| 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 | Mapping of voltage sensor positions in resting and inactivated mammalian sodium channels by LRET.
Kubota T, Durek T, Dang B, Finol-Urdaneta RK, Craik DJ, Kent SB, French RJ, Bezanilla F, Correa AM., Free PMC Article | 04/14/2018 |
| the role of the intracellular IFM motif of rNav1.4 (skeletal muscle isoform of the rat Na(+) channel) on the alpha-beta1 functional interaction | Characterization of specific allosteric effects of the Na(+) channel β1 subunit on the Na(v)1.4 isoform.
Sánchez-Solano A, Islas AA, Scior T, Paiz-Candia B, Millan-PerezPeña L, Salinas-Stefanon EM. | 09/9/2017 |
| Role of Asparagines in Coupling the Pore and Votage-Sensor Domain in Voltage-Gated Sodium Channels | Important Role of Asparagines in Coupling the Pore and Votage-Sensor Domain in Voltage-Gated Sodium Channels.
Sheets MF, Fozzard HA, Hanck DA., Free PMC Article | 09/17/2016 |
| 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. | Molecular dynamics study of binding of µ-conotoxin GIIIA to the voltage-gated sodium channel Na(v)1.4.
Mahdavi S, Kuyucak S., Free PMC Article | 12/12/2015 |
| The relationships between voltage sensors and pore conformations in an inactivation deficient Nav1.4 channel, were investigated. | Multiple pore conformations driven by asynchronous movements of voltage sensors in a eukaryotic sodium channel.
Goldschen-Ohm MP, Capes DL, Oelstrom KM, Chanda B., Free PMC Article | 06/22/2013 |
| Effectiveness of SkM1-based antiarrhythmic therapy critically depends on the delivery vehicle, with viral gene delivery seeming to be superior. | Effect of skeletal muscle Na(+) channel delivered via a cell platform on cardiac conduction and arrhythmia induction.
Boink GJ, Lu J, Driessen HE, Duan L, Sosunov EA, Anyukhovsky EP, Shlapakova IN, Lau DH, Rosen TS, Danilo P, Jia Z, Ozgen N, Bobkov Y, Guo Y, Brink PR, Kryukova Y, Robinson RB, Entcheva E, Cohen IS, Rosen MR., Free PMC Article | 10/27/2012 |
| SkM1 gene transfer reduces the incidence of inducible ventricular tachycardia / ventricular fibrillation. | SkM1 and Cx32 improve conduction in canine myocardial infarcts yet only SkM1 is antiarrhythmic.
Boink GJ, Lau DH, Shlapakova IN, Sosunov EA, Anyukhovsky EP, Driessen HE, Dun W, Chen M, Danilo P Jr, Rosen TS, Őzgen N, Duffy HS, Kryukova Y, Boyden PA, Robinson RB, Brink PR, Cohen IS, Rosen MR., Free PMC Article | 09/22/2012 |
| Anthopleurin elicited opposing effects on the gating mode, kinetics and charge immobilized during open- versus closed-state fast inactivation of Nav1.4 channels. | Open- and closed-state fast inactivation in sodium channels: differential effects of a site-3 anemone toxin.
Groome J, Lehmann-Horn F, Holzherr B., Free PMC Article | 05/28/2011 |
| 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 | A molecular switch between the outer and the inner vestibules of the voltage-gated Na+ channel.
Zarrabi T, Cervenka R, Sandtner W, Lukacs P, Koenig X, Hilber K, Mille M, Lipkind GM, Fozzard HA, Todt H., Free PMC Article | 01/15/2011 |
| 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. | Ion permeation and block of the gating pore in the voltage sensor of NaV1.4 channels with hypokalemic periodic paralysis mutations.
Sokolov S, Scheuer T, Catterall WA., Free PMC Article | 11/13/2010 |
| 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. | μ-conotoxin KIIIA derivatives with divergent affinities versus efficacies in blocking voltage-gated sodium channels.
Zhang MM, Han TS, Olivera BM, Bulaj G, Yoshikami D., Free PMC Article | 08/9/2010 |
| Expression of skeletal SkM1 but not cardiac SCN5A Na+ channel isoform preserves normal conduction in a depolarized cardiac syncytium. | Expression of skeletal but not cardiac Na+ channel isoform preserves normal conduction in a depolarized cardiac syncytium.
Protas L, Dun W, Jia Z, Lu J, Bucchi A, Kumari S, Chen M, Cohen IS, Rosen MR, Entcheva E, Robinson RB., Free PMC Article | 01/21/2010 |
| 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 | Analysis of a heme-dependent signal transduction system in Corynebacterium diphtheriae: deletion of the chrAS genes results in heme sensitivity and diminished heme-dependent activation of the hmuO promoter.
Bibb LA, King ND, Kunkle CA, Schmitt MP., Free PMC Article | 01/21/2010 |
| Data demonstrate that arachidonic acid (AA), but not the metabolic products of AA, can voltage-dependently modulate rNa(V)1.4 currents. | Modulation of muscle rNaV1.4 Na+ channel isoform by arachidonic acid and its non-metabolized analog.
Gu H, Fang YJ, He YL, Sun J, Zhu J, Mei YA. | 01/21/2010 |
| 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. | Depolarization-activated gating pore current conducted by mutant sodium channels in potassium-sensitive normokalemic periodic paralysis.
Sokolov S, Scheuer T, Catterall WA., Free PMC Article | 01/21/2010 |
| 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 . | Gating pore currents in DIIS4 mutations of NaV1.4 associated with periodic paralysis: saturation of ion flux and implications for disease pathogenesis.
Struyk AF, Markin VS, Francis D, Cannon SC., Free PMC Article | 01/21/2010 |
| muO conotoxins inhibit NaV1.4 channels by interfering with their voltage sensors in domain-2. | muO conotoxins inhibit NaV channels by interfering with their voltage sensors in domain-2.
Leipold E, DeBie H, Zorn S, Borges A, Olivera BM, Terlau H, Heinemann SH. | 01/21/2010 |
| Binding of beta-scorpion toxin modifies Nav1.4 channel function and provides insight into early gating transitions of sodium channels. | beta-Scorpion toxin modifies gating transitions in all four voltage sensors of the sodium channel.
Campos FV, Chanda B, Beirão PS, Bezanilla F., Free PMC Article | 01/21/2010 |
| 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. | A Na+ channel mutation linked to hypokalemic periodic paralysis exposes a proton-selective gating pore.
Struyk AF, Cannon SC., Free PMC Article | 01/21/2010 |
| 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). | Minimal sodium channel pore consisting of S5-P-S6 segments preserves intracellular pharmacology.
Pincin C, Ferrera L, Moran O. | 01/21/2010 |
| We demonstrate that a pH-independent current is found in Na(V)1.4, but not in the cardiac isoform (Na(V)1.5). | Isoform-dependent interaction of voltage-gated sodium channels with protons.
Khan A, Kyle JW, Hanck DA, Lipkind GM, Fozzard HA., Free PMC Article | 01/21/2010 |
| 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. | Beta1-subunit modulates the Nav1.4 sodium channel by changing the surface charge.
Ferrera L, Moran O. | 01/21/2010 |
| an energetically equivalent cation-pi interaction underlies both use-dependent and tonic block of Nav1.4 by TTX | A cation-pi interaction discriminates among sodium channels that are either sensitive or resistant to tetrodotoxin block.
Santarelli VP, Eastwood AL, Dougherty DA, Horn R, Ahern CA. | 01/21/2010 |
| Chimeric channels of NaV1.4 and NaV1.5 also indicated that the C-terminal domain is largely responsible for calmodulin effects on inactivation | Modulation of skeletal and cardiac voltage-gated sodium channels by calmodulin.
Young KA, Caldwell JH., Free PMC Article | 01/21/2010 |
| 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. | A tryptophan residue (W736) in the amino-terminus of the P-segment of domain II is involved in pore formation in Na(v)1.4 voltage-gated sodium channels.
Carbonneau E, Vijayaragavan K, Chahine M. | 01/21/2010 |