The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating
about
Charged residues distribution modulates selectivity of the open state of human isoforms of the voltage dependent anion-selective channelOpening and closing the metabolite gateThe structural biology of β-barrel membrane proteins: a summary of recent reportsσ-1 receptor at the mitochondrial-associated endoplasmic reticulum membrane is responsible for mitochondrial metabolic regulationThe 3D structures of VDAC represent a native conformationX-ray crystallography over the past decade for novel drug discovery - where are we heading next?Obstructing toxin pathways by targeted pore blockageRegulation of mitochondrial function by voltage dependent anion channels in ethanol metabolism and the Warburg effectMembrane protein structure determination - the next generationStructure-guided simulations illuminate the mechanism of ATP transport through VDAC1Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorBHomologue structure of the SLAC1 anion channel for closing stomata in leavesA Transporter Converted into a Sensor, a Phototaxis Signaling Mutant of Bacteriorhodopsin at 3.0 ÅHigh Resolution Structure and Double Electron-Electron Resonance of the Zebrafish Voltage-dependent Anion Channel 2 Reveal an Oligomeric PopulationHigh-Resolution NMR Determination of the Dynamic Structure of Membrane ProteinsChannel-forming activities in the glycosomal fraction from the bloodstream form of Trypanosoma bruceiProtein targeting and transport as a necessary consequence of increased cellular complexityPxmp2 is a channel-forming protein in Mammalian peroxisomal membrane.Photoaffinity labeling with cholesterol analogues precisely maps a cholesterol-binding site in voltage-dependent anion channel-1.Mechanism of α-synuclein translocation through a VDAC nanopore revealed by energy landscape modeling of escape time distributions.Control of human VDAC-2 scaffold dynamics by interfacial tryptophans is position specific.From Constructs to Crystals - Towards Structure Determination of β-barrel Outer Membrane Proteins.How does a β-barrel integral membrane protein insert into the membrane?Evidence of Distinct Channel Conformations and Substrate Binding Affinities for the Mitochondrial Outer Membrane Protein Translocase Pore Tom40.Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.Molecular basis for the differential interaction of plant mitochondrial VDAC proteins with tRNAs.Presequence recognition by the tom40 channel contributes to precursor translocation into the mitochondrial matrixAcidification asymmetrically affects voltage-dependent anion channel implicating the involvement of salt bridges.Evidence supporting the 19 β-strand model for Tom40 from cysteine scanning and protease site accessibility studies.Voltage-dependent structural changes of the membrane-bound anion channel hVDAC1 probed by SEIRA and electrochemical impedance spectroscopy.Cysteine residues impact the stability and micelle interaction dynamics of the human mitochondrial β-barrel anion channel hVDAC-2The voltage-dependent anion selective channel 1 (VDAC1) topography in the mitochondrial outer membrane as detected in intact cell.A 3-dimensional trimeric β-barrel model for Chlamydia MOMP contains conserved and novel elements of Gram-negative bacterial porinsStructural adaptations of proteins to different biological membranes.Charge asymmetry in the proteins of the outer membrane.Weakly stable regions and protein-protein interactions in beta-barrel membrane proteinsβ-Barrel mobility underlies closure of the voltage-dependent anion channelThe protein import pore Tom40 in the microsporidian Nosema bombycis.Lipid dynamics and protein-lipid interactions in 2D crystals formed with the β-barrel integral membrane protein VDAC1.Structure-based analysis of VDAC1: N-terminus location, translocation, channel gating and association with anti-apoptotic proteins.
P2860
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P2860
The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating
description
2008 nî lūn-bûn
@nan
2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
The crystal structure of mouse ...... nsights into metabolite gating
@ast
The crystal structure of mouse ...... nsights into metabolite gating
@en
The crystal structure of mouse ...... nsights into metabolite gating
@nl
type
label
The crystal structure of mouse ...... nsights into metabolite gating
@ast
The crystal structure of mouse ...... nsights into metabolite gating
@en
The crystal structure of mouse ...... nsights into metabolite gating
@nl
prefLabel
The crystal structure of mouse ...... nsights into metabolite gating
@ast
The crystal structure of mouse ...... nsights into metabolite gating
@en
The crystal structure of mouse ...... nsights into metabolite gating
@nl
P2093
P2860
P50
P3181
P356
P1476
The crystal structure of mouse ...... nsights into metabolite gating
@en
P2093
Jeff Abramson
Ligia Toro
Rachna Ujwal
Salem Faham
P2860
P304
P3181
P356
10.1073/PNAS.0809634105
P407
P577
2008-11-18T00:00:00Z