 17591984
20. Binding of beta-scorpion toxin modifies Nav1.4 channel function and provides insight into early gating transitions of sodium channels. PMID: 17698594
21. muO conotoxins inhibit NaV1.4 channels by interfering with their voltage sensors in domain-2. PMID: 18698149
22. Missense mutations R666G, R663H,R666S and R666C (respectively) result in a low-amplitude inward current at the resting potential that may lead to the pathological sarcolemmal depolarization during attacks of weakness in hypokalemic periodic paralysis . PMID: 18824591
23. Expression of skeletal SkM1 but not cardiac SCN5A Na+ channel isoform preserves normal conduction in a depolarized cardiac syncytium. PMID: 18977767
24. Potassium-sensitive normokalemic periodic paralysis mutations in rat Na(V)1.4 (R669Q/G/W) cause gating pore current that is activated by depolarization and therefore is conducted in the activated state of the voltage sensor. PMID: 19052238
25. Data demonstrate that arachidonic acid (AA), but not the metabolic products of AA, can voltage-dependently modulate rNa(V)1.4 currents. PMID: 19097141

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KEGG: rno:25722

STRING: 10116.ENSRNOP00000016841

UniGene: Rn.9700