ライフサイエンスコーパス: VSD

1 VSD binding enhances secretion in vivo subject to voltag

2 VSD charge displacements within the membrane electric fi

3 VSD imaging may thus be a promising technique to trace T

4 VSD IV did not appear to participate in channel opening.

5 VSD-to-PD coupling is not fully explained by far connect

6 VSDs consist of four transmembrane segments, S1-S4, form

7 VSDs sense changes in the transmembrane voltage and conv

8 ong molecular dynamics simulations of Kv 1.2-VSD in LPPG micelles and a 1-palmitoyl-2-oleoyl-glycero-

9 1 may strengthen the coupling between hKv1.3-VSD movement and pore opening, inducing the modification

10 rth transmembrane helix (S4) of the Na(V)1.4 VSDs can result in a leak current through the VSD and hy

11 tively, were compared with 3103 ASD and 4180 VSD patients nationally.

12 s reveal novel mechanisms whereby the NaV1.5 VSDs regulate channel activation and inactivation.

13 lividans) as a surrogate because it lacks a VSD and exhibits an activation coupled to C-type inactiv

14 itial step that makes the resting state of a VSD accessible to a variety of biophysical and structura

15 ly independent but biased by VSD activation, VSDs II and III were each found to supply approximately

16 subject to voltage, and mutations affecting VSD conformation alter binding and secretion in parallel

17 ange in exercise function was observed after VSD closure, except for increased peak oxygen (O(2)) pul

18 inding to a single alpha-subunit affects all VSDs equally.

19 lecular dynamics simulations suggest altered VSD exposure to membrane lipids.

20 P2 in coupling retigabine binding to altered VSD function.

21 mechanical circulatory support (MCS) for AMI-VSD is unknown.

22 n choosing a percutaneous MCS device for AMI-VSD.

23 cutaneous MCS normalized hemodynamics in AMI-VSD, pulmonary capillary wedge pressure and shunting wer

24 provides the optimal form of support in AMI-VSD.

25 lidated cardiovascular model to simulate AMI-VSD with parameters adjusted to replicate average hemody

26 rameters reported in the literature with AMI-VSD.

27 n and 89 children at MSMC undergoing ASD and VSD closure, respectively, were compared with 3103 ASD a

28 n costs fell by 33% and 35% at MSMC (ASD and VSD, respectively), whereas they rose by 16% to 17% nati

29 ra (length of stay, 1 and 3 days for ASD and VSD, respectively).

30 getic interaction between Ca(2+) binding and VSD activation by investigating the effects of internal

31 ltage dependence of both channel opening and VSD activation, reported by a fluorophore labeling posit

32 ures during the third month of pregnancy and VSD in two pollution model.Our results contribute to the

33 y the interaction between Ca(2+) sensors and VSDs.

34 n of the voltage dependence of the available VSD structures, at present, they all represent the activ

35 ally highly significant correlations between VSD function and physicochemical properties of gating po

36 al underpinnings of the relationship between VSD movement and fluorophore response remain unclear.

37 An applied bias VSD leads to multiple Andreev reflections (MAR), which i

38 ence of membrane potential, toxins that bind VSD and modulate the gating behavior of K(v) channels ex

39 g is intrinsically independent but biased by VSD activation, VSDs II and III were each found to suppl

40 -dependent gating of K(V)7.1 as triggered by VSD activations to the intermediate and then activated s

41 fferent mechanisms, other than the canonical VSD-pore coupling, are at work in voltage-dependent ion

42 in (VSD) with strong similarity to canonical VSDs in voltage-dependent cation channels and enzymes.

43 tion of the structure of a potassium channel VSD in the intermediate state has previously proven elus

44 human KCNQ1 voltage-gated potassium channel VSD in the intermediate state.

45 bset of plant SNAREs commandeer K(+) channel VSDs to coordinate membrane trafficking with K(+) uptake

46 pollutant model, associations with all CHDs, VSD, and TF for O3 were generally consistent compared to

47 Ci-VSD can be reconstituted into liposomes of various compo

48 protocol for the expression of eukaryotic Ci-VSD in Escherichia coli at milligram levels.

49 relaxation EPR spectroscopy measurement, Ci-VSD reconstitutes essentially randomly in proteoliposome

50 site for generating sufficient amounts of Ci-VSD protein for high-resolution structural studies.

51 ined model of the hHv1 dimer based on the Ci-VSD structure at resting state.

52 oltage dependence of the VSD from Ci-VSP (Ci-VSD) is dramatically right shifted, so that at 0 mV it p

53 like VGKC show domain-swapped configuration: VSD of one subunit is covalently connected to its PD by

54 Our cohort contained VSD data on 250 601 infants, including 186 502 children

55 After adjusting for covariates (VSD site, age at last dose, sex, and calendar month of t

56 rganizations in the Vaccine Safety Datalink (VSD) project.

57 and enrolled in the Vaccine Safety Datalink (VSD) through November 2009.

58 oband, as well as ventricular septal defect (VSD) and double-outlet right ventricle (DORV).

59 Transcatheter ventricular septal defect (VSD) closure is a safe and efficacious alternative to su

60 Ventricular septal defect (VSD) is a lethal complication of acute myocardial infarc

61 defect (ASD) and ventricular septal defect (VSD) surgeries in children 2 months to 19 years of age a

62 sed risk of CHDs, ventricular septal defect (VSD), and tetralogy of fallot (TF) with increasing O3 ex

63 ith no associated ventricular septal defect (VSD).

64 ical closure of a ventricular septal defect (VSD).

65 Intramural ventricular septal defects (VSDs) are interventricular communications through right

66 Ventricular septal defects (VSDs) were associated with the highest bromoform (aOR =

67 % penetrance and ventricular septal defects (VSDs) with ~15% penetrance; Fz2(+/-);Fz7(-/-) mice exhib

68 termed muscular ventricular septal defects (VSDs), are common, yet less is known about how they aris

69 dition, the stabilization of the depolarized VSD conformation, a hallmark for most Kv channels, requi

70 zes the activation sequence of the different VSDs of the Na(v)1.4 channel.

71 containing proteins may produce differential VSD relaxation in vivo.

72 utations slowed INa activation, although DII-VSD activation occurred at higher potentials (A735V) or

73 A735V shifted DII-VSD voltage dependence to depolarized potentials, wherea

74 ials, whereas G752R significantly slowed DII-VSD kinetics.

75 current activation, indicating that the DII-VSD allosterically regulates the rate of INa activation

76 We then used the DII-VSD construct to probe the molecular pathology of 2 Brug

77 acellular media within the DI, DII, and DIII VSDs are approximately 2 A long, similar to those of K(v

78 In particular, DIII-VSD deactivation kinetics were modulated by depolarizing

79 d trans-fascial staining of the CN by direct VSD administration.

80 nnels we show functional data distinguishing VSD-to-PD far from near connections.

81 conformational changes within the 4 (DI-DIV) VSDs to define molecular mechanisms of NaV1.5 modulation

82 ontains a functional voltage-sensing domain (VSD) and a phosphatase domain.

83 g a proton-permeable voltage-sensing domain (VSD) and lacking the pore domain typical of other voltag

84 ardiac Na(+) channel voltage-sensing domain (VSD) conformational dynamics simultaneously with other g

85 The voltage-sensing domain (VSD) is a conserved structural module that regulates the

86 The voltage-sensing domain (VSD) is the common scaffold responsible for the function

87 1 interacts with the voltage sensing domain (VSD) of Kv1.3 through W172 in the transmembrane segment

88 the structure of the voltage-sensing domain (VSD) of the Kv1.2 potassium channel in the resting state

89 The voltage sensing domain (VSD) of the voltage-gated proton channel Hv1 mediates a

90 Subsequent voltage-sensing domain (VSD) relaxation, including inward, 15-angstrom S4-helix

91 the S4 helix of the voltage-sensing domain (VSD) that are displaced in response to changes in transm

92 (K(V)) channels, the voltage-sensing domain (VSD) undergoes sequential activation from the resting st

93 are carried out by a voltage-sensing domain (VSD) with strong similarity to canonical VSDs in voltage

94 al models of the Hv1 voltage-sensing domain (VSD), both in a hyperpolarized state and a depolarized s

95 the CNBD and channel voltage sensing domain (VSD), possibly acting as a sliding crank that converts t

96 ractions between the voltage-sensing domain (VSD), the Ca(2+)-binding sites, and the pore domain gove

97 teractions among the voltage sensing domain (VSD), the cytosolic domain (CTD), and the pore gate doma

98 main surrounded by a voltage-sensing domain (VSD), which is critical for sensing transmembrane potent

99 x S4 of the K(V) 1.2 voltage-sensing domain (VSD).

100 teractions within the voltage sensor domain (VSD) during membrane depolarization.

101 at interacts with the voltage-sensor domain (VSD) of domain IV.

102 alpha-helices of the voltage sensor domain (VSD) of Kv channels.

103 nzymes regulated by a voltage-sensor domain (VSD) related to the VSD found in voltage-gated ion chann

104 unit is composed of a voltage sensor domain (VSD), a central pore-gate domain, and a large cytoplasmi

105 the membrane-spanning voltage sensor domain (VSD), and the cNMP-dependent gating is mediated by the i

106 Gating charges in voltage-sensing domains (VSD) of voltage-sensitive ion channels and enzymes are c

107 Voltage sensor domains (VSD) are transmembrane proteins that respond to changes

108 y four nonidentical voltage-sensing domains (VSDs I-IV).

109 Voltage-sensing domains (VSDs) are membrane protein modules found in ion channels

110 whereby the NaV1.5 voltage-sensing domains (VSDs) are perturbed to pathologically or therapeutically

111 hanges of the KCNQ3 voltage-sensing domains (VSDs) in response to voltage, retigabine, and PIP2.

112 potential via their voltage-sensing domains (VSDs) that control the status of the S6 bundle crossing

113 It contains four voltage-sensing domains (VSDs) that regulate the opening of the pore domain and e

114 tionally couple the voltage-sensing domains (VSDs) to the pore.

115 Voltage-sensing domains (VSDs) underlie the movement of voltage-gated ion channel

116 x consisting of two voltage-sensing domains (VSDs), each containing a gated proton permeation pathway

117 t is a dimer of two voltage-sensing domains (VSDs), each containing a pore pathway, a voltage sensor

118 surrounded by four voltage sensing domains (VSDs).

119 controlled by four voltage-sensing domains (VSDs).

120 Voltage sensor domains (VSDs) are membrane-bound protein modules that confer vol

121 movement of all four voltage sensor domains (VSDs) followed by channel opening via a last concerted c

122 induce pores in the voltage-sensor domains (VSDs) of different VGICs and that these pores form more

123 membrane, binds the voltage sensor domains (VSDs) of K(+) channels to confer a voltage dependence on

124 Voltage sensor domains (VSDs) regulate ion channels and enzymes by transporting

125 ion channels feature voltage sensor domains (VSDs) that exist in three distinct conformations during

126 The S4 helix of voltage sensor domains (VSDs) transfers its gating charges across the membrane e

127 the channels include voltage-sensor domains (VSDs), their conductance is thought to be independent of

128 d of four homologous voltage sensor domains (VSDs; DI, DII, DIII, and DIV) in which their S4 segments

129 d model of intermediate conformations during VSD gating.

130 lation and wide-scale voltage sensitive dye (VSD) imaging in mice to map altered cortical connectivit

131 tials, we developed a voltage-sensitive dye (VSD) imaging technique based on a double-sided microscop

132 near-infrared cyanine voltage-sensitive dye (VSD) imaging, which visualizes membrane potential variat

133 optical imaging with voltage-sensitive dye (VSD) in an animal experimental setting using anaesthetiz

134 nses seen with RH1692 voltage sensitive dye (VSD), with similar signal amplitude.

135 Voltage sensitive fluorescent dyes (VSDs) are important tools for probing signal transductio

136 wever, the available voltage-sensitive dyes (VSDs) are not always spectrally compatible with newly av

137 Each VSD displayed unique kinetics, consistent with distinct

138 The emission of each VSD is shifted by at least 100 nm to the red of its one-

139 and the contribution to pore opening of each VSD remain largely unknown.

140 netics of conformational changes within each VSD, using voltage-clamp fluorometry.

141 r gating charge that originates from earlier VSD movements.

142 e transmembrane length of S4 from engineered VSDs expressed in Xenopus oocytes.

143 network as a whole, scaling the ChR2-evoked VSD responses from the stroke groups to match the sham g

144 % penetrance; Fz2(+/-);Fz7(-/-) mice exhibit VSDs with ~50% penetrance and cleft palate with less tha

145 est that gating in Hv1 is tuned by extensive VSD-VSD interactions between the gates and voltage senso

146 Here, we describe a series of 19 fluorinated VSDs based on the hemicyanine class of chromophores.

147 ned unchanged (3 days for ASD and 4 days for VSD) in the observed time periods.

148 VSD is unknown and open channel blockers for VSDs have not yet been identified.

149 voltage sensors, we discovered that the four VSDs of CaV1.2 channels undergo voltage-evoked conformat

150 ural model of the resting states of the four VSDs of Na(v)1.4 relaxed in their membrane/solution envi

151 open state, with a smaller contribution from VSD I ( approximately 16 meV).

152 of the hyperpolarized state of a functioning VSD and also a framework for understanding the dynamics

153 indings indicate that an intact alphaB helix/VSD interface is required for effective coupling of Ca(2

154 hich act as open channel blockers on the Hv1 VSD and find that a highly conserved phenylalanine in th

155 nidinothiazole derivatives block the two Hv1 VSDs in a cooperative way, and use one of the compounds

156 ically charged residues across a hydrophobic VSD constriction called the gating pore or hydrophobic p

157 c transport measurements of the interlayer I-VSD characteristics indicate that layer-indirect e-h pai

158 e altered the conformation of the Domain III VSD, which is the same VSD that many tested LQT3 mutatio

159 ion between the activation of the Domain III-VSD and the strength of the inhibition of the channel by

160 include drug interaction with the Domain III-VSD.

161 e for arginine as a mobile charge carrier in VSD.

162 n = 10), we collected spontaneous changes in VSD signal that reflect underlying membrane potential ch

163 demonstrate that poration is more likely in VSDs that are more hydrated and are electrostatically mo

164 We further show that pores in VSDs can expand into so-called complex pores, which beco

165 sly reported between THM4 and CVDs including VSDs.

166 repair of conotruncal anomalies, intramural VSDs are uniquely associated with postoperative morbidit

167 Forty-nine patients (11%) had intramural VSDs, and 207 (47%) had nonintramural VSDs.

168 It is important to recognize intramural VSDs in the postoperative period.

169 sessed the prevalence of residual intramural VSDs and their effect on postoperative course.

170 In addition, those with intramural VSDs had longer postoperative hospital length of stay co

171 Patients with intramural VSDs were more likely to reach the primary composite out

172 olecular dynamics simulation of the isolated VSD from the KvAP channel in a hydrated lipid bilayer on

173 el opening is dependent on activation of its VSDs.

174 hat a conformational change in the domain IV VSD after depolarization is necessary and sufficient to

175 n maximum of NBD-labeled loop region of KvAP-VSD (residues 110-117) suggests a significant change in

176 ddle motif in activated conformation of KvAP-VSD by site-directed fluorescence approaches, using the

177 SD appears to more closely resemble the KvAP-VSD.

178 ty of I287 are important to control the main VSD energy barrier underlying transitions between restin

179 Although the structures of many VSD-containing ion channels are now available, our under

180 t influence the susceptibility to membranous VSDs in Nkx2-5(+/-) animals.

181 the septum even in the absence of a muscular VSD.

182 pattern that is disrupted around a muscular VSD.

183 ted with the risk of membranous and muscular VSD in Nkx2-5(+/-) but not wild-type animals.

184 chromosome 6 locus overlaps one for muscular VSD susceptibility.

185 pan (Sspn) that affects the risk of muscular VSD in mice.

186 mutants have a higher incidence of muscular VSD than Nkx2-5(+/-) mice.

187 se cardiac malformations, including muscular VSDs.

188 ized to be the mechanistic basis of muscular VSDs.

189 to voltage and the photostability of the new VSDs in a series of experimental preparations ranging in

190 unit S4 residues is key for the noncanonical VSD-to-PD coupling.

191 amural VSDs, and 207 (47%) had nonintramural VSDs.

192 wed for residual intramural or nonintramural VSDs.

193 tcome compared with those with nonintramural VSDs or no residual VSD (14 of 49 [29%] versus 15 of 207

194 stay compared with those with nonintramural VSDs or no residual VSD (20 days [interquartile range, 1

195 Our findings suggest the applicability of VSD imaging for real-time, functional imaging guidance d

196 its, probably result from the enhancement of VSD function, as demonstrated by optically tracking VSD

197 utated subunits points to an independence of VSD movements, with each subunit incrementally contribut

198 nsible for the development and modulation of VSD relaxation.

199 an obligatory model, in which activation of VSDs II and III is necessary to open the pore.

200 fast kinetic components in the activation of VSDs II and III were compatible with the ionic current p

201 a, Wnt5a or Wnt11, an increased frequency of VSDs is observed with Dvl3, Wnt3a and Wnt11; an increase

202 le to overcome the inherent lipophilicity of VSDs by dynamic encapsulation and high-affinity ligands

203 ir formation can lead to severe unfolding of VSDs from the channel.

204 (2+) sensor occupancy has a strong impact on VSD activation through a coordinated interaction mechani

205 generated from GCaMP3 mice, GCaMP6s mice, or VSD sensors.

206 greement with the homologous region of other VSDs.

207 charge, thereby confirming that the reported VSD structure is likely an intermediate along the channe

208 A residual VSD was present in 256 of the 442 subjects (58%), of whi

209 actors for poor outcomes, including residual VSD size and operative complexity.

210 those with nonintramural VSDs or no residual VSD (14 of 49 [29%] versus 15 of 207 [7%] versus 6 of 18

211 those with nonintramural VSDs or no residual VSD (20 days [interquartile range, 11-42 days] versus 7

212 Among residual VSDs after repair of conotruncal anomalies, intramural V

213 cellular caged Ca(2+), we optically resolved VSD activation prompted by Ca(2+) binding to the gating

214 The resulting VSD structures are in good agreement with the consensus

215 it is considered a voltage-sensing domain's (VSD) intrinsic property.

216 ion of the Domain III VSD, which is the same VSD that many tested LQT3 mutations affect.

217 tage-activated ion channels, voltage sensor (VSD) activation induces pore opening via VSD-pore coupli

218 potassium channels (VGKC), voltage sensors (VSD) endow voltage-sensitivity to pore domains (PDs) thr

219 on of secondary structure elements in Shaker-VSD appears to more closely resemble the KvAP-VSD.

220 ere are clear differences between the Shaker-VSD and Kv1.2/2.1 chimera in the S2-S3 linker and S3 tra

221 Our results suggest that the Shaker-VSD in LPPG micelles is in a native-like fold and is lik

222 d from shift (TALOS+) showed that the Shaker-VSD shares many structural features with the homologous

223 Double-sided VSD imaging enabled simultaneous recording of membrane p

224 Using data obtained from double-sided VSD imaging, we analyzed neuronal dynamics in both senso

225 ith the consensus model of the resting state VSD and the spin-spin distance histograms from ESR/DEER

226 We anticipate that such VSDs become dysfunctional and unable to respond to chang

227 te clinical outcomes>30 years after surgical VSD closure.

228 and need for subsequent catheter or surgical VSD closure.

229 val up to 40 years after successful surgical VSD closure is slightly lower than in the general Dutch

230 Patients who underwent surgical VSD closure during childhood between 1968 and 1980 were

231 and molecule-specific targeting of synthetic VSDs in the brain.

232 se the free energy necessary to activate the VSD.

233 ocally, mutations in the Slo1 that alter the VSD-CTD interaction can specifically change the effects

234 teract with the VSD or the CTD and alter the VSD-CTD interface of the Slo1, which enables the beta su

235 indicating that the beta subunits alter the VSD-CTD interface.

236 Although the VSD operation in Ci-VSP exhibits original voltage depend

237 d how the interdomain interactions among the VSD, CTD, and PGD are altered by the beta subunits to af

238 disrupt the disulfide bond formation at the VSD-CTD interface of mouse Slo1, indicating that the bet

239 , forms a direct structural link between the VSD and C-linker-CNBD.

240 a putative binding site located between the VSD and the TRP box, disclosing differences in the bindi

241 In conclusion, our data reveal that both the VSD and the lipid phosphatase domain of Mm-VSP are funct

242 tilized NMR spectroscopy to characterize the VSD derived from Shaker potassium channel in 1-palmitoyl

243 ker K(+) channel's pore domain (PD) from the VSD prevented the mode-shift of the gating currents.

244 However, for Hv1, the VSD functions as both the voltage sensor and the conduct

245 ward displacement, leading to changes in the VSD internal salt-bridge network, resulting in a reshapi

246 The location of the activation gate in the VSD is unknown and open channel blockers for VSDs have n

247 2,047 second doses) were administered in the VSD population.

248 the direct intervention of the linker in the VSD-PD coupling process.

249 C-terminal (Q250-K257) linker motifs in the VSD-PD coupling.

250 nd fourth (S4) transmembrane segments of the VSD alters the equilibrium between resting and active co

251 ated at positions located in the core of the VSD and apply mutant cycle analysis to determine how the

252 To address whether the functions of the VSD and phosphatase domain are retained in Mm-VSP, we to

253 While testing the functionality of the VSD and phosphatase domain, we observed slight differenc

254 The voltage dependence of the VSD from Ci-VSP (Ci-VSD) is dramatically right shifted,

255 nd water molecules in the loop region of the VSD in micelles and membranes.

256 This work illuminates the structure of the VSD intermediate state and demonstrates that intermediat

257 cantly perturb the voltage dependence of the VSD movement, suggesting a unique voltage sensing mechan

258 alanine in the charge transfer center of the VSD plays a key role in blocker binding.

259 nalysis of transient sensing currents of the VSD revealed distinct roles for the N-terminal (M240-S24

260 (237) and Gly(239) residues on the S2 of the VSD that form direct interactions with Ile(135) on the H

261 ydrophobic plug that seals the center of the VSD, as suggested by molecular dynamics simulations.

262 re for the resting state conformation of the VSD, in agreement with experiments showing that the larg

263 hin the VSD and with an inherent bias of the VSD, when hydrated around a central Phe residue, to the

264 derives from the different mechanisms of the VSD-pore coupling that lead to the IO and AO states, res

265 diate state, the hand-like C-terminus of the VSD-pore linker (S4-S5L) interacts with the pore in the

266 udy its gating process in the absence of the VSD.

267 between residues located in the core of the VSD.

268 into a rotational upward displacement of the VSD.

269 n of the PD imposes a mechanical load on the VSD, which causes its mode-shift.

270 termediate state to the activated state, the VSD-pore coupling has less efficacy in opening the pore,

271 s, known as omega-currents, pass through the VSD and are distinct from K(+) currents passing through

272 SDs can result in a leak current through the VSD and hypokalemic periodic paralysis (HypoPP), but the

273 n activation, outward S4 motion tightens the VSD-pore linker, perturbing linker-S6-helix packing.

274 a voltage-sensor domain (VSD) related to the VSD found in voltage-gated ion channels.

275 bits Hv1 proton conduction by binding to the VSD from its intracellular side.

276 The Mm-VSP phosphatase domain, fused to the VSD of a nonmammalian VSP, was also functional: activati

277 When the VSD activates from the intermediate state to the activat

278 at the pore in KCNQ1 channels opens when the VSD activates to both intermediate and fully activated s

279 ch that a beta subunit may interact with the VSD or the CTD and alter the VSD-CTD interface of the Sl

280 hydration of amino acid residues within the VSD and with an inherent bias of the VSD, when hydrated

281 The VSDs switch from a resting to an active conformation upo

282 tribution of an interface formed between the VSDs and the alphaB helices located at the top of the CT

283 (ii) The VSDs could facilitate gating (supplementing the pore gat

284 s of the first transmembrane segments of the VSDs form the intersubunit interface that mediates coupl

285 The movement of the VSDs results in a transfer of the S4 gating charges acro

286 eciable proton currents, indicating that the VSDs had different topologies.

287 detected as proton leak currents through the VSDs.

288 -sensitive KCNQ channels that contributes to VSD-pore coupling via PIP2, and thereby influences the u

289 ivation of Hv1 involves a process similar to VSD relaxation, a process previously described for volta

290 results are relevant for understanding toxin-VSD interaction and gating mechanisms of K(v) channels i

291 ction, as demonstrated by optically tracking VSD depolarization-evoked conformational rearrangements.

292 echocardiography 1 day before transcatheter VSD closure and 6 months after intervention (closure gro

293 with conservative management, transcatheter VSD closure prevents deterioration in exercise capacity

294 tage-gated proton channel Hv1 is made of two VSDs and lacks the PD.

295 from the closed to the open state in the two VSDs are known to occur cooperatively; however, the unde

296 of the length of the S3-S4 linker in various VSD-containing proteins may produce differential VSD rel

297 or (VSD) activation induces pore opening via VSD-pore coupling.

298 tructures, its transplantation in the Ci-VSP VSD scaffold yielded similar results as the native Ci-VS

299 We found that the Mm-VSP VSD, fused to a viral potassium channel, was able to dri

300 ast intracortical inhibition detectable with VSD imaging, indicated weakened inhibition as an importa

301 Sixty patients with VSD aged 12 to 60 years underwent cardiopulmonary exerci