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 movements are coupled to BK channel opening with a u

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

7 VSDs sense changes in the transmembrane voltage and conv

8 1 may strengthen the coupling between hKv1.3-VSD movement and pore opening, inducing the modification

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

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

11 l has a different architecture, containing a VSD, but lacking a pore domain.

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

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

14 The risk of a VSD is not only complex but dynamic.

15 To learn about VSD-lipid interactions, we used nuclear magnetic resonan

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

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

18 s leading to channel opening even before all VSDs have moved.

19 P2 in coupling retigabine binding to altered VSD function.

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

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

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

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

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

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

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

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

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

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

30 Depolarization is sensed by VSD-charged residues residing in the membrane field, ind

31 ltage-sensing residues, we probed the BK(Ca) VSD for evidence of cooperativity between charge-carryin

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

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

34 exclude the possibility that the Hv channel VSD assembles with an as yet unknown protein in the cell

35 The Hv channel VSD by itself supports H(+) flux.

36 termine and refine a model of the Kv channel VSD in the resting conformation.

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

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

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

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

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

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

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

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

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

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

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

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

49 ge, enrolled in the Vaccine Safety Datalink (VSD) who received RV5 from May 2006-February 2010.

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

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

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

53 right ventricle, ventricular septal defect (VSD), atrioventricular (AV) cushion defects, and thicken

54 ith no associated ventricular septal defect (VSD).

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

56 ricle (DORV) and ventricular septal defects (VSD).

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

58 the incidence of ventricular septal defects (VSDs) caused by a heterozygous Nkx2-5 knockout mutation.

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

60 % penetrance and ventricular septal defects (VSDs) with ~15% penetrance; Fz2(+/-);Fz7(-/-) mice exhib

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

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

63 nd N-terminal vacuolar sorting determinants (VSDs) to the vacuole are largely unknown.

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

65 containing proteins may produce differential VSD relaxation in vivo.

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

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

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

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

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

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

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

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

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

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

76 he first four form a voltage-sensing domain (VSD) and the last two form the pore domain (PD).

77 ng one transmembrane voltage-sensing domain (VSD) and two intracellular high affinity Ca(2+)-sensing

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

79 1 interacts with the voltage sensing domain (VSD) of Kv1.3 through W172 in the transmembrane segment

80 1 interacts with the voltage-sensing domain (VSD) of Kv7.1.

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

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

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

84 he S4 segment in the voltage-sensing domain (VSD) spontaneously converts into a 3(10) helix over a st

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

86 s found to contain a voltage-sensing domain (VSD), similar to those of voltage-gated sodium, potassiu

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

88 annels share a common voltage sensor domain (VSD) consisting of four transmembrane helices, including

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

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

91 ation of the isolated Voltage-Sensor Domain (VSD) of the prokaryotic Na(+) channel NaChBac in a lipid

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

93 adopt a transmembrane voltage sensor domain (VSD) that moves in response to physiological variations

94 hannel genes encode a voltage sensor domain (VSD) without a pore domain.

95 ed to a transmembrane voltage-sensor domain (VSD).

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

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

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

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

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

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

102 Voltage-sensing domains (VSDs) of voltage-gated potassium (Kv) channels undergo a

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

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

105 Voltage-sensing domains (VSDs) undergo conformational changes in response to the

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

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

108 d ion channels four voltage-sensing domains (VSDs), one from each subunit, control one ion permeation

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

110 the motion of their voltage-sensing domains (VSDs).

111 surrounded by four voltage sensing domains (VSDs).

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

113 Voltage-sensor domains (VSDs) are specialized transmembrane segments that confer

114 Voltage sensor domains (VSDs) are structurally and functionally conserved protei

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

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

117 el suggests that the voltage-sensor domains (VSDs) of the reported structure are not fully activated.

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

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

120 nferred through four voltage-sensor domains (VSDs) where positively charged residues in the fourth tr

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

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

123 d model of intermediate conformations during VSD gating.

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

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

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

127 d an orderly shift of voltage-sensitive dye (VSD) signals along the AI tonotopic axis, demonstrating

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

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

130 tical activity using voltage-sensitive dyes (VSDs) in the developing rat in vivo.

131 Each VSD displayed unique kinetics, consistent with distinct

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

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

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

135 r gating charge that originates from earlier VSD movements.

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

137 The equilibrated VSD configuration is consistent with the biotin-avidin a

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

139 % penetrance; Fz2(+/-);Fz7(-/-) mice exhibit VSDs with ~50% penetrance and cleft palate with less tha

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

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

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

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

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

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

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

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

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

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

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

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

152 sly reported between THM4 and CVDs including VSDs.

153 ues residing in the membrane field, inducing VSD activation that facilitates channel gating.

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

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

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

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

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

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

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

161 e the activated conformation of the isolated-VSD in the membrane using restrain-driven molecular dyna

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

163 ed that the micelle uniformly coats the KvAP VSD and approximates the chemical environment of a phosp

164 The solution structure of the KvAP VSD solubilized within phospholipid micelles is similar

165 nerate a model of the down state of the KvAP VSD using molecular-dynamics simulations of the VSD in a

166 in comparison to the membrane-embedded KvAP-VSD, the structural dynamics of the NaChBac-VSD reveals

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

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

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

170 pattern that is disrupted around a muscular VSD.

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

172 chromosome 6 locus overlaps one for muscular VSD susceptibility.

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

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

175 se cardiac malformations, including muscular VSDs.

176 ized to be the mechanistic basis of muscular VSDs.

177 plementation assays we show that the NaChBac-VSD can provide a conduit to the transport of ions in th

178 verall three-dimensional fold of the NaChBac-VSD closely mirrors those seen in KvAP, Kv1.2, Kv1.2-2.1

179 -VSD, the structural dynamics of the NaChBac-VSD reveals a much tighter helix packing, with subtle di

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

181 excitation wavelengths afforded by these new VSDs spans 440-670 nm; the two-photon excitation range i

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

183 wed for residual intramural or nonintramural VSDs.

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

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

186 lts suggest that the overall architecture of VSD's is remarkably conserved among K(+) and Na(+) chann

187 that the kinetics and voltage dependence of VSD movement in Ci-VSP can be tuned over 2 orders of mag

188 and which are associated with development of VSD and DORV.

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

190 nsible for the development and modulation of VSD relaxation.

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

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

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

194 The set of VSDs, thus, affords an extended toolkit for optical reco

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

196 greement with the homologous region of other VSDs.

197 via the interactions among the channel pore, VSD and CTD.

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

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

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

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

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

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

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

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

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

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

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

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

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

211 ivity, the topographic order of subthreshold VSD maps was reduced in layer IV and even further degrad

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

213 and need for subsequent catheter or surgical VSD closure.

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

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

216 ts affected in the trafficking of C-terminal VSD containing proteins, we isolated the ribosomal bioge

217 tial for intracellular signals to affect the VSD in order to modulate the function of its host molecu

218 igate the mechanism of how KCNE1 affects the VSD to alter the voltage dependence of channel activatio

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

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

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

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

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

224 ct interaction between RCK1 and RCK2 and the VSD.

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

226 epending on various interactions between the VSD and its host molecules.

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

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

229 We characterized the VSD-phospholipid micelle interactions using nuclear Over

230 Mg(2)(+) activated K(+) channels contain the VSD and a large cytosolic domain (CTD) that binds Ca(2)(

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

232 However, the VSD movements and coupling to the channel or phosphatase

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

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

235 2,047 second doses) were administered in the VSD population.

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

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

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

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

240 along likely pathways for activation of the VSD and opening of the pore domain.

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

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

243 be the principal functional component of the VSD because it carries, in most channels, a large portio

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

245 structure and phospholipid interface of the VSD from the voltage-dependent K(+) channel KvAP (prokar

246 es, in most channels, a large portion of the VSD gating charge.

247 using molecular-dynamics simulations of the VSD in a lipid bilayer in excess water.

248 ion bridges between all four segments of the VSD in the voltage-gated Shaker K channel.

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

250 243W, respectively, into the S4 helix of the VSD of one, two, three, and four subunits.

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

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

253 e stimuli, revealing the adaptability of the VSD to its host molecules and showing the potential for

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

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

256 xation experiments, we show that much of the VSD, including the pronounced kink in S3 and the S3-S4 p

257 ial, acting upon key charged residues of the VSD, reveals that the applied field varies rapidly over

258 r molecules from hydrating the center of the VSD, thus breaking the proton conduction pathway.

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

260 To clarify the role of the VSD-PD linker as a putative partner for electrostatic in

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

262 ane segments in the hydrated interior of the VSD.

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

264 nhancing MTS accessibility to the top of the VSD.

265 ried out for 118 mutants covering all of the VSD.

266 ed the effect of [Ca(2+)](i) increase on the VSD rearrangements.

267 prevent the effect of Ca(2+) release on the VSD, revealing a functionally distinct interaction betwe

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

269 ence of channel activation, we perturbed the VSD of Kv7.1 by mutagenesis and chemical modification in

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

271 sensor only proteins have suggested that the VSD and the PD can fold independently.

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

273 cid allows permeation of cations through the VSD.

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

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

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

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

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

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

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

281 S4 toward a water-filled crevice within the VSD and allows salt-bridge interactions with negatively

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

283 The VSDs of large-conductance, voltage- and Ca(2+)-activated

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

285 ate reveal the pore in an open state and the VSDs in an up state.

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

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

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

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

290 detected as proton leak currents through the VSDs.

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

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

293 sitions R3 next to D112 in the transmembrane VSD to form the ion selectivity filter in the channel's

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