Correct folding of the beta-barrel of the human membrane protein VDAC requires a lipid bilayer.
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Opening and closing the metabolite gateThe crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gatingControl of human VDAC-2 scaffold dynamics by interfacial tryptophans is position specific.A novel Mitosomal β-barrel Outer Membrane Protein in EntamoebaLipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.Differential contribution of tryptophans to the folding and stability of the attachment invasion locus transmembrane β-barrel from Yersinia pestis.Cysteine residues impact the stability and micelle interaction dynamics of the human mitochondrial β-barrel anion channel hVDAC-2Influence of protein-micelle ratios and cysteine residues on the kinetic stability and unfolding rates of human mitochondrial VDAC-2Charge asymmetry in the proteins of the outer membrane.Lipid dynamics and protein-lipid interactions in 2D crystals formed with the β-barrel integral membrane protein VDAC1.Bacterial expression, purification and characterization of a rice voltage-dependent, anion-selective channel isoform, OsVDAC4.Physical determinants of β-barrel membrane protein folding in lipid vesiclesMembrane interactions control residue fluctuations of outer membrane porins.Helicobacter pylori VacA toxin/subunit p34: targeting of an anion channel to the inner mitochondrial membrane.Bacterial porin disrupts mitochondrial membrane potential and sensitizes host cells to apoptosis.Solubilization and characterization of the anthrax toxin pore in detergent micellesBeta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro.Omp85(Tt) from Thermus thermophilus HB27: an ancestral type of the Omp85 protein family.The N-terminal helix is a post-assembly clamp in the bacterial outer membrane protein PagP.Outer Membrane Protein Folding and Topology from a Computational Transfer Free Energy Scale.Origami in outer membrane mimetics: correlating the first detailed images of refolded VDAC with over 20 years of biochemical data.Concentration dependent ion selectivity in VDAC: a molecular dynamics simulation study.Co-translational association of cell-free expressed membrane proteins with supplied lipid bilayers.Flexibility of the N-terminal mVDAC1 segment controls the channel's gating behavior.Benzoquinone ansamycin 17AAG binds to mitochondrial voltage-dependent anion channel and inhibits cell invasion.Interaction of heat shock protein 70 with membranes depends on the lipid environment.Solution NMR of membrane proteins in bilayer mimics: small is beautiful, but sometimes bigger is better.Mitochondrial outer membrane proteins assist Bid in Bax-mediated lipidic pore formationMechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?The influence of sterols on the conformation of recombinant mitochondrial porin in detergent.The role of lipids in VDAC oligomerization.Voltage Dependence of Conformational Dynamics and Subconducting States of VDAC-1.Predictions suggesting a participation of beta-sheet configuration in the M2 domain of the P2X(7) receptor: a novel conformation?Two-step folding of recombinant mitochondrial porin in detergent.Effects of ergosterol on the structure and activity of Neurospora mitochondrial porin in liposomes.Phosphorylation of purified mitochondrial Voltage-Dependent Anion Channel by c-Jun N-terminal Kinase-3 modifies channel voltage-dependence.Approaches for Preparation and Biophysical Characterization of Transmembrane β-BarrelsThermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: case study from bacteria and humans
P2860
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P2860
Correct folding of the beta-barrel of the human membrane protein VDAC requires a lipid bilayer.
description
2007 nî lūn-bûn
@nan
2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Correct folding of the beta-ba ...... VDAC requires a lipid bilayer.
@ast
Correct folding of the beta-ba ...... VDAC requires a lipid bilayer.
@en
type
label
Correct folding of the beta-ba ...... VDAC requires a lipid bilayer.
@ast
Correct folding of the beta-ba ...... VDAC requires a lipid bilayer.
@en
prefLabel
Correct folding of the beta-ba ...... VDAC requires a lipid bilayer.
@ast
Correct folding of the beta-ba ...... VDAC requires a lipid bilayer.
@en
P2093
P1476
Correct folding of the beta-ba ...... VDAC requires a lipid bilayer.
@en
P2093
Baladhandapani Shanmugavadivu
Hans-Jürgen Apell
Thomas Meins
P356
10.1016/J.JMB.2007.01.066
P407
P577
2007-02-03T00:00:00Z