ライフサイエンスコーパス: VDAC

1 VDAC acts as an early sensor of lipid toxicity and its G

2 VDAC also interacts with antiapoptotic proteins from the

3 VDAC channels were reconstituted into planar phospholipi

4 VDAC has three isoforms with >70% sequence similarity an

5 VDAC is a 283-residue integral membrane protein that for

6 VDAC is a beta-barrel protein located in the outer mitoc

7 VDAC is also a substrate for plasmin; hence, it mimics f

8 VDAC is characterized by its ability to "gate" between a

9 VDAC, a major protein of the mitochondrial outer membran

10 VDACs play an important role in the regulated flux of me

11 VDACs recruit Parkin to defective mitochondria.

12 VDACs specifically interact with Parkin on defective mit

13 The voltage-dependent anion channel 1 (VDAC-1) is an important protein of the outer mitochondri

14 e kinase, voltage-dependent anion channel 1 (VDAC-1), HSP60, and Grp75.

15 tified as voltage-dependent anion channel-1 (VDAC-1) by both matrix-assisted laser desorption ionizat

16 oltage-dependent anion channels 1, 2, and 3 (VDACs 1, 2, and 3), pore-forming proteins in the outer m

17 AC, and (ii) the ClC-2, ClC-3, ClC-4, ClC-5, VDAC, CaCC, MDR-1 and CFTR gene products do not contribu

18 between amino acids Ile(5) and Asn(37) and a VDAC region including amino acids (20)GYGFG(24).

19 itochondrial outer-membrane protein VDAC2, a VDAC isoform present in low abundance that interacts spe

20 clear that the two nonlamellar lipids affect VDAC gating.

21 With VDAC3 to the greatest extent, all VDAC isoforms contributed to the maintenance of mitochon

22 This also amplifies VDAC enzymatic and channel activities regulation by calc

23 unocaptured not only CPT1a but also ACSL and VDAC, further strengthening findings with blue native el

24 protein interaction between CPT1a, ACSL, and VDAC.

25 In planar lipid bilayers, Bax and VDAC form a channel through which cytochrome c can pass.

26 sis is associated with formation of CyPD and VDAC oligomers, consistent with mPTP formation.

27 at there is an interaction between G3139 and VDAC, a protein that can facilitate the physiologic exch

28 and t-PA serve as a bridge between GRP78 and VDAC bringing them together to facilitate Pg activation.

29 and that its association with t-PA, Pg, and VDAC on the cell surface may be part of a system control

30 (PTP) to Ca2+ through a Bcl-xL-sensitive and VDAC-mediated process.

31 itochondria outer membrane protein Tom40 and VDAC are confirmed by independent mutagenesis and chemic

32 Thus, an interaction between Bcl-xL and VDAC promotes matrix Ca(2+) accumulation by increasing C

33 dy suggesting a physical association between VDAC-1 and GABA(A) receptors in rat brain membranes.

34 ysiologically detectable interaction between VDAC channels isolated from mammalian mitochondria and e

35 The functional interactions between VDAC and alpha-syn, revealed by the present study, point

36 HXK II is unable to bind VDAC phosphorylated by GSK3beta and dissociates from the

37 nuclear magnetic resonance spectra for both VDAC-1, a beta-barrel membrane protein, and the G-protei

38 Furthermore, both VDAC anion selectivity and single channel conductance in

39 ical experiments indicate that micelle-bound VDAC is in intermediate exchange between monomer and tri

40 ion of mitochondrial energetics, governed by VDAC and tubulin at the mitochondria-cytosol interface.

41 exposure, and this release was prevented by VDAC blocker.

42 in block of voltage-dependent anion channel (VDAC) "rescued" mitochondrial membrane potential and met

43 ch contains voltage-dependent anion channel (VDAC) 2.

44 through the voltage-dependent anion channel (VDAC) and/or adenine nucleotide transporter (ANT) or to

45 through the voltage-dependent anion channel (VDAC) because this channel provides primary permeation p

46 ane protein voltage-dependent anion channel (VDAC) blocks traffic through the channel and reduces oxi

47 The voltage-dependent anion channel (VDAC) constitutes the major pathway for the entry and ex

48 The voltage-dependent anion channel (VDAC) governs the free exchange of ions and metabolites

49 rial marker voltage-dependent anion channel (VDAC) have various expression levels in different mitoch

50 The voltage-dependent anion channel (VDAC) in the outer membrane of mitochondria serves an es

51 e-localized voltage-dependent anion channel (VDAC) is a known Ca(2+) permeability pathway that direct

52 The voltage-dependent anion channel (VDAC) is the major pathway for ATP, ADP, and other respi

53 The voltage-dependent anion channel (VDAC) is the major pathway mediating the transfer of met

54 The voltage-dependent anion channel (VDAC) is the major permeability pathway for metabolites

55 The voltage-dependent anion channel (VDAC) is the most abundant protein in the outer mitochon

56 The voltage-dependent anion channel (VDAC) mediates and gates the flux of metabolites and ion

57 The voltage-dependent anion channel (VDAC) mediates trafficking of small molecules and ions a

58 locking the voltage-dependent anion channel (VDAC) of mitochondrial outer membrane.

59 kage of the voltage-dependent anion channel (VDAC) of the mitochondrial outer membrane by dimeric tub

60 ct with the voltage-dependent anion channel (VDAC) of the outer mitochondrial membrane.

61 entified as voltage-dependent anion channel (VDAC) oligomerization.

62 Voltage-dependent anion channel (VDAC) proteins are major components of the outer mitocho

63 rylation of voltage-dependent anion channel (VDAC) through a protein kinase Cepsilon (PKCepsilon)-dep

64 al membrane voltage-dependent anion channel (VDAC) via a hydrophobic interaction that is independent

65 The voltage-dependent anion channel (VDAC), a major pore-forming protein in the outer membran

66 fication of voltage-dependent anion channel (VDAC), a membrane channel and NADH oxidase, as a cause o

67 ore, namely voltage-dependent anion channel (VDAC), adenine nucleotide translocase (ANT), and hexokin

68 cluding the voltage-dependent anion channel (VDAC), adenine nucleotide translocator (ANT), and cyclop

69 on with the voltage-dependent anion channel (VDAC), an abundant outer mitochondrial membrane protein.

70 e synthase, voltage-dependent anion channel (VDAC), and cytochrome c oxidase subunit 4 (COX IV).

71 tochondrial voltage-dependent anion channel (VDAC), can insert into phospholipid membranes by an auto

72 through the voltage-dependent anion channel (VDAC), comprising three isoforms--VDAC1, 2, and 3.

73 rotein, the voltage-dependent anion channel (VDAC), is implicated in the control of apoptosis, includ

74 rotein, the voltage-dependent anion channel (VDAC), is increasingly implicated in the control of apop

75 (LCAS), and voltage-dependent anion channel (VDAC), isolated from rat liver mitochondrial outer membr

76 tors of the voltage-dependent anion channel (VDAC), Konig polyanion, and 4,4'-diisothiocyanatostilben

77 ed that the voltage-dependent anion channel (VDAC), located on the outer membrane of mitochondria, pl

78 h block the voltage-dependent anion channel (VDAC), prevented O2*--induced CCR.

79 ties of the voltage-dependent anion channel (VDAC), the major channel in MOM.

80 dent on the voltage-dependent anion channel (VDAC), the major channel of MOM, remains controversial.

81 blocks the voltage-dependent anion channel (VDAC), the major channel of the mitochondrial outer memb

82 transporter voltage-dependent anion channel (VDAC), the protein translocator of the outer membrane 40

83 ed with the voltage-dependent anion channel (VDAC), which is also a t-PA-binding protein in these cel

84 through the voltage-dependent anion channel (VDAC)-1/glucose-regulated protein 75 (Grp75)/inositol 1,

85 SL) and the voltage-dependent anion channel (VDAC).

86 ike protein voltage-dependent anion channel (VDAC).

87 inds to the voltage-dependent anion channel (VDAC).

88 esence of a voltage-dependent anion channel (VDAC).

89 he level of voltage-dependent anion channel (VDAC).

90 d the human voltage-dependent anion channel (VDAC); however, a functional relationship between these

91 ponent, the voltage-dependent anion channel (VDAC); intracellular acidification; mitochondrial hyperp

92 f the human voltage dependent anion channel (VDAC-1) as an example of a polytopic integral membrane p

93 voltage-dependent mitochondrial ion channel (VDAC) reduces single-channel conductance and generates e

94 e voltage-dependent anion-selective channel (VDAC), which can form a large conductance and permanentl

95 ontent, and voltage-dependent anion channel [VDAC] content) as well as Q(10) content was determined.

96 ns the outer mitochondrial membrane channel, VDAC, in an open configuration.

97 The mitochondrial channel, VDAC, regulates metabolite flux across the outer membran

98 closure of voltage-dependent anion channels (VDAC) in the mitochondrial outer membrane after ethanol

99 The voltage-dependent anion channels (VDAC) were identified as components of M. avium vacuoles

100 Pi through voltage-dependent anion channels (VDAC).

101 Voltage-dependent anion channels (VDACs) are a family of small pore-forming proteins of th

102 mmals, the Voltage-dependent anion channels (VDACs) are predominant proteins of the outer mitochondri

103 Voltage-dependent anion channels (VDACs) are the most abundant proteins in the outer mitoc

104 r membrane voltage-dependent anion channels (VDACs) in this process.

105 y, through voltage dependant anion channels (VDACs) interacting with microtubule-associated protein 1

106 Voltage-dependent anion channels (VDACs), also known as mitochondrial porins, are small ch

107 ochondrial voltage-dependent anion channels (VDACs)--a novel target for anti-cancer drugs.

108 with the titration of the negatively charged VDAC residues at low pH values.

109 n the membrane, whereas cardiolipin disrupts VDAC supramolecular assemblies.

110 Each VDAC is sufficient to support Parkin recruitment and mit

111 ed VDAC-1 resemble those of micelle-embedded VDAC-1, indicating a similar structure and function in t

112 the native ligand NADH to nanodisc-embedded VDAC-1 resemble those of micelle-embedded VDAC-1, indica

113 Four nucleus-encoded VDACs have been identified in Arabidopsis thaliana.

114 e demonstrate that PG significantly enhances VDAC oligomerization in the membrane, whereas cardiolipi

115 owever, it still remains unknown how exactly VDAC supramolecular assembly can be regulated in the mem

116 ogaster, porin is the ubiquitously expressed VDAC isoform.

117 NMR spectroscopy demonstrates a well folded VDAC-1 protein and native NADH binding functionality.

118 the theory with experiments is excellent for VDAC.

119 nt and validation of a new in vivo model for VDAC function in Drosophila should provide a valuable to

120 ipulations proved GSK3 to be responsible for VDAC phosphorylation in normal cells.

121 at much higher voltages than is typical for VDAC.

122 f mitochondrial porins that is distinct from VDAC, TOM40, and MDM10.

123 Furthermore, VDAC-reconstituted liposomes permeated cytochrome c afte

124 Here, VDAC has been expressed, purified, and refolded into a f

125 pore opening via the promotion of hexokinase-VDAC interaction at the outer mitochondrial membrane.

126 ve oxygen consumption ratio (OCR) and higher VDAC protein levels when compared to WT and Myd88(-/-) c

127 These results highlight VDAC-2 as a critical inhibitor of Bak-mediated apoptotic

128 xplore the ion transport properties of human VDAC isoform 1 (hVDAC1; PDB:2K4T) embedded in an implici

129 mus molecular dynamics simulations of human VDAC isoform 1 in DOPE/DOPC mixed bilayers in 1 M KCl so

130 NMR) solution structure of recombinant human VDAC-1 reconstituted in detergent micelles.

131 We find that PE induces voltage asymmetry in VDAC current-voltage characteristics by promoting channe

132 of tubulin result in substantial changes in VDAC closure.

133 The observed differences in VDAC behavior in PC and PE membranes cannot be explained

134 results, and the known importance of E73 in VDAC physiology, VDAC dimerization likely plays a signif

135 olism regulation in multiple ways, including VDAC's permeability modulation and the effect of electro

136 that PKA and GSK-3beta decrease and increase VDAC conductance, respectively.

137 Tubulin strikingly increases VDAC voltage sensitivity and at physiological salt condi

138 t physiological salt conditions could induce VDAC closure at <10 mV transmembrane potentials.

139 intact cells and antagonized tubulin-induced VDAC blockage in planar bilayers.

140 e outer mitochondrial membrane by inhibiting VDAC closure.

141 icate at least a partial entry of G3139 into VDAC, forming an unstable bound state, which is responsi

142 ydropathy profiles (beta-pattern) with known VDAC sequences indicates the same fundamental folding pa

143 at VDAC-like proteins are part of the larger VDAC family but the modifications are indicative of spec

144 een R6/2 and WT included: in striatum, lower VDAC and the mitochondrially encoded cytochrome oxidase

145 on channel from outer mitochondrial membrane VDAC, bacterial porin OmpC (outer membrane protein C), a

146 the L-type Ca(2+) channel and mitochondrial VDAC.

147 The mitochondrial VDAC coimmunoprecipitated with the L-type Ca(2+) channel

148 polarity, and membrane composition modulate VDAC currents.

149 The monomeric VDAC channel shows an accelerated pH titration of its tr

150 l phenotypes remarkably reminiscent of mouse VDAC mutants.

151 , whereas higher eukaryotes express multiple VDACs, with humans and mice each harboring three distinc

152 Notably, VDAC phosphorylation level correlated with steatosis sev

153 for the NADH-dependent reductase activity of VDAC.

154 e calculated insertion rate per unit area of VDAC by 8 and 9 orders of magnitude, respectively.

155 ilized cells, suggesting low availability of VDAC pores within the cell.

156 ydeoxythymidine, induces partial blockage of VDAC and a change in selectivity from favoring anions to

157 that prior to the characteristic blockage of VDAC, tubulin first binds to the membrane in a lipid-dep

158 se it has been suggested that the closure of VDAC leads to the opening of another outer mitochondrial

159 duce voltage-sensitive reversible closure of VDAC reconstituted into planar phospholipid membranes.

160 s tubulin promotes single-channel closure of VDAC, we hypothesized that tubulin is a dynamic regulato

161 enesis in hepatocytes mediated by closure of VDAC.

162 TP is a heterooligomeric complex composed of VDAC, SPG7, and CypD.

163 ion by promoting the closed configuration of VDAC.

164 early indicate a fundamental conservation of VDAC function.

165 The voltage dependence of VDAC's permeability is puzzling, because the existence o

166 ata showed that 1), the physical diameter of VDAC pores in cardiac mitochondria is >or=3 nm but <or=6

167 uable tool for further genetic dissection of VDAC role(s) in mitochondrial biology and disease, and a

168 ce from the electrophysiologic evaluation of VDAC channels reconstituted into phospholipid membranes

169 imulations and single-channel experiments of VDAC-1 show agreement for the current-voltage relationsh

170 Electron microscopy reveals the formation of VDAC-1 multimers, an observation that is consistent with

171 The essential life-sustaining function of VDAC in metabolite trafficking is believed to be regulat

172 ith caspase-8 affected the voltage gating of VDAC by inducing channel closure.

173 The inactivation of VDAC-1 function either by pharmacological means or siRNA

174 nin-permeabilized hepatocytes, indicative of VDAC closure.

175 We propose that inhibition of VDAC by free tubulin limits mitochondrial metabolism in

176 Inhibitors of VDAC, 4'-diisothiocyano-2,2'-disulfonic acid stilbene (D

177 process results in an oriented insertion of VDAC channels and an increase in insertion rate per unit

178 this is due to the preferential insertion of VDAC into CL-rich domains.

179 orB with VDAC, similar to the interaction of VDAC with antiapoptotic Bcl-2 proteins, resulting in an

180 The involvement of VDAC oligomerization in apoptosis has been suggested in

181 Although multiple isoforms of VDAC have been found in different organisms, only one is

182 etailed analysis of the blockage kinetics of VDAC reconstituted into planar lipid membranes suggests

183 lipid accumulation triggers a rapid lack of VDAC phosphorylation by glycogen synthase kinase 3 (GSK3

184 Here, we show that the mechanism of VDAC blockage by tubulin involves tubulin interaction wi

185 way via the induction and oligomerization of VDAC.

186 differences in the insertion orientation of VDAC in these membranes.

187 re-sensitive conditional-lethal phenotype of VDAC-deficient yeast, whereas CG17139 and CG17140 demons

188 al alpha-helix is located inside the pore of VDAC in the open state and remains associated with beta-

189 nhibited by NADH and require the presence of VDAC, a voltage-dependent anion channel present in the o

190 culate that by decreasing the probability of VDAC opening, Bid reduces metabolite exchange between mi

191 Here, we report that properties of VDAC channels reconstituted into planar phospholipid mem

192 The off-rate of VDAC blockage by tubulin does not depend on the lipid co

193 Only PorA/C1 increases the overall rate of VDAC insertion (50-fold) over the self-catalyzed rate.

194 ity of TbTim50 plays a role in regulation of VDAC expression.

195 We also found that the response of VDAC gating to acidification was highly asymmetric.

196 Although, we could not establish a role of VDAC channels in the transport of known secreted M. aviu

197 helpful insights into the regulatory role of VDAC in the protective effect of cytosolic acidification

198 difference leads to the anion selectivity of VDAC.

199 ich is homologous to the primary sequence of VDAC residues Tyr224-Lys255.

200 The similarity of VDAC mutant phenotypes in the fly and mouse clearly indi

201 R measurements revealed the binding sites of VDAC-1 for the Bcl-2 protein Bcl-x(L), for reduced beta-

202 The tubulin-blocked state of VDAC is impermeant for ATP but only partially closed for

203 l cue for regulating the oligomeric state of VDAC.

204 The available structures of VDAC proteins show a wide beta-stranded barrel pore, wit

205 antibody directed against the N terminus of VDAC-1 immunoprecipitated labeled 35-kDa protein from a

206 ions contribute to differential stability of VDACs and may have implications in their in vivo regulat

207 However, the oligomeric VDAC-2 complexes are diminished, and Bak does not intera

208 not induce cytochrome c release by acting on VDAC.

209 or mitochondria metabolism and apoptosis, on VDAC oligomerization.

210 nd [K+], we determined the effect of Ca2+ on VDAC activity.

211 that alpha-syn toxicity in yeast depends on VDAC.

212 other ansamycins are due to their effects on VDAC and that this may play a role in their clinical act

213 investigated the effects of pH variations on VDAC gating properties.

214 unctionally demarcate hVDAC-2 from the other VDACs.

215 The maxi Cl- channel (p-VDAC) blocker Gd3+, the ClC-2 inhibitor Cd2+, and the MD

216 kt, GSK3beta is activated and phosphorylates VDAC.

217 known importance of E73 in VDAC physiology, VDAC dimerization likely plays a significant role in mit

218 PorB interacts with the mitochondrial porin VDAC (voltage-dependent anion channel).

219 bition of binding and even induces prolonged VDAC closures.

220 283-residue integral human membrane protein VDAC-1, which has a rotational correlation time of about

221 mediated by binding to an accessory protein, VDAC-1.

222 Purified VDAC binds to K5 but only when reconstituted into liposo

223 In liposomes, the purified VDAC displays Ca2+-dependent control of the molecular cu

224 ments, at submicromolar [Ca2+], the purified VDAC or isolated OMM does not show sustained large condu

225 In the presence of cholesterol, recombinant VDAC-1 can form voltage-gated channels in phospholipid b

226 We reconstituted VDAC into planar lipid membranes and found that acidific

227 into mitochondria and significantly reduced VDAC oligomerization and AIF release.

228 he mechanisms for how these factors regulate VDAC-1, and which changes they trigger in the channel, a

229 de transport data suggest that GSK regulates VDAC and that VDAC may be an important regulatory site i

230 ght influence MOM permeability by regulating VDAC gating.

231 ng purified mitochondria expressing a single VDAC isoform, we found that erastin alters the permeabil

232 -oligomeric complexes that still retain some VDAC-2.

233 Thus, in nonalcoholic steatosis VDAC exhibits reduced threonine phosphorylation, which i

234 The submicrosecond VDAC-1 voltage response shows intrinsic structural chang

235 There is accumulating evidence supporting VDAC's role in mitochondrial metabolic regulation and ap

236 Cell surface VDAC is a receptor for plasminogen kringle 5, which prom

237 re consistent with pore blockage rather than VDAC closure.

238 ata suggest that GSK regulates VDAC and that VDAC may be an important regulatory site in ischemia/rep

239 , thus initiating apoptosis, it appears that VDAC may be an important pharmacologic target of G3139.

240 sate of rat brain membranes, confirming that VDAC-1 is the species labeled by [(3)H]6-AziP.

241 In this study, we demonstrate that VDAC binds tissue-type plasminogen activator (t-PA) on h

242 tructure and channel formation indicate that VDAC-like proteins are part of the larger VDAC family bu

243 Here we report that VDAC catalyzes the insertion of PorA/C1 and KcsA by incr

244 ool to probe bilayer mechanics, we show that VDAC channels are much more sensitive to the presence of

245 These studies suggest that VDAC is a receptor for K5.

246 We hypothesize that VDACs serve as mitochondrial docking sites to recruit Pa

247 n recruitment and mitophagy, suggesting that VDACs can function redundantly.

248 The VDAC-interacting region of Bcl-xL was characterized by N

249 mensional structure of the nucleotide by the VDAC channel.

250 ) receptor were co-immunoprecipitated by the VDAC-1 antibody suggesting a physical association betwee

251 tubulin's negatively charged tail enters the VDAC pore, inverting its anionic selectivity to cationic

252 However, the VDAC level was unaltered when the phosphatase-inactive m

253 e occurs preferentially from one side of the VDAC channel.

254 omolar G3139 induces rapid flickering of the VDAC conductance and, occasionally, a complete conductan

255 tage-dependent asymmetric distortions of the VDAC-1 barrel and the displacement of particular charged

256 onductance, indicating a closed state of the VDAC.

257 Our characterization of the VDAC/Bcl-xL complex offers initial structural insight in

258 1 and -3 isoforms, and peptides based on the VDAC sequence disrupted Bcl-xL binding.

259 ce of intracellular barriers restricting the VDAC pore availability in vivo.

260 eir temperature dependence suggests that the VDAC structure does not change conformation above and be

261 of ions and metabolites passing through the VDAC pore.

262 itochondrial intermembrane space through the VDAC.

263 Thus, the VDAC gating is dependent on the physiological concentrat

264 Bcl-x(L) interacts with the VDAC barrel laterally at strands 17 and 18.

265 These VDAC residues correspond to a GXXXG repeat motif commonl

266 In the absence of all three VDACs, the recruitment of Parkin to defective mitochondr

267 ve effects of HKI and HKII, possibly through VDAC phosphorylation by PKCepsilon.

268 ious proposal that ATP translocation through VDAC is facilitated by a set of specific interactions be

269 Hexokinases are known to bind to VDAC and directly couple intramitochondrial ATP synthesi

270 . avium mmpL4 proteins were found to bind to VDAC-1 protein.

271 Hexokinase II (HXK II) also binds to VDAC.

272 and beta-tubulin tails contribute equally to VDAC blockade and what effects might be due to sequence

273 These results demonstrate that ligands to VDAC proteins can induce non-apoptotic cell death select

274 Binding of t-PA to VDAC induced a decrease in K(m) and an increase in the V

275 Binding of t-PA to VDAC occurs between a t-PA fibronectin type I finger dom

276 served with varying degrees of similarity to VDAC.

277 uorescence cross-correlation spectroscopy to VDAC reconstituted into giant unilamellar vesicles, we d

278 referentially localized in close vicinity to VDAC, presumably at the inner boundary membrane, whereas

279 ned direct evidence for binding of Bcl-xL to VDAC in a detergent micelle system.

280 Reversal of tubulin-VDAC interaction by erastin antagonizes Warburg metaboli

281 find that voltage sensitivity of the tubulin-VDAC blockage practically does not depend on the lipid c

282 This tubulin-VDAC interaction requires tubulin anionic C-terminal tai

283 nce mitochondrial respiration through tuning VDAC sensitivity to blockage by tubulin.

284 s suggest that Bcl-xL can bind to one or two VDAC molecules forming heterodimers and heterotrimers.

285 resistance to erastin, implicating these two VDAC isoforms in the mechanism of action of erastin.

286 Thus, O2*- triggers apoptosis via VDAC-dependent permeabilization of the mitochondrial out

287 s resulted in accelerated Pg activation when VDAC, t-PA, and Pg were bound together.

288 These phenomena occur only when VDAC is in the "open" conformation and therefore are con

289 al metabolic regulation and apoptosis, where VDAC oligomerization has been implicated with these proc

290 nstrated the direct interaction of Bcl2 with VDAC, leading to reduced channel conductance.

291 Experiments with VDAC-1 mutants identified amino acids that regulate the

292 e diminished, and Bak does not interact with VDAC-2 in Bax-deficient HCT116 cells.

293 rrelated with their ability to interact with VDAC.

294 , perhaps partly via direct interaction with VDAC and reduction of metabolite flow across the mitocho

295 c Bcl-xL may be through its interaction with VDAC.

296 intracellular Ca2+ via its interaction with VDAC.

297 Erastin, a compound that interacts with VDAC, blocked and reversed mitochondrial depolarization

298 the protein-protein interaction of PorB with VDAC, similar to the interaction of VDAC with antiapopto

299 ntibodies against these sequences react with VDAC and detect this protein on the plasma membrane of h

300 rate that Parkin specifically interacts with VDACs when the function of mitochondria is disrupted by